HEADER HYDROLASE 16-OCT-08 3EWO TITLE IBV NSP3 ADRP DOMAIN CAVEAT 3EWO CHIRALITY ERROR AT CA CENTER OF HIS B 100. COMPND MOL_ID: 1; COMPND 2 MOLECULE: NON-STRUCTURAL PROTEIN 3; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: NSP3 ADRP DOMAIN; COMPND 5 SYNONYM: NSP3, PAPAIN-LIKE PROTEINASE, PL-PRO, P195; COMPND 6 EC: 3.4.22.-; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: AVIAN INFECTIOUS BRONCHITIS VIRUS; SOURCE 3 ORGANISM_COMMON: IBV; SOURCE 4 GENE: 1A; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1 KEYWDS GLOBULAR LIKE, CYTOPLASM, HYDROLASE, MEMBRANE, METAL- KEYWDS 2 BINDING, PROTEASE, RIBOSOMAL FRAMESHIFTING, RNA-BINDING, KEYWDS 3 THIOL PROTEASE, TRANSMEMBRANE, ZINC, ZINC-FINGER EXPDTA X-RAY DIFFRACTION AUTHOR Y.XU,L.CONG,C.CHEN,L.WEI,Q.ZHAO,X.XU,Y.MA,M.BARTLAM,Z.RAO REVDAT 1 13-JAN-09 3EWO 0 JRNL AUTH Y.XU,L.CONG,C.CHEN,L.WEI,Q.ZHAO,X.XU,Y.MA, JRNL AUTH 2 M.BARTLAM,Z.RAO JRNL TITL CRYSTAL STRUCTURES OF TWO CORONAVIRUS JRNL TITL 2 ADP-RIBOSE-1''-MONOPHOSPHATASES AND THEIR JRNL TITL 3 COMPLEXES WITH ADP-RIBOSE: A SYSTEMATIC STRUCTURAL JRNL TITL 4 ANALYSIS OF THE VIRAL ADRP DOMAIN. JRNL REF J.VIROL. V. 83 1083 2009 JRNL REFN ISSN 0022-538X JRNL PMID 18987156 JRNL DOI 10.1128/JVI.01862-08 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0019 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON 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) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 24396 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) : 0.174 REMARK 3 R VALUE (WORKING SET) : 0.171 REMARK 3 FREE R VALUE : 0.238 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1298 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) : 1089 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00 REMARK 3 BIN R VALUE (WORKING SET) : 0.1940 REMARK 3 BIN FREE R VALUE SET COUNT : 47 REMARK 3 BIN FREE R VALUE : 0.2780 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2604 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 202 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.75 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.25000 REMARK 3 B22 (A**2) : 0.12000 REMARK 3 B33 (A**2) : -0.46000 REMARK 3 B12 (A**2) : 1.31000 REMARK 3 B13 (A**2) : -0.14000 REMARK 3 B23 (A**2) : -0.22000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.591 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.149 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.107 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.673 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2648 ; 0.016 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3574 ; 1.588 ; 1.958 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 337 ; 7.954 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 107 ;36.100 ;24.486 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 448 ;15.864 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;22.660 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 405 ; 0.106 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1967 ; 0.007 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1321 ; 0.219 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1844 ; 0.313 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 161 ; 0.132 ; 0.200 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): 62 ; 0.179 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 0.143 ; 0.200 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): 1723 ; 1.448 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2707 ; 2.212 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1030 ; 3.633 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 867 ; 5.050 ; 4.500 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 : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 3EWO COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-OCT-08. REMARK 100 THE RCSB ID CODE IS RCSB049860. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 23-NOV-07 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PHOTON FACTORY REMARK 200 BEAMLINE : BL-5A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9798 REMARK 200 MONOCHROMATOR : GRAPHITE REMARK 200 OPTICS : MONOCHROMATER REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25343 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 80.2 REMARK 200 DATA REDUNDANCY : 7.100 REMARK 200 R MERGE (I) : 0.41000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL 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) : 1.85 REMARK 200 COMPLETENESS FOR SHELL (%) : 90.0 REMARK 200 DATA REDUNDANCY IN SHELL : 7.10 REMARK 200 R MERGE FOR SHELL (I) : 0.41000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD REMARK 200 SOFTWARE USED: SOLVE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 41.68 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.12M MAGNESIUM CHLORIDE REMARK 280 HEXAHYDRATE, 0.1M HEPES PH 7.5, 22% W/V PEG 3350, VAPOR REMARK 280 DIFFUSION, TEMPERATURE 291.0K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 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 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 LEU B -2 REMARK 465 GLY B -1 REMARK 465 SER B 0 REMARK 465 VAL B 1 REMARK 465 LYS B 2 REMARK 465 PRO B 3 REMARK 465 ALA B 4 REMARK 465 THR B 5 REMARK 465 CYS B 6 REMARK 465 GLU B 7 REMARK 465 PHE B 134 REMARK 465 LYS B 174 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O ARG B 106 N LEU B 109 1.88 REMARK 500 O ARG B 106 N LYS B 108 2.12 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 B 105 N - CA - C ANGL. DEV. = -17.6 DEGREES REMARK 500 ARG B 106 CB - CA - C ANGL. DEV. = 33.2 DEGREES REMARK 500 ARG B 106 N - CA - C ANGL. DEV. = -41.1 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 LYS B 33 -57.03 76.38 REMARK 500 HIS B 100 -74.57 57.92 REMARK 500 ASP B 102 105.62 67.25 REMARK 500 ASN B 104 71.01 3.46 REMARK 500 LEU B 105 115.81 -36.63 REMARK 500 ARG B 106 -70.27 -147.02 REMARK 500 GLU B 107 -37.02 -34.37 REMARK 500 SER B 130 33.27 70.28 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ARG B 99 HIS B 100 118.37 REMARK 500 HIS B 100 GLY B 101 121.42 REMARK 500 GLY B 101 ASP B 102 50.00 REMARK 500 ASN B 104 LEU B 105 128.65 REMARK 500 LEU B 105 ARG B 106 87.18 REMARK 500 ARG B 106 GLU B 107 -147.07 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 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: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 HIS B 100 122.6 ALPHA-CARBON REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3EWP RELATED DB: PDB REMARK 900 RELATED ID: 3EWQ RELATED DB: PDB REMARK 900 RELATED ID: 3EWR RELATED DB: PDB DBREF 3EWO A 1 174 UNP P0C6V5 R1A_IBVM 1005 1178 DBREF 3EWO B 1 174 UNP P0C6V5 R1A_IBVM 1005 1178 SEQADV 3EWO LEU A -2 UNP P0C6V5 EXPRESSION TAG SEQADV 3EWO GLY A -1 UNP P0C6V5 EXPRESSION TAG SEQADV 3EWO SER A 0 UNP P0C6V5 EXPRESSION TAG SEQADV 3EWO LEU B -2 UNP P0C6V5 EXPRESSION TAG SEQADV 3EWO GLY B -1 UNP P0C6V5 EXPRESSION TAG SEQADV 3EWO SER B 0 UNP P0C6V5 EXPRESSION TAG SEQRES 1 A 177 LEU GLY SER VAL LYS PRO ALA THR CYS GLU LYS PRO LYS SEQRES 2 A 177 PHE LEU GLU TYR LYS THR CYS VAL GLY ASP LEU ALA VAL SEQRES 3 A 177 VAL ILE ALA LYS ALA LEU ASP GLU PHE LYS GLU PHE CYS SEQRES 4 A 177 ILE VAL ASN ALA ALA ASN GLU HIS MET SER HIS GLY GLY SEQRES 5 A 177 GLY VAL ALA LYS ALA ILE ALA ASP PHE CYS GLY PRO ASP SEQRES 6 A 177 PHE VAL GLU TYR CYS ALA ASP TYR VAL LYS LYS HIS GLY SEQRES 7 A 177 PRO GLN GLN LYS LEU VAL THR PRO SER PHE VAL LYS GLY SEQRES 8 A 177 ILE GLN CYS VAL ASN ASN VAL VAL GLY PRO ARG HIS GLY SEQRES 9 A 177 ASP SER ASN LEU ARG GLU LYS LEU VAL ALA ALA TYR LYS SEQRES 10 A 177 SER VAL LEU VAL GLY GLY VAL VAL ASN TYR VAL VAL PRO SEQRES 11 A 177 VAL LEU SER SER GLY ILE PHE GLY VAL ASP PHE LYS ILE SEQRES 12 A 177 SER ILE ASP ALA MET ARG GLU ALA PHE LYS GLY CYS ALA SEQRES 13 A 177 ILE ARG VAL LEU LEU PHE SER LEU SER GLN GLU HIS ILE SEQRES 14 A 177 ASP TYR PHE ASP ALA THR CYS LYS SEQRES 1 B 177 LEU GLY SER VAL LYS PRO ALA THR CYS GLU LYS PRO LYS SEQRES 2 B 177 PHE LEU GLU TYR LYS THR CYS VAL GLY ASP LEU ALA VAL SEQRES 3 B 177 VAL ILE ALA LYS ALA LEU ASP GLU PHE LYS GLU PHE CYS SEQRES 4 B 177 ILE VAL ASN ALA ALA ASN GLU HIS MET SER HIS GLY GLY SEQRES 5 B 177 GLY VAL ALA LYS ALA ILE ALA ASP PHE CYS GLY PRO ASP SEQRES 6 B 177 PHE VAL GLU TYR CYS ALA ASP TYR VAL LYS LYS HIS GLY SEQRES 7 B 177 PRO GLN GLN LYS LEU VAL THR PRO SER PHE VAL LYS GLY SEQRES 8 B 177 ILE GLN CYS VAL ASN ASN VAL VAL GLY PRO ARG HIS GLY SEQRES 9 B 177 ASP SER ASN LEU ARG GLU LYS LEU VAL ALA ALA TYR LYS SEQRES 10 B 177 SER VAL LEU VAL GLY GLY VAL VAL ASN TYR VAL VAL PRO SEQRES 11 B 177 VAL LEU SER SER GLY ILE PHE GLY VAL ASP PHE LYS ILE SEQRES 12 B 177 SER ILE ASP ALA MET ARG GLU ALA PHE LYS GLY CYS ALA SEQRES 13 B 177 ILE ARG VAL LEU LEU PHE SER LEU SER GLN GLU HIS ILE SEQRES 14 B 177 ASP TYR PHE ASP ALA THR CYS LYS FORMUL 3 HOH *202(H2 O) HELIX 1 1 ASP A 20 PHE A 32 1 13 HELIX 2 2 GLY A 49 GLY A 60 1 12 HELIX 3 3 GLY A 60 GLY A 75 1 16 HELIX 4 4 ASN A 104 LEU A 117 1 14 HELIX 5 5 ASP A 137 LYS A 150 1 14 HELIX 6 6 SER A 162 CYS A 173 1 12 HELIX 7 7 ASP B 20 LYS B 33 1 14 HELIX 8 8 GLY B 49 GLY B 60 1 12 HELIX 9 9 GLY B 60 GLY B 75 1 16 HELIX 10 10 GLU B 107 SER B 115 1 9 HELIX 11 11 ASP B 137 LYS B 150 1 14 HELIX 12 12 SER B 162 CYS B 173 1 12 SHEET 1 A 6 GLU A 13 VAL A 18 0 SHEET 2 A 6 ARG A 155 SER A 160 1 O VAL A 156 N GLU A 13 SHEET 3 A 6 ASN A 123 PRO A 127 1 N TYR A 124 O LEU A 157 SHEET 4 A 6 PHE A 35 ALA A 40 1 N VAL A 38 O VAL A 125 SHEET 5 A 6 ILE A 89 VAL A 95 1 O ASN A 93 N ASN A 39 SHEET 6 A 6 LYS A 79 THR A 82 -1 N THR A 82 O VAL A 92 SHEET 1 B 6 GLU B 13 VAL B 18 0 SHEET 2 B 6 ARG B 155 SER B 160 1 O VAL B 156 N GLU B 13 SHEET 3 B 6 ASN B 123 PRO B 127 1 N TYR B 124 O ARG B 155 SHEET 4 B 6 PHE B 35 ALA B 40 1 N VAL B 38 O VAL B 125 SHEET 5 B 6 ILE B 89 VAL B 95 1 O VAL B 95 N ASN B 39 SHEET 6 B 6 LYS B 79 THR B 82 -1 N THR B 82 O VAL B 92 CRYST1 41.139 43.201 48.940 78.02 80.06 73.57 P 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 0.024308 -0.007168 -0.003100 0.00000 SCALE2 0.000000 0.024133 -0.004113 0.00000 SCALE3 0.000000 0.000000 0.021044 0.00000 ATOM 1 N LEU A -2 46.581 11.285 20.580 1.00 45.99 N ATOM 2 CA LEU A -2 45.619 10.799 21.620 1.00 45.78 C ATOM 3 C LEU A -2 44.285 11.546 21.547 1.00 45.12 C ATOM 4 O LEU A -2 44.173 12.598 20.887 1.00 44.27 O ATOM 5 CB LEU A -2 46.222 10.838 23.048 1.00 45.87 C ATOM 6 CG LEU A -2 46.793 9.553 23.704 1.00 47.41 C ATOM 7 CD1 LEU A -2 45.866 8.310 23.564 1.00 48.11 C ATOM 8 CD2 LEU A -2 48.214 9.206 23.239 1.00 47.39 C ATOM 9 N GLY A -1 43.281 10.974 22.213 1.00 44.25 N ATOM 10 CA GLY A -1 41.919 11.485 22.169 1.00 43.72 C ATOM 11 C GLY A -1 41.074 10.756 21.139 1.00 43.53 C ATOM 12 O GLY A -1 41.610 10.090 20.252 1.00 43.28 O ATOM 13 N SER A 0 39.750 10.875 21.255 1.00 43.00 N ATOM 14 CA SER A 0 38.842 10.225 20.312 1.00 42.84 C ATOM 15 C SER A 0 37.978 11.239 19.564 1.00 43.06 C ATOM 16 O SER A 0 37.715 12.336 20.079 1.00 42.57 O ATOM 17 CB SER A 0 37.962 9.205 21.032 1.00 43.09 C ATOM 18 OG SER A 0 38.756 8.126 21.503 1.00 43.41 O ATOM 19 N VAL A 1 37.569 10.888 18.338 1.00 43.08 N ATOM 20 CA VAL A 1 36.635 11.733 17.591 1.00 43.40 C ATOM 21 C VAL A 1 35.228 11.367 18.047 1.00 44.11 C ATOM 22 O VAL A 1 34.998 10.232 18.484 1.00 44.36 O ATOM 23 CB VAL A 1 36.797 11.640 16.037 1.00 43.38 C ATOM 24 CG1 VAL A 1 38.244 11.895 15.626 1.00 42.68 C ATOM 25 CG2 VAL A 1 36.319 10.313 15.489 1.00 43.20 C ATOM 26 N LYS A 2 34.301 12.321 17.983 1.00 44.56 N ATOM 27 CA LYS A 2 32.912 12.034 18.344 1.00 45.24 C ATOM 28 C LYS A 2 32.438 10.825 17.524 1.00 45.24 C ATOM 29 O LYS A 2 32.602 10.811 16.295 1.00 44.84 O ATOM 30 CB LYS A 2 32.019 13.252 18.098 1.00 45.50 C ATOM 31 CG LYS A 2 30.608 13.145 18.687 1.00 46.82 C ATOM 32 CD LYS A 2 30.074 14.539 19.064 1.00 49.79 C ATOM 33 CE LYS A 2 28.658 14.488 19.637 1.00 51.87 C ATOM 34 NZ LYS A 2 27.606 14.446 18.573 1.00 52.54 N ATOM 35 N PRO A 3 31.892 9.788 18.200 1.00 45.43 N ATOM 36 CA PRO A 3 31.438 8.600 17.465 1.00 45.27 C ATOM 37 C PRO A 3 30.324 8.946 16.481 1.00 45.00 C ATOM 38 O PRO A 3 29.505 9.840 16.753 1.00 44.76 O ATOM 39 CB PRO A 3 30.918 7.669 18.574 1.00 45.18 C ATOM 40 CG PRO A 3 31.601 8.141 19.801 1.00 45.47 C ATOM 41 CD PRO A 3 31.680 9.630 19.649 1.00 45.37 C ATOM 42 N ALA A 4 30.323 8.246 15.346 1.00 45.01 N ATOM 43 CA ALA A 4 29.341 8.429 14.279 1.00 44.97 C ATOM 44 C ALA A 4 27.933 8.125 14.783 1.00 44.89 C ATOM 45 O ALA A 4 27.758 7.273 15.665 1.00 44.99 O ATOM 46 CB ALA A 4 29.686 7.514 13.095 1.00 45.16 C ATOM 47 N THR A 5 26.939 8.819 14.224 1.00 44.70 N ANISOU 47 N THR A 5 5527 5713 5742 -25 113 86 N ATOM 48 CA THR A 5 25.528 8.533 14.529 1.00 44.47 C ANISOU 48 CA THR A 5 5379 5740 5774 -43 167 154 C ATOM 49 C THR A 5 24.939 7.443 13.639 1.00 43.63 C ANISOU 49 C THR A 5 5185 5706 5685 -68 239 183 C ATOM 50 O THR A 5 23.892 6.879 13.949 1.00 44.04 O ANISOU 50 O THR A 5 5176 5794 5764 -61 236 237 O ATOM 51 CB THR A 5 24.644 9.779 14.466 1.00 44.81 C ANISOU 51 CB THR A 5 5380 5823 5820 -17 186 165 C ATOM 52 OG1 THR A 5 23.335 9.443 14.947 1.00 46.44 O ANISOU 52 OG1 THR A 5 5619 5922 6103 -223 132 229 O ATOM 53 CG2 THR A 5 24.550 10.318 13.037 1.00 45.09 C ANISOU 53 CG2 THR A 5 5496 5876 5760 -26 169 221 C ATOM 54 N CYS A 6 25.609 7.139 12.535 1.00 42.57 N ANISOU 54 N CYS A 6 5024 5605 5544 -120 322 233 N ATOM 55 CA CYS A 6 25.234 5.961 11.769 1.00 41.35 C ANISOU 55 CA CYS A 6 4867 5417 5424 -171 459 249 C ATOM 56 C CYS A 6 25.838 4.694 12.370 1.00 39.66 C ANISOU 56 C CYS A 6 4620 5170 5279 -235 429 262 C ATOM 57 O CYS A 6 26.773 4.733 13.169 1.00 40.10 O ANISOU 57 O CYS A 6 4715 5183 5335 -230 380 274 O ATOM 58 CB CYS A 6 25.625 6.099 10.311 1.00 41.97 C ANISOU 58 CB CYS A 6 4902 5550 5493 -135 463 243 C ATOM 59 SG CYS A 6 27.375 6.350 10.103 1.00 46.27 S ANISOU 59 SG CYS A 6 5456 6338 5785 -122 1056 184 S ATOM 60 N GLU A 7 25.276 3.569 11.962 1.00 37.18 N ANISOU 60 N GLU A 7 4328 4738 5058 -332 510 330 N ATOM 61 CA GLU A 7 25.594 2.269 12.503 1.00 34.85 C ANISOU 61 CA GLU A 7 3964 4416 4859 -444 562 378 C ATOM 62 C GLU A 7 26.604 1.538 11.622 1.00 31.68 C ANISOU 62 C GLU A 7 3498 3967 4572 -564 634 435 C ATOM 63 O GLU A 7 26.550 1.634 10.393 1.00 30.28 O ANISOU 63 O GLU A 7 3168 3814 4521 -614 647 412 O ATOM 64 CB GLU A 7 24.295 1.456 12.581 1.00 35.42 C ANISOU 64 CB GLU A 7 4008 4505 4945 -488 534 363 C ATOM 65 CG GLU A 7 23.535 1.345 11.231 1.00 38.67 C ANISOU 65 CG GLU A 7 4543 4914 5233 -478 529 333 C ATOM 66 CD GLU A 7 23.245 2.697 10.547 1.00 42.77 C ANISOU 66 CD GLU A 7 5122 5609 5517 -529 656 203 C ATOM 67 OE1 GLU A 7 22.608 3.595 11.170 1.00 43.84 O ANISOU 67 OE1 GLU A 7 5165 5770 5719 -634 517 68 O ATOM 68 OE2 GLU A 7 23.646 2.854 9.370 1.00 44.26 O ANISOU 68 OE2 GLU A 7 5315 5942 5560 -528 1017 208 O ATOM 69 N LYS A 8 27.504 0.798 12.262 1.00 28.60 N ANISOU 69 N LYS A 8 3120 3487 4260 -751 652 512 N ATOM 70 CA LYS A 8 28.400 -0.102 11.555 1.00 26.53 C ANISOU 70 CA LYS A 8 2902 3103 4075 -905 629 623 C ATOM 71 C LYS A 8 27.615 -1.100 10.698 1.00 25.38 C ANISOU 71 C LYS A 8 2843 2884 3913 -896 696 641 C ATOM 72 O LYS A 8 26.492 -1.498 11.059 1.00 23.72 O ANISOU 72 O LYS A 8 2584 2660 3768 -1158 857 746 O ATOM 73 CB LYS A 8 29.333 -0.840 12.530 1.00 26.87 C ANISOU 73 CB LYS A 8 3066 3053 4090 -902 559 583 C ATOM 74 CG LYS A 8 28.674 -1.956 13.316 1.00 25.93 C ANISOU 74 CG LYS A 8 2765 3116 3969 -1006 614 665 C ATOM 75 CD LYS A 8 29.663 -2.677 14.219 1.00 27.09 C ANISOU 75 CD LYS A 8 2759 3340 4191 -975 563 653 C ATOM 76 CE LYS A 8 29.981 -1.810 15.430 1.00 31.71 C ANISOU 76 CE LYS A 8 3152 4045 4850 -477 116 650 C ATOM 77 NZ LYS A 8 31.106 -2.373 16.256 1.00 36.06 N ANISOU 77 NZ LYS A 8 3421 4661 5619 -427 124 592 N ATOM 78 N PRO A 9 28.190 -1.490 9.559 1.00 23.99 N ANISOU 78 N PRO A 9 2756 2624 3734 -931 790 709 N ATOM 79 CA PRO A 9 27.551 -2.514 8.760 1.00 23.53 C ANISOU 79 CA PRO A 9 2774 2445 3721 -1032 831 735 C ATOM 80 C PRO A 9 27.812 -3.889 9.375 1.00 23.53 C ANISOU 80 C PRO A 9 2868 2354 3716 -1017 858 757 C ATOM 81 O PRO A 9 28.709 -4.042 10.217 1.00 23.00 O ANISOU 81 O PRO A 9 2742 2300 3695 -1164 957 853 O ATOM 82 CB PRO A 9 28.281 -2.413 7.427 1.00 22.91 C ANISOU 82 CB PRO A 9 2729 2338 3636 -958 875 749 C ATOM 83 CG PRO A 9 29.664 -2.036 7.834 1.00 22.99 C ANISOU 83 CG PRO A 9 2694 2444 3595 -1026 824 796 C ATOM 84 CD PRO A 9 29.463 -1.051 8.950 1.00 24.00 C ANISOU 84 CD PRO A 9 2735 2595 3789 -981 753 681 C ATOM 85 N LYS A 10 27.039 -4.868 8.923 1.00 23.41 N ANISOU 85 N LYS A 10 2933 2192 3770 -1174 901 747 N ATOM 86 CA LYS A 10 27.153 -6.259 9.372 1.00 24.15 C ANISOU 86 CA LYS A 10 3155 2234 3785 -1199 945 723 C ATOM 87 C LYS A 10 28.443 -6.898 8.935 1.00 23.09 C ANISOU 87 C LYS A 10 3080 2028 3663 -1279 916 702 C ATOM 88 O LYS A 10 28.982 -7.733 9.639 1.00 22.70 O ANISOU 88 O LYS A 10 2975 2060 3588 -1374 1053 785 O ATOM 89 CB LYS A 10 25.970 -7.073 8.844 1.00 25.11 C ANISOU 89 CB LYS A 10 3370 2234 3936 -1244 914 679 C ATOM 90 CG LYS A 10 25.981 -8.560 9.151 1.00 29.36 C ANISOU 90 CG LYS A 10 4152 2779 4223 -931 1069 697 C ATOM 91 CD LYS A 10 25.956 -8.916 10.653 1.00 33.61 C ANISOU 91 CD LYS A 10 4958 3345 4464 -884 1176 673 C ATOM 92 CE LYS A 10 25.028 -10.123 10.935 1.00 32.11 C ANISOU 92 CE LYS A 10 4686 3062 4451 -896 1373 520 C ATOM 93 NZ LYS A 10 25.422 -11.434 10.332 1.00 30.66 N ANISOU 93 NZ LYS A 10 4437 2913 4298 -1043 1555 492 N ATOM 94 N PHE A 11 28.936 -6.505 7.761 1.00 21.75 N ANISOU 94 N PHE A 11 2983 1783 3497 -1432 887 631 N ATOM 95 CA PHE A 11 30.241 -6.942 7.306 1.00 20.99 C ANISOU 95 CA PHE A 11 2826 1605 3545 -1537 742 527 C ATOM 96 C PHE A 11 30.902 -5.827 6.531 1.00 19.87 C ANISOU 96 C PHE A 11 2706 1550 3293 -1505 762 555 C ATOM 97 O PHE A 11 30.269 -4.849 6.198 1.00 20.13 O ANISOU 97 O PHE A 11 2645 1715 3287 -1606 787 502 O ATOM 98 CB PHE A 11 30.155 -8.168 6.405 1.00 22.24 C ANISOU 98 CB PHE A 11 3074 1652 3721 -1434 655 488 C ATOM 99 CG PHE A 11 29.618 -9.382 7.107 1.00 22.43 C ANISOU 99 CG PHE A 11 3160 1413 3946 -1694 573 452 C ATOM 100 CD1 PHE A 11 30.468 -10.173 7.878 1.00 25.29 C ANISOU 100 CD1 PHE A 11 3791 1452 4365 -1544 476 528 C ATOM 101 CD2 PHE A 11 28.277 -9.701 7.042 1.00 26.65 C ANISOU 101 CD2 PHE A 11 3777 1998 4348 -1296 321 244 C ATOM 102 CE1 PHE A 11 29.986 -11.294 8.539 1.00 26.02 C ANISOU 102 CE1 PHE A 11 3834 1596 4454 -1700 460 431 C ATOM 103 CE2 PHE A 11 27.771 -10.795 7.707 1.00 23.57 C ANISOU 103 CE2 PHE A 11 3351 1385 4217 -1796 354 390 C ATOM 104 CZ PHE A 11 28.625 -11.606 8.468 1.00 24.84 C ANISOU 104 CZ PHE A 11 3333 1728 4375 -1638 374 185 C ATOM 105 N LEU A 12 32.170 -6.030 6.229 1.00 19.24 N ANISOU 105 N LEU A 12 2630 1576 3102 -1512 715 519 N ATOM 106 CA LEU A 12 32.946 -5.102 5.410 1.00 18.80 C ANISOU 106 CA LEU A 12 2431 1726 2983 -1525 670 478 C ATOM 107 C LEU A 12 32.220 -4.795 4.092 1.00 18.17 C ANISOU 107 C LEU A 12 2330 1743 2829 -1451 587 500 C ATOM 108 O LEU A 12 31.821 -5.714 3.382 1.00 17.57 O ANISOU 108 O LEU A 12 2366 1466 2841 -1492 432 325 O ATOM 109 CB LEU A 12 34.302 -5.721 5.135 1.00 18.76 C ANISOU 109 CB LEU A 12 2363 1839 2924 -1490 635 512 C ATOM 110 CG LEU A 12 35.265 -4.960 4.205 1.00 19.63 C ANISOU 110 CG LEU A 12 2334 1936 3187 -1656 639 490 C ATOM 111 CD1 LEU A 12 35.743 -3.634 4.827 1.00 20.90 C ANISOU 111 CD1 LEU A 12 2257 2414 3268 -1323 835 744 C ATOM 112 CD2 LEU A 12 36.405 -5.900 3.901 1.00 18.70 C ANISOU 112 CD2 LEU A 12 1711 2276 3115 -1545 502 485 C ATOM 113 N GLU A 13 32.055 -3.515 3.766 1.00 17.31 N ANISOU 113 N GLU A 13 2110 1813 2651 -1438 619 508 N ATOM 114 CA GLU A 13 31.415 -3.148 2.504 1.00 17.87 C ANISOU 114 CA GLU A 13 2054 1996 2739 -1444 629 647 C ATOM 115 C GLU A 13 32.308 -2.230 1.704 1.00 17.28 C ANISOU 115 C GLU A 13 1898 2070 2597 -1392 546 713 C ATOM 116 O GLU A 13 32.784 -1.227 2.230 1.00 18.02 O ANISOU 116 O GLU A 13 2138 2116 2590 -1510 556 744 O ATOM 117 CB GLU A 13 30.096 -2.452 2.718 1.00 18.01 C ANISOU 117 CB GLU A 13 1941 2088 2812 -1487 603 576 C ATOM 118 CG GLU A 13 29.080 -3.320 3.501 1.00 21.64 C ANISOU 118 CG GLU A 13 2477 2584 3160 -1386 689 685 C ATOM 119 CD GLU A 13 27.790 -2.597 3.748 1.00 25.64 C ANISOU 119 CD GLU A 13 2783 3108 3849 -1380 586 758 C ATOM 120 OE1 GLU A 13 27.698 -1.420 3.353 1.00 26.36 O ANISOU 120 OE1 GLU A 13 2587 3329 4098 -1173 489 1036 O ATOM 121 OE2 GLU A 13 26.874 -3.185 4.361 1.00 28.07 O ANISOU 121 OE2 GLU A 13 3214 3534 3914 -1146 923 750 O ATOM 122 N TYR A 14 32.482 -2.561 0.435 1.00 16.66 N ANISOU 122 N TYR A 14 1763 2104 2462 -1388 415 715 N ATOM 123 CA TYR A 14 33.257 -1.691 -0.478 1.00 16.69 C ANISOU 123 CA TYR A 14 1718 2145 2475 -1407 333 755 C ATOM 124 C TYR A 14 32.375 -0.994 -1.514 1.00 16.95 C ANISOU 124 C TYR A 14 1791 2230 2418 -1509 255 775 C ATOM 125 O TYR A 14 31.399 -1.577 -2.024 1.00 18.22 O ANISOU 125 O TYR A 14 1965 2432 2523 -1384 98 802 O ATOM 126 CB TYR A 14 34.305 -2.502 -1.221 1.00 16.94 C ANISOU 126 CB TYR A 14 1696 2190 2548 -1460 281 728 C ATOM 127 CG TYR A 14 35.498 -2.921 -0.416 1.00 17.04 C ANISOU 127 CG TYR A 14 1590 2290 2594 -1483 218 707 C ATOM 128 CD1 TYR A 14 36.461 -1.973 0.018 1.00 17.58 C ANISOU 128 CD1 TYR A 14 1387 2591 2701 -1568 88 520 C ATOM 129 CD2 TYR A 14 35.740 -4.265 -0.177 1.00 16.96 C ANISOU 129 CD2 TYR A 14 1317 2766 2361 -1330 363 844 C ATOM 130 CE1 TYR A 14 37.575 -2.379 0.736 1.00 16.65 C ANISOU 130 CE1 TYR A 14 1377 2286 2662 -1420 228 461 C ATOM 131 CE2 TYR A 14 36.846 -4.676 0.520 1.00 16.73 C ANISOU 131 CE2 TYR A 14 1043 2899 2413 -1397 -41 683 C ATOM 132 CZ TYR A 14 37.771 -3.722 0.975 1.00 17.68 C ANISOU 132 CZ TYR A 14 1342 2760 2613 -1418 290 849 C ATOM 133 OH TYR A 14 38.869 -4.148 1.678 1.00 19.27 O ANISOU 133 OH TYR A 14 1530 3073 2716 -1414 232 789 O ATOM 134 N LYS A 15 32.734 0.255 -1.820 1.00 17.05 N ANISOU 134 N LYS A 15 1843 2216 2418 -1440 153 700 N ATOM 135 CA LYS A 15 32.191 1.002 -2.937 1.00 16.96 C ANISOU 135 CA LYS A 15 1793 2313 2337 -1519 279 791 C ATOM 136 C LYS A 15 33.383 1.620 -3.638 1.00 16.25 C ANISOU 136 C LYS A 15 1663 2161 2349 -1334 267 732 C ATOM 137 O LYS A 15 34.468 1.727 -3.061 1.00 16.47 O ANISOU 137 O LYS A 15 1754 2088 2414 -1404 309 755 O ATOM 138 CB LYS A 15 31.197 2.075 -2.475 1.00 17.47 C ANISOU 138 CB LYS A 15 1734 2483 2420 -1540 323 810 C ATOM 139 CG LYS A 15 30.013 1.486 -1.617 1.00 18.65 C ANISOU 139 CG LYS A 15 1888 2898 2300 -1536 511 1025 C ATOM 140 CD LYS A 15 28.950 2.559 -1.278 1.00 19.99 C ANISOU 140 CD LYS A 15 2061 2811 2724 -1796 392 968 C ATOM 141 CE LYS A 15 27.605 1.950 -0.800 1.00 22.71 C ANISOU 141 CE LYS A 15 2040 3562 3025 -2130 361 684 C ATOM 142 NZ LYS A 15 26.896 1.231 -1.905 1.00 28.93 N ANISOU 142 NZ LYS A 15 2459 4656 3874 -2068 -136 686 N ATOM 143 N THR A 16 33.189 2.007 -4.880 1.00 17.02 N ANISOU 143 N THR A 16 1741 2239 2484 -1261 199 777 N ATOM 144 CA THR A 16 34.259 2.683 -5.634 1.00 17.38 C ANISOU 144 CA THR A 16 1600 2261 2739 -1254 140 809 C ATOM 145 C THR A 16 33.769 3.932 -6.309 1.00 17.92 C ANISOU 145 C THR A 16 1540 2394 2872 -1097 80 888 C ATOM 146 O THR A 16 32.585 4.039 -6.623 1.00 19.00 O ANISOU 146 O THR A 16 1748 2493 2977 -993 -76 1005 O ATOM 147 CB THR A 16 34.828 1.825 -6.779 1.00 18.34 C ANISOU 147 CB THR A 16 1758 2446 2763 -1234 37 819 C ATOM 148 OG1 THR A 16 33.787 1.546 -7.720 1.00 19.78 O ANISOU 148 OG1 THR A 16 2014 2600 2901 -1738 155 819 O ATOM 149 CG2 THR A 16 35.438 0.544 -6.271 1.00 18.40 C ANISOU 149 CG2 THR A 16 2023 1968 2997 -1272 146 599 C ATOM 150 N CYS A 17 34.694 4.855 -6.583 1.00 17.91 N ANISOU 150 N CYS A 17 1562 2342 2900 -950 145 864 N ATOM 151 CA CYS A 17 34.390 6.029 -7.377 1.00 17.36 C ANISOU 151 CA CYS A 17 1468 2281 2845 -923 152 865 C ATOM 152 C CYS A 17 35.610 6.478 -8.157 1.00 17.67 C ANISOU 152 C CYS A 17 1632 2299 2780 -745 191 906 C ATOM 153 O CYS A 17 36.685 6.694 -7.573 1.00 16.52 O ANISOU 153 O CYS A 17 1287 2166 2823 -875 81 1035 O ATOM 154 CB CYS A 17 33.930 7.165 -6.476 1.00 16.30 C ANISOU 154 CB CYS A 17 1215 2029 2946 -1079 211 869 C ATOM 155 SG CYS A 17 33.188 8.491 -7.429 1.00 21.21 S ANISOU 155 SG CYS A 17 2040 2739 3277 -964 166 647 S ATOM 156 N VAL A 18 35.424 6.686 -9.458 1.00 17.73 N ANISOU 156 N VAL A 18 1789 2381 2566 -570 193 913 N ATOM 157 CA VAL A 18 36.494 7.216 -10.333 1.00 19.58 C ANISOU 157 CA VAL A 18 2233 2553 2651 -506 186 986 C ATOM 158 C VAL A 18 36.153 8.683 -10.585 1.00 19.79 C ANISOU 158 C VAL A 18 2258 2634 2626 -461 121 976 C ATOM 159 O VAL A 18 34.992 9.015 -10.908 1.00 21.18 O ANISOU 159 O VAL A 18 2370 2792 2886 -437 -98 1095 O ATOM 160 CB VAL A 18 36.536 6.473 -11.673 1.00 19.49 C ANISOU 160 CB VAL A 18 2254 2546 2605 -507 331 1051 C ATOM 161 CG1 VAL A 18 37.559 7.092 -12.642 1.00 21.84 C ANISOU 161 CG1 VAL A 18 2569 2923 2806 -775 423 979 C ATOM 162 CG2 VAL A 18 36.875 5.024 -11.471 1.00 20.48 C ANISOU 162 CG2 VAL A 18 2550 2742 2486 -374 358 1290 C ATOM 163 N GLY A 19 37.104 9.574 -10.355 1.00 18.87 N ANISOU 163 N GLY A 19 2296 2605 2268 -414 191 833 N ATOM 164 CA GLY A 19 36.861 10.956 -10.709 1.00 19.42 C ANISOU 164 CA GLY A 19 2359 2675 2343 -423 88 581 C ATOM 165 C GLY A 19 37.580 11.943 -9.827 1.00 19.36 C ANISOU 165 C GLY A 19 2412 2717 2224 -396 76 470 C ATOM 166 O GLY A 19 38.387 11.558 -8.978 1.00 19.91 O ANISOU 166 O GLY A 19 2475 2891 2199 -377 1 429 O ATOM 167 N ASP A 20 37.294 13.217 -10.080 1.00 19.50 N ANISOU 167 N ASP A 20 2426 2686 2296 -461 93 347 N ATOM 168 CA ASP A 20 37.824 14.334 -9.322 1.00 19.20 C ANISOU 168 CA ASP A 20 2382 2611 2300 -502 -10 278 C ATOM 169 C ASP A 20 37.347 14.223 -7.897 1.00 18.89 C ANISOU 169 C ASP A 20 2372 2472 2331 -512 -91 207 C ATOM 170 O ASP A 20 36.279 13.643 -7.645 1.00 18.87 O ANISOU 170 O ASP A 20 2398 2391 2377 -436 -37 197 O ATOM 171 CB ASP A 20 37.296 15.632 -9.914 1.00 19.67 C ANISOU 171 CB ASP A 20 2455 2703 2316 -568 85 348 C ATOM 172 CG ASP A 20 37.850 15.910 -11.286 1.00 22.03 C ANISOU 172 CG ASP A 20 2768 3119 2481 -500 -25 348 C ATOM 173 OD1 ASP A 20 37.198 16.673 -12.054 1.00 26.43 O ANISOU 173 OD1 ASP A 20 3776 3351 2914 -717 605 858 O ATOM 174 OD2 ASP A 20 38.914 15.341 -11.610 1.00 24.17 O ANISOU 174 OD2 ASP A 20 2744 3877 2560 -505 118 544 O ATOM 175 N LEU A 21 38.085 14.836 -6.968 1.00 18.25 N ANISOU 175 N LEU A 21 2189 2423 2321 -583 -223 224 N ATOM 176 CA LEU A 21 37.682 14.773 -5.565 1.00 17.24 C ANISOU 176 CA LEU A 21 2019 2282 2247 -708 -242 134 C ATOM 177 C LEU A 21 36.211 15.161 -5.320 1.00 16.35 C ANISOU 177 C LEU A 21 1849 2063 2299 -815 -346 147 C ATOM 178 O LEU A 21 35.511 14.510 -4.549 1.00 15.63 O ANISOU 178 O LEU A 21 1831 2103 2005 -603 -218 242 O ATOM 179 CB LEU A 21 38.582 15.659 -4.708 1.00 17.30 C ANISOU 179 CB LEU A 21 1796 2433 2341 -801 -309 130 C ATOM 180 CG LEU A 21 38.338 15.499 -3.204 1.00 17.00 C ANISOU 180 CG LEU A 21 1849 2449 2159 -696 -171 193 C ATOM 181 CD1 LEU A 21 38.874 14.167 -2.642 1.00 14.83 C ANISOU 181 CD1 LEU A 21 1676 1667 2291 -616 -463 139 C ATOM 182 CD2 LEU A 21 38.894 16.633 -2.438 1.00 13.53 C ANISOU 182 CD2 LEU A 21 1084 1885 2168 -1096 -392 -48 C ATOM 183 N ALA A 22 35.744 16.212 -5.984 1.00 16.22 N ANISOU 183 N ALA A 22 1827 1999 2336 -925 -326 189 N ATOM 184 CA ALA A 22 34.396 16.717 -5.773 1.00 16.84 C ANISOU 184 CA ALA A 22 1864 1900 2632 -1047 -352 178 C ATOM 185 C ALA A 22 33.330 15.660 -6.070 1.00 17.31 C ANISOU 185 C ALA A 22 1915 1944 2719 -1057 -335 144 C ATOM 186 O ALA A 22 32.320 15.571 -5.358 1.00 18.42 O ANISOU 186 O ALA A 22 2157 1942 2896 -1188 -239 216 O ATOM 187 CB ALA A 22 34.159 17.963 -6.604 1.00 16.59 C ANISOU 187 CB ALA A 22 1925 1854 2521 -967 -475 217 C ATOM 188 N VAL A 23 33.552 14.903 -7.139 1.00 16.85 N ANISOU 188 N VAL A 23 1757 1921 2722 -1056 -303 198 N ATOM 189 CA VAL A 23 32.716 13.768 -7.530 1.00 16.89 C ANISOU 189 CA VAL A 23 1684 2023 2707 -1142 -399 183 C ATOM 190 C VAL A 23 32.668 12.695 -6.442 1.00 16.20 C ANISOU 190 C VAL A 23 1617 1948 2590 -1120 -407 120 C ATOM 191 O VAL A 23 31.598 12.140 -6.102 1.00 15.12 O ANISOU 191 O VAL A 23 1321 1939 2483 -1340 -200 143 O ATOM 192 CB VAL A 23 33.217 13.191 -8.876 1.00 17.51 C ANISOU 192 CB VAL A 23 1840 2052 2760 -1142 -369 260 C ATOM 193 CG1 VAL A 23 32.427 12.010 -9.333 1.00 20.37 C ANISOU 193 CG1 VAL A 23 2154 2774 2809 -1079 -439 198 C ATOM 194 CG2 VAL A 23 33.212 14.298 -9.971 1.00 19.39 C ANISOU 194 CG2 VAL A 23 2219 2415 2732 -1047 -397 394 C ATOM 195 N VAL A 24 33.840 12.373 -5.926 1.00 15.55 N ANISOU 195 N VAL A 24 1536 1759 2612 -1089 -370 78 N ATOM 196 CA VAL A 24 34.011 11.365 -4.892 1.00 16.72 C ANISOU 196 CA VAL A 24 1792 1859 2699 -874 -428 0 C ATOM 197 C VAL A 24 33.271 11.768 -3.605 1.00 16.87 C ANISOU 197 C VAL A 24 1722 1858 2830 -823 -400 6 C ATOM 198 O VAL A 24 32.522 10.986 -3.077 1.00 17.95 O ANISOU 198 O VAL A 24 2095 1744 2978 -803 -488 89 O ATOM 199 CB VAL A 24 35.520 11.118 -4.620 1.00 16.03 C ANISOU 199 CB VAL A 24 1700 1691 2696 -815 -417 0 C ATOM 200 CG1 VAL A 24 35.707 10.198 -3.419 1.00 15.73 C ANISOU 200 CG1 VAL A 24 1848 1746 2382 -861 -311 88 C ATOM 201 CG2 VAL A 24 36.208 10.557 -5.874 1.00 15.86 C ANISOU 201 CG2 VAL A 24 1425 1986 2614 -807 -219 102 C ATOM 202 N ILE A 25 33.482 13.004 -3.138 1.00 17.07 N ANISOU 202 N ILE A 25 1762 1957 2765 -761 -454 -157 N ATOM 203 CA ILE A 25 32.810 13.544 -1.948 1.00 16.58 C ANISOU 203 CA ILE A 25 1558 1932 2808 -859 -294 -174 C ATOM 204 C ILE A 25 31.311 13.629 -2.165 1.00 16.01 C ANISOU 204 C ILE A 25 1595 1769 2717 -920 -351 -234 C ATOM 205 O ILE A 25 30.505 13.357 -1.237 1.00 14.89 O ANISOU 205 O ILE A 25 1421 1754 2482 -1049 -328 -325 O ATOM 206 CB ILE A 25 33.353 14.950 -1.584 1.00 16.91 C ANISOU 206 CB ILE A 25 1484 2000 2941 -897 -329 -291 C ATOM 207 CG1 ILE A 25 34.887 14.926 -1.368 1.00 19.15 C ANISOU 207 CG1 ILE A 25 1780 2460 3035 -873 -14 49 C ATOM 208 CG2 ILE A 25 32.572 15.567 -0.370 1.00 16.12 C ANISOU 208 CG2 ILE A 25 1063 2076 2986 -1019 -216 -312 C ATOM 209 CD1 ILE A 25 35.440 14.168 -0.196 1.00 19.53 C ANISOU 209 CD1 ILE A 25 1243 2648 3528 -899 -173 -407 C ATOM 210 N ALA A 26 30.917 13.990 -3.385 1.00 15.40 N ANISOU 210 N ALA A 26 1532 1643 2673 -923 -325 -224 N ATOM 211 CA ALA A 26 29.496 14.052 -3.684 1.00 14.99 C ANISOU 211 CA ALA A 26 1395 1519 2780 -1146 -236 -158 C ATOM 212 C ALA A 26 28.833 12.675 -3.462 1.00 16.16 C ANISOU 212 C ALA A 26 1601 1604 2933 -1070 -214 -141 C ATOM 213 O ALA A 26 27.774 12.605 -2.808 1.00 17.05 O ANISOU 213 O ALA A 26 1586 1835 3057 -1107 -55 59 O ATOM 214 CB ALA A 26 29.262 14.557 -5.075 1.00 15.04 C ANISOU 214 CB ALA A 26 1279 1572 2862 -1088 -267 -205 C ATOM 215 N LYS A 27 29.461 11.608 -3.979 1.00 16.07 N ANISOU 215 N LYS A 27 1743 1491 2871 -1248 -247 -145 N ATOM 216 CA LYS A 27 29.002 10.239 -3.707 1.00 16.09 C ANISOU 216 CA LYS A 27 1843 1442 2827 -1141 -313 -225 C ATOM 217 C LYS A 27 28.966 9.890 -2.218 1.00 15.58 C ANISOU 217 C LYS A 27 1749 1431 2738 -1136 -282 -148 C ATOM 218 O LYS A 27 27.941 9.418 -1.696 1.00 15.25 O ANISOU 218 O LYS A 27 1452 1601 2741 -1198 -290 -310 O ATOM 219 CB LYS A 27 29.889 9.245 -4.450 1.00 16.94 C ANISOU 219 CB LYS A 27 1948 1619 2868 -1128 -238 -225 C ATOM 220 CG LYS A 27 29.419 7.812 -4.360 1.00 16.87 C ANISOU 220 CG LYS A 27 2098 1231 3078 -1309 -186 -235 C ATOM 221 CD LYS A 27 30.097 7.044 -5.436 1.00 20.19 C ANISOU 221 CD LYS A 27 2225 1629 3816 -1639 506 -209 C ATOM 222 CE LYS A 27 30.153 5.566 -5.168 1.00 24.01 C ANISOU 222 CE LYS A 27 2214 2215 4694 -1933 625 -128 C ATOM 223 NZ LYS A 27 28.835 4.899 -5.166 1.00 26.01 N ANISOU 223 NZ LYS A 27 2820 2462 4599 -2242 -111 -660 N ATOM 224 N ALA A 28 30.092 10.122 -1.541 1.00 15.02 N ANISOU 224 N ALA A 28 1660 1519 2526 -1120 -312 -129 N ATOM 225 CA ALA A 28 30.239 9.836 -0.108 1.00 14.75 C ANISOU 225 CA ALA A 28 1665 1490 2446 -1166 -270 195 C ATOM 226 C ALA A 28 29.221 10.556 0.804 1.00 14.74 C ANISOU 226 C ALA A 28 1613 1579 2406 -1223 -218 228 C ATOM 227 O ALA A 28 28.764 9.966 1.772 1.00 14.35 O ANISOU 227 O ALA A 28 1544 1663 2243 -1279 -179 371 O ATOM 228 CB ALA A 28 31.663 10.172 0.353 1.00 13.80 C ANISOU 228 CB ALA A 28 1535 1272 2434 -1136 -348 149 C ATOM 229 N LEU A 29 28.897 11.825 0.519 1.00 14.97 N ANISOU 229 N LEU A 29 1749 1586 2351 -1264 -175 168 N ATOM 230 CA LEU A 29 27.973 12.588 1.333 1.00 15.61 C ANISOU 230 CA LEU A 29 1521 1782 2627 -1355 -65 264 C ATOM 231 C LEU A 29 26.551 12.068 1.182 1.00 17.21 C ANISOU 231 C LEU A 29 1702 1990 2845 -1315 -119 139 C ATOM 232 O LEU A 29 25.791 12.104 2.153 1.00 17.00 O ANISOU 232 O LEU A 29 1419 2146 2893 -1456 219 159 O ATOM 233 CB LEU A 29 28.034 14.105 1.053 1.00 15.94 C ANISOU 233 CB LEU A 29 1789 1654 2614 -1297 -117 126 C ATOM 234 CG LEU A 29 29.237 14.892 1.640 1.00 15.38 C ANISOU 234 CG LEU A 29 1699 1694 2449 -1432 -40 262 C ATOM 235 CD1 LEU A 29 29.376 16.338 1.079 1.00 15.05 C ANISOU 235 CD1 LEU A 29 2088 1317 2310 -935 73 259 C ATOM 236 CD2 LEU A 29 29.178 14.945 3.158 1.00 16.66 C ANISOU 236 CD2 LEU A 29 1906 1999 2425 -1641 206 295 C ATOM 237 N ASP A 30 26.217 11.570 -0.008 1.00 18.26 N ANISOU 237 N ASP A 30 1629 2205 3104 -1283 -150 189 N ATOM 238 CA ASP A 30 24.951 10.906 -0.218 1.00 18.82 C ANISOU 238 CA ASP A 30 1620 2278 3253 -1472 -178 336 C ATOM 239 C ASP A 30 24.860 9.464 0.328 1.00 20.72 C ANISOU 239 C ASP A 30 1836 2524 3510 -1415 -206 406 C ATOM 240 O ASP A 30 23.771 9.057 0.817 1.00 20.62 O ANISOU 240 O ASP A 30 1799 2485 3548 -1452 -220 602 O ATOM 241 CB ASP A 30 24.534 10.895 -1.686 1.00 18.89 C ANISOU 241 CB ASP A 30 1435 2387 3352 -1475 -180 272 C ATOM 242 CG ASP A 30 23.106 10.385 -1.845 1.00 20.87 C ANISOU 242 CG ASP A 30 2055 2389 3484 -1634 -329 57 C ATOM 243 OD1 ASP A 30 22.220 11.010 -1.225 1.00 19.06 O ANISOU 243 OD1 ASP A 30 1613 2338 3291 -1683 -300 287 O ATOM 244 OD2 ASP A 30 22.875 9.347 -2.520 1.00 24.94 O ANISOU 244 OD2 ASP A 30 3302 2577 3594 -1653 -353 -366 O ATOM 245 N GLU A 31 25.958 8.700 0.225 1.00 20.67 N ANISOU 245 N GLU A 31 1788 2582 3484 -1464 -250 499 N ATOM 246 CA GLU A 31 25.951 7.314 0.732 1.00 22.18 C ANISOU 246 CA GLU A 31 1987 2752 3686 -1630 -123 662 C ATOM 247 C GLU A 31 26.249 7.217 2.223 1.00 22.12 C ANISOU 247 C GLU A 31 2073 2704 3627 -1554 -91 789 C ATOM 248 O GLU A 31 25.741 6.335 2.870 1.00 20.61 O ANISOU 248 O GLU A 31 1729 2539 3561 -1746 -102 970 O ATOM 249 CB GLU A 31 26.950 6.381 0.025 1.00 22.56 C ANISOU 249 CB GLU A 31 2053 2792 3725 -1775 35 716 C ATOM 250 CG GLU A 31 27.213 6.678 -1.377 1.00 26.22 C ANISOU 250 CG GLU A 31 2094 3354 4515 -2320 234 568 C ATOM 251 CD GLU A 31 26.560 5.786 -2.344 1.00 33.34 C ANISOU 251 CD GLU A 31 3088 4274 5304 -2381 637 517 C ATOM 252 OE1 GLU A 31 25.822 4.858 -1.927 1.00 33.76 O ANISOU 252 OE1 GLU A 31 2574 4625 5628 -2883 1096 597 O ATOM 253 OE2 GLU A 31 26.790 6.055 -3.543 1.00 33.95 O ANISOU 253 OE2 GLU A 31 2861 4520 5517 -3068 1160 403 O ATOM 254 N PHE A 32 27.100 8.092 2.751 1.00 21.22 N ANISOU 254 N PHE A 32 1925 2573 3563 -1589 -79 848 N ATOM 255 CA PHE A 32 27.524 7.964 4.134 1.00 22.57 C ANISOU 255 CA PHE A 32 2351 2646 3575 -1513 111 882 C ATOM 256 C PHE A 32 26.883 9.080 4.957 1.00 24.31 C ANISOU 256 C PHE A 32 2578 2830 3826 -1454 180 851 C ATOM 257 O PHE A 32 26.858 10.238 4.531 1.00 23.43 O ANISOU 257 O PHE A 32 2586 2539 3776 -1712 372 1106 O ATOM 258 CB PHE A 32 29.067 7.984 4.239 1.00 21.60 C ANISOU 258 CB PHE A 32 2287 2494 3423 -1539 17 899 C ATOM 259 CG PHE A 32 29.765 6.807 3.560 1.00 21.35 C ANISOU 259 CG PHE A 32 2410 2650 3051 -1645 76 981 C ATOM 260 CD1 PHE A 32 29.146 5.570 3.466 1.00 22.90 C ANISOU 260 CD1 PHE A 32 3254 2597 2849 -1475 62 961 C ATOM 261 CD2 PHE A 32 31.064 6.932 3.051 1.00 23.46 C ANISOU 261 CD2 PHE A 32 3013 2929 2969 -1338 103 865 C ATOM 262 CE1 PHE A 32 29.784 4.473 2.858 1.00 23.07 C ANISOU 262 CE1 PHE A 32 3071 2515 3177 -1471 237 1153 C ATOM 263 CE2 PHE A 32 31.719 5.824 2.455 1.00 22.21 C ANISOU 263 CE2 PHE A 32 2890 2296 3249 -1779 331 934 C ATOM 264 CZ PHE A 32 31.050 4.592 2.354 1.00 23.30 C ANISOU 264 CZ PHE A 32 2836 