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*** bam ***elNémo ID: 2407261536261335317Job options:ID = 2407261536261335317 JOBID = bam USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER bam HEADER MEMBRANE PROTEIN 28-APR-11 2YHC TITLE STRUCTURE OF BAMD FROM E. COLI COMPND MOL_ID: 1; COMPND 2 MOLECULE: UPF0169 LIPOPROTEIN YFIO; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 29-245; COMPND 5 SYNONYM: BAMD; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 469008; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET24D KEYWDS LIPOPROTEIN, ESSENTIAL BAM COMPONENT, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR K.ZETH,R.ALBRECHT REVDAT 3 08-MAY-24 2YHC 1 REMARK REVDAT 2 10-AUG-11 2YHC 1 JRNL REMARK VERSN REVDAT 1 01-JUN-11 2YHC 0 JRNL AUTH R.ALBRECHT,K.ZETH JRNL TITL STRUCTURAL BASIS OF OUTER MEMBRANE PROTEIN BIOGENESIS IN JRNL TITL 2 BACTERIA. JRNL REF J.BIOL.CHEM. V. 286 27792 2011 JRNL REFN ISSN 0021-9258 JRNL PMID 21586578 JRNL DOI 10.1074/JBC.M111.238931 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0071 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.39 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 16896 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) : 0.200 REMARK 3 R VALUE (WORKING SET) : 0.198 REMARK 3 FREE R VALUE : 0.233 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 890 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) : 1.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1234 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0 REMARK 3 BIN R VALUE (WORKING SET) : 0.2730 REMARK 3 BIN FREE R VALUE SET COUNT : 65 REMARK 3 BIN FREE R VALUE : 0.3710 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1704 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 4 REMARK 3 SOLVENT ATOMS : 84 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.67 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.53000 REMARK 3 B22 (A**2) : -0.44000 REMARK 3 B33 (A**2) : 0.33000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.58000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.157 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.139 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.100 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.041 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1774 ; 0.024 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2415 ; 2.095 ; 1.936 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 215 ; 5.794 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 99 ;38.216 ;24.040 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 289 ;19.081 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;16.730 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 255 ; 0.156 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1405 ; 0.012 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1063 ; 1.320 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1710 ; 2.317 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 711 ; 4.005 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 701 ; 6.231 ; 4.500 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 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 11 A 40 REMARK 3 ORIGIN FOR THE GROUP (A): 28.7807 31.1916 6.2709 REMARK 3 T TENSOR REMARK 3 T11: 0.2014 T22: 0.0290 REMARK 3 T33: 0.0906 T12: -0.0399 REMARK 3 T13: 0.0180 T23: 0.0270 REMARK 3 L TENSOR REMARK 3 L11: 4.9656 L22: 2.8769 REMARK 3 L33: 2.7929 L12: 0.6217 REMARK 3 L13: -0.1348 L23: -0.3655 REMARK 3 S TENSOR REMARK 3 S11: 0.0472 S12: 0.2085 S13: 0.4499 REMARK 3 S21: 0.0855 S22: -0.0983 S23: -0.0359 REMARK 3 S31: -0.3602 S32: 0.2007 S33: 0.0511 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 41 A 62 REMARK 3 ORIGIN FOR THE GROUP (A): 30.1939 23.0100 10.1827 REMARK 3 T TENSOR REMARK 3 T11: 0.0781 T22: 0.0133 REMARK 3 T33: 0.0513 T12: -0.0275 REMARK 3 T13: 0.0032 T23: -0.0019 REMARK 3 L TENSOR REMARK 3 L11: 3.7045 L22: 1.5557 REMARK 3 L33: 1.4309 L12: 0.5802 REMARK 3 L13: 0.2684 L23: 0.2619 REMARK 3 S TENSOR REMARK 3 S11: 0.0324 S12: -0.0461 S13: -0.0120 REMARK 3 S21: 0.0721 S22: -0.0173 S23: -0.1105 REMARK 3 S31: -0.1893 S32: 0.1161 S33: -0.0152 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 : A 63 A 84 REMARK 3 ORIGIN FOR THE GROUP (A): 26.7608 14.2795 11.5769 REMARK 3 T TENSOR REMARK 3 T11: 0.0631 T22: 0.0056 REMARK 3 T33: 0.0845 T12: -0.0074 REMARK 3 T13: 0.0068 T23: 0.0121 REMARK 3 L TENSOR REMARK 3 L11: 3.8546 L22: 1.1959 REMARK 3 L33: 3.1862 L12: 0.2014 REMARK 3 L13: 1.2340 L23: 0.4032 REMARK 3 S TENSOR REMARK 3 S11: 0.1114 S12: -0.1036 S13: -0.3696 REMARK 3 S21: 0.0263 S22: -0.0077 S23: -0.1107 REMARK 3 S31: 0.1565 S32: 0.0310 S33: -0.1037 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 : A 85 A 140 REMARK 3 ORIGIN FOR THE GROUP (A): 15.7440 12.0643 16.9061 REMARK 3 T TENSOR REMARK 3 T11: 0.0665 T22: 0.1045 REMARK 3 T33: 0.0987 T12: -0.0241 REMARK 3 T13: 0.0352 T23: 0.0424 REMARK 3 L TENSOR REMARK 3 L11: 7.5401 L22: 3.0223 REMARK 3 L33: 3.6888 L12: 3.6334 REMARK 3 L13: 0.7361 L23: 0.3104 REMARK 3 S TENSOR REMARK 3 S11: 0.0437 S12: -0.6024 S13: -0.5293 REMARK 3 S21: -0.0239 S22: -0.1352 S23: -0.2152 REMARK 3 S31: 0.1388 S32: -0.1412 S33: 0.0915 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 141 A 184 REMARK 3 ORIGIN FOR THE GROUP (A): 1.6043 -0.9952 14.6290 REMARK 3 T TENSOR REMARK 3 T11: 0.0424 T22: 0.1627 REMARK 3 T33: 0.0946 T12: -0.0534 REMARK 3 T13: 0.0300 T23: -0.0233 REMARK 3 L TENSOR REMARK 3 L11: 2.9072 L22: 5.2930 REMARK 3 L33: 0.6654 L12: 3.6010 REMARK 3 L13: 0.8582 L23: 0.9480 REMARK 3 S TENSOR REMARK 3 S11: -0.1410 S12: 0.0776 S13: 0.0458 REMARK 3 S21: -0.2747 S22: 0.1502 S23: 0.0220 REMARK 3 S31: -0.0948 S32: 0.0610 S33: -0.0092 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 185 A 233 REMARK 3 ORIGIN FOR THE GROUP (A): -2.0928 -3.4566 25.8886 REMARK 3 T TENSOR REMARK 3 T11: 0.0762 T22: 0.2031 REMARK 3 T33: 0.1274 T12: -0.0383 REMARK 3 T13: 0.0214 T23: -0.0130 REMARK 3 L TENSOR REMARK 3 L11: 1.7010 L22: 1.8520 REMARK 3 L33: 2.4916 L12: 1.4079 REMARK 3 L13: 1.6358 L23: 1.4326 REMARK 3 S TENSOR REMARK 3 S11: 0.0688 S12: -0.2454 S13: 0.0664 REMARK 3 S21: 0.2088 S22: -0.1162 S23: -0.0066 REMARK 3 S31: -0.0401 S32: -0.2235 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 : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS. REMARK 4 REMARK 4 2YHC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-APR-11. REMARK 100 THE DEPOSITION ID IS D_1290048152. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X10SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16896 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.900 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 200 DATA REDUNDANCY : 6.200 REMARK 200 R MERGE (I) : 0.04000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 20.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.51000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS REMARK 200 SOFTWARE USED: SHARP, DM, BUCCANEER REMARK 200 STARTING MODEL: NONE REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 33.14 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.84 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 10% I-PROH, 0.1 M HEPES REMARK 280 PH 7.5 . REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 16.71400 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ASP A 9 REMARK 465 ASN A 10 REMARK 465 SER A 102 REMARK 465 ALA A 103 REMARK 465 LEU A 104 REMARK 465 GLN A 105 REMARK 465 GLY A 106 REMARK 465 PHE A 107 REMARK 465 PHE A 108 REMARK 465 GLY A 109 REMARK 465 VAL A 110 REMARK 465 ASP A 111 REMARK 465 ARG A 112 REMARK 465 SER A 113 REMARK 465 ASP A 114 REMARK 465 ARG A 115 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OE2 GLU A 199 NH1 ARG A 203 1.92 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 THR A 140 CA THR A 140 CB 0.165 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 LEU A 147 CB - CG - CD1 ANGL. DEV. = 12.6 DEGREES REMARK 500 ARG A 203 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 THR A 140 -61.89 -29.13 REMARK 500 HIS A 228 24.60 -144.74 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 URE A 1234 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2YH9 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE DIMERIC BAME FROM E. COLI DBREF 2YHC A 9 225 UNP P0AC02 YFIO_ECOLI 29 245 SEQADV 2YHC LEU A 226 UNP P0AC02 EXPRESSION TAG SEQADV 2YHC GLU A 227 UNP P0AC02 EXPRESSION TAG SEQADV 2YHC HIS A 228 UNP P0AC02 EXPRESSION TAG SEQADV 2YHC HIS A 229 UNP P0AC02 EXPRESSION TAG SEQADV 2YHC HIS A 230 UNP P0AC02 EXPRESSION TAG SEQADV 2YHC HIS A 231 UNP P0AC02 EXPRESSION TAG SEQADV 2YHC HIS A 232 UNP P0AC02 EXPRESSION TAG SEQADV 2YHC HIS A 233 UNP P0AC02 EXPRESSION TAG SEQADV 2YHC GLN A 119 UNP P0AC02 HIS 139 CONFLICT SEQRES 1 A 225 ASP ASN PRO PRO ASN GLU ILE TYR ALA THR ALA GLN GLN SEQRES 2 A 225 LYS LEU GLN ASP GLY ASN TRP ARG GLN ALA ILE THR GLN SEQRES 3 A 225 LEU GLU ALA LEU ASP ASN ARG TYR PRO PHE GLY PRO TYR SEQRES 4 A 225 SER GLN GLN VAL GLN LEU ASP LEU ILE TYR ALA TYR TYR SEQRES 5 A 225 LYS ASN ALA ASP LEU PRO LEU ALA GLN ALA ALA ILE ASP SEQRES 6 A 225 ARG PHE ILE ARG LEU ASN PRO THR HIS PRO ASN ILE ASP SEQRES 7 A 225 TYR VAL MET TYR MET ARG GLY LEU THR ASN MET ALA LEU SEQRES 8 A 225 ASP ASP SER ALA LEU GLN GLY PHE PHE GLY VAL ASP ARG SEQRES 9 A 225 SER ASP ARG ASP PRO GLN GLN ALA ARG ALA ALA PHE SER SEQRES 10 A 225 ASP PHE SER LYS LEU VAL ARG GLY TYR PRO ASN SER GLN SEQRES 11 A 225 TYR THR THR ASP ALA THR LYS ARG LEU VAL PHE LEU LYS SEQRES 12 A 225 ASP ARG LEU ALA LYS TYR GLU TYR SER VAL ALA GLU TYR SEQRES 13 A 225 TYR THR GLU ARG GLY ALA TRP VAL ALA VAL VAL ASN ARG SEQRES 14 A 225 VAL GLU GLY MET LEU ARG ASP TYR PRO ASP THR GLN ALA SEQRES 15 A 225 THR ARG ASP ALA LEU PRO LEU MET GLU ASN ALA TYR ARG SEQRES 16 A 225 GLN MET GLN MET ASN ALA GLN ALA GLU LYS VAL ALA LYS SEQRES 17 A 225 ILE ILE ALA ALA ASN SER SER ASN THR LEU GLU HIS HIS SEQRES 18 A 225 HIS HIS HIS HIS HET URE A1234 4 HETNAM URE UREA FORMUL 2 URE C H4 N2 O FORMUL 3 HOH *84(H2 O) HELIX 1 1 PRO A 11 GLY A 26 1 16 HELIX 2 2 ASN A 27 TYR A 42 1 16 HELIX 3 3 TYR A 47 ASN A 62 1 16 HELIX 4 4 ASP A 64 ASN A 79 1 16 HELIX 5 5 ASN A 84 ASP A 101 1 18 HELIX 6 6 PRO A 117 ARG A 132 1 16 HELIX 7 7 TYR A 139 GLY A 169 1 31 HELIX 8 8 ALA A 170 TYR A 185 1 16 HELIX 9 9 THR A 188 MET A 205 1 18 HELIX 10 10 MET A 207 ASN A 221 1 15 SITE 1 AC1 4 ALA A 173 ASN A 176 ARG A 177 HOH A2065 CRYST1 53.112 33.428 57.783 90.00 111.41 90.00 P 1 21 1 2 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 0.018828 0.000000 0.007382 0.00000 SCALE2 0.000000 0.029915 0.000000 0.00000 SCALE3 0.000000 0.000000 0.018589 0.00000 ATOM 1 N PRO A 11 39.669 35.129 5.110 1.00 68.24 N ANISOU 1 N PRO A 11 8739 8287 8903 -1543 83 948 N ATOM 2 CA PRO A 11 40.073 35.378 6.500 1.00 68.47 C ANISOU 2 CA PRO A 11 8784 8238 8994 -1667 -59 812 C ATOM 3 C PRO A 11 39.194 34.579 7.468 1.00 65.96 C ANISOU 3 C PRO A 11 8602 7894 8566 -1521 -121 639 C ATOM 4 O PRO A 11 38.178 35.096 7.963 1.00 65.70 O ANISOU 4 O PRO A 11 8760 7668 8537 -1507 -135 538 O ATOM 5 CB PRO A 11 39.877 36.888 6.670 1.00 70.29 C ANISOU 5 CB PRO A 11 9132 8199 9377 -1850 -83 820 C ATOM 6 CG PRO A 11 38.918 37.311 5.542 1.00 69.77 C ANISOU 6 CG PRO A 11 9168 8023 9319 -1751 32 957 C ATOM 7 CD PRO A 11 39.041 36.301 4.453 1.00 69.33 C ANISOU 7 CD PRO A 11 8993 8232 9116 -1604 133 1067 C ATOM 8 N PRO A 12 39.609 33.334 7.779 1.00 64.79 N ANISOU 8 N PRO A 12 8345 7934 8337 -1414 -153 615 N ATOM 9 CA PRO A 12 38.623 32.339 8.281 1.00 61.56 C ANISOU 9 CA PRO A 12 8053 7518 7818 -1236 -161 516 C ATOM 10 C PRO A 12 37.827 32.834 9.488 1.00 60.46 C ANISOU 10 C PRO A 12 8103 7228 7640 -1287 -237 373 C ATOM 11 O PRO A 12 36.655 32.536 9.602 1.00 58.22 O ANISOU 11 O PRO A 12 7956 6867 7297 -1168 -192 309 O ATOM 12 CB PRO A 12 39.482 31.122 8.645 1.00 61.47 C ANISOU 12 CB PRO A 12 7874 7696 7784 -1162 -217 538 C ATOM 13 CG PRO A 12 40.812 31.352 7.915 1.00 65.47 C ANISOU 13 CG PRO A 12 8149 8343 8385 -1246 -185 654 C ATOM 14 CD PRO A 12 40.997 32.833 7.840 1.00 65.32 C ANISOU 14 CD PRO A 12 8170 8207 8442 -1462 -198 680 C ATOM 15 N ASN A 13 38.440 33.631 10.371 1.00 61.49 N ANISOU 15 N ASN A 13 8237 7323 7802 -1476 -343 307 N ATOM 16 CA ASN A 13 37.670 34.086 11.528 1.00 60.57 C ANISOU 16 CA ASN A 13 8309 7086 7621 -1522 -393 130 C ATOM 17 C ASN A 13 36.544 35.085 11.210 1.00 58.33 C ANISOU 17 C ASN A 13 8196 6547 7417 -1503 -296 63 C ATOM 18 O ASN A 13 35.404 34.939 11.711 1.00 55.94 O ANISOU 18 O ASN A 13 8036 6173 7045 -1400 -254 -50 O ATOM 19 CB ASN A 13 38.547 34.410 12.742 1.00 64.08 C ANISOU 19 CB ASN A 13 8723 7609 8017 -1716 -554 32 C ATOM 20 CG ASN A 13 38.276 33.465 13.896 1.00 67.11 C ANISOU 20 CG ASN A 13 9154 8141 8203 -1651 -635 -32 C ATOM 21 OD1 ASN A 13 38.600 32.268 13.842 1.00 71.30 O ANISOU 21 OD1 ASN A 13 9569 8838 8684 -1531 -662 91 O ATOM 22 ND2 ASN A 13 37.623 33.987 14.942 1.00 69.31 N ANISOU 22 ND2 ASN A 13 9611 8351 8373 -1721 -658 -223 N ATOM 23 N GLU A 14 36.838 36.021 10.304 1.00 58.49 N ANISOU 23 N GLU A 14 8183 6443 7597 -1583 -250 162 N ATOM 24 CA GLU A 14 35.823 36.912 9.766 1.00 56.55 C ANISOU 24 CA GLU A 14 8065 5953 7467 -1532 -160 170 C ATOM 25 C GLU A 14 34.814 36.267 8.808 1.00 52.71 C ANISOU 25 C GLU A 14 7591 5507 6931 -1315 -63 275 C ATOM 26 O GLU A 14 33.665 36.659 8.792 1.00 51.24 O ANISOU 26 O GLU A 14 7520 5160 6788 -1220 -12 229 O ATOM 27 CB GLU A 14 36.417 38.225 9.191 1.00 59.55 C ANISOU 27 CB GLU A 14 8421 6150 8056 -1706 -153 270 C ATOM 28 CG GLU A 14 35.356 39.065 8.480 1.00 62.48 C ANISOU 28 CG GLU A 14 8903 6268 8570 -1617 -64 346 C ATOM 29 CD GLU A 14 35.551 40.589 8.631 1.00 70.54 C ANISOU 29 CD GLU A 14 9997 6962 9845 -1792 -75 323 C ATOM 30 OE1 GLU A 14 36.674 41.094 8.345 1.00 71.49 O ANISOU 30 OE1 GLU A 14 10015 7077 10070 -1994 -109 431 O ATOM 31 OE2 GLU A 14 34.561 41.277 9.015 1.00 71.69 O ANISOU 31 OE2 GLU A 14 10292 6841 10108 -1725 -40 197 O ATOM 32 N ILE A 15 35.241 35.306 7.998 1.00 49.91 N ANISOU 32 N ILE A 15 7107 5364 6492 -1240 -37 402 N ATOM 33 CA ILE A 15 34.287 34.495 7.277 1.00 47.65 C ANISOU 33 CA ILE A 15 6835 5147 6122 -1051 31 441 C ATOM 34 C ILE A 15 33.352 33.765 8.233 1.00 42.45 C ANISOU 34 C ILE A 15 6269 4482 5378 -946 18 288 C ATOM 35 O ILE A 15 32.136 33.695 7.979 1.00 39.99 O ANISOU 35 O ILE A 15 6027 4104 5062 -826 69 270 O ATOM 36 CB ILE A 15 34.991 33.475 6.361 1.00 47.39 C ANISOU 36 CB ILE A 15 6650 5348 6007 -993 67 543 C ATOM 37 CG1 ILE A 15 35.826 34.248 5.337 1.00 52.35 C ANISOU 37 CG1 ILE A 15 7180 6011 6698 -1102 111 715 C ATOM 38 CG2 ILE A 15 33.964 32.627 5.666 1.00 47.07 C ANISOU 38 CG2 ILE A 15 6637 5370 5876 -820 124 539 C ATOM 39 CD1 ILE A 15 35.900 33.548 3.990 1.00 56.00 C ANISOU 39 CD1 ILE A 15 7547 6676 7054 -1003 202 821 C ATOM 40 N TYR A 16 33.902 33.255 9.343 1.00 41.84 N ANISOU 40 N TYR A 16 6180 4486 5230 -999 -53 196 N ATOM 41 CA TYR A 16 33.026 32.541 10.253 1.00 38.77 C ANISOU 41 CA TYR A 16 5876 4112 4742 -914 -53 86 C ATOM 42 C TYR A 16 32.035 33.460 10.893 1.00 38.06 C ANISOU 42 C TYR A 16 5930 3846 4684 -925 -17 -47 C ATOM 43 O TYR A 16 30.860 33.140 10.894 1.00 37.82 O ANISOU 43 O TYR A 16 5952 3783 4634 -805 49 -83 O ATOM 44 CB TYR A 16 33.752 31.745 11.312 1.00 39.31 C ANISOU 44 CB TYR A 16 5905 4326 4706 -959 -143 56 C ATOM 45 CG TYR A 16 32.729 31.016 12.190 1.00 39.73 C ANISOU 45 CG TYR A 16 6053 4397 4647 -877 -122 -21 C ATOM 46 CD1 TYR A 16 32.035 29.883 11.739 1.00 36.37 C ANISOU 46 CD1 TYR A 16 5604 4008 4207 -734 -66 33 C ATOM 47 CD2 TYR A 16 32.443 31.498 13.464 1.00 41.38 C ANISOU 47 CD2 TYR A 16 6373 4588 4761 -960 -148 -157 C ATOM 48 CE1 TYR A 16 31.081 29.258 12.522 1.00 38.55 C ANISOU 48 CE1 TYR A 16 5954 4293 4400 -682 -35 -13 C ATOM 49 CE2 TYR A 16 31.496 30.877 14.252 1.00 43.37 C ANISOU 49 CE2 TYR A 16 6702 4880 4896 -898 -104 -210 C ATOM 50 CZ TYR A 16 30.837 29.744 13.801 1.00 40.83 C ANISOU 50 CZ TYR A 16 6344 4589 4581 -764 -49 -120 C ATOM 51 OH TYR A 16 29.843 29.193 14.584 1.00 39.28 O ANISOU 51 OH TYR A 16 6215 4423 4286 -723 9 -158 O ATOM 52 N ALA A 17 32.495 34.620 11.349 1.00 40.73 N ANISOU 52 N ALA A 17 6318 4060 5098 -1067 -51 -125 N ATOM 53 CA ALA A 17 31.585 35.613 11.914 1.00 42.17 C ANISOU 53 CA ALA A 17 6637 4035 5351 -1067 3 -283 C ATOM 54 C ALA A 17 30.561 36.007 10.886 1.00 41.18 C ANISOU 54 C ALA A 17 6520 3764 5360 -928 91 -191 C ATOM 55 O ALA A 17 29.393 36.130 11.202 1.00 40.59 O ANISOU 55 O ALA A 17 6513 3604 5306 -821 163 -285 O ATOM 56 CB ALA A 17 32.346 36.835 12.479 1.00 45.85 C ANISOU 56 CB ALA A 17 7153 4355 5911 -1262 -53 -401 C ATOM 57 N THR A 18 30.982 36.211 9.639 1.00 41.18 N ANISOU 57 N THR A 18 6439 3760 5446 -929 88 5 N ATOM 58 CA THR A 18 30.000 36.481 8.614 1.00 42.55 C ANISOU 58 CA THR A 18 6609 3849 5710 -794 146 127 C ATOM 59 C THR A 18 28.928 35.400 8.425 1.00 41.75 C ANISOU 59 C THR A 18 6484 3879 5500 -628 182 121 C ATOM 60 O THR A 18 27.699 35.699 8.344 1.00 42.77 O ANISOU 60 O THR A 18 6642 3904 5704 -509 231 101 O ATOM 61 CB THR A 18 30.676 36.742 7.270 1.00 43.82 C ANISOU 61 CB THR A 18 6681 4054 5915 -834 137 362 C ATOM 62 OG1 THR A 18 31.526 37.884 7.391 1.00 48.50 O ANISOU 62 OG1 THR A 18 7291 4480 6659 -1000 113 390 O ATOM 63 CG2 THR A 18 29.607 37.048 6.270 1.00 45.54 C ANISOU 63 CG2 THR A 18 6897 4209 6198 -697 172 504 C ATOM 64 N ALA A 19 29.362 34.140 8.384 1.00 40.28 N ANISOU 64 N ALA A 19 6234 3907 5163 -619 159 134 N ATOM 65 CA ALA A 19 28.422 33.004 8.220 1.00 39.15 C ANISOU 65 CA ALA A 19 6065 3877 4935 -492 187 119 C ATOM 66 C ALA A 19 27.421 32.954 9.383 1.00 39.09 C ANISOU 66 C ALA A 19 6130 3805 4916 -450 231 -34 C ATOM 67 O ALA A 19 26.189 32.677 9.202 1.00 38.59 O ANISOU 67 O ALA A 19 6052 3736 4874 -339 279 -45 O ATOM 68 CB ALA A 19 29.211 31.661 8.098 1.00 37.06 C ANISOU 68 CB ALA A 19 5725 3804 4553 -498 156 143 C ATOM 69 N GLN A 20 27.919 33.277 10.585 1.00 39.10 N ANISOU 69 N GLN A 20 6202 3777 4878 -547 218 -157 N ATOM 70 CA GLN A 20 27.062 33.230 11.780 1.00 40.33 C ANISOU 70 CA GLN A 20 6431 3915 4977 -524 280 -316 C ATOM 71 C GLN A 20 25.950 34.286 11.640 1.00 41.79 C ANISOU 71 C GLN A 20 6650 3909 5321 -436 365 -380 C ATOM 72 O GLN A 20 24.773 34.048 12.009 1.00 41.06 O ANISOU 72 O GLN A 20 6553 3822 5226 -339 451 -450 O ATOM 73 CB GLN A 20 27.887 33.522 13.051 1.00 43.56 C ANISOU 73 CB GLN A 20 6916 4353 5280 -666 237 -450 C ATOM 74 CG GLN A 20 28.367 32.307 13.776 1.00 44.95 C ANISOU 74 CG GLN A 20 7073 4738 5270 -705 182 -422 C ATOM 75 CD GLN A 20 28.889 32.619 15.172 1.00 51.91 C ANISOU 75 CD GLN A 20 8037 5687 6000 -839 138 -565 C ATOM 76 OE1 GLN A 20 29.443 33.711 15.430 1.00 58.34 O ANISOU 76 OE1 GLN A 20 8902 6405 6861 -951 102 -678 O ATOM 77 NE2 GLN A 20 28.736 31.665 16.089 1.00 51.34 N ANISOU 77 NE2 GLN A 20 7981 5787 5740 -846 132 -556 N ATOM 78 N GLN A 21 26.296 35.450 11.064 1.00 41.20 N ANISOU 78 N GLN A 21 6590 3654 5409 -462 346 -336 N ATOM 79 CA GLN A 21 25.266 36.456 10.903 1.00 44.19 C ANISOU 79 CA GLN A 21 6989 3820 5983 -355 421 -372 C ATOM 80 C GLN A 21 24.275 36.031 9.858 1.00 42.92 C ANISOU 80 C GLN A 21 6725 3712 5869 -204 430 -215 C ATOM 81 O GLN A 21 23.102 36.357 9.988 1.00 42.67 O ANISOU 81 O GLN A 21 6671 3593 5949 -78 503 -264 O ATOM 82 CB GLN A 21 25.798 37.874 10.533 1.00 46.47 C ANISOU 82 CB GLN A 21 7323 3850 6486 -416 399 -336 C ATOM 83 CG GLN A 21 26.918 38.471 11.347 1.00 48.33 C ANISOU 83 CG GLN A 21 7644 4006 6714 -604 361 -480 C ATOM 84 CD GLN A 21 27.290 39.892 10.879 1.00 49.28 C ANISOU 84 CD GLN A 21 7801 3821 7103 -666 349 -426 C ATOM 85 OE1 GLN A 21 27.782 40.079 9.729 1.00 47.91 O ANISOU 85 OE1 GLN A 21 7560 3635 7007 -691 298 -171 O ATOM 86 NE2 GLN A 21 27.101 40.901 11.773 1.00 43.73 N ANISOU 86 NE2 GLN A 21 7206 2867 6542 -703 403 -668 N ATOM 87 N LYS A 22 24.756 35.343 8.807 1.00 42.17 N ANISOU 87 N LYS A 22 6558 3770 5693 -219 356 -37 N ATOM 88 CA LYS A 22 23.874 34.889 7.717 1.00 41.61 C ANISOU 88 CA LYS A 22 6388 3791 5631 -101 340 103 C ATOM 89 C LYS A 22 22.902 33.867 8.256 1.00 41.05 C ANISOU 89 C LYS A 22 6277 3838 5483 -36 386 1 C ATOM 90 O LYS A 22 21.703 33.864 7.918 1.00 40.58 O ANISOU 90 O LYS A 22 6140 3778 5502 77 408 28 O ATOM 91 CB LYS A 22 24.690 34.329 6.545 1.00 43.00 C ANISOU 91 CB LYS A 22 6509 4132 5697 -149 267 265 C ATOM 92 CG LYS A 22 25.456 35.436 5.786 1.00 43.22 C ANISOU 92 CG LYS A 22 6548 4055 5818 -208 235 428 C ATOM 93 CD LYS A 22 24.507 36.517 5.351 1.00 50.40 C ANISOU 93 CD LYS A 22 7448 4783 6918 -104 239 536 C ATOM 94 CE LYS A 22 25.150 37.349 4.281 1.00 54.71 C ANISOU 94 CE LYS A 22 7982 5281 7524 -156 196 779 C ATOM 95 NZ LYS A 22 24.747 38.783 4.279 1.00 60.04 N ANISOU 95 NZ LYS A 22 8693 5650 8471 -110 206 872 N ATOM 96 N LEU A 23 23.412 33.029 9.138 1.00 40.11 N ANISOU 96 N LEU A 23 6198 3817 5223 -115 398 -101 N ATOM 97 CA LEU A 23 22.542 32.004 9.806 1.00 42.28 C ANISOU 97 CA LEU A 23 6443 4197 5425 -82 455 -180 C ATOM 98 C LEU A 23 21.483 32.725 10.689 1.00 45.61 C ANISOU 98 C LEU A 23 6880 4514 5935 -15 569 -311 C ATOM 99 O LEU A 23 20.297 32.367 10.719 1.00 43.83 O ANISOU 99 O LEU A 23 6569 4331 5752 67 630 -324 O ATOM 100 CB LEU A 23 23.446 31.110 10.657 1.00 42.56 C ANISOU 100 CB LEU A 23 6530 4339 5302 -186 436 -224 C ATOM 101 CG LEU A 23 23.464 29.583 10.527 1.00 43.28 C ANISOU 101 CG LEU A 23 6570 4569 5307 -196 411 -173 C ATOM 102 CD1 LEU A 23 23.047 29.047 9.156 1.00 42.86 C ANISOU 102 CD1 LEU A 23 6421 4563 5301 -136 370 -90 C ATOM 103 CD2 LEU A 23 24.798 28.980 11.036 1.00 45.35 C ANISOU 103 CD2 LEU A 23 6869 4900 5462 -285 350 -151 C ATOM 104 N GLN A 24 21.902 33.782 11.378 1.00 45.45 N ANISOU 104 N GLN A 24 6956 4354 5959 -51 604 -423 N ATOM 105 CA GLN A 24 20.958 34.508 12.223 1.00 50.43 C ANISOU 105 CA GLN A 24 7606 4876 6679 23 736 -589 C ATOM 106 C GLN A 24 19.862 35.229 11.397 1.00 51.41 C ANISOU 106 C GLN A 24 7625 4864 7044 189 765 -514 C ATOM 107 O GLN A 24 18.692 35.269 11.833 1.00 54.42 O ANISOU 107 O GLN A 24 7934 5245 7498 296 880 -601 O ATOM 108 CB GLN A 24 21.711 35.468 13.149 1.00 51.01 C ANISOU 108 CB GLN A 24 7818 4820 6743 -69 763 -768 C ATOM 109 CG GLN A 24 20.889 36.008 14.274 1.00 57.04 C ANISOU 109 CG GLN A 24 8624 5523 7526 -18 923 -1007 C ATOM 110 CD GLN A 24 20.573 35.008 15.401 1.00 59.25 C ANISOU 110 CD GLN A 24 8918 6042 7551 -71 1006 -1103 C ATOM 111 OE1 GLN A 24 21.194 35.059 16.475 1.00 64.70 O ANISOU 111 OE1 GLN A 24 9724 6809 8052 -194 1019 -1256 O ATOM 112 NE2 GLN A 24 19.574 34.142 15.184 1.00 59.83 N ANISOU 112 NE2 GLN A 24 8870 6242 7622 11 1062 -1010 N ATOM 113 N ASP A 25 20.238 35.754 10.230 1.00 50.20 N ANISOU 113 N ASP A 25 7448 4621 7005 210 662 -338 N ATOM 114 CA ASP A 25 19.292 36.292 9.241 1.00 51.58 C ANISOU 114 CA ASP A 25 7504 4713 7382 364 640 -187 C ATOM 115 C ASP A 25 18.409 35.228 8.596 1.00 48.13 C ANISOU 115 C ASP A 25 6918 4491 6878 422 600 -87 C ATOM 116 O ASP A 25 17.410 35.566 7.961 1.00 48.95 O ANISOU 116 O ASP A 25 6892 4571 7134 556 582 16 O ATOM 117 CB ASP A 25 20.014 36.951 8.042 1.00 53.35 C ANISOU 117 CB ASP A 25 7738 4851 7682 342 521 35 C ATOM 118 CG ASP A 25 20.837 38.178 8.391 1.00 59.37 C ANISOU 118 CG ASP A 25 8623 5350 8585 278 538 -12 C ATOM 119 OD1 ASP A 25 20.537 38.924 9.374 1.00 59.35 O ANISOU 119 OD1 ASP A 25 8685 5149 8718 312 643 -217 O ATOM 120 OD2 ASP A 25 21.788 38.408 7.583 1.00 62.29 O ANISOU 120 OD2 ASP A 25 9016 5716 8935 187 447 162 O ATOM 121 N GLY A 26 18.806 33.958 8.648 1.00 43.10 N ANISOU 121 N GLY A 26 6287 4056 6032 319 566 -98 N ATOM 122 CA GLY A 26 18.045 32.985 7.952 1.00 41.77 C ANISOU 122 CA GLY A 26 5986 4061 5822 348 515 -20 C ATOM 123 C GLY A 26 18.435 32.950 6.499 1.00 38.94 C ANISOU 123 C GLY A 26 5590 3779 5427 341 375 162 C ATOM 124 O GLY A 26 17.636 32.490 5.667 1.00 40.38 O ANISOU 124 O GLY A 26 5644 4090 5608 387 306 243 O ATOM 125 N ASN A 27 19.640 33.459 6.200 1.00 38.01 N ANISOU 125 N ASN A 27 5574 3600 5269 274 334 225 N ATOM 126 CA ASN A 27 20.147 33.412 4.806 1.00 38.30 C ANISOU 126 CA ASN A 27 5581 3747 5225 249 223 405 C ATOM 127 C ASN A 27 20.897 32.095 4.671 1.00 34.77 C ANISOU 127 C ASN A 27 5153 3479 4580 148 202 341 C ATOM 128 O ASN A 27 22.174 32.047 4.742 1.00 33.22 O ANISOU 128 O ASN A 27 5032 3285 4304 58 203 339 O ATOM 129 CB ASN A 27 21.080 34.585 4.501 1.00 38.45 C ANISOU 129 CB ASN A 27 5678 3620 5313 215 207 525 C ATOM 130 CG ASN A 27 21.385 34.700 2.996 1.00 44.31 C ANISOU 130 CG ASN A 27 6371 4498 5968 204 108 753 C ATOM 131 OD1 ASN A 27 21.299 33.704 2.273 1.00 43.54 O ANISOU 131 OD1 ASN A 27 6214 4632 5696 185 57 759 O ATOM 132 ND2 ASN A 27 21.748 35.933 2.511 1.00 45.14 N ANISOU 132 ND2 ASN A 27 6503 4457 6192 207 86 943 N ATOM 133 N TRP A 28 20.118 31.000 4.589 1.00 35.38 N ANISOU 133 N TRP A 28 5152 3685 4606 159 191 275 N ATOM 134 CA TRP A 28 20.715 29.675 4.580 1.00 32.65 C ANISOU 134 CA TRP A 28 4824 3456 4126 78 185 192 C ATOM 135 C TRP A 28 21.660 29.466 3.423 1.00 32.74 C ANISOU 135 C TRP A 28 4840 3590 4009 37 124 261 C ATOM 136 O TRP A 28 22.722 28.874 3.617 1.00 33.58 O ANISOU 136 O TRP A 28 4994 3720 4045 -23 146 209 O ATOM 137 CB TRP A 28 19.632 28.584 4.490 1.00 32.88 C ANISOU 137 CB TRP A 28 4757 3580 4156 84 172 120 C ATOM 138 CG TRP A 28 18.438 28.874 5.404 1.00 33.29 C ANISOU 138 CG TRP A 28 4753 3556 4339 138 242 80 C ATOM 139 CD1 TRP A 28 17.140 28.989 5.023 1.00 36.92 C ANISOU 139 CD1 TRP A 28 5073 4066 4890 203 214 111 C ATOM 140 CD2 TRP A 28 18.474 29.132 6.815 1.00 33.99 C ANISOU 140 CD2 TRP A 28 4910 3535 4471 133 357 -1 C ATOM 141 NE1 TRP A 28 16.329 29.227 6.134 1.00 36.49 N ANISOU 141 NE1 TRP A 28 4980 3932 4950 246 328 46 N ATOM 142 CE2 TRP A 28 17.143 29.345 7.232 1.00 38.14 C ANISOU 142 CE2 TRP A 28 5330 4049 5114 201 421 -28 C ATOM 143 CE3 TRP A 28 19.501 29.119 7.786 1.00 31.49 C ANISOU 143 CE3 TRP A 28 4722 3159 4085 67 408 -58 C ATOM 144 CZ2 TRP A 28 16.808 29.633 8.565 1.00 40.78 C ANISOU 144 CZ2 TRP A 28 5697 4312 5485 213 559 -125 C ATOM 145 CZ3 TRP A 28 19.166 29.397 9.115 1.00 34.38 C ANISOU 145 CZ3 TRP A 28 5130 3466 4467 67 519 -148 C ATOM 146 CH2 TRP A 28 17.826 29.658 9.482 1.00 37.58 C ANISOU 146 CH2 TRP A 28 5441 3862 4976 141 606 -189 C ATOM 147 N ARG A 29 21.280 29.908 2.226 1.00 33.10 N ANISOU 147 N ARG A 29 4825 3734 4016 71 52 383 N ATOM 148 CA ARG A 29 22.112 29.666 1.109 1.00 35.37 C ANISOU 148 CA ARG A 29 5113 4182 4143 26 16 437 C ATOM 149 C ARG A 29 23.500 30.234 1.268 1.00 35.33 C ANISOU 149 C ARG A 29 5179 4118 4125 -28 63 497 C ATOM 150 O ARG A 29 24.461 29.547 0.967 1.00 32.93 O ANISOU 150 O ARG A 29 4880 3919 3713 -78 88 443 O ATOM 151 CB ARG A 29 21.496 30.233 -0.152 1.00 37.42 C ANISOU 151 CB ARG A 29 5303 4579 4335 63 -76 601 C ATOM 152 CG ARG A 29 20.754 29.235 -0.940 1.00 44.96 C ANISOU 152 CG ARG A 29 6177 5739 5166 55 -150 517 C ATOM 153 CD ARG A 29 20.055 29.960 -2.142 1.00 49.45 C ANISOU 153 CD ARG A 29 6665 6471 5654 95 -271 721 C ATOM 154 NE ARG A 29 20.865 31.078 -2.649 1.00 56.58 N ANISOU 154 NE ARG A 29 7617 7363 6519 92 -264 948 N ATOM 155 CZ ARG A 29 20.404 32.126 -3.348 1.00 60.48 C ANISOU 155 CZ ARG A 29 8065 7888 7027 145 -349 1211 C ATOM 156 NH1 ARG A 29 19.111 32.246 -3.656 1.00 58.93 N ANISOU 156 NH1 ARG A 29 7755 7755 6880 222 -463 1284 N ATOM 157 NH2 ARG A 29 21.252 33.070 -3.752 1.00 62.77 N ANISOU 157 NH2 ARG A 29 8407 8144 7298 117 -326 1426 N ATOM 158 N GLN A 30 23.610 31.530 1.631 1.00 36.30 N ANISOU 158 N GLN A 30 5341 4075 4374 -20 75 611 N ATOM 159 CA GLN A 30 24.959 32.151 1.817 1.00 35.53 C ANISOU 159 CA GLN A 30 5300 3910 4290 -103 111 670 C ATOM 160 C GLN A 30 25.721 31.570 2.969 1.00 33.78 C ANISOU 160 C GLN A 30 5122 3634 4081 -158 157 512 C ATOM 161 O GLN A 30 26.957 31.411 2.918 1.00 34.07 O ANISOU 161 O GLN A 30 5154 3725 4065 -231 174 520 O ATOM 162 CB GLN A 30 24.807 33.696 1.988 1.00 36.60 C ANISOU 162 CB GLN A 30 5473 3831 4602 -93 109 810 C ATOM 163 CG GLN A 30 24.529 34.365 0.726 1.00 41.84 C ANISOU 163 CG GLN A 30 6092 4562 5241 -64 55 1046 C ATOM 164 CD GLN A 30 25.027 35.850 0.680 1.00 44.12 C ANISOU 164 CD GLN A 30 6426 4637 5701 -107 63 1237 C ATOM 165 OE1 GLN A 30 25.845 36.302 1.512 1.00 47.93 O ANISOU 165 OE1 GLN A 30 6972 4949 6290 -193 109 1163 O ATOM 166 NE2 GLN A 30 24.572 36.569 -0.294 1.00 50.59 N ANISOU 166 NE2 GLN A 30 7209 5468 6545 -61 8 1487 N ATOM 167 N ALA A 31 25.010 31.249 4.056 1.00 31.70 N ANISOU 167 N ALA A 31 4885 3277 3881 -124 177 381 N ATOM 168 CA ALA A 31 25.677 30.677 5.191 1.00 32.31 C ANISOU 168 CA ALA A 31 5006 3329 3944 -178 203 263 C ATOM 169 C ALA A 31 26.282 29.284 4.776 1.00 30.09 C ANISOU 169 C ALA A 31 4675 3203 3556 -187 197 222 C ATOM 170 O ALA A 31 27.456 29.015 5.106 1.00 28.52 O ANISOU 170 O ALA A 31 4474 3029 3334 -240 199 213 O ATOM 171 CB ALA A 31 24.698 30.492 6.325 1.00 31.15 C ANISOU 171 CB ALA A 31 4890 3100 3846 -143 240 151 C ATOM 172 N ILE A 32 25.534 28.480 4.020 1.00 29.82 N ANISOU 172 N ILE A 32 4591 3264 3475 -138 185 193 N ATOM 173 CA ILE A 32 26.016 27.157 3.534 1.00 26.92 C ANISOU 173 CA ILE A 32 4183 3009 3038 -136 190 117 C ATOM 174 C ILE A 32 27.258 27.356 2.672 1.00 28.26 C ANISOU 174 C ILE A 32 4318 3290 3129 -163 206 175 C ATOM 175 O ILE A 32 28.299 26.692 2.865 1.00 28.43 O ANISOU 175 O ILE A 32 4312 3340 3151 -173 232 132 O ATOM 176 CB ILE A 32 24.910 26.397 2.727 1.00 27.31 C ANISOU 176 CB ILE A 32 4186 3142 3050 -102 164 51 C ATOM 177 CG1 ILE A 32 23.844 25.887 3.813 1.00 25.67 C ANISOU 177 CG1 ILE A 32 3987 2824 2944 -94 173 -17 C ATOM 178 CG2 ILE A 32 25.467 25.269 1.887 1.00 29.48 C ANISOU 178 CG2 ILE A 32 4423 3533 3247 -102 175 -49 C ATOM 179 CD1 ILE A 32 22.483 25.495 3.185 1.00 30.18 C ANISOU 179 CD1 ILE A 32 4489 3456 3520 -77 134 -59 C ATOM 180 N THR A 33 27.232 28.367 1.802 1.00 28.61 N ANISOU 180 N THR A 33 4354 3392 3125 -177 195 301 N ATOM 181 CA THR A 33 28.400 28.591 0.988 1.00 30.58 C ANISOU 181 CA THR A 33 4560 3771 3290 -219 231 376 C ATOM 182 C THR A 33 29.651 28.824 1.783 1.00 29.66 C ANISOU 182 C THR A 33 4433 3588 3247 -277 256 392 C ATOM 183 O THR A 33 30.724 28.271 1.476 1.00 31.35 O ANISOU 183 O THR A 33 4575 3913 3421 -288 301 368 O ATOM 184 CB THR A 33 28.100 29.719 -0.029 1.00 30.84 C ANISOU 184 CB THR A 33 4589 3870 3260 -237 210 561 C ATOM 185 OG1 THR A 33 27.124 29.211 -0.950 1.00 32.97 O ANISOU 185 OG1 THR A 33 4835 4285 3409 -188 172 530 O ATOM 186 CG2 THR A 33 29.308 30.102 -0.845 1.00 33.97 C ANISOU 186 CG2 THR A 33 4935 4409 3563 -303 266 679 C ATOM 187 N GLN A 34 29.580 29.806 2.681 1.00 31.90 N ANISOU 187 N GLN A 34 4775 3707 3639 -323 228 443 N ATOM 188 CA GLN A 34 30.752 30.181 3.453 1.00 33.11 C ANISOU 188 CA GLN A 34 4914 3809 3856 -409 226 457 C ATOM 189 C GLN A 34 31.188 29.073 4.402 1.00 31.62 C ANISOU 189 C GLN A 34 4706 3630 3678 -388 212 343 C ATOM 190 O GLN A 34 32.418 28.856 4.558 1.00 31.51 O ANISOU 190 O GLN A 34 4613 3684 3678 -430 212 360 O ATOM 191 CB GLN A 34 30.400 31.421 4.248 1.00 34.97 C ANISOU 191 CB GLN A 34 5235 3849 4202 -464 196 483 C ATOM 192 CG GLN A 34 29.968 32.490 3.312 1.00 39.53 C ANISOU 192 CG GLN A 34 5825 4384 4811 -468 202 633 C ATOM 193 CD GLN A 34 31.134 33.291 2.847 1.00 46.24 C ANISOU 193 CD GLN A 34 6629 5251 5691 -586 218 774 C ATOM 194 OE1 GLN A 34 32.234 32.776 2.734 1.00 54.03 O ANISOU 194 OE1 GLN A 34 7530 6374 6624 -636 241 768 O ATOM 195 NE2 GLN A 34 30.930 34.561 2.655 1.00 41.44 N ANISOU 195 NE2 GLN A 34 6064 4484 5197 -633 210 904 N ATOM 196 N LEU A 35 30.233 28.394 5.007 1.00 29.56 N ANISOU 196 N LEU A 35 4499 3311 3423 -328 199 252 N ATOM 197 CA LEU A 35 30.582 27.248 5.911 1.00 29.93 C ANISOU 197 CA LEU A 35 4529 3357 3485 -305 181 186 C ATOM 198 C LEU A 35 31.231 26.084 5.101 1.00 29.72 C ANISOU 198 C LEU A 35 4405 3437 3450 -240 215 156 C ATOM 199 O LEU A 35 32.248 25.497 5.573 1.00 30.98 O ANISOU 199 O LEU A 35 4496 3621 3655 -232 201 165 O ATOM 200 CB LEU A 35 29.397 26.761 6.731 1.00 28.12 C ANISOU 200 CB LEU A 35 4373 3045 3267 -271 176 122 C ATOM 201 CG LEU A 35 28.870 27.793 7.795 1.00 28.61 C ANISOU 201 CG LEU A 35 4527 3008 3337 -324 166 108 C ATOM 202 CD1 LEU A 35 27.462 27.459 8.189 1.00 31.59 C ANISOU 202 CD1 LEU A 35 4946 3336 3720 -277 199 53 C ATOM 203 CD2 LEU A 35 29.784 27.996 9.010 1.00 35.24 C ANISOU 203 CD2 LEU A 35 5388 3847 4154 -406 117 105 C ATOM 204 N GLU A 36 30.699 25.758 3.944 1.00 30.75 N ANISOU 204 N GLU A 36 4520 3635 3527 -192 256 114 N ATOM 205 CA GLU A 36 31.309 24.669 3.111 1.00 31.15 C ANISOU 205 CA GLU A 36 4485 3786 3566 -127 311 34 C ATOM 206 C GLU A 36 32.759 25.005 2.728 1.00 31.41 C ANISOU 206 C GLU A 36 4410 3935 3590 -150 355 96 C ATOM 207 O GLU A 36 33.617 24.165 2.740 1.00 31.95 O ANISOU 207 O GLU A 36 4386 4036 3720 -93 389 50 O ATOM 208 CB GLU A 36 30.447 24.413 1.864 1.00 32.72 C ANISOU 208 CB GLU A 36 4695 4076 3662 -99 340 -45 C ATOM 209 CG GLU A 36 29.194 23.543 2.237 1.00 33.28 C ANISOU 209 CG GLU A 36 4820 4038 3787 -69 305 -149 C ATOM 210 CD GLU A 36 28.377 23.184 0.989 1.00 36.96 C ANISOU 210 CD GLU A 36 5279 4616 4147 -59 309 -254 C ATOM 211 OE1 GLU A 36 28.731 23.686 -0.091 1.00 41.71 O ANISOU 211 OE1 GLU A 36 5850 5391 4606 -71 336 -227 O ATOM 212 OE2 GLU A 36 27.368 22.430 1.034 1.00 39.48 O ANISOU 212 OE2 GLU A 36 5617 4875 4510 -55 280 -357 O ATOM 213 N ALA A 37 33.013 26.254 2.376 1.00 32.04 N ANISOU 213 N ALA A 37 4490 4068 3618 -234 359 213 N ATOM 214 CA ALA A 37 34.360 26.687 1.989 1.00 32.60 C ANISOU 214 CA ALA A 37 4441 4260 3688 -285 409 296 C ATOM 215 C ALA A 37 35.308 26.582 3.189 1.00 34.05 C ANISOU 215 C ALA A 37 4560 4383 3994 -315 350 321 C ATOM 216 O ALA A 37 36.462 26.206 3.018 1.00 37.05 O ANISOU 216 O ALA A 37 4792 4868 4419 -298 392 333 O ATOM 217 CB ALA A 37 34.302 28.130 1.434 1.00 35.75 C ANISOU 217 CB ALA A 37 4867 4685 4032 -393 415 449 C ATOM 218 N LEU A 38 34.837 26.892 4.390 1.00 32.39 N ANISOU 218 N LEU A 38 4447 4030 3829 -357 256 327 N ATOM 219 CA LEU A 38 35.656 26.688 5.569 1.00 34.03 C ANISOU 219 CA LEU A 38 4600 4217 4112 -389 176 349 C ATOM 220 C LEU A 38 35.911 25.191 5.830 1.00 34.26 C ANISOU 220 C LEU A 38 4559 4254 4204 -260 175 300 C ATOM 221 O LEU A 38 36.994 24.798 6.180 1.00 35.06 O ANISOU 221 O LEU A 38 4525 4414 4382 -242 145 345 O ATOM 222 CB LEU A 38 35.004 27.324 6.785 1.00 34.62 C ANISOU 222 CB LEU A 38 4810 4167 4176 -466 88 340 C ATOM 223 CG LEU A 38 35.106 28.842 6.958 1.00 38.56 C ANISOU 223 CG LEU A 38 5361 4608 4681 -610 61 379 C ATOM 224 CD1 LEU A 38 34.240 29.284 8.099 1.00 41.51 C ANISOU 224 CD1 LEU A 38 5885 4855 5034 -649 7 308 C ATOM 225 CD2 LEU A 38 36.575 29.260 7.238 1.00 44.41 C ANISOU 225 CD2 LEU A 38 5966 5433 5476 -727 8 443 C ATOM 226 N ASP A 39 34.873 24.396 5.651 1.00 32.82 N ANISOU 226 N ASP A 39 4462 3996 4011 -174 204 218 N ATOM 227 CA ASP A 39 35.017 22.968 5.943 1.00 34.81 C ANISOU 227 CA ASP A 39 4667 4196 4365 -57 203 179 C ATOM 228 C ASP A 39 35.928 22.325 4.898 1.00 38.03 C ANISOU 228 C ASP A 39 4922 4697 4831 39 300 122 C ATOM 229 O ASP A 39 36.724 21.432 5.260 1.00 37.51 O ANISOU 229 O ASP A 39 4740 4608 4902 132 289 139 O ATOM 230 CB ASP A 39 33.640 22.324 6.038 1.00 34.34 C ANISOU 230 CB ASP A 39 4732 4014 4300 -21 209 103 C ATOM 231 CG ASP A 39 33.734 20.828 6.475 1.00 42.93 C ANISOU 231 CG ASP A 39 5786 4992 5534 84 200 88 C ATOM 232 OD1 ASP A 39 34.347 20.543 7.555 1.00 45.60 O ANISOU 232 OD1 ASP A 39 6085 5304 5937 90 120 206 O ATOM 233 OD2 ASP A 39 33.297 20.017 5.634 1.00 46.33 O ANISOU 233 OD2 ASP A 39 6217 5376 6012 154 270 -39 O ATOM 234 N ASN A 40 35.852 22.797 3.649 1.00 37.45 N ANISOU 234 N ASN A 40 4838 4739 4654 21 396 67 N ATOM 235 CA AASN A 40 36.846 22.427 2.539 0.50 45.21 C ANISOU 235 CA AASN A 40 5660 5877 5641 91 525 4 C ATOM 236 CA BASN A 40 36.697 22.196 2.694 0.50 44.77 C ANISOU 236 CA BASN A 40 5621 5781 5608 109 512 -11 C ATOM 237 C ASN A 40 38.221 22.641 2.938 1.00 44.90 C ANISOU 237 C ASN A 40 5446 5918 5698 81 515 108 C ATOM 238 O ASN A 40 39.086 21.820 2.756 1.00 45.70 O ANISOU 238 O ASN A 40 5388 6057 5917 196 578 65 O ATOM 239 CB AASN A 40 36.777 23.260 1.189 0.50 46.14 C ANISOU 239 CB AASN A 40 5777 6182 5573 25 627 -1 C ATOM 240 CB BASN A 40 36.106 22.394 1.233 0.50 43.53 C ANISOU 240 CB BASN A 40 5511 5754 5275 100 619 -118 C ATOM 241 CG AASN A 40 37.766 22.691 0.044 0.50 54.03 C ANISOU 241 CG AASN A 40 6607 7375 6548 109 796 -102 C ATOM 242 CG BASN A 40 34.705 21.742 1.001 0.50 49.92 C ANISOU 242 CG BASN A 40 6461 6460 6045 131 598 -256 C ATOM 243 OD1AASN A 40 37.749 21.496 -0.264 0.50 60.47 O ANISOU 243 OD1AASN A 40 7393 8154 7430 241 863 -280 O ATOM 244 OD1BASN A 40 34.393 20.669 1.541 0.50 59.61 O ANISOU 244 OD1BASN A 40 7712 7525 7412 206 571 -339 O ATOM 245 ND2AASN A 40 38.617 23.552 -0.503 0.50 58.71 N ANISOU 245 ND2AASN A 40 7086 8155 7065 28 870 10 N ATOM 246 ND2BASN A 40 33.906 22.373 0.120 0.50 54.78 N ANISOU 246 ND2BASN A 40 7152 7183 6480 70 609 -267 N ATOM 247 N ARG A 41 38.462 23.866 3.388 1.00 38.99 N ANISOU 247 N ARG A 41 4735 5107 4973 -669 327 -119 N ATOM 248 CA ARG A 41 39.833 24.338 3.628 1.00 40.27 C ANISOU 248 CA ARG A 41 4817 5300 5182 -753 341 -117 C ATOM 249 C ARG A 41 40.445 23.719 4.931 1.00 41.43 C ANISOU 249 C ARG A 41 4903 5389 5451 -709 264 -163 C ATOM 250 O ARG A 41 41.629 23.338 4.955 1.00 41.44 O ANISOU 250 O ARG A 41 4768 5453 5525 -728 275 -216 O ATOM 251 CB ARG A 41 39.854 25.882 3.708 1.00 42.04 C ANISOU 251 CB ARG A 41 5135 5465 5374 -856 338 -5 C ATOM 252 CG ARG A 41 41.231 26.441 3.960 1.00 46.29 C ANISOU 252 CG ARG A 41 5590 6030 5970 -961 350 -2 C ATOM 253 CD ARG A 41 41.207 27.974 3.957 1.00 56.23 C ANISOU 253 CD ARG A 41 6939 7203 7223 -1072 349 108 C ATOM 254 NE ARG A 41 40.813 28.435 2.641 1.00 63.13 N ANISOU 254 NE ARG A 41 7848 8142 7998 -1119 418 203 N ATOM 255 CZ ARG A 41 41.685 28.835 1.728 1.00 69.90 C ANISOU 255 CZ ARG A 41 8630 9115 8815 -1235 498 254 C ATOM 256 NH1 ARG A 41 42.983 28.824 2.030 1.00 70.49 N ANISOU 256 NH1 ARG A 41 8583 9238 8961 -1308 519 203 N ATOM 257 NH2 ARG A 41 41.271 29.243 0.528 1.00 72.15 N ANISOU 257 NH2 ARG A 41 8950 9481 8983 -1284 554 363 N ATOM 258 N TYR A 42 39.664 23.642 6.000 1.00 39.73 N ANISOU 258 N TYR A 42 4774 5071 5252 -655 186 -136 N ATOM 259 CA TYR A 42 40.191 23.114 7.254 1.00 39.53 C ANISOU 259 CA TYR A 42 4697 5013 5310 -625 103 -150 C ATOM 260 C TYR A 42 39.275 22.002 7.743 1.00 39.65 C ANISOU 260 C TYR A 42 4735 4977 5355 -520 58 -153 C ATOM 261 O TYR A 42 38.544 22.159 8.729 1.00 41.36 O ANISOU 261 O TYR A 42 5038 5135 5541 -502 1 -109 O ATOM 262 CB TYR A 42 40.286 24.154 8.314 1.00 40.26 C ANISOU 262 CB TYR A 42 4863 5054 5382 -689 44 -109 C ATOM 263 CG TYR A 42 40.987 25.417 7.886 1.00 43.73 C ANISOU 263 CG TYR A 42 5304 5504 5808 -807 84 -92 C ATOM 264 CD1 TYR A 42 42.384 25.477 7.817 1.00 48.60 C ANISOU 264 CD1 TYR A 42 5791 6191 6484 -876 90 -118 C ATOM 265 CD2 TYR A 42 40.252 26.560 7.555 1.00 47.56 C ANISOU 265 CD2 TYR A 42 5910 5919 6240 -853 113 -42 C ATOM 266 CE1 TYR A 42 43.022 26.614 7.380 1.00 50.55 C ANISOU 266 CE1 TYR A 42 6032 6446 6729 -1000 133 -92 C ATOM 267 CE2 TYR A 42 40.872 27.691 7.170 1.00 46.22 C ANISOU 267 CE2 TYR A 42 5743 5736 6083 -968 144 -7 C ATOM 268 CZ TYR A 42 42.251 27.722 7.065 1.00 53.53 C ANISOU 268 CZ TYR A 42 6543 6739 7059 -1049 159 -29 C ATOM 269 OH TYR A 42 42.862 28.891 6.677 1.00 59.39 O ANISOU 269 OH TYR A 42 7282 7460 7823 -1181 194 18 O ATOM 270 N PRO A 43 39.318 20.852 7.074 1.00 39.76 N ANISOU 270 N PRO A 43 4658 5014 5433 -454 86 -213 N ATOM 271 CA PRO A 43 38.298 19.872 7.490 1.00 40.04 C ANISOU 271 CA PRO A 43 4726 4979 5508 -368 46 -204 C ATOM 272 C PRO A 43 38.579 19.168 8.823 1.00 39.40 C ANISOU 272 C PRO A 43 4608 4847 5516 -330 -54 -149 C ATOM 273 O PRO A 43 37.680 18.524 9.361 1.00 37.40 O ANISOU 273 O PRO A 43 4397 4533 5280 -281 -91 -107 O ATOM 274 CB PRO A 43 38.369 18.813 6.354 1.00 41.94 C ANISOU 274 CB PRO A 43 4866 5248 5820 -315 103 -308 C ATOM 275 CG PRO A 43 39.768 18.859 5.920 1.00 41.25 C ANISOU 275 CG PRO A 43 4649 5240 5785 -347 138 -368 C ATOM 276 CD PRO A 43 40.109 20.373 5.925 1.00 41.35 C ANISOU 276 CD PRO A 43 4732 5302 5677 -455 161 -304 C ATOM 277 N PHE A 44 39.804 19.236 9.308 1.00 36.66 N ANISOU 277 N PHE A 44 4169 4533 5225 -356 -98 -142 N ATOM 278 CA PHE A 44 40.128 18.714 10.637 1.00 37.13 C ANISOU 278 CA PHE A 44 4195 4570 5343 -332 -211 -63 C ATOM 279 C PHE A 44 40.826 19.781 11.451 1.00 36.36 C ANISOU 279 C PHE A 44 4117 4531 5169 -418 -260 -35 C ATOM 280 O PHE A 44 41.703 19.461 12.271 1.00 38.24 O ANISOU 280 O PHE A 44 4266 4799 5465 -418 -352 5 O ATOM 281 CB PHE A 44 40.983 17.443 10.546 1.00 38.10 C ANISOU 281 CB PHE A 44 4152 4669 5657 -259 -252 -82 C ATOM 282 CG PHE A 44 40.213 16.280 10.003 1.00 41.43 C ANISOU 282 CG PHE A 44 4555 5005 6180 -175 -227 -114 C ATOM 283 CD1 PHE A 44 39.298 15.618 10.808 1.00 47.48 C ANISOU 283 CD1 PHE A 44 5380 5693 6967 -138 -290 -14 C ATOM 284 CD2 PHE A 44 40.358 15.889 8.697 1.00 45.55 C ANISOU 284 CD2 PHE A 44 5003 5536 6768 -145 -135 -249 C ATOM 285 CE1 PHE A 44 38.553 14.557 10.295 1.00 51.34 C ANISOU 285 CE1 PHE A 44 5850 6088 7570 -73 -266 -49 C ATOM 286 CE2 PHE A 44 39.651 14.774 8.183 1.00 42.70 C ANISOU 286 CE2 PHE A 44 4615 5090 6517 -72 -116 -308 C ATOM 287 CZ PHE A 44 38.743 14.140 8.984 1.00 49.08 C ANISOU 287 CZ PHE A 44 5482 5797 7367 -39 -184 -205 C ATOM 288 N GLY A 45 40.413 21.033 11.241 1.00 34.28 N ANISOU 288 N GLY A 45 3964 4276 4787 -489 -208 -54 N ATOM 289 CA GLY A 45 40.901 22.178 12.011 1.00 37.37 C ANISOU 289 CA GLY A 45 4390 4699 5109 -580 -248 -52 C ATOM 290 C GLY A 45 40.294 22.270 13.420 1.00 36.23 C ANISOU 290 C GLY A 45 4326 4560 4878 -584 -329 -5 C ATOM 291 O GLY A 45 39.323 21.521 13.762 1.00 36.48 O ANISOU 291 O GLY A 45 4403 4566 4891 -519 -341 44 O ATOM 292 N PRO A 46 40.865 23.144 14.273 1.00 36.66 N ANISOU 292 N PRO A 46 4390 4663 4877 -666 -385 -26 N ATOM 293 CA PRO A 46 40.373 23.336 15.660 1.00 38.04 C ANISOU 293 CA PRO A 46 4633 4885 4937 -687 -457 -8 C ATOM 294 C PRO A 46 38.897 23.734 15.713 1.00 37.12 C ANISOU 294 C PRO A 46 4654 4716 4733 -665 -395 -25 C ATOM 295 O PRO A 46 38.185 23.388 16.733 1.00 40.36 O ANISOU 295 O PRO A 46 5108 5177 5051 -649 -433 11 O ATOM 296 CB PRO A 46 41.234 24.524 16.193 1.00 37.23 C ANISOU 296 CB PRO A 46 4520 4828 4798 -799 -497 -84 C ATOM 297 CG PRO A 46 41.707 25.225 14.995 1.00 36.63 C ANISOU 297 CG PRO A 46 4425 4688 4804 -841 -415 -130 C ATOM 298 CD PRO A 46 41.944 24.126 13.958 1.00 37.16 C ANISOU 298 CD PRO A 46 4403 4747 4970 -762 -373 -84 C ATOM 299 N TYR A 47 38.444 24.378 14.642 1.00 35.84 N ANISOU 299 N TYR A 47 4547 4470 4600 -664 -303 -67 N ATOM 300 CA TYR A 47 37.013 24.857 14.616 1.00 34.89 C ANISOU 300 CA TYR A 47 4546 4292 4419 -635 -245 -88 C ATOM 301 C TYR A 47 36.103 24.020 13.744 1.00 33.02 C ANISOU 301 C TYR A 47 4318 4013 4215 -550 -192 -44 C ATOM 302 O TYR A 47 35.000 24.434 13.453 1.00 32.84 O ANISOU 302 O TYR A 47 4373 3940 4164 -523 -142 -59 O ATOM 303 CB TYR A 47 36.939 26.334 14.309 1.00 34.45 C ANISOU 303 CB TYR A 47 4558 4164 4366 -695 -204 -158 C ATOM 304 CG TYR A 47 37.886 27.083 15.236 1.00 42.06 C ANISOU 304 CG TYR A 47 5500 5170 5311 -789 -265 -224 C ATOM 305 CD1 TYR A 47 37.661 27.152 16.621 1.00 44.51 C ANISOU 305 CD1 TYR A 47 5833 5559 5519 -809 -322 -271 C ATOM 306 CD2 TYR A 47 39.021 27.678 14.733 1.00 46.83 C ANISOU 306 CD2 TYR A 47 6048 5756 5988 -867 -266 -241 C ATOM 307 CE1 TYR A 47 38.576 27.837 17.444 1.00 47.59 C ANISOU 307 CE1 TYR A 47 6193 6006 5884 -905 -387 -350 C ATOM 308 CE2 TYR A 47 39.887 28.381 15.518 1.00 47.00 C ANISOU 308 CE2 TYR A 47 6039 5812 6006 -963 -325 -312 C ATOM 309 CZ TYR A 47 39.689 28.445 16.862 1.00 47.62 C ANISOU 309 CZ TYR A 47 6141 5969 5985 -980 -390 -373 C ATOM 310 OH TYR A 47 40.657 29.135 17.567 1.00 51.74 O ANISOU 310 OH TYR A 47 6618 6538 6503 -1086 -457 -458 O ATOM 311 N SER A 48 36.604 22.909 13.253 1.00 32.50 N ANISOU 311 N SER A 48 4163 3962 4224 -510 -203 -4 N ATOM 312 CA SER A 48 35.858 22.164 12.256 1.00 32.81 C ANISOU 312 CA SER A 48 4199 3961 4308 -442 -149 5 C ATOM 313 C SER A 48 34.573 21.598 12.841 1.00 30.61 C ANISOU 313 C SER A 48 3972 3666 3992 -393 -154 42 C ATOM 314 O SER A 48 33.574 21.542 12.161 1.00 27.51 O ANISOU 314 O SER A 48 3619 3237 3598 -356 -103 30 O ATOM 315 CB SER A 48 36.684 21.087 11.549 1.00 33.94 C ANISOU 315 CB SER A 48 4222 4113 4561 -406 -152 3 C ATOM 316 OG SER A 48 37.227 20.228 12.500 1.00 44.05 O ANISOU 316 OG SER A 48 5431 5411 5893 -388 -235 57 O ATOM 317 N GLN A 49 34.583 21.218 14.137 1.00 29.42 N ANISOU 317 N GLN A 49 3816 3561 3800 -403 -218 94 N ATOM 318 CA GLN A 49 33.311 20.667 14.660 1.00 30.41 C ANISOU 318 CA GLN A 49 3984 3686 3886 -370 -208 140 C ATOM 319 C GLN A 49 32.249 21.767 14.745 1.00 28.30 C ANISOU 319 C GLN A 49 3812 3411 3528 -380 -150 76 C ATOM 320 O GLN A 49 31.026 21.544 14.517 1.00 26.49 O ANISOU 320 O GLN A 49 3613 3157 3295 -341 -105 79 O ATOM 321 CB GLN A 49 33.549 20.040 16.011 1.00 31.33 C ANISOU 321 CB GLN A 49 4072 3876 3956 -391 -286 231 C ATOM 322 CG GLN A 49 34.171 18.627 15.931 1.00 36.97 C ANISOU 322 CG GLN A 49 4683 4558 4805 -352 -348 328 C ATOM 323 CD GLN A 49 35.691 18.665 15.869 1.00 47.19 C ANISOU 323 CD GLN A 49 5892 5873 6164 -366 -409 320 C ATOM 324 OE1 GLN A 49 36.310 19.717 15.984 1.00 52.83 O ANISOU 324 OE1 GLN A 49 6624 6637 6811 -420 -411 254 O ATOM 325 NE2 GLN A 49 36.304 17.485 15.694 1.00 54.30 N ANISOU 325 NE2 GLN A 49 6687 6727 7219 -317 -462 385 N ATOM 326 N GLN A 50 32.702 22.969 15.107 1.00 29.46 N ANISOU 326 N GLN A 50 3998 3575 3620 -432 -154 12 N ATOM 327 CA GLN A 50 31.789 24.117 15.094 1.00 30.56 C ANISOU 327 CA GLN A 50 4217 3675 3718 -432 -101 -65 C ATOM 328 C GLN A 50 31.151 24.360 13.715 1.00 29.68 C ANISOU 328 C GLN A 50 4128 3477 3674 -386 -45 -70 C ATOM 329 O GLN A 50 29.908 24.528 13.613 1.00 29.63 O ANISOU 329 O GLN A 50 4157 3443 3656 -341 -6 -85 O ATOM 330 CB GLN A 50 32.477 25.443 15.590 1.00 31.92 C ANISOU 330 CB GLN A 50 4420 3844 3862 -502 -116 -153 C ATOM 331 CG GLN A 50 31.452 26.616 15.433 1.00 36.58 C ANISOU 331 CG GLN A 50 5085 4352 4461 -483 -60 -236 C ATOM 332 CD GLN A 50 30.319 26.540 16.492 1.00 41.15 C ANISOU 332 CD GLN A 50 5689 4996 4951 -459 -36 -284 C ATOM 333 OE1 GLN A 50 29.099 26.306 16.198 1.00 43.41 O ANISOU 333 OE1 GLN A 50 5987 5259 5247 -395 12 -273 O ATOM 334 NE2 GLN A 50 30.733 26.667 17.749 1.00 41.95 N ANISOU 334 NE2 GLN A 50 5786 5204 4951 -516 -70 -336 N ATOM 335 N VAL A 51 32.006 24.396 12.680 1.00 28.86 N ANISOU 335 N VAL A 51 3991 3347 3629 -400 -42 -56 N ATOM 336 CA VAL A 51 31.554 24.601 11.311 1.00 29.19 C ANISOU 336 CA VAL A 51 4044 3342 3704 -371 2 -46 C ATOM 337 C VAL A 51 30.562 23.471 10.956 1.00 29.59 C ANISOU 337 C VAL A 51 4073 3406 3766 -304 16 -24 C ATOM 338 O VAL A 51 29.508 23.743 10.286 1.00 27.99 O ANISOU 338 O VAL A 51 3901 3175 3560 -266 44 -27 O ATOM 339 CB VAL A 51 32.747 24.694 10.376 1.00 30.00 C ANISOU 339 CB VAL A 51 4100 3458 3842 -413 9 -36 C ATOM 340 CG1 VAL A 51 32.267 24.648 8.899 1.00 32.39 C ANISOU 340 CG1 VAL A 51 4401 3759 4146 -387 54 -16 C ATOM 341 CG2 VAL A 51 33.430 26.105 10.723 1.00 31.04 C ANISOU 341 CG2 VAL A 51 4269 3549 3977 -491 1 -58 C ATOM 342 N GLN A 52 30.915 22.213 11.296 1.00 27.48 N ANISOU 342 N GLN A 52 3741 3170 3531 -292 -12 1 N ATOM 343 CA GLN A 52 30.034 21.131 10.882 1.00 29.55 C ANISOU 343 CA GLN A 52 3973 3423 3833 -241 0 12 C ATOM 344 C GLN A 52 28.661 21.218 11.607 1.00 27.09 C ANISOU 344 C GLN A 52 3705 3109 3478 -220 14 23 C ATOM 345 O GLN A 52 27.629 20.846 10.970 1.00 26.86 O ANISOU 345 O GLN A 52 3668 3065 3471 -182 38 14 O ATOM 346 CB GLN A 52 30.694 19.775 11.181 1.00 28.39 C ANISOU 346 CB GLN A 52 3743 3276 3766 -232 -38 45 C ATOM 347 CG GLN A 52 31.860 19.541 10.180 1.00 34.39 C ANISOU 347 CG GLN A 52 4434 4043 4591 -235 -32 2 C ATOM 348 CD GLN A 52 32.965 18.666 10.769 1.00 45.61 C ANISOU 348 CD GLN A 52 5768 5461 6101 -233 -87 34 C ATOM 349 OE1 GLN A 52 32.883 18.155 11.918 1.00 46.20 O ANISOU 349 OE1 GLN A 52 5837 5531 6186 -232 -142 112 O ATOM 350 NE2 GLN A 52 34.043 18.524 9.999 1.00 49.46 N ANISOU 350 NE2 GLN A 52 6178 5964 6651 -234 -76 -18 N ATOM 351 N LEU A 53 28.639 21.641 12.877 1.00 27.82 N ANISOU 351 N LEU A 53 3829 3235 3506 -248 2 31 N ATOM 352 CA LEU A 53 27.368 21.704 13.579 1.00 30.66 C ANISOU 352 CA LEU A 53 4213 3618 3817 -232 30 27 C ATOM 353 C LEU A 53 26.494 22.765 12.930 1.00 29.46 C ANISOU 353 C LEU A 53 4104 3422 3667 -198 71 -33 C ATOM 354 O LEU A 53 25.255 22.622 12.762 1.00 27.28 O ANISOU 354 O LEU A 53 3820 3143 3401 -157 101 -41 O ATOM 355 CB LEU A 53 27.589 22.043 15.065 1.00 30.53 C ANISOU 355 CB LEU A 53 4218 3679 3704 -279 16 25 C ATOM 356 CG LEU A 53 27.663 20.682 15.808 1.00 44.61 C ANISOU 356 CG LEU A 53 5951 5517 5483 -297 -19 133 C ATOM 357 CD1 LEU A 53 28.544 20.820 17.092 1.00 48.10 C ANISOU 357 CD1 LEU A 53 6393 6058 5825 -358 -72 164 C ATOM 358 CD2 LEU A 53 26.246 20.360 16.146 1.00 42.27 C ANISOU 358 CD2 LEU A 53 5652 5249 5160 -283 31 146 C ATOM 359 N ASP A 54 27.142 23.888 12.553 1.00 29.00 N ANISOU 359 N ASP A 54 4084 3322 3613 -215 67 -68 N ATOM 360 CA ASP A 54 26.367 24.935 11.914 1.00 28.95 C ANISOU 360 CA ASP A 54 4115 3253 3633 -178 91 -99 C ATOM 361 C ASP A 54 25.933 24.502 10.565 1.00 27.13 C ANISOU 361 C ASP A 54 3860 3011 3437 -141 92 -61 C ATOM 362 O ASP A 54 24.810 24.868 10.186 1.00 28.20 O ANISOU 362 O ASP A 54 4000 3123 3591 -91 104 -67 O ATOM 363 CB ASP A 54 27.195 26.207 11.709 1.00 30.69 C ANISOU 363 CB ASP A 54 4378 3408 3875 -216 81 -121 C ATOM 364 CG ASP A 54 27.508 26.917 13.015 1.00 36.08 C ANISOU 364 CG ASP A 54 5088 4095 4527 -255 78 -198 C ATOM 365 OD1 ASP A 54 26.709 26.828 13.989 1.00 38.18 O ANISOU 365 OD1 ASP A 54 5353 4406 4747 -237 100 -251 O ATOM 366 OD2 ASP A 54 28.532 27.674 13.033 1.00 38.14 O ANISOU 366 OD2 ASP A 54 5366 4316 4809 -313 59 -218 O ATOM 367 N LEU A 55 26.767 23.709 9.838 1.00 26.04 N ANISOU 367 N LEU A 55 3684 2901 3310 -162 79 -33 N ATOM 368 CA LEU A 55 26.291 23.236 8.520 1.00 27.44 C ANISOU 368 CA LEU A 55 3830 3097 3500 -132 83 -23 C ATOM 369 C LEU A 55 25.131 22.296 8.623 1.00 25.57 C ANISOU 369 C LEU A 55 3555 2877 3284 -93 87 -34 C ATOM 370 O LEU A 55 24.205 22.338 7.791 1.00 25.93 O ANISOU 370 O LEU A 55 3588 2934 3331 -58 86 -39 O ATOM 371 CB LEU A 55 27.389 22.455 7.778 1.00 27.05 C ANISOU 371 CB LEU A 55 3729 3087 3460 -161 80 -29 C ATOM 372 CG LEU A 55 28.224 23.416 6.884 1.00 34.94 C ANISOU 372 CG LEU A 55 4748 4098 4428 -201 90 -7 C ATOM 373 CD1 LEU A 55 29.498 22.620 6.460 1.00 35.99 C ANISOU 373 CD1 LEU A 55 4811 4285 4577 -234 100 -36 C ATOM 374 CD2 LEU A 55 27.442 23.880 5.613 1.00 34.51 C ANISOU 374 CD2 LEU A 55 4708 4072 4332 -182 93 23 C ATOM 375 N ILE A 56 25.157 21.407 9.647 1.00 26.94 N ANISOU 375 N ILE A 56 3702 3059 3476 -104 85 -28 N ATOM 376 CA ILE A 56 23.998 20.492 9.934 1.00 27.32 C ANISOU 376 CA ILE A 56 3708 3116 3555 -83 95 -24 C ATOM 377 C ILE A 56 22.705 21.296 10.019 1.00 27.01 C ANISOU 377 C ILE A 56 3687 3080 3495 -46 118 -44 C ATOM 378 O ILE A 56 21.648 20.972 9.441 1.00 25.97 O ANISOU 378 O ILE A 56 3516 2959 3393 -16 120 -57 O ATOM 379 CB ILE A 56 24.260 19.648 11.168 1.00 26.61 C ANISOU 379 CB ILE A 56 3598 3037 3477 -115 88 23 C ATOM 380 CG1 ILE A 56 25.319 18.555 10.818 1.00 27.33 C ANISOU 380 CG1 ILE A 56 3638 3101 3646 -129 55 42 C ATOM 381 CG2 ILE A 56 22.982 18.892 11.565 1.00 27.62 C ANISOU 381 CG2 ILE A 56 3684 3176 3633 -111 109 44 C ATOM 382 CD1 ILE A 56 