2678 3336 -1402 82 1103 C ATOM 265 N LYS A 33 26.309 8.770 6.124 1.00 25.34 N ANISOU 265 N LYS A 33 2770 2911 3944 -1410 244 764 N ATOM 266 CA LYS A 33 25.786 9.880 6.943 1.00 27.31 C ANISOU 266 CA LYS A 33 2889 3185 4300 -1216 225 559 C ATOM 267 C LYS A 33 26.962 10.807 7.270 1.00 26.97 C ANISOU 267 C LYS A 33 2845 3057 4345 -1160 188 555 C ATOM 268 O LYS A 33 26.908 12.039 7.117 1.00 28.16 O ANISOU 268 O LYS A 33 2880 3230 4588 -1077 227 585 O ATOM 269 CB LYS A 33 25.127 9.367 8.241 1.00 29.04 C ANISOU 269 CB LYS A 33 3188 3378 4469 -1174 211 430 C ATOM 270 CG LYS A 33 24.891 10.470 9.321 1.00 32.28 C ANISOU 270 CG LYS A 33 3454 3826 4984 -985 164 262 C ATOM 271 CD LYS A 33 23.710 11.413 8.982 1.00 34.76 C ANISOU 271 CD LYS A 33 3784 3904 5517 -1193 388 105 C ATOM 272 CE LYS A 33 23.342 12.307 10.173 1.00 32.65 C ANISOU 272 CE LYS A 33 3521 3522 5361 -1687 373 118 C ATOM 273 NZ LYS A 33 24.279 13.467 10.323 1.00 31.83 N ANISOU 273 NZ LYS A 33 2620 3506 5966 -2693 652 280 N ATOM 274 N GLU A 34 28.029 10.191 7.741 1.00 25.65 N ANISOU 274 N GLU A 34 2604 2938 4204 -1085 162 475 N ATOM 275 CA GLU A 34 29.259 10.902 8.047 1.00 24.08 C ANISOU 275 CA GLU A 34 2511 2691 3945 -1101 75 313 C ATOM 276 C GLU A 34 30.360 9.900 7.784 1.00 21.95 C ANISOU 276 C GLU A 34 2252 2492 3592 -1117 4 266 C ATOM 277 O GLU A 34 30.107 8.671 7.751 1.00 20.90 O ANISOU 277 O GLU A 34 2019 2336 3584 -1148 -159 199 O ATOM 278 CB GLU A 34 29.274 11.413 9.501 1.00 25.50 C ANISOU 278 CB GLU A 34 2761 2810 4117 -1038 117 351 C ATOM 279 CG GLU A 34 29.218 10.317 10.573 1.00 29.42 C ANISOU 279 CG GLU A 34 2997 3412 4769 -1017 468 211 C ATOM 280 CD GLU A 34 27.929 10.292 11.407 1.00 36.21 C ANISOU 280 CD GLU A 34 3996 3989 5773 -1017 705 -77 C ATOM 281 OE1 GLU A 34 27.381 9.184 11.596 1.00 36.33 O ANISOU 281 OE1 GLU A 34 3671 4346 5784 -1442 1146 97 O ATOM 282 OE2 GLU A 34 27.490 11.358 11.906 1.00 39.65 O ANISOU 282 OE2 GLU A 34 4532 4444 6089 -527 568 -294 O ATOM 283 N PHE A 35 31.561 10.423 7.561 1.00 20.12 N ANISOU 283 N PHE A 35 2119 2283 3242 -1121 -70 143 N ATOM 284 CA PHE A 35 32.708 9.621 7.183 1.00 18.64 C ANISOU 284 CA PHE A 35 1979 2159 2942 -1231 -52 186 C ATOM 285 C PHE A 35 34.016 10.302 7.473 1.00 17.39 C ANISOU 285 C PHE A 35 1808 2053 2743 -1342 18 243 C ATOM 286 O PHE A 35 34.090 11.541 7.637 1.00 16.21 O ANISOU 286 O PHE A 35 1690 1884 2583 -1421 182 540 O ATOM 287 CB PHE A 35 32.688 9.223 5.703 1.00 17.92 C ANISOU 287 CB PHE A 35 1951 2082 2775 -1270 -109 38 C ATOM 288 CG PHE A 35 32.678 10.373 4.752 1.00 16.50 C ANISOU 288 CG PHE A 35 1756 1784 2727 -1517 -25 11 C ATOM 289 CD1 PHE A 35 33.880 10.885 4.206 1.00 15.76 C ANISOU 289 CD1 PHE A 35 1925 1958 2105 -1316 87 -51 C ATOM 290 CD2 PHE A 35 31.480 10.968 4.397 1.00 15.87 C ANISOU 290 CD2 PHE A 35 1699 1636 2694 -1414 85 -84 C ATOM 291 CE1 PHE A 35 33.850 11.954 3.327 1.00 16.73 C ANISOU 291 CE1 PHE A 35 1952 1955 2448 -1367 179 -308 C ATOM 292 CE2 PHE A 35 31.442 12.037 3.508 1.00 17.27 C ANISOU 292 CE2 PHE A 35 1931 1994 2635 -1230 465 -83 C ATOM 293 CZ PHE A 35 32.619 12.525 2.961 1.00 17.77 C ANISOU 293 CZ PHE A 35 2016 2029 2706 -1352 215 -275 C ATOM 294 N CYS A 36 35.037 9.462 7.561 1.00 16.44 N ANISOU 294 N CYS A 36 1675 2009 2560 -1352 12 294 N ATOM 295 CA CYS A 36 36.430 9.910 7.564 1.00 16.14 C ANISOU 295 CA CYS A 36 1710 1872 2551 -1491 82 376 C ATOM 296 C CYS A 36 36.983 9.901 6.144 1.00 15.90 C ANISOU 296 C CYS A 36 1800 1809 2431 -1470 176 322 C ATOM 297 O CYS A 36 36.840 8.907 5.398 1.00 17.18 O ANISOU 297 O CYS A 36 2099 1883 2545 -1598 286 494 O ATOM 298 CB CYS A 36 37.282 8.997 8.428 1.00 15.72 C ANISOU 298 CB CYS A 36 1520 1929 2522 -1444 -18 280 C ATOM 299 SG CYS A 36 39.074 9.267 8.243 1.00 17.34 S ANISOU 299 SG CYS A 36 1532 2372 2681 -1602 -47 577 S ATOM 300 N ILE A 37 37.629 11.000 5.747 1.00 15.73 N ANISOU 300 N ILE A 37 1914 1668 2395 -1440 231 389 N ATOM 301 CA ILE A 37 38.407 10.971 4.489 1.00 15.45 C ANISOU 301 CA ILE A 37 1888 1646 2334 -1377 168 362 C ATOM 302 C ILE A 37 39.930 10.784 4.722 1.00 15.34 C ANISOU 302 C ILE A 37 1787 1690 2351 -1422 129 376 C ATOM 303 O ILE A 37 40.553 11.517 5.534 1.00 16.01 O ANISOU 303 O ILE A 37 1776 1862 2443 -1410 109 299 O ATOM 304 CB ILE A 37 38.124 12.152 3.556 1.00 15.59 C ANISOU 304 CB ILE A 37 1939 1693 2292 -1443 293 386 C ATOM 305 CG1 ILE A 37 38.667 11.802 2.152 1.00 18.60 C ANISOU 305 CG1 ILE A 37 2457 1947 2660 -1408 132 431 C ATOM 306 CG2 ILE A 37 38.721 13.502 4.156 1.00 15.53 C ANISOU 306 CG2 ILE A 37 2213 1510 2176 -1378 310 328 C ATOM 307 CD1 ILE A 37 38.607 12.922 1.132 1.00 22.15 C ANISOU 307 CD1 ILE A 37 2560 2811 3045 -1109 -159 837 C ATOM 308 N VAL A 38 40.505 9.801 4.028 1.00 14.52 N ANISOU 308 N VAL A 38 1646 1564 2307 -1309 0 405 N ATOM 309 CA VAL A 38 41.913 9.471 4.180 1.00 14.52 C ANISOU 309 CA VAL A 38 1611 1582 2321 -1306 -37 419 C ATOM 310 C VAL A 38 42.726 10.333 3.214 1.00 14.63 C ANISOU 310 C VAL A 38 1520 1762 2274 -1318 -58 483 C ATOM 311 O VAL A 38 42.492 10.383 2.012 1.00 14.50 O ANISOU 311 O VAL A 38 1440 1792 2277 -1348 -267 414 O ATOM 312 CB VAL A 38 42.235 7.980 3.978 1.00 14.38 C ANISOU 312 CB VAL A 38 1647 1628 2187 -1140 -69 479 C ATOM 313 CG1 VAL A 38 43.731 7.727 4.037 1.00 14.31 C ANISOU 313 CG1 VAL A 38 1781 1381 2273 -1211 83 514 C ATOM 314 CG2 VAL A 38 41.517 7.124 5.047 1.00 14.84 C ANISOU 314 CG2 VAL A 38 1862 1505 2271 -1413 -111 240 C ATOM 315 N ASN A 39 43.710 11.014 3.774 1.00 15.44 N ANISOU 315 N ASN A 39 1565 1925 2377 -1391 -87 441 N ATOM 316 CA ASN A 39 44.595 11.775 2.922 1.00 15.60 C ANISOU 316 CA ASN A 39 1554 2032 2341 -1368 25 528 C ATOM 317 C ASN A 39 45.961 11.079 2.783 1.00 16.82 C ANISOU 317 C ASN A 39 1714 2315 2361 -1237 135 514 C ATOM 318 O ASN A 39 46.509 10.567 3.758 1.00 16.27 O ANISOU 318 O ASN A 39 1453 2256 2473 -1298 125 708 O ATOM 319 CB ASN A 39 44.724 13.193 3.492 1.00 16.19 C ANISOU 319 CB ASN A 39 1879 1925 2346 -1303 -66 468 C ATOM 320 CG ASN A 39 45.620 14.094 2.647 1.00 15.95 C ANISOU 320 CG ASN A 39 1644 1985 2431 -1524 82 275 C ATOM 321 OD1 ASN A 39 45.880 13.843 1.467 1.00 17.06 O ANISOU 321 OD1 ASN A 39 1434 2331 2716 -1550 135 144 O ATOM 322 ND2 ASN A 39 46.056 15.181 3.249 1.00 18.78 N ANISOU 322 ND2 ASN A 39 2566 1925 2643 -1965 -251 269 N ATOM 323 N ALA A 40 46.482 11.086 1.549 1.00 17.39 N ANISOU 323 N ALA A 40 1681 2505 2420 -1180 280 388 N ATOM 324 CA ALA A 40 47.751 10.463 1.173 1.00 17.52 C ANISOU 324 CA ALA A 40 1732 2487 2435 -1306 271 291 C ATOM 325 C ALA A 40 48.807 11.540 1.355 1.00 17.68 C ANISOU 325 C ALA A 40 1816 2503 2399 -1275 242 145 C ATOM 326 O ALA A 40 49.218 12.178 0.393 1.00 17.55 O ANISOU 326 O ALA A 40 2121 2235 2313 -1272 246 104 O ATOM 327 CB ALA A 40 47.697 10.002 -0.302 1.00 17.28 C ANISOU 327 CB ALA A 40 1572 2521 2470 -1374 268 187 C ATOM 328 N ALA A 41 49.226 11.702 2.604 1.00 17.75 N ANISOU 328 N ALA A 41 1772 2609 2363 -1264 247 86 N ATOM 329 CA ALA A 41 49.993 12.821 3.081 1.00 18.47 C ANISOU 329 CA ALA A 41 1742 2824 2452 -1204 214 -9 C ATOM 330 C ALA A 41 51.489 12.557 3.042 1.00 18.48 C ANISOU 330 C ALA A 41 1622 2864 2534 -1268 235 -45 C ATOM 331 O ALA A 41 51.953 11.413 2.813 1.00 17.67 O ANISOU 331 O ALA A 41 1327 2988 2396 -1276 198 -82 O ATOM 332 CB ALA A 41 49.572 13.132 4.515 1.00 18.64 C ANISOU 332 CB ALA A 41 1812 2856 2412 -1227 177 -120 C ATOM 333 N ASN A 42 52.238 13.625 3.308 1.00 19.44 N ANISOU 333 N ASN A 42 1807 2929 2649 -1246 284 -8 N ATOM 334 CA ASN A 42 53.640 13.510 3.665 1.00 19.74 C ANISOU 334 CA ASN A 42 1795 2993 2713 -1229 213 -4 C ATOM 335 C ASN A 42 53.835 13.874 5.154 1.00 20.43 C ANISOU 335 C ASN A 42 1865 3007 2889 -1288 226 -39 C ATOM 336 O ASN A 42 52.902 14.361 5.807 1.00 19.22 O ANISOU 336 O ASN A 42 1648 2779 2872 -1577 180 -88 O ATOM 337 CB ASN A 42 54.567 14.325 2.717 1.00 20.31 C ANISOU 337 CB ASN A 42 1979 2989 2746 -1208 332 27 C ATOM 338 CG ASN A 42 54.310 15.826 2.733 1.00 21.42 C ANISOU 338 CG ASN A 42 2127 3395 2617 -884 438 103 C ATOM 339 OD1 ASN A 42 54.189 16.434 3.775 1.00 23.18 O ANISOU 339 OD1 ASN A 42 2765 3268 2773 -901 291 -7 O ATOM 340 ND2 ASN A 42 54.311 16.440 1.553 1.00 24.32 N ANISOU 340 ND2 ASN A 42 2329 3855 3056 -581 468 475 N ATOM 341 N GLU A 43 55.059 13.672 5.669 1.00 21.00 N ANISOU 341 N GLU A 43 1878 3084 3017 -1247 158 -56 N ATOM 342 CA GLU A 43 55.253 13.744 7.100 1.00 21.72 C ANISOU 342 CA GLU A 43 1910 3163 3178 -1264 163 22 C ATOM 343 C GLU A 43 55.254 15.209 7.561 1.00 21.34 C ANISOU 343 C GLU A 43 1855 3071 3181 -1400 254 49 C ATOM 344 O GLU A 43 55.027 15.483 8.738 1.00 20.91 O ANISOU 344 O GLU A 43 1825 2945 3173 -1483 410 130 O ATOM 345 CB GLU A 43 56.509 13.006 7.532 1.00 22.69 C ANISOU 345 CB GLU A 43 2120 3245 3255 -1277 237 23 C ATOM 346 CG GLU A 43 57.753 13.704 7.084 1.00 25.47 C ANISOU 346 CG GLU A 43 2195 3711 3769 -1154 -11 255 C ATOM 347 CD GLU A 43 58.995 13.101 7.668 1.00 30.92 C ANISOU 347 CD GLU A 43 3198 4266 4281 -1165 -14 527 C ATOM 348 OE1 GLU A 43 60.071 13.502 7.220 1.00 28.20 O ANISOU 348 OE1 GLU A 43 1904 4461 4349 -1559 -157 559 O ATOM 349 OE2 GLU A 43 58.893 12.226 8.559 1.00 33.15 O ANISOU 349 OE2 GLU A 43 4151 4369 4073 -1065 44 699 O ATOM 350 N HIS A 44 55.475 16.130 6.622 1.00 20.45 N ANISOU 350 N HIS A 44 1654 3091 3024 -1433 362 197 N ATOM 351 CA HIS A 44 55.368 17.570 6.888 1.00 21.17 C ANISOU 351 CA HIS A 44 1696 3192 3156 -1575 380 196 C ATOM 352 C HIS A 44 53.946 18.102 6.786 1.00 21.52 C ANISOU 352 C HIS A 44 1926 3157 3092 -1540 346 236 C ATOM 353 O HIS A 44 53.687 19.274 7.105 1.00 21.79 O ANISOU 353 O HIS A 44 1996 3152 3130 -1515 451 375 O ATOM 354 CB HIS A 44 56.256 18.398 5.933 1.00 22.23 C ANISOU 354 CB HIS A 44 1874 3314 3258 -1556 413 183 C ATOM 355 CG HIS A 44 57.641 17.866 5.779 1.00 24.22 C ANISOU 355 CG HIS A 44 1680 3667 3854 -1639 166 -45 C ATOM 356 ND1 HIS A 44 58.696 18.296 6.558 1.00 28.75 N ANISOU 356 ND1 HIS A 44 2347 4132 4443 -1552 90 -297 N ATOM 357 CD2 HIS A 44 58.149 16.946 4.926 1.00 24.04 C ANISOU 357 CD2 HIS A 44 1688 3653 3793 -1692 252 -292 C ATOM 358 CE1 HIS A 44 59.794 17.650 6.198 1.00 26.22 C ANISOU 358 CE1 HIS A 44 1864 3896 4202 -1761 337 -337 C ATOM 359 NE2 HIS A 44 59.488 16.826 5.210 1.00 27.67 N ANISOU 359 NE2 HIS A 44 2181 4053 4279 -1598 370 -290 N ATOM 360 N MET A 45 53.018 17.245 6.367 1.00 20.88 N ANISOU 360 N MET A 45 1789 3125 3019 -1651 329 205 N ATOM 361 CA MET A 45 51.616 17.645 6.177 1.00 20.98 C ANISOU 361 CA MET A 45 1855 3093 3022 -1515 227 169 C ATOM 362 C MET A 45 51.561 18.884 5.312 1.00 22.86 C ANISOU 362 C MET A 45 2138 3274 3274 -1380 269 210 C ATOM 363 O MET A 45 50.778 19.793 5.595 1.00 24.57 O ANISOU 363 O MET A 45 2368 3488 3479 -1217 248 176 O ATOM 364 CB MET A 45 50.933 17.910 7.530 1.00 19.49 C ANISOU 364 CB MET A 45 1522 2935 2947 -1723 264 113 C ATOM 365 CG MET A 45 50.929 16.714 8.470 1.00 18.32 C ANISOU 365 CG MET A 45 1526 2817 2617 -1801 -96 -50 C ATOM 366 SD MET A 45 49.668 15.498 7.795 1.00 15.45 S ANISOU 366 SD MET A 45 1627 2205 2037 -1622 146 77 S ATOM 367 CE MET A 45 50.555 14.042 8.211 1.00 17.91 C ANISOU 367 CE MET A 45 1651 3034 2120 -1898 335 146 C ATOM 368 N SER A 46 52.420 18.922 4.283 1.00 22.93 N ANISOU 368 N SER A 46 2145 3205 3359 -1491 294 400 N ATOM 369 CA SER A 46 52.471 19.984 3.289 1.00 24.42 C ANISOU 369 CA SER A 46 2429 3273 3575 -1458 339 488 C ATOM 370 C SER A 46 51.342 20.012 2.219 1.00 23.55 C ANISOU 370 C SER A 46 2522 3046 3378 -1591 382 546 C ATOM 371 O SER A 46 50.843 21.063 1.885 1.00 25.32 O ANISOU 371 O SER A 46 2796 3218 3606 -1594 464 599 O ATOM 372 CB SER A 46 53.865 19.999 2.644 1.00 24.70 C ANISOU 372 CB SER A 46 2451 3201 3731 -1584 393 650 C ATOM 373 OG SER A 46 54.159 21.267 2.094 1.00 30.84 O ANISOU 373 OG SER A 46 3113 4022 4583 -1065 146 580 O ATOM 374 N HIS A 47 50.883 18.890 1.689 1.00 23.63 N ANISOU 374 N HIS A 47 2634 3132 3213 -1579 308 544 N ATOM 375 CA HIS A 47 49.723 18.945 0.768 1.00 21.42 C ANISOU 375 CA HIS A 47 2221 2951 2965 -1632 262 486 C ATOM 376 C HIS A 47 49.989 19.826 -0.477 1.00 21.00 C ANISOU 376 C HIS A 47 2108 2992 2878 -1651 384 560 C ATOM 377 O HIS A 47 49.092 20.531 -0.976 1.00 21.56 O ANISOU 377 O HIS A 47 2185 3116 2892 -1562 394 517 O ATOM 378 CB HIS A 47 48.438 19.434 1.467 1.00 20.73 C ANISOU 378 CB HIS A 47 2164 2840 2872 -1672 224 455 C ATOM 379 CG HIS A 47 48.242 18.894 2.855 1.00 20.66 C ANISOU 379 CG HIS A 47 1905 3099 2846 -1599 176 256 C ATOM 380 ND1 HIS A 47 48.460 17.572 3.182 1.00 19.79 N ANISOU 380 ND1 HIS A 47 2019 2817 2682 -2034 270 414 N ATOM 381 CD2 HIS A 47 47.892 19.512 4.006 1.00 19.88 C ANISOU 381 CD2 HIS A 47 1815 3060 2677 -1636 92 27 C ATOM 382 CE1 HIS A 47 48.267 17.404 4.476 1.00 18.17 C ANISOU 382 CE1 HIS A 47 1930 2679 2293 -2016 67 -41 C ATOM 383 NE2 HIS A 47 47.885 18.556 4.994 1.00 18.64 N ANISOU 383 NE2 HIS A 47 1964 2518 2600 -1963 9 161 N ATOM 384 N GLY A 48 51.205 19.769 -0.994 1.00 21.41 N ANISOU 384 N GLY A 48 2145 3120 2870 -1626 288 525 N ATOM 385 CA GLY A 48 51.561 20.607 -2.144 1.00 20.12 C ANISOU 385 CA GLY A 48 1743 3146 2755 -1818 474 678 C ATOM 386 C GLY A 48 51.143 20.007 -3.479 1.00 20.22 C ANISOU 386 C GLY A 48 1710 3185 2784 -1787 416 728 C ATOM 387 O GLY A 48 51.044 20.746 -4.469 1.00 20.67 O ANISOU 387 O GLY A 48 1570 3385 2895 -1872 223 788 O ATOM 388 N GLY A 49 50.907 18.682 -3.530 1.00 19.80 N ANISOU 388 N GLY A 49 1743 3070 2708 -1752 517 704 N ATOM 389 CA GLY A 49 50.607 17.985 -4.794 1.00 19.49 C ANISOU 389 CA GLY A 49 1869 2778 2756 -1743 568 604 C ATOM 390 C GLY A 49 49.583 16.870 -4.642 1.00 20.21 C ANISOU 390 C GLY A 49 2013 2841 2823 -1549 518 534 C ATOM 391 O GLY A 49 49.279 16.482 -3.526 1.00 19.40 O ANISOU 391 O GLY A 49 1845 2763 2763 -1673 644 622 O ATOM 392 N GLY A 50 49.064 16.390 -5.782 1.00 19.56 N ANISOU 392 N GLY A 50 2036 2605 2789 -1637 544 511 N ATOM 393 CA GLY A 50 48.250 15.206 -5.872 1.00 19.62 C ANISOU 393 CA GLY A 50 2278 2392 2782 -1498 492 429 C ATOM 394 C GLY A 50 46.957 15.328 -5.117 1.00 18.57 C ANISOU 394 C GLY A 50 2189 2133 2731 -1446 470 428 C ATOM 395 O GLY A 50 46.412 16.431 -4.941 1.00 19.35 O ANISOU 395 O GLY A 50 2483 2124 2743 -1507 436 515 O ATOM 396 N VAL A 51 46.455 14.193 -4.645 1.00 17.16 N ANISOU 396 N VAL A 51 1987 1868 2665 -1492 360 391 N ATOM 397 CA VAL A 51 45.273 14.211 -3.843 1.00 17.07 C ANISOU 397 CA VAL A 51 1907 1913 2665 -1373 373 284 C ATOM 398 C VAL A 51 45.347 15.007 -2.525 1.00 16.48 C ANISOU 398 C VAL A 51 1732 1838 2689 -1348 330 301 C ATOM 399 O VAL A 51 44.353 15.561 -2.109 1.00 17.33 O ANISOU 399 O VAL A 51 1904 1842 2839 -1195 251 164 O ATOM 400 CB VAL A 51 44.795 12.770 -3.573 1.00 16.88 C ANISOU 400 CB VAL A 51 1921 1767 2723 -1439 424 436 C ATOM 401 CG1 VAL A 51 45.778 12.081 -2.616 1.00 17.70 C ANISOU 401 CG1 VAL A 51 2015 2037 2673 -1384 169 304 C ATOM 402 CG2 VAL A 51 43.368 12.772 -3.040 1.00 16.97 C ANISOU 402 CG2 VAL A 51 1655 2187 2605 -1185 236 219 C ATOM 403 N ALA A 52 46.495 15.055 -1.862 1.00 16.52 N ANISOU 403 N ALA A 52 1732 1969 2575 -1165 322 328 N ATOM 404 CA ALA A 52 46.675 15.900 -0.677 1.00 14.65 C ANISOU 404 CA ALA A 52 1515 1728 2323 -1185 399 392 C ATOM 405 C ALA A 52 46.372 17.366 -0.958 1.00 15.74 C ANISOU 405 C ALA A 52 1597 2020 2362 -1126 423 432 C ATOM 406 O ALA A 52 45.841 18.070 -0.108 1.00 15.85 O ANISOU 406 O ALA A 52 1652 1922 2446 -1045 419 527 O ATOM 407 CB ALA A 52 48.088 15.742 -0.153 1.00 14.62 C ANISOU 407 CB ALA A 52 1432 1769 2352 -1242 332 293 C ATOM 408 N LYS A 53 46.771 17.829 -2.145 1.00 15.15 N ANISOU 408 N LYS A 53 1480 1989 2284 -1224 413 574 N ATOM 409 CA LYS A 53 46.467 19.170 -2.617 1.00 15.59 C ANISOU 409 CA LYS A 53 1592 1960 2368 -1253 438 553 C ATOM 410 C LYS A 53 44.984 19.379 -2.845 1.00 14.88 C ANISOU 410 C LYS A 53 1525 1940 2187 -1139 488 533 C ATOM 411 O LYS A 53 44.459 20.383 -2.451 1.00 14.17 O ANISOU 411 O LYS A 53 1384 1928 2072 -1056 629 417 O ATOM 412 CB LYS A 53 47.257 19.475 -3.901 1.00 15.77 C ANISOU 412 CB LYS A 53 1618 2019 2353 -1229 487 611 C ATOM 413 CG LYS A 53 46.957 20.891 -4.460 1.00 17.16 C ANISOU 413 CG LYS A 53 1845 2095 2577 -1340 565 755 C ATOM 414 CD LYS A 53 47.616 21.131 -5.824 1.00 18.98 C ANISOU 414 CD LYS A 53 2540 2082 2589 -1223 365 578 C ATOM 415 CE LYS A 53 47.110 22.444 -6.466 1.00 22.80 C ANISOU 415 CE LYS A 53 3332 2277 3053 -1202 430 450 C ATOM 416 NZ LYS A 53 47.000 23.614 -5.525 1.00 27.60 N ANISOU 416 NZ LYS A 53 4416 2322 3747 -1562 475 646 N ATOM 417 N ALA A 54 44.312 18.416 -3.469 1.00 14.81 N ANISOU 417 N ALA A 54 1333 2119 2173 -1206 480 404 N ATOM 418 CA ALA A 54 42.869 18.519 -3.697 1.00 15.77 C ANISOU 418 CA ALA A 54 1531 2246 2214 -1148 403 402 C ATOM 419 C ALA A 54 42.121 18.539 -2.351 1.00 15.82 C ANISOU 419 C ALA A 54 1392 2290 2326 -1187 485 482 C ATOM 420 O ALA A 54 41.109 19.265 -2.187 1.00 16.73 O ANISOU 420 O ALA A 54 1871 2174 2310 -1048 599 508 O ATOM 421 CB ALA A 54 42.405 17.335 -4.528 1.00 15.26 C ANISOU 421 CB ALA A 54 1492 2161 2143 -1355 282 432 C ATOM 422 N ILE A 55 42.602 17.752 -1.385 1.00 15.44 N ANISOU 422 N ILE A 55 1341 2170 2354 -1239 485 406 N ATOM 423 CA ILE A 55 41.889 17.637 -0.086 1.00 15.40 C ANISOU 423 CA ILE A 55 1298 2134 2418 -1256 440 327 C ATOM 424 C ILE A 55 42.121 18.928 0.679 1.00 16.15 C ANISOU 424 C ILE A 55 1309 2247 2578 -1229 461 228 C ATOM 425 O ILE A 55 41.196 19.488 1.248 1.00 17.11 O ANISOU 425 O ILE A 55 1313 2366 2821 -1383 474 232 O ATOM 426 CB ILE A 55 42.337 16.417 0.713 1.00 15.42 C ANISOU 426 CB ILE A 55 1380 2161 2318 -1312 395 205 C ATOM 427 CG1 ILE A 55 41.814 15.137 0.048 1.00 17.89 C ANISOU 427 CG1 ILE A 55 1492 2575 2730 -1175 210 321 C ATOM 428 CG2 ILE A 55 41.878 16.534 2.202 1.00 16.69 C ANISOU 428 CG2 ILE A 55 1485 2291 2563 -1373 572 378 C ATOM 429 CD1 ILE A 55 42.484 13.813 0.470 1.00 14.95 C ANISOU 429 CD1 ILE A 55 1252 1916 2512 -1123 336 548 C ATOM 430 N ALA A 56 43.350 19.444 0.627 1.00 16.51 N ANISOU 430 N ALA A 56 1299 2128 2843 -1308 454 187 N ATOM 431 CA ALA A 56 