25.955 17.916 12.070 1.00 27.26 C ANISOU 382 CD1 ILE A 56 3612 3098 3648 -163 24 122 C ATOM 383 N TYR A 57 22.798 22.349 10.794 1.00 25.23 N ANISOU 383 N TYR A 57 3510 2847 3231 -48 132 -58 N ATOM 384 CA TYR A 57 21.637 23.209 11.033 1.00 25.91 C ANISOU 384 CA TYR A 57 3603 2923 3319 -3 158 -97 C ATOM 385 C TYR A 57 21.195 23.915 9.783 1.00 27.46 C ANISOU 385 C TYR A 57 3803 3078 3551 45 136 -91 C ATOM 386 O TYR A 57 20.004 23.936 9.435 1.00 26.12 O ANISOU 386 O TYR A 57 3593 2917 3413 95 137 -101 O ATOM 387 CB TYR A 57 22.008 24.156 12.204 1.00 26.31 C ANISOU 387 CB TYR A 57 3699 2969 3328 -23 179 -143 C ATOM 388 CG TYR A 57 21.047 25.201 12.416 1.00 29.64 C ANISOU 388 CG TYR A 57 4124 3358 3778 30 208 -210 C ATOM 389 CD1 TYR A 57 19.846 24.956 13.031 1.00 29.90 C ANISOU 389 CD1 TYR A 57 4108 3446 3807 57 254 -249 C ATOM 390 CD2 TYR A 57 21.339 26.496 11.974 1.00 34.54 C ANISOU 390 CD2 TYR A 57 4790 3882 4450 53 189 -233 C ATOM 391 CE1 TYR A 57 18.952 25.998 13.306 1.00 35.93 C ANISOU 391 CE1 TYR A 57 4858 4177 4616 118 287 -336 C ATOM 392 CE2 TYR A 57 20.450 27.538 12.236 1.00 32.12 C ANISOU 392 CE2 TYR A 57 4479 3518 4208 114 212 -307 C ATOM 393 CZ TYR A 57 19.265 27.257 12.892 1.00 39.64 C ANISOU 393 CZ TYR A 57 5373 4533 5155 152 261 -367 C ATOM 394 OH TYR A 57 18.341 28.237 13.139 1.00 39.98 O ANISOU 394 OH TYR A 57 5389 4521 5280 224 289 -458 O ATOM 395 N ALA A 58 22.154 24.490 9.063 1.00 24.70 N ANISOU 395 N ALA A 58 3494 2696 3195 26 110 -63 N ATOM 396 CA ALA A 58 21.814 25.225 7.867 1.00 27.80 C ANISOU 396 CA ALA A 58 3895 3062 3605 60 81 -24 C ATOM 397 C ALA A 58 21.201 24.348 6.764 1.00 26.24 C ANISOU 397 C ALA A 58 3641 2935 3394 77 57 -9 C ATOM 398 O ALA A 58 20.213 24.726 6.138 1.00 28.65 O ANISOU 398 O ALA A 58 3924 3246 3716 127 30 11 O ATOM 399 CB ALA A 58 23.094 25.915 7.391 1.00 28.88 C ANISOU 399 CB ALA A 58 4081 3167 3726 10 68 19 C ATOM 400 N TYR A 59 21.714 23.112 6.595 1.00 26.38 N ANISOU 400 N TYR A 59 3624 3005 3394 39 63 -31 N ATOM 401 CA TYR A 59 21.138 22.208 5.596 1.00 26.99 C ANISOU 401 CA TYR A 59 3639 3149 3467 48 43 -53 C ATOM 402 C TYR A 59 19.703 21.844 5.999 1.00 26.40 C ANISOU 402 C TYR A 59 3513 3079 3440 86 44 -78 C ATOM 403 O TYR A 59 18.821 21.849 5.162 1.00 27.87 O ANISOU 403 O TYR A 59 3656 3309 3623 116 11 -82 O ATOM 404 CB TYR A 59 21.905 20.883 5.597 1.00 24.55 C ANISOU 404 CB TYR A 59 3290 2859 3177 6 55 -98 C ATOM 405 CG TYR A 59 23.247 20.946 4.874 1.00 26.28 C ANISOU 405 CG TYR A 59 3521 3109 3355 -32 57 -101 C ATOM 406 CD1 TYR A 59 23.440 21.753 3.720 1.00 31.25 C ANISOU 406 CD1 TYR A 59 4171 3798 3905 -40 44 -69 C ATOM 407 CD2 TYR A 59 24.359 20.244 5.435 1.00 27.99 C ANISOU 407 CD2 TYR A 59 3721 3301 3613 -62 73 -122 C ATOM 408 CE1 TYR A 59 24.730 21.795 3.098 1.00 33.04 C ANISOU 408 CE1 TYR A 59 4395 4073 4085 -88 63 -73 C ATOM 409 CE2 TYR A 59 25.578 20.308 4.836 1.00 31.54 C ANISOU 409 CE2 TYR A 59 4162 3785 4036 -95 83 -136 C ATOM 410 CZ TYR A 59 25.735 21.052 3.666 1.00 29.55 C ANISOU 410 CZ TYR A 59 3925 3606 3696 -111 86 -120 C ATOM 411 OH TYR A 59 26.965 20.988 3.109 1.00 36.42 O ANISOU 411 OH TYR A 59 4770 4529 4537 -153 111 -143 O ATOM 412 N TYR A 60 19.488 21.617 7.308 1.00 26.15 N ANISOU 412 N TYR A 60 3480 3017 3440 80 82 -88 N ATOM 413 CA TYR A 60 18.141 21.284 7.769 1.00 28.49 C ANISOU 413 CA TYR A 60 3715 3332 3779 105 100 -109 C ATOM 414 C TYR A 60 17.178 22.417 7.522 1.00 28.86 C ANISOU 414 C TYR A 60 3755 3372 3840 173 87 -110 C ATOM 415 O TYR A 60 16.070 22.201 6.933 1.00 30.60 O ANISOU 415 O TYR A 60 3904 3631 4093 207 61 -123 O ATOM 416 CB TYR A 60 18.182 20.908 9.289 1.00 29.83 C ANISOU 416 CB TYR A 60 3886 3498 3949 71 152 -105 C ATOM 417 CG TYR A 60 16.813 20.846 9.844 1.00 29.51 C ANISOU 417 CG TYR A 60 3783 3493 3938 92 188 -127 C ATOM 418 CD1 TYR A 60 15.982 19.733 9.591 1.00 32.20 C ANISOU 418 CD1 TYR A 60 4039 3862 4336 71 187 -129 C ATOM 419 CD2 TYR A 60 16.322 21.870 10.671 1.00 34.47 C ANISOU 419 CD2 TYR A 60 4421 4127 4549 127 230 -160 C ATOM 420 CE1 TYR A 60 14.677 19.682 10.114 1.00 35.41 C ANISOU 420 CE1 TYR A 60 4369 4312 4773 82 228 -149 C ATOM 421 CE2 TYR A 60 15.027 21.808 11.179 1.00 39.05 C ANISOU 421 CE2 TYR A 60 4923 4756 5158 148 276 -195 C ATOM 422 CZ TYR A 60 14.230 20.716 10.890 1.00 39.70 C ANISOU 422 CZ TYR A 60 4919 4876 5289 122 276 -180 C ATOM 423 OH TYR A 60 12.948 20.689 11.436 1.00 44.98 O ANISOU 423 OH TYR A 60 5496 5605 5988 134 330 -214 O ATOM 424 N LYS A 61 17.587 23.638 7.885 1.00 28.58 N ANISOU 424 N LYS A 61 3783 3279 3799 196 94 -99 N ATOM 425 CA LYS A 61 16.681 24.790 7.750 1.00 31.88 C ANISOU 425 CA LYS A 61 4187 3656 4271 274 79 -102 C ATOM 426 C LYS A 61 16.445 25.099 6.258 1.00 31.55 C ANISOU 426 C LYS A 61 4132 3629 4227 305 1 -35 C ATOM 427 O LYS A 61 15.364 25.621 5.904 1.00 34.29 O ANISOU 427 O LYS A 61 4426 3971 4632 377 -34 -23 O ATOM 428 CB LYS A 61 17.259 26.047 8.468 1.00 30.03 C ANISOU 428 CB LYS A 61 4023 3329 4059 285 100 -119 C ATOM 429 CG LYS A 61 17.209 25.983 10.020 1.00 35.57 C ANISOU 429 CG LYS A 61 4724 4047 4746 265 174 -205 C ATOM 430 CD LYS A 61 15.786 25.885 10.461 1.00 40.41 C ANISOU 430 CD LYS A 61 5248 4701 5404 318 212 -262 C ATOM 431 CE LYS A 61 15.625 25.761 11.961 1.00 48.70 C ANISOU 431 CE LYS A 61 6285 5811 6410 288 297 -346 C ATOM 432 NZ LYS A 61 14.452 26.680 12.382 1.00 50.71 N ANISOU 432 NZ LYS A 61 6473 6047 6747 374 339 -447 N ATOM 433 N ASN A 62 17.430 24.823 5.403 1.00 30.78 N ANISOU 433 N ASN A 62 4073 3563 4060 254 -26 8 N ATOM 434 CA ASN A 62 17.313 25.032 3.937 1.00 32.26 C ANISOU 434 CA ASN A 62 4248 3810 4200 262 -96 78 C ATOM 435 C ASN A 62 16.560 23.919 3.205 1.00 33.89 C ANISOU 435 C ASN A 62 4369 4131 4376 256 -127 35 C ATOM 436 O ASN A 62 16.402 23.995 1.984 1.00 34.79 O ANISOU 436 O ASN A 62 4462 4332 4424 256 -190 79 O ATOM 437 CB ASN A 62 18.706 25.121 3.284 1.00 33.07 C ANISOU 437 CB ASN A 62 4411 3935 4218 195 -97 125 C ATOM 438 CG ASN A 62 18.679 25.867 1.965 1.00 33.31 C ANISOU 438 CG ASN A 62 4452 4015 4189 199 -164 236 C ATOM 439 OD1 ASN A 62 17.955 26.917 1.805 1.00 35.23 O ANISOU 439 OD1 ASN A 62 4697 4197 4493 262 -214 320 O ATOM 440 ND2 ASN A 62 19.434 25.357 1.023 1.00 34.61 N ANISOU 440 ND2 ASN A 62 4615 4294 4242 135 -166 243 N ATOM 441 N ALA A 63 16.103 22.937 3.962 1.00 32.93 N ANISOU 441 N ALA A 63 4442 4092 3977 458 -142 -11 N ATOM 442 CA ALA A 63 15.442 21.735 3.440 1.00 33.58 C ANISOU 442 CA ALA A 63 4426 4315 4016 409 -128 -55 C ATOM 443 C ALA A 63 16.338 20.910 2.532 1.00 34.11 C ANISOU 443 C ALA A 63 4523 4388 4049 304 -91 -39 C ATOM 444 O ALA A 63 15.840 20.175 1.661 1.00 36.31 O ANISOU 444 O ALA A 63 4750 4770 4277 280 -109 -78 O ATOM 445 CB ALA A 63 14.088 22.082 2.730 1.00 37.86 C ANISOU 445 CB ALA A 63 4907 4971 4507 511 -211 -68 C ATOM 446 N ASP A 64 17.659 20.980 2.739 1.00 32.09 N ANISOU 446 N ASP A 64 4335 4040 3818 245 -41 -4 N ATOM 447 CA ASP A 64 18.626 20.037 2.125 1.00 32.90 C ANISOU 447 CA ASP A 64 4435 4164 3900 159 8 -28 C ATOM 448 C ASP A 64 18.753 18.815 3.001 1.00 31.04 C ANISOU 448 C ASP A 64 4143 3904 3745 107 45 -97 C ATOM 449 O ASP A 64 19.762 18.616 3.629 1.00 29.42 O ANISOU 449 O ASP A 64 3957 3630 3590 71 85 -88 O ATOM 450 CB ASP A 64 20.014 20.735 2.056 1.00 31.83 C ANISOU 450 CB ASP A 64 4375 3960 3758 120 43 45 C ATOM 451 CG ASP A 64 20.003 21.905 1.109 1.00 40.02 C ANISOU 451 CG ASP A 64 5483 5007 4717 138 -1 152 C ATOM 452 OD1 ASP A 64 19.399 21.781 0.027 1.00 38.90 O ANISOU 452 OD1 ASP A 64 5323 4975 4482 157 -36 159 O ATOM 453 OD2 ASP A 64 20.677 22.920 1.391 1.00 40.08 O ANISOU 453 OD2 ASP A 64 5564 4913 4751 117 -8 238 O ATOM 454 N LEU A 65 17.717 17.968 3.037 1.00 29.75 N ANISOU 454 N LEU A 65 3906 3799 3598 92 20 -154 N ATOM 455 CA LEU A 65 17.651 16.989 4.101 1.00 29.07 C ANISOU 455 CA LEU A 65 3775 3673 3598 31 38 -173 C ATOM 456 C LEU A 65 18.664 15.872 3.887 1.00 27.76 C ANISOU 456 C LEU A 65 3624 3433 3491 -25 54 -215 C ATOM 457 O LEU A 65 19.248 15.401 4.840 1.00 29.77 O ANISOU 457 O LEU A 65 3883 3610 3820 -58 71 -189 O ATOM 458 CB LEU A 65 16.174 16.477 4.204 1.00 29.04 C ANISOU 458 CB LEU A 65 3676 3763 3594 6 1 -204 C ATOM 459 CG LEU A 65 15.175 17.569 4.609 1.00 29.10 C ANISOU 459 CG LEU A 65 3642 3861 3553 90 -16 -183 C ATOM 460 CD1 LEU A 65 13.727 16.998 4.634 1.00 36.77 C ANISOU 460 CD1 LEU A 65 4485 4971 4513 54 -49 -222 C ATOM 461 CD2 LEU A 65 15.511 18.145 5.950 1.00 32.60 C ANISOU 461 CD2 LEU A 65 4098 4271 4017 113 20 -148 C ATOM 462 N PRO A 66 18.863 15.421 2.657 1.00 29.93 N ANISOU 462 N PRO A 66 3898 3742 3730 -24 41 -290 N ATOM 463 CA PRO A 66 19.911 14.361 2.497 1.00 30.51 C ANISOU 463 CA PRO A 66 3978 3741 3874 -44 50 -364 C ATOM 464 C PRO A 66 21.252 14.926 2.871 1.00 27.82 C ANISOU 464 C PRO A 66 3672 3368 3531 -21 102 -315 C ATOM 465 O PRO A 66 22.060 14.231 3.527 1.00 26.92 O ANISOU 465 O PRO A 66 3555 3165 3510 -29 106 -326 O ATOM 466 CB PRO A 66 19.821 13.983 1.003 1.00 31.74 C ANISOU 466 CB PRO A 66 4114 3991 3953 -29 30 -483 C ATOM 467 CG PRO A 66 18.316 14.309 0.660 1.00 35.04 C ANISOU 467 CG PRO A 66 4499 4503 4310 -37 -18 -470 C ATOM 468 CD PRO A 66 18.079 15.633 1.433 1.00 32.74 C ANISOU 468 CD PRO A 66 4234 4217 3989 0 4 -334 C ATOM 469 N LEU A 67 21.544 16.199 2.548 1.00 28.37 N ANISOU 469 N LEU A 67 3775 3496 3507 1 130 -247 N ATOM 470 CA LEU A 67 22.862 16.705 2.992 1.00 28.06 C ANISOU 470 CA LEU A 67 3758 3426 3479 -6 174 -201 C ATOM 471 C LEU A 67 22.938 16.820 4.493 1.00 27.48 C ANISOU 471 C LEU A 67 3693 3262 3487 -16 172 -144 C ATOM 472 O LEU A 67 24.020 16.561 5.088 1.00 27.04 O ANISOU 472 O LEU A 67 3628 3166 3482 -25 190 -141 O ATOM 473 CB LEU A 67 23.147 18.126 2.372 1.00 28.82 C ANISOU 473 CB LEU A 67 3900 3580 3472 -11 191 -114 C ATOM 474 CG LEU A 67 23.307 18.077 0.831 1.00 33.07 C ANISOU 474 CG LEU A 67 4421 4257 3885 -17 203 -145 C ATOM 475 CD1 LEU A 67 23.700 19.532 0.385 1.00 33.29 C ANISOU 475 CD1 LEU A 67 4507 4319 3824 -53 211 -5 C ATOM 476 CD2 LEU A 67 24.551 17.225 0.515 1.00 32.60 C ANISOU 476 CD2 LEU A 67 4302 4256 3831 -25 253 -242 C ATOM 477 N ALA A 68 21.853 17.259 5.131 1.00 26.86 N ANISOU 477 N ALA A 68 3619 3179 3407 -7 149 -106 N ATOM 478 CA ALA A 68 21.851 17.270 6.622 1.00 26.78 C ANISOU 478 CA ALA A 68 3601 3129 3447 -20 149 -66 C ATOM 479 C ALA A 68 22.089 15.875 7.164 1.00 27.13 C ANISOU 479 C ALA A 68 3610 3125 3571 -59 136 -74 C ATOM 480 O ALA A 68 22.919 15.726 8.099 1.00 27.15 O ANISOU 480 O ALA A 68 3614 3090 3612 -70 141 -37 O ATOM 481 CB ALA A 68 20.533 17.787 7.188 1.00 26.97 C ANISOU 481 CB ALA A 68 3603 3203 3441 4 131 -53 C ATOM 482 N GLN A 69 21.330 14.885 6.656 1.00 27.74 N ANISOU 482 N GLN A 69 3661 3198 3682 -85 106 -114 N ATOM 483 CA GLN A 69 21.511 13.536 7.172 1.00 29.92 C ANISOU 483 CA GLN A 69 3921 3383 4062 -131 70 -105 C ATOM 484 C GLN A 69 22.943 12.961 7.061 1.00 29.25 C ANISOU 484 C GLN A 69 3851 3216 4048 -95 64 -141 C ATOM 485 O GLN A 69 23.476 12.405 8.051 1.00 27.51 O ANISOU 485 O GLN A 69 3630 2923 3899 -109 37 -78 O ATOM 486 CB GLN A 69 20.455 12.629 6.518 1.00 32.22 C ANISOU 486 CB GLN A 69 4187 3665 4392 -178 24 -158 C ATOM 487 CG GLN A 69 20.511 11.184 7.007 1.00 40.57 C ANISOU 487 CG GLN A 69 5244 4584 5586 -245 -39 -137 C ATOM 488 CD GLN A 69 19.547 10.375 6.136 1.00 53.58 C ANISOU 488 CD GLN A 69 6871 6212 7277 -300 -93 -222 C ATOM 489 OE1 GLN A 69 19.940 9.850 5.083 1.00 59.17 O ANISOU 489 OE1 GLN A 69 7593 6867 8022 -258 -122 -358 O ATOM 490 NE2 GLN A 69 18.275 10.340 6.521 1.00 52.12 N ANISOU 490 NE2 GLN A 69 6636 6099 7070 -392 -105 -162 N ATOM 491 N ALA A 70 23.573 13.195 5.912 1.00 27.31 N ANISOU 491 N ALA A 70 3605 3010 3762 -45 89 -232 N ATOM 492 CA ALA A 70 24.940 12.749 5.699 1.00 30.73 C ANISOU 492 CA ALA A 70 4021 3415 4242 5 94 -293 C ATOM 493 C ALA A 70 25.920 13.472 6.607 1.00 27.42 C ANISOU 493 C ALA A 70 3597 3014 3807 9 123 -214 C ATOM 494 O ALA A 70 26.874 12.858 7.120 1.00 28.79 O ANISOU 494 O ALA A 70 3746 3135 4058 42 98 -218 O ATOM 495 CB ALA A 70 25.360 12.943 4.255 1.00 29.28 C ANISOU 495 CB ALA A 70 3813 3335 3977 45 130 -408 C ATOM 496 N ALA A 71 25.720 14.784 6.773 1.00 27.36 N ANISOU 496 N ALA A 71 3613 3076 3708 -17 163 -152 N ATOM 497 CA ALA A 71 26.606 15.535 7.613 1.00 27.24 C ANISOU 497 CA ALA A 71 3595 3075 3680 -28 181 -97 C ATOM 498 C ALA A 71 26.448 15.060 9.102 1.00 26.12 C ANISOU 498 C ALA A 71 3451 2882 3592 -43 140 -25 C ATOM 499 O ALA A 71 27.443 14.968 9.830 1.00 26.05 O ANISOU 499 O ALA A 71 3417 2870 3610 -35 127 -1 O ATOM 500 CB ALA A 71 26.224 17.128 7.540 1.00 25.67 C ANISOU 500 CB ALA A 71 3442 2919 3392 -56 208 -52 C ATOM 501 N ILE A 72 25.221 14.781 9.524 1.00 25.95 N ANISOU 501 N ILE A 72 3441 2850 3569 -71 120 14 N ATOM 502 CA ILE A 72 25.007 14.208 10.908 1.00 25.94 C ANISOU 502 CA ILE A 72 3427 2836 3594 -107 82 105 C ATOM 503 C ILE A 72 25.712 12.850 11.080 1.00 28.03 C ANISOU 503 C ILE A 72 3682 2995 3974 -96 21 129 C ATOM 504 O ILE A 72 26.470 12.620 12.026 1.00 27.68 O ANISOU 504 O ILE A 72 3625 2943 3950 -90 -11 195 O ATOM 505 CB ILE A 72 23.533 14.062 11.167 1.00 25.60 C ANISOU 505 CB ILE A 72 3374 2834 3520 -157 78 142 C ATOM 506 CG1 ILE A 72 22.977 15.500 11.360 1.00 23.79 C ANISOU 506 CG1 ILE A 72 3146 2709 3185 -135 121 117 C ATOM 507 CG2 ILE A 72 23.255 13.242 12.478 1.00 27.12 C ANISOU 507 CG2 ILE A 72 3542 3034 3727 -226 39 264 C ATOM 508 CD1 ILE A 72 21.429 15.518 11.196 1.00 25.97 C ANISOU 508 CD1 ILE A 72 3388 3059 3421 -154 125 110 C ATOM 509 N ASP A 73 25.566 11.994 10.107 1.00 28.99 N ANISOU 509 N ASP A 73 3810 3033 4174 -77 -5 58 N ATOM 510 CA ASP A 73 26.188 10.680 10.204 1.00 31.64 C ANISOU 510 CA ASP A 73 4145 3229 4647 -43 -84 57 C ATOM 511 C ASP A 73 27.711 10.750 10.272 1.00 29.61 C ANISOU 511 C ASP A 73 3852 2982 4415 45 -87 16 C ATOM 512 O ASP A 73 28.347 10.089 11.062 1.00 30.79 O ANISOU 512 O ASP A 73 3994 3061 4643 74 -157 83 O ATOM 513 CB ASP A 73 25.683 9.853 9.016 1.00 31.19 C ANISOU 513 CB ASP A 73 4099 3083 4667 -31 -115 -61 C ATOM 514 CG ASP A 73 24.214 9.347 9.242 1.00 39.29 C ANISOU 514 CG ASP A 73 5146 4065 5716 -143 -151 10 C ATOM 515 OD1 ASP A 73 23.669 9.499 10.382 1.00 44.62 O ANISOU 515 OD1 ASP A 73 5818 4785 6352 -226 -152 161 O ATOM 516 OD2 ASP A 73 23.628 8.745 8.316 1.00 42.85 O ANISOU 516 OD2 ASP A 73 5604 4456 6221 -156 -182 -89 O ATOM 517 N ARG A 74 28.270 11.688 9.505 1.00 29.68 N ANISOU 517 N ARG A 74 3832 3104 4340 76 -12 -74 N ATOM 518 CA ARG A 74 29.703 11.821 9.516 1.00 32.55 C ANISOU 518 CA ARG A 74 4134 3519 4713 142 -4 -118 C ATOM 519 C ARG A 74 30.182 12.387 10.842 1.00 31.03 C ANISOU 519 C ARG A 74 3931 3375 4484 110 -16 -6 C ATOM 520 O ARG A 74 31.184 11.948 11.356 1.00 33.38 O ANISOU 520 O ARG A 74 4181 3666 4837 165 -65 5 O ATOM 521 CB ARG A 74 30.138 12.662 8.316 1.00 32.26 C ANISOU 521 CB ARG A 74 4061 3614 4584 148 82 -220 C ATOM 522 CG ARG A 74 31.665 12.922 8.230 1.00 42.34 C ANISOU 522 CG ARG A 74 5242 4997 5847 192 107 -271 C ATOM 523 CD ARG A 74 32.054 13.525 6.844 1.00 51.80 C ANISOU 523 CD ARG A 74 6390 6348 6943 181 193 -366 C ATOM 524 NE ARG A 74 33.465 13.943 6.913 1.00 54.58 N ANISOU 524 NE ARG A 74 6634 6838 7267 184 226 -387 N ATOM 525 CZ ARG A 74 34.452 13.362 6.225 1.00 63.91 C ANISOU 525 CZ ARG A 74 7696 8129 8458 271 243 -519 C ATOM 526 NH1 ARG A 74 34.182 12.381 5.358 1.00 67.04 N ANISOU 526 NH1 ARG A 74 8079 8502 8892 369 227 -658 N ATOM 527 NH2 ARG A 74 35.708 13.776 6.375 1.00 64.59 N ANISOU 527 NH2 ARG A 74 7662 8366 8513 261 273 -530 N ATOM 528 N PHE A 75 29.441 13.335 11.409 1.00 30.17 N ANISOU 528 N PHE A 75 3860 3322 4280 32 19 62 N ATOM 529 CA PHE A 75 29.810 13.961 12.723 1.00 30.38 C ANISOU 529 CA PHE A 75 3875 3419 4250 -1 5 141 C ATOM 530 C PHE A 75 29.767 12.885 13.819 1.00 31.32 C ANISOU 530 C PHE A 75 3992 3485 4422 3 -80 254 C ATOM 531 O PHE A 75 30.643 12.866 14.688 1.00 32.88 O ANISOU 531 O PHE A 75 4152 3730 4612 21 -124 302 O ATOM 532 CB PHE A 75 28.857 15.138 13.034 1.00 28.08 C ANISOU 532 CB PHE A 75 3625 3192 3853 -62 52 153 C ATOM 533 CG PHE A 75 29.236 15.927 14.283 1.00 27.11 C ANISOU 533 CG PHE A 75 3488 3156 3657 -91 39 184 C ATOM 534 CD1 PHE A 75 29.086 15.398 15.541 1.00 30.96 C ANISOU 534 CD1 PHE A 75 3960 3688 4117 -106 -10 274 C ATOM 535 CD2 PHE A 75 29.840 17.229 14.108 1.00 31.06 C ANISOU 535 CD2 PHE A 75 3989 3696 4116 -113 70 119 C ATOM 536 CE1 PHE A 75 29.462 16.146 16.690 1.00 30.81 C ANISOU 536 CE1 PHE A 75 3919 3781 4007 -129 -24 278 C ATOM 537 CE2 PHE A 75 30.209 18.000 15.221 1.00 30.60 C ANISOU 537 CE2 PHE A 75 3919 3710 3996 -142 48 113 C ATOM 538 CZ PHE A 75 29.992 17.437 16.552 1.00 31.71 C ANISOU 538 CZ PHE A 75 4035 3925 4088 -142 2 182 C ATOM 539 N ILE A 76 28.737 12.030 13.804 1.00 30.75 N ANISOU 539 N ILE A 76 3959 3326 4396 -27 -112 312 N ATOM 540 CA ILE A 76 28.536 11.005 14.830 1.00 34.76 C ANISOU 540 CA ILE A 76 4480 3776 4952 -58 -201 463 C ATOM 541 C ILE A 76 29.646 9.990 14.725 1.00 37.53 C ANISOU 541 C ILE A 76 4814 4002 5443 37 -293 461 C ATOM 542 O ILE A 76 30.230 9.578 15.772 1.00 38.38 O ANISOU 542 O ILE A 76 4907 4113 5563 50 -374 583 O ATOM 543 CB ILE A 76 27.192 10.295 14.681 1.00 34.79 C ANISOU 543 CB ILE A 76 4523 3704 4991 -139 -218 525 C ATOM 544 CG1 ILE A 76 26.110 11.242 15.151 1.00 36.59 C ANISOU 544 CG1 ILE A 76 4739 4096 5066 -220 -143 550 C ATOM 545 CG2 ILE A 76 27.256 8.845 15.466 1.00 41.99 C ANISOU 545 CG2 ILE A 76 5462 4472 6021 -172 -348 701 C ATOM 546 CD1 ILE A 76 24.703 10.768 14.696 1.00 41.14 C ANISOU 546 CD1 ILE A 76 5326 4642 5662 -301 -135 567 C ATOM 547 N ARG A 77 29.992 9.597 13.479 1.00 37.88 N ANISOU 547 N ARG A 77 4850 3956 5586 119 -288 313 N ATOM 548 CA ARG A 77 31.085 8.596 13.272 1.00 40.01 C ANISOU 548 CA ARG A 77 5088 4107 6006 249 -382 263 C ATOM 549 C ARG A 77 32.402 9.147 13.758 1.00 40.98 C ANISOU 549 C ARG A 77 5127 4363 6081 314 -379 251 C ATOM 550 O ARG A 77 33.224 8.427 14.370 1.00 42.78 O ANISOU 550 O ARG A 77 5324 4535 6397 399 -486 308 O ATOM 551 CB ARG A 77 31.245 8.323 11.752 1.00 40.00 C ANISOU 551 CB ARG A 77 5067 4062 6071 333 -349 52 C ATOM 552 CG ARG A 77 32.155 7.141 11.393 1.00 46.47 C ANISOU 552 CG ARG A 77 5851 4738 7066 493 -456 -49 C ATOM 553 CD ARG A 77 32.153 6.906 9.886 1.00 47.20 C ANISOU 553 CD ARG A 77 5917 4829 7189 568 -413 -282 C ATOM 554 NE ARG A 77 30.881 7.274 9.302 1.00 50.63 N ANISOU 554 NE ARG A 77 6412 5278 7545 449 -346 -290 N ATOM 555 CZ ARG A 77 30.647 8.186 8.342 1.00 52.00 C ANISOU 555 CZ ARG A 77 6559 5620 7577 414 -227 -389 C ATOM 556 NH1 ARG A 77 31.645 8.818 7.724 1.00 57.01 N ANISOU 556 NH1 ARG A 77 7103 6434 8125 475 -148 -499 N ATOM 557 NH2 ARG A 77 29.375 8.433 7.968 1.00 45.37 N ANISOU 557 NH2 ARG A 77 5780 4779 6681 312 -194 -369 N ATOM 558 N LEU A 78 32.668 10.410 13.423 1.00 40.52 N ANISOU 558 N LEU A 78 5025 4474 5894 276 -269 173 N ATOM 559 CA LEU A 78 33.982 11.004 13.698 1.00 41.57 C ANISOU 559 CA LEU A 78 5060 4748 5985 316 -259 134 C ATOM 560 C LEU A 78 34.135 11.545 15.123 1.00 41.38 C ANISOU 560 C LEU A 78 5032 4820 5870 252 -291 263 C ATOM 561 O LEU A 78 35.279 11.645 15.633 1.00 41.35 O ANISOU 561 O LEU A 78 4941 4908 5863 299 -334 261 O ATOM 562 CB LEU A 78 34.283 12.087 12.693 1.00 43.23 C ANISOU 562 CB LEU A 78 5227 5087 6110 281 -141 9 C ATOM 563 CG LEU A 78 34.620 11.653 11.224 1.00 46.29 C ANISOU 563 CG LEU A 78 5564 5478 6547 363 -101 -152 C ATOM 564 CD1 LEU A 78 33.459 10.912 10.564 1.00 50.40 C ANISOU 564 CD1 LEU A 78 6174 5853 7125 371 -113 -180 C ATOM 565 CD2 LEU A 78 34.947 12.934 10.466 1.00 49.57 C ANISOU 565 CD2 LEU A 78 5936 6061 6837 281 15 -210 C ATOM 566 N ASN A 79 33.020 11.839 15.786 1.00 37.03 N ANISOU 566 N ASN A 79 4558 4273 5240 154 -277 363 N ATOM 567 CA ASN A 79 33.018 12.434 17.109 1.00 39.53 C ANISOU 567 CA ASN A 79 4867 4718 5437 89 -296 456 C ATOM 568 C ASN A 79 31.962 11.766 17.983 1.00 41.38 C ANISOU 568 C ASN A 79 5161 4921 5642 31 -345 620 C ATOM 569 O ASN A 79 31.058 12.450 18.469 1.00 41.52 O ANISOU 569 O ASN A 79 5203 5038 5535 -54 -291 641 O ATOM 570 CB ASN A 79 32.668 13.934 16.975 1.00 37.32 C ANISOU 570 CB ASN A 79 4600 4544 5037 11 -197 367 C ATOM 571 CG ASN A 79 33.459 14.645 15.904 1.00 39.18 C ANISOU 571 CG ASN A 79 4793 4799 5296 23 -135 235 C ATOM 572 OD1 ASN A 79 34.649 14.871 16.082 1.00 38.98 O ANISOU 572 OD1 ASN A 79 4685 4854 5273 41 -156 200 O ATOM 573 ND2 ASN A 79 32.795 15.067 14.821 1.00 36.43 N ANISOU 573 ND2 ASN A 79 4491 4403 4946 0 -59 170 N ATOM 574 N PRO A 80 32.065 10.428 18.208 1.00 45.76 N ANISOU 574 N PRO A 80 5732 5341 6312 72 -454 740 N ATOM 575 CA PRO A 80 30.991 9.681 18.858 1.00 47.12 C ANISOU 575 CA PRO A 80 5965 5465 6475 -17 -501 920 C ATOM 576 C PRO A 80 30.735 10.137 20.277 1.00 48.36 C ANISOU 576 C PRO A 80 6101 5829 6445 -104 -507 1054 C ATOM 577 O PRO A 80 29.615 10.060 20.731 1.00 49.50 O ANISOU 577 O PRO A 80 6269 6035 6504 -211 -481 1154 O ATOM 578 CB PRO A 80 31.480 8.226 18.845 1.00 49.84 C ANISOU 578 CB PRO A 80 6334 5598 7004 58 -646 1023 C ATOM 579 CG PRO A 80 32.891 8.265 18.492 1.00 49.23 C ANISOU 579 CG PRO A 80 6187 5517 7002 206 -681 903 C ATOM 580 CD PRO A 80 33.194 9.566 17.832 1.00 45.51 C ANISOU 580 CD PRO A 80 5661 5195 6435 206 -545 708 C ATOM 581 N THR A 81 31.749 10.685 20.939 1.00 48.45 N ANISOU 581 N THR A 81 6052 5979 6377 -62 -532 1032 N ATOM 582 CA THR A 81 31.533 11.139 22.290 1.00 48.42 C ANISOU 582 CA THR A 81 6020 6202 6175 -138 -541 1131 C ATOM 583 C THR A 81 31.489 12.648 22.554 1.00 45.40 C ANISOU 583 C THR A 81 5602 6018 5632 -167 -447 965 C ATOM 584 O THR A 81 31.615 13.084 23.708 1.00 45.95 O ANISOU 584 O THR A 81 5630 6298 5533 -203 -469 1000 O ATOM 585 CB THR A 81 32.553 10.505 23.224 1.00 50.87 C ANISOU 585 CB THR A 81 6291 6557 6479 -91 -678 1278 C ATOM 586 OG1 THR A 81 32.140 10.752 24.577 1.00 58.19 O ANISOU 586 OG1 THR A 81 7195 7727 7186 -184 -693 1408 O ATOM 587 CG2 THR A 81 33.965 11.060 22.905 1.00 46.96 C ANISOU 587 CG2 THR A 81 5720 6092 6030 14 -692 1117 C ATOM 588 N HIS A 82 31.252 13.426 21.517 1.00 41.39 N ANISOU 588 N HIS A 82 5113 5441 5172 -154 -352 790 N ATOM 589 CA HIS A 82 31.268 14.884 21.580 1.00 38.67 C ANISOU 589 CA HIS A 82 4754 5210 4727 -172 -282 622 C ATOM 590 C HIS A 82 30.262 15.480 22.577 1.00 39.36 C ANISOU 590 C HIS A 82 4836 5489 4629 -232 -248 620 C ATOM 591 O HIS A 82 29.166 14.958 22.660 1.00 38.97 O ANISOU 591 O HIS A 82 4803 5455 4549 -273 -224 711 O ATOM 592 CB HIS A 82 30.886 15.417 20.174 1.00 36.48 C ANISOU 592 CB HIS A 82 4521 4794 4545 -157 -197 490 C ATOM 593 CG HIS A 82 31.290 16.840 19.981 1.00 35.64 C ANISOU 593 CG HIS A 82 4412 4727 4403 -167 -155 330 C ATOM 594 ND1 HIS A 82 30.451 17.898 20.276 1.00 36.58 N ANISOU 594 ND1 HIS A 82 4560 4911 4429 -192 -112 239 N ATOM 595 CD2 HIS A 82 32.475 17.381 19.594 1.00 38.88 C ANISOU 595 CD2 HIS A 82 4789 5122 4863 -163 -163 249 C ATOM 596 CE1 HIS A 82 31.114 19.032 20.073 1.00 42.88 C ANISOU 596 CE1 HIS A 82 5361 5693 5238 -205 -107 113 C ATOM 597 NE2 HIS A 82 32.335 18.740 19.637 1.00 38.18 N ANISOU 597 NE2 HIS A 82 4725 5057 4724 -204 -132 128 N ATOM 598 N PRO A 83 30.605 16.584 23.294 1.00 41.98 N ANISOU 598 N PRO A 83 5136 5976 4839 -238 -246 497 N ATOM 599 CA PRO A 83 29.637 17.179 24.242 1.00 42.64 C ANISOU 599 CA PRO A 83 5198 6269 4735 -271 -213 450 C ATOM 600 C PRO A 83 28.322 17.603 23.600 1.00 42.08 C ANISOU 600 C PRO A 83 5161 6153 4674 -265 -126 369 C ATOM 601 O PRO A 83 27.326 17.729 24.306 1.00 41.89 O ANISOU 601 O PRO A 83 5099 6315 4502 -286 -93 366 O ATOM 602 CB PRO A 83 30.363 18.404 24.776 1.00 45.76 C ANISOU 602 CB PRO A 83 5569 6762 5057 -260 -234 267 C ATOM 603 CG PRO A 83 31.850 18.037 24.655 1.00 45.56 C ANISOU 603 CG PRO A 83 5514 6672 5123 -251 -309 315 C ATOM 604 CD PRO A 83 31.905 17.299 23.346 1.00 41.54 C ANISOU 604 CD PRO A 83 5047 5932 4805 -222 -284 385 C ATOM 605 N ASN A 84 28.272 17.795 22.281 1.00 38.82 N ANISOU 605 N ASN A 84 4804 5528 4419 -235 -90 308 N ATOM 606 CA ASN A 84 27.022 18.276 21.684 1.00 37.75 C ANISOU 606 CA ASN A 84 4694 5365 4286 -216 -22 228 C ATOM 607 C ASN A 84 26.328 17.174 20.907 1.00 35.83 C ANISOU 607 C ASN A 84 4466 5018 4131 -240 -3 353 C ATOM 608 O ASN A 84 25.506 17.429 20.034 1.00 34.74 O ANISOU 608 O ASN A 84 4351 4807 4041 -220 41 295 O ATOM 609 CB ASN A 84 27.311 19.497 20.783 1.00 38.18 C ANISOU 609 CB ASN A 84 4804 5273 4429 -172 -4 61 C ATOM 610 CG ASN A 84 27.793 20.700 21.580 1.00 44.09 C ANISOU 610 CG ASN A 84 5546 6104 5103 -160 -34 -91 C ATOM 611 OD1 ASN A 84 27.090 21.241 22.460 1.00 50.68 O ANISOU 611 OD1 ASN A 84 6348 7099 5808 -135 -28 -187 O ATOM 612 ND2 ASN A 84 29.000 21.099 21.323 1.00 44.79 N ANISOU 612 ND2 ASN A 84 5650 6101 5266 -182 -69 -127 N ATOM 613 N ILE A 85 26.716 15.933 21.162 1.00 40.20 N ANISOU 613 N ILE A 85 4067 6279 4930 -609 -35 965 N ATOM 614 CA ILE A 85 26.056 14.828 20.486 1.00 41.07 C ANISOU 614 CA ILE A 85 4197 6124 5285 -440 17 1017 C ATOM 615 C ILE A 85 24.533 14.783 20.698 1.00 38.73 C ANISOU 615 C ILE A 85 4053 5813 4852 -453 37 949 C ATOM 616 O ILE A 85 23.767 14.346 19.854 1.00 36.05 O ANISOU 616 O ILE A 85 3816 5246 4635 -347 118 861 O ATOM 617 CB ILE A 85 26.804 13.540 20.824 1.00 44.70 C ANISOU 617 CB ILE A 85 4400 6541 6044 -358 -86 1336 C ATOM 618 CG1 ILE A 85 26.723 12.600 19.644 1.00 50.36 C ANISOU 618 CG1 ILE A 85 5112 6898 7125 -165 35 1253 C ATOM 619 CG2 ILE A 85 26.366 12.977 22.122 1.00 46.38 C ANISOU 619 CG2 ILE A 85 4519 6953 6150 -471 -257 1649 C ATOM 620 CD1 ILE A 85 27.791 12.949 18.604 1.00 47.15 C ANISOU 620 CD1 ILE A 85 4645 6418 6851 -109 168 1043 C ATOM 621 N ASP A 86 24.098 15.250 21.848 1.00 38.15 N ANISOU 621 N ASP A 86 3969 6023 4503 -609 -29 965 N ATOM 622 CA ASP A 86 22.683 15.284 22.140 1.00 38.08 C ANISOU 622 CA ASP A 86 4055 6063 4353 -639 8 863 C ATOM 623 C ASP A 86 21.985 16.136 21.080 1.00 34.36 C ANISOU 623 C ASP A 86 3778 5367 3911 -535 122 546 C ATOM 624 O ASP A 86 20.925 15.810 20.594 1.00 34.78 O ANISOU 624 O ASP A 86 3905 5289 4019 -458 168 488 O ATOM 625 CB ASP A 86 22.446 15.745 23.597 1.00 38.59 C ANISOU 625 CB ASP A 86 4039 6544 4079 -872 -49 864 C ATOM 626 CG ASP A 86 22.835 17.209 23.831 1.00 43.37 C ANISOU 626 CG ASP A 86 4702 7271 4505 -973 -4 563 C ATOM 627 OD1 ASP A 86 23.888 17.716 23.304 1.00 43.40 O ANISOU 627 OD1 ASP A 86 4726 7162 4601 -944 -9 530 O ATOM 628 OD2 ASP A 86 22.079 17.859 24.588 1.00 48.72 O ANISOU 628 OD2 ASP A 86 5389 8169 4953 -1104 46 336 O ATOM 629 N TYR A 87 22.574 17.254 20.736 1.00 34.24 N ANISOU 629 N TYR A 87 3837 5312 3859 -559 146 371 N ATOM 630 CA TYR A 87 21.989 18.115 19.784 1.00 32.45 C ANISOU 630 CA TYR A 87 3781 4869 3681 -491 200 148 C ATOM 631 C TYR A 87 22.064 17.496 18.384 1.00 31.55 C ANISOU 631 C TYR A 87 3731 4507 3749 -383 247 198 C ATOM 632 O TYR A 87 21.146 17.628 17.595 1.00 29.08 O ANISOU 632 O TYR A 87 3531 4042 3476 -325 269 109 O ATOM 633 CB TYR A 87 22.716 19.515 19.875 1.00 33.69 C ANISOU 633 CB TYR A 87 3998 5038 3763 -593 186 -18 C ATOM 634 CG TYR A 87 22.189 20.562 18.898 1.00 35.73 C ANISOU 634 CG TYR A 87 4436 5029 4113 -547 192 -194 C ATOM 635 CD1 TYR A 87 20.827 20.738 18.716 1.00 35.71 C ANISOU 635 CD1 TYR A 87 4488 4911 4168 -448 195 -304 C ATOM 636 CD2 TYR A 87 23.063 21.437 18.278 1.00 43.68 C ANISOU 636 CD2 TYR A 87 5529 5922 5147 -629 171 -226 C ATOM 637 CE1 TYR A 87 20.332 21.664 17.826 1.00 37.32 C ANISOU 637 CE1 TYR A 87 4825 4855 4499 -402 150 -396 C ATOM 638 CE2 TYR A 87 22.591 22.461 17.399 1.00 44.52 C ANISOU 638 CE2 TYR A 87 5798 5762 5353 -622 126 -318 C ATOM 639 CZ TYR A 87 21.216 22.508 17.139 1.00 44.98 C ANISOU 639 CZ TYR A 87 5903 5680 5508 -494 104 -378 C ATOM 640 OH TYR A 87 20.761 23.481 16.284 1.00 42.04 O ANISOU 640 OH TYR A 87 5662 5036 5275 -485 13 -402 O ATOM 641 N VAL A 88 23.169 16.838 18.051 1.00 30.38 N ANISOU 641 N VAL A 88 3489 4338 3716 -372 265 318 N ATOM 642 CA VAL A 88 23.240 16.218 16.737 1.00 31.62 C ANISOU 642 CA VAL A 88 3684 4301 4030 -305 350 287 C ATOM 643 C VAL A 88 22.189 15.127 16.606 1.00 33.06 C ANISOU 643 C VAL A 88 3869 4384 4308 -227 370 334 C ATOM 644 O VAL A 88 21.582 14.978 15.561 1.00 31.48 O ANISOU 644 O VAL A 88 3773 4052 4138 -213 429 233 O ATOM 645 CB VAL A 88 24.614 15.696 16.524 1.00 34.48 C ANISOU 645 CB VAL A 88 3888 4674 4540 -295 390 350 C ATOM 646 CG1 VAL A 88 24.696 14.869 15.232 1.00 33.17 C ANISOU 646 CG1 VAL A 88 3716 4334 4554 -241 521 251 C ATOM 647 CG2 VAL A 88 25.532 16.941 16.470 1.00 32.12 C ANISOU 647 CG2 VAL A 88 3617 4483 4105 -417 376 276 C ATOM 648 N MET A 89 21.965 14.382 17.684 1.00 34.02 N ANISOU 648 N MET A 89 3876 4597 4454 -218 306 506 N ATOM 649 CA AMET A 89 20.868 13.363 17.481 0.50 37.41 C ANISOU 649 CA AMET A 89 4327 4912 4975 -177 325 549 C ATOM 650 CA BMET A 89 20.847 13.412 17.843 0.50 38.89 C ANISOU 650 CA BMET A 89 4494 5157 5126 -193 299 585 C ATOM 651 C MET A 89 19.511 14.008 17.543 1.00 33.10 C ANISOU 651 C MET A 89 3892 4434 4249 -203 318 429 C ATOM 652 O MET A 89 18.677 13.476 16.891 1.00 33.54 O ANISOU 652 O MET A 89 4003 4378 4364 -181 353 391 O ATOM 653 CB AMET A 89 20.911 12.164 18.466 0.50 40.57 C ANISOU 653 CB AMET A 89 4575 5344 5497 -187 242 824 C ATOM 654 CB BMET A 89 20.879 12.903 19.338 0.50 41.05 C ANISOU 654 CB BMET A 89 4620 5637 5339 -269 185 840 C ATOM 655 CG AMET A 89 22.226 11.446 18.611 0.50 42.63 C ANISOU 655 CG AMET A 89 4660 5520 6019 -132 202 1001 C ATOM 656 CG BMET A 89 22.294 12.393 19.804 0.50 50.49 C ANISOU 656 CG BMET A 89 5632 6852 6699 -262 105 1069 C ATOM 657 SD AMET A 89 22.504 10.550 17.187 0.50 62.85 S ANISOU 657 SD AMET A 89 7219 7733 8930 -8 345 841 S ATOM 658 SD BMET A 89 22.513 10.753 20.620 0.50 66.05 S ANISOU 658 SD BMET A 89 7398 8757 8941 -265 -46 1500 S ATOM 659 CE AMET A 89 23.908 11.551 16.652 0.50 59.82 C ANISOU 659 CE AMET A 89 6787 7441 8499 -3 416 679 C ATOM 660 CE BMET A 89 21.013 9.810 20.338 0.50 66.55 C ANISOU 660 CE BMET A 89 7565 8647 9074 -273 -11 1511 C ATOM 661 N TYR A 90 19.305 15.138 18.200 1.00 30.40 N ANISOU 661 N TYR A 90 3570 4253 3729 -248 283 333 N ATOM 662 CA TYR A 90 18.028 15.831 18.021 1.00 29.73 C ANISOU 662 CA TYR A 90 3559 4166 3569 -226 288 167 C ATOM 663 C TYR A 90 17.807 16.212 16.539 1.00 29.29 C ANISOU 663 C TYR A 90 3640 3896 3596 -179 299 77 C ATOM 664 O TYR A 90 16.672 16.086 15.973 1.00 29.44 O ANISOU 664 O TYR A 90 3697 3859 3632 -151 291 36 O ATOM 665 CB TYR A 90 18.046 17.069 18.852 1.00 29.32 C ANISOU 665 CB TYR A 90 3492 4255 3392 -268 268 15 C ATOM 666 CG TYR A 90 16.818 17.939 18.773 1.00 31.37 C ANISOU 666 CG TYR A 90 3777 4482 3659 -211 269 -195 C ATOM 667 CD1 TYR A 90 15.576 17.491 19.183 1.00 32.80 C ANISOU 667 CD1 TYR A 90 3873 4788 3803 -202 294 -233 C ATOM 668 CD2 TYR A 90 16.943 19.239 18.291 1.00 31.98 C ANISOU 668 CD2 TYR A 90 3943 4390 3817 -172 233 -347 C ATOM 669 CE1 TYR A 90 14.477 18.357 19.093 1.00 33.47 C ANISOU 669 CE1 TYR A 90 3929 4832 3954 -120 294 -452 C ATOM 670 CE2 TYR A 90 15.871 20.127 18.224 1.00 33.42 C ANISOU 670 CE2 TYR A 90 4116 4481 4103 -87 207 -537 C ATOM 671 CZ TYR A 90 14.645 19.658 18.613 1.00 40.03 C ANISOU 671 CZ TYR A 90 4835 5449 4924 -45 243 -599 C ATOM 672 OH TYR A 90 13.586 20.533 18.523 1.00 40.04 O ANISOU 672 OH TYR A 90 4776 5351 5086 69 217 -801 O ATOM 673 N MET A 91 18.867 16.768 15.947 1.00 27.90 N ANISOU 673 N MET A 91 3521 3644 3436 -208 304 59 N ATOM 674 CA MET A 91 18.803 17.164 14.558 1.00 28.25 C ANISOU 674 CA MET A 91 3687 3548 3497 -238 300 14 C ATOM 675 C MET A 91 18.600 15.966 13.686 1.00 28.37 C ANISOU 675 C MET A 91 3702 3507 3568 -252 374 33 C ATOM 676 O MET A 91 17.934 16.097 12.666 1.00 29.82 O ANISOU 676 O MET A 91 3973 3642 3716 -302 355 0 O ATOM 677 CB MET A 91 20.126 17.895 14.086 1.00 28.58 C ANISOU 677 CB MET A 91 3775 3572 3514 -327 307 4 C ATOM 678 CG MET A 91 20.320 19.178 14.775 1.00 34.05 C ANISOU 678 CG MET A 91 4496 4273 4169 -348 231 -46 C ATOM 679 SD MET A 91 18.922 20.239 14.398 1.00 42.33 S ANISOU 679 SD MET A 91 5645 5162 5276 -299 112 -110 S ATOM 680 CE MET A 91 18.820 20.313 12.619 1.00 35.83 C ANISOU 680 CE MET A 91 4952 4230 4432 -410 58 -3 C ATOM 681 N ARG A 92 19.142 14.804 14.045 1.00 26.99 N ANISOU 681 N ARG A 92 3423 3330 3501 -224 445 88 N ATOM 682 CA ARG A 92 18.925 13.642 13.155 1.00 30.25 C ANISOU 682 CA ARG A 92 3836 3637 4021 -245 536 43 C ATOM 683 C ARG A 92 17.423 13.237 13.182 1.00 30.82 C ANISOU 683 C ARG A 92 3942 3709 4061 -246 497 56 C ATOM 684 O ARG A 92 16.804 12.953 12.147 1.00 30.58 O ANISOU 684 O ARG A 92 3979 3639 4002 -320 526 -25 O ATOM 685 CB ARG A 92 19.764 12.451 13.629 1.00 32.08 C ANISOU 685 CB ARG A 92 3920 3789 4479 -183 597 111 C ATOM 686 CG ARG A 92 19.951 11.435 12.564 1.00 35.93 C ANISOU 686 CG ARG A 92 4391 4125 5137 -209 733 -32 C ATOM 687 CD ARG A 92 20.800 10.289 13.094 1.00 45.98 C ANISOU 687 CD ARG A 92 5482 5245 6744 -106 768 45 C ATOM 688 NE ARG A 92 20.010 9.103 12.882 1.00 63.63 N ANISOU 688 NE ARG A 92 7721 7296 9157 -112 804 23 N ATOM 689 CZ ARG A 92 20.024 8.368 11.775 1.00 64.77 C ANISOU 689 CZ ARG A 92 7872 7289 9449 -160 960 -223 C ATOM 690 NH1 ARG A 92 20.868 8.644 10.771 1.00 67.18 N ANISOU 690 NH1 ARG A 92 8153 7636 9735 -212 1111 -474 N ATOM 691 NH2 ARG A 92 19.211 7.355 11.699 1.00 65.28 N ANISOU 691 NH2 ARG A 92 7955 7184 9664 -189 974 -236 N ATOM 692 N GLY A 93 16.837 13.292 14.369 1.00 30.43 N ANISOU 692 N GLY A 93 3829 3752 3979 -201 431 147 N ATOM 693 CA GLY A 93 15.402 13.081 14.476 1.00 31.15 C ANISOU 693 CA GLY A 93 3920 3897 4019 -215 396 144 C ATOM 694 C GLY A 93 14.601 14.106 13.691 1.00 28.50 C ANISOU 694 C GLY A 93 3660 3574 3596 -217 333 52 C ATOM 695 O GLY A 93 13.630 13.744 13.028 1.00 31.35 O ANISOU 695 O GLY A 93 4038 3932 3942 -263 318 34 O ATOM 696 N LEU A 94 14.921 15.397 13.813 1.00 28.58 N ANISOU 696 N LEU A 94 3700 3589 3570 -178 272 13 N ATOM 697 CA LEU A 94 14.183 16.403 13.090 1.00 30.20 C ANISOU 697 CA LEU A 94 3958 3749 3767 -169 166 -18 C ATOM 698 C LEU A 94 14.266 16.161 11.562 1.00 30.58 C ANISOU 698 C LEU A 94 4110 3745 3764 -299 154 16 C ATOM 699 O LEU A 94 13.279 16.343 10.834 1.00 30.12 O ANISOU 699 O LEU A 94 4064 3699 3682 -339 58 49 O ATOM 700 CB LEU A 94 14.770 17.793 13.429 1.00 29.45 C ANISOU 700 CB LEU A 94 3894 3595 3701 -127 100 -56 C ATOM 701 CG LEU A 94 14.459 18.317 14.852 1.00 31.58 C ANISOU 701 CG LEU A 94 4052 3950 3996 -37 110 -169 C ATOM 702 CD1 LEU A 94 15.066 19.643 14.923 1.00 32.52 C ANISOU 702 CD1 LEU A 94 4227 3954 4176 -27 48 -235 C ATOM 703 CD2 LEU A 94 12.969 18.334 15.012 1.00 34.41 C ANISOU 703 CD2 LEU A 94 4305 4360 4410 40 75 -235 C ATOM 704 N THR A 95 15.488 15.865 11.068 1.00 30.81 N ANISOU 704 N THR A 95 4192 3752 3764 -386 246 -1 N ATOM 705 CA THR A 95 15.693 15.640 9.624 1.00 30.55 C ANISOU 705 CA THR A 95 4240 3739 3627 -570 275 -25 C ATOM 706 C THR A 95 14.868 14.432 9.097 1.00 33.06 C ANISOU 706 C THR A 95 4540 4090 3931 -647 340 -86 C ATOM 707 O THR A 95 14.151 14.523 8.045 1.00 33.33 O ANISOU 707 O THR A 95 4626 4203 3836 -803 269 -71 O ATOM 708 CB THR A 95 17.194 15.427 9.342 1.00 30.19 C ANISOU 708 CB THR A 95 4197 3699 3575 -642 413 -99 C ATOM 709 OG1 THR A 95 17.920 16.637 9.738 1.00 29.52 O ANISOU 709 OG1 THR A 95 4139 3600 3475 -621 335 -35 O ATOM 710 CG2 THR A 95 17.387 15.205 7.775 1.00 33.78 C ANISOU 710 CG2 THR A 95 4718 4253 3864 -898 479 -183 C ATOM 711 N ASN A 96 14.939 13.304 9.844 1.00 31.63 N ANISOU 711 N ASN A 96 4281 3851 3885 -564 450 -129 N ATOM 712 CA ASN A 96 14.173 12.121 9.450 1.00 34.62 C ANISOU 712 CA ASN A 96 4647 4216 4293 -649 512 -196 C ATOM 713 C ASN A 96 12.696 12.365 9.556 1.00 35.38 C ANISOU 713 C ASN A 96 4723 4403 4319 -649 381 -119 C ATOM 714 O ASN A 96 11.898 11.903 8.748 1.00 38.08 O ANISOU 714 O ASN A 96 5083 4804 4582 -794 370 -160 O ATOM 715 CB ASN A 96 14.613 10.903 10.241 1.00 34.19 C ANISOU 715 CB ASN A 96 4511 4025 4455 -571 622 -207 C ATOM 716 CG ASN A 96 15.900 10.333 9.697 1.00 41.00 C ANISOU 716 CG ASN A 96 5353 4776 5449 -600 779 -353 C ATOM 717 OD1 ASN A 96 15.973 9.997 8.507 1.00 44.73 O ANISOU 717 OD1 ASN A 96 5868 5265 5863 -762 885 -547 O ATOM 718 ND2 ASN A 96 16.881 10.125 10.563 1.00 34.90 N ANISOU 718 ND2 ASN A 96 4487 3911 4863 -463 803 -282 N ATOM 719 N MET A 97 12.304 13.131 10.571 1.00 35.11 N ANISOU 719 N MET A 97 4625 4403 4312 -498 285 -32 N ATOM 720 CA MET A 97 10.883 13.481 10.714 1.00 35.59 C ANISOU 720 CA MET A 97 4610 4564 4346 -469 167 8 C ATOM 721 C MET A 97 10.417 14.390 9.557 1.00 37.05 C ANISOU 721 C MET A 97 4841 4783 4454 -543 13 61 C ATOM 722 O MET A 97 9.321 14.200 9.013 1.00 38.76 O ANISOU 722 O MET A 97 5009 5094 4623 -623 -73 95 O ATOM 723 CB MET A 97 10.598 14.052 12.131 1.00 34.99 C ANISOU 723 CB MET A 97 4418 4543 4332 -303 143 12 C ATOM 724 CG MET A 97 9.165 13.936 12.539 1.00 39.44 C ANISOU 724 CG MET A 97 4841 5246 4898 -282 98 1 C ATOM 725 SD MET A 97 8.921 14.370 14.209 1.00 38.30 S ANISOU 725 SD MET A 97 4537 5244 4770 -166 141 -70 S ATOM 726 CE MET A 97 7.112 14.401 14.215 1.00 43.36 C ANISOU 726 CE MET A 97 4979 6068 5429 -154 83 -126 C ATOM 727 N ALA A 98 11.273 15.273 9.091 1.00 35.78 N ANISOU 727 N ALA A 98 4769 4562 4265 -564 -36 99 N ATOM 728 CA ALA A 98 10.966 16.149 7.944 1.00 39.22 C ANISOU 728 CA ALA A 98 5258 5025 4619 -687 -221 227 C ATOM 729 C ALA A 98 10.912 15.303 6.663 1.00 41.49 C ANISOU 729 C ALA A 98 5612 5451 4700 -971 -172 199 C ATOM 730 O ALA A 98 10.110 15.593 5.749 1.00 43.43 O ANISOU 730 O ALA A 98 5852 5815 4835 -1125 -343 325 O ATOM 731 CB ALA A 98 12.033 17.280 7.835 1.00 37.88 C ANISOU 731 CB ALA A 98 5178 4752 4462 -687 -279 294 C ATOM 732 N LEU A 99 11.686 14.207 6.617 1.00 39.71 N ANISOU 732 N LEU A 99 5423 5219 4444 -1049 57 21 N ATOM 733 CA LEU A 99 11.720 13.414 5.400 1.00 42.25 C ANISOU 733 CA LEU A 99 5799 5674 4581 -1341 149 -98 C ATOM 734 C LEU A 99 10.433 12.628 5.332 1.00 44.62 C ANISOU 734 C LEU A 99 6038 6045 4871 -1400 118 -118 C ATOM 735 O LEU A 99 10.040 12.244 4.258 1.00 48.50 O ANISOU 735 O LEU A 99 6558 6702 5167 -1676 111 -171 O ATOM 736 CB LEU A 99 12.896 12.451 5.359 1.00 40.09 C ANISOU 736 CB LEU A 99 5542 5325 4366 -1382 417 -340 C ATOM 737 CG LEU A 99 14.159 13.081 4.869 1.00 39.10 C ANISOU 737 CG LEU A 99 5466 5244 4144 -1473 474 -371 C ATOM 738 CD1 LEU A 99 15.285 12.184 5.265 1.00 41.51 C ANISOU 738 CD1 LEU A 99 5714 5418 4641 -1383 722 -591 C ATOM 739 CD2 LEU A 99 14.104 13.193 3.352 1.00 43.34 C ANISOU 739 CD2 LEU A 99 6069 6037 4361 -1855 466 -421 C ATOM 740 N ASP A 100 9.852 12.326 6.496 1.00 46.10 N ANISOU 740 N ASP A 100 6134 6141 5242 -1182 120 -93 N ATOM 741 CA ASP A 100 8.526 11.696 6.580 1.00 50.54 C ANISOU 741 CA ASP A 100 6608 6793 5800 -1233 71 -82 C ATOM 742 C ASP A 100 7.390 12.675 6.296 1.00 54.39 C ANISOU 742 C ASP A 100 7004 7425 6238 -1216 -183 102 C ATOM 743 O ASP A 100 6.296 12.222 5.888 1.00 57.16 O ANISOU 743 O ASP A 100 7278 7926 6512 -1354 -254 120 O ATOM 744 CB ASP A 100 8.285 11.070 7.962 1.00 48.34 C ANISOU 744 CB ASP A 100 6243 6419 5705 -1053 154 -95 C ATOM 745 CG ASP A 100 7.041 10.070 7.986 1.00 51.15 C ANISOU 745 CG ASP A 100 6520 6869 6047 -1185 157 -117 C ATOM 746 OD1 ASP A 100 6.912 9.125 7.134 1.00 56.96 O ANISOU 746 OD1 ASP A 100 7315 7613 6713 -1425 235 -239 O ATOM 747 OD2 ASP A 100 6.216 10.239 8.890 1.00 54.19 O ANISOU 747 OD2 ASP A 100 6771 7332 6486 -1068 96 -39 O ATOM 748 N ASP A 101 7.643 13.969 6.530 1.00 56.55 N ANISOU 748 N ASP A 101 7265 7632 6592 -1049 -323 232 N ATOM 749 CA ASP A 101 6.658 15.076 6.486 1.00 61.49 C ANISOU 749 CA ASP A 101 7759 8291 7314 -937 -585 415 C ATOM 750 C ASP A 101 6.025 15.378 7.855 1.00 62.46 C ANISOU 750 C ASP A 101 7704 8359 7669 -641 -573 356 C ATOM 751 O ASP A 101 6.539 16.213 8.629 1.00 63.30 O ANISOU 751 O ASP A 101 7802 8322 7929 -437 -566 325 O ATOM 752 CB ASP A 101 5.559 14.851 5.429 1.00 65.26 C ANISOU 752 CB ASP A 101 8167 8981 7649 -1161 -757 534 C ATOM 753 CG ASP A 101 6.023 15.183 4.067 1.00 69.19 C ANISOU 753 CG ASP A 101 8793 9582 7914 -1454 -875 669 C ATOM 754 OD1 ASP A 101 6.923 16.045 3.987 1.00 68.13 O ANISOU 754 OD1 ASP A 101 8755 9323 7810 -1413 -920 753 O ATOM 755 OD2 ASP A 101 5.502 14.595 3.090 1.00 76.50 O ANISOU 755 OD2 ASP A 101 9722 10741 8605 -1761 -922 688 O ATOM 756 N ASP A 116 5.287 2.838 3.999 1.00 70.23 N ANISOU 756 N ASP A 116 9208 9020 8456 -2852 846 -1340 N ATOM 757 CA ASP A 116 6.561 3.554 3.721 1.00 69.74 C ANISOU 757 CA ASP A 116 9191 8925 8381 -2698 919 -1404 C ATOM 758 C ASP A 116 6.902 4.348 4.952 1.00 65.34 C ANISOU 758 C ASP A 116 8581 8286 7958 -2314 807 -1089 C ATOM 759 O ASP A 116 7.226 5.546 4.863 1.00 65.33 O ANISOU 759 O ASP A 116 8576 8450 7797 -2188 705 -952 O ATOM 760 CB ASP A 116 6.447 4.562 2.575 1.00 70.50 C ANISOU 760 CB ASP A 116 9308 9421 8059 -2893 817 -1399 C ATOM 761 CG ASP A 116 5.191 4.368 1.723 1.00 77.37 C ANISOU 761 CG ASP A 116 10151 10620 8624 -3263 705 -1421 C ATOM 762 OD1 ASP A 116 4.036 4.313 2.256 1.00 80.67 O ANISOU 762 OD1 ASP A 116 10477 11121 9051 -3237 547 -1214 O ATOM 763 OD2 ASP A 116 5.381 4.295 0.484 1.00 84.40 O ANISOU 763 OD2 ASP A 116 11096 11738 9234 -3613 776 -1654 O ATOM 764 N PRO A 117 6.819 3.720 6.128 1.00 63.14 N ANISOU 764 N PRO A 117 8260 7770 7962 -2156 813 -957 N ATOM 765 CA PRO A 117 7.146 4.545 7.295 1.00 58.28 C ANISOU 765 CA PRO A 117 7584 7155 7404 -1843 713 -684 C ATOM 766 C PRO A 117 8.651 4.597 7.595 1.00 55.11 C ANISOU 766 C PRO A 117 7210 6510 7218 -1642 821 -726 C ATOM 767 O PRO A 117 9.020 4.975 8.690 1.00 53.25 O ANISOU 767 O PRO A 117 6924 6230 7078 -1422 760 -518 O ATOM 768 CB PRO A 117 6.450 3.777 8.420 1.00 58.83 C ANISOU 768 CB PRO A 117 7585 7135 7633 -1836 672 -508 C ATOM 769 CG PRO A 117 6.692 2.345 8.007 1.00 62.16 C ANISOU 769 CG PRO A 117 8072 7233 8314 -2017 817 -710 C ATOM 770 CD PRO A 117 6.547 2.318 6.503 1.00 64.99 C ANISOU 770 CD PRO A 117 8498 7720 8475 -2266 899 -1025 C ATOM 771 N GLN A 118 9.512 4.198 6.671 1.00 53.30 N ANISOU 771 N GLN A 118 7036 6154 7063 -1736 987 -1011 N ATOM 772 CA GLN A 118 10.967 4.207 6.912 1.00 51.53 C ANISOU 772 CA GLN A 118 6791 5713 7074 -1544 1100 -1075 C ATOM 773 C GLN A 118 11.511 5.481 7.639 1.00 46.20 C ANISOU 773 C GLN A 118 6090 5170 6295 -1306 981 -829 C ATOM 774 O GLN A 118 12.286 5.367 8.559 1.00 43.23 O ANISOU 774 O GLN A 118 5655 4622 6149 -1108 981 -704 O ATOM 775 CB GLN A 118 11.754 3.937 5.604 1.00 54.86 C ANISOU 775 CB GLN A 118 7243 6121 7480 -1715 1312 -1476 C ATOM 776 CG GLN A 118 11.657 5.080 4.593 1.00 58.36 C ANISOU 776 CG GLN A 118 7744 6959 7470 -1886 1262 -1511 C ATOM 777 CD GLN A 118 12.523 4.874 3.371 1.00 65.09 C ANISOU 777 CD GLN A 118 8606 7883 8240 -2102 1489 -1908 C ATOM 778 OE1 GLN A 118 13.757 4.827 3.451 1.00 66.55 O ANISOU 778 OE1 GLN A 118 8731 7928 8628 -1969 1637 -2049 O ATOM 779 NE2 GLN A 118 11.880 4.780 2.224 1.00 68.57 N ANISOU 779 NE2 GLN A 118 9100 8594 8357 -2464 1517 -2099 N ATOM 780 N GLN A 119 11.124 6.674 7.212 1.00 45.42 N ANISOU 780 N GLN A 119 6026 5358 5875 -1343 866 -756 N ATOM 781 CA GLN A 119 11.699 7.929 7.799 1.00 41.78 C ANISOU 781 CA GLN A 119 5551 4978 5345 -1143 767 -578 C ATOM 782 C GLN A 119 11.166 8.141 9.233 1.00 40.06 C ANISOU 782 C GLN A 119 5258 4768 5197 -962 646 -336 C ATOM 783 O GLN A 119 11.882 8.563 10.166 1.00 37.11 O ANISOU 783 O GLN A 119 4843 4353 4904 -788 625 -221 O ATOM 784 CB GLN A 119 11.342 9.159 6.926 1.00 42.49 C ANISOU 784 CB GLN A 119 5694 5319 5130 -1247 642 -536 C ATOM 785 CG GLN A 119 11.441 8.957 5.368 1.00 48.64 C ANISOU 785 CG GLN A 119 6542 6238 5698 -1558 724 -747 C ATOM 786 CD GLN A 119 12.798 8.783 4.842 1.00 49.12 C ANISOU 786 CD GLN A 119 6622 6246 5796 -1614 916 -964 C ATOM 787 OE1 GLN A 119 13.779 8.769 5.589 1.00 55.77 O ANISOU 787 OE1 GLN A 119 7417 6915 6857 -1402 986 -952 O ATOM 788 NE2 GLN A 119 12.890 8.656 3.514 1.00 50.20 N ANISOU 788 NE2 GLN A 119 6804 6576 5696 -1932 1008 -1179 N ATOM 789 N ALA A 120 9.896 7.788 9.422 1.00 40.82 N ANISOU 789 N ALA A 120 5316 4955 5240 -1042 578 -276 N ATOM 790 CA ALA A 120 9.313 7.862 10.772 1.00 40.89 C ANISOU 790 CA ALA A 120 5226 5034 5278 -934 499 -89 C ATOM 791 C ALA A 120 10.003 6.891 11.731 1.00 39.71 C ANISOU 791 C ALA A 120 5045 4681 5361 -888 556 12 C ATOM 792 O ALA A 120 10.240 7.212 12.887 1.00 39.92 O ANISOU 792 O ALA A 120 5002 4775 5390 -783 505 173 O ATOM 793 CB ALA A 120 7.821 7.638 10.740 1.00 41.54 C ANISOU 793 CB ALA A 120 5241 5290 5253 -1057 429 -61 C ATOM 794 N ARG A 121 10.277 5.670 11.264 1.00 42.55 N ANISOU 794 N ARG A 121 5441 4792 5933 -990 651 -78 N ATOM 795 CA ARG A 121 11.048 4.716 12.072 1.00 42.31 C ANISOU 795 CA ARG A 121 5365 4491 6220 -930 671 56 C ATOM 796 C ARG A 121 12.440 5.227 12.426 1.00 40.96 C ANISOU 796 C ARG A 121 5159 4256 6149 -743 683 99 C ATOM 797 O ARG A 121 12.917 5.008 13.529 1.00 40.72 O ANISOU 797 O ARG A 121 5047 4176 6247 -666 609 338 O ATOM 798 CB ARG A 121 11.148 3.348 11.371 1.00 47.33 C ANISOU 798 CB ARG A 121 6033 4790 7160 -1051 781 -109 C ATOM 799 CG ARG A 121 11.596 2.209 12.277 1.00 49.08 C ANISOU 799 CG ARG A 121 6187 4679 7784 -1016 740 109 C ATOM 800 CD ARG A 121 11.336 0.819 11.577 1.00 59.40 C ANISOU 800 CD ARG A 121 7530 5613 9426 -1173 838 -84 C ATOM 801 NE ARG A 121 9.925 0.407 11.599 1.00 66.34 N ANISOU 801 NE ARG A 121 8451 6613 10143 -1410 784 -30 N ATOM 802 CZ ARG A 121 9.061 0.532 10.590 1.00 67.17 C ANISOU 802 CZ ARG A 121 8624 6898 9999 -1594 850 -287 C ATOM 803 NH1 ARG A 121 9.436 1.076 9.440 1.00 69.33 N ANISOU 803 NH1 ARG A 121 8947 7275 10121 -1599 967 -605 N ATOM 804 NH2 ARG A 121 7.819 0.105 10.735 1.00 70.73 N ANISOU 804 NH2 ARG A 121 9079 7464 10332 -1810 786 -203 N ATOM 805 N ALA A 122 13.130 5.811 11.442 1.00 41.15 N ANISOU 805 N ALA A 122 5231 4291 6113 -712 773 -123 N ATOM 806 CA ALA A 122 14.414 6.450 11.704 1.00 40.79 C ANISOU 806 CA ALA A 122 5143 4242 6114 -561 785 -98 C ATOM 807 C ALA A 122 14.271 7.579 12.723 1.00 37.70 C ANISOU 807 C ALA A 122 4728 4096 5500 -477 652 101 C ATOM 808 O ALA A 122 15.087 7.647 13.639 1.00 39.19 O ANISOU 808 O ALA A 122 4836 4271 5782 -380 608 259 O ATOM 809 CB ALA A 122 15.098 6.930 10.391 1.00 41.24 C ANISOU 809 CB ALA A 122 5255 4330 6086 -608 912 -378 C ATOM 810 N ALA A 123 13.251 8.439 12.608 1.00 34.55 N ANISOU 810 N ALA A 123 4373 3918 4837 -517 586 85 N ATOM 811 CA ALA A 123 13.093 9.544 13.595 1.00 32.92 C ANISOU 811 CA ALA A 123 4121 3921 4466 -433 490 192 C ATOM 812 C ALA A 123 12.798 8.978 14.981 1.00 33.84 C ANISOU 812 C ALA A 123 4134 4117 4607 -453 439 393 C ATOM 813 O ALA A 123 13.340 9.455 15.966 1.00 34.62 O ANISOU 813 O ALA A 123 4171 4333 4651 -407 396 494 O ATOM 814 CB ALA A 123 11.972 10.523 13.183 1.00 31.97 C ANISOU 814 CB ALA A 123 4022 3971 4153 -447 423 116 C ATOM 815 N PHE A 124 11.957 7.939 15.052 1.00 35.20 N ANISOU 815 N PHE A 124 4287 4248 4840 -566 437 460 N ATOM 816 CA PHE A 124 11.616 7.359 16.353 1.00 37.43 C ANISOU 816 CA PHE A 124 4469 4645 5106 -653 371 697 C ATOM 817 C PHE A 124 12.892 6.837 17.032 1.00 38.63 C ANISOU 817 C PHE A 124 4570 4650 5456 -612 328 909 C ATOM 818 O PHE A 124 13.153 7.093 18.235 1.00 40.16 O ANISOU 818 O PHE A 124 4674 5056 5528 -650 248 1103 O ATOM 819 CB PHE A 124 10.522 6.293 16.138 1.00 39.21 C ANISOU 819 CB PHE A 124 4696 4817 5384 -817 373 738 C ATOM 820 CG PHE A 124 10.299 5.426 17.285 1.00 41.89 C ANISOU 820 CG PHE A 124 4952 5206 5757 -964 297 1029 C ATOM 821 CD1 PHE A 124 9.428 5.801 18.329 1.00 45.94 C ANISOU 821 CD1 PHE A 124 5356 6114 5986 -1088 258 1120 C ATOM 822 CD2 PHE A 124 10.947 4.209 17.355 1.00 49.00 C ANISOU 822 CD2 PHE A 124 5861 5766 6990 -1000 259 1221 C ATOM 823 CE1 PHE A 124 9.229 4.906 19.459 1.00 44.53 C ANISOU 823 CE1 PHE A 124 5094 6038 5789 -1308 169 1455 C ATOM 824 CE2 PHE A 124 10.741 3.344 18.479 1.00 53.38 C ANISOU 824 CE2 PHE A 124 6336 6354 7592 -1182 136 1590 C ATOM 825 CZ PHE A 124 9.886 3.728 19.508 1.00 48.46 C ANISOU 825 CZ PHE A 124 5622 6181 6609 -1356 90 1716 C ATOM 826 N SER A 125 13.706 6.140 16.252 1.00 40.37 N ANISOU 826 N SER A 125 4824 4534 5981 -546 381 855 N ATOM 827 CA SER A 125 14.943 5.622 16.767 1.00 43.16 C ANISOU 827 CA SER A 125 5087 4706 6606 -471 328 1048 C ATOM 828 C SER A 125 15.840 6.760 17.214 1.00 41.12 C ANISOU 828 C SER A 125 4788 4656 6180 -378 303 1051 C ATOM 829 O SER A 125 16.357 6.722 18.355 1.00 41.66 O ANISOU 829 O SER A 125 4748 4850 6233 -406 184 1324 O ATOM 830 CB SER A 125 15.622 4.730 15.754 1.00 45.10 C ANISOU 830 CB SER A 125 5336 4545 7254 -394 428 893 C ATOM 831 OG SER A 125 16.976 4.522 16.144 1.00 51.84 O ANISOU 831 OG SER A 125 6060 5248 8389 -263 385 1031 O ATOM 832 N ASP A 126 15.978 7.807 16.370 1.00 38.68 N ANISOU 832 N ASP A 126 4564 4415 5717 -310 393 775 N ATOM 833 CA ASP A 126 16.858 8.940 16.736 1.00 37.84 C ANISOU 833 CA ASP A 126 4434 4477 5467 -246 372 758 C ATOM 834 C ASP A 126 16.484 9.553 18.075 1.00 36.45 C ANISOU 834 C ASP A 126 4198 4620 5030 -321 276 898 C ATOM 835 O ASP A 126 17.354 9.813 18.953 1.00 37.66 O ANISOU 835 O ASP A 126 4261 4906 5144 -334 204 1045 O ATOM 836 CB ASP A 126 16.802 10.073 15.667 1.00 36.79 C ANISOU 836 CB ASP A 126 4420 4380 5177 -215 448 484 C ATOM 837 CG ASP A 126 17.232 9.617 14.296 1.00 43.32 C ANISOU 837 CG ASP A 126 5298 4996 6164 -208 566 299 C ATOM 838 OD1 ASP A 126 18.114 8.713 14.190 1.00 45.77 O ANISOU 838 OD1 ASP A 126 5519 5111 6762 -159 619 316 O ATOM 839 OD2 ASP A 126 16.634 10.130 13.310 1.00 47.18 O ANISOU 839 OD2 ASP A 126 5898 5526 6503 -266 603 131 O ATOM 840 N PHE A 127 15.204 9.908 18.201 1.00 35.55 N ANISOU 840 N PHE A 127 4118 4675 4715 -386 285 808 N ATOM 841 CA PHE A 127 14.691 10.609 19.386 1.00 36.72 C ANISOU 841 CA PHE A 127 4190 5172 4590 -476 247 821 C ATOM 842 C PHE A 127 14.665 9.731 20.607 1.00 38.04 C ANISOU 842 C PHE A 127 4239 5510 4705 -643 159 1127 C ATOM 843 O PHE A 127 14.899 10.193 21.751 1.00 39.37 O ANISOU 843 O PHE A 127 4314 5997 4647 -761 113 1201 O ATOM 844 CB PHE A 127 13.248 11.171 19.154 1.00 33.90 C ANISOU 844 CB PHE A 127 3845 4949 4087 -484 294 610 C ATOM 845 CG PHE A 127 13.196 12.376 18.265 1.00 33.75 C ANISOU 845 CG PHE A 127 3910 4841 4071 -351 323 360 C ATOM 846 CD1 PHE A 127 14.120 13.460 18.402 1.00 32.73 C ANISOU 846 CD1 PHE A 127 3809 4717 3912 -290 316 269 C ATOM 847 CD2 PHE A 127 12.170 12.468 17.290 1.00 33.40 C ANISOU 847 CD2 PHE A 127 3909 4719 4061 -316 332 242 C ATOM 848 CE1 PHE A 127 14.024 14.600 17.516 1.00 32.10 C ANISOU 848 CE1 PHE A 127 3817 4511 3868 -192 309 86 C ATOM 849 CE2 PHE A 127 12.121 13.553 16.393 1.00 33.31 C ANISOU 849 CE2 PHE A 127 3972 4607 4077 -218 308 90 C ATOM 850 CZ PHE A 127 13.032 14.647 16.552 1.00 32.72 C ANISOU 850 CZ PHE A 127 3935 4500 3997 -156 292 21 C ATOM 851 N SER A 128 14.251 8.481 20.423 1.00 41.81 N ANISOU 851 N SER A 128 4715 5814 5357 -706 129 1308 N ATOM 852 CA SER A 128 14.315 7.544 21.552 1.00 44.23 C ANISOU 852 CA SER A 128 4910 6238 5657 -897 -2 1693 C ATOM 853 C SER A 128 15.823 7.338 21.984 1.00 46.56 C ANISOU 853 C SER A 128 5125 6439 6127 -849 -119 1948 C ATOM 854 O SER A 128 16.132 7.287 23.209 1.00 46.22 O ANISOU 854 O SER A 128 4963 6694 5905 -1030 -252 2238 O ATOM 855 CB SER A 128 13.465 6.276 21.304 1.00 48.87 C ANISOU 855 CB SER A 128 5517 6636 6416 -1005 -27 1847 C ATOM 856 OG SER A 128 13.945 5.532 20.199 1.00 54.64 O ANISOU 856 OG SER A 128 6321 6885 7555 -854 7 1796 O ATOM 857 N LYS A 129 16.743 7.274 21.009 1.00 46.80 N ANISOU 857 N LYS A 129 5193 6119 6470 -636 -69 1831 N ATOM 858 CA LYS A 129 18.189 7.190 21.358 1.00 48.58 C ANISOU 858 CA LYS A 129 5300 6279 6881 -565 -169 2031 C ATOM 859 C LYS A 129 18.638 8.434 22.131 1.00 47.87 C ANISOU 859 C LYS A 129 5170 6592 6425 -636 -191 1974 C ATOM 860 O LYS A 129 19.476 8.307 23.026 1.00 51.71 O ANISOU 860 O LYS A 129 5516 7235 6897 -721 -341 2268 O ATOM 861 CB LYS A 129 19.125 6.934 20.131 1.00 48.73 C ANISOU 861 CB LYS A 129 5326 5891 7299 -333 -71 1846 C ATOM 862 CG LYS A 129 19.092 5.449 19.539 1.00 55.35 C ANISOU 862 CG LYS A 129 6132 6259 8639 -264 -71 1933 C ATOM 863 CD LYS A 129 20.431 5.047 18.780 1.00 61.64 C ANISOU 863 CD LYS A 129 6809 6705 9906 -49 -8 1825 C ATOM 864 CE LYS A 129 20.382 5.379 17.264 1.00 61.79 C ANISOU 864 CE LYS A 129 6951 6586 9939 39 242 1327 C ATOM 865 NZ LYS A 129 21.627 6.003 16.607 1.00 63.65 N ANISOU 865 NZ LYS A 129 7111 6831 10240 164 359 1093 N ATOM 866 N LEU A 130 18.166 9.629 21.747 1.00 44.30 N ANISOU 866 N LEU A 130 4830 6278 5723 -602 -57 1605 N ATOM 867 CA LEU A 130 18.412 10.912 22.445 1.00 43.47 C ANISOU 867 CA LEU A 130 4708 6520 5288 -683 -48 1459 C ATOM 868 C LEU A 130 17.894 10.857 23.909 1.00 46.85 C ANISOU 868 C LEU A 130 5023 7397 5379 -956 -130 1634 C ATOM 869 O LEU A 130 18.695 11.095 24.852 1.00 48.91 O ANISOU 869 O LEU A 130 5174 7936 5475 -1103 -232 1798 O ATOM 870 CB LEU A 130 17.808 12.110 21.669 1.00 40.58 C ANISOU 870 CB LEU A 130 4480 6118 4820 -581 93 1041 C ATOM 871 CG LEU A 130 17.687 13.457 22.400 1.00 38.84 C ANISOU 871 CG LEU A 130 4248 6203 4306 -668 127 807 C ATOM 872 CD1 LEU A 130 19.085 13.967 22.887 1.00 40.77 C ANISOU 872 CD1 LEU A 130 4435 6559 4496 -723 65 872 C ATOM 873 CD2 LEU A 130 17.071 14.530 21.465 1.00 38.57 C ANISOU 873 CD2 LEU A 130 4342 6004 4310 -526 224 453 C ATOM 874 N VAL A 131 16.627 10.464 24.108 1.00 45.57 N ANISOU 874 N VAL A 131 4867 7344 5103 -1062 -95 1624 N ATOM 875 CA VAL A 131 15.988 10.489 25.433 1.00 50.45 C ANISOU 875 CA VAL A 131 5368 8463 5338 -1369 -128 1718 C ATOM 876 C VAL A 131 16.609 9.479 26.387 1.00 53.64 C ANISOU 876 C VAL A 131 5643 9015 5723 -1597 -343 2254 C ATOM 877 O VAL A 131 16.759 9.719 27.612 1.00 57.45 O ANISOU 877 O VAL A 131 6003 9991 5834 -1896 -419 2390 O ATOM 878 CB VAL A 131 14.451 10.177 25.353 1.00 50.21 C ANISOU 878 CB VAL A 131 5343 8522 5212 -1446 -36 1601 C ATOM 879 CG1 VAL A 131 13.923 10.031 26.764 1.00 55.47 C ANISOU 879 CG1 VAL A 131 5856 9753 5465 -1822 -71 1743 C ATOM 880 CG2 VAL A 131 13.769 11.293 24.679 1.00 48.41 C ANISOU 880 CG2 VAL A 131 5181 8247 4966 -1264 133 1112 C ATOM 881 N ARG A 132 16.960 8.332 25.825 1.00 55.91 N ANISOU 881 N ARG A 132 5945 8877 6423 -1476 -451 2561 N ATOM 882 CA ARG A 132 17.867 7.438 26.480 1.00 61.88 C ANISOU 882 CA ARG A 132 6566 9607 7340 -1587 -695 3095 C ATOM 883 C ARG A 132 19.328 7.686 26.013 1.00 63.13 C ANISOU 883 C ARG A 132 6680 9510 7795 -1347 -738 3097 C ATOM 884 O ARG A 132 20.001 6.820 25.399 1.00 67.18 O ANISOU 884 O ARG A 132 7150 9564 8813 -1145 -814 3284 O ATOM 885 CB ARG A 132 17.447 5.996 26.299 1.00 63.85 C ANISOU 885 CB ARG A 132 6809 9518 7932 -1616 -814 3457 C ATOM 886 CG ARG A 132 17.843 5.352 25.010 1.00 66.12 C ANISOU 886 CG ARG A 132 7166 9157 8801 -1283 -761 3363 C ATOM 887 CD ARG A 132 18.013 3.858 25.169 1.00 75.45 C ANISOU 887 CD ARG A 132 8263 9969 10436 -1327 -972 3858 C ATOM 888 NE ARG A 132 18.303 3.225 23.888 1.00 81.76 N ANISOU 888 NE ARG A 132 9117 10139 11807 -1022 -870 3658 N ATOM 889 CZ ARG A 132 17.389 2.932 22.966 1.00 82.80 C ANISOU 889 CZ ARG A 132 9399 10029 12033 -968 -698 3354 C ATOM 890 NH1 ARG A 132 16.100 3.193 23.174 1.00 81.77 N ANISOU 890 NH1 ARG A 132 9362 10208 11500 -1169 -623 3244 N ATOM 891 NH2 ARG A 132 17.775 2.366 21.829 1.00 85.30 N ANISOU 891 NH2 ARG A 132 9745 9819 12847 -729 -594 3138 N ATOM 892 N GLY A 133 19.827 8.880 26.285 1.00 61.11 N ANISOU 892 N GLY A 133 6417 9548 7252 -1372 -675 2852 N ATOM 893 CA GLY A 133 21.252 9.034 26.411 1.00 59.18 C ANISOU 893 CA GLY A 133 6052 9284 7150 -1307 -794 3013 C ATOM 894 C GLY A 133 21.449 10.257 27.267 1.00 59.13 C ANISOU 894 C GLY A 133 6020 9802 6646 -1529 -767 2827 C ATOM 895 O GLY A 133 22.427 10.385 28.012 1.00 59.67 O ANISOU 895 O GLY A 133 5936 10132 6603 -1678 -930 3073 O ATOM 896 N TYR A 134 20.508 11.183 27.152 1.00 55.82 N ANISOU 896 N TYR A 134 5733 9531 5946 -1556 -561 2368 N ATOM 897 CA TYR A 134 20.713 12.517 27.696 1.00 56.04 C ANISOU 897 CA TYR A 134 5763 9925 5604 -1699 -474 2033 C ATOM 898 C TYR A 134 19.392 12.885 28.231 1.00 56.59 C ANISOU 898 C TYR A 134 5856 10311 5335 -1879 -341 1766 C ATOM 899 O TYR A 134 18.776 13.797 27.711 1.00 53.45 O ANISOU 899 O TYR A 134 5566 9808 4934 -1740 -152 1296 O ATOM 900 CB TYR A 134 21.199 13.491 26.581 1.00 51.36 C ANISOU 900 CB TYR A 134 5307 8992 5215 -1418 -331 1640 C ATOM 901 CG TYR A 134 22.408 12.920 25.960 1.00 53.36 C ANISOU 901 CG TYR A 134 5502 8938 5835 -1238 -433 1895 C ATOM 902 CD1 TYR A 134 23.680 13.153 26.531 1.00 55.37 C ANISOU 902 CD1 TYR A 134 5608 9401 6028 -1349 -567 2077 C ATOM 903 CD2 TYR A 134 22.316 12.068 24.838 1.00 52.76 C ANISOU 903 CD2 TYR A 134 5480 8388 6179 -977 -398 1952 C ATOM 904 CE1 TYR A 134 24.829 12.572 25.972 1.00 57.10 C ANISOU 904 CE1 TYR A 134 5713 9347 6637 -1165 -658 2306 C ATOM 905 CE2 TYR A 134 23.480 11.476 24.299 1.00 52.56 C ANISOU 905 CE2 TYR A 134 5346 8088 6535 -808 -468 2141 C ATOM 906 CZ TYR A 134 24.690 11.731 24.857 1.00 56.87 C ANISOU 906 CZ TYR A 134 5727 8832 7050 -886 -594 2313 C ATOM 907 OH TYR A 134 25.812 11.164 24.312 1.00 63.64 O ANISOU 907 OH TYR A 134 6432 9429 8321 -700 -647 2463 O ATOM 908 N PRO A 135 18.933 12.154 29.281 1.00 61.69 N ANISOU 908 N PRO A 135 6377 11356 5709 -2206 -451 2086 N ATOM 909 CA PRO A 135 17.585 12.494 29.741 1.00 63.15 C ANISOU 909 CA PRO A 135 6550 11874 5569 -2384 -282 1771 C ATOM 910 C PRO A 135 17.529 13.948 30.249 1.00 64.39 C ANISOU 910 C PRO A 135 6687 12375 5403 -2497 -103 1220 C ATOM 911 O PRO A 135 16.434 14.486 30.397 1.00 66.27 O ANISOU 911 O PRO A 135 6909 12786 5487 -2537 92 799 O ATOM 912 CB PRO A 135 17.277 11.443 30.825 1.00 67.11 C ANISOU 912 CB PRO A 135 6907 12801 5792 -2787 -453 2266 C ATOM 913 CG PRO A 135 18.577 10.615 31.026 1.00 69.00 C ANISOU 913 CG PRO A 135 7067 12916 6232 -2818 -758 2889 C ATOM 914 CD PRO A 135 19.309 10.789 29.683 1.00 63.99 C ANISOU 914 CD PRO A 135 6556 11628 6129 -2334 -710 2736 C ATOM 915 N ASN A 136 18.684 14.592 30.410 1.00 62.95 N ANISOU 915 N ASN A 136 6501 12232 5187 -2517 -159 1186 N ATOM 916 CA ASN A 136 18.738 15.993 30.854 1.00 64.56 C ANISOU 916 CA ASN A 136 6698 12691 5141 -2630 6 639 C ATOM 917 C ASN A 136 19.110 17.067 29.775 1.00 61.34 C ANISOU 917 C ASN A 136 6454 11776 5076 -2275 115 248 C ATOM 918 O ASN A 136 19.331 18.253 30.080 1.00 64.10 O ANISOU 918 O ASN A 136 6812 12240 5302 -2356 223 -180 O ATOM 919 CB ASN A 136 19.590 16.085 32.157 1.00 68.80 C ANISOU 919 CB ASN A 136 7078 13836 5226 -3080 -121 824 C ATOM 920 CG ASN A 136 19.045 15.178 33.330 1.00 75.70 C ANISOU 920 CG ASN A 136 7781 15319 5663 -3532 -222 1183 C ATOM 921 OD1 ASN A 136 19.810 14.455 34.005 1.00 80.53 O ANISOU 921 OD1 ASN A 136 8273 16217 6107 -3805 -484 1750 O ATOM 922 ND2 ASN A 136 17.741 15.279 33.616 1.00 76.74 N ANISOU 922 ND2 ASN A 136 7874 15688 5594 -3646 -24 855 N ATOM 923 N SER A 137 19.113 16.661 28.513 1.00 56.35 N ANISOU 923 N SER A 137 5950 10594 4865 -1917 90 377 N ATOM 924 CA SER A 137 19.383 17.559 27.385 1.00 52.85 C ANISOU 924 CA SER A 137 5666 9683 4732 -1620 165 90 C ATOM 925 C SER A 137 18.333 18.663 27.271 1.00 52.02 C ANISOU 925 C SER A 137 5605 9517 4643 -1542 347 -452 C ATOM 926 O SER A 137 17.143 18.447 27.608 1.00 52.64 O ANISOU 926 O SER A 137 5606 9769 4626 -1585 438 -588 O ATOM 927 CB SER A 137 19.393 16.752 26.109 1.00 49.47 C ANISOU 927 CB SER A 137 5340 8779 4678 -1326 118 332 C ATOM 928 OG SER A 137 19.494 17.644 25.042 1.00 48.70 O ANISOU 928 OG SER A 137 5391 8303 4810 -1104 187 66 O ATOM 929 N GLN A 138 18.745 19.830 26.826 1.00 50.44 N ANISOU 929 N GLN A 138 5504 9071 4590 -1437 393 -754 N ATOM 930 CA GLN A 138 17.778 20.876 26.482 1.00 52.81 C ANISOU 930 CA GLN A 138 5845 9154 5067 -1282 525 -1224 C ATOM 931 C GLN A 138 16.749 20.451 25.417 1.00 50.60 C ANISOU 931 C GLN A 138 5624 8536 5065 -1004 528 -1159 C ATOM 932 O GLN A 138 15.661 21.022 25.356 1.00 50.08 O ANISOU 932 O GLN A 138 5509 8402 5118 -899 623 -1489 O ATOM 933 CB GLN A 138 18.435 22.212 26.107 1.00 54.23 C ANISOU 933 CB GLN A 138 6139 9044 5424 -1224 533 -1503 C ATOM 934 CG GLN A 138 18.888 22.382 24.690 1.00 54.37 C ANISOU 934 CG GLN A 138 6337 8554 5769 -986 442 -1328 C ATOM 935 CD GLN A 138 18.930 23.867 24.193 1.00 63.01 C ANISOU 935 CD GLN A 138 7545 9271 7127 -896 455 -1662 C ATOM 936 OE1 GLN A 138 19.991 24.533 24.270 1.00 60.57 O ANISOU 936 OE1 GLN A 138 7299 8919 6794 -1021 419 -1700 O ATOM 937 NE2 GLN A 138 17.773 24.378 23.681 1.00 62.42 N ANISOU 937 NE2 GLN A 138 7480 8908 7331 -689 484 -1876 N ATOM 938 N TYR A 139 17.090 19.431 24.628 1.00 48.62 N ANISOU 938 N TYR A 139 5449 8100 4925 -902 428 -755 N ATOM 939 CA TYR A 139 16.225 18.991 23.511 1.00 46.87 C ANISOU 939 CA TYR A 139 5297 7569 4942 -680 421 -684 C ATOM 940 C TYR A 139 15.252 17.886 23.891 1.00 49.99 C ANISOU 940 C TYR A 139 5585 8184 5226 -747 442 -541 C ATOM 941 O TYR A 139 14.402 17.511 23.076 1.00 47.98 O ANISOU 941 O TYR A 139 5363 7734 5133 -604 444 -513 O ATOM 942 CB TYR A 139 17.122 18.540 22.328 1.00 43.75 C ANISOU 942 CB TYR A 139 5043 6842 4739 -557 334 -407 C ATOM 943 CG TYR A 139 18.141 19.572 22.051 1.00 44.39 C ANISOU 943 CG TYR A 139 5211 6775 4878 -555 311 -511 C ATOM 944 CD1 TYR A 139 17.785 20.797 21.461 1.00 42.24 C ANISOU 944 CD1 TYR A 139 5032 6239 4778 -451 317 -767 C ATOM 945 CD2 TYR A 139 19.448 19.383 22.444 1.00 41.88 C ANISOU 945 CD2 TYR A 139 4864 6586 4462 -678 264 -343 C ATOM 946 CE1 TYR A 139 18.747 21.763 21.229 1.00 40.00 C ANISOU 946 CE1 TYR A 139 4840 5809 4551 -492 282 -840 C ATOM 947 CE2 TYR A 139 20.371 20.384 22.280 1.00 42.11 C ANISOU 947 CE2 TYR A 139 4961 6524 4517 -720 247 -457 C ATOM 948 CZ TYR A 139 19.999 21.547 21.640 1.00 42.46 C ANISOU 948 CZ TYR A 139 5125 6286 4721 -634 261 -702 C ATOM 949 OH TYR A 139 20.923 22.535 21.450 1.00 51.57 O ANISOU 949 OH TYR A 139 6358 7322 5913 -708 231 -788 O ATOM 950 N THR A 140 15.409 17.339 25.103 1.00 53.64 N ANISOU 950 N THR A 140 5917 9069 5393 -1005 439 -414 N ATOM 951 CA ATHR A 140 14.518 16.396 25.833 0.50 57.07 C ANISOU 951 CA ATHR A 140 6217 9844 5622 -1189 457 -278 C ATOM 952 CA BTHR A 140 14.604 16.150 25.370 0.50 56.49 C ANISOU 952 CA BTHR A 140 6197 9603 5664 -1104 425 -182 C ATOM 953 C THR A 140 13.041 16.464 25.551 1.00 55.79 C ANISOU 953 C THR A 140 5993 9679 5526 -1098 561 -513 C ATOM 954 O THR A 140 12.282 15.549 25.181 1.00 54.07 O ANISOU 954 O THR A 140 5764 9416 5363 -1082 542 -333 O ATOM 955 CB ATHR A 140 14.675 16.555 27.470 0.50 60.57 C ANISOU 955 CB ATHR A 140 6486 10908 5619 -1572 493 -341 C ATOM 956 CB BTHR A 140 15.354 15.007 26.370 0.50 59.56 C ANISOU 956 CB BTHR A 140 6495 10312 5822 -1393 292 290 C ATOM 957 OG1ATHR A 140 13.693 15.744 28.122 0.50 67.55 O ANISOU 957 OG1ATHR A 140 7234 12153 6278 -1787 523 -231 O ATOM 958 OG1BTHR A 140 16.639 14.639 25.835 0.50 60.27 O ANISOU 958 OG1BTHR A 140 6664 10116 6120 -1284 167 578 O ATOM 959 CG2ATHR A 140 14.477 17.967 27.953 0.50 63.32 C ANISOU 959 CG2ATHR A 140 6774 11409 5877 -1605 648 -897 C ATOM 960 CG2BTHR A 140 14.464 13.708 26.692 0.50 62.26 C ANISOU 960 CG2BTHR A 140 6759 10814 6085 -1549 251 590 C ATOM 961 N THR A 141 12.595 17.668 25.898 1.00 51.61 N ANISOU 961 N THR A 141 6213 6990 6405 -1243 433 -693 N ATOM 962 CA THR A 141 11.171 17.958 25.974 1.00 51.59 C ANISOU 962 CA THR A 141 6172 6928 6501 -1221 559 -837 C ATOM 963 C THR A 141 10.497 17.966 24.594 1.00 48.43 C ANISOU 963 C THR A 141 5668 6457 6275 -1058 519 -792 C ATOM 964 O THR A 141 9.473 17.332 24.445 1.00 46.20 O ANISOU 964 O THR A 141 5344 6163 6047 -1016 560 -830 O ATOM 965 CB THR A 141 10.902 19.263 26.768 1.00 53.88 C ANISOU 965 CB THR A 141 6476 7145 6853 -1316 675 -1011 C ATOM 966 OG1 THR A 141 11.338 19.058 28.117 1.00 56.64 O ANISOU 966 OG1 THR A 141 6965 7571 6983 -1528 720 -1058 O ATOM 967 CG2 THR A 141 9.398 19.619 26.718 1.00 55.88 C ANISOU 967 CG2 THR A 141 6619 7284 7327 -1273 813 -1196 C ATOM 968 N ASP A 142 11.095 18.673 23.628 1.00 45.81 N ANISOU 968 N ASP A 142 5318 6077 6009 -1000 429 -705 N ATOM 969 CA ASP A 142 10.669 18.580 22.231 1.00 43.49 C ANISOU 969 CA ASP A 142 4988 5728 5810 -912 345 -616 C ATOM 970 C ASP A 142 10.817 17.166 21.622 1.00 40.80 C ANISOU 970 C ASP A 142 4657 5481 5363 -882 326 -525 C ATOM 971 O ASP A 142 9.944 16.753 20.879 1.00 39.82 O ANISOU 971 O ASP A 142 4510 5320 5300 -831 296 -499 O ATOM 972 CB ASP A 142 11.382 19.582 21.333 1.00 43.05 C ANISOU 972 CB ASP A 142 4958 5612 5787 -925 252 -533 C ATOM 973 CG ASP A 142 10.624 19.789 20.048 1.00 48.27 C ANISOU 973 CG ASP A 142 5616 6167 6559 -896 135 -452 C ATOM 974 OD1 ASP A 142 9.363 19.905 20.165 1.00 48.32 O ANISOU 974 OD1 ASP A 142 5546 6062 6752 -842 115 -513 O ATOM 975 OD2 ASP A 142 11.192 19.700 18.915 1.00 45.10 O ANISOU 975 OD2 ASP A 142 5287 5787 6063 -948 64 -335 O ATOM 976 N ALA A 143 11.904 16.433 21.909 1.00 38.61 N ANISOU 976 N ALA A 143 4400 5302 4968 -917 328 -480 N ATOM 977 CA ALA A 143 11.973 15.061 21.431 1.00 38.81 C ANISOU 977 CA ALA A 143 4406 5388 4952 -887 322 -427 C ATOM 978 C ALA A 143 10.847 14.175 21.968 1.00 37.75 C ANISOU 978 C ALA A 143 4265 5272 4808 -864 353 -465 C ATOM 979 O ALA A 143 10.322 13.329 21.249 1.00 34.91 O ANISOU 979 O ALA A 143 3885 4921 4458 -814 348 -434 O ATOM 980 CB ALA A 143 13.373 14.407 21.686 1.00 39.33 C ANISOU 980 CB ALA A 143 4445 5506 4991 -924 294 -386 C ATOM 981 N THR A 144 10.478 14.357 23.248 1.00 40.19 N ANISOU 981 N THR A 144 4604 5587 5078 -930 401 -545 N ATOM 982 CA THR A 144 9.425 13.543 23.826 1.00 41.19 C ANISOU 982 CA THR A 144 4738 5736 5176 -952 459 -602 C ATOM 983 C THR A 144 8.073 13.904 23.183 1.00 39.21 C ANISOU 983 C THR A 144 4414 5400 5084 -870 504 -670 C ATOM 984 O THR A 144 7.245 13.013 22.885 1.00 39.42 O ANISOU 984 O THR A 144 4411 5435 5131 -828 513 -665 O ATOM 985 CB THR A 144 9.356 13.703 25.381 1.00 42.56 C ANISOU 985 CB THR A 144 4998 5941 5234 -1118 529 -696 C ATOM 986 OG1 THR A 144 10.642 13.391 25.912 1.00 50.63 O ANISOU 986 OG1 THR A 144 6088 7009 6139 -1204 416 -595 O ATOM 987 CG2 THR A 144 8.326 12.708 25.970 1.00 47.00 C ANISOU 987 CG2 THR A 144 5591 6539 5728 -1186 601 -755 C ATOM 988 N LYS A 145 7.885 15.186 22.867 1.00 40.54 N ANISOU 988 N LYS A 145 4540 5464 5397 -844 497 -716 N ATOM 989 CA LYS A 145 6.665 15.612 22.181 1.00 40.32 C ANISOU 989 CA LYS A 145 4418 5302 5599 -768 471 -755 C ATOM 990 C LYS A 145 6.582 14.998 20.797 1.00 39.12 C ANISOU 990 C LYS A 145 4279 5148 5437 -705 343 -604 C ATOM 991 O LYS A 145 5.504 14.499 20.370 1.00 39.22 O ANISOU 991 O LYS A 145 4238 5108 5557 -659 314 -606 O ATOM 992 CB LYS A 145 6.590 17.134 22.111 1.00 41.54 C ANISOU 992 CB LYS A 145 4520 5310 5954 -764 439 -813 C ATOM 993 CG LYS A 145 6.341 17.794 23.475 1.00 48.42 C ANISOU 993 CG LYS A 145 5358 6150 6888 -846 611 -1025 C ATOM 994 CD LYS A 145 6.546 19.348 23.404 1.00 56.35 C ANISOU 994 CD LYS A 145 6312 7006 8093 -843 570 -1078 C ATOM 995 CE LYS A 145 5.858 20.042 24.584 1.00 62.29 C ANISOU 995 CE LYS A 145 6977 7667 9023 -921 774 -1354 C ATOM 996 NZ LYS A 145 5.478 21.494 24.366 1.00 67.04 N ANISOU 996 NZ LYS A 145 7438 8033 10000 -878 729 -1455 N ATOM 997 N ARG A 146 7.694 14.977 20.087 1.00 35.54 N ANISOU 997 N ARG A 146 3899 4750 4854 -727 280 -490 N ATOM 998 CA ARG A 146 7.666 14.425 18.755 1.00 36.45 C ANISOU 998 CA ARG A 146 4057 4868 4923 -726 195 -377 C ATOM 999 C ARG A 146 7.483 12.919 18.763 1.00 35.66 C ANISOU 999 C ARG A 146 3953 4864 4730 -702 247 -370 C ATOM 1000 O ARG A 146 6.880 12.380 17.846 1.00 35.77 O ANISOU 1000 O ARG A 146 3984 4856 4749 -695 192 -315 O ATOM 1001 CB ARG A 146 8.933 14.816 17.985 1.00 36.27 C ANISOU 1001 CB ARG A 146 4114 4879 4787 -802 167 -302 C ATOM 1002 CG ARG A 146 8.984 16.339 17.800 1.00 38.82 C ANISOU 1002 CG ARG A 146 4457 5085 5208 -838 77 -282 C ATOM 1003 CD ARG A 146 10.075 16.719 16.955 1.00 38.77 C ANISOU 1003 CD ARG A 146 4544 5106 5079 -943 55 -211 C ATOM 1004 NE ARG A 146 10.066 18.148 16.670 1.00 43.11 N ANISOU 1004 NE ARG A 146 5132 5529 5719 -996 -67 -165 N ATOM 1005 CZ ARG A 146 9.706 18.651 15.490 1.00 46.40 C ANISOU 1005 CZ ARG A 146 5649 5840 6143 -1100 -236 -46 C ATOM 1006 NH1 ARG A 146 9.332 17.831 14.507 1.00 42.49 N ANISOU 1006 NH1 ARG A 146 5235 5366 5542 -1172 -279 26 N ATOM 1007 NH2 ARG A 146 9.741 19.978 15.305 1.00 49.72 N ANISOU 1007 NH2 ARG A 146 6100 6122 6668 -1156 -380 9 N ATOM 1008 N LEU A 147 8.012 12.253 19.787 1.00 35.40 N ANISOU 1008 N LEU A 147 3911 4923 4616 -709 325 -412 N ATOM 1009 CA LEU A 147 7.856 10.816 19.948 1.00 35.34 C ANISOU 1009 CA LEU A 147 3895 4986 4547 -693 350 -401 C ATOM 1010 C LEU A 147 6.385 10.439 20.096 1.00 35.39 C ANISOU 1010 C LEU A 147 3867 4958 4622 -657 368 -445 C ATOM 1011 O LEU A 147 6.016 9.389 19.662 1.00 37.75 O ANISOU 1011 O LEU A 147 4163 5285 4894 -632 358 -411 O ATOM 1012 CB LEU A 147 8.537 10.314 21.208 1.00 36.40 C ANISOU 1012 CB LEU A 147 4040 5184 4606 -742 370 -418 C ATOM 1013 CG LEU A 147 9.806 9.409 21.079 1.00 43.13 C ANISOU 1013 CG LEU A 147 4872 6075 5441 -754 325 -357 C ATOM 1014 CD1 LEU A 147 10.331 8.896 19.768 1.00 39.56 C ANISOU 1014 CD1 LEU A 147 4381 5619 5030 -725 339 -335 C ATOM 1015 CD2 LEU A 147 10.893 9.975 21.856 1.00 43.70 C ANISOU 1015 CD2 LEU A 147 4954 6147 5503 -816 288 -349 C ATOM 1016 N VAL A 148 5.558 11.271 20.688 1.00 37.38 N ANISOU 1016 N VAL A 148 4075 5137 4991 -660 406 -539 N ATOM 1017 CA VAL A 148 4.118 10.945 20.727 1.00 37.36 C ANISOU 1017 CA VAL A 148 3999 5074 5120 -627 435 -606 C ATOM 1018 C VAL A 148 3.525 10.832 19.338 1.00 36.39 C ANISOU 1018 C VAL A 148 3858 4872 5095 -570 303 -509 C ATOM 1019 O VAL A 148 2.803 9.854 19.016 1.00 36.17 O ANISOU 1019 O VAL A 148 3815 4858 5069 -544 292 -488 O ATOM 1020 CB VAL A 148 3.309 11.876 21.693 1.00 39.68 C ANISOU 1020 CB VAL A 148 4209 5278 5592 -660 546 -787 C ATOM 1021 CG1 VAL A 148 3.376 13.280 21.309 1.00 47.22 C ANISOU 1021 CG1 VAL A 148 5111 6097 6734 -633 478 -800 C ATOM 1022 CG2 VAL A 148 1.779 11.492 21.714 1.00 41.73 C ANISOU 1022 CG2 VAL A 148 4349 5454 6054 -630 598 -890 C ATOM 1023 N PHE A 149 3.889 11.789 18.475 1.00 36.28 N ANISOU 1023 N PHE A 149 3875 4778 5134 -580 185 -432 N ATOM 1024 CA PHE A 149 3.386 11.746 17.144 1.00 36.32 C ANISOU 1024 CA PHE A 149 3913 4698 5189 -590 22 -315 C ATOM 1025 C PHE A 149 3.954 10.607 16.367 1.00 36.83 C ANISOU 1025 C PHE A 149 4081 4881 5031 -632 35 -234 C ATOM 1026 O PHE A 149 3.240 10.033 15.577 1.00 35.80 O ANISOU 1026 O PHE A 149 3975 4718 4910 -645 -48 -173 O ATOM 1027 CB PHE A 149 3.656 13.059 16.428 1.00 38.73 C ANISOU 1027 CB PHE A 149 4260 4877 5577 -643 -133 -234 C ATOM 1028 CG PHE A 149 3.024 14.241 17.091 1.00 41.29 C ANISOU 1028 CG PHE A 149 4451 5037 6199 -597 -162 -329 C ATOM 1029 CD1 PHE A 149 1.692 14.203 17.490 1.00 43.48 C ANISOU 1029 CD1 PHE A 149 4566 5187 6769 -530 -161 -431 C ATOM 1030 CD2 PHE A 149 3.756 15.380 17.340 1.00 45.03 C ANISOU 1030 CD2 PHE A 149 4940 5472 6696 -625 -169 -343 C ATOM 1031 CE1 PHE A 149 1.101 15.276 18.121 1.00 46.64 C ANISOU 1031 CE1 PHE A 149 4803 5410 7509 -495 -149 -571 C ATOM 1032 CE2 PHE A 149 3.154 16.476 17.942 1.00 48.83 C ANISOU 1032 CE2 PHE A 149 5280 5779 7495 -586 -182 -458 C ATOM 1033 CZ PHE A 149 1.800 16.407 18.325 1.00 48.10 C ANISOU 1033 CZ PHE A 149 5004 5544 7726 -521 -165 -585 C ATOM 1034 N LEU A 150 5.249 10.339 16.543 1.00 34.69 N ANISOU 1034 N LEU A 150 3859 4725 4594 -665 130 -242 N ATOM 1035 CA LEU A 150 5.856 9.248 15.810 1.00 35.30 C ANISOU 1035 CA LEU A 150 3998 4891 4525 -711 176 -212 C ATOM 1036 C LEU A 150 5.237 7.894 16.164 1.00 36.11 C ANISOU 1036 C LEU A 150 4052 5043 4626 -650 222 -239 C ATOM 1037 O LEU A 150 5.035 7.052 15.248 1.00 37.05 O ANISOU 1037 O LEU A 150 4217 5177 4684 -686 213 -207 O ATOM 1038 CB LEU A 150 7.399 9.265 15.948 1.00 34.04 C ANISOU 1038 CB LEU A 150 3848 4805 4282 -754 269 -243 C ATOM 1039 CG LEU A 150 7.977 10.527 15.255 1.00 31.65 C ANISOU 1039 CG LEU A 150 3623 4455 3945 -853 223 -205 C ATOM 1040 CD1 LEU A 150 9.320 10.867 15.774 1.00 32.44 C ANISOU 1040 CD1 LEU A 150 3692 4604 4032 -869 304 -252 C ATOM 1041 CD2 LEU A 150 8.027 10.315 13.678 1.00 35.46 C ANISOU 1041 CD2 LEU A 150 4244 4931 4300 -1012 200 -152 C ATOM 1042 N LYS A 151 5.035 7.678 17.454 1.00 37.41 N ANISOU 1042 N LYS A 151 4149 5236 4830 -595 278 -300 N ATOM 1043 CA LYS A 151 4.519 6.365 17.957 1.00 38.58 C ANISOU 1043 CA LYS A 151 4266 5434 4958 -564 316 -320 C ATOM 1044 C LYS A 151 3.128 6.196 17.402 1.00 39.44 C ANISOU 1044 C LYS A 151 4355 5480 5149 -537 265 -308 C ATOM 1045 O LYS A 151 2.777 5.081 16.983 1.00 37.89 O ANISOU 1045 O LYS A 151 4169 5314 4915 -528 262 -284 O ATOM 1046 CB LYS A 151 4.514 6.308 19.488 1.00 35.90 C ANISOU 1046 CB LYS A 151 3904 5131 4604 -581 373 -382 C ATOM 1047 CG LYS A 151 5.879 6.150 20.150 1.00 43.71 C ANISOU 1047 CG LYS A 151 4916 6170 5522 -625 369 -363 C ATOM 1048 CD LYS A 151 5.642 5.977 21.665 1.00 47.83 C ANISOU 1048 CD LYS A 151 5471 6723 5980 -707 394 -403 C ATOM 1049 CE LYS A 151 6.515 6.874 22.543 1.00 54.15 C ANISOU 1049 CE LYS A 151 6312 7528 6734 -787 391 -420 C ATOM 1050 NZ LYS A 151 7.429 6.114 23.467 1.00 55.10 N ANISOU 1050 NZ LYS A 151 6485 7677 6775 -885 296 -351 N ATOM 1051 N ASP A 152 2.363 7.292 17.328 1.00 39.79 N ANISOU 1051 N ASP A 152 4359 5417 5344 -526 207 -324 N ATOM 1052 CA ASP A 152 1.014 7.267 16.749 1.00 40.02 C ANISOU 1052 CA ASP A 152 4336 5336 5532 -502 110 -304 C ATOM 1053 C ASP A 152 1.078 6.826 15.277 1.00 40.97 C ANISOU 1053 C ASP A 152 4565 5447 5554 -560 -13 -178 C ATOM 1054 O ASP A 152 0.326 5.936 14.845 1.00 40.97 O ANISOU 1054 O ASP A 152 4566 5443 5557 -555 -50 -149 O ATOM 1055 CB ASP A 152 0.354 8.665 16.886 1.00 41.96 C ANISOU 1055 CB ASP A 152 4486 5416 6040 -484 32 -346 C ATOM 1056 CG ASP A 152 -1.059 8.721 16.368 1.00 47.60 C ANISOU 1056 CG ASP A 152 5100 5967 7018 -455 -106 -330 C ATOM 1057 OD1 ASP A 152 -1.964 8.026 16.892 1.00 45.68 O ANISOU 1057 OD1 ASP A 152 4758 5726 6872 -417 -21 -420 O ATOM 1058 OD2 ASP A 152 -1.286 9.506 15.409 1.00 56.28 O ANISOU 1058 OD2 ASP A 152 6220 6916 8250 -489 -327 -217 O ATOM 1059 N ARG A 153 1.971 7.446 14.528 1.00 40.08 N ANISOU 1059 N ARG A 153 4557 5333 5338 -644 -63 -113 N ATOM 1060 CA ARG A 153 2.193 7.163 13.096 1.00 41.68 C ANISOU 1060 CA ARG A 153 4913 5535 5389 -779 -148 -14 C ATOM 1061 C ARG A 153 2.605 5.728 12.821 1.00 40.19 C ANISOU 1061 C ARG A 153 4762 5465 5042 -801 -16 -53 C ATOM 1062 O ARG A 153 1.981 5.053 11.993 1.00 41.39 O ANISOU 1062 O ARG A 153 4983 5601 5143 -864 -79 -5 O ATOM 1063 CB ARG A 153 3.266 8.099 12.521 1.00 42.53 C ANISOU 1063 CB ARG A 153 5136 5642 5383 -905 -164 24 C ATOM 1064 CG ARG A 153 3.776 7.601 11.140 1.00 48.03 C ANISOU 1064 CG ARG A 153 6020 6383 5846 -1110 -153 69 C ATOM 1065 CD ARG A 153 4.089 8.782 10.242 1.00 58.57 C ANISOU 1065 CD ARG A 153 7519 7638 7096 -1306 -297 171 C ATOM 1066 NE ARG A 153 3.917 8.515 8.812 1.00 59.57 N ANISOU 1066 NE ARG A 153 7874 7744 7014 -1568 -393 262 N ATOM 1067 CZ ARG A 153 4.613 7.619 8.123 1.00 62.26 C ANISOU 1067 CZ ARG A 153 8326 8199 7131 -1726 -197 175 C ATOM 1068 NH1 ARG A 153 5.517 6.878 8.744 1.00 64.68 N ANISOU 1068 NH1 ARG A 153 8495 8622 7456 -1612 74 6 N ATOM 1069 NH2 ARG A 153 4.415 7.463 6.815 1.00 57.84 N ANISOU 1069 NH2 ARG A 153 8013 7618 6347 -2022 -279 249 N ATOM 1070 N LEU A 154 3.617 5.256 13.525 1.00 37.41 N ANISOU 1070 N LEU A 154 4356 5211 4646 -753 143 -138 N ATOM 1071 CA LEU A 154 4.129 3.904 13.371 1.00 37.13 C ANISOU 1071 CA LEU A 154 4311 5253 4543 -760 260 -193 C ATOM 1072 C LEU A 154 3.122 2.859 13.829 1.00 37.66 C ANISOU 1072 C LEU A 154 4316 5328 4666 -671 245 -194 C ATOM 1073 O LEU A 154 2.989 1.879 13.168 1.00 37.44 O ANISOU 1073 O LEU A 154 4323 5317 4586 -710 271 -201 O ATOM 1074 CB LEU A 154 5.396 3.705 14.163 1.00 35.80 C ANISOU 1074 CB LEU A 154 4062 5137 4405 -720 370 -266 C ATOM 1075 CG LEU A 154 6.464 4.682 13.526 1.00 37.35 C ANISOU 1075 CG LEU A 154 4320 5329 4542 -832 411 -282 C ATOM 1076 CD1 LEU A 154 7.525 4.694 14.530 1.00 39.70 C ANISOU 1076 CD1 LEU A 154 4511 5650 4924 -769 469 -335 C ATOM 1077 CD2 LEU A 154 6.928 4.069 12.202 1.00 42.88 C ANISOU 1077 CD2 LEU A 154 5105 6046 5142 -988 514 -337 C ATOM 1078 N ALA A 155 2.424 3.107 14.931 1.00 38.45 N ANISOU 1078 N ALA A 155 4333 5411 4866 -580 221 -204 N ATOM 1079 CA ALA A 155 1.381 2.159 15.342 1.00 40.79 C ANISOU 1079 CA ALA A 155 4579 5712 5206 -526 219 -213 C ATOM 1080 C ALA A 155 0.225 2.057 14.324 1.00 43.68 C ANISOU 1080 C ALA A 155 4979 6007 5609 -553 109 -154 C ATOM 1081 O ALA A 155 -0.245 0.938 14.010 1.00 43.78 O ANISOU 1081 O ALA A 155 5001 6042 5591 -552 113 -146 O ATOM 1082 CB ALA A 155 0.842 2.566 16.723 1.00 42.10 C ANISOU 1082 CB ALA A 155 4664 5872 5459 -481 256 -273 C ATOM 1083 N LYS A 156 -0.259 3.200 13.792 1.00 45.25 N ANISOU 1083 N LYS A 156 5196 6101 5897 -587 -21 -100 N ATOM 1084 CA LYS A 156 -1.229 3.171 12.686 1.00 45.60 C ANISOU 1084 CA LYS A 156 5297 6046 5983 -653 -196 -4 C ATOM 1085 C LYS A 156 -0.812 2.286 11.495 1.00 45.55 C ANISOU 1085 C LYS A 156 5451 6098 5759 -785 -189 40 C ATOM 1086 O LYS A 156 -1.656 1.621 10.859 1.00 44.73 O ANISOU 1086 O LYS A 156 5388 5959 5648 -828 -280 92 O ATOM 1087 CB LYS A 156 -1.607 4.588 12.228 1.00 46.85 C ANISOU 1087 CB LYS A 156 5465 6048 6288 -702 -396 78 C ATOM 1088 CG LYS A 156 -2.565 5.287 13.217 1.00 50.72 C ANISOU 1088 CG LYS A 156 5751 6419 7103 -579 -421 4 C ATOM 1089 CD LYS A 156 -2.814 6.786 12.919 