43.678 20.722 1.302 1.00 16.67 C ANISOU 431 CA ALA A 56 1380 2098 2854 -1131 499 144 C ATOM 432 C ALA A 56 42.869 21.912 0.773 1.00 16.83 C ANISOU 432 C ALA A 56 1373 2093 2926 -1052 524 187 C ATOM 433 O ALA A 56 42.365 22.726 1.561 1.00 15.98 O ANISOU 433 O ALA A 56 1244 1891 2933 -1125 614 214 O ATOM 434 CB ALA A 56 45.201 21.021 1.169 1.00 16.52 C ANISOU 434 CB ALA A 56 1308 2052 2913 -1283 444 228 C ATOM 435 N ASP A 57 42.862 22.070 -0.559 1.00 17.75 N ANISOU 435 N ASP A 57 1487 2139 3117 -944 397 152 N ATOM 436 CA ASP A 57 42.045 23.066 -1.244 1.00 19.96 C ANISOU 436 CA ASP A 57 1797 2481 3304 -923 453 287 C ATOM 437 C ASP A 57 40.555 22.897 -0.875 1.00 20.04 C ANISOU 437 C ASP A 57 1793 2442 3379 -835 471 311 C ATOM 438 O ASP A 57 39.868 23.872 -0.575 1.00 22.47 O ANISOU 438 O ASP A 57 2230 2821 3484 -726 473 288 O ATOM 439 CB ASP A 57 42.258 22.988 -2.763 1.00 20.25 C ANISOU 439 CB ASP A 57 1755 2575 3361 -919 501 342 C ATOM 440 CG ASP A 57 43.668 23.412 -3.200 1.00 23.65 C ANISOU 440 CG ASP A 57 2431 3063 3493 -921 553 383 C ATOM 441 OD1 ASP A 57 44.484 23.817 -2.352 1.00 25.13 O ANISOU 441 OD1 ASP A 57 2411 3467 3667 -1501 746 -30 O ATOM 442 OD2 ASP A 57 43.982 23.315 -4.415 1.00 27.26 O ANISOU 442 OD2 ASP A 57 2862 3593 3900 -1138 1061 1012 O ATOM 443 N PHE A 58 40.069 21.662 -0.862 1.00 19.49 N ANISOU 443 N PHE A 58 1531 2442 3431 -1064 502 319 N ATOM 444 CA PHE A 58 38.672 21.370 -0.482 1.00 18.85 C ANISOU 444 CA PHE A 58 1519 2253 3390 -1099 571 313 C ATOM 445 C PHE A 58 38.343 21.801 0.971 1.00 19.18 C ANISOU 445 C PHE A 58 1699 2054 3533 -1156 480 239 C ATOM 446 O PHE A 58 37.445 22.606 1.194 1.00 19.62 O ANISOU 446 O PHE A 58 1795 2061 3597 -1190 355 141 O ATOM 447 CB PHE A 58 38.371 19.894 -0.710 1.00 18.22 C ANISOU 447 CB PHE A 58 1155 2414 3352 -1179 672 387 C ATOM 448 CG PHE A 58 36.951 19.526 -0.421 1.00 19.80 C ANISOU 448 CG PHE A 58 1338 2787 3399 -1288 726 496 C ATOM 449 CD1 PHE A 58 35.955 19.779 -1.347 1.00 22.02 C ANISOU 449 CD1 PHE A 58 1058 3691 3617 -1270 800 658 C ATOM 450 CD2 PHE A 58 36.617 18.969 0.795 1.00 20.50 C ANISOU 450 CD2 PHE A 58 1543 2864 3381 -1409 948 579 C ATOM 451 CE1 PHE A 58 34.607 19.441 -1.055 1.00 23.08 C ANISOU 451 CE1 PHE A 58 1335 3585 3848 -1485 823 830 C ATOM 452 CE2 PHE A 58 35.284 18.647 1.091 1.00 20.59 C ANISOU 452 CE2 PHE A 58 1092 3098 3631 -1316 595 584 C ATOM 453 CZ PHE A 58 34.301 18.888 0.162 1.00 21.55 C ANISOU 453 CZ PHE A 58 1370 3203 3612 -1364 834 853 C ATOM 454 N CYS A 59 39.087 21.277 1.944 1.00 19.17 N ANISOU 454 N CYS A 59 1995 1743 3542 -1260 444 128 N ATOM 455 CA CYS A 59 38.803 21.495 3.350 1.00 18.79 C ANISOU 455 CA CYS A 59 2009 1583 3547 -1404 569 140 C ATOM 456 C CYS A 59 39.033 22.930 3.757 1.00 19.65 C ANISOU 456 C CYS A 59 2314 1553 3597 -1236 575 111 C ATOM 457 O CYS A 59 38.345 23.438 4.645 1.00 21.53 O ANISOU 457 O CYS A 59 2581 1781 3815 -1301 493 83 O ATOM 458 CB CYS A 59 39.653 20.586 4.205 1.00 18.23 C ANISOU 458 CB CYS A 59 2011 1423 3490 -1367 542 148 C ATOM 459 SG CYS A 59 39.181 18.893 4.056 1.00 19.40 S ANISOU 459 SG CYS A 59 2393 1679 3299 -1517 495 75 S ATOM 460 N GLY A 60 40.033 23.542 3.113 1.00 19.92 N ANISOU 460 N GLY A 60 2513 1420 3635 -1331 593 160 N ATOM 461 CA GLY A 60 40.255 25.002 3.100 1.00 19.15 C ANISOU 461 CA GLY A 60 2570 1198 3505 -1334 591 131 C ATOM 462 C GLY A 60 41.273 25.471 4.106 1.00 20.19 C ANISOU 462 C GLY A 60 2763 1312 3593 -1265 744 203 C ATOM 463 O GLY A 60 41.956 24.662 4.726 1.00 19.30 O ANISOU 463 O GLY A 60 2541 1267 3523 -1310 729 328 O ATOM 464 N PRO A 61 41.389 26.808 4.256 1.00 20.49 N ANISOU 464 N PRO A 61 2940 1299 3543 -1263 720 74 N ATOM 465 CA PRO A 61 42.315 27.525 5.104 1.00 21.01 C ANISOU 465 CA PRO A 61 3003 1520 3460 -1178 710 22 C ATOM 466 C PRO A 61 42.402 27.033 6.531 1.00 21.53 C ANISOU 466 C PRO A 61 3057 1608 3515 -1187 736 5 C ATOM 467 O PRO A 61 43.517 26.948 7.051 1.00 21.67 O ANISOU 467 O PRO A 61 3188 1647 3395 -1155 685 -39 O ATOM 468 CB PRO A 61 41.808 28.970 5.039 1.00 21.67 C ANISOU 468 CB PRO A 61 3155 1609 3469 -1171 647 -15 C ATOM 469 CG PRO A 61 41.162 29.091 3.715 1.00 21.77 C ANISOU 469 CG PRO A 61 3139 1404 3726 -1342 676 121 C ATOM 470 CD PRO A 61 40.545 27.719 3.461 1.00 21.08 C ANISOU 470 CD PRO A 61 3006 1293 3710 -1230 617 11 C ATOM 471 N ASP A 62 41.258 26.661 7.135 1.00 22.22 N ANISOU 471 N ASP A 62 3235 1858 3350 -1024 847 -82 N ATOM 472 CA ASP A 62 41.224 26.141 8.491 1.00 22.39 C ANISOU 472 CA ASP A 62 3194 1868 3445 -1159 863 -50 C ATOM 473 C ASP A 62 42.078 24.887 8.557 1.00 20.89 C ANISOU 473 C ASP A 62 2904 1834 3196 -1321 928 -38 C ATOM 474 O ASP A 62 42.805 24.666 9.521 1.00 20.43 O ANISOU 474 O ASP A 62 2756 1721 3284 -1537 868 -53 O ATOM 475 CB ASP A 62 39.783 25.773 8.918 1.00 24.12 C ANISOU 475 CB ASP A 62 3382 2198 3582 -922 829 -133 C ATOM 476 CG ASP A 62 38.810 26.962 8.946 1.00 28.28 C ANISOU 476 CG ASP A 62 4199 2611 3932 -846 681 -330 C ATOM 477 OD1 ASP A 62 38.926 27.812 9.875 1.00 30.66 O ANISOU 477 OD1 ASP A 62 4793 3042 3815 -829 617 -731 O ATOM 478 OD2 ASP A 62 37.862 26.977 8.082 1.00 30.66 O ANISOU 478 OD2 ASP A 62 4760 3001 3888 -586 676 -471 O ATOM 479 N PHE A 63 41.931 24.023 7.560 1.00 20.07 N ANISOU 479 N PHE A 63 2842 1846 2938 -1360 998 15 N ATOM 480 CA PHE A 63 42.599 22.733 7.595 1.00 19.75 C ANISOU 480 CA PHE A 63 2928 1790 2786 -1427 895 -17 C ATOM 481 C PHE A 63 44.129 22.897 7.403 1.00 20.52 C ANISOU 481 C PHE A 63 3055 1872 2869 -1464 774 -18 C ATOM 482 O PHE A 63 44.949 22.302 8.142 1.00 20.70 O ANISOU 482 O PHE A 63 3177 1831 2855 -1474 750 45 O ATOM 483 CB PHE A 63 41.908 21.791 6.593 1.00 19.12 C ANISOU 483 CB PHE A 63 2802 1787 2675 -1485 924 52 C ATOM 484 CG PHE A 63 42.698 20.542 6.261 1.00 19.08 C ANISOU 484 CG PHE A 63 2822 1735 2690 -1366 799 -105 C ATOM 485 CD1 PHE A 63 42.573 19.377 7.025 1.00 18.48 C ANISOU 485 CD1 PHE A 63 2407 1448 3165 -1596 586 -248 C ATOM 486 CD2 PHE A 63 43.556 20.532 5.176 1.00 17.03 C ANISOU 486 CD2 PHE A 63 2125 1927 2416 -1621 938 -138 C ATOM 487 CE1 PHE A 63 43.329 18.229 6.701 1.00 16.39 C ANISOU 487 CE1 PHE A 63 2345 1410 2471 -1555 715 -498 C ATOM 488 CE2 PHE A 63 44.294 19.391 4.851 1.00 17.95 C ANISOU 488 CE2 PHE A 63 2228 1715 2876 -1608 881 -137 C ATOM 489 CZ PHE A 63 44.190 18.248 5.623 1.00 17.87 C ANISOU 489 CZ PHE A 63 2301 1607 2879 -1359 759 -37 C ATOM 490 N VAL A 64 44.505 23.751 6.447 1.00 19.91 N ANISOU 490 N VAL A 64 2825 1962 2778 -1649 823 5 N ATOM 491 CA VAL A 64 45.902 24.026 6.157 1.00 20.64 C ANISOU 491 CA VAL A 64 2789 2096 2955 -1728 673 -58 C ATOM 492 C VAL A 64 46.551 24.602 7.403 1.00 21.85 C ANISOU 492 C VAL A 64 2961 2290 3049 -1658 597 -25 C ATOM 493 O VAL A 64 47.597 24.122 7.834 1.00 22.15 O ANISOU 493 O VAL A 64 2956 2408 3052 -1745 613 -79 O ATOM 494 CB VAL A 64 46.036 24.931 4.916 1.00 19.56 C ANISOU 494 CB VAL A 64 2530 2113 2789 -1876 721 0 C ATOM 495 CG1 VAL A 64 47.476 25.589 4.799 1.00 20.80 C ANISOU 495 CG1 VAL A 64 2480 2278 3142 -2005 777 60 C ATOM 496 CG2 VAL A 64 45.743 24.114 3.708 1.00 20.14 C ANISOU 496 CG2 VAL A 64 2573 2065 3012 -1890 928 50 C ATOM 497 N GLU A 65 45.886 25.587 8.005 1.00 23.01 N ANISOU 497 N GLU A 65 3104 2496 3140 -1639 507 -37 N ATOM 498 CA GLU A 65 46.363 26.191 9.245 1.00 25.00 C ANISOU 498 CA GLU A 65 3317 2669 3512 -1578 399 55 C ATOM 499 C GLU A 65 46.511 25.170 10.403 1.00 24.19 C ANISOU 499 C GLU A 65 3184 2638 3369 -1564 300 47 C ATOM 500 O GLU A 65 47.534 25.177 11.084 1.00 25.07 O ANISOU 500 O GLU A 65 3383 2645 3497 -1529 238 100 O ATOM 501 CB GLU A 65 45.459 27.365 9.620 1.00 25.05 C ANISOU 501 CB GLU A 65 3343 2671 3501 -1556 380 -6 C ATOM 502 CG GLU A 65 45.436 27.770 11.096 1.00 27.46 C ANISOU 502 CG GLU A 65 3518 2927 3987 -1567 532 166 C ATOM 503 CD GLU A 65 44.578 29.007 11.308 1.00 27.86 C ANISOU 503 CD GLU A 65 3451 2978 4156 -1688 521 226 C ATOM 504 OE1 GLU A 65 43.356 28.860 11.518 1.00 29.25 O ANISOU 504 OE1 GLU A 65 3150 3469 4494 -1964 990 862 O ATOM 505 OE2 GLU A 65 45.111 30.130 11.213 1.00 30.41 O ANISOU 505 OE2 GLU A 65 3060 2955 5537 -2367 450 346 O ATOM 506 N TYR A 66 45.509 24.309 10.607 1.00 23.91 N ANISOU 506 N TYR A 66 3099 2582 3404 -1589 276 -3 N ATOM 507 CA TYR A 66 45.567 23.251 11.645 1.00 23.50 C ANISOU 507 CA TYR A 66 2824 2716 3388 -1569 184 -100 C ATOM 508 C TYR A 66 46.815 22.369 11.506 1.00 23.30 C ANISOU 508 C TYR A 66 2675 2797 3381 -1519 159 -144 C ATOM 509 O TYR A 66 47.567 22.201 12.471 1.00 23.41 O ANISOU 509 O TYR A 66 2736 2768 3388 -1442 297 -75 O ATOM 510 CB TYR A 66 44.302 22.358 11.619 1.00 23.30 C ANISOU 510 CB TYR A 66 2809 2628 3415 -1639 184 -100 C ATOM 511 CG TYR A 66 44.275 21.341 12.749 1.00 21.29 C ANISOU 511 CG TYR A 66 2419 2431 3236 -1892 157 -64 C ATOM 512 CD1 TYR A 66 43.645 21.635 13.962 1.00 20.41 C ANISOU 512 CD1 TYR A 66 2536 2056 3163 -1885 193 -239 C ATOM 513 CD2 TYR A 66 44.938 20.108 12.625 1.00 20.02 C ANISOU 513 CD2 TYR A 66 2129 2364 3114 -1983 276 -96 C ATOM 514 CE1 TYR A 66 43.647 20.720 15.015 1.00 22.02 C ANISOU 514 CE1 TYR A 66 2798 2328 3238 -1694 64 -236 C ATOM 515 CE2 TYR A 66 44.964 19.199 13.664 1.00 21.14 C ANISOU 515 CE2 TYR A 66 2363 2663 3005 -1879 -189 -275 C ATOM 516 CZ TYR A 66 44.305 19.496 14.845 1.00 23.18 C ANISOU 516 CZ TYR A 66 2772 2600 3433 -1842 86 -24 C ATOM 517 OH TYR A 66 44.363 18.603 15.876 1.00 22.23 O ANISOU 517 OH TYR A 66 2727 2420 3300 -2303 64 194 O ATOM 518 N CYS A 67 46.996 21.782 10.322 1.00 23.29 N ANISOU 518 N CYS A 67 2538 2972 3337 -1510 170 -166 N ATOM 519 CA CYS A 67 48.164 20.943 10.013 1.00 23.93 C ANISOU 519 CA CYS A 67 2648 3086 3356 -1424 64 -276 C ATOM 520 C CYS A 67 49.477 21.721 10.213 1.00 24.56 C ANISOU 520 C CYS A 67 2675 3159 3498 -1450 129 -229 C ATOM 521 O CYS A 67 50.434 21.194 10.773 1.00 24.89 O ANISOU 521 O CYS A 67 2730 3277 3447 -1393 93 -366 O ATOM 522 CB CYS A 67 48.133 20.427 8.575 1.00 24.58 C ANISOU 522 CB CYS A 67 2677 3178 3483 -1358 15 -248 C ATOM 523 SG CYS A 67 46.752 19.374 8.191 1.00 22.84 S ANISOU 523 SG CYS A 67 2491 3265 2919 -1530 168 -363 S ATOM 524 N ALA A 68 49.496 22.967 9.756 1.00 25.40 N ANISOU 524 N ALA A 68 2846 3211 3593 -1481 151 -252 N ATOM 525 CA ALA A 68 50.684 23.826 9.886 1.00 26.39 C ANISOU 525 CA ALA A 68 3078 3280 3670 -1494 118 -147 C ATOM 526 C ALA A 68 51.070 24.082 11.346 1.00 26.62 C ANISOU 526 C ALA A 68 3169 3276 3666 -1477 108 -179 C ATOM 527 O ALA A 68 52.224 23.923 11.719 1.00 26.44 O ANISOU 527 O ALA A 68 3221 3184 3638 -1569 145 -123 O ATOM 528 CB ALA A 68 50.459 25.143 9.165 1.00 27.88 C ANISOU 528 CB ALA A 68 3222 3515 3855 -1389 48 -201 C ATOM 529 N ASP A 69 50.087 24.436 12.172 1.00 27.22 N ANISOU 529 N ASP A 69 3395 3308 3638 -1463 109 -153 N ATOM 530 CA ASP A 69 50.326 24.756 13.584 1.00 27.65 C ANISOU 530 CA ASP A 69 3494 3385 3627 -1423 58 -109 C ATOM 531 C ASP A 69 50.741 23.491 14.337 1.00 27.19 C ANISOU 531 C ASP A 69 3433 3385 3511 -1509 11 -130 C ATOM 532 O ASP A 69 51.560 23.538 15.238 1.00 26.14 O ANISOU 532 O ASP A 69 3257 3288 3385 -1574 -106 -139 O ATOM 533 CB ASP A 69 49.070 25.359 14.235 1.00 28.43 C ANISOU 533 CB ASP A 69 3641 3454 3706 -1384 92 -87 C ATOM 534 CG ASP A 69 48.640 26.693 13.606 1.00 31.10 C ANISOU 534 CG ASP A 69 4001 3684 4129 -1216 127 -103 C ATOM 535 OD1 ASP A 69 49.457 27.320 12.880 1.00 33.50 O ANISOU 535 OD1 ASP A 69 4724 3757 4247 -1121 106 47 O ATOM 536 OD2 ASP A 69 47.466 27.099 13.840 1.00 33.85 O ANISOU 536 OD2 ASP A 69 4623 3878 4358 -750 368 -291 O ATOM 537 N TYR A 70 50.185 22.364 13.927 1.00 26.08 N ANISOU 537 N TYR A 70 3243 3295 3368 -1688 -18 -145 N ATOM 538 CA TYR A 70 50.452 21.087 14.570 1.00 25.93 C ANISOU 538 CA TYR A 70 3113 3373 3365 -1731 -13 -192 C ATOM 539 C TYR A 70 51.867 20.573 14.308 1.00 26.32 C ANISOU 539 C TYR A 70 3132 3488 3379 -1729 -66 -257 C ATOM 540 O TYR A 70 52.568 20.162 15.235 1.00 26.55 O ANISOU 540 O TYR A 70 3195 3507 3384 -1700 -44 -225 O ATOM 541 CB TYR A 70 49.416 20.046 14.139 1.00 24.50 C ANISOU 541 CB TYR A 70 2888 3140 3278 -1935 15 -143 C ATOM 542 CG TYR A 70 49.361 18.865 15.072 1.00 23.94 C ANISOU 542 CG TYR A 70 2735 3075 3283 -2098 183 -126 C ATOM 543 CD1 TYR A 70 48.239 18.643 15.916 1.00 22.89 C ANISOU 543 CD1 TYR A 70 2733 2713 3251 -2256 385 -93 C ATOM 544 CD2 TYR A 70 50.408 17.939 15.105 1.00 23.68 C ANISOU 544 CD2 TYR A 70 2257 3225 3515 -2438 45 58 C ATOM 545 CE1 TYR A 70 48.235 17.591 16.787 1.00 23.01 C ANISOU 545 CE1 TYR A 70 2717 2680 3346 -2403 516 -8 C ATOM 546 CE2 TYR A 70 50.389 16.858 15.972 1.00 24.32 C ANISOU 546 CE2 TYR A 70 2576 2962 3700 -2343 105 201 C ATOM 547 CZ TYR A 70 49.300 16.685 16.798 1.00 22.47 C ANISOU 547 CZ TYR A 70 2246 2965 3327 -2286 242 241 C ATOM 548 OH TYR A 70 49.277 15.579 17.625 1.00 22.41 O ANISOU 548 OH TYR A 70 2520 2777 3216 -2344 221 107 O ATOM 549 N VAL A 71 52.280 20.588 13.044 1.00 27.11 N ANISOU 549 N VAL A 71 3160 3591 3546 -1737 -115 -333 N ATOM 550 CA VAL A 71 53.623 20.138 12.676 1.00 27.49 C ANISOU 550 CA VAL A 71 3139 3697 3608 -1753 -188 -405 C ATOM 551 C VAL A 71 54.658 21.102 13.273 1.00 28.96 C ANISOU 551 C VAL A 71 3338 3926 3738 -1668 -192 -400 C ATOM 552 O VAL A 71 55.718 20.672 13.724 1.00 29.94 O ANISOU 552 O VAL A 71 3414 4111 3849 -1632 -238 -399 O ATOM 553 CB VAL A 71 53.764 19.920 11.140 1.00 27.11 C ANISOU 553 CB VAL A 71 3077 3660 3562 -1765 -196 -390 C ATOM 554 CG1 VAL A 71 55.174 19.600 10.751 1.00 26.21 C ANISOU 554 CG1 VAL A 71 2848 3548 3562 -1906 -155 -569 C ATOM 555 CG2 VAL A 71 52.857 18.751 10.668 1.00 24.48 C ANISOU 555 CG2 VAL A 71 2676 3248 3374 -1983 -234 -365 C ATOM 556 N LYS A 72 54.346 22.395 13.316 1.00 30.36 N ANISOU 556 N LYS A 72 3495 4130 3910 -1637 -201 -462 N ATOM 557 CA LYS A 72 55.288 23.333 13.956 1.00 31.53 C ANISOU 557 CA LYS A 72 3603 4304 4072 -1620 -258 -456 C ATOM 558 C LYS A 72 55.422 23.018 15.443 1.00 31.48 C ANISOU 558 C LYS A 72 3538 4358 4062 -1569 -254 -435 C ATOM 559 O LYS A 72 56.513 23.057 15.989 1.00 31.13 O ANISOU 559 O LYS A 72 3400 4319 4108 -1706 -236 -409 O ATOM 560 CB LYS A 72 54.939 24.810 13.712 1.00 32.07 C ANISOU 560 CB LYS A 72 3683 4362 4138 -1613 -283 -523 C ATOM 561 CG LYS A 72 55.927 25.770 14.418 1.00 33.12 C ANISOU 561 CG LYS A 72 3864 4362 4356 -1681 -288 -386 C ATOM 562 CD LYS A 72 55.970 27.179 13.840 1.00 34.00 C ANISOU 562 CD LYS A 72 3916 4590 4409 -1620 -337 -499 C ATOM 563 CE LYS A 72 56.762 28.143 14.760 1.00 36.28 C ANISOU 563 CE LYS A 72 3853 5028 4901 -1683 -450 -494 C ATOM 564 NZ LYS A 72 58.251 27.906 14.771 1.00 39.24 N ANISOU 564 NZ LYS A 72 3896 5585 5426 -1638 -422 -616 N ATOM 565 N LYS A 73 54.320 22.648 16.092 1.00 31.37 N ANISOU 565 N LYS A 73 3497 4355 4066 -1556 -276 -407 N ATOM 566 CA LYS A 73 54.358 22.403 17.535 1.00 31.72 C ANISOU 566 CA LYS A 73 3541 4427 4082 -1424 -313 -373 C ATOM 567 C LYS A 73 54.932 21.023 17.894 1.00 31.42 C ANISOU 567 C LYS A 73 3503 4393 4039 -1367 -357 -389 C ATOM 568 O LYS A 73 55.702 20.903 18.850 1.00 31.16 O ANISOU 568 O LYS A 73 3262 4422 4154 -1466 -374 -314 O ATOM 569 CB LYS A 73 52.966 22.614 18.148 1.00 32.23 C ANISOU 569 CB LYS A 73 3660 4501 4085 -1413 -295 -375 C ATOM 570 CG LYS A 73 52.803 22.076 19.549 1.00 34.10 C ANISOU 570 CG LYS A 73 3942 4838 4174 -1317 -350 -345 C ATOM 571 CD LYS A 73 51.563 22.632 20.216 1.00 38.69 C ANISOU 571 CD LYS A 73 4458 5643 4599 -1398 -342 -216 C ATOM 572 CE LYS A 73 51.169 21.803 21.445 1.00 40.86 C ANISOU 572 CE LYS A 73 4833 5810 4882 -1414 -386 -93 C ATOM 573 NZ LYS A 73 52.269 21.616 22.446 1.00 42.35 N ANISOU 573 NZ LYS A 73 5083 5982 5023 -1343 -319 -118 N ATOM 574 N HIS A 74 54.546 19.998 17.132 1.00 30.98 N ANISOU 574 N HIS A 74 3477 4312 3980 -1271 -369 -449 N ATOM 575 CA HIS A 74 54.875 18.605 17.451 1.00 30.58 C ANISOU 575 CA HIS A 74 3478 4203 3936 -1222 -434 -529 C ATOM 576 C HIS A 74 55.896 17.928 16.521 1.00 30.13 C ANISOU 576 C HIS A 74 3507 4078 3861 -1182 -539 -525 C ATOM 577 O HIS A 74 56.361 16.827 16.802 1.00 30.58 O ANISOU 577 O HIS A 74 3687 4178 3751 -1029 -627 -431 O ATOM 578 CB HIS A 74 53.579 17.780 17.538 1.00 31.28 C ANISOU 578 CB HIS A 74 3533 4280 4069 -1172 -429 -582 C ATOM 579 CG HIS A 74 52.647 18.257 18.602 1.00 32.38 C ANISOU 579 CG HIS A 74 3526 4550 4225 -1220 -401 -685 C ATOM 580 ND1 HIS A 74 51.404 18.786 18.321 1.00 34.69 N ANISOU 580 ND1 HIS A 74 3743 4837 4601 -1176 -524 -874 N ATOM 581 CD2 HIS A 74 52.802 18.350 19.944 1.00 34.41 C ANISOU 581 CD2 HIS A 74 3695 4887 4491 -1130 -311 -651 C ATOM 582 CE1 HIS A 74 50.812 19.138 19.450 1.00 33.20 C ANISOU 582 CE1 HIS A 74 3691 4659 4262 -1279 -565 -850 C ATOM 583 NE2 HIS A 74 51.641 18.890 20.449 1.00 35.47 N ANISOU 583 NE2 HIS A 74 4141 4760 4575 -1061 -298 -824 N ATOM 584 N GLY A 75 56.245 18.583 15.416 1.00 29.12 N ANISOU 584 N GLY A 75 3353 3934 3775 -1217 -562 -591 N ATOM 585 CA GLY A 75 57.162 18.004 14.451 1.00 27.60 C ANISOU 585 CA GLY A 75 3061 3686 3738 -1235 -613 -601 C ATOM 586 C GLY A 75 56.424 17.137 13.442 1.00 26.58 C ANISOU 586 C GLY A 75 2900 3510 3687 -1233 -595 -620 C ATOM 587 O GLY A 75 55.198 16.989 13.520 1.00 26.00 O ANISOU 587 O GLY A 75 2900 3397 3581 -1298 -646 -652 O ATOM 588 N PRO A 76 57.170 16.547 12.498 1.00 26.29 N ANISOU 588 N PRO A 76 2777 3457 3755 -1248 -594 -596 N ATOM 589 CA PRO A 76 56.627 15.685 11.432 1.00 25.71 C ANISOU 589 CA PRO A 76 2608 3487 3672 -1209 -601 -561 C ATOM 590 C PRO A 76 55.859 14.505 12.041 1.00 25.04 C ANISOU 590 C PRO A 76 2591 3345 3577 -1237 -573 -448 C ATOM 591 O PRO A 76 56.209 14.054 13.129 1.00 24.79 O ANISOU 591 O PRO A 76 2427 3416 3574 -1234 -600 -446 O ATOM 592 CB PRO A 76 57.874 15.192 10.695 1.00 25.68 C ANISOU 592 CB PRO A 76 2517 3498 3742 -1203 -634 -576 C ATOM 593 CG PRO A 76 59.020 15.392 11.720 1.00 26.36 C ANISOU 593 CG PRO A 76 2685 3610 3720 -1250 -737 -738 C ATOM 594 CD PRO A 76 58.641 16.638 12.455 1.00 26.21 C ANISOU 594 CD PRO A 76 2592 3515 3848 -1225 -623 -615 C ATOM 595 N GLN A 77 54.819 14.037 11.331 1.00 24.88 N ANISOU 595 N GLN A 77 2601 