1.00 57.55 C ANISOU 1089 CD LYS A 156 6579 7092 8196 -606 -623 63 C ATOM 1090 CE LYS A 156 -3.617 7.429 14.034 1.00 58.99 C ANISOU 1090 CE LYS A 156 6521 7157 8736 -486 -564 -84 C ATOM 1091 NZ LYS A 156 -3.440 8.922 14.104 1.00 66.53 N ANISOU 1091 NZ LYS A 156 7418 7956 9904 -490 -673 -83 N ATOM 1092 N TYR A 157 0.482 2.325 11.166 1.00 44.30 N ANISOU 1092 N TYR A 157 5378 6016 5437 -870 -72 2 N ATOM 1093 CA TYR A 157 0.980 1.587 10.041 1.00 42.87 C ANISOU 1093 CA TYR A 157 5342 5882 5065 -1035 -5 -13 C ATOM 1094 C TYR A 157 0.919 0.134 10.437 1.00 41.67 C ANISOU 1094 C TYR A 157 5104 5795 4933 -943 121 -95 C ATOM 1095 O TYR A 157 0.390 -0.657 9.669 1.00 41.65 O ANISOU 1095 O TYR A 157 5180 5788 4857 -1026 98 -79 O ATOM 1096 CB TYR A 157 2.393 1.957 9.645 1.00 43.37 C ANISOU 1096 CB TYR A 157 5480 5997 5000 -1159 137 -84 C ATOM 1097 CG TYR A 157 2.929 1.033 8.602 1.00 42.57 C ANISOU 1097 CG TYR A 157 5494 5946 4734 -1343 285 -172 C ATOM 1098 CD1 TYR A 157 2.542 1.154 7.294 1.00 49.61 C ANISOU 1098 CD1 TYR A 157 6613 6807 5431 -1601 199 -105 C ATOM 1099 CD2 TYR A 157 3.817 0.022 8.933 1.00 43.69 C ANISOU 1099 CD2 TYR A 157 5517 6146 4938 -1283 504 -330 C ATOM 1100 CE1 TYR A 157 2.972 0.264 6.355 1.00 52.44 C ANISOU 1100 CE1 TYR A 157 7088 7212 5624 -1805 374 -221 C ATOM 1101 CE2 TYR A 157 4.268 -0.842 8.009 1.00 46.81 C ANISOU 1101 CE2 TYR A 157 5982 6564 5240 -1451 673 -456 C ATOM 1102 CZ TYR A 157 3.844 -0.726 6.715 1.00 52.11 C ANISOU 1102 CZ TYR A 157 6893 7225 5680 -1721 635 -417 C ATOM 1103 OH TYR A 157 4.305 -1.575 5.708 1.00 61.37 O ANISOU 1103 OH TYR A 157 8168 8425 6725 -1952 848 -580 O ATOM 1104 N GLU A 158 1.440 -0.212 11.609 1.00 39.30 N ANISOU 1104 N GLU A 158 4660 5543 4727 -798 227 -168 N ATOM 1105 CA GLU A 158 1.428 -1.633 12.066 1.00 39.15 C ANISOU 1105 CA GLU A 158 4559 5562 4752 -721 306 -226 C ATOM 1106 C GLU A 158 0.001 -2.165 12.184 1.00 38.65 C ANISOU 1106 C GLU A 158 4480 5475 4730 -670 211 -170 C ATOM 1107 O GLU A 158 -0.220 -3.324 11.825 1.00 37.62 O ANISOU 1107 O GLU A 158 4360 5358 4575 -685 243 -192 O ATOM 1108 CB GLU A 158 2.163 -1.881 13.387 1.00 37.02 C ANISOU 1108 CB GLU A 158 4164 5320 4580 -612 362 -270 C ATOM 1109 CG GLU A 158 3.693 -1.466 13.421 1.00 41.59 C ANISOU 1109 CG GLU A 158 4712 5906 5183 -645 450 -336 C ATOM 1110 CD GLU A 158 4.556 -2.378 12.494 1.00 50.41 C ANISOU 1110 CD GLU A 158 5818 7014 6323 -729 582 -448 C ATOM 1111 OE1 GLU A 158 4.341 -3.624 12.418 1.00 51.71 O ANISOU 1111 OE1 GLU A 158 5935 7162 6550 -705 606 -485 O ATOM 1112 OE2 GLU A 158 5.436 -1.860 11.779 1.00 51.36 O ANISOU 1112 OE2 GLU A 158 5975 7132 6406 -841 684 -521 O ATOM 1113 N TYR A 159 -0.928 -1.332 12.681 1.00 38.25 N ANISOU 1113 N TYR A 159 4385 5374 4773 -615 109 -120 N ATOM 1114 CA TYR A 159 -2.380 -1.720 12.697 1.00 40.14 C ANISOU 1114 CA TYR A 159 4582 5563 5106 -579 16 -83 C ATOM 1115 C TYR A 159 -2.912 -2.060 11.284 1.00 41.58 C ANISOU 1115 C TYR A 159 4888 5699 5213 -697 -98 -7 C ATOM 1116 O TYR A 159 -3.612 -3.104 11.066 1.00 40.95 O ANISOU 1116 O TYR A 159 4806 5623 5129 -695 -112 0 O ATOM 1117 CB TYR A 159 -3.215 -0.632 13.340 1.00 41.03 C ANISOU 1117 CB TYR A 159 4593 5592 5406 -522 -55 -83 C ATOM 1118 CG TYR A 159 -4.707 -0.927 13.242 1.00 43.93 C ANISOU 1118 CG TYR A 159 4882 5873 5938 -496 -153 -65 C ATOM 1119 CD1 TYR A 159 -5.345 -1.687 14.204 1.00 47.46 C ANISOU 1119 CD1 TYR A 159 5226 6357 6448 -436 -51 -143 C ATOM 1120 CD2 TYR A 159 -5.444 -0.468 12.161 1.00 49.07 C ANISOU 1120 CD2 TYR A 159 5571 6394 6680 -561 -366 39 C ATOM 1121 CE1 TYR A 159 -6.726 -1.995 14.088 1.00 48.33 C ANISOU 1121 CE1 TYR A 159 5244 6382 6736 -419 -124 -144 C ATOM 1122 CE2 TYR A 159 -6.820 -0.778 12.011 1.00 56.01 C ANISOU 1122 CE2 TYR A 159 6356 7168 7759 -539 -486 62 C ATOM 1123 CZ TYR A 159 -7.444 -1.514 12.985 1.00 52.08 C ANISOU 1123 CZ TYR A 159 5725 6713 7348 -456 -346 -44 C ATOM 1124 OH TYR A 159 -8.767 -1.780 12.805 1.00 58.64 O ANISOU 1124 OH TYR A 159 6447 7431 8401 -441 -454 -35 O ATOM 1125 N SER A 160 -2.550 -1.267 10.293 1.00 42.18 N ANISOU 1125 N SER A 160 5097 5733 5197 -836 -184 54 N ATOM 1126 CA SER A 160 -3.008 -1.520 8.924 1.00 44.13 C ANISOU 1126 CA SER A 160 5516 5931 5319 -1020 -316 141 C ATOM 1127 C SER A 160 -2.476 -2.894 8.486 1.00 41.94 C ANISOU 1127 C SER A 160 5304 5749 4883 -1085 -139 48 C ATOM 1128 O SER A 160 -3.187 -3.706 7.814 1.00 41.43 O ANISOU 1128 O SER A 160 5315 5667 4760 -1165 -199 80 O ATOM 1129 CB SER A 160 -2.567 -0.329 7.999 1.00 46.54 C ANISOU 1129 CB SER A 160 5995 6176 5512 -1217 -444 230 C ATOM 1130 OG SER A 160 -2.613 -0.649 6.596 1.00 58.66 O ANISOU 1130 OG SER A 160 7774 7697 6816 -1491 -522 294 O ATOM 1131 N VAL A 161 -1.246 -3.195 8.881 1.00 40.96 N ANISOU 1131 N VAL A 161 5131 5704 4728 -1050 72 -77 N ATOM 1132 CA VAL A 161 -0.618 -4.464 8.507 1.00 40.64 C ANISOU 1132 CA VAL A 161 5102 5716 4624 -1103 254 -202 C ATOM 1133 C VAL A 161 -1.342 -5.630 9.214 1.00 39.51 C ANISOU 1133 C VAL A 161 4835 5579 4599 -949 246 -207 C ATOM 1134 O VAL A 161 -1.679 -6.626 8.555 1.00 39.63 O ANISOU 1134 O VAL A 161 4908 5592 4556 -1024 273 -236 O ATOM 1135 CB VAL A 161 0.877 -4.491 8.814 1.00 41.48 C ANISOU 1135 CB VAL A 161 5131 5860 4769 -1091 453 -342 C ATOM 1136 CG1 VAL A 161 1.449 -5.841 8.450 1.00 44.83 C ANISOU 1136 CG1 VAL A 161 5513 6291 5228 -1133 634 -498 C ATOM 1137 CG2 VAL A 161 1.617 -3.410 7.975 1.00 40.94 C ANISOU 1137 CG2 VAL A 161 5208 5793 4553 -1291 493 -356 C ATOM 1138 N ALA A 162 -1.610 -5.486 10.513 1.00 38.09 N ANISOU 1138 N ALA A 162 4510 5404 4560 -771 212 -182 N ATOM 1139 CA ALA A 162 -2.367 -6.503 11.284 1.00 37.82 C ANISOU 1139 CA ALA A 162 4380 5376 4613 -660 195 -176 C ATOM 1140 C ALA A 162 -3.749 -6.752 10.686 1.00 38.37 C ANISOU 1140 C ALA A 162 4499 5406 4675 -697 72 -102 C ATOM 1141 O ALA A 162 -4.214 -7.907 10.621 1.00 38.13 O ANISOU 1141 O ALA A 162 4457 5382 4649 -686 84 -115 O ATOM 1142 CB ALA A 162 -2.474 -6.123 12.784 1.00 35.89 C ANISOU 1142 CB ALA A 162 4018 5148 4471 -539 189 -169 C ATOM 1143 N GLU A 163 -4.402 -5.694 10.222 1.00 38.81 N ANISOU 1143 N GLU A 163 4601 5397 4747 -748 -73 -18 N ATOM 1144 CA GLU A 163 -5.695 -5.831 9.535 1.00 41.11 C ANISOU 1144 CA GLU A 163 4934 5611 5074 -805 -247 73 C ATOM 1145 C GLU A 163 -5.619 -6.603 8.253 1.00 41.50 C ANISOU 1145 C GLU A 163 5160 5668 4940 -980 -257 87 C ATOM 1146 O GLU A 163 -6.436 -7.523 8.017 1.00 39.64 O ANISOU 1146 O GLU A 163 4928 5419 4715 -987 -304 107 O ATOM 1147 CB GLU A 163 -6.224 -4.475 9.223 1.00 44.58 C ANISOU 1147 CB GLU A 163 5384 5938 5617 -847 -445 173 C ATOM 1148 CG GLU A 163 -7.131 -3.924 10.256 1.00 51.15 C ANISOU 1148 CG GLU A 163 6012 6698 6725 -698 -492 157 C ATOM 1149 CD GLU A 163 -8.191 -3.037 9.627 1.00 61.01 C ANISOU 1149 CD GLU A 163 7237 7761 8181 -751 -773 274 C ATOM 1150 OE1 GLU A 163 -7.848 -2.104 8.865 1.00 63.49 O ANISOU 1150 OE1 GLU A 163 7670 8001 8451 -870 -931 371 O ATOM 1151 OE2 GLU A 163 -9.367 -3.297 9.883 1.00 62.98 O ANISOU 1151 OE2 GLU A 163 7346 7926 8659 -689 -852 272 O ATOM 1152 N TYR A 164 -4.658 -6.240 7.417 1.00 41.18 N ANISOU 1152 N TYR A 164 5274 5649 4722 -1149 -198 61 N ATOM 1153 CA TYR A 164 -4.367 -6.988 6.205 1.00 44.82 C ANISOU 1153 CA TYR A 164 5926 6132 4971 -1373 -129 15 C ATOM 1154 C TYR A 164 -4.143 -8.495 6.479 1.00 42.50 C ANISOU 1154 C TYR A 164 5546 5892 4712 -1294 58 -120 C ATOM 1155 O TYR A 164 -4.728 -9.337 5.801 1.00 43.89 O ANISOU 1155 O TYR A 164 5812 6056 4810 -1397 32 -116 O ATOM 1156 CB TYR A 164 -3.139 -6.393 5.491 1.00 46.68 C ANISOU 1156 CB TYR A 164 6311 6401 5025 -1576 2 -61 C ATOM 1157 CG TYR A 164 -2.743 -7.264 4.304 1.00 52.80 C ANISOU 1157 CG TYR A 164 7276 7206 5578 -1846 158 -179 C ATOM 1158 CD1 TYR A 164 -3.579 -7.366 3.188 1.00 59.23 C ANISOU 1158 CD1 TYR A 164 8329 7977 6199 -2103 -13 -70 C ATOM 1159 CD2 TYR A 164 -1.551 -8.004 4.312 1.00 55.10 C ANISOU 1159 CD2 TYR A 164 7499 7551 5888 -1861 474 -412 C ATOM 1160 CE1 TYR A 164 -3.241 -8.164 2.116 1.00 63.53 C ANISOU 1160 CE1 TYR A 164 9071 8554 6514 -2392 157 -202 C ATOM 1161 CE2 TYR A 164 -1.201 -8.812 3.223 1.00 60.50 C ANISOU 1161 CE2 TYR A 164 8337 8248 6401 -2130 667 -574 C ATOM 1162 CZ TYR A 164 -2.038 -8.865 2.122 1.00 64.46 C ANISOU 1162 CZ TYR A 164 9111 8731 6651 -2411 525 -474 C ATOM 1163 OH TYR A 164 -1.727 -9.661 1.012 1.00 71.71 O ANISOU 1163 OH TYR A 164 10219 9668 7360 -2732 737 -653 O ATOM 1164 N TYR A 165 -3.371 -8.809 7.518 1.00 40.63 N ANISOU 1164 N TYR A 165 5132 5693 4613 -1116 206 -217 N ATOM 1165 CA TYR A 165 -3.108 -10.197 7.916 1.00 39.66 C ANISOU 1165 CA TYR A 165 4900 5583 4587 -1029 331 -324 C ATOM 1166 C TYR A 165 -4.363 -10.900 8.408 1.00 39.58 C ANISOU 1166 C TYR A 165 4830 5560 4650 -922 209 -238 C ATOM 1167 O TYR A 165 -4.553 -12.101 8.186 1.00 38.62 O ANISOU 1167 O TYR A 165 4703 5430 4541 -934 256 -290 O ATOM 1168 CB TYR A 165 -1.993 -10.266 8.965 1.00 40.51 C ANISOU 1168 CB TYR A 165 4839 5698 4854 -887 438 -405 C ATOM 1169 CG TYR A 165 -0.693 -10.170 8.304 1.00 45.05 C ANISOU 1169 CG TYR A 165 5436 6267 5414 -1008 620 -557 C ATOM 1170 CD1 TYR A 165 -0.494 -10.847 7.103 1.00 48.72 C ANISOU 1170 CD1 TYR A 165 6006 6719 5787 -1201 762 -690 C ATOM 1171 CD2 TYR A 165 0.352 -9.445 8.854 1.00 45.48 C ANISOU 1171 CD2 TYR A 165 5405 6324 5552 -956 675 -596 C ATOM 1172 CE1 TYR A 165 0.687 -10.803 6.457 1.00 57.23 C ANISOU 1172 CE1 TYR A 165 7094 7784 6866 -1349 983 -882 C ATOM 1173 CE2 TYR A 165 1.590 -9.391 8.154 1.00 49.05 C ANISOU 1173 CE2 TYR A 165 5858 6759 6020 -1091 879 -775 C ATOM 1174 CZ TYR A 165 1.717 -10.068 6.981 1.00 52.18 C ANISOU 1174 CZ TYR A 165 6349 7141 6334 -1289 1042 -925 C ATOM 1175 OH TYR A 165 2.912 -10.080 6.256 1.00 56.59 O ANISOU 1175 OH TYR A 165 6899 7677 6924 -1462 1300 -1155 O ATOM 1176 N THR A 166 -5.238 -10.129 9.052 1.00 36.98 N ANISOU 1176 N THR A 166 4446 5216 4388 -831 67 -126 N ATOM 1177 CA THR A 166 -6.538 -10.626 9.466 1.00 37.43 C ANISOU 1177 CA THR A 166 4438 5251 4531 -759 -37 -61 C ATOM 1178 C THR A 166 -7.393 -11.007 8.250 1.00 38.56 C ANISOU 1178 C THR A 166 4712 5350 4589 -899 -152 -2 C ATOM 1179 O THR A 166 -8.089 -12.084 8.247 1.00 37.61 O ANISOU 1179 O THR A 166 4571 5226 4493 -881 -166 -1 O ATOM 1180 CB THR A 166 -7.269 -9.590 10.350 1.00 36.42 C ANISOU 1180 CB THR A 166 4199 5094 4544 -663 -126 -6 C ATOM 1181 OG1 THR A 166 -6.528 -9.462 11.555 1.00 36.28 O ANISOU 1181 OG1 THR A 166 4089 5127 4567 -569 -13 -64 O ATOM 1182 CG2 THR A 166 -8.703 -10.102 10.737 1.00 36.48 C ANISOU 1182 CG2 THR A 166 4115 5065 4680 -612 -203 26 C ATOM 1183 N GLU A 167 -7.389 -10.121 7.269 1.00 39.35 N ANISOU 1183 N GLU A 167 4957 5408 4585 -1056 -261 65 N ATOM 1184 CA GLU A 167 -8.118 -10.355 6.031 1.00 42.86 C ANISOU 1184 CA GLU A 167 5578 5797 4909 -1254 -415 149 C ATOM 1185 C GLU A 167 -7.667 -11.705 5.404 1.00 44.44 C ANISOU 1185 C GLU A 167 5878 6050 4959 -1365 -242 28 C ATOM 1186 O GLU A 167 -8.475 -12.416 4.802 1.00 44.97 O ANISOU 1186 O GLU A 167 6027 6087 4974 -1458 -333 71 O ATOM 1187 CB GLU A 167 -7.899 -9.137 5.104 1.00 43.50 C ANISOU 1187 CB GLU A 167 5844 5823 4862 -1462 -563 245 C ATOM 1188 CG GLU A 167 -8.569 -9.256 3.745 1.00 50.00 C ANISOU 1188 CG GLU A 167 6913 6575 5511 -1746 -774 364 C ATOM 1189 CD GLU A 167 -8.422 -7.969 2.883 1.00 57.12 C ANISOU 1189 CD GLU A 167 8024 7396 6284 -1992 -991 504 C ATOM 1190 OE1 GLU A 167 -8.129 -6.846 3.403 1.00 58.81 O ANISOU 1190 OE1 GLU A 167 8144 7576 6624 -1892 -1041 540 O ATOM 1191 OE2 GLU A 167 -8.591 -8.115 1.665 1.00 66.18 O ANISOU 1191 OE2 GLU A 167 9452 8510 7184 -2316 -1116 580 O ATOM 1192 N ARG A 168 -6.412 -12.081 5.619 1.00 45.14 N ANISOU 1192 N ARG A 168 5926 6196 5029 -1342 3 -134 N ATOM 1193 CA ARG A 168 -5.768 -13.278 5.039 1.00 47.66 C ANISOU 1193 CA ARG A 168 6295 6534 5281 -1449 212 -305 C ATOM 1194 C ARG A 168 -5.902 -14.517 5.899 1.00 46.91 C ANISOU 1194 C ARG A 168 6016 6435 5373 -1253 271 -362 C ATOM 1195 O ARG A 168 -5.662 -15.624 5.425 1.00 50.06 O ANISOU 1195 O ARG A 168 6433 6818 5771 -1325 399 -489 O ATOM 1196 CB ARG A 168 -4.239 -13.027 4.874 1.00 49.08 C ANISOU 1196 CB ARG A 168 6467 6736 5444 -1520 452 -484 C ATOM 1197 CG ARG A 168 -3.716 -12.030 3.803 1.00 54.29 C ANISOU 1197 CG ARG A 168 7352 7410 5866 -1805 490 -502 C ATOM 1198 CD ARG A 168 -4.540 -11.827 2.568 1.00 63.00 C ANISOU 1198 CD ARG A 168 8744 8493 6701 -2105 332 -392 C ATOM 1199 NE ARG A 168 -5.288 -13.005 2.178 1.00 72.42 N ANISOU 1199 NE ARG A 168 9980 9670 7866 -2154 317 -408 N ATOM 1200 CZ ARG A 168 -4.850 -13.982 1.384 1.00 76.34 C ANISOU 1200 CZ ARG A 168 10578 10176 8251 -2360 548 -610 C ATOM 1201 NH1 ARG A 168 -3.625 -13.938 0.870 1.00 79.45 N ANISOU 1201 NH1 ARG A 168 11027 10592 8567 -2549 845 -843 N ATOM 1202 NH2 ARG A 168 -5.655 -15.014 1.116 1.00 77.23 N ANISOU 1202 NH2 ARG A 168 10722 10267 8353 -2382 499 -601 N ATOM 1203 N GLY A 169 -6.267 -14.338 7.164 1.00 45.19 N ANISOU 1203 N GLY A 169 5633 6224 5315 -1035 184 -277 N ATOM 1204 CA GLY A 169 -6.292 -15.400 8.167 1.00 43.92 C ANISOU 1204 CA GLY A 169 5315 6055 5316 -876 212 -304 C ATOM 1205 C GLY A 169 -4.898 -15.901 8.533 1.00 43.89 C ANISOU 1205 C GLY A 169 5204 6026 5445 -830 364 -444 C ATOM 1206 O GLY A 169 -4.712 -17.095 8.824 1.00 45.12 O ANISOU 1206 O GLY A 169 5272 6132 5740 -779 395 -504 O ATOM 1207 N ALA A 170 -3.924 -14.989 8.499 1.00 44.54 N ANISOU 1207 N ALA A 170 5282 6119 5521 -852 439 -494 N ATOM 1208 CA ALA A 170 -2.511 -15.272 8.774 1.00 44.21 C ANISOU 1208 CA ALA A 170 5114 6027 5656 -819 574 -636 C ATOM 1209 C ALA A 170 -2.317 -15.007 10.245 1.00 42.78 C ANISOU 1209 C ALA A 170 4804 5844 5604 -655 460 -535 C ATOM 1210 O ALA A 170 -1.683 -14.028 10.614 1.00 40.28 O ANISOU 1210 O ALA A 170 4467 5548 5288 -634 468 -524 O ATOM 1211 CB ALA A 170 -1.589 -14.372 7.910 1.00 45.94 C ANISOU 1211 CB ALA A 170 5411 6263 5782 -965 724 -750 C ATOM 1212 N TRP A 171 -2.925 -15.864 11.084 1.00 41.36 N ANISOU 1212 N TRP A 171 4567 5645 5503 -571 347 -454 N ATOM 1213 CA TRP A 171 -3.076 -15.553 12.516 1.00 39.47 C ANISOU 1213 CA TRP A 171 4277 5425 5293 -487 223 -332 C ATOM 1214 C TRP A 171 -1.740 -15.370 13.222 1.00 38.82 C ANISOU 1214 C TRP A 171 4093 5285 5373 -450 210 -358 C ATOM 1215 O TRP A 171 -1.601 -14.511 14.115 1.00 36.99 O ANISOU 1215 O TRP A 171 3867 5094 5095 -431 152 -283 O ATOM 1216 CB TRP A 171 -3.957 -16.575 13.244 1.00 39.25 C ANISOU 1216 CB TRP A 171 4240 5386 5288 -465 115 -248 C ATOM 1217 CG TRP A 171 -5.203 -16.906 12.494 1.00 39.34 C ANISOU 1217 CG TRP A 171 4326 5432 5191 -499 121 -234 C ATOM 1218 CD1 TRP A 171 -5.602 -18.140 12.054 1.00 45.49 C ANISOU 1218 CD1 TRP A 171 5107 6166 6013 -517 112 -259 C ATOM 1219 CD2 TRP A 171 -6.219 -15.978 12.086 1.00 42.70 C ANISOU 1219 CD2 TRP A 171 4824 5919 5482 -526 109 -187 C ATOM 1220 NE1 TRP A 171 -6.821 -18.029 11.395 1.00 44.32 N ANISOU 1220 NE1 TRP A 171 5042 6062 5737 -561 96 -222 N ATOM 1221 CE2 TRP A 171 -7.211 -16.711 11.411 1.00 42.60 C ANISOU 1221 CE2 TRP A 171 4857 5897 5433 -565 78 -174 C ATOM 1222 CE3 TRP A 171 -6.375 -14.582 12.214 1.00 40.88 C ANISOU 1222 CE3 TRP A 171 4608 5726 5197 -522 100 -155 C ATOM 1223 CZ2 TRP A 171 -8.343 -16.106 10.890 1.00 43.13 C ANISOU 1223 CZ2 TRP A 171 4976 5978 5432 -601 14 -116 C ATOM 1224 CZ3 TRP A 171 -7.464 -13.998 11.684 1.00 38.45 C ANISOU 1224 CZ3 TRP A 171 4341 5421 4847 -552 41 -109 C ATOM 1225 CH2 TRP A 171 -8.436 -14.742 11.001 1.00 38.41 C ANISOU 1225 CH2 TRP A 171 4376 5393 4826 -594 -15 -83 C ATOM 1226 N VAL A 172 -0.759 -16.171 12.844 1.00 39.06 N ANISOU 1226 N VAL A 172 4015 5203 5625 -449 260 -475 N ATOM 1227 CA VAL A 172 0.525 -15.968 13.507 1.00 40.08 C ANISOU 1227 CA VAL A 172 4017 5245 5968 -413 214 -493 C ATOM 1228 C VAL A 172 1.116 -14.587 13.170 1.00 39.64 C ANISOU 1228 C VAL A 172 3993 5256 5811 -438 326 -543 C ATOM 1229 O VAL A 172 1.676 -13.916 14.059 1.00 39.07 O ANISOU 1229 O VAL A 172 3888 5183 5774 -409 241 -474 O ATOM 1230 CB VAL A 172 1.572 -17.034 13.151 1.00 42.16 C ANISOU 1230 CB VAL A 172 4096 5327 6598 -401 250 -646 C ATOM 1231 CG1 VAL A 172 2.989 -16.617 13.753 1.00 44.39 C ANISOU 1231 CG1 VAL A 172 4219 5497 7152 -367 192 -673 C ATOM 1232 CG2 VAL A 172 1.128 -18.460 13.599 1.00 46.22 C ANISOU 1232 CG2 VAL A 172 4556 5731 7272 -373 91 -581 C ATOM 1233 N ALA A 173 1.083 -14.188 11.883 1.00 39.68 N ANISOU 1233 N ALA A 173 4075 5309 5693 -522 507 -663 N ATOM 1234 CA ALA A 173 1.554 -12.830 11.534 1.00 39.35 C ANISOU 1234 CA ALA A 173 4095 5332 5523 -575 593 -688 C ATOM 1235 C ALA A 173 0.786 -11.718 12.238 1.00 37.73 C ANISOU 1235 C ALA A 173 3984 5224 5126 -536 473 -521 C ATOM 1236 O ALA A 173 1.380 -10.711 12.591 1.00 37.62 O ANISOU 1236 O ALA A 173 3961 5232 5101 -527 474 -507 O ATOM 1237 CB ALA A 173 1.437 -12.607 10.068 1.00 41.39 C ANISOU 1237 CB ALA A 173 4482 5629 5616 -731 763 -805 C ATOM 1238 N VAL A 174 -0.543 -11.876 12.396 1.00 35.76 N ANISOU 1238 N VAL A 174 3812 5024 4753 -521 386 -418 N ATOM 1239 CA VAL A 174 -1.324 -10.903 13.200 1.00 36.42 C ANISOU 1239 CA VAL A 174 3936 5170 4734 -485 297 -303 C ATOM 1240 C VAL A 174 -0.745 -10.798 14.620 1.00 36.67 C ANISOU 1240 C VAL A 174 3897 5190 4844 -438 229 -257 C ATOM 1241 O VAL A 174 -0.509 -9.689 15.126 1.00 35.03 O ANISOU 1241 O VAL A 174 3702 5016 4593 -435 226 -234 O ATOM 1242 CB VAL A 174 -2.831 -11.315 13.279 1.00 35.82 C ANISOU 1242 CB VAL A 174 3899 5116 4593 -478 230 -233 C ATOM 1243 CG1 VAL A 174 -3.573 -10.407 14.206 1.00 34.68 C ANISOU 1243 CG1 VAL A 174 3749 5009 4419 -454 184 -174 C ATOM 1244 CG2 VAL A 174 -3.449 -11.305 11.847 1.00 36.73 C ANISOU 1244 CG2 VAL A 174 4111 5228 4617 -557 245 -247 C ATOM 1245 N VAL A 175 -0.545 -11.943 15.293 1.00 36.21 N ANISOU 1245 N VAL A 175 3782 5076 4899 -424 149 -230 N ATOM 1246 CA VAL A 175 -0.096 -11.910 16.692 1.00 37.70 C ANISOU 1246 CA VAL A 175 3953 5244 5127 -438 29 -149 C ATOM 1247 C VAL A 175 1.295 -11.246 16.760 1.00 38.64 C ANISOU 1247 C VAL A 175 4005 5319 5359 -427 35 -186 C ATOM 1248 O VAL A 175 1.561 -10.473 17.677 1.00 38.36 O ANISOU 1248 O VAL A 175 4000 5310 5264 -456 -21 -129 O ATOM 1249 CB VAL A 175 -0.035 -13.332 17.304 1.00 39.18 C ANISOU 1249 CB VAL A 175 4105 5343 5440 -458 -115 -87 C ATOM 1250 CG1 VAL A 175 0.776 -13.348 18.589 1.00 40.42 C ANISOU 1250 CG1 VAL A 175 4256 5435 5668 -518 -293 13 C ATOM 1251 CG2 VAL A 175 -1.498 -13.914 17.553 1.00 38.67 C ANISOU 1251 CG2 VAL A 175 4124 5338 5231 -496 -129 -33 C ATOM 1252 N ASN A 176 2.162 -11.567 15.803 1.00 37.68 N ANISOU 1252 N ASN A 176 3789 5123 5404 -405 119 -300 N ATOM 1253 CA ASN A 176 3.500 -10.921 15.761 1.00 42.34 C ANISOU 1253 CA ASN A 176 4291 5663 6135 -401 154 -366 C ATOM 1254 C ASN A 176 3.440 -9.405 15.641 1.00 41.61 C ANISOU 1254 C ASN A 176 4288 5675 5847 -420 233 -360 C ATOM 1255 O ASN A 176 4.180 -8.665 16.348 1.00 41.68 O ANISOU 1255 O ASN A 176 4272 5675 5889 -422 180 -328 O ATOM 1256 CB ASN A 176 4.382 -11.505 14.643 1.00 42.79 C ANISOU 1256 CB ASN A 176 4218 5620 6418 -408 300 -550 C ATOM 1257 CG ASN A 176 4.707 -12.916 14.860 1.00 49.29 C ANISOU 1257 CG ASN A 176 4897 6288 7542 -377 204 -575 C ATOM 1258 OD1 ASN A 176 4.633 -13.413 15.987 1.00 53.33 O ANISOU 1258 OD1 ASN A 176 5392 6738 8133 -359 -27 -427 O ATOM 1259 ND2 ASN A 176 5.043 -13.617 13.782 1.00 51.35 N ANISOU 1259 ND2 ASN A 176 5064 6473 7975 -400 374 -767 N ATOM 1260 N ARG A 177 2.546 -8.919 14.771 1.00 40.01 N ANISOU 1260 N ARG A 177 4192 5554 5456 -446 328 -378 N ATOM 1261 CA ARG A 177 2.503 -7.483 14.533 1.00 38.51 C ANISOU 1261 CA ARG A 177 4077 5428 5126 -472 373 -369 C ATOM 1262 C ARG A 177 1.951 -6.785 15.779 1.00 37.70 C ANISOU 1262 C ARG A 177 4006 5370 4950 -446 281 -273 C ATOM 1263 O ARG A 177 2.502 -5.749 16.227 1.00 37.70 O ANISOU 1263 O ARG A 177 4008 5384 4934 -452 281 -266 O ATOM 1264 CB ARG A 177 1.624 -7.180 13.348 1.00 39.27 C ANISOU 1264 CB ARG A 177 4286 5562 5074 -531 425 -378 C ATOM 1265 CG ARG A 177 2.209 -7.387 12.034 1.00 44.12 C ANISOU 1265 CG ARG A 177 4935 6157 5670 -635 555 -491 C ATOM 1266 CD ARG A 177 3.326 -6.290 11.758 1.00 42.83 C ANISOU 1266 CD ARG A 177 4779 5999 5497 -699 640 -551 C ATOM 1267 NE ARG A 177 4.036 -6.752 10.597 1.00 47.85 N ANISOU 1267 NE ARG A 177 5428 6608 6144 -835 819 -713 N ATOM 1268 CZ ARG A 177 4.776 -6.033 9.750 1.00 48.47 C ANISOU 1268 CZ ARG A 177 5579 6700 6139 -990 956 -809 C ATOM 1269 NH1 ARG A 177 4.903 -4.715 9.882 1.00 51.89 N ANISOU 1269 NH1 ARG A 177 6082 7166 6465 -1012 900 -729 N ATOM 1270 NH2 ARG A 177 5.350 -6.663 8.708 1.00 55.00 N ANISOU 1270 NH2 ARG A 177 6418 7500 6981 -1154 1168 -1003 N ATOM 1271 N VAL A 178 0.886 -7.364 16.357 1.00 36.07 N ANISOU 1271 N VAL A 178 3824 5182 4700 -441 225 -219 N ATOM 1272 CA VAL A 178 0.261 -6.693 17.492 1.00 37.16 C ANISOU 1272 CA VAL A 178 3998 5362 4759 -465 198 -179 C ATOM 1273 C VAL A 178 1.160 -6.725 18.728 1.00 39.16 C ANISOU 1273 C VAL A 178 4250 5600 5031 -513 119 -137 C ATOM 1274 O VAL A 178 1.168 -5.795 19.542 1.00 38.27 O ANISOU 1274 O VAL A 178 4177 5521 4845 -563 130 -135 O ATOM 1275 CB VAL A 178 -1.143 -7.299 17.858 1.00 36.70 C ANISOU 1275 CB VAL A 178 3964 5327 4652 -486 192 -161 C ATOM 1276 CG1 VAL A 178 -1.727 -6.533 19.050 1.00 40.18 C ANISOU 1276 CG1 VAL A 178 4433 5806 5026 -554 227 -179 C ATOM 1277 CG2 VAL A 178 -2.036 -7.142 16.666 1.00 38.44 C ANISOU 1277 CG2 VAL A 178 4186 5542 4878 -450 223 -181 C ATOM 1278 N GLU A 179 1.915 -7.782 18.904 1.00 40.62 N ANISOU 1278 N GLU A 179 4387 5714 5332 -518 21 -102 N ATOM 1279 CA GLU A 179 2.706 -7.848 20.130 1.00 42.59 C ANISOU 1279 CA GLU A 179 4651 5921 5610 -597 -124 -23 C ATOM 1280 C GLU A 179 3.819 -6.844 19.994 1.00 42.99 C ANISOU 1280 C GLU A 179 4654 5955 5726 -573 -101 -57 C ATOM 1281 O GLU A 179 4.317 -6.319 21.010 1.00 42.06 O ANISOU 1281 O GLU A 179 4584 5835 5564 -654 -191 0 O ATOM 1282 CB GLU A 179 3.252 -9.260 20.352 1.00 44.61 C ANISOU 1282 CB GLU A 179 4844 6056 6051 -610 -298 42 C ATOM 1283 CG GLU A 179 2.158 -10.223 20.761 1.00 50.64 C ANISOU 1283 CG GLU A 179 5686 6838 6715 -673 -350 102 C ATOM 1284 CD GLU A 179 2.663 -11.521 21.330 1.00 60.80 C ANISOU 1284 CD GLU A 179 6946 7987 8170 -733 -591 212 C ATOM 1285 OE1 GLU A 179 3.805 -11.914 20.985 1.00 64.92 O ANISOU 1285 OE1 GLU A 179 7316 8366 8985 -667 -687 198 O ATOM 1286 OE2 GLU A 179 1.884 -12.152 22.110 1.00 65.52 O ANISOU 1286 OE2 GLU A 179 7664 8605 8627 -859 -685 302 O ATOM 1287 N GLY A 180 4.208 -6.556 18.754 1.00 40.93 N ANISOU 1287 N GLY A 180 4321 5686 5545 -494 21 -150 N ATOM 1288 CA GLY A 180 5.214 -5.528 18.520 1.00 42.25 C ANISOU 1288 CA GLY A 180 4449 5846 5757 -486 71 -196 C ATOM 1289 C GLY A 180 4.698 -4.136 18.788 1.00 42.61 C ANISOU 1289 C GLY A 180 4589 5979 5620 -507 132 -191 C ATOM 1290 O GLY A 180 5.413 -3.204 19.312 1.00 42.87 O ANISOU 1290 O GLY A 180 4627 6014 5646 -535 113 -183 O ATOM 1291 N MET A 181 3.432 -3.940 18.455 1.00 39.62 N ANISOU 1291 N MET A 181 4272 5655 5127 -497 195 -202 N ATOM 1292 CA MET A 181 2.800 -2.707 18.784 1.00 40.52 C ANISOU 1292 CA MET A 181 4437 5812 5146 -514 241 -215 C ATOM 1293 C MET A 181 2.685 -2.562 20.312 1.00 40.24 C ANISOU 1293 C MET A 181 4452 5800 5038 -603 202 -191 C ATOM 1294 O MET A 181 2.912 -1.472 20.834 1.00 40.88 O ANISOU 1294 O MET A 181 4559 5896 5079 -641 232 -217 O ATOM 1295 CB MET A 181 1.372 -2.696 18.206 1.00 39.58 C ANISOU 1295 CB MET A 181 4334 5705 5000 -490 282 -233 C ATOM 1296 CG MET A 181 1.366 -2.689 16.708 1.00 42.41 C ANISOU 1296 CG MET A 181 4700 6042 5374 -465 299 -239 C ATOM 1297 SD MET A 181 -0.288 -2.865 16.020 1.00 41.08 S ANISOU 1297 SD MET A 181 4548 5853 5207 -455 273 -224 S ATOM 1298 CE MET A 181 -1.144 -3.580 17.432 1.00 55.56 C ANISOU 1298 CE MET A 181 6349 7715 7048 -460 286 -238 C ATOM 1299 N LEU A 182 2.299 -3.626 21.000 1.00 42.22 N ANISOU 1299 N LEU A 182 4737 6052 5253 -666 140 -148 N ATOM 1300 CA LEU A 182 2.094 -3.585 22.472 1.00 44.71 C ANISOU 1300 CA LEU A 182 5154 6396 5437 -830 107 -126 C ATOM 1301 C LEU A 182 3.407 -3.402 23.192 1.00 48.10 C ANISOU 1301 C LEU A 182 5616 6788 5872 -908 -28 -53 C ATOM 1302 O LEU A 182 3.502 -2.614 24.184 1.00 48.49 O ANISOU 1302 O LEU A 182 5760 6869 5794 -1046 -13 -67 O ATOM 1303 CB LEU A 182 1.370 -4.843 22.974 1.00 46.21 C ANISOU 1303 CB LEU A 182 5402 6590 5566 -920 52 -80 C ATOM 1304 CG LEU A 182 0.958 -4.906 24.424 1.00 51.30 C ANISOU 1304 CG LEU A 182 6198 7275 6018 -1160 46 -71 C ATOM 1305 CD1 LEU A 182 0.122 -3.662 24.830 1.00 50.67 C ANISOU 1305 CD1 LEU A 182 6139 7256 5858 -1227 268 -230 C ATOM 1306 CD2 LEU A 182 0.194 -6.221 24.655 1.00 51.74 C ANISOU 1306 CD2 LEU A 182 6305 7330 6022 -1241 -6 -22 C ATOM 1307 N ARG A 183 4.438 -4.112 22.711 1.00 47.04 N ANISOU 1307 N ARG A 183 5392 6571 5912 -835 -158 9 N ATOM 1308 CA ARG A 183 5.773 -3.916 23.267 1.00 49.57 C ANISOU 1308 CA ARG A 183 5694 6819 6319 -889 -315 79 C ATOM 1309 C ARG A 183 6.301 -2.480 23.045 1.00 48.10 C ANISOU 1309 C ARG A 183 5490 6668 6118 -849 -209 11 C ATOM 1310 O ARG A 183 6.769 -1.841 24.018 1.00 49.67 O ANISOU 1310 O ARG A 183 5771 6870 6232 -972 -280 51 O ATOM 1311 CB ARG A 183 6.717 -4.966 22.645 1.00 49.56 C ANISOU 1311 CB ARG A 183 5535 6686 6609 -797 -443 110 C ATOM 1312 CG ARG A 183 8.040 -5.110 23.284 1.00 55.73 C ANISOU 1312 CG ARG A 183 6257 7337 7581 -857 -673 201 C ATOM 1313 CD ARG A 183 8.912 -5.981 22.365 1.00 57.20 C ANISOU 1313 CD ARG A 183 6213 7373 8148 -729 -710 147 C ATOM 1314 NE ARG A 183 9.464 -5.202 21.241 1.00 61.23 N ANISOU 1314 NE ARG A 183 6605 7909 8749 -618 -486 -10 N ATOM 1315 CZ ARG A 183 10.270 -5.710 20.296 1.00 63.56 C ANISOU 1315 CZ ARG A 183 6696 8092 9362 -537 -415 -132 C ATOM 1316 NH1 ARG A 183 10.619 -6.994 20.322 1.00 62.95 N ANISOU 1316 NH1 ARG A 183 6473 7849 9597 -517 -560 -121 N ATOM 1317 NH2 ARG A 183 10.741 -4.927 19.335 1.00 63.26 N ANISOU 1317 NH2 ARG A 183 6598 8095 9345 -498 -194 -278 N ATOM 1318 N ASP A 184 6.211 -1.941 21.823 1.00 44.98 N ANISOU 1318 N ASP A 184 5016 6296 5779 -715 -54 -80 N ATOM 1319 CA ASP A 184 6.837 -0.663 21.436 1.00 46.43 C ANISOU 1319 CA ASP A 184 5175 6492 5974 -681 25 -132 C ATOM 1320 C ASP A 184 6.006 0.654 21.448 1.00 45.07 C ANISOU 1320 C ASP A 184 5069 6385 5670 -687 153 -195 C ATOM 1321 O ASP A 184 6.558 1.769 21.654 1.00 43.96 O ANISOU 1321 O ASP A 184 4941 6247 5515 -706 172 -215 O ATOM 1322 CB ASP A 184 7.407 -0.777 20.034 1.00 47.19 C ANISOU 1322 CB ASP A 184 5166 6556 6209 -587 105 -195 C ATOM 1323 CG ASP A 184 8.607 -1.731 19.963 1.00 55.69 C ANISOU 1323 CG ASP A 184 6108 7525 7526 -575 12 -191 C ATOM 1324 OD1 ASP A 184 9.021 -2.297 21.022 1.00 59.56 O ANISOU 1324 OD1 ASP A 184 6589 7948 8093 -632 -178 -98 O ATOM 1325 OD2 ASP A 184 9.097 -1.970 18.822 1.00 60.71 O ANISOU 1325 OD2 ASP A 184 6646 8126 8295 -532 123 -289 O ATOM 1326 N TYR A 185 4.702 0.536 21.249 1.00 44.20 N ANISOU 1326 N TYR A 185 5063 6059 5672 -653 124 -159 N ATOM 1327 CA TYR A 185 3.822 1.672 21.135 1.00 42.92 C ANISOU 1327 CA TYR A 185 5019 5817 5472 -642 78 -121 C ATOM 1328 C TYR A 185 2.597 1.402 22.053 1.00 42.90 C ANISOU 1328 C TYR A 185 5014 5798 5487 -510 69 -123 C ATOM 1329 O TYR A 185 1.466 1.550 21.591 1.00 40.38 O ANISOU 1329 O TYR A 185 4723 5452 5169 -462 55 -114 O ATOM 1330 CB TYR A 185 3.345 1.821 19.682 1.00 43.48 C ANISOU 1330 CB TYR A 185 5136 5873 5511 -708 79 -90 C ATOM 1331 CG TYR A 185 4.447 1.674 18.666 1.00 44.28 C ANISOU 1331 CG TYR A 185 5203 6046 5576 -865 126 -109 C ATOM 1332 CD1 TYR A 185 5.576 2.503 18.735 1.00 43.13 C ANISOU 1332 CD1 TYR A 185 5088 5912 5387 -991 114 -127 C ATOM 1333 CD2 TYR A 185 4.370 0.733 17.627 1.00 45.75 C ANISOU 1333 CD2 TYR A 185 5320 6303 5761 -902 187 -126 C ATOM 1334 CE1 TYR A 185 6.624 2.388 17.821 1.00 45.26 C ANISOU 1334 CE1 TYR A 185 5304 6284 5608 -1163 174 -173 C ATOM 1335 CE2 TYR A 185 5.445 0.619 16.712 1.00 49.10 C ANISOU 1335 CE2 TYR A 185 5689 6825 6140 -1063 246 -181 C ATOM 1336 CZ TYR A 185 6.555 1.463 16.823 1.00 49.95 C ANISOU 1336 CZ TYR A 185 5816 6963 6199 -1199 244 -208 C ATOM 1337 OH TYR A 185 7.647 1.433 15.940 1.00 51.50 O ANISOU 1337 OH TYR A 185 5943 7291 6334 -1390 315 -286 O ATOM 1338 N PRO A 186 2.822 1.025 23.332 1.00 44.22 N ANISOU 1338 N PRO A 186 5149 5992 5662 -467 72 -142 N ATOM 1339 CA PRO A 186 1.698 0.486 24.108 1.00 45.12 C ANISOU 1339 CA PRO A 186 5243 6134 5766 -390 88 -151 C ATOM 1340 C PRO A 186 0.581 1.483 24.327 1.00 46.71 C ANISOU 1340 C PRO A 186 5490 6303 5954 -326 63 -190 C ATOM 1341 O PRO A 186 -0.564 1.040 24.539 1.00 46.75 O ANISOU 1341 O PRO A 186 5455 6355 5952 -274 91 -217 O ATOM 1342 CB PRO A 186 2.327 0.066 25.455 1.00 44.48 C ANISOU 1342 CB PRO A 186 5151 6080 5670 -397 77 -158 C ATOM 1343 CG PRO A 186 3.578 0.821 25.551 1.00 44.97 C ANISOU 1343 CG PRO A 186 5235 6109 5740 -445 43 -167 C ATOM 1344 CD PRO A 186 4.074 0.999 24.117 1.00 45.35 C ANISOU 1344 CD PRO A 186 5270 6150 5811 -504 57 -159 C ATOM 1345 N ASP A 187 0.846 2.801 24.304 1.00 46.87 N ANISOU 1345 N ASP A 187 5588 6247 5975 -328 1 -210 N ATOM 1346 CA ASP A 187 -0.269 3.656 24.757 1.00 49.75 C ANISOU 1346 CA ASP A 187 5976 6580 6348 -235 -43 -286 C ATOM 1347 C ASP A 187 -1.045 4.384 23.650 1.00 49.42 C ANISOU 1347 C ASP A 187 5988 6447 6344 -194 -125 -293 C ATOM 1348 O ASP A 187 -1.870 5.313 23.910 1.00 51.10 O ANISOU 1348 O ASP A 187 6227 6598 6589 -99 -206 -379 O ATOM 1349 CB ASP A 187 0.178 4.580 25.898 1.00 50.60 C ANISOU 1349 CB ASP A 187 6129 6658 6437 -224 -81 -341 C ATOM 1350 CG ASP A 187 1.202 5.540 25.475 1.00 58.57 C ANISOU 1350 CG ASP A 187 7238 7568 7449 -292 -154 -303 C ATOM 1351 OD1 ASP A 187 1.221 5.877 24.255 1.00 66.50 O ANISOU 1351 OD1 ASP A 187 8301 8501 8464 -335 -204 -254 O ATOM 1352 OD2 ASP A 187 2.002 5.970 26.346 1.00 66.27 O ANISOU 1352 OD2 ASP A 187 8241 8536 8402 -323 -167 -317 O ATOM 1353 N THR A 188 -0.818 3.942 22.416 1.00 46.71 N ANISOU 1353 N THR A 188 5658 6091 5998 -262 -118 -216 N ATOM 1354 CA THR A 188 -1.335 4.669 21.245 1.00 44.64 C ANISOU 1354 CA THR A 188 5487 5722 5754 -264 -222 -194 C ATOM 1355 C THR A 188 -2.778 4.168 20.982 1.00 44.37 C ANISOU 1355 C THR A 188 5378 5722 5761 -158 -219 -239 C ATOM 1356 O THR A 188 -3.143 3.034 21.350 1.00 41.31 O ANISOU 1356 O THR A 188 4877 5453 5367 -139 -111 -251 O ATOM 1357 CB THR A 188 -0.479 4.396 19.962 1.00 43.58 C ANISOU 1357 CB THR A 188 5401 5583 5573 -417 -206 -100 C ATOM 1358 OG1 THR A 188 -0.554 2.994 19.662 1.00 43.09 O ANISOU 1358 OG1 THR A 188 5225 5633 5512 -425 -93 -84 O ATOM 1359 CG2 THR A 188 1.007 4.732 20.177 1.00 40.09 C ANISOU 1359 CG2 THR A 188 4994 5151 5087 -544 -186 -75 C ATOM 1360 N GLN A 189 -3.538 5.001 20.271 1.00 44.97 N ANISOU 1360 N GLN A 189 5528 5682 5875 -106 -355 -257 N ATOM 1361 CA GLN A 189 -4.866 4.643 19.739 1.00 45.58 C ANISOU 1361 CA GLN A 189 5543 5774 6001 -15 -383 -299 C ATOM 1362 C GLN A 189 -4.857 3.356 18.836 1.00 45.11 C ANISOU 1362 C GLN A 189 5432 5800 5907 -95 -281 -214 C ATOM 1363 O GLN A 189 -5.781 2.516 18.885 1.00 45.36 O ANISOU 1363 O GLN A 189 5353 5924 5959 -37 -220 -252 O ATOM 1364 CB GLN A 189 -5.431 5.819 18.899 1.00 47.07 C ANISOU 1364 CB GLN A 189 5861 5782 6240 32 -595 -309 C ATOM 1365 CG GLN A 189 -6.825 5.508 18.317 1.00 49.27 C ANISOU 1365 CG GLN A 189 6068 6068 6584 139 -650 -365 C ATOM 1366 CD GLN A 189 -7.857 5.114 19.419 1.00 54.42 C ANISOU 1366 CD GLN A 189 6526 6862 7289 282 -566 -531 C ATOM 1367 OE1 GLN A 189 -8.732 4.260 19.185 1.00 62.23 O ANISOU 1367 OE1 GLN A 189 7396 7956 8292 313 -501 -561 O ATOM 1368 NE2 GLN A 189 -7.767 5.744 20.596 1.00 49.64 N ANISOU 1368 NE2 GLN A 189 5890 6270 6702 351 -567 -644 N ATOM 1369 N ALA A 190 -3.870 3.262 17.946 1.00 44.01 N ANISOU 1369 N ALA A 190 5375 5633 5714 -236 -273 -113 N ATOM 1370 CA ALA A 190 -3.734 2.080 17.122 1.00 42.77 C ANISOU 1370 CA ALA A 190 5166 5559 5526 -312 -177 -56 C ATOM 1371 C ALA A 190 -3.522 0.793 17.868 1.00 41.89 C ANISOU 1371 C ALA A 190 4923 5578 5415 -298 -36 -73 C ATOM 1372 O ALA A 190 -4.154 -0.184 17.481 1.00 42.90 O ANISOU 1372 O ALA A 190 4983 5765 5550 -283 12 -67 O ATOM 1373 CB ALA A 190 -2.670 2.264 16.043 1.00 44.08 C ANISOU 1373 CB ALA A 190 5429 5698 5622 -484 -183 21 C ATOM 1374 N THR A 191 -2.686 0.759 18.917 1.00 40.49 N ANISOU 1374 N THR A 191 4721 5436 5228 -307 10 -91 N ATOM 1375 CA THR A 191 -2.488 -0.450 19.721 1.00 40.56 C ANISOU 1375 CA THR A 191 4633 5541 5234 -300 103 -99 C ATOM 1376 C THR A 191 -3.833 -0.794 20.425 1.00 41.65 C ANISOU 1376 C THR A 191 4707 5738 5382 -214 122 -151 C ATOM 1377 O THR A 191 -4.164 -2.003 20.582 1.00 41.32 O ANISOU 1377 O THR A 191 4602 5771 5328 -229 182 -137 O ATOM 1378 CB THR A 191 -1.346 -0.267 20.728 1.00 40.51 C ANISOU 1378 CB THR A 191 4633 5543 5216 -328 115 -107 C ATOM 1379 OG1 THR A 191 -0.154 -0.033 19.976 1.00 39.95 O ANISOU 1379 OG1 THR A 191 4595 5450 5136 -423 111 -80 O ATOM 1380 CG2 THR A 191 -1.097 -1.532 21.580 1.00 42.78 C ANISOU 1380 CG2 THR A 191 4852 5903 5501 -330 168 -104 C ATOM 1381 N ARG A 192 -4.567 0.242 20.869 1.00 42.32 N ANISOU 1381 N ARG A 192 4802 5794 5484 -136 66 -224 N ATOM 1382 CA ARG A 192 -5.935 0.060 21.412 1.00 45.33 C ANISOU 1382 CA ARG A 192 5094 6256 5874 -61 87 -315 C ATOM 1383 C ARG A 192 -6.822 -0.661 20.405 1.00 45.57 C ANISOU 1383 C ARG A 192 5079 6312 5923 -56 94 -294 C ATOM 1384 O ARG A 192 -7.395 -1.714 20.723 1.00 48.09 O ANISOU 1384 O ARG A 192 5320 6739 6214 -81 171 -301 O ATOM 1385 CB ARG A 192 -6.524 1.436 21.840 1.00 45.78 C ANISOU 1385 CB ARG A 192 5158 6261 5974 43 -2 -433 C ATOM 1386 CG ARG A 192 -7.940 1.463 22.365 1.00 50.55 C ANISOU 1386 CG ARG A 192 5640 6965 6600 132 13 -581 C ATOM 1387 CD ARG A 192 -8.259 2.845 23.054 1.00 51.72 C ANISOU 1387 CD ARG A 192 5787 7066 6800 245 -77 -735 C ATOM 1388 NE ARG A 192 -7.194 3.222 23.986 1.00 55.00 N ANISOU 1388 NE ARG A 192 6267 7465 7167 197 -53 -716 N ATOM 1389 CZ ARG A 192 -7.198 2.951 25.297 1.00 58.17 C ANISOU 1389 CZ ARG A 192 6604 7997 7500 163 44 -788 C ATOM 1390 NH1 ARG A 192 -8.255 2.346 25.876 1.00 57.02 N ANISOU 1390 NH1 ARG A 192 6324 8024 7315 158 136 -898 N ATOM 1391 NH2 ARG A 192 -6.149 3.316 26.031 1.00 54.90 N ANISOU 1391 NH2 ARG A 192 6266 7549 7046 116 46 -754 N ATOM 1392 N ASP A 193 -6.921 -0.102 19.197 1.00 45.60 N ANISOU 1392 N ASP A 193 5149 6215 5963 -42 5 -262 N ATOM 1393 CA ASP A 193 -7.696 -0.673 18.092 1.00 45.48 C ANISOU 1393 CA ASP A 193 5111 6205 5964 -43 -9 -234 C ATOM 1394 C ASP A 193 -7.228 -2.090 17.671 1.00 44.82 C ANISOU 1394 C ASP A 193 5003 6185 5840 -137 89 -151 C ATOM 1395 O ASP A 193 -8.011 -2.940 17.211 1.00 42.93 O ANISOU 1395 O ASP A 193 4709 6000 5604 -139 118 -145 O ATOM 1396 CB ASP A 193 -7.589 0.205 16.843 1.00 47.08 C ANISOU 1396 CB ASP A 193 5433 6269 6185 -56 -139 -186 C ATOM 1397 CG ASP A 193 -8.204 1.628 17.001 1.00 52.30 C ANISOU 1397 CG ASP A 193 6142 6818 6909 54 -299 -270 C ATOM 1398 OD1 ASP A 193 -9.033 1.884 17.903 1.00 53.34 O ANISOU 1398 OD1 ASP A 193 6174 7003 7090 169 -304 -401 O ATOM 1399 OD2 ASP A 193 -7.821 2.499 16.174 1.00 53.79 O ANISOU 1399 OD2 ASP A 193 6478 6864 7095 12 -432 -211 O ATOM 1400 N ALA A 194 -5.933 -2.339 17.767 1.00 42.57 N ANISOU 1400 N ALA A 194 4758 5889 5529 -210 128 -98 N ATOM 1401 CA ALA A 194 -5.407 -3.634 17.370 1.00 40.34 C ANISOU 1401 CA ALA A 194 4447 5650 5232 -277 194 -50 C ATOM 1402 C ALA A 194 -5.489 -4.754 18.417 1.00 38.81 C ANISOU 1402 C ALA A 194 4193 5530 5022 -282 251 -55 C ATOM 1403 O ALA A 194 -5.352 -5.925 18.087 1.00 36.63 O ANISOU 1403 O ALA A 194 3896 5275 4748 -320 276 -24 O ATOM 1404 CB ALA A 194 -3.957 -3.438 16.899 1.00 40.56 C ANISOU 1404 CB ALA A 194 4522 5642 5248 -353 197 -22 C ATOM 1405 N LEU A 195 -5.656 -4.455 19.704 1.00 36.92 N ANISOU 1405 N LEU A 195 3940 5327 4762 -261 260 -93 N ATOM 1406 CA LEU A 195 -5.695 -5.585 20.624 1.00 37.30 C ANISOU 1406 CA LEU A 195 3965 5438 4771 -309 295 -76 C ATOM 1407 C LEU A 195 -6.796 -6.643 20.278 1.00 37.06 C ANISOU 1407 C LEU A 195 3890 5468 4721 -338 323 -64 C ATOM 1408 O LEU A 195 -6.515 -7.822 20.398 1.00 35.87 O ANISOU 1408 O LEU A 195 3756 5318 4556 -395 320 -15 O ATOM 1409 CB LEU A 195 -5.871 -5.155 22.108 1.00 38.92 C ANISOU 1409 CB LEU A 195 4166 5698 4923 -316 310 -124 C ATOM 1410 CG LEU A 195 -4.637 -4.389 22.518 1.00 41.18 C ANISOU 1410 CG LEU A 195 4503 5920 5224 -306 278 -120 C ATOM 1411 CD1 LEU A 195 -4.920 -3.799 23.935 1.00 45.07 C ANISOU 1411 CD1 LEU A 195 4993 6471 5659 -310 293 -183 C ATOM 1412 CD2 LEU A 195 -3.412 -5.282 22.440 1.00 40.73 C ANISOU 1412 CD2 LEU A 195 4473 5818 5185 -352 254 -58 C ATOM 1413 N PRO A 196 -8.003 -6.225 19.890 1.00 36.12 N ANISOU 1413 N PRO A 196 3719 5393 4610 -297 330 -116 N ATOM 1414 CA PRO A 196 -8.982 -7.303 19.572 1.00 37.05 C ANISOU 1414 CA PRO A 196 3793 5580 4706 -342 359 -103 C ATOM 1415 C PRO A 196 -8.584 -8.188 18.353 1.00 36.63 C ANISOU 1415 C PRO A 196 3771 5463 4685 -364 341 -31 C ATOM 1416 O PRO A 196 -9.035 -9.364 18.270 1.00 35.37 O ANISOU 1416 O PRO A 196 3601 5337 4500 -424 354 1 O ATOM 1417 CB PRO A 196 -10.252 -6.556 19.316 1.00 36.88 C ANISOU 1417 CB PRO A 196 3693 5614 4706 -276 355 -194 C ATOM 1418 CG PRO A 196 -10.057 -5.200 19.948 1.00 38.94 C ANISOU 1418 CG PRO A 196 3954 5853 4987 -202 328 -272 C ATOM 1419 CD PRO A 196 -8.642 -4.894 19.912 1.00 37.48 C ANISOU 1419 CD PRO A 196 3863 5565 4812 -211 301 -203 C ATOM 1420 N LEU A 197 -7.729 -7.683 17.457 1.00 36.53 N ANISOU 1420 N LEU A 197 3798 5368 4715 -337 313 -13 N ATOM 1421 CA LEU A 197 -7.241 -8.512 16.315 1.00 35.39 C ANISOU 1421 CA LEU A 197 3670 5185 4592 -369 310 25 C ATOM 1422 C LEU A 197 -6.386 -9.588 16.888 1.00 34.66 C ANISOU 1422 C LEU A 197 3589 5078 4503 -405 304 45 C ATOM 1423 O LEU A 197 -6.344 -10.726 16.422 1.00 33.12 O ANISOU 1423 O LEU A 197 3393 4869 4323 -431 292 61 O ATOM 1424 CB LEU A 197 -6.402 -7.677 15.277 1.00 35.90 C ANISOU 1424 CB LEU A 197 3774 5192 4672 -373 292 24 C ATOM 1425 CG LEU A 197 -7.128 -6.589 14.453 1.00 38.90 C ANISOU 1425 CG LEU A 197 4186 5543 5050 -352 248 22 C ATOM 1426 CD1 LEU A 197 -6.081 -5.873 13.631 1.00 41.42 C ANISOU 1426 CD1 LEU A 197 4574 5810 5352 -410 229 36 C ATOM 1427 CD2 LEU A 197 -8.124 -7.104 13.526 1.00 42.46 C ANISOU 1427 CD2 LEU A 197 4621 6009 5503 -356 237 34 C ATOM 1428 N MET A 198 -5.622 -9.247 17.910 1.00 36.67 N ANISOU 1428 N MET A 198 3862 5319 4753 -402 292 38 N ATOM 1429 CA MET A 198 -4.706 -10.222 18.482 1.00 35.54 C ANISOU 1429 CA MET A 198 3740 5137 4628 -425 247 53 C ATOM 1430 C MET A 198 -5.483 -11.251 19.312 1.00 38.53 C ANISOU 1430 C MET A 198 4147 5537 4954 -484 223 95 C ATOM 1431 O MET A 198 -5.201 -12.453 19.265 1.00 36.51 O ANISOU 1431 O MET A 198 3922 5229 4720 -512 160 120 O ATOM 1432 CB MET A 198 -3.627 -9.507 19.353 1.00 36.72 C ANISOU 1432 CB MET A 198 3906 5261 4785 -410 226 35 C ATOM 1433 CG MET A 198 -2.732 -10.525 20.056 1.00 40.82 C ANISOU 1433 CG MET A 198 4451 5726 5333 -424 144 45 C ATOM 1434 SD MET A 198 -1.254 -9.645 20.704 1.00 47.04 S ANISOU 1434 SD MET A 198 5234 6484 6154 -398 115 5 S ATOM 1435 CE MET A 198 -1.613 -9.404 22.422 1.00 48.50 C ANISOU 1435 CE MET A 198 5490 6685 6254 -441 88 49 C ATOM 1436 N GLU A 199 -6.474 -10.778 20.063 1.00 38.54 N ANISOU 1436 N GLU A 199 4140 5620 4884 -515 265 90 N ATOM 1437 CA GLU A 199 -7.282 -11.730 20.866 1.00 40.34 C ANISOU 1437 CA GLU A 199 4399 5901 5028 -620 256 127 C ATOM 1438 C GLU A 199 -7.960 -12.701 19.869 1.00 39.50 C ANISOU 1438 C GLU A 199 4281 5790 4938 -644 251 151 C ATOM 1439 O GLU A 199 -7.862 -13.915 19.964 1.00 39.76 O ANISOU 1439 O GLU A 199 4376 5772 4960 -710 183 203 O ATOM 1440 CB GLU A 199 -8.338 -11.012 21.699 1.00 40.80 C ANISOU 1440 CB GLU A 199 4411 6090 5000 -660 328 77 C ATOM 1441 CG GLU A 199 -9.144 -12.047 22.503 1.00 43.38 C ANISOU 1441 CG GLU A 199 4774 6498 5210 -819 330 112 C ATOM 1442 CD GLU A 199 -10.226 -11.454 23.374 1.00 44.62 C ANISOU 1442 CD GLU A 199 4860 6829 5264 -888 420 28 C ATOM 1443 OE1 GLU A 199 -10.280 -10.232 23.576 1.00 48.32 O ANISOU 1443 OE1 GLU A 199 5261 7340 5759 -799 464 -63 O ATOM 1444 OE2 GLU A 199 -11.019 -12.235 23.923 1.00 45.00 O ANISOU 1444 OE2 GLU A 199 4922 6979 5197 -1048 442 42 O ATOM 1445 N ASN A 200 -8.527 -12.128 18.823 1.00 37.68 N ANISOU 1445 N ASN A 200 3984 5589 4744 -582 299 114 N ATOM 1446 CA ASN A 200 -9.105 -12.960 17.764 1.00 38.92 C ANISOU 1446 CA ASN A 200 4129 5738 4920 -598 294 133 C ATOM 1447 C ASN A 200 -8.143 -13.972 17.103 1.00 37.05 C ANISOU 1447 C ASN A 200 3938 5394 4746 -589 229 156 C ATOM 1448 O ASN A 200 -8.478 -15.139 16.905 1.00 37.18 O ANISOU 1448 O ASN A 200 3988 5385 4755 -643 186 188 O ATOM 1449 CB ASN A 200 -9.789 -12.088 16.693 1.00 37.43 C ANISOU 1449 CB ASN A 200 3877 5582 4763 -531 333 91 C ATOM 1450 CG ASN A 200 -10.401 -12.937 15.590 1.00 40.87 C ANISOU 1450 CG ASN A 200 4303 6014 5210 -555 325 110 C ATOM 1451 OD1 ASN A 200 -11.350 -13.689 15.870 1.00 37.45 O ANISOU 1451 OD1 ASN A 200 3857 5643 4731 -628 333 124 O ATOM 1452 ND2 ASN A 200 -9.818 -12.896 14.390 1.00 39.14 N ANISOU 1452 ND2 ASN A 200 4098 5733 5042 -518 312 108 N ATOM 1453 N ALA A 201 -6.905 -13.567 16.817 1.00 35.78 N ANISOU 1453 N ALA A 201 3775 5173 4648 -525 212 124 N ATOM 1454 CA ALA A 201 -6.021 -14.401 16.111 1.00 34.41 C ANISOU 1454 CA ALA A 201 3605 4924 4544 -502 161 97 C ATOM 1455 C ALA A 201 -5.655 -15.598 16.989 1.00 35.21 C ANISOU 1455 C ALA A 201 3775 4947 4658 -535 48 128 C ATOM 1456 O ALA A 201 -5.511 -16.699 16.481 1.00 37.45 O ANISOU 1456 O ALA A 201 4077 5162 4989 -534 -23 115 O ATOM 1457 CB ALA A 201 -4.705 -13.577 15.744 1.00 34.49 C ANISOU 1457 CB ALA A 201 3576 4920 4609 -447 179 30 C ATOM 1458 N TYR A 202 -5.473 -15.379 18.297 1.00 36.83 N ANISOU 1458 N TYR A 202 4028 5147 4818 -569 13 164 N ATOM 1459 CA TYR A 202 -5.203 -16.478 19.198 1.00 39.17 C ANISOU 1459 CA TYR A 202 4425 5352 5105 -628 -125 214 C ATOM 1460 C TYR A 202 -6.446 -17.375 19.222 1.00 41.74 C ANISOU 1460 C TYR A 202 4810 5702 5350 -742 -138 282 C ATOM 1461 O TYR A 202 -6.343 -18.598 19.105 1.00 43.65 O ANISOU 1461 O TYR A 202 5127 5838 5619 -773 -263 309 O ATOM 1462 CB TYR A 202 -4.892 -15.949 20.635 1.00 39.67 C ANISOU 1462 CB TYR A 202 4543 5427 5102 -674 -151 249 C ATOM 1463 CG TYR A 202 -3.418 -15.473 20.877 1.00 37.82 C ANISOU 1463 CG TYR A 202 4285 5127 4959 -580 -206 193 C ATOM 1464 CD1 TYR A 202 -2.363 -16.314 20.662 1.00 42.27 C ANISOU 1464 CD1 TYR A 202 4857 5566 5636 -516 -346 148 C ATOM 1465 CD2 TYR A 202 -3.170 -14.222 21.409 1.00 41.77 C ANISOU 1465 CD2 TYR A 202 4752 5692 5425 -563 -129 176 C ATOM 1466 CE1 TYR A 202 -1.051 -15.889 20.919 1.00 42.48 C ANISOU 1466 CE1 TYR A 202 4840 5553 5748 -437 -397 78 C ATOM 1467 CE2 TYR A 202 -1.852 -13.752 21.674 1.00 39.26 C ANISOU 1467 CE2 TYR A 202 4409 5327 5180 -496 -175 125 C ATOM 1468 CZ TYR A 202 -0.821 -14.613 21.436 1.00 42.43 C ANISOU 1468 CZ TYR A 202 4805 5623 5695 -438 -306 76 C ATOM 1469 OH TYR A 202 0.473 -14.200 21.705 1.00 47.11 O ANISOU 1469 OH TYR A 202 5352 6183 6366 -374 -357 7 O ATOM 1470 N ARG A 203 -7.637 -16.791 19.415 1.00 42.04 N ANISOU 1470 N ARG A 203 4810 5876 5287 -809 -22 299 N ATOM 1471 CA ARG A 203 -8.840 -17.656 19.430 1.00 44.23 C ANISOU 1471 CA ARG A 203 5127 6201 5478 -940 -25 351 C ATOM 1472 C ARG A 203 -8.992 -18.518 18.191 1.00 43.93 C ANISOU 1472 C ARG A 203 5083 6098 5511 -907 -61 344 C ATOM 1473 O ARG A 203 -9.469 -19.651 18.296 1.00 44.95 O ANISOU 1473 O ARG A 203 5299 6184 5597 -1015 -143 402 O ATOM 1474 CB ARG A 203 -10.115 -16.893 19.757 1.00 43.90 C ANISOU 1474 CB ARG A 203 5006 6341 5334 -1007 110 328 C ATOM 1475 CG ARG A 203 -9.910 -16.253 21.110 1.00 46.36 C ANISOU 1475 CG ARG A 203 5342 6711 5564 -1063 129 325 C ATOM 1476 CD ARG A 203 -11.182 -16.134 21.756 1.00 44.26 C ANISOU 1476 CD ARG A 203 5034 6619 5162 -1203 218 304 C ATOM 1477 NE ARG A 203 -10.985 -16.232 23.187 1.00 57.50 N ANISOU 1477 NE ARG A 203 6803 8330 6713 -1348 189 340 N ATOM 1478 CZ ARG A 203 -11.036 -15.161 23.928 1.00 55.67 C ANISOU 1478 CZ ARG A 203 6509 8206 6438 -1334 272 267 C ATOM 1479 NH1 ARG A 203 -11.228 -14.033 23.284 1.00 62.09 N ANISOU 1479 NH1 ARG A 203 7184 9065 7343 -1169 359 169 N ATOM 1480 NH2 ARG A 203 -10.896 -15.189 25.229 1.00 54.14 N ANISOU 1480 NH2 ARG A 203 6396 8061 6114 -1480 257 290 N ATOM 1481 N GLN A 204 -8.576 -17.991 17.030 1.00 43.75 N ANISOU 1481 N GLN A 204 4972 6068 5582 -778 -7 275 N ATOM 1482 CA GLN A 204 -8.719 -18.686 15.776 1.00 42.56 C ANISOU 1482 CA GLN A 204 4804 5877 5489 -749 -22 251 C ATOM 1483 C GLN A 204 -7.799 -19.889 15.794 1.00 44.85 C ANISOU 1483 C GLN A 204 5171 6011 5857 -729 -177 240 C ATOM 1484 O GLN A 204 -8.107 -20.932 15.164 1.00 44.64 O ANISOU 1484 O GLN A 204 5182 5924 5855 -752 -243 242 O ATOM 1485 CB GLN A 204 -8.501 -17.787 14.539 1.00 42.81 C ANISOU 1485 CB GLN A 204 4739 5952 5574 -652 72 180 C ATOM 1486 CG GLN A 204 -9.542 -16.682 14.313 1.00 42.39 C ANISOU 1486 CG GLN A 204 4622 6018 5466 -656 178 183 C ATOM 1487 CD GLN A 204 -10.959 -17.183 14.145 1.00 47.52 C ANISOU 1487 CD GLN A 204 5262 6737 6058 -735 196 215 C ATOM 1488 OE1 GLN A 204 -11.200 -18.213 13.486 1.00 45.87 O ANISOU 1488 OE1 GLN A 204 5081 6486 5861 -769 154 229 O ATOM 1489 NE2 GLN A 204 -11.925 -16.464 14.753 1.00 45.12 N ANISOU 1489 NE2 GLN A 204 4905 6547 5693 -765 255 210 N ATOM 1490 N MET A 205 -6.701 -19.762 16.532 1.00 43.76 N ANISOU 1490 N MET A 205 5059 5802 5766 -682 -254 221 N ATOM 1491 CA MET A 205 -5.737 -20.839 16.751 1.00 47.35 C ANISOU 1491 CA MET A 205 5586 6090 6315 -643 -443 194 C ATOM 1492 C MET A 205 -6.025 -21.795 17.970 1.00 49.37 C ANISOU 1492 C MET A 205 6016 6241 6500 -772 -616 308 C ATOM 1493 O MET A 205 -5.194 -22.619 18.368 1.00 50.19 O ANISOU 1493 O MET A 205 6209 6177 6685 -740 -819 297 O ATOM 1494 CB MET A 205 -4.340 -20.175 16.814 1.00 46.66 C ANISOU 1494 CB MET A 205 5419 5982 6327 -520 -449 93 C ATOM 1495 CG MET A 205 -3.931 -19.587 15.444 1.00 43.56 C ANISOU 1495 CG MET A 205 4884 5669 5998 -432 -320 -28 C ATOM 1496 SD MET A 205 -2.209 -19.027 15.436 1.00 46.96 S ANISOU 1496 SD MET A 205 5209 6090 6545 -318 -337 -174 S ATOM 1497 CE MET A 205 -2.330 -17.702 16.611 1.00 42.10 C ANISOU 1497 CE MET A 205 4623 5543 5830 -364 -262 -78 C ATOM 1498 N GLN A 206 -7.208 -21.631 18.566 1.00 50.37 N ANISOU 1498 N GLN A 206 6191 6475 6472 -929 -539 407 N ATOM 1499 CA GLN A 206 -7.628 -22.262 19.852 1.00 52.68 C ANISOU 1499 CA GLN A 206 6652 6729 6633 -1118 -657 527 C ATOM 1500 C GLN A 206 -6.694 -22.052 21.012 1.00 52.83 C ANISOU 1500 C GLN A 206 6753 6672 6649 -1120 -769 552 C ATOM 1501 O GLN A 206 -6.580 -22.886 21.921 1.00 54.02 O ANISOU 1501 O GLN A 206 7086 6702 6739 -1249 -960 643 O ATOM 1502 CB GLN A 206 -8.053 -23.763 19.708 1.00 54.78 C ANISOU 1502 CB GLN A 206 7071 6861 6882 -1230 -833 597 C ATOM 1503 CG GLN A 206 -7.582 -24.545 18.466 1.00 60.25 C ANISOU 1503 CG GLN A 206 7732 7418 7740 -1085 -925 511 C ATOM 1504 CD GLN A 206 -8.437 -24.314 17.243 1.00 64.80 C ANISOU 1504 CD GLN A 206 8183 8125 8315 -1060 -749 467 C ATOM 1505 OE1 GLN A 206 -9.318 -23.455 17.257 1.00 69.39 O ANISOU 1505 OE1 GLN A 206 8678 8892 8797 -1118 -561 485 O ATOM 1506 NE2 GLN A 206 -8.191 -25.081 16.171 1.00 66.80 N ANISOU 1506 NE2 GLN A 206 8421 8278 8683 -970 -821 395 N ATOM 1507 N MET A 207 -6.038 -20.899 21.019 1.00 50.69 N ANISOU 1507 N MET A 207 6360 6467 6431 -995 -661 478 N ATOM 1508 CA MET A 207 -5.031 -20.664 22.013 1.00 51.37 C ANISOU 1508 CA MET A 207 6506 6476 6535 -975 -771 485 C ATOM 1509 C MET A 207 -5.582 -19.892 23.210 1.00 52.14 C ANISOU 1509 C MET A 207 6642 6709 6460 -1119 -676 550 C ATOM 1510 O MET A 207 -5.426 -18.660 23.316 1.00 50.44 O ANISOU 1510 O MET A 207 6316 6608 6243 -1050 -529 494 O ATOM 1511 CB MET A 207 -3.834 -19.982 21.381 1.00 50.01 C ANISOU 1511 CB MET A 207 6192 6284 6525 -770 -739 358 C ATOM 1512 CG MET A 207 -3.243 -20.788 20.241 1.00 50.12 C ANISOU 1512 CG MET A 207 6153 6188 6703 -641 -829 259 C ATOM 1513 SD MET A 207 -1.609 -20.133 19.768 1.00 49.00 S ANISOU 1513 SD MET A 207 5850 6031 6737 -443 -825 86 S ATOM 1514 CE MET A 207 -1.207 -21.527 18.657 1.00 48.07 C ANISOU 1514 CE MET A 207 5707 5775 6783 -340 -977 -35 C ATOM 1515 N ASN A 208 -6.246 -20.633 24.103 1.00 53.92 N ANISOU 1515 N ASN A 208 7031 6926 6531 -1336 -765 661 N ATOM 1516 CA ASN A 208 -7.028 -20.018 25.175 1.00 55.52 C ANISOU 1516 CA ASN A 208 7257 7305 6534 -1520 -646 701 C ATOM 1517 C ASN A 208 -6.238 -19.245 26.247 1.00 55.70 C ANISOU 1517 C ASN A 208 7308 7330 6525 -1513 -666 698 C ATOM 1518 O ASN A 208 -6.670 -18.142 26.656 1.00 56.10 O ANISOU 1518 O ASN A 208 7261 7561 6492 -1533 -484 646 O ATOM 1519 CB ASN A 208 -7.870 -21.095 25.849 1.00 58.32 C ANISOU 1519 CB ASN A 208 7795 7657 6706 -1798 -745 820 C ATOM 1520 CG ASN A 208 -7.082 -22.359 26.093 1.00 62.08 C ANISOU 1520 CG ASN A 208 8486 7865 7235 -1832 -1054 912 C ATOM 1521 OD1 ASN A 208 -6.670 -22.648 27.222 1.00 70.86 O ANISOU 1521 OD1 ASN A 208 9779 8892 8252 -1971 -1219 998 O ATOM 1522 ND2 ASN A 208 -6.856 -23.124 25.024 1.00 66.60 N ANISOU 1522 ND2 ASN A 208 9045 8293 7966 -1700 -1153 884 N ATOM 1523 N ALA A 209 -5.094 -19.774 26.714 1.00 55.87 N ANISOU 1523 N ALA A 209 7456 7153 6620 -1478 -895 737 N ATOM 1524 CA ALA A 209 -4.352 -19.063 27.774 1.00 55.88 C ANISOU 1524 CA ALA A 209 7494 7156 6583 -1485 -926 740 C ATOM 1525 C ALA A 209 -3.946 -17.712 27.200 1.00 53.40 C ANISOU 1525 C ALA A 209 6968 6942 6380 -1280 -737 615 C ATOM 1526 O ALA A 209 -4.100 -16.663 27.836 1.00 51.78 O ANISOU 1526 O ALA A 209 6715 6870 6089 -1310 -606 587 O ATOM 1527 CB ALA A 209 -3.116 -19.856 28.270 1.00 56.88 C ANISOU 1527 CB ALA A 209 7776 7032 6803 -1449 -1233 786 C ATOM 1528 N GLN A 210 -3.446 -17.753 25.968 1.00 52.45 N ANISOU 1528 N GLN A 210 6729 6758 6443 -1087 -728 537 N ATOM 1529 CA GLN A 210 -2.987 -16.553 25.298 1.00 50.42 C ANISOU 1529 CA GLN A 210 6296 6577 6285 -918 -575 429 C ATOM 1530 C GLN A 210 -4.105 -15.537 25.035 1.00 49.11 C ANISOU 1530 C GLN A 210 6024 6604 6032 -941 -343 397 C ATOM 1531 O GLN A 210 -3.952 -14.335 25.299 1.00 49.85 O ANISOU 1531 O GLN A 210 6048 6779 6113 -893 -238 347 O ATOM 1532 CB GLN A 210 -2.338 -16.935 23.986 1.00 49.78 C ANISOU 1532 CB GLN A 210 6119 6410 6383 -756 -608 348 C ATOM 1533 CG GLN A 210 -0.923 -17.473 24.187 1.00 52.75 C ANISOU 1533 CG GLN A 210 6522 6620 6899 -661 -816 304 C ATOM 1534 CD GLN A 210 -0.848 -18.989 24.240 1.00 54.79 C ANISOU 1534 CD GLN A 210 6911 6702 7205 -691 -1052 345 C ATOM 1535 OE1 GLN A 210 -1.867 -19.696 24.206 1.00 59.88 O ANISOU 1535 OE1 GLN A 210 7650 7347 7755 -813 -1063 430 O ATOM 1536 NE2 GLN A 210 0.368 -19.499 24.354 1.00 57.12 N ANISOU 1536 NE2 GLN A 210 7213 6839 7650 -581 -1261 278 N ATOM 1537 N ALA A 211 -5.199 -16.019 24.489 1.00 48.16 N ANISOU 1537 N ALA A 211 5890 6544 5864 -1004 -283 415 N ATOM 1538 CA ALA A 211 -6.362 -15.190 24.237 1.00 47.03 C ANISOU 1538 CA ALA A 211 5640 6577 5651 -1022 -96 370 C ATOM 1539 C ALA A 211 -6.924 -14.522 25.539 1.00 48.72 C ANISOU 1539 C ALA A 211 5871 6932 5708 -1149 -20 362 C ATOM 1540 O ALA A 211 -7.267 -13.324 25.576 1.00 47.27 O ANISOU 1540 O ALA A 211 5580 6862 5518 -1087 108 277 O ATOM 1541 CB ALA A 211 -7.374 -16.028 23.557 1.00 49.08 C ANISOU 1541 CB ALA A 211 5897 6867 5883 -1088 -79 395 C ATOM 1542 N GLU A 212 -6.970 -15.284 26.637 1.00 51.07 N ANISOU 1542 N GLU A 212 6314 7217 5874 -1335 -116 442 N ATOM 1543 CA GLU A 212 -7.475 -14.719 27.880 1.00 51.64 C ANISOU 1543 CA GLU A 212 6404 7442 5775 -1484 -37 421 C ATOM 1544 C GLU A 212 -6.555 -13.622 28.401 1.00 51.18 C ANISOU 1544 C GLU A 212 6320 7364 5761 -1377 -27 372 C ATOM 1545 O GLU A 212 -7.038 -12.653 28.984 1.00 52.10 O ANISOU 1545 O GLU A 212 6365 