3301 3551 -1195 -438 -300 N ATOM 596 CA GLN A 77 53.896 12.996 11.784 1.00 23.81 C ANISOU 596 CA GLN A 77 2573 3094 3379 -1189 -360 -227 C ATOM 597 C GLN A 77 53.742 11.964 10.665 1.00 23.68 C ANISOU 597 C GLN A 77 2563 3087 3345 -1123 -355 -169 C ATOM 598 O GLN A 77 53.582 12.335 9.503 1.00 24.02 O ANISOU 598 O GLN A 77 2766 3051 3309 -1053 -379 -115 O ATOM 599 CB GLN A 77 52.534 13.616 12.102 1.00 23.36 C ANISOU 599 CB GLN A 77 2545 3024 3306 -1310 -259 -213 C ATOM 600 CG GLN A 77 52.602 14.807 13.081 1.00 23.69 C ANISOU 600 CG GLN A 77 2600 3328 3073 -1532 -63 -111 C ATOM 601 CD GLN A 77 52.961 14.363 14.481 1.00 25.63 C ANISOU 601 CD GLN A 77 2786 3652 3299 -1867 196 359 C ATOM 602 OE1 GLN A 77 52.438 13.351 14.963 1.00 24.13 O ANISOU 602 OE1 GLN A 77 2393 3962 2812 -2373 762 724 O ATOM 603 NE2 GLN A 77 53.852 15.115 15.157 1.00 23.64 N ANISOU 603 NE2 GLN A 77 2273 3651 3058 -2416 524 535 N ATOM 604 N GLN A 78 53.812 10.677 11.010 1.00 22.99 N ANISOU 604 N GLN A 78 2440 2987 3306 -1059 -300 -82 N ATOM 605 CA GLN A 78 53.528 9.604 10.054 1.00 22.81 C ANISOU 605 CA GLN A 78 2348 3019 3298 -1077 -192 -26 C ATOM 606 C GLN A 78 52.016 9.439 9.896 1.00 22.33 C ANISOU 606 C GLN A 78 2315 2993 3174 -995 -197 26 C ATOM 607 O GLN A 78 51.550 8.783 8.949 1.00 21.64 O ANISOU 607 O GLN A 78 2344 2866 3012 -1082 -221 -68 O ATOM 608 CB GLN A 78 54.087 8.265 10.537 1.00 23.39 C ANISOU 608 CB GLN A 78 2355 3121 3412 -1038 -151 -13 C ATOM 609 CG GLN A 78 55.584 8.069 10.369 1.00 26.15 C ANISOU 609 CG GLN A 78 2646 3428 3860 -1512 271 104 C ATOM 610 CD GLN A 78 56.005 8.072 8.900 1.00 31.27 C ANISOU 610 CD GLN A 78 3098 4153 4630 -1876 706 416 C ATOM 611 OE1 GLN A 78 56.649 9.023 8.445 1.00 30.29 O ANISOU 611 OE1 GLN A 78 2353 4099 5056 -2537 1037 576 O ATOM 612 NE2 GLN A 78 55.610 7.011 8.138 1.00 29.81 N ANISOU 612 NE2 GLN A 78 2257 4347 4722 -2355 1161 877 N ATOM 613 N LYS A 79 51.277 9.963 10.882 1.00 21.18 N ANISOU 613 N LYS A 79 2194 2779 3073 -869 -172 -27 N ATOM 614 CA LYS A 79 49.802 9.931 10.919 1.00 20.60 C ANISOU 614 CA LYS A 79 2127 2741 2959 -868 -81 126 C ATOM 615 C LYS A 79 49.288 11.115 11.737 1.00 19.33 C ANISOU 615 C LYS A 79 2011 2577 2755 -880 -44 149 C ATOM 616 O LYS A 79 49.822 11.444 12.803 1.00 19.80 O ANISOU 616 O LYS A 79 1985 2704 2831 -1058 22 287 O ATOM 617 CB LYS A 79 49.258 8.627 11.497 1.00 20.28 C ANISOU 617 CB LYS A 79 1900 2735 3071 -911 -87 48 C ATOM 618 CG LYS A 79 47.712 8.521 11.452 1.00 24.07 C ANISOU 618 CG LYS A 79 2606 3284 3254 -923 -303 114 C ATOM 619 CD LYS A 79 47.225 7.534 12.442 1.00 21.15 C ANISOU 619 CD LYS A 79 1443 3418 3173 -1625 -277 201 C ATOM 620 CE LYS A 79 45.737 7.281 12.358 1.00 24.76 C ANISOU 620 CE LYS A 79 2247 3709 3452 -1374 -409 253 C ATOM 621 NZ LYS A 79 45.451 6.228 13.319 1.00 23.05 N ANISOU 621 NZ LYS A 79 2126 3902 2728 -1325 -534 151 N ATOM 622 N LEU A 80 48.264 11.766 11.205 1.00 17.61 N ANISOU 622 N LEU A 80 1787 2326 2577 -792 35 156 N ATOM 623 CA LEU A 80 47.617 12.869 11.878 1.00 16.54 C ANISOU 623 CA LEU A 80 1819 2089 2376 -649 2 120 C ATOM 624 C LEU A 80 46.113 12.879 11.566 1.00 16.61 C ANISOU 624 C LEU A 80 1953 2093 2262 -447 -69 87 C ATOM 625 O LEU A 80 45.680 13.053 10.429 1.00 17.82 O ANISOU 625 O LEU A 80 1965 2386 2416 -604 -35 208 O ATOM 626 CB LEU A 80 48.258 14.177 11.492 1.00 15.91 C ANISOU 626 CB LEU A 80 1863 1894 2286 -661 -21 107 C ATOM 627 CG LEU A 80 47.778 15.389 12.266 1.00 15.56 C ANISOU 627 CG LEU A 80 2045 1697 2169 -840 -121 155 C ATOM 628 CD1 LEU A 80 48.207 15.343 13.747 1.00 19.23 C ANISOU 628 CD1 LEU A 80 2946 1534 2826 -947 -361 -188 C ATOM 629 CD2 LEU A 80 48.324 16.586 11.532 1.00 17.42 C ANISOU 629 CD2 LEU A 80 1859 1537 3220 -1205 -104 -51 C ATOM 630 N VAL A 81 45.333 12.679 12.605 1.00 15.83 N ATOM 631 CA VAL A 81 43.869 12.778 12.498 1.00 16.18 C ATOM 632 C VAL A 81 43.433 14.191 12.843 1.00 15.79 C ATOM 633 O VAL A 81 43.542 14.636 13.997 1.00 17.50 O ANISOU 633 O VAL A 81 2260 2264 2124 -361 194 -70 O ATOM 634 CB VAL A 81 43.173 11.741 13.393 1.00 15.26 C ATOM 635 CG1 VAL A 81 41.679 11.851 13.238 1.00 15.16 C ATOM 636 CG2 VAL A 81 43.578 10.332 12.959 1.00 17.49 C ATOM 637 N THR A 82 42.940 14.906 11.847 1.00 14.47 N ANISOU 637 N THR A 82 1625 1807 2064 -736 314 301 N ATOM 638 CA THR A 82 42.595 16.312 12.017 1.00 15.50 C ANISOU 638 CA THR A 82 1805 1871 2210 -884 541 417 C ATOM 639 C THR A 82 41.102 16.582 11.783 1.00 15.81 C ANISOU 639 C THR A 82 1974 1823 2209 -1030 497 474 C ATOM 640 O THR A 82 40.381 15.723 11.267 1.00 17.15 O ANISOU 640 O THR A 82 2161 1913 2441 -1028 442 331 O ATOM 641 CB THR A 82 43.397 17.200 10.988 1.00 15.40 C ANISOU 641 CB THR A 82 1812 1892 2148 -997 543 508 C ATOM 642 OG1 THR A 82 42.937 16.922 9.670 1.00 16.49 O ANISOU 642 OG1 THR A 82 1895 1795 2575 -1399 558 386 O ATOM 643 CG2 THR A 82 44.901 16.946 11.046 1.00 15.36 C ANISOU 643 CG2 THR A 82 1641 1888 2304 -1080 690 626 C ATOM 644 N PRO A 83 40.624 17.789 12.155 1.00 15.24 N ANISOU 644 N PRO A 83 1839 1829 2122 -987 656 384 N ATOM 645 CA PRO A 83 39.346 18.285 11.689 1.00 15.93 C ANISOU 645 CA PRO A 83 1914 1865 2271 -1071 629 399 C ATOM 646 C PRO A 83 39.307 18.419 10.197 1.00 16.55 C ANISOU 646 C PRO A 83 1917 1911 2459 -1045 553 285 C ATOM 647 O PRO A 83 40.349 18.662 9.547 1.00 15.92 O ANISOU 647 O PRO A 83 1621 2023 2402 -1234 767 369 O ATOM 648 CB PRO A 83 39.260 19.713 12.297 1.00 15.14 C ANISOU 648 CB PRO A 83 1826 1675 2249 -1186 573 413 C ATOM 649 CG PRO A 83 40.588 20.005 12.782 1.00 16.02 C ANISOU 649 CG PRO A 83 1945 1910 2229 -955 593 467 C ATOM 650 CD PRO A 83 41.218 18.704 13.130 1.00 15.63 C ANISOU 650 CD PRO A 83 1925 1686 2325 -1129 577 421 C ATOM 651 N SER A 84 38.109 18.369 9.651 1.00 15.50 N ANISOU 651 N SER A 84 1576 1749 2564 -1312 475 169 N ATOM 652 CA SER A 84 37.964 18.608 8.214 1.00 15.98 C ANISOU 652 CA SER A 84 1648 1860 2562 -1265 461 183 C ATOM 653 C SER A 84 37.395 20.012 7.921 1.00 17.41 C ANISOU 653 C SER A 84 1778 2097 2737 -1198 448 144 C ATOM 654 O SER A 84 37.562 20.569 6.810 1.00 16.62 O ANISOU 654 O SER A 84 1494 2053 2767 -1374 551 183 O ATOM 655 CB SER A 84 37.001 17.568 7.676 1.00 16.27 C ANISOU 655 CB SER A 84 1643 2057 2479 -1246 441 165 C ATOM 656 OG SER A 84 35.739 17.887 8.192 1.00 16.29 O ANISOU 656 OG SER A 84 1627 1958 2602 -1034 405 388 O ATOM 657 N PHE A 85 36.607 20.515 8.887 1.00 19.02 N ANISOU 657 N PHE A 85 2348 2056 2822 -1120 309 50 N ATOM 658 CA PHE A 85 35.842 21.777 8.759 1.00 18.61 C ANISOU 658 CA PHE A 85 2306 1870 2892 -1205 217 -30 C ATOM 659 C PHE A 85 34.805 21.705 7.625 1.00 18.48 C ANISOU 659 C PHE A 85 2184 1850 2985 -1300 244 -26 C ATOM 660 O PHE A 85 34.409 22.713 7.036 1.00 17.28 O ANISOU 660 O PHE A 85 2143 1598 2825 -1355 287 -86 O ATOM 661 CB PHE A 85 36.798 22.974 8.609 1.00 18.70 C ANISOU 661 CB PHE A 85 2410 1866 2828 -1221 202 80 C ATOM 662 CG PHE A 85 37.816 23.069 9.700 1.00 18.46 C ANISOU 662 CG PHE A 85 2510 1664 2841 -1290 227 41 C ATOM 663 CD1 PHE A 85 37.489 23.653 10.922 1.00 22.34 C ANISOU 663 CD1 PHE A 85 3226 2180 3081 -1201 -46 30 C ATOM 664 CD2 PHE A 85 39.100 22.566 9.520 1.00 19.84 C ANISOU 664 CD2 PHE A 85 2915 1692 2929 -1493 -61 175 C ATOM 665 CE1 PHE A 85 38.435 23.750 11.952 1.00 21.06 C ANISOU 665 CE1 PHE A 85 2866 2061 3075 -1234 5 327 C ATOM 666 CE2 PHE A 85 40.055 22.655 10.546 1.00 21.99 C ANISOU 666 CE2 PHE A 85 3187 2183 2985 -1241 33 165 C ATOM 667 CZ PHE A 85 39.712 23.252 11.765 1.00 21.59 C ANISOU 667 CZ PHE A 85 3109 2119 2974 -1089 79 81 C ATOM 668 N VAL A 86 34.355 20.478 7.354 1.00 18.63 N ANISOU 668 N VAL A 86 2222 1767 3087 -1309 257 -149 N ATOM 669 CA VAL A 86 33.279 20.202 6.390 1.00 18.32 C ANISOU 669 CA VAL A 86 1935 1880 3142 -1472 329 -24 C ATOM 670 C VAL A 86 32.226 19.362 7.085 1.00 18.75 C ANISOU 670 C VAL A 86 1860 2008 3256 -1407 381 -53 C ATOM 671 O VAL A 86 32.553 18.339 7.721 1.00 18.66 O ANISOU 671 O VAL A 86 1832 1841 3415 -1550 404 50 O ATOM 672 CB VAL A 86 33.810 19.429 5.162 1.00 18.38 C ANISOU 672 CB VAL A 86 1823 1970 3187 -1524 344 -24 C ATOM 673 CG1 VAL A 86 32.712 19.223 4.131 1.00 18.91 C ANISOU 673 CG1 VAL A 86 2125 2059 3000 -1355 150 49 C ATOM 674 CG2 VAL A 86 35.009 20.211 4.521 1.00 18.35 C ANISOU 674 CG2 VAL A 86 1888 1925 3159 -1634 219 116 C ATOM 675 N LYS A 87 30.976 19.792 6.968 1.00 18.69 N ANISOU 675 N LYS A 87 1816 2018 3264 -1323 513 -19 N ATOM 676 CA LYS A 87 29.854 19.063 7.561 1.00 18.56 C ANISOU 676 CA LYS A 87 1405 2203 3441 -1339 531 -183 C ATOM 677 C LYS A 87 29.847 17.658 6.995 1.00 18.86 C ANISOU 677 C LYS A 87 1508 2254 3402 -1314 565 -53 C ATOM 678 O LYS A 87 30.056 17.495 5.795 1.00 19.52 O ANISOU 678 O LYS A 87 1338 2490 3585 -1260 656 -264 O ATOM 679 CB LYS A 87 28.560 19.751 7.224 1.00 19.83 C ANISOU 679 CB LYS A 87 1718 2374 3442 -1214 547 -196 C ATOM 680 CG LYS A 87 27.438 19.146 8.012 1.00 20.24 C ANISOU 680 CG LYS A 87 1183 2449 4056 -1331 749 -108 C ATOM 681 CD LYS A 87 26.063 19.516 7.502 1.00 28.41 C ANISOU 681 CD LYS A 87 2300 3539 4952 -1408 656 -79 C ATOM 682 CE LYS A 87 25.121 19.666 8.685 1.00 28.39 C ANISOU 682 CE LYS A 87 1759 3769 5258 -2009 1095 411 C ATOM 683 NZ LYS A 87 23.757 19.067 8.425 1.00 30.60 N ANISOU 683 NZ LYS A 87 2272 3215 6136 -2411 501 93 N ATOM 684 N GLY A 88 29.596 16.650 7.833 1.00 18.52 N ANISOU 684 N GLY A 88 1537 2154 3344 -1353 538 18 N ATOM 685 CA GLY A 88 29.640 15.274 7.355 1.00 18.49 C ANISOU 685 CA GLY A 88 1723 2097 3204 -1483 608 217 C ATOM 686 C GLY A 88 30.965 14.559 7.334 1.00 18.21 C ANISOU 686 C GLY A 88 1819 2016 3082 -1530 538 277 C ATOM 687 O GLY A 88 31.016 13.317 7.258 1.00 18.75 O ANISOU 687 O GLY A 88 1974 2047 3102 -1547 610 480 O ATOM 688 N ILE A 89 32.050 15.331 7.305 1.00 17.76 N ANISOU 688 N ILE A 89 1878 1998 2873 -1519 540 383 N ATOM 689 CA ILE A 89 33.373 14.758 7.288 1.00 16.90 C ANISOU 689 CA ILE A 89 1931 1878 2611 -1526 505 261 C ATOM 690 C ILE A 89 33.893 14.824 8.705 1.00 16.71 C ANISOU 690 C ILE A 89 1895 1852 2601 -1551 278 288 C ATOM 691 O ILE A 89 34.243 15.915 9.238 1.00 17.02 O ANISOU 691 O ILE A 89 2184 1671 2608 -1556 0 113 O ATOM 692 CB ILE A 89 34.304 15.450 6.217 1.00 16.76 C ANISOU 692 CB ILE A 89 1898 1992 2476 -1482 568 393 C ATOM 693 CG1 ILE A 89 33.620 15.450 4.838 1.00 16.90 C ANISOU 693 CG1 ILE A 89 1810 2037 2571 -1432 734 284 C ATOM 694 CG2 ILE A 89 35.675 14.731 6.136 1.00 16.44 C ANISOU 694 CG2 ILE A 89 1972 2035 2238 -1484 743 270 C ATOM 695 CD1 ILE A 89 34.540 15.996 3.710 1.00 16.53 C ANISOU 695 CD1 ILE A 89 2018 1853 2408 -1480 638 296 C ATOM 696 N GLN A 90 33.912 13.653 9.332 1.00 16.73 N ANISOU 696 N GLN A 90 1812 1879 2664 -1569 171 163 N ATOM 697 CA GLN A 90 34.187 13.524 10.763 1.00 16.82 C ANISOU 697 CA GLN A 90 1715 2069 2604 -1593 238 167 C ATOM 698 C GLN A 90 35.577 13.973 11.069 1.00 16.52 C ANISOU 698 C GLN A 90 1653 2081 2542 -1564 222 174 C ATOM 699 O GLN A 90 35.816 14.576 12.105 1.00 16.19 O ANISOU 699 O GLN A 90 1414 2329 2405 -1471 347 217 O ATOM 700 CB GLN A 90 34.096 12.090 11.216 1.00 16.97 C ANISOU 700 CB GLN A 90 1839 2025 2581 -1613 223 321 C ATOM 701 CG GLN A 90 32.674 11.656 11.388 1.00 18.57 C ANISOU 701 CG GLN A 90 1951 2298 2805 -1815 372 110 C ATOM 702 CD GLN A 90 32.557 10.203 11.716 1.00 22.44 C ANISOU 702 CD GLN A 90 2911 2534 3079 -1333 465 126 C ATOM 703 OE1 GLN A 90 32.557 9.357 10.819 1.00 23.35 O ANISOU 703 OE1 GLN A 90 2786 2695 3390 -1195 725 1 O ATOM 704 NE2 GLN A 90 32.424 9.893 13.003 1.00 23.17 N ANISOU 704 NE2 GLN A 90 2704 2921 3179 -1719 955 237 N ATOM 705 N CYS A 91 36.476 13.645 10.161 1.00 16.00 N ANISOU 705 N CYS A 91 1683 2056 2338 -1543 283 196 N ATOM 706 CA CYS A 91 37.891 13.960 10.307 1.00 16.03 C ANISOU 706 CA CYS A 91 1704 2021 2364 -1565 198 188 C ATOM 707 C CYS A 91 38.595 13.632 9.022 1.00 15.85 C ANISOU 707 C CYS A 91 1701 1994 2325 -1538 231 222 C ATOM 708 O CYS A 91 38.075 12.944 8.129 1.00 15.93 O ANISOU 708 O CYS A 91 1701 2220 2131 -1613 258 268 O ATOM 709 CB CYS A 91 38.545 13.184 11.473 1.00 16.48 C ANISOU 709 CB CYS A 91 1674 2093 2492 -1594 184 131 C ATOM 710 SG CYS A 91 38.318 11.361 11.369 1.00 19.44 S ANISOU 710 SG CYS A 91 2256 2311 2819 -1887 -115 87 S ATOM 711 N VAL A 92 39.807 14.154 8.904 1.00 15.25 N ANISOU 711 N VAL A 92 1557 1980 2258 -1462 216 172 N ATOM 712 CA VAL A 92 40.669 13.727 7.859 1.00 15.16 C ANISOU 712 CA VAL A 92 1617 1791 2351 -1367 313 267 C ATOM 713 C VAL A 92 41.773 12.912 8.544 1.00 14.69 C ANISOU 713 C VAL A 92 1550 1786 2244 -1311 295 331 C ATOM 714 O VAL A 92 42.439 13.420 9.457 1.00 15.00 O ANISOU 714 O VAL A 92 1716 1929 2054 -1160 221 162 O ATOM 715 CB VAL A 92 41.359 14.958 7.163 1.00 15.11 C ANISOU 715 CB VAL A 92 1670 1738 2330 -1351 329 313 C ATOM 716 CG1 VAL A 92 42.214 14.507 6.012 1.00 14.93 C ANISOU 716 CG1 VAL A 92 1757 1589 2326 -1354 323 190 C ATOM 717 CG2 VAL A 92 40.335 15.987 6.680 1.00 15.60 C ANISOU 717 CG2 VAL A 92 1650 1922 2353 -1379 521 248 C ATOM 718 N ASN A 93 41.995 11.692 8.069 1.00 14.33 N ANISOU 718 N ASN A 93 1501 1678 2263 -1195 371 372 N ATOM 719 CA ASN A 93 43.092 10.882 8.513 1.00 14.90 C ANISOU 719 CA ASN A 93 1495 1682 2483 -1219 308 404 C ATOM 720 C ASN A 93 44.212 10.972 7.478 1.00 15.12 C ANISOU 720 C ASN A 93 1579 1714 2448 -1138 352 397 C ATOM 721 O ASN A 93 44.179 10.330 6.406 1.00 15.02 O ANISOU 721 O ASN A 93 1588 1689 2428 -1269 213 498 O ATOM 722 CB ASN A 93 42.695 9.432 8.702 1.00 15.32 C ANISOU 722 CB ASN A 93 1561 1679 2579 -1050 375 489 C ATOM 723 CG ASN A 93 43.746 8.629 9.430 1.00 16.27 C ANISOU 723 CG ASN A 93 1493 1866 2822 -1213 286 550 C ATOM 724 OD1 ASN A 93 44.881 9.087 9.662 1.00 15.64 O ANISOU 724 OD1 ASN A 93 1335 2223 2384 -1024 625 739 O ATOM 725 ND2 ASN A 93 43.380 7.400 9.780 1.00 18.97 N ANISOU 725 ND2 ASN A 93 1516 2505 3185 -823 456 1192 N ATOM 726 N ASN A 94 45.208 11.766 7.834 1.00 15.05 N ANISOU 726 N ASN A 94 1514 1682 2520 -1227 248 324 N ATOM 727 CA ASN A 94 46.428 11.960 7.002 1.00 15.51 C ANISOU 727 CA ASN A 94 1563 1810 2517 -1153 314 241 C ATOM 728 C ASN A 94 47.462 10.886 7.294 1.00 16.16 C ANISOU 728 C ASN A 94 1540 1970 2628 -1258 309 117 C ATOM 729 O ASN A 94 48.115 10.931 8.333 1.00 16.17 O ANISOU 729 O ASN A 94 1709 1946 2487 -1374 111 77 O ATOM 730 CB ASN A 94 47.050 13.312 7.300 1.00 17.38 C ANISOU 730 CB ASN A 94 1871 2084 2647 -1034 343 161 C ATOM 731 CG ASN A 94 46.091 14.469 7.079 1.00 18.32 C ANISOU 731 CG ASN A 94 2074 2283 2603 -985 251 388 C ATOM 732 OD1 ASN A 94 46.083 15.042 6.004 1.00 19.17 O ANISOU 732 OD1 ASN A 94 2339 2149 2795 -1447 935 726 O ATOM 733 ND2 ASN A 94 45.266 14.810 8.106 1.00 16.80 N ANISOU 733 ND2 ASN A 94 1912 2130 2340 -1639 359 363 N ATOM 734 N VAL A 95 47.566 9.888 6.412 1.00 15.41 N ANISOU 734 N VAL A 95 1373 1787 2694 -1265 414 23 N ATOM 735 CA VAL A 95 48.458 8.763 6.587 1.00 15.90 C ANISOU 735 CA VAL A 95 1433 1740 2868 -1235 479 56 C ATOM 736 C VAL A 95 49.663 8.890 5.643 1.00 16.45 C ANISOU 736 C VAL A 95 1543 1823 2882 -1203 403 43 C ATOM 737 O VAL A 95 49.491 9.115 4.438 1.00 17.89 O ANISOU 737 O VAL A 95 1776 1980 3039 -1214 298 173 O ATOM 738 CB VAL A 95 47.719 7.481 6.266 1.00 15.38 C ANISOU 738 CB VAL A 95 1401 1597 2845 -1199 480 -37 C ATOM 739 CG1 VAL A 95 48.666 6.251 6.318 1.00 16.31 C ANISOU 739 CG1 VAL A 95 1334 1903 2960 -1205 699 49 C ATOM 740 CG2 VAL A 95 46.531 7.298 7.246 1.00 16.08 C ANISOU 740 CG2 VAL A 95 1636 1822 2649 -824 724 -100 C ATOM 741 N VAL A 96 50.875 8.761 6.179 1.00 16.56 N ANISOU 741 N VAL A 96 1572 1752 2966 -1152 403 52 N ATOM 742 CA VAL A 96 52.068 8.751 5.318 1.00 16.12 C ANISOU 742 CA VAL A 96 1399 1751 2974 -1092 351 -27 C ATOM 743 C VAL A 96 52.406 7.275 4.963 1.00 16.09 C ANISOU 743 C VAL A 96 1318 1764 3030 -1110 411 35 C ATOM 744 O VAL A 96 52.847 6.513 5.814 1.00 16.74 O ANISOU 744 O VAL A 96 1434 1851 3075 -1095 493 143 O ATOM 745 CB VAL A 96 53.279 9.439 5.978 1.00 16.53 C ANISOU 745 CB VAL A 96 1491 1765 3022 -1116 399 21 C ATOM 746 CG1 VAL A 96 54.521 9.457 5.014 1.00 17.76 C ANISOU 746 CG1 VAL A 96 1893 1969 2885 -802 274 -32 C ATOM 747 CG2 VAL A 96 52.909 10.852 6.496 1.00 16.28 C ANISOU 747 CG2 VAL A 96 1408 1681 3097 -1045 225 13 C ATOM 748 N GLY A 97 52.186 6.875 3.719 1.00 15.67 N ANISOU 748 N GLY A 97 1288 1659 3008 -1183 416 -106 N ATOM 749 CA GLY A 97 52.557 5.527 3.304 1.00 17.21 C ANISOU 749 CA GLY A 97 1513 1843 3181 -1120 249 -156 C ATOM 750 C GLY A 97 54.025 5.353 2.883 1.00 17.16 C ANISOU 750 C GLY A 97 1536 1742 3242 -1312 185 -149 C ATOM 751 O GLY A 97 54.801 6.322 2.848 1.00 17.57 O ANISOU 751 O GLY A 97 1492 1819 3365 -1390 91 -243 O ATOM 752 N PRO A 98 54.425 4.099 2.552 1.00 17.00 N ANISOU 752 N PRO A 98 1563 1668 3227 -1282 91 -153 N ATOM 753 CA PRO A 98 55.762 3.801 2.092 1.00 16.51 C ANISOU 753 CA PRO A 98 1482 1636 3153 -1302 78 -139 C ATOM 754 C PRO A 98 55.964 4.260 0.648 1.00 16.77 C ANISOU 754 C PRO A 98 1520 1666 3185 -1338 66 -85 C ATOM 755 O PRO A 98 54.998 4.641 -0.035 1.00 18.06 O ANISOU 755 O PRO A 98 1703 1719 3437 -1452 290 -95 O ATOM 756 CB PRO A 98 55.835 2.264 2.190 1.00 17.47 C ANISOU 756 CB PRO A 98 1542 1854 3239 -1332 71 -19 C ATOM 757 CG PRO A 98 54.451 1.852 1.976 1.00 15.94 C ANISOU 757 CG PRO A 98 1338 1636 3082 -1202 -81 -286 C ATOM 758 CD PRO A 98 53.603 2.881 2.644 1.00 16.91 C ANISOU 758 CD PRO A 98 1595 1632 3197 -1355 -11 -156 C ATOM 759 N ARG A 99 57.216 4.262 0.204 1.00 17.49 N ANISOU 759 N ARG A 99 1732 1731 3180 -1253 109 -115 N ATOM 760 CA ARG A 99 57.536 4.662 -1.162 1.00 17.67 C ANISOU 760 CA ARG A 99 1724 1798 3190 -1271 126 21 C ATOM 761 C ARG A 99 58.182 3.532 -1.975 1.00 17.94 C ANISOU 761 C ARG A 99 1593 1927 3295 -1195 107 87 C ATOM 762 O ARG A 99 58.716 2.592 -1.418 1.00 17.68 O ANISOU 762 O ARG A 99 1647 1786 3283 -1290 241 235 O ATOM 763 CB ARG A 99 58.413 5.899 -1.150 1.00 16.80 C ANISOU 763 CB ARG A 99 1681 1554 3148 -1211 51 -57 C ATOM 764 CG ARG A 99 57.753 7.075 -0.410 1.00 19.19 C ANISOU 764 CG ARG A 99 1885 2130 3276 -1115 -15 89 C ATOM 765 CD ARG A 99 58.582 