7632 5798 -1402 98 288 O ATOM 1546 CB GLU A 212 -7.687 -15.817 28.885 1.00 53.74 C ANISOU 1546 CB GLU A 212 6858 7693 5867 -1744 -155 533 C ATOM 1547 CG GLU A 212 -8.643 -16.850 28.311 1.00 56.86 C ANISOU 1547 CG GLU A 212 7277 8112 6216 -1860 -160 578 C ATOM 1548 CD GLU A 212 -10.102 -16.430 28.412 1.00 64.07 C ANISOU 1548 CD GLU A 212 8060 9290 6994 -1982 43 488 C ATOM 1549 OE1 GLU A 212 -10.516 -15.852 29.475 1.00 62.31 O ANISOU 1549 OE1 GLU A 212 7820 9245 6612 -2124 141 430 O ATOM 1550 OE2 GLU A 212 -10.833 -16.727 27.423 1.00 64.21 O ANISOU 1550 OE2 GLU A 212 7988 9343 7068 -1939 98 463 O ATOM 1551 N LYS A 213 -5.241 -13.752 28.152 1.00 50.62 N ANISOU 1551 N LYS A 213 6292 7115 5827 -1251 -159 403 N ATOM 1552 CA LYS A 213 -4.266 -12.743 28.521 1.00 50.68 C ANISOU 1552 CA LYS A 213 6270 7094 5893 -1145 -159 357 C ATOM 1553 C LYS A 213 -4.583 -11.425 27.819 1.00 48.18 C ANISOU 1553 C LYS A 213 5794 6871 5643 -1003 4 249 C ATOM 1554 O LYS A 213 -4.612 -10.365 28.455 1.00 46.88 O ANISOU 1554 O LYS A 213 5596 6784 5432 -995 76 187 O ATOM 1555 CB LYS A 213 -2.827 -13.212 28.160 1.00 51.55 C ANISOU 1555 CB LYS A 213 6415 7010 6161 -1026 -327 381 C ATOM 1556 CG LYS A 213 -1.704 -12.868 29.189 1.00 58.31 C ANISOU 1556 CG LYS A 213 7343 7796 7015 -1027 -437 393 C ATOM 1557 CD LYS A 213 -0.809 -11.712 28.751 1.00 62.54 C ANISOU 1557 CD LYS A 213 7760 8329 7674 -863 -375 305 C ATOM 1558 CE LYS A 213 0.519 -11.675 29.558 1.00 67.78 C ANISOU 1558 CE LYS A 213 8485 8886 8381 -844 -530 315 C ATOM 1559 NZ LYS A 213 0.425 -11.528 31.077 1.00 71.17 N ANISOU 1559 NZ LYS A 213 9048 9345 8649 -996 -580 372 N ATOM 1560 N VAL A 214 -4.780 -11.483 26.498 1.00 45.75 N ANISOU 1560 N VAL A 214 5401 6539 5444 -894 43 224 N ATOM 1561 CA VAL A 214 -5.103 -10.278 25.753 1.00 44.55 C ANISOU 1561 CA VAL A 214 5129 6447 5353 -773 158 137 C ATOM 1562 C VAL A 214 -6.398 -9.655 26.272 1.00 44.17 C ANISOU 1562 C VAL A 214 5021 6562 5200 -829 272 65 C ATOM 1563 O VAL A 214 -6.497 -8.421 26.383 1.00 43.40 O ANISOU 1563 O VAL A 214 4861 6509 5121 -750 330 -21 O ATOM 1564 CB VAL A 214 -5.241 -10.565 24.203 1.00 42.89 C ANISOU 1564 CB VAL A 214 4856 6190 5249 -683 172 133 C ATOM 1565 CG1 VAL A 214 -5.498 -9.232 23.462 1.00 43.15 C ANISOU 1565 CG1 VAL A 214 4802 6259 5336 -575 253 58 C ATOM 1566 CG2 VAL A 214 -3.948 -11.204 23.711 1.00 45.47 C ANISOU 1566 CG2 VAL A 214 5213 6383 5681 -630 69 161 C ATOM 1567 N ALA A 215 -7.410 -10.481 26.548 1.00 43.55 N ANISOU 1567 N ALA A 215 4953 6578 5017 -965 298 83 N ATOM 1568 CA ALA A 215 -8.664 -9.968 27.109 1.00 45.92 C ANISOU 1568 CA ALA A 215 5167 7071 5211 -1036 414 -21 C ATOM 1569 C ALA A 215 -8.395 -9.198 28.421 1.00 48.87 C ANISOU 1569 C ALA A 215 5561 7515 5493 -1089 441 -80 C ATOM 1570 O ALA A 215 -9.030 -8.144 28.725 1.00 48.57 O ANISOU 1570 O ALA A 215 5415 7601 5439 -1042 533 -224 O ATOM 1571 CB ALA A 215 -9.656 -11.085 27.342 1.00 46.80 C ANISOU 1571 CB ALA A 215 5298 7287 5196 -1225 436 12 C ATOM 1572 N LYS A 216 -7.415 -9.689 29.192 1.00 50.03 N ANISOU 1572 N LYS A 216 5848 7572 5590 -1173 343 20 N ATOM 1573 CA LYS A 216 -7.006 -8.966 30.423 1.00 51.26 C ANISOU 1573 CA LYS A 216 6042 7776 5658 -1225 353 -24 C ATOM 1574 C LYS A 216 -6.367 -7.600 30.084 1.00 49.44 C ANISOU 1574 C LYS A 216 5743 7484 5560 -1025 368 -102 C ATOM 1575 O LYS A 216 -6.724 -6.548 30.704 1.00 48.82 O ANISOU 1575 O LYS A 216 5601 7508 5438 -1006 443 -226 O ATOM 1576 CB LYS A 216 -6.079 -9.858 31.278 1.00 52.06 C ANISOU 1576 CB LYS A 216 6325 7772 5683 -1363 210 112 C ATOM 1577 CG LYS A 216 -5.190 -9.098 32.343 1.00 59.83 C ANISOU 1577 CG LYS A 216 7370 8735 6627 -1370 173 96 C ATOM 1578 CD LYS A 216 -4.496 -9.986 33.452 1.00 66.55 C ANISOU 1578 CD LYS A 216 8420 9509 7357 -1555 15 224 C ATOM 1579 CE LYS A 216 -3.387 -10.962 32.921 1.00 66.56 C ANISOU 1579 CE LYS A 216 8518 9276 7497 -1482 -188 348 C ATOM 1580 NZ LYS A 216 -3.947 -12.342 32.588 1.00 68.95 N ANISOU 1580 NZ LYS A 216 8904 9538 7757 -1601 -266 442 N ATOM 1581 N ILE A 217 -5.415 -7.626 29.144 1.00 46.01 N ANISOU 1581 N ILE A 217 5322 6886 5274 -893 292 -39 N ATOM 1582 CA ILE A 217 -4.748 -6.435 28.677 1.00 46.13 C ANISOU 1582 CA ILE A 217 5293 6830 5403 -738 293 -91 C ATOM 1583 C ILE A 217 -5.758 -5.390 28.244 1.00 47.18 C ANISOU 1583 C ILE A 217 5316 7045 5565 -647 379 -216 C ATOM 1584 O ILE A 217 -5.677 -4.224 28.627 1.00 48.94 O ANISOU 1584 O ILE A 217 5516 7279 5800 -583 394 -305 O ATOM 1585 CB ILE A 217 -3.733 -6.791 27.528 1.00 45.28 C ANISOU 1585 CB ILE A 217 5197 6575 5434 -646 220 -21 C ATOM 1586 CG1 ILE A 217 -2.755 -7.880 28.033 1.00 44.99 C ANISOU 1586 CG1 ILE A 217 5255 6449 5390 -716 102 71 C ATOM 1587 CG2 ILE A 217 -3.083 -5.489 26.840 1.00 42.97 C ANISOU 1587 CG2 ILE A 217 4865 6220 5243 -519 227 -71 C ATOM 1588 CD1 ILE A 217 -1.750 -8.315 26.987 1.00 45.94 C ANISOU 1588 CD1 ILE A 217 5356 6451 5649 -628 32 96 C ATOM 1589 N ILE A 218 -6.733 -5.799 27.433 1.00 47.81 N ANISOU 1589 N ILE A 218 5328 7172 5666 -634 418 -232 N ATOM 1590 CA ILE A 218 -7.766 -4.870 26.966 1.00 48.47 C ANISOU 1590 CA ILE A 218 5300 7321 5796 -533 467 -363 C ATOM 1591 C ILE A 218 -8.575 -4.290 28.122 1.00 49.93 C ANISOU 1591 C ILE A 218 5416 7670 5887 -577 538 -514 C ATOM 1592 O ILE A 218 -8.797 -3.075 28.184 1.00 50.81 O ANISOU 1592 O ILE A 218 5468 7782 6054 -461 536 -644 O ATOM 1593 CB ILE A 218 -8.692 -5.483 25.838 1.00 47.20 C ANISOU 1593 CB ILE A 218 5074 7182 5678 -514 483 -354 C ATOM 1594 CG1 ILE A 218 -9.416 -6.719 26.292 1.00 52.62 C ANISOU 1594 CG1 ILE A 218 5754 7989 6250 -673 531 -325 C ATOM 1595 CG2 ILE A 218 -7.886 -5.911 24.578 1.00 47.16 C ANISOU 1595 CG2 ILE A 218 5125 7024 5768 -462 420 -235 C ATOM 1596 CD1 ILE A 218 -10.640 -7.034 25.446 1.00 53.42 C ANISOU 1596 CD1 ILE A 218 5753 8166 6376 -657 568 -374 C ATOM 1597 N ALA A 219 -9.017 -5.113 29.057 1.00 51.82 N ANISOU 1597 N ALA A 219 5664 8048 5977 -753 594 -513 N ATOM 1598 CA ALA A 219 -9.936 -4.547 30.058 1.00 54.26 C ANISOU 1598 CA ALA A 219 5872 8557 6185 -810 687 -698 C ATOM 1599 C ALA A 219 -9.196 -3.443 30.859 1.00 54.32 C ANISOU 1599 C ALA A 219 5916 8527 6197 -752 666 -764 C ATOM 1600 O ALA A 219 -9.798 -2.409 31.212 1.00 53.42 O ANISOU 1600 O ALA A 219 5694 8504 6100 -671 707 -961 O ATOM 1601 CB ALA A 219 -10.542 -5.634 30.969 1.00 56.22 C ANISOU 1601 CB ALA A 219 6139 8988 6233 -1066 759 -684 C ATOM 1602 N ALA A 220 -7.869 -3.623 31.035 1.00 53.88 N ANISOU 1602 N ALA A 220 6003 8321 6148 -770 586 -611 N ATOM 1603 CA ALA A 220 -7.057 -2.789 31.926 1.00 55.64 C ANISOU 1603 CA ALA A 220 6284 8509 6347 -759 560 -644 C ATOM 1604 C ALA A 220 -6.347 -1.572 31.263 1.00 55.38 C ANISOU 1604 C ALA A 220 6256 8313 6472 -565 490 -664 C ATOM 1605 O ALA A 220 -5.752 -0.717 31.928 1.00 55.81 O ANISOU 1605 O ALA A 220 6350 8336 6521 -540 465 -711 O ATOM 1606 CB ALA A 220 -6.023 -3.684 32.639 1.00 55.88 C ANISOU 1606 CB ALA A 220 6467 8479 6285 -908 495 -480 C ATOM 1607 N ASN A 221 -6.385 -1.446 29.960 1.00 54.70 N ANISOU 1607 N ASN A 221 6146 8121 6516 -447 449 -627 N ATOM 1608 CA ASN A 221 -5.634 -0.309 29.453 1.00 54.73 C ANISOU 1608 CA ASN A 221 6190 7974 6631 -320 372 -630 C ATOM 1609 C ASN A 221 -6.391 1.016 29.490 1.00 55.11 C ANISOU 1609 C ASN A 221 6168 8033 6737 -192 356 -812 C ATOM 1610 O ASN A 221 -7.130 1.352 28.556 1.00 55.64 O ANISOU 1610 O ASN A 221 6178 8067 6895 -88 322 -866 O ATOM 1611 CB ASN A 221 -4.920 -0.571 28.119 1.00 56.40 C ANISOU 1611 CB ASN A 221 6449 8040 6941 -277 311 -496 C ATOM 1612 CG ASN A 221 -5.849 -0.704 27.010 1.00 54.56 C ANISOU 1612 CG ASN A 221 6153 7809 6770 -215 314 -515 C ATOM 1613 OD1 ASN A 221 -6.879 -1.335 27.182 1.00 61.67 O ANISOU 1613 OD1 ASN A 221 6977 8831 7623 -252 375 -564 O ATOM 1614 ND2 ASN A 221 -5.505 -0.130 25.809 1.00 53.00 N ANISOU 1614 ND2 ASN A 221 5992 7479 6666 -141 243 -474 N ATOM 1615 N SER A 222 -6.149 1.788 30.551 1.00 55.26 N ANISOU 1615 N SER A 222 6202 8082 6713 -193 358 -910 N ATOM 1616 CA SER A 222 -6.829 3.070 30.734 1.00 56.17 C ANISOU 1616 CA SER A 222 6251 8201 6891 -60 323 -1115 C ATOM 1617 C SER A 222 -6.408 4.031 29.668 1.00 55.52 C ANISOU 1617 C SER A 222 6239 7907 6948 71 188 -1077 C ATOM 1618 O SER A 222 -5.289 3.936 29.139 1.00 53.74 O ANISOU 1618 O SER A 222 6125 7553 6740 31 140 -907 O ATOM 1619 CB SER A 222 -6.473 3.734 32.084 1.00 57.35 C ANISOU 1619 CB SER A 222 6422 8406 6964 -94 342 -1223 C ATOM 1620 OG SER A 222 -6.477 2.774 33.122 1.00 63.73 O ANISOU 1620 OG SER A 222 7228 9381 7607 -274 448 -1195 O ATOM 1621 N SER A 223 -7.274 5.007 29.386 1.00 55.88 N ANISOU 1621 N SER A 223 6224 7917 7091 219 111 -1248 N ATOM 1622 CA SER A 223 -6.883 6.134 28.550 1.00 57.39 C ANISOU 1622 CA SER A 223 6520 7885 7399 329 -56 -1224 C ATOM 1623 C SER A 223 -6.005 7.114 29.318 1.00 58.05 C ANISOU 1623 C SER A 223 6700 7883 7472 332 -114 -1252 C ATOM 1624 O SER A 223 -5.520 8.092 28.729 1.00 58.33 O ANISOU 1624 O SER A 223 6856 7723 7584 387 -263 -1216 O ATOM 1625 CB SER A 223 -8.091 6.872 27.990 1.00 58.98 C ANISOU 1625 CB SER A 223 6644 8040 7726 498 -169 -1400 C ATOM 1626 OG SER A 223 -8.970 7.228 29.030 1.00 60.10 O ANISOU 1626 OG SER A 223 6640 8332 7864 569 -123 -1660 O ATOM 1627 N ASN A 224 -5.826 6.869 30.622 1.00 59.73 N ANISOU 1627 N ASN A 224 6875 8240 7581 256 -7 -1316 N ATOM 1628 CA ASN A 224 -5.004 7.722 31.456 1.00 61.98 C ANISOU 1628 CA ASN A 224 7245 8462 7842 247 -51 -1348 C ATOM 1629 C ASN A 224 -3.554 7.378 31.193 1.00 61.31 C ANISOU 1629 C ASN A 224 7292 8282 7721 131 -62 -1116 C ATOM 1630 O ASN A 224 -3.082 6.373 31.703 1.00 62.23 O ANISOU 1630 O ASN A 224 7402 8500 7743 8 34 -1020 O ATOM 1631 CB ASN A 224 -5.281 7.515 32.976 1.00 64.14 C ANISOU 1631 CB ASN A 224 7440 8938 7991 177 71 -1492 C ATOM 1632 CG ASN A 224 -6.748 7.641 33.358 1.00 68.25 C ANISOU 1632 CG ASN A 224 7783 9630 8520 255 129 -1755 C ATOM 1633 OD1 ASN A 224 -7.388 6.663 33.784 1.00 72.24 O ANISOU 1633 OD1 ASN A 224 8184 10346 8918 149 270 -1789 O ATOM 1634 ND2 ASN A 224 -7.283 8.853 33.251 1.00 74.04 N ANISOU 1634 ND2 ASN A 224 8480 10277 9376 433 11 -1960 N ATOM 1635 N THR A 225 -2.850 8.193 30.416 1.00 61.16 N ANISOU 1635 N THR A 225 7390 8072 7774 157 -190 -1037 N ATOM 1636 CA THR A 225 -1.406 8.000 30.193 1.00 60.34 C ANISOU 1636 CA THR A 225 7389 7899 7639 40 -198 -857 C ATOM 1637 C THR A 225 -0.526 8.547 31.368 1.00 60.02 C ANISOU 1637 C THR A 225 7406 7854 7543 -9 -207 -884 C ATOM 1638 O THR A 225 -0.736 9.683 31.850 1.00 62.05 O ANISOU 1638 O THR A 225 7702 8047 7828 65 -286 -1013 O ATOM 1639 CB THR A 225 -0.985 8.562 28.790 1.00 60.74 C ANISOU 1639 CB THR A 225 7544 7776 7759 35 -315 -753 C ATOM 1640 OG1 THR A 225 -1.785 7.939 27.772 1.00 60.72 O ANISOU 1640 OG1 THR A 225 7487 7791 7792 66 -300 -723 O ATOM 1641 CG2 THR A 225 0.521 8.334 28.500 1.00 59.54 C ANISOU 1641 CG2 THR A 225 7463 7591 7569 -106 -305 -597 C ATOM 1642 N LEU A 226 0.430 7.731 31.844 1.00 58.01 N ANISOU 1642 N LEU A 226 7158 7664 7219 -125 -143 -774 N ATOM 1643 CA LEU A 226 1.263 8.086 33.050 1.00 56.98 C ANISOU 1643 CA LEU A 226 7078 7548 7024 -185 -150 -793 C ATOM 1644 C LEU A 226 2.442 9.015 32.732 1.00 56.63 C ANISOU 1644 C LEU A 226 7142 7359 7017 -219 -250 -731 C ATOM 1645 O LEU A 226 2.995 8.930 31.635 1.00 55.44 O ANISOU 1645 O LEU A 226 7019 7138 6909 -259 -281 -624 O ATOM 1646 CB LEU A 226 1.752 6.817 33.789 1.00 55.19 C ANISOU 1646 CB LEU A 226 6823 7437 6709 -295 -74 -710 C ATOM 1647 CG LEU A 226 0.907 6.319 34.996 1.00 55.23 C ANISOU 1647 CG LEU A 226 6779 7603 6602 -332 10 -806 C ATOM 1648 CD1 LEU A 226 -0.625 6.276 34.841 1.00 52.19 C ANISOU 1648 CD1 LEU A 226 6295 7318 6217 -263 76 -942 C ATOM 1649 CD2 LEU A 226 1.453 5.008 35.543 1.00 50.00 C ANISOU 1649 CD2 LEU A 226 6133 7011 5855 -460 36 -685 C ATOM 1650 N GLU A 227 2.790 9.914 33.663 1.00 57.24 N ANISOU 1650 N GLU A 227 7277 7403 7067 -218 -297 -808 N ATOM 1651 CA GLU A 227 3.845 10.899 33.425 1.00 58.46 C ANISOU 1651 CA GLU A 227 7544 7421 7247 -264 -401 -760 C ATOM 1652 C GLU A 227 4.986 10.719 34.412 1.00 58.07 C ANISOU 1652 C GLU A 227 7514 7416 7134 -363 -387 -720 C ATOM 1653 O GLU A 227 4.749 10.470 35.594 1.00 57.42 O ANISOU 1653 O GLU A 227 7406 7428 6982 -365 -340 -789 O ATOM 1654 CB GLU A 227 3.287 12.337 33.466 1.00 61.59 C ANISOU 1654 CB GLU A 227 8022 7686 7694 -166 -521 -889 C ATOM 1655 CG GLU A 227 2.270 12.628 32.308 1.00 65.84 C ANISOU 1655 CG GLU A 227 8565 8134 8317 -66 -591 -917 C ATOM 1656 CD GLU A 227 2.406 14.035 31.669 1.00 72.00 C ANISOU 1656 CD GLU A 227 9504 8691 9162 -42 -786 -926 C ATOM 1657 OE1 GLU A 227 2.116 15.050 32.375 1.00 74.99 O ANISOU 1657 OE1 GLU A 227 9934 8989 9570 46 -884 -1072 O ATOM 1658 OE2 GLU A 227 2.784 14.105 30.456 1.00 70.85 O ANISOU 1658 OE2 GLU A 227 9439 8449 9030 -122 -848 -793 O ATOM 1659 N HIS A 228 6.222 10.816 33.927 1.00 57.04 N ANISOU 1659 N HIS A 228 7423 7230 7018 -458 -427 -615 N ATOM 1660 CA HIS A 228 7.386 10.579 34.760 1.00 57.36 C ANISOU 1660 CA HIS A 228 7467 7312 7017 -548 -431 -577 C ATOM 1661 C HIS A 228 8.489 11.523 34.324 1.00 57.10 C ANISOU 1661 C HIS A 228 7511 7180 7003 -634 -514 -538 C ATOM 1662 O HIS A 228 9.632 11.283 34.592 1.00 56.42 O ANISOU 1662 O HIS A 228 7405 7126 6907 -723 -522 -493 O ATOM 1663 CB HIS A 228 7.811 9.086 34.713 1.00 57.54 C ANISOU 1663 CB HIS A 228 7393 7436 7035 -592 -371 -494 C ATOM 1664 CG HIS A 228 9.296 8.861 34.513 1.00 62.93 C ANISOU 1664 CG HIS A 228 8051 8116 7744 -686 -408 -428 C ATOM 1665 ND1 HIS A 228 9.923 9.012 33.291 1.00 64.79 N ANISOU 1665 ND1 HIS A 228 8263 8324 8029 -744 -413 -387 N ATOM 1666 CD2 HIS A 228 10.274 8.488 35.379 1.00 65.63 C ANISOU 1666 CD2 HIS A 228 8377 8491 8068 -740 -445 -414 C ATOM 1667 CE1 HIS A 228 11.207 8.728 33.406 1.00 61.70 C ANISOU 1667 CE1 HIS A 228 7818 7968 7656 -823 -438 -369 C ATOM 1668 NE2 HIS A 228 11.452 8.407 34.662 1.00 66.73 N ANISOU 1668 NE2 HIS A 228 8460 8631 8265 -811 -470 -382 N ATOM 1669 N HIS A 229 8.120 12.645 33.717 1.00 57.12 N ANISOU 1669 N HIS A 229 7612 7058 7033 -613 -592 -565 N ATOM 1670 CA HIS A 229 9.115 13.685 33.402 1.00 57.53 C ANISOU 1670 CA HIS A 229 7773 7006 7079 -726 -688 -528 C ATOM 1671 C HIS A 229 9.765 14.335 34.608 1.00 56.11 C ANISOU 1671 C HIS A 229 7649 6809 6863 -757 -737 -577 C ATOM 1672 O HIS A 229 10.851 14.869 34.518 1.00 57.00 O ANISOU 1672 O HIS A 229 7815 6883 6958 -882 -790 -535 O ATOM 1673 CB HIS A 229 8.489 14.747 32.493 1.00 60.20 C ANISOU 1673 CB HIS A 229 8242 7182 7449 -705 -801 -536 C ATOM 1674 CG HIS A 229 7.195 15.307 33.009 1.00 63.55 C ANISOU 1674 CG HIS A 229 8698 7537 7909 -532 -857 -667 C ATOM 1675 ND1 HIS A 229 7.135 16.179 34.075 1.00 66.89 N ANISOU 1675 ND1 HIS A 229 9186 7904 8326 -478 -926 -780 N ATOM 1676 CD2 HIS A 229 5.915 15.117 32.608 1.00 67.31 C ANISOU 1676 CD2 HIS A 229 9134 8005 8435 -397 -855 -729 C ATOM 1677 CE1 HIS A 229 5.874 16.500 34.310 1.00 68.86 C ANISOU 1677 CE1 HIS A 229 9421 8121 8622 -313 -960 -923 C ATOM 1678 NE2 HIS A 229 5.116 15.882 33.427 1.00 68.70 N ANISOU 1678 NE2 HIS A 229 9335 8128 8641 -261 -922 -894 N ATOM 1679 N HIS A 230 9.064 14.336 35.732 1.00 54.24 N ANISOU 1679 N HIS A 230 7400 6607 6602 -655 -717 -678 N ATOM 1680 CA HIS A 230 9.545 14.836 36.978 1.00 53.19 C ANISOU 1680 CA HIS A 230 7313 6476 6420 -678 -751 -737 C ATOM 1681 C HIS A 230 10.451 13.823 37.724 1.00 51.08 C ANISOU 1681 C HIS A 230 6967 6335 6108 -758 -695 -678 C ATOM 1682 O HIS A 230 10.918 14.116 38.819 1.00 50.00 O ANISOU 1682 O HIS A 230 6868 6211 5919 -792 -725 -716 O ATOM 1683 CB HIS A 230 8.334 15.267 37.861 1.00 54.54 C ANISOU 1683 CB HIS A 230 7495 6653 6573 -547 -748 -901 C ATOM 1684 CG HIS A 230 7.314 14.179 38.083 1.00 52.26 C ANISOU 1684 CG HIS A 230 7088 6509 6260 -479 -628 -940 C ATOM 1685 ND1 HIS A 230 6.535 13.658 37.072 1.00 47.88 N ANISOU 1685 ND1 HIS A 230 6470 5963 5757 -419 -588 -913 N ATOM 1686 CD2 HIS A 230 6.976 13.494 39.206 1.00 51.41 C ANISOU 1686 CD2 HIS A 230 6924 6546 6065 -491 -543 -996 C ATOM 1687 CE1 HIS A 230 5.739 12.722 37.560 1.00 47.90 C ANISOU 1687 CE1 HIS A 230 6376 6110 5712 -390 -482 -957 C ATOM 1688 NE2 HIS A 230 5.973 12.616 38.859 1.00 49.66 N ANISOU 1688 NE2 HIS A 230 6607 6420 5843 -441 -453 -1008 N ATOM 1689 N HIS A 231 10.695 12.649 37.143 1.00 49.35 N ANISOU 1689 N HIS A 231 6644 6196 5912 -783 -633 -594 N ATOM 1690 CA HIS A 231 11.603 11.666 37.807 1.00 49.66 C ANISOU 1690 CA HIS A 231 6614 6324 5930 -845 -626 -545 C ATOM 1691 C HIS A 231 12.975 11.809 37.176 1.00 51.91 C ANISOU 1691 C HIS A 231 6866 6595 6262 -949 -669 -492 C ATOM 1692 O HIS A 231 13.049 11.832 35.933 1.00 52.97 O ANISOU 1692 O HIS A 231 6969 6715 6440 -978 -646 -459 O ATOM 1693 CB HIS A 231 11.168 10.211 37.554 1.00 45.34 C ANISOU 1693 CB HIS A 231 5968 5864 5397 -809 -561 -499 C ATOM 1694 CG HIS A 231 9.817 9.833 38.118 1.00 41.12 C ANISOU 1694 CG HIS A 231 5440 5384 4802 -740 -499 -548 C ATOM 1695 ND1 HIS A 231 9.421 8.509 38.232 1.00 40.97 N ANISOU 1695 ND1 HIS A 231 5361 5444 4761 -738 -456 -504 N ATOM 1696 CD2 HIS A 231 8.825 10.571 38.680 1.00 44.70 C ANISOU 1696 CD2 HIS A 231 5943 5837 5204 -686 -477 -655 C ATOM 1697 CE1 HIS A 231 8.209 8.454 38.779 1.00 43.12 C ANISOU 1697 CE1 HIS A 231 5647 5779 4959 -706 -394 -573 C ATOM 1698 NE2 HIS A 231 7.828 9.689 39.071 1.00 41.37 N ANISOU 1698 NE2 HIS A 231 5476 5520 4724 -666 -400 -679 N ATOM 1699 N HIS A 232 14.044 11.841 37.953 1.00 55.52 N ANISOU 1699 N HIS A 232 7318 7072 6706 -1017 -727 -492 N ATOM 1700 CA AHIS A 232 15.472 11.875 37.501 0.50 58.19 C ANISOU 1700 CA AHIS A 232 7585 7434 7089 -1128 -766 -472 C ATOM 1701 CA BHIS A 232 15.280 11.719 37.202 0.50 57.85 C ANISOU 1701 CA BHIS A 232 7528 7397 7057 -1115 -745 -465 C ATOM 1702 C HIS A 232 16.296 10.642 37.762 1.00 56.98 C ANISOU 1702 C HIS A 232 7298 7365 6987 -1131 -790 -461 C ATOM 1703 O HIS A 232 16.439 10.334 38.928 1.00 56.14 O ANISOU 1703 O HIS A 232 7220 7262 6848 -1114 -850 -463 O ATOM 1704 CB AHIS A 232 16.375 13.111 37.995 0.50 60.31 C ANISOU 1704 CB AHIS A 232 7939 7650 7325 -1233 -845 -496 C ATOM 1705 CB BHIS A 232 15.918 13.131 36.726 0.50 60.88 C ANISOU 1705 CB BHIS A 232 7997 7710 7424 -1236 -791 -473 C ATOM 1706 CG AHIS A 232 15.944 13.842 39.230 0.50 66.97 C ANISOU 1706 CG AHIS A 232 8912 8434 8100 -1197 -892 -539 C ATOM 1707 CG BHIS A 232 14.957 14.135 36.109 0.50 65.88 C ANISOU 1707 CG BHIS A 232 8766 8231 8035 -1214 -799 -473 C ATOM 1708 ND1AHIS A 232 14.837 14.671 39.264 0.50 71.82 N ANISOU 1708 ND1AHIS A 232 9641 8965 8683 -1126 -887 -584 N ATOM 1709 ND1BHIS A 232 14.733 14.214 34.746 0.50 71.20 N ANISOU 1709 ND1BHIS A 232 9440 8886 8726 -1260 -772 -435 N ATOM 1710 CD2AHIS A 232 16.582 14.011 40.417 0.50 71.95 C ANISOU 1710 CD2AHIS A 232 9574 9073 8690 -1234 -957 -561 C ATOM 1711 CD2BHIS A 232 14.247 15.153 36.663 0.50 71.37 C ANISOU 1711 CD2BHIS A 232 9604 8816 8698 -1158 -857 -519 C ATOM 1712 CE1AHIS A 232 14.772 15.255 40.451 0.50 75.20 C ANISOU 1712 CE1AHIS A 232 10154 9366 9052 -1116 -932 -646 C ATOM 1713 CE1BHIS A 232 13.890 15.205 34.496 0.50 72.64 C ANISOU 1713 CE1BHIS A 232 9772 8935 8892 -1226 -830 -443 C ATOM 1714 NE2AHIS A 232 15.817 14.868 41.170 0.50 75.05 N ANISOU 1714 NE2AHIS A 232 10097 9403 9017 -1190 -972 -622 N ATOM 1715 NE2BHIS A 232 13.581 15.791 35.642 0.50 72.90 N ANISOU 1715 NE2BHIS A 232 9884 8909 8906 -1152 -884 -505 N ATOM 1716 N HIS A 233 16.922 10.028 36.768 1.00 55.84 N ANISOU 1716 N HIS A 233 7017 7282 6919 -1161 -766 -463 N ATOM 1717 CA HIS A 233 17.896 8.950 36.952 1.00 55.96 C ANISOU 1717 CA HIS A 233 6885 7364 7014 -1154 -825 -489 C ATOM 1718 C HIS A 233 19.270 9.301 36.349 1.00 58.22 C ANISOU 1718 C HIS A 233 7047 7720 7355 -1270 -839 -554 C ATOM 1719 O HIS A 233 19.480 10.444 35.910 1.00 59.21 O ANISOU 1719 O HIS A 233 7233 7834 7430 -1385 -808 -556 O ATOM 1720 CB HIS A 233 17.317 7.650 36.375 1.00 54.16 C ANISOU 1720 CB HIS A 233 6571 7165 6841 -1063 -787 -473 C ATOM 1721 CG HIS A 233 16.197 7.121 37.214 1.00 48.85 C ANISOU 1721 CG HIS A 233 6001 6452 6108 -982 -794 -420 C ATOM 1722 ND1 HIS A 233 14.877 7.214 36.833 1.00 46.49 N ANISOU 1722 ND1 HIS A 233 5767 6137 5759 -935 -701 -392 N ATOM 1723 CD2 HIS A 233 16.191 6.688 38.498 1.00 43.53 C ANISOU 1723 CD2 HIS A 233 5394 5757 5389 -969 -885 -397 C ATOM 1724 CE1 HIS A 233 14.109 6.743 37.798 1.00 37.78 C ANISOU 1724 CE1 HIS A 233 4739 5028 4587 -898 -717 -366 C ATOM 1725 NE2 HIS A 233 14.887 6.418 38.815 1.00 44.44 N ANISOU 1725 NE2 HIS A 233 5598 5867 5422 -929 -828 -360 N TER 1726 HIS A 233 HETATM 1727 C URE A1234 4.922 -10.882 10.540 1.00 65.12 C HETATM 1728 O URE A1234 5.331 -10.332 9.519 1.00 65.82 O HETATM 1729 N1 URE A1234 5.321 -12.095 10.909 1.00 64.91 N HETATM 1730 N2 URE A1234 4.033 -10.253 11.304 1.00 65.10 N HETATM 1731 O HOH A2001 34.423 38.553 5.780 1.00 43.36 O HETATM 1732 O HOH A2002 35.977 43.344 6.752 1.00 40.89 O HETATM 1733 O HOH A2003 24.294 39.203 8.110 1.00 72.29 O HETATM 1734 O HOH A2004 23.819 28.375 -3.724 1.00 31.01 O HETATM 1735 O HOH A2005 19.440 30.787 12.632 1.00 38.84 O HETATM 1736 O HOH A2006 37.371 25.849 10.963 1.00 38.10 O HETATM 1737 O HOH A2007 41.895 26.412 11.295 1.00 38.99 O HETATM 1738 O HOH A2008 18.725 31.064 1.585 1.00 33.69 O HETATM 1739 O HOH A2009 24.530 27.457 -1.190 1.00 27.89 O HETATM 1740 O HOH A2010 25.591 31.389 -1.796 1.00 23.90 O HETATM 1741 O HOH A2011 23.553 33.115 -1.725 1.00 34.61 O HETATM 1742 O HOH A2012 24.098 31.763 -5.115 1.00 40.30 O HETATM 1743 O HOH A2013 31.686 26.952 -0.809 1.00 25.19 O HETATM 1744 O HOH A2014 34.134 30.800 3.300 1.00 37.90 O HETATM 1745 O HOH A2015 25.341 22.616 -0.585 1.00 34.92 O HETATM 1746 O HOH A2016 29.903 25.349 -1.631 1.00 37.49 O HETATM 1747 O HOH A2017 37.565 26.169 0.580 1.00 37.08 O HETATM 1748 O HOH A2018 36.373 23.805 9.165 1.00 38.85 O HETATM 1749 O HOH A2019 32.804 17.635 6.288 1.00 49.02 O HETATM 1750 O HOH A2020 34.273 21.937 9.339 1.00 42.71 O HETATM 1751 O HOH A2021 33.604 25.050 -1.047 1.00 37.60 O HETATM 1752 O HOH A2022 39.162 30.585 4.029 1.00 49.25 O HETATM 1753 O HOH A2023 37.871 28.567 -0.415 1.00 48.00 O HETATM 1754 O HOH A2024 36.483 17.506 11.875 1.00 40.43 O HETATM 1755 O HOH A2025 38.655 19.008 14.765 1.00 50.13 O HETATM 1756 O HOH A2026 39.458 25.126 12.117 1.00 30.68 O HETATM 1757 O HOH A2027 35.302 23.130 16.972 1.00 33.43 O HETATM 1758 O HOH A2028 39.880 29.850 20.092 1.00 43.51 O HETATM 1759 O HOH A2029 28.551 19.154 8.683 1.00 33.49 O HETATM 1760 O HOH A2030 28.467 18.653 3.498 1.00 37.50 O HETATM 1761 O HOH A2031 13.017 21.327 6.546 1.00 48.59 O HETATM 1762 O HOH A2032 11.332 17.964 11.418 1.00 30.76 O HETATM 1763 O HOH A2033 20.120 17.689 0.251 1.00 38.82 O HETATM 1764 O HOH A2034 22.899 23.268 -0.354 1.00 38.16 O HETATM 1765 O HOH A2035 21.631 11.415 3.269 1.00 29.40 O HETATM 1766 O HOH A2036 26.548 16.569 3.763 1.00 24.47 O HETATM 1767 O HOH A2037 19.184 10.017 9.064 1.00 61.11 O HETATM 1768 O HOH A2038 27.771 10.548 6.005 1.00 27.97 O HETATM 1769 O HOH A2039 29.656 16.642 9.610 1.00 31.07 O HETATM 1770 O HOH A2040 4.408 -6.384 25.868 1.00 39.78 O HETATM 1771 O HOH A2041 34.809 14.578 19.573 1.00 49.77 O HETATM 1772 O HOH A2042 35.499 9.819 21.354 1.00 50.14 O HETATM 1773 O HOH A2043 25.739 15.612 24.808 1.00 34.60 O HETATM 1774 O HOH A2044 24.478 20.443 23.401 1.00 33.31 O HETATM 1775 O HOH A2045 30.924 21.888 23.110 1.00 34.09 O HETATM 1776 O HOH A2046 13.485 22.971 20.221 1.00 38.55 O HETATM 1777 O HOH A2047 3.412 11.119 6.784 1.00 63.52 O HETATM 1778 O HOH A2048 8.724 7.381 6.049 1.00 39.68 O HETATM 1779 O HOH A2049 6.423 12.082 10.634 1.00 48.85 O HETATM 1780 O HOH A2050 7.148 0.670 13.136 1.00 43.34 O HETATM 1781 O HOH A2051 20.197 5.654 27.393 1.00 39.02 O HETATM 1782 O HOH A2052 14.108 11.932 29.600 1.00 56.11 O HETATM 1783 O HOH A2053 18.548 14.777 36.557 1.00 50.77 O HETATM 1784 O HOH A2054 13.239 20.566 24.453 1.00 28.09 O HETATM 1785 O HOH A2055 7.386 16.520 26.313 1.00 42.17 O HETATM 1786 O HOH A2056 3.175 15.550 21.736 1.00 33.32 O HETATM 1787 O HOH A2057 1.012 8.384 20.668 1.00 39.50 O HETATM 1788 O HOH A2058 -2.133 7.564 19.471 1.00 40.13 O HETATM 1789 O HOH A2059 2.900 -5.865 4.500 1.00 74.18 O HETATM 1790 O HOH A2060 4.591 -4.695 15.200 1.00 38.79 O HETATM 1791 O HOH A2061 -10.682 -13.339 8.323 1.00 28.84 O HETATM 1792 O HOH A2062 -7.579 -11.079 13.823 1.00 30.30 O HETATM 1793 O HOH A2063 -9.994 -6.454 0.012 1.00 46.87 O HETATM 1794 O HOH A2064 0.368 -16.317 9.700 1.00 47.25 O HETATM 1795 O HOH A2065 5.775 -9.490 13.320 1.00 51.29 O HETATM 1796 O HOH A2066 7.065 -12.145 16.163 1.00 58.49 O HETATM 1797 O HOH A2067 4.092 -7.744 23.515 1.00 35.65 O HETATM 1798 O HOH A2068 3.007 4.398 23.367 1.00 35.73 O HETATM 1799 O HOH A2069 -2.491 4.863 27.482 1.00 46.56 O HETATM 1800 O HOH A2070 2.309 7.376 22.644 1.00 49.53 O HETATM 1801 O HOH A2071 -8.698 -2.766 22.966 1.00 34.53 O HETATM 1802 O HOH A2072 -11.872 -20.905 19.094 1.00 40.82 O HETATM 1803 O HOH A2073 -4.820 -24.714 16.900 1.00 58.49 O HETATM 1804 O HOH A2074 -4.060 -24.321 20.386 1.00 42.01 O HETATM 1805 O HOH A2075 -8.349 -25.330 24.218 1.00 34.37 O HETATM 1806 O HOH A2076 -3.419 -2.907 29.928 1.00 34.24 O HETATM 1807 O HOH A2077 -5.198 0.122 34.339 1.00 33.95 O HETATM 1808 O HOH A2078 -9.232 4.159 33.443 1.00 33.72 O HETATM 1809 O HOH A2079 -5.883 3.948 35.554 1.00 42.56 O HETATM 1810 O HOH A2080 -9.226 9.142 31.522 1.00 37.56 O HETATM 1811 O HOH A2081 -9.978 6.444 34.154 1.00 26.49 O HETATM 1812 O HOH A2082 7.583 8.265 31.835 1.00 46.39 O HETATM 1813 O HOH A2083 10.546 10.715 31.602 1.00 41.31 O HETATM 1814 O HOH A2084 13.861 9.737 33.896 1.00 60.35 O CONECT 1727 1728 1729 1730 CONECT 1728 1727 CONECT 1729 1727 CONECT 1730 1727 MASTER 436 0 1 10 0 0 1 6 1792 1 4 18 END If you find results from this site 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