8.353 -0.526 1.00 18.19 C ANISOU 765 CD ARG A 99 1947 1462 3500 -1343 -125 -38 C ATOM 766 NE ARG A 99 59.916 8.184 0.039 1.00 20.48 N ANISOU 766 NE ARG A 99 2279 2220 3280 -1115 247 121 N ATOM 767 CZ ARG A 99 60.975 8.948 -0.235 1.00 20.17 C ANISOU 767 CZ ARG A 99 2106 2242 3315 -1346 65 277 C ATOM 768 NH1 ARG A 99 60.902 9.999 -1.061 1.00 18.89 N ANISOU 768 NH1 ARG A 99 1903 2213 3058 -1340 147 358 N ATOM 769 NH2 ARG A 99 62.122 8.663 0.334 1.00 19.62 N ANISOU 769 NH2 ARG A 99 1816 2543 3094 -940 282 483 N ATOM 770 N HIS A 100 58.149 3.663 -3.304 1.00 19.64 N ANISOU 770 N HIS A 100 1767 2270 3422 -1035 23 58 N ATOM 771 CA HIS A 100 58.738 2.694 -4.217 1.00 21.28 C ANISOU 771 CA HIS A 100 1959 2496 3630 -925 -49 53 C ATOM 772 C HIS A 100 60.138 2.316 -3.753 1.00 21.86 C ANISOU 772 C HIS A 100 2007 2581 3718 -936 -100 61 C ATOM 773 O HIS A 100 60.926 3.195 -3.370 1.00 21.33 O ANISOU 773 O HIS A 100 1860 2319 3923 -1275 -143 108 O ATOM 774 CB HIS A 100 58.873 3.299 -5.625 1.00 22.20 C ANISOU 774 CB HIS A 100 2154 2658 3623 -733 -44 -28 C ATOM 775 CG HIS A 100 59.561 2.386 -6.585 1.00 25.88 C ANISOU 775 CG HIS A 100 2596 3072 4165 -690 -109 -288 C ATOM 776 ND1 HIS A 100 58.898 1.381 -7.264 1.00 29.38 N ANISOU 776 ND1 HIS A 100 3204 3345 4614 -576 -36 -457 N ATOM 777 CD2 HIS A 100 60.866 2.265 -6.911 1.00 25.46 C ANISOU 777 CD2 HIS A 100 2407 3041 4223 -960 512 -534 C ATOM 778 CE1 HIS A 100 59.767 0.717 -8.007 1.00 28.35 C ANISOU 778 CE1 HIS A 100 2864 3327 4579 -702 220 -462 C ATOM 779 NE2 HIS A 100 60.965 1.231 -7.804 1.00 29.89 N ANISOU 779 NE2 HIS A 100 3092 3550 4713 -580 494 -407 N ATOM 780 N GLY A 101 60.455 1.028 -3.785 1.00 21.25 N ANISOU 780 N GLY A 101 1883 2430 3760 -906 -110 72 N ATOM 781 CA GLY A 101 61.806 0.608 -3.423 1.00 22.20 C ANISOU 781 CA GLY A 101 1919 2656 3857 -909 -65 69 C ATOM 782 C GLY A 101 62.067 0.437 -1.935 1.00 22.62 C ANISOU 782 C GLY A 101 1952 2811 3829 -805 -152 18 C ATOM 783 O GLY A 101 63.107 -0.075 -1.572 1.00 24.12 O ANISOU 783 O GLY A 101 2085 3080 3999 -814 -71 -30 O ATOM 784 N ASP A 102 61.137 0.852 -1.066 1.00 23.49 N ANISOU 784 N ASP A 102 2081 2984 3857 -832 -144 94 N ATOM 785 CA ASP A 102 61.321 0.714 0.399 1.00 23.38 C ANISOU 785 CA ASP A 102 2124 3016 3743 -816 -146 112 C ATOM 786 C ASP A 102 61.325 -0.768 0.771 1.00 23.67 C ANISOU 786 C ASP A 102 2176 3052 3764 -782 -183 98 C ATOM 787 O ASP A 102 60.662 -1.575 0.114 1.00 22.82 O ANISOU 787 O ASP A 102 2019 3069 3579 -836 -257 44 O ATOM 788 CB ASP A 102 60.244 1.460 1.200 1.00 23.32 C ANISOU 788 CB ASP A 102 2040 3030 3790 -885 -124 168 C ATOM 789 CG ASP A 102 60.393 2.978 1.134 1.00 24.18 C ANISOU 789 CG ASP A 102 2143 3281 3763 -932 43 213 C ATOM 790 OD1 ASP A 102 61.317 3.471 0.448 1.00 23.11 O ANISOU 790 OD1 ASP A 102 1497 2902 4380 -1782 315 169 O ATOM 791 OD2 ASP A 102 59.576 3.693 1.758 1.00 23.17 O ANISOU 791 OD2 ASP A 102 1894 3714 3195 -940 67 508 O ATOM 792 N SER A 103 62.124 -1.138 1.778 1.00 24.16 N ANISOU 792 N SER A 103 2315 3082 3782 -772 -171 21 N ATOM 793 CA SER A 103 62.204 -2.545 2.165 1.00 24.72 C ANISOU 793 CA SER A 103 2396 3126 3870 -729 -196 47 C ATOM 794 C SER A 103 60.939 -2.911 2.934 1.00 23.82 C ANISOU 794 C SER A 103 2212 2998 3841 -730 -162 57 C ATOM 795 O SER A 103 60.302 -2.048 3.532 1.00 23.53 O ANISOU 795 O SER A 103 2163 2987 3789 -832 -280 94 O ATOM 796 CB SER A 103 63.448 -2.854 2.991 1.00 25.02 C ANISOU 796 CB SER A 103 2461 3209 3833 -743 -139 -27 C ATOM 797 OG SER A 103 63.622 -1.887 4.009 1.00 29.46 O ANISOU 797 OG SER A 103 3325 3624 4245 -822 -223 -133 O ATOM 798 N ASN A 104 60.568 -4.180 2.900 1.00 24.33 N ANISOU 798 N ASN A 104 2306 2994 3943 -647 -237 5 N ATOM 799 CA ASN A 104 59.380 -4.635 3.643 1.00 24.28 C ANISOU 799 CA ASN A 104 2317 2918 3989 -647 -172 -3 C ATOM 800 C ASN A 104 58.107 -3.885 3.182 1.00 23.76 C ANISOU 800 C ASN A 104 2230 2882 3915 -635 -132 52 C ATOM 801 O ASN A 104 57.225 -3.579 3.985 1.00 22.93 O ANISOU 801 O ASN A 104 1941 2896 3875 -568 -137 132 O ATOM 802 CB ASN A 104 59.608 -4.435 5.146 1.00 25.97 C ANISOU 802 CB ASN A 104 2642 3058 4165 -642 -184 -22 C ATOM 803 CG ASN A 104 58.861 -5.448 6.009 1.00 28.04 C ANISOU 803 CG ASN A 104 3062 3000 4589 -783 -183 -350 C ATOM 804 OD1 ASN A 104 58.648 -6.600 5.615 1.00 36.81 O ANISOU 804 OD1 ASN A 104 4499 4043 5445 -406 -371 -523 O ATOM 805 ND2 ASN A 104 58.490 -5.030 7.218 1.00 29.90 N ANISOU 805 ND2 ASN A 104 3132 2804 5424 -838 -416 -688 N ATOM 806 N LEU A 105 58.038 -3.585 1.881 1.00 22.73 N ANISOU 806 N LEU A 105 2032 2739 3862 -703 -99 75 N ATOM 807 CA LEU A 105 56.937 -2.807 1.334 1.00 21.63 C ANISOU 807 CA LEU A 105 1959 2507 3751 -835 31 83 C ATOM 808 C LEU A 105 55.544 -3.312 1.737 1.00 20.95 C ANISOU 808 C LEU A 105 1895 2426 3639 -882 54 51 C ATOM 809 O LEU A 105 54.707 -2.513 2.126 1.00 19.73 O ANISOU 809 O LEU A 105 1593 2424 3477 -1147 257 201 O ATOM 810 CB LEU A 105 57.024 -2.711 -0.189 1.00 21.93 C ANISOU 810 CB LEU A 105 1909 2614 3809 -853 72 48 C ATOM 811 CG LEU A 105 56.043 -1.729 -0.832 1.00 21.61 C ANISOU 811 CG LEU A 105 2011 2296 3902 -969 8 76 C ATOM 812 CD1 LEU A 105 56.427 -0.256 -0.586 1.00 21.75 C ANISOU 812 CD1 LEU A 105 1786 2232 4245 -1651 465 379 C ATOM 813 CD2 LEU A 105 55.966 -1.995 -2.291 1.00 22.33 C ANISOU 813 CD2 LEU A 105 1956 2663 3862 -971 175 -17 C ATOM 814 N ARG A 106 55.293 -4.609 1.627 1.00 20.95 N ANISOU 814 N ARG A 106 2002 2326 3631 -821 38 10 N ATOM 815 CA ARG A 106 53.921 -5.079 1.831 1.00 22.32 C ANISOU 815 CA ARG A 106 2439 2282 3758 -782 -116 -59 C ATOM 816 C ARG A 106 53.499 -4.876 3.279 1.00 21.82 C ANISOU 816 C ARG A 106 2348 2261 3681 -670 -215 -41 C ATOM 817 O ARG A 106 52.443 -4.340 3.546 1.00 22.27 O ANISOU 817 O ARG A 106 2504 2313 3643 -383 -259 -92 O ATOM 818 CB ARG A 106 53.738 -6.538 1.371 1.00 22.57 C ANISOU 818 CB ARG A 106 2501 2292 3781 -783 -154 -124 C ATOM 819 CG ARG A 106 53.727 -6.672 -0.158 1.00 24.84 C ANISOU 819 CG ARG A 106 3150 2278 4009 -811 -11 -95 C ATOM 820 CD ARG A 106 53.763 -8.148 -0.604 1.00 24.09 C ANISOU 820 CD ARG A 106 2669 2450 4032 -1042 -32 -114 C ATOM 821 NE ARG A 106 52.577 -8.843 -0.134 1.00 24.45 N ANISOU 821 NE ARG A 106 2493 2517 4278 -1687 495 335 N ATOM 822 CZ ARG A 106 52.267 -10.115 -0.392 1.00 26.78 C ANISOU 822 CZ ARG A 106 2837 2830 4507 -1355 486 299 C ATOM 823 NH1 ARG A 106 53.073 -10.890 -1.111 1.00 25.66 N ANISOU 823 NH1 ARG A 106 2360 3222 4167 -1342 575 347 N ATOM 824 NH2 ARG A 106 51.130 -10.613 0.096 1.00 26.87 N ANISOU 824 NH2 ARG A 106 2784 2807 4617 -1718 703 518 N ATOM 825 N GLU A 107 54.351 -5.284 4.211 1.00 21.72 N ANISOU 825 N GLU A 107 2418 2170 3664 -617 -291 70 N ATOM 826 CA GLU A 107 54.119 -5.027 5.622 1.00 21.05 C ANISOU 826 CA GLU A 107 2381 2007 3609 -737 -273 197 C ATOM 827 C GLU A 107 53.892 -3.547 5.931 1.00 19.12 C ANISOU 827 C GLU A 107 2044 1868 3350 -807 -252 195 C ATOM 828 O GLU A 107 52.993 -3.204 6.687 1.00 18.35 O ANISOU 828 O GLU A 107 2002 1737 3232 -897 -133 255 O ATOM 829 CB GLU A 107 55.256 -5.595 6.449 1.00 21.20 C ANISOU 829 CB GLU A 107 2506 1910 3637 -807 -285 191 C ATOM 830 CG GLU A 107 55.083 -7.133 6.739 1.00 23.77 C ANISOU 830 CG GLU A 107 2676 2272 4081 -814 -454 295 C ATOM 831 CD GLU A 107 56.158 -7.639 7.680 1.00 25.38 C ANISOU 831 CD GLU A 107 3003 2385 4253 -881 -335 199 C ATOM 832 OE1 GLU A 107 56.990 -6.809 8.141 1.00 30.73 O ANISOU 832 OE1 GLU A 107 2938 3221 5514 -1594 -1031 56 O ATOM 833 OE2 GLU A 107 56.189 -8.846 7.962 1.00 31.69 O ANISOU 833 OE2 GLU A 107 4398 2338 5303 -909 -418 24 O ATOM 834 N LYS A 108 54.673 -2.662 5.329 1.00 17.40 N ANISOU 834 N LYS A 108 1750 1733 3126 -832 -219 337 N ATOM 835 CA LYS A 108 54.460 -1.226 5.549 1.00 17.34 C ANISOU 835 CA LYS A 108 1592 1885 3109 -866 -145 279 C ATOM 836 C LYS A 108 53.121 -0.738 4.942 1.00 16.18 C ANISOU 836 C LYS A 108 1375 1749 3021 -900 28 306 C ATOM 837 O LYS A 108 52.431 0.029 5.565 1.00 16.26 O ANISOU 837 O LYS A 108 1078 1919 3181 -970 98 297 O ATOM 838 CB LYS A 108 55.635 -0.419 5.005 1.00 16.99 C ANISOU 838 CB LYS A 108 1777 1699 2975 -999 -150 352 C ATOM 839 CG LYS A 108 56.993 -0.639 5.766 1.00 17.99 C ANISOU 839 CG LYS A 108 1658 1966 3210 -951 -126 418 C ATOM 840 CD LYS A 108 58.154 0.069 5.110 1.00 19.24 C ANISOU 840 CD LYS A 108 1946 2160 3202 -904 -194 260 C ATOM 841 CE LYS A 108 59.510 -0.179 5.828 1.00 17.65 C ANISOU 841 CE LYS A 108 1639 2222 2842 -1211 -232 341 C ATOM 842 NZ LYS A 108 60.653 0.369 5.022 1.00 21.50 N ANISOU 842 NZ LYS A 108 2713 2251 3203 -1054 -317 345 N ATOM 843 N LEU A 109 52.779 -1.157 3.731 1.00 15.51 N ANISOU 843 N LEU A 109 1230 1769 2895 -966 90 347 N ATOM 844 CA LEU A 109 51.417 -0.909 3.181 1.00 15.67 C ANISOU 844 CA LEU A 109 1278 1940 2734 -839 317 355 C ATOM 845 C LEU A 109 50.248 -1.365 4.055 1.00 15.79 C ANISOU 845 C LEU A 109 1528 1795 2674 -875 438 434 C ATOM 846 O LEU A 109 49.341 -0.587 4.285 1.00 15.01 O ANISOU 846 O LEU A 109 1409 1859 2433 -987 762 480 O ATOM 847 CB LEU A 109 51.247 -1.530 1.801 1.00 15.95 C ANISOU 847 CB LEU A 109 1215 2085 2759 -883 230 402 C ATOM 848 CG LEU A 109 52.121 -0.825 0.765 1.00 15.13 C ANISOU 848 CG LEU A 109 866 2124 2757 -1041 61 402 C ATOM 849 CD1 LEU A 109 52.332 -1.687 -0.461 1.00 16.78 C ANISOU 849 CD1 LEU A 109 763 2631 2981 -1098 1 185 C ATOM 850 CD2 LEU A 109 51.527 0.515 0.409 1.00 20.62 C ANISOU 850 CD2 LEU A 109 1620 2625 3590 -801 -196 188 C ATOM 851 N VAL A 110 50.232 -2.644 4.448 1.00 16.94 N ANISOU 851 N VAL A 110 1715 2037 2683 -909 513 431 N ATOM 852 CA VAL A 110 49.219 -3.161 5.373 1.00 16.98 C ANISOU 852 CA VAL A 110 1900 1869 2682 -905 436 334 C ATOM 853 C VAL A 110 49.098 -2.303 6.629 1.00 17.23 C ANISOU 853 C VAL A 110 1860 1904 2782 -807 388 305 C ATOM 854 O VAL A 110 47.993 -1.972 7.022 1.00 18.55 O ANISOU 854 O VAL A 110 2135 1843 3067 -605 318 164 O ATOM 855 CB VAL A 110 49.451 -4.658 5.737 1.00 16.46 C ANISOU 855 CB VAL A 110 1868 1727 2658 -967 487 344 C ATOM 856 CG1 VAL A 110 48.307 -5.168 6.656 1.00 15.66 C ANISOU 856 CG1 VAL A 110 1786 1781 2384 -939 544 246 C ATOM 857 CG2 VAL A 110 49.539 -5.493 4.461 1.00 16.63 C ANISOU 857 CG2 VAL A 110 1949 1645 2721 -1344 673 313 C ATOM 858 N ALA A 111 50.230 -1.947 7.239 1.00 17.61 N ANISOU 858 N ALA A 111 1797 2085 2807 -823 259 271 N ATOM 859 CA ALA A 111 50.236 -1.120 8.453 1.00 16.82 C ANISOU 859 CA ALA A 111 1571 2125 2692 -789 313 339 C ATOM 860 C ALA A 111 49.654 0.278 8.206 1.00 16.34 C ANISOU 860 C ALA A 111 1483 2076 2649 -793 280 384 C ATOM 861 O ALA A 111 49.006 0.847 9.060 1.00 15.61 O ANISOU 861 O ALA A 111 1346 1973 2610 -794 282 405 O ATOM 862 CB ALA A 111 51.679 -1.020 9.046 1.00 18.04 C ANISOU 862 CB ALA A 111 1828 2245 2782 -787 218 329 C ATOM 863 N ALA A 112 49.900 0.831 7.031 1.00 16.30 N ANISOU 863 N ALA A 112 1400 2137 2654 -769 207 444 N ATOM 864 CA ALA A 112 49.367 2.146 6.667 1.00 15.32 C ANISOU 864 CA ALA A 112 1331 1891 2599 -874 275 364 C ATOM 865 C ALA A 112 47.827 2.058 6.577 1.00 15.49 C ANISOU 865 C ALA A 112 1501 1896 2488 -873 339 361 C ATOM 866 O ALA A 112 47.090 2.857 7.145 1.00 16.11 O ANISOU 866 O ALA A 112 1577 1725 2817 -892 431 408 O ATOM 867 CB ALA A 112 49.931 2.537 5.351 1.00 15.68 C ANISOU 867 CB ALA A 112 1498 1946 2513 -708 213 404 C ATOM 868 N TYR A 113 47.339 1.075 5.863 1.00 14.15 N ANISOU 868 N TYR A 113 1387 1646 2343 -1140 326 279 N ATOM 869 CA TYR A 113 45.875 0.919 5.738 1.00 15.24 C ANISOU 869 CA TYR A 113 1807 1670 2313 -1197 233 292 C ATOM 870 C TYR A 113 45.249 0.620 7.102 1.00 15.31 C ANISOU 870 C TYR A 113 1885 1601 2329 -1150 189 357 C ATOM 871 O TYR A 113 44.194 1.121 7.439 1.00 16.78 O ANISOU 871 O TYR A 113 2266 1818 2291 -1086 175 357 O ATOM 872 CB TYR A 113 45.563 -0.155 4.701 1.00 14.76 C ANISOU 872 CB TYR A 113 1736 1717 2155 -1300 286 343 C ATOM 873 CG TYR A 113 45.628 0.349 3.293 1.00 15.31 C ANISOU 873 CG TYR A 113 2014 1495 2307 -1391 223 360 C ATOM 874 CD1 TYR A 113 44.624 1.171 2.782 1.00 15.18 C ANISOU 874 CD1 TYR A 113 2096 1577 2093 -1552 -30 198 C ATOM 875 CD2 TYR A 113 46.686 -0.005 2.465 1.00 17.19 C ANISOU 875 CD2 TYR A 113 2342 1815 2374 -1665 49 358 C ATOM 876 CE1 TYR A 113 44.678 1.645 1.488 1.00 15.88 C ANISOU 876 CE1 TYR A 113 2389 1711 1932 -1397 -20 151 C ATOM 877 CE2 TYR A 113 46.771 0.479 1.149 1.00 16.71 C ANISOU 877 CE2 TYR A 113 2477 1735 2136 -1608 47 615 C ATOM 878 CZ TYR A 113 45.755 1.302 0.672 1.00 15.67 C ANISOU 878 CZ TYR A 113 1876 1827 2250 -1422 105 565 C ATOM 879 OH TYR A 113 45.793 1.744 -0.631 1.00 16.87 O ANISOU 879 OH TYR A 113 1934 2072 2400 -1523 292 695 O ATOM 880 N LYS A 114 45.927 -0.171 7.917 1.00 16.73 N ANISOU 880 N LYS A 114 2158 1704 2491 -1121 161 352 N ATOM 881 CA LYS A 114 45.404 -0.493 9.227 1.00 15.34 C ANISOU 881 CA LYS A 114 2071 1380 2377 -1253 297 523 C ATOM 882 C LYS A 114 45.247 0.750 10.094 1.00 16.21 C ANISOU 882 C LYS A 114 2167 1506 2483 -1092 284 581 C ATOM 883 O LYS A 114 44.322 0.854 10.908 1.00 16.21 O ANISOU 883 O LYS A 114 2192 1411 2555 -1245 291 712 O ATOM 884 CB LYS A 114 46.252 -1.564 9.922 1.00 15.31 C ANISOU 884 CB LYS A 114 2013 1377 2426 -1302 230 417 C ATOM 885 CG LYS A 114 45.734 -2.989 9.641 1.00 17.45 C ANISOU 885 CG LYS A 114 2825 1138 2665 -1166 148 729 C ATOM 886 CD LYS A 114 46.608 -4.002 10.363 1.00 23.51 C ANISOU 886 CD LYS A 114 3743 1614 3575 -1402 596 694 C ATOM 887 CE LYS A 114 46.535 -5.344 9.690 1.00 25.42 C ANISOU 887 CE LYS A 114 4035 1841 3780 -1489 883 813 C ATOM 888 NZ LYS A 114 45.660 -6.273 10.436 1.00 26.71 N ANISOU 888 NZ LYS A 114 3391 2701 4055 -1835 1546 1004 N ATOM 889 N SER A 115 46.138 1.695 9.866 1.00 16.15 N ANISOU 889 N SER A 115 2093 1546 2497 -1166 304 565 N ATOM 890 CA SER A 115 46.198 2.993 10.552 1.00 16.59 C ANISOU 890 CA SER A 115 2200 1748 2356 -1047 387 497 C ATOM 891 C SER A 115 45.120 3.984 10.099 1.00 16.43 C ANISOU 891 C SER A 115 2136 1762 2345 -1106 466 450 C ATOM 892 O SER A 115 44.887 4.978 10.759 1.00 16.46 O ANISOU 892 O SER A 115 2050 1813 2389 -1142 616 419 O ATOM 893 CB SER A 115 47.617 3.581 10.455 1.00 17.31 C ANISOU 893 CB SER A 115 2426 1770 2379 -1032 304 567 C ATOM 894 OG SER A 115 47.827 4.442 9.337 1.00 18.29 O ANISOU 894 OG SER A 115 2245 1881 2823 -1216 513 571 O ATOM 895 N VAL A 116 44.463 3.689 8.981 1.00 16.20 N ANISOU 895 N VAL A 116 1944 1890 2319 -1153 446 507 N ATOM 896 CA VAL A 116 43.294 4.417 8.496 1.00 16.23 C ANISOU 896 CA VAL A 116 2068 1839 2259 -1224 527 558 C ATOM 897 C VAL A 116 42.172 4.438 9.542 1.00 16.33 C ANISOU 897 C VAL A 116 2051 1788 2366 -1346 418 514 C ATOM 898 O VAL A 116 41.468 5.435 9.721 1.00 17.06 O ANISOU 898 O VAL A 116 1932 1879 2668 -1462 462 495 O ATOM 899 CB VAL A 116 42.801 3.804 7.121 1.00 15.46 C ANISOU 899 CB VAL A 116 1889 1755 2229 -1261 457 503 C ATOM 900 CG1 VAL A 116 41.398 4.220 6.769 1.00 16.49 C ANISOU 900 CG1 VAL A 116 1955 1838 2470 -1320 542 561 C ATOM 901 CG2 VAL A 116 43.760 4.214 5.978 1.00 15.12 C ANISOU 901 CG2 VAL A 116 1865 1998 1881 -1221 610 607 C ATOM 902 N LEU A 117 42.035 3.341 10.257 1.00 16.91 N ANISOU 902 N LEU A 117 2319 1826 2277 -1345 407 571 N ATOM 903 CA LEU A 117 40.928 3.182 11.195 1.00 16.46 C ANISOU 903 CA LEU A 117 2245 1831 2178 -1414 367 542 C ATOM 904 C LEU A 117 40.968 4.177 12.341 1.00 16.88 C ANISOU 904 C LEU A 117 2303 2012 2096 -1340 308 575 C ATOM 905 O LEU A 117 42.040 4.476 12.885 1.00 16.77 O ANISOU 905 O LEU A 117 2095 2203 2073 -1510 233 619 O ATOM 906 CB LEU A 117 40.935 1.788 11.718 1.00 17.11 C ANISOU 906 CB LEU A 117 2348 1801 2350 -1515 351 632 C ATOM 907 CG LEU A 117 40.288 0.799 10.755 1.00 17.43 C ANISOU 907 CG LEU A 117 2745 1840 2037 -1638 510 549 C ATOM 908 CD1 LEU A 117 41.205 0.411 9.669 1.00 25.62 C ANISOU 908 CD1 LEU A 117 3991 2249 3494 -1687 224 586 C ATOM 909 CD2 LEU A 117 40.019 -0.378 11.622 1.00 20.87 C ANISOU 909 CD2 LEU A 117 3103 2035 2792 -2073 155 719 C ATOM 910 N VAL A 118 39.806 4.737 12.651 1.00 16.38 N ANISOU 910 N VAL A 118 2229 1917 2077 -1312 307 529 N ATOM 911 CA VAL A 118 39.691 5.784 13.677 1.00 18.37 C ANISOU 911 CA VAL A 118 2417 2276 2286 -1062 274 523 C ATOM 912 C VAL A 118 38.554 5.377 14.602 1.00 18.14 C ANISOU 912 C VAL A 118 2388 2281 2220 -1095 286 568 C ATOM 913 O VAL A 118 37.461 5.059 14.137 1.00 19.73 O ANISOU 913 O VAL A 118 2796 2361 2340 -961 89 605 O ATOM 914 CB VAL A 118 39.467 7.207 13.038 1.00 16.69 C ANISOU 914 CB VAL A 118 2230 1987 2123 -1236 361 504 C ATOM 915 CG1 VAL A 118 39.222 8.298 14.121 1.00 17.06 C ANISOU 915 CG1 VAL A 118 1823 2347 2310 -1200 466 444 C ATOM 916 CG2 VAL A 118 40.653 7.600 12.139 1.00 21.19 C ANISOU 916 CG2 VAL A 118 2791 2668 2590 -773 403 451 C ATOM 917 N GLY A 119 38.779 5.355 15.912 1.00 19.65 N ANISOU 917 N GLY A 119 2483 2468 2514 -1047 320 640 N ATOM 918 CA GLY A 119 37.706 4.892 16.809 1.00 20.43 C ANISOU 918 CA GLY A 119 2571 2640 2549 -1132 459 565 C ATOM 919 C GLY A 119 36.452 5.738 16.718 1.00 20.71 C ANISOU 919 C GLY A 119 2512 2691 2663 -1202 386 586 C ATOM 920 O GLY A 119 36.511 6.931 16.824 1.00 22.18 O ANISOU 920 O GLY A 119 2691 2835 2900 -1223 387 413 O ATOM 921 N GLY A 120 35.285 5.138 16.528 1.00 21.58 N ANISOU 921 N GLY A 120 2595 2841 2760 -1161 492 560 N ATOM 922 CA GLY A 120 34.080 5.949 16.376 1.00 21.38 C ANISOU 922 CA GLY A 120 2454 2868 2799 -1084 536 554 C ATOM 923 C GLY A 120 33.749 6.341 14.949 1.00 21.43 C ANISOU 923 C GLY A 120 2385 2926 2832 -999 563 487 C ATOM 924 O GLY A 120 32.875 7.181 14.721 1.00 24.16 O ANISOU 924 O GLY A 120 2818 3343 3017 -863 556 460 O ATOM 925 N VAL A 121 34.437 5.752 13.978 1.00 20.09 N ANISOU 925 N VAL A 121 2028 2750 2853 -1210 608 489 N ATOM 926 CA VAL A 121 34.209 6.071 12.574 1.00 17.78 C ANISOU 926 CA VAL A 121 1757 2356 2643 -1306 661 530 C ATOM 927 C VAL A 121 33.977 4.738 11.887 1.00 17.02 C ANISOU 927 C VAL A 121 1605 2208 2651 -1345 610 536 C ATOM 928 O VAL A 121 34.786 3.825 12.028 1.00 17.56 O ANISOU 928 O VAL A 121 1701 2314 2655 -1343 622 591 O ATOM 929 CB VAL A 121 35.482 6.713 11.908 1.00 17.24 C ANISOU 929 CB VAL A 121 1707 2135 2706 -1385 670 457 C ATOM 930 CG1 VAL A 121 35.318 6.731 10.398 1.00 16.27 C ANISOU 930 CG1 VAL A 121 1752 1949 2478 -1121 697 755 C ATOM 931 CG2 VAL A 121 35.752 8.150 12.435 1.00 18.15 C ANISOU 931 CG2 VAL A 121 1817 2254 2823 -1374 811 593 C ATOM 932 N VAL A 122 32.874 4.610 11.151 1.00 16.61 N ANISOU 932 N VAL A 122 1675 2089 2547 -1374 575 465 N ATOM 933 CA VAL A 122 32.611 3.367 10.482 1.00 16.62 C ANISOU 933 CA VAL A 122 1510 2149 2654 -1416 402 373 C ATOM 934 C VAL A 122 32.672 3.501 8.984 1.00 16.41 C ANISOU 934 C VAL A 122 1442 2153 2637 -1372 372 416 C ATOM 935 O VAL A 122 32.864 2.506 8.295 1.00 16.99 O ANISOU 935 O VAL A 122 1538 2044 2872 -1401 230 316 O ATOM 936 CB VAL A 122 31.236 2.844 10.862 1.00 16.60 C ANISOU 936 CB VAL A 122 1617 2130 2561 -1420 504 393 C ATOM 937 CG1 VAL A 122 31.171 2.604 12.388 1.00 18.42 C ANISOU 937 CG1 VAL A 122 1972 2128 2898 -1666 343 173 C ATOM 938 CG2 VAL A 122 30.173 3.831 10.400 1.00 17.36 C ANISOU 938 CG2 VAL A 122 1596 2199 2798 -1515 243 493 C ATOM 939 N ASN A 123 32.531 4.721 8.465 1.00 16.87 N ANISOU 939 N ASN A 123 1453 2263 2692 -1306 252 409 N ATOM 940 CA ASN A 123 32.612 4.950 7.015 1.00 15.85 C ANISOU 940 CA ASN A 123 1414 2302 2305 -1319 440 517 C ATOM 941 C ASN A 123 33.899 5.680 6.614 1.00 15.39 C ANISOU 941 C ASN A 123 1302 2257 2286 -1311 296 473 C ATOM 942 O ASN A 123 34.257 6.680 7.222 1.00 15.49 O ANISOU 942 O ASN A 123 1475 2197 2213 -1211 593 527 O ATOM 943 CB ASN A 123 31.414 5.754 6.537 1.00 15.75 C ANISOU 943 CB ASN A 123 1369 2281 2334 -1344 314 524 C ATOM 944 CG ASN A 123 30.058 5.102 6.934 1.00 16.95 C ANISOU 944 CG ASN A 123 1324 2790 2326 -1311 645 443 C ATOM 945 OD1 ASN A 123 29.937 3.882 6.910 1.00 17.97 O ANISOU 945 OD1 ASN A 123 1709 2805 2314 -1586 731 384 O ATOM 946 ND2 ASN A 123 29.059 5.933 7.228 1.00 16.77 N ANISOU 946 ND2 ASN A 123 1445 2640 2284 -1535 619 38 N ATOM 947 N TYR A 124 34.552 5.198 5.573 1.00 14.97 N ANISOU 947 N TYR A 124 1335 2220 2131 -1296 284 523 N ATOM 948 CA TYR A 124 35.857 5.763 5.152 1.00 15.39 C ANISOU 948 CA TYR A 124 1549 2178 2121 -1297 348 608 C ATOM 949 C TYR A 124 35.926 6.023 3.675 1.00 15.01 C ANISOU 949 C TYR A 124 1590 2194 1920 -1341 301 673 C ATOM 950 O TYR A 124 35.426 5.232 2.874 1.00 15.86 O ANISOU 950 O TYR A 124 1757 2244 2023 -1421 388 673 O ATOM 951 CB TYR A 124 37.008 4.833 5.537 1.00 15.06 C ANISOU 951 CB TYR A 124 1462 2198 2059 -1321 225 694 C ATOM 952 CG TYR A 124 37.149 4.599 7.017 1.00 16.61 C ANISOU 952 CG TYR A 124 1740 2313 2256 -1250 158 651 C ATOM 953 CD1 TYR A 124 38.065 5.342 7.757 1.00 13.87 C ANISOU 953 CD1 TYR A 124 1503 1889 1876 -1365 -102 594 C ATOM 954 CD2 TYR A 124 36.356 3.636 7.684 1.00 16.14 C ANISOU 954 CD2 TYR A 124 1785 2094 2253 -1132 90 704 C ATOM 955 CE1 TYR A 124 38.224 5.134 9.110 1.00 14.34 C ANISOU 955 CE1 TYR A 124 1462 1815 2169 -1158 375 543 C ATOM 956 CE2 TYR A 124 36.482 3.431 9.050 1.00 14.92 C ANISOU 956 CE2 TYR A 124 1635 2032 2001 -1206 225 669 C ATOM 957 CZ TYR A 124 37.433 4.196 9.762 1.00 15.60 C ANISOU 957 CZ TYR A 124 1886 1921 2120 -1484 69 707 C ATOM 958 OH TYR A 124 37.610 4.020 11.125 1.00 17.12 O ANISOU 958 OH TYR A 124 2230 2051 2223 -1485 107 779 O ATOM 959 N VAL A 125 36.618 7.100 3.293 1.00 14.85 N ANISOU 959 N VAL A 125 1469 2096 2078 -1260 176 547 N ATOM 960 CA VAL A 125 36.831 7.371 1.870 1.00 14.10 C ANISOU 960 CA VAL A 125 1224 2193 1940 -1136 297 638 C ATOM 961 C VAL A 125 38.345 7.351 1.684 1.00 15.29 C ANISOU 961 C VAL A 125 1279 2184 2345 -1109 209 551 C ATOM 962 O VAL A 125 39.048 8.216 2.205 1.00 15.43 O ANISOU 962 O VAL A 125 1093 2141 2626 -1209 52 518 O ATOM 963 CB VAL A 125 36.197 8.730 1.414 1.00 14.15 C ANISOU 963 CB VAL A 125 1235 2256 1884 -1126 267 615 C ATOM 964 CG1 VAL A 125 36.588 9.101 -0.038 1.00 13.74 C ANISOU 964 CG1 VAL A 125 1297 2634 1288 -1127 298 728 C ATOM 965 CG2 VAL A 125 34.694 8.676 1.457 1.00 14.79 C ANISOU 965 CG2 VAL A 125 1306 2422 1889 -1285 183 757 C ATOM 966 N VAL A 126 38.810 6.360 0.922 1.00 14.62 N ANISOU 966 N VAL A 126 1130 2143 2283 -1070 400 549 N ATOM 967 CA VAL A 126 40.215 5.928 0.926 1.00 15.07 C ANISOU 967 CA VAL A 126 1170 2304 2250 -1007 326 529 C ATOM 968 C VAL A 126 40.813 6.045 -0.482 1.00 15.08 C ANISOU 968 C VAL A 126 1110 2288 2330 -1136 306 612 C ATOM 969 O VAL A 126 40.222 5.504 -1.462 1.00 15.07 O ANISOU 969 O VAL A 126 869 2513 2340 -1070 239 476 O ATOM 970 CB VAL A 126 40.316 4.451 1.390 1.00 14.57 C ANISOU 970 CB VAL A 126 1106 2302 2127 -1086 364 604 C ATOM 971 CG1 VAL A 126 41.735 4.051 1.689 1.00 14.98 C ANISOU 971 CG1 VAL A 126 1292 2416 1981 -846 649 762 C ATOM 972 CG2 VAL A 126 39.452 4.204 2.638 1.00 15.69 C ANISOU 972 CG2 VAL A 126 1252 2605 2103 -1056 550 418 C ATOM 973 N PRO A 127 42.006 6.697 -0.600 1.00 15.78 N ANISOU 973 N PRO A 127 1190 2331 2472 -1112 178 549 N ATOM 974 CA PRO A 127 42.710 6.688 -1.871 1.00 15.56 C ANISOU 974 CA PRO A 127 1290 2155 2465 -1173 220 586 C ATOM 975 C PRO A 127 43.632 5.455 -1.973 1.00 15.55 C ANISOU 975 C PRO A 127 1343 2069 2496 -1103 121 565 C ATOM 976 O PRO A 127 43.771 4.706 -1.007 1.00 15.23 O ANISOU 976 O PRO A 127 1486 1807 2494 -1131 63 767 O ATOM 977 CB PRO A 127 43.586 7.958 -1.797 1.00 15.54 C ANISOU 977 CB PRO A 127 1292 2068 2542 -1241 70 551 C ATOM 978 CG PRO A 127 43.980 8.028 -0.350 1.00 15.30 C ANISOU 978 CG PRO A 127 1107 2371 2334 -1126 420 534 C ATOM 979 CD PRO A 127 42.726 7.496 0.420 1.00 15.68 C ANISOU 979 CD PRO A 127 1184 2263 2508 -1251 213 566 C ATOM 980 N VAL A 128 44.253 5.251 -3.129 1.00 16.11 N ANISOU 980 N VAL A 128 1470 2085 2564 -1082 86 508 N ATOM 981 CA VAL A 128 45.250 4.181 -3.285 1.00 15.86 C ANISOU 981 CA VAL A 128 1518 2074 2435 -1099 133 394 C ATOM 982 C VAL A 128 46.527 4.693 -2.697 1.00 15.11 C ANISOU 982 C VAL A 128 1316 2052 2372 -1144 206 406 C ATOM 983 O VAL A 128 47.314 5.400 -3.350 1.00 14.79 O ANISOU 983 O VAL A 128 1606 1807 2206 -1305 331 420 O ATOM 984 CB VAL A 128 45.401 3.691 -4.742 1.00 16.94 C ANISOU 984 CB VAL A 128 1482 2295 2658 -1021 141 349 C ATOM 985 CG1 VAL A 128 46.390 2.543 -4.813 1.00 16.30 C ANISOU 985 CG1 VAL A 128 1641 2114 2437 -1020 187 200 C ATOM 986 CG2 VAL A 128 44.005 3.208 -5.267 1.00 16.31 C ANISOU 986 CG2 VAL A 128 1412 1978 2805 -1408 -19 205 C ATOM 987 N LEU A 129 46.757 4.351 -1.444 1.00 14.76 N ANISOU 987 N LEU A 129 1189 1999 2417 -1205 179 414 N ATOM 988 CA LEU A 129 47.923 4.896 -0.743 1.00 16.08 C ANISOU 988 CA LEU A 129 1520 2052 2535 -1135 114 402 C ATOM 989 C LEU A 129 49.198 4.578 -1.512 1.00 16.76 C ANISOU 989 C LEU A 129 1546 2222 2599 -1103 123 369 C ATOM 990 O LEU A 129 49.330 3.507 -2.159 1.00 16.97 O ANISOU 990 O LEU A 129 1544 2250 2650 -1162 167 421 O ATOM 991 CB LEU A 129 47.987 4.350 0.687 1.00 17.89 C ANISOU 991 CB LEU A 129 1870 2339 2588 -961 -70 285 C ATOM 992 CG LEU A 129 46.933 4.792 1.722 1.00 15.91 C ANISOU 992 CG LEU A 129 1442 1999 2603 -1354 46 473 C ATOM 993 CD1 LEU A 129 47.190 4.124 3.023 1.00 15.66 C ANISOU 993 CD1 LEU A 129 1597 1797 2553 -1405 -287 712 C ATOM 994 CD2 LEU A 129 47.089 6.383 1.886 1.00 17.97 C ANISOU 994 CD2 LEU A 129 2102 1736 2988 -1652 -393 471 C ATOM 995 N SER A 130 50.127 5.520 -1.458 1.00 15.99 N ANISOU 995 N SER A 130 1375 2160 2540 -1127 208 452 N ATOM 996 CA SER A 130 51.489 5.371 -2.028 1.00 17.94 C ANISOU 996 CA SER A 130 1666 2437 2713 -981 202 466 C ATOM 997 C SER A 130 51.568 5.270 -3.553 1.00 18.42 C ANISOU 997 C SER A 130 1778 2414 2805 -987 200 424 C ATOM 998 O SER A 130 52.661 5.148 -4.086 1.00 17.71 O ANISOU 998 O SER A 130 1729 2170 2828 -1172 374 547 O ATOM 999 CB SER A 130 52.209 4.168 -1.386 1.00 16.54 C ANISOU 999 CB SER A 130 1319 2343 2620 -1072 269 537 C ATOM 1000 OG SER A 130 52.370 4.404 -0.006 1.00 16.53 O ANISOU 1000 OG SER A 130 1257 2389 2632 -1125 158 838 O ATOM 1001 N SER A 131 50.421 5.326 -4.246 1.00 18.76 N ANISOU 1001 N SER A 131 1805 2407 2913 -1074 121 273 N ATOM 1002 CA SER A 131 50.411 5.154 -5.716 1.00 19.95 C ANISOU 1002 CA SER A 131 1993 2579 3006 -1004 104 168 C ATOM 1003 C SER A 131 50.552 6.433 -6.565 1.00 20.63 C ANISOU 1003 C SER A 131 2028 2667 3141 -1074 167 116 C ATOM 1004 O SER A 131 50.565 6.357 -7.800 1.00 21.13 O ANISOU 1004 O SER A 131 2127 2658 3242 -1186 203 55 O ATOM 1005 CB SER A 131 49.145 4.440 -6.147 1.00 19.47 C ANISOU 1005 CB SER A 131 1814 2646 2938 -919 44 116 C ATOM 1006 OG SER A 131 48.065 5.318 -5.973 1.00 20.25 O ANISOU 1006 OG SER A 131 1982 3080 2632 -776 -64 116 O ATOM 1007 N GLY A 132 50.601 7.602 -5.932 1.00 20.62 N ANISOU 1007 N GLY A 132 2161 2494 3177 -1140 119 -27 N ATOM 1008 CA GLY A 132 50.954 8.821 -6.682 1.00 22.44 C ANISOU 1008 CA GLY A 132 2278 2837 3409 -1078 198 45 C ATOM 1009 C GLY A 132 52.444 9.142 -6.668 1.00 22.93 C ANISOU 1009 C GLY A 132 2376 2827 3509 -1013 140 -38 C ATOM 1010 O GLY A 132 53.261 8.390 -7.215 1.00 23.40 O ANISOU 1010 O GLY A 132 2190 3113 3585 -1092 324 80 O ATOM 1011 N ILE A 133 52.793 10.261 -6.023 1.00 23.46 N ANISOU 1011 N ILE A 133 2440 2830 3641 -1045 175 57 N ATOM 1012 CA ILE A 133 54.189 10.708 -5.897 1.00 22.75 C ANISOU 1012 CA ILE A 133 2427 2628 3587 -1107 210 47 C ATOM 1013 C ILE A 133 55.090 9.617 -5.289 1.00 21.39 C ANISOU 1013 C ILE A 133 2342 2405 3380 -1056 243 136 C ATOM 1014 O ILE A 133 56.259 9.487 -5.668 1.00 19.89 O ANISOU 1014 O ILE A 133 2060 2246 3250 -1257 358 266 O ATOM 1015 CB ILE A 133 54.330 12.076 -5.109 1.00 23.03 C ANISOU 1015 CB ILE A 133 2516 2638 3593 -1062 277 55 C ATOM 1016 CG1 ILE A 133 55.778 12.551 -5.123 1.00 23.00 C ANISOU 1016 CG1 ILE A 133 2383 2507 3848 -1110 230 -97 C ATOM 1017 CG2 ILE A 133 53.792 11.981 -3.653 1.00 22.93 C ANISOU 1017 CG2 ILE A 133 2670 2597 3444 -1199 274 39 C ATOM 1018 CD1 ILE A 133 55.981 13.929 -4.555 1.00 23.94 C ANISOU 1018 CD1 ILE A 133 2578 2744 3773 -1181 242 54 C ATOM 1019 N PHE A 134 54.539 8.836 -4.366 1.00 19.89 N ANISOU 1019 N PHE A 134 2036 2328 3193 -1205 429 235 N ATOM 1020 CA PHE A 134 55.299 7.780 -3.665 1.00 19.27 C ANISOU 1020 CA PHE A 134 2128 2153 3039 -1028 435 294 C ATOM 1021 C PHE A 134 55.729 6.585 -4.531 1.00 19.39 C ANISOU 1021 C PHE A 134 2073 2201 3092 -1061 409 348 C ATOM 1022 O PHE A 134 56.615 5.813 -4.154 1.00 19.19 O ANISOU 1022 O PHE A 134 2059 2051 3179 -1073 374 367 O ATOM 1023 CB PHE A 134 54.544 7.350 -2.376 1.00 19.83 C ANISOU 1023 CB PHE A 134 2255 2143 3135 -931 429 189 C ATOM 1024 CG PHE A 134 54.691 8.342 -1.249 1.00 21.01 C ANISOU 1024 CG PHE A 134 2504 2437 3040 -799 443 227 C ATOM 1025 CD1 PHE A 134 55.346 9.561 -1.472 1.00 21.52 C ANISOU 1025 CD1 PHE A 134 2689 2134 3351 -945 425 249 C ATOM 1026 CD2 PHE A 134 54.202 8.079 0.026 1.00 18.66 C ANISOU 1026 CD2 PHE A 134 1916 2515 2658 -756 976 -95 C ATOM 1027 CE1 PHE A 134 55.486 10.514 -0.440 1.00 20.74 C ANISOU 1027 CE1 PHE A 134 2777 2372 2730 -1028 552 137 C ATOM 1028 CE2 PHE A 134 54.349 9.038 1.056 1.00 19.99 C ANISOU 1028 CE2 PHE A 134 2371 2209 3014 -1161 777 -31 C ATOM 1029 CZ PHE A 134 54.977 10.249 0.814 1.00 22.67 C ANISOU 1029 CZ PHE A 134 2784 2592 3234 -782 546 136 C ATOM 1030 N GLY A 135 55.087 6.430 -5.684 1.00 19.79 N ANISOU 1030 N GLY A 135 2190 2299 3029 -992 424 401 N ATOM 1031 CA GLY A 135 55.554 5.535 -6.741 1.00 18.99 C ANISOU 1031 CA GLY A 135 2063 2227 2926 -881 504 338 C ATOM 1032 C GLY A 135 55.387 4.037 -6.607 1.00 19.90 C ANISOU 1032 C GLY A 135 2179 2419 2964 -824 469 382 C ATOM 1033 O GLY A 135 56.020 3.277 -7.353 1.00 20.55 O ANISOU 1033 O GLY A 135 2314 2379 3113 -789 550 302 O ATOM 1034 N VAL A 136 54.508 3.607 -5.695 1.00 19.49 N ANISOU 1034 N VAL A 136 2206 2313 2883 -920 404 427 N ATOM 1035 CA VAL A 136 54.212 2.190 -5.488 1.00 18.65 C ANISOU 1035 CA VAL A 136 2100 2228 2758 -889 321 495 C ATOM 1036 C VAL A 136 53.154 1.700 -6.483 1.00 18.00 C ANISOU 1036 C VAL A 136 2018 2112 2711 -1000 459 481 C ATOM 1037 O VAL A 136 52.204 2.401 -6.767 1.00 18.25 O ANISOU 1037 O VAL A 136 1958 2326 2650 -1182 564 609 O ATOM 1038 CB VAL A 136 53.752 1.932 -4.039 1.00 18.50 C ANISOU 1038 CB VAL A 136 1999 2194 2833 -965 216 510 C ATOM 1039 CG1 VAL A 136 53.440 0.430 -3.834 1.00 17.04 C ANISOU 1039 CG1 VAL A 136 1720 2100 2651 -946 189 652 C ATOM 1040 CG2 VAL A 136 54.828 2.457 -3.055 1.00 19.98 C ANISOU 1040 CG2 VAL A 136 2561 2281 2748 -514 -80 525 C ATOM 1041 N ASP A 137 53.339 0.491 -6.995 1.00 18.80 N ANISOU 1041 N ASP A 137 2135 2224 2781 -994 452 328 N ATOM 1042 CA ASP A 137 52.404 -0.164 -7.898 1.00 18.05 C ANISOU 1042 CA ASP A 137 1938 1949 2968 -1114 481 195 C ATOM 1043 C ASP A 137 50.992 -0.203 -7.273 1.00 18.06 C ANISOU 1043 C ASP A 137 2035 1933 2893 -1035 408 65 C ATOM 1044 O ASP A 137 50.808 -0.687 -6.156 1.00 18.81 O ANISOU 1044 O ASP A 137 2154 1751 3240 -1095 434 132 O ATOM 1045 CB ASP A 137 52.963 -1.579 -8.214 1.00 18.05 C ANISOU 1045 CB ASP A 137 1794 2066 2995 -1055 590 202 C ATOM 1046 CG ASP A 137 52.034 -2.420 -9.088 1.00 19.40 C ANISOU 1046 CG ASP A 137 2007 2013 3349 -929 380 228 C ATOM 1047 OD1 ASP A 137 50.983 -1.923 -9.503 1.00 21.39 O ANISOU 1047 OD1 ASP A 137 1949 2220 3956 -1377 86 548 O ATOM 1048 OD2 ASP A 137 52.355 -3.592 -9.380 1.00 24.23 O ANISOU 1048 OD2 ASP A 137 2794 2678 3734 -1059 338 330 O ATOM 1049 N PHE A 138 50.011 0.372 -7.960 1.00 17.45 N ANISOU 1049 N PHE A 138 1840 1984 2805 -1128 322 -83 N ATOM 1050 CA PHE A 138 48.650 0.457 -7.411 1.00 17.13 C ANISOU 1050 CA PHE A 138 1820 1964 2723 -1286 241 -102 C ATOM 1051 C PHE A 138 48.094 -0.899 -7.073 1.00 17.13 C ANISOU 1051 C PHE A 138 1732 1975 2802 -1212 229 -119 C ATOM 1052 O PHE A 138 47.276 -1.018 -6.184 1.00 17.24 O ANISOU 1052 O PHE A 138 1810 2007 2732 -1355 304 -58 O ATOM 1053 CB PHE A 138 47.690 1.208 -8.353 1.00 17.23 C ANISOU 1053 CB PHE A 138 1777 2067 2702 -1276 232 -80 C ATOM 1054 CG PHE A 138 47.417 0.480 -9.668 1.00 17.31 C ANISOU 1054 CG PHE A 138 1916 2104 2556 -1371 72 3 C ATOM 1055 CD1 PHE A 138 46.304 -0.362 -9.795 1.00 18.08 C ANISOU 1055 CD1 PHE A 138 2174 2185 2509 -1611 34 0 C ATOM 1056 CD2 PHE A 138 48.247 0.682 -10.776 1.00 17.65 C ANISOU 1056 CD2 PHE A 138 1980 2237 2487 -1283 105 -194 C ATOM 1057 CE1 PHE A 138 46.034 -1.042 -11.008 1.00 17.91 C ANISOU 1057 CE1 PHE A 138 1911 2433 2458 -1755 478 307 C ATOM 1058 CE2 PHE A 138 47.986 0.035 -11.995 1.00 19.60 C ANISOU 1058 CE2 PHE A 138 1852 2691 2901 -1474 124 123 C ATOM 1059 CZ PHE A 138 46.874 -0.842 -12.108 1.00 20.93 C ANISOU 1059 CZ PHE A 138 2472 2638 2841 -1257 74 63 C ATOM 1060 N LYS A 139 48.530 -1.924 -7.788 1.00 16.72 N ANISOU 1060 N LYS A 139 1640 1878 2833 -1272 88 -202 N ATOM 1061 CA LYS A 139 48.031 -3.257 -7.505 1.00 17.23 C ANISOU 1061 CA LYS A 139 1539 1975 3032 -1412 176 -152 C ATOM 1062 C LYS A 139 48.410 -3.800 -6.110 1.00 16.57 C ANISOU 1062 C LYS A 139 1431 1867 2997 -1246 65 -165 C ATOM 1063 O LYS A 139 47.553 -4.369 -5.405 1.00 18.18 O ANISOU 1063 O LYS A 139 1744 2075 3088 -1076 65 -169 O ATOM 1064 CB LYS A 139 48.451 -4.231 -8.604 1.00 16.64 C ANISOU 1064 CB LYS A 139 1483 1910 2929 -1424 114 -273 C ATOM 1065 CG LYS A 139 47.944 -3.857 -10.003 1.00 17.95 C ANISOU 1065 CG LYS A 139 1740 2029 3051 -1624 218 -182 C ATOM 1066 CD LYS A 139 48.240 -4.996 -10.997 1.00 19.71 C ANISOU 1066 CD LYS A 139 1968 2384 3136 -1633 223 -185 C ATOM 1067 CE LYS A 139 47.615 -4.685 -12.359 1.00 24.31 C ANISOU 1067 CE LYS A 139 2825 2956 3453 -1938 328 -366 C ATOM 1068 NZ LYS A 139 47.565 -5.886 -13.275 1.00 27.63 N ANISOU 1068 NZ LYS A 139 3358 3558 3582 -1679 765 -197 N ATOM 1069 N ILE A 140 49.676 -3.667 -5.735 1.00 17.46 N ANISOU 1069 N ILE A 140 1541 1927 3165 -1131 -8 -90 N ATOM 1070 CA ILE A 140 50.167 -4.065 -4.413 1.00 17.87 C ANISOU 1070 CA ILE A 140 1480 1895 3415 -1029 -103 86 C ATOM 1071 C ILE A 140 49.542 -3.221 -3.299 1.00 17.27 C ANISOU 1071 C ILE A 140 1422 1736 3403 -1033 -129 102 C ATOM 1072 O ILE A 140 49.254 -3.741 -2.209 1.00 16.60 O ANISOU 1072 O ILE A 140 1274 1555 3476 -1151 -157 280 O ATOM 1073 CB ILE A 140 51.718 -3.935 -4.313 1.00 18.57 C ANISOU 1073 CB ILE A 140 1663 1951 3438 -962 -155 87 C ATOM 1074 CG1 ILE A 140 52.391 -4.696 -5.459 1.00 20.86 C ANISOU 1074 CG1 ILE A 140 1752 2240 3932 -785 -128 146 C ATOM 1075 CG2 ILE A 140 52.216 -4.441 -2.968 1.00 20.51 C ANISOU 1075 CG2 ILE A 140 1676 2452 3662 -911 -295 -12 C ATOM 1076 CD1 ILE A 140 53.856 -4.397 -5.630 1.00 24.14 C ANISOU 1076 CD1 ILE A 140 2572 2309 4289 -801 -355 298 C ATOM 1077 N SER A 141 49.347 -1.921 -3.548 1.00 16.49 N ANISOU 1077 N SER A 141 1277 1545 3440 -1150 -170 154 N ATOM 1078 CA SER A 141 48.666 -1.067 -2.575 1.00 16.07 C ANISOU 1078 CA SER A 141 1248 1535 3324 -1126 -175 59 C ATOM 1079 C SER A 141 47.222 -1.522 -2.339 1.00 16.73 C ANISOU 1079 C SER A 141 1370 1647 3338 -1083 -186 -1 C ATOM 1080 O SER A 141 46.775 -1.682 -1.178 1.00 16.60 O ANISOU 1080 O SER A 141 1291 1618 3396 -1186 -150 12 O ATOM 1081 CB SER A 141 48.675 0.380 -3.048 1.00 17.02 C ANISOU 1081 CB SER A 141 1414 1644 3406 -1005 -233 -38 C ATOM 1082 OG SER A 141 48.210 1.227 -2.014 1.00 18.72 O ANISOU 1082 OG SER A 141 1639 2079 3392 -1070 27 160 O ATOM 1083 N ILE A 142 46.492 -1.739 -3.434 1.00 16.56 N ANISOU 1083 N ILE A 142 1316 1697 3278 -1096 -225 59 N ATOM 1084 CA ILE A 142 45.117 -2.277 -3.335 1.00 16.22 C ANISOU 1084 CA ILE A 142 1239 1774 3146 -971 -239 16 C ATOM 1085 C ILE A 142 45.040 -3.650 -2.665 1.00 16.70 C ANISOU 1085 C ILE A 142 1354 1848 3141 -924 -189 -2 C ATOM 1086 O ILE A 142 44.171 -3.859 -1.778 1.00 16.96 O ANISOU 1086 O ILE A 142 1622 1825 2993 -860 -138 -57 O ATOM 1087 CB ILE A 142 44.400 -2.226 -4.699 1.00 17.24 C ANISOU 1087 CB ILE A 142 1419 1844 3286 -938 -223 106 C ATOM 1088 CG1 ILE A 142 44.255 -0.739 -5.115 1.00 15.06 C ANISOU 1088 CG1 ILE A 142 1349 1380 2990 -914 -136 126 C ATOM 1089 CG2 ILE A 142 43.015 -2.937 -4.629 1.00 16.30 C ANISOU 1089 CG2 ILE A 142 1152 1711 3330 -1032 -598 -13 C ATOM 1090 CD1 ILE A 142 43.826 -0.530 -6.534 1.00 14.48 C ANISOU 1090 CD1 ILE A 142 1539 1430 2530 -636 323 283 C ATOM 1091 N ASP A 143 45.881 -4.606 -3.072 1.00 17.01 N ANISOU 1091 N ASP A 143 1290 2011 3163 -910 -141 75 N ATOM 1092 CA ASP A 143 45.988 -5.871 -2.289 1.00 17.50 C ANISOU 1092 CA ASP A 143 1476 1984 3188 -912 -144 11 C ATOM 1093 C ASP A 143 46.304 -5.654 -0.795 1.00 17.39 C ANISOU 1093 C ASP A 143 1543 1958 3107 -919 -122 44 C ATOM 1094 O ASP A 143 45.727 -6.312 0.049 1.00 18.53 O ANISOU 1094 O ASP A 143 1856 2073 3112 -680 -91 88 O ATOM 1095 CB ASP A 143 47.038 -6.830 -2.827 1.00 18.06 C ANISOU 1095 CB ASP A 143 1494 2201 3166 -961 -174 10 C ATOM 1096 CG ASP A 143 46.819 -7.212 -4.255 1.00 19.98 C ANISOU 1096 CG ASP A 143 1488 2469 3634 -910 -249 -98 C ATOM 1097 OD1 ASP A 143 45.766 -6.876 -4.820 1.00 22.12 O ANISOU 1097 OD1 ASP A 143 1004 3307 4091 -930 -246 143 O ATOM 1098 OD2 ASP A 143 47.728 -7.854 -4.810 1.00 21.70 O ANISOU 1098 OD2 ASP A 143 1310 3008 3926 -982 -201 -131 O ATOM 1099 N ALA A 144 47.252 -4.768 -0.479 1.00 17.14 N ANISOU 1099 N ALA A 144 1668 1829 3016 -929 -140 -58 N ATOM 1100 CA ALA A 144 47.505 -4.385 0.930 1.00 17.57 C ANISOU 1100 CA ALA A 144 1765 1908 3001 -1004 9 -42 C ATOM 1101 C ALA A 144 46.220 -3.941 1.675 1.00 16.90 C ANISOU 1101 C ALA A 144 1733 1841 2845 -984 75 20 C ATOM 1102 O ALA A 144 46.000 -4.303 2.844 1.00 16.83 O ANISOU 1102 O ALA A 144 1814 1761 2818 -945 -4 -76 O ATOM 1103 CB ALA A 144 48.544 -3.290 0.984 1.00 16.66 C ANISOU 1103 CB ALA A 144 1634 1832 2864 -1247 -6 -104 C ATOM 1104 N MET A 145 45.377 -3.167 0.986 1.00 16.38 N ANISOU 1104 N MET A 145 1696 1747 2780 -972 154 80 N ATOM 1105 CA MET A 145 44.134 -2.649 1.572 1.00 15.62 C ANISOU 1105 CA MET A 145 1644 1661 2628 -1045 154 163 C ATOM 1106 C MET A 145 43.185 -3.771 1.927 1.00 16.43 C ANISOU 1106 C MET A 145 1756 1743 2741 -1167 224 249 C ATOM 1107 O MET A 145 42.628 -3.813 3.046 1.00 16.24 O ANISOU 1107 O MET A 145 1759 1612 2799 -1063 141 166 O ATOM 1108 CB MET A 145 43.469 -1.621 0.649 1.00 14.98 C ANISOU 1108 CB MET A 145 1587 1567 2537 -945 146 202 C ATOM 1109 CG MET A 145 42.235 -0.905 1.254 1.00 16.40 C ANISOU 1109 CG MET A 145 1671 1935 2624 -978 316 182 C ATOM 1110 SD MET A 145 41.241 0.006 0.055 1.00 11.85 S ANISOU 1110 SD MET A 145 1186 1152 2164 -859 95 366 S ATOM 1111 CE MET A 145 40.879 -1.311 -1.057 1.00 15.62 C ANISOU 1111 CE MET A 145 1488 2502 1944 -994 847 586 C ATOM 1112 N ARG A 146 43.018 -4.700 0.995 1.00 16.19 N ANISOU 1112 N ARG A 146 1674 1739 2738 -1377 301 310 N ATOM 1113 CA ARG A 146 42.062 -5.813 1.214 1.00 18.34 C ANISOU 1113 CA ARG A 146 2050 2027 2890 -1459 319 538 C ATOM 1114 C ARG A 146 42.521 -6.653 2.387 1.00 18.32 C ANISOU 1114 C ARG A 146 2012 2085 2863 -1451 363 631 C ATOM 1115 O ARG A 146 41.716 -7.098 3.198 1.00 21.18 O ANISOU 1115 O ARG A 146 2403 2692 2953 -1152 320 541 O ATOM 1116 CB ARG A 146 41.954 -6.659 -0.049 1.00 17.96 C ANISOU 1116 CB ARG A 146 2006 1954 2861 -1572 344 552 C ATOM 1117 CG ARG A 146 41.349 -5.910 -1.240 1.00 21.43 C ANISOU 1117 CG ARG A 146 2479 2367 3294 -1669 379 689 C ATOM 1118 CD ARG A 146 40.645 -6.890 -2.131 1.00 25.21 C ANISOU 1118 CD ARG A 146 2947 3208 3420 -1653 919 1244 C ATOM 1119 NE ARG A 146 39.538 -7.478 -1.395 1.00 30.07 N ANISOU 1119 NE ARG A 146 3777 3426 4221 -1923 1088 1692 N ATOM 1120 CZ ARG A 146 38.278 -7.506 -1.811 1.00 29.13 C ANISOU 1120 CZ ARG A 146 3219 3738 4111 -1911 1419 1678 C ATOM 1121 NH1 ARG A 146 37.951 -6.984 -2.981 1.00 30.44 N ANISOU 1121 NH1 ARG A 146 3660 3801 4103 -1976 1584 1709 N ATOM 1122 NH2 ARG A 146 37.341 -8.053 -1.044 1.00 32.95 N ANISOU 1122 NH2 ARG A 146 4153 3311 5056 -2454 1259 1787 N ATOM 1123 N GLU A 147 43.816 -6.900 2.463 1.00 18.82 N ANISOU 1123 N GLU A 147 2064 2251 2834 -1331 317 731 N ATOM 1124 CA GLU A 147 44.419 -7.609 3.592 1.00 19.29 C ANISOU 1124 CA GLU A 147 2052 2364 2909 -1304 380 922 C ATOM 1125 C GLU A 147 44.254 -6.839 4.931 1.00 18.25 C ANISOU 1125 C GLU A 147 2006 2158 2769 -1200 345 838 C ATOM 1126 O GLU A 147 43.932 -7.436 5.952 1.00 17.65 O ANISOU 1126 O GLU A 147 2146 1868 2690 -1396 395 882 O ATOM 1127 CB GLU A 147 45.914 -7.866 3.288 1.00 19.06 C ANISOU 1127 CB GLU A 147 1971 2398 2872 -1291 366 942 C ATOM 1128 CG GLU A 147 46.711 -8.354 4.498 1.00 20.67 C ANISOU 1128 CG GLU A 147 1853 2913 3086 -1464 629 1272 C ATOM 1129 CD GLU A 147 48.058 -8.947 4.152 1.00 22.36 C ANISOU 1129 CD GLU A 147 2411 2849 3234 -1237 491 1294 C ATOM 1130 OE1 GLU A 147 48.575 -8.726 3.019 1.00 27.41 O ANISOU 1130 OE1 GLU A 147 2643 4135 3634 -1271 1126 1667 O ATOM 1131 OE2 GLU A 147 48.635 -9.579 5.061 1.00 26.63 O ANISOU 1131 OE2 GLU A 147 2947 2785 4383 -1372 960 2145 O ATOM 1132 N ALA A 148 44.503 -5.528 4.936 1.00 16.56 N ANISOU 1132 N ALA A 148 1861 1765 2664 -1235 366 862 N ATOM 1133 CA ALA A 148 44.301 -4.698 6.130 1.00 16.69 C ANISOU 1133 CA ALA A 148 1948 1676 2718 -1241 407 803 C ATOM 1134 C ALA A 148 42.854 -4.724 6.667 1.00 17.53 C ANISOU 1134 C ALA A 148 2227 1679 2754 -1142 460 688 C ATOM 1135 O ALA A 148 42.628 -4.832 7.882 1.00 19.37 O ANISOU 1135 O ALA A 148 2518 1882 2959 -1060 475 676 O ATOM 1136 CB ALA A 148 44.703 -3.283 5.850 1.00 16.18 C ANISOU 1136 CB ALA A 148 2084 1456 2604 -1174 347 791 C ATOM 1137 N PHE A 149 41.885 -4.646 5.760 1.00 17.61 N ANISOU 1137 N PHE A 149 2220 1522 2949 -1244 448 536 N ATOM 1138 CA PHE A 149 40.489 -4.426 6.138 1.00 17.79 C ANISOU 1138 CA PHE A 149 2316 1360 3081 -1361 477 438 C ATOM 1139 C PHE A 149 39.675 -5.674 6.262 1.00 18.60 C ANISOU 1139 C PHE A 149 2458 1378 3229 -1363 496 432 C ATOM 1140 O PHE A 149 38.543 -5.607 6.731 1.00 20.00 O ANISOU 1140 O PHE A 149 2584 1555 3459 -1380 512 430 O ATOM 1141 CB PHE A 149 39.786 -3.499 5.139 1.00 17.11 C ANISOU 1141 CB PHE A 149 2325 1364 2812 -1380 386 431 C ATOM 1142 CG PHE A 149 40.325 -2.086 5.148 1.00 17.74 C ANISOU 1142 CG PHE A 149 2505 1300 2932 -1430 385 356 C ATOM 1143 CD1 PHE A 149 41.028 -1.611 6.243 1.00 17.79 C ANISOU 1143 CD1 PHE A 149 2665 1264 2828 -1422 37 227 C ATOM 1144 CD2 PHE A 149 40.108 -1.245 4.068 1.00 17.18 C ANISOU 1144 CD2 PHE A 149 2473 1409 2645 -1333 553 562 C ATOM 1145 CE1 PHE A 149 41.547 -0.288 6.258 1.00 15.00 C ANISOU 1145 CE1 PHE A 149 2264 1138 2297 -1278 112 311 C ATOM 1146 CE2 PHE A 149 40.617 0.083 4.085 1.00 15.72 C ANISOU 1146 CE2 PHE A 149 2125 1383 2463 -1374 713 -37 C ATOM 1147 CZ PHE A 149 41.331 0.533 5.169 1.00 15.87 C ANISOU 1147 CZ PHE A 149 2218 1370 2440 -1429 448 74 C ATOM 1148 N LYS A 150 40.227 -6.792 5.816 1.00 19.97 N ANISOU 1148 N LYS A 150 2601 1556 3431 -1383 520 344 N ATOM 1149 CA LYS A 150 39.493 -8.065 5.842 1.00 20.67 C ANISOU 1149 CA LYS A 150 2848 1560 3446 -1404 594 345 C ATOM 1150 C LYS A 150 38.941 -8.345 7.235 1.00 22.04 C ANISOU 1150 C LYS A 150 2992 1834 3545 -1281 621 250 C ATOM 1151 O LYS A 150 39.648 -8.160 8.262 1.00 21.85 O ANISOU 1151 O LYS A 150 3050 1710 3539 -1324 592 273 O ATOM 1152 CB LYS A 150 40.415 -9.207 5.390 1.00 21.16 C ANISOU 1152 CB LYS A 150 2754 1704 3582 -1451 578 321 C ATOM 1153 CG LYS A 150 39.753 -10.544 5.111 1.00 24.06 C ANISOU 1153 CG LYS A 150 3420 2014 3706 -1255 456 345 C ATOM 1154 CD LYS A 150 40.800 -11.450 4.462 1.00 29.21 C ANISOU 1154 CD LYS A 150 4255 2916 3924 -1173 400 335 C ATOM 1155 CE LYS A 150 40.163 -12.658 3.788 1.00 33.44 C ANISOU 1155 CE LYS A 150 4524 3824 4354 -1332 250 385 C ATOM 1156 NZ LYS A 150 39.780 -12.387 2.354 1.00 36.65 N ANISOU 1156 NZ LYS A 150 4643 4502 4781 -1489 373 497 N ATOM 1157 N GLY A 151 37.689 -8.788 7.290 1.00 22.16 N ANISOU 1157 N GLY A 151 3038 1887 3494 -1236 709 288 N ATOM 1158 CA GLY A 151 37.056 -9.131 8.549 1.00 23.62 C ANISOU 1158 CA GLY A 151 3272 2168 3534 -1104 768 323 C ATOM 1159 C GLY A 151 36.451 -7.926 9.242 1.00 24.38 C ANISOU 1159 C GLY A 151 3354 2361 3549 -1044 834 367 C ATOM 1160 O GLY A 151 35.733 -8.063 10.232 1.00 26.41 O ANISOU 1160 O GLY A 151 3811 2568 3653 -994 821 338 O ATOM 1161 N CYS A 152 36.743 -6.740 8.718 1.00 24.56 N ANISOU 1161 N CYS A 152 3314 2432 3584 -930 760 399 N ATOM 1162 CA CYS A 152 36.464 -5.499 9.430 1.00 24.73 C ANISOU 1162 CA CYS A 152 3096 2619 3681 -904 804 487 C ATOM 1163 C CYS A 152 35.060 -4.989 9.121 1.00 23.61 C ANISOU 1163 C CYS A 152 2958 2490 3521 -915 782 520 C ATOM 1164 O CYS A 152 34.657 -4.917 7.961 1.00 24.99 O ANISOU 1164 O CYS A 152 3184 2540 3771 -818 716 474 O ATOM 1165 CB CYS A 152 37.501 -4.432 9.072 1.00 24.91 C ANISOU 1165 CB CYS A 152 3076 2653 3733 -817 689 463 C ATOM 1166 SG CYS A 152 39.085 -4.614 9.926 1.00 30.84 S ANISOU 1166 SG CYS A 152 3506 3812 4397 -476 731 507 S ATOM 1167 N ALA A 153 34.321 -4.636 10.168 1.00 21.78 N ANISOU 1167 N ALA A 153 2464 2322 3487 -1147 795 481 N ATOM 1168 CA ALA A 153 32.998 -4.045 10.007 1.00 20.08 C ANISOU 1168 CA ALA A 153 2149 2196 3285 -1261 881 538 C ATOM 1169 C ALA A 153 33.092 -2.543 9.759 1.00 18.86 C ANISOU 1169 C ALA A 153 1792 2174 3199 -1317 908 477 C ATOM 1170 O ALA A 153 32.790 -1.739 10.640 1.00 19.11 O ANISOU 1170 O ALA A 153 1661 2295 3304 -1422 793 454 O ATOM 1171 CB ALA A 153 32.138 -4.330 11.228 1.00 20.69 C ANISOU 1171 CB ALA A 153 2080 2336 3444 -1362 866 487 C ATOM 1172 N ILE A 154 33.512 -2.173 8.553 1.00 19.24 N ANISOU 1172 N ILE A 154 2138 2103 3067 -1212 691 548 N ATOM 1173 CA ILE A 154 33.438 -0.786 8.109 1.00 17.90 C ANISOU 1173 CA ILE A 154 1747 2204 2851 -1251 827 628 C ATOM 1174 C ILE A 154 32.888 -0.691 6.690 1.00 16.69 C ANISOU 1174 C ILE A 154 1526 2198 2615 -1179 796 522 C ATOM 1175 O ILE A 154 32.738 -1.702 6.003 1.00 16.60 O ANISOU 1175 O ILE A 154 1584 2245 2478 -1104 861 624 O ATOM 1176 CB ILE A 154 34.817 -0.103 8.162 1.00 18.02 C ANISOU 1176 CB ILE A 154 1777 2216 2852 -1198 756 568 C ATOM 1177 CG1 ILE A 154 35.780 -0.768 7.177 1.00 17.85 C ANISOU 1177 CG1 ILE A 154 1702 2217 2861 -1355 751 538 C ATOM 1178 CG2 ILE A 154 35.378 -0.145 9.575 1.00 18.12 C ANISOU 1178 CG2 ILE A 154 1789 2362 2730 -1201 1044 621 C ATOM 1179 CD1 ILE A 154 37.240 -0.517 7.487 1.00 18.84 C ANISOU 1179 CD1 ILE A 154 1786 2287 3084 -1184 790 698 C ATOM 1180 N ARG A 155 32.590 0.529 6.256 1.00 15.96 N ANISOU 1180 N ARG A 155 1408 2165 2490 -1152 758 394 N ATOM 1181 CA ARG A 155 32.311 0.792 4.865 1.00 15.66 C ANISOU 1181 CA ARG A 155 1427 2148 2373 -1174 767 311 C ATOM 1182 C ARG A 155 33.486 1.573 4.267 1.00 15.42 C ANISOU 1182 C ARG A 155 1540 2131 2187 -1193 774 345 C ATOM 1183 O ARG A 155 33.967 2.516 4.872 1.00 15.99 O ANISOU 1183 O ARG A 155 1687 2306 2082 -1118 998 377 O ATOM 1184 CB ARG A 155 31.048 1.594 4.709 1.00 15.39 C ANISOU 1184 CB ARG A 155 1482 1929 2435 -1139 786 290 C ATOM 1185 CG ARG A 155 29.819 0.847 5.368 1.00 16.33 C ANISOU 1185 CG ARG A 155 1353 2206 2644 -1029 994 286 C ATOM 1186 CD ARG A 155 28.513 1.541 5.041 1.00 17.74 C ANISOU 1186 CD ARG A 155 1745 1907 3088 -1207 817 609 C ATOM 1187 NE ARG A 155 27.422 0.958 5.847 1.00 18.57 N ANISOU 1187 NE ARG A 155 1598 2248 3208 -932 735 -62 N ATOM 1188 CZ ARG A 155 27.188 1.300 7.105 1.00 19.21 C ANISOU 1188 CZ ARG A 155 1754 2373 3169 -1042 644 260 C ATOM 1189 NH1 ARG A 155 27.949 2.255 7.697 1.00 16.78 N ANISOU 1189 NH1 ARG A 155 1815 1460 3099 -1231 548 359 N ATOM 1190 NH2 ARG A 155 26.207 0.702 7.758 1.00 20.68 N ANISOU 1190 NH2 ARG A 155 1547 2416 3892 -649 140 -197 N ATOM 1191 N VAL A 156 33.918 1.162 3.097 1.00 15.43 N ANISOU 1191 N VAL A 156 1558 2089 2215 -1275 675 314 N ATOM 1192 CA VAL A 156 35.079 1.820 2.429 1.00 15.33 C ANISOU 1192 CA VAL A 156 1670 2082 2072 -1259 660 381 C ATOM 1193 C VAL A 156 34.723 2.218 1.009 1.00 15.13 C ANISOU 1193 C VAL A 156 1753 2017 1977 -1320 663 342 C ATOM 1194 O VAL A 156 34.450 1.381 0.172 1.00 15.83 O ANISOU 1194 O VAL A 156 2024 2029 1961 -1423 661 249 O ATOM 1195 CB VAL A 156 36.303 0.892 2.396 1.00 14.79 C ANISOU 1195 CB VAL A 156 1599 2061 1960 -1216 690 272 C ATOM 1196 CG1 VAL A 156 37.456 1.503 1.540 1.00 14.30 C ANISOU 1196 CG1 VAL A 156 1503 1975 1954 -1241 447 424 C ATOM 1197 CG2 VAL A 156 36.749 0.525 3.814 1.00 15.69 C ANISOU 1197 CG2 VAL A 156 1696 2039 2226 -1089 382 386 C ATOM 1198 N LEU A 157 34.743 3.511 0.745 1.00 15.45 N ANISOU 1198 N LEU A 157 1854 1909 2105 -1088 568 336 N ATOM 1199 CA LEU A 157 34.690 4.005 -0.628 1.00 15.12 C ANISOU 1199 CA LEU A 157 1643 2001 2100 -1188 619 397 C ATOM 1200 C LEU A 157 36.124 4.212 -1.174 1.00 15.40 C ANISOU 1200 C LEU A 157 1578 2048 2225 -1144 532 327 C ATOM 1201 O LEU A 157 36.802 5.173 -0.803 1.00 14.84 O ANISOU 1201 O LEU A 157 1626 1835 2174 -1297 510 302 O ATOM 1202 CB LEU A 157 33.888 5.307 -0.672 1.00 14.80 C ANISOU 1202 CB LEU A 157 1606 1943 2072 -1204 588 459 C ATOM 1203 CG LEU A 157 33.757 6.073 -2.000 1.00 16.27 C ANISOU 1203 CG LEU A 157 1933 2072 2174 -1257 498 396 C ATOM 1204 CD1 LEU A 157 33.326 5.220 -3.159 1.00 19.49 C ANISOU 1204 CD1 LEU A 157 2320 2463 2619 -1482 481 547 C ATOM 1205 CD2 LEU A 157 32.828 7.289 -1.848 1.00 16.50 C ANISOU 1205 CD2 LEU A 157 1823 2229 2215 -1117 709 521 C ATOM 1206 N LEU A 158 36.583 3.309 -2.038 1.00 14.64 N ANISOU 1206 N LEU A 158 1323 1978 2260 -1182 502 308 N ATOM 1207 CA LEU A 158 37.917 3.456 -2.650 1.00 15.21 C ANISOU 1207 CA LEU A 158 1387 2127 2264 -1153 504 370 C ATOM 1208 C LEU A 158 37.807 4.412 -3.845 1.00 14.98 C ANISOU 1208 C LEU A 158 1430 2062 2199 -1256 399 495 C ATOM 1209 O LEU A 158 36.901 4.282 -4.654 1.00 15.63 O ANISOU 1209 O LEU A 158 1548 2118 2271 -1354 348 564 O ATOM 1210 CB LEU A 158 38.442 2.098 -3.129 1.00 15.50 C ANISOU 1210 CB LEU A 158 1253 2191 2442 -1146 589 396 C ATOM 1211 CG LEU A 158 39.739 2.183 -3.997 1.00 14.01 C ANISOU 1211 CG LEU A 158 1268 1927 2126 -994 784 174 C ATOM 1212 CD1 LEU A 158 40.870 2.463 -3.039 1.00 14.26 C ANISOU 1212 CD1 LEU A 158 876 2068 2471 -995 307 192 C ATOM 1213 CD2 LEU A 158 40.011 0.886 -4.771 1.00 17.09 C ANISOU 1213 CD2 LEU A 158 1721 2290 2481 -978 416 347 C ATOM 1214 N PHE A 159 38.738 5.360 -4.010 1.00 15.41 N ANISOU 1214 N PHE A 159 1546 2118 2189 -1227 342 387 N ATOM 1215 CA PHE A 159 38.607 6.258 -5.127 1.00 13.97 C ANISOU 1215 CA PHE A 159 1415 1941 1951 -1182 434 420 C ATOM 1216 C PHE A 159 39.959 6.516 -5.767 1.00 14.31 C ANISOU 1216 C PHE A 159 1484 1964 1989 -1157 530 471 C ATOM 1217 O PHE A 159 41.004 6.314 -5.143 1.00 14.61 O ANISOU 1217 O PHE A 159 1558 2014 1979 -1269 428 496 O ATOM 1218 CB PHE A 159 37.969 7.585 -4.710 1.00 13.53 C ANISOU 1218 CB PHE A 159 1227 2011 1901 -1157 402 275 C ATOM 1219 CG PHE A 159 38.876 8.482 -3.899 1.00 14.37 C ANISOU 1219 CG PHE A 159 1389 1820 2248 -1204 374 340 C ATOM 1220 CD1 PHE A 159 39.673 9.485 -4.515 1.00 17.74 C ANISOU 1220 CD1 PHE A 159 1563 2486 2689 -1337 127 54 C ATOM 1221 CD2 PHE A 159 38.954 8.319 -2.519 1.00 14.01 C ANISOU 1221 CD2 PHE A 159 1246 2076 2002 -1341 -45 200 C ATOM 1222 CE1 PHE A 159 40.509 10.317 -3.716 1.00 15.61 C ANISOU 1222 CE1 PHE A 159 1710 1966 2254 -1576 -126 249 C ATOM 1223 CE2 PHE A 159 39.784 9.125 -1.750 1.00 18.70 C ANISOU 1223 CE2 PHE A 159 1996 2469 2638 -984 -118 249 C ATOM 1224 CZ PHE A 159 40.534 10.127 -2.344 1.00 16.43 C ANISOU 1224 CZ PHE A 159 1375 2217 2650 -1484 -87 158 C ATOM 1225 N SER A 160 39.894 6.968 -7.013 1.00 14.97 N ANISOU 1225 N SER A 160 1630 2047 2008 -1042 623 447 N ATOM 1226 CA SER A 160 41.083 7.307 -7.797 1.00 15.23 C ANISOU 1226 CA SER A 160 1548 2127 2111 -1132 655 589 C ATOM 1227 C SER A 160 40.686 8.152 -8.996 1.00 15.76 C ANISOU 1227 C SER A 160 1655 2144 2188 -1044 565 541 C ATOM 1228 O SER A 160 39.540 8.089 -9.469 1.00 17.00 O ANISOU 1228 O SER A 160 1706 2390 2364 -980 632 668 O ATOM 1229 CB SER A 160 41.773 6.028 -8.316 1.00 14.73 C ANISOU 1229 CB SER A 160 1435 2132 2030 -1012 730 532 C ATOM 1230 OG SER A 160 42.928 6.319 -9.133 1.00 18.24 O ANISOU 1230 OG SER A 160 2021 2735 2172 -853 740 722 O ATOM 1231 N LEU A 161 41.660 8.889 -9.534 1.00 16.62 N ANISOU 1231 N LEU A 161 1883 2170 2261 -1054 529 570 N ATOM 1232 CA LEU A 161 41.480 9.521 -10.850 1.00 17.78 C ANISOU 1232 CA LEU A 161 2089 2313 2354 -1009 436 545 C ATOM 1233 C LEU A 161 41.528 8.485 -11.976 1.00 18.78 C ANISOU 1233 C LEU A 161 2238 2468 2427 -1050 347 563 C ATOM 1234 O LEU A 161 41.009 8.725 -13.057 1.00 20.22 O ANISOU 1234 O LEU A 161 2516 2663 2503 -1147 350 621 O ATOM 1235 CB LEU A 161 42.523 10.604 -11.090 1.00 19.21 C ANISOU 1235 CB LEU A 161 2540 2262 2494 -995 319 522 C ATOM 1236 CG LEU A 161 42.272 11.931 -10.347 1.00 20.70 C ANISOU 1236 CG LEU A 161 2698 2419 2746 -807 380 477 C ATOM 1237 CD1 LEU A 161 43.515 12.781 -10.478 1.00 22.93 C ANISOU 1237 CD1 LEU A 161 3216 2324 3170 -1099 253 500 C ATOM 1238 CD2 LEU A 161 41.057 12.673 -10.904 1.00 21.59 C ANISOU 1238 CD2 LEU A 161 2847 2349 3007 -848 590 545 C ATOM 1239 N SER A 162 42.152 7.340 -11.722 1.00 19.49 N ANISOU 1239 N SER A 162 2405 2480 2520 -1015 320 551 N ATOM 1240 CA SER A 162 42.442 6.363 -12.787 1.00 21.16 C ANISOU 1240 CA SER A 162 2580 2756 2703 -996 246 542 C ATOM 1241 C SER A 162 41.460 5.180 -12.832 1.00 21.73 C ANISOU 1241 C SER A 162 2596 2911 2750 -1004 182 528 C ATOM 1242 O SER A 162 41.321 4.437 -11.847 1.00 20.87 O ANISOU 1242 O SER A 162 2590 2816 2522 -1177 282 609 O ATOM 1243 CB SER A 162 43.887 5.853 -12.646 1.00 21.91 C ANISOU 1243 CB SER A 162 2855 2720 2748 -831 295 491 C ATOM 1244 OG SER A 162 44.098 4.722 -13.475 1.00 26.80 O ANISOU 1244 OG SER A 162 3491 3417 3273 -732 327 701 O ATOM 1245 N GLN A 163 40.793 5.004 -13.977 1.00 21.76 N ANISOU 1245 N GLN A 163 2536 2991 2741 -1031 117 447 N ATOM 1246 CA GLN A 163 39.845 3.883 -14.145 1.00 22.17 C ANISOU 1246 CA GLN A 163 2517 3001 2902 -1014 58 456 C ATOM 1247 C GLN A 163 40.561 2.536 -13.969 1.00 22.35 C ANISOU 1247 C GLN A 163 2504 3056 2933 -977 69 413 C ATOM 1248 O GLN A 163 40.017 1.629 -13.369 1.00 22.60 O ANISOU 1248 O GLN A 163 2580 3169 2835 -937 155 491 O ATOM 1249 CB GLN A 163 39.141 3.949 -15.503 1.00 22.26 C ANISOU 1249 CB GLN A 163 2540 2974 2942 -993 16 525 C ATOM 1250 CG GLN A 163 37.970 2.921 -15.720 1.00 22.48 C ANISOU 1250 CG GLN A 163 2520 3064 2957 -952 -26 508 C ATOM 1251 CD GLN A 163 36.834 3.047 -14.712 1.00 25.84 C ANISOU 1251 CD GLN A 163 2785 3363 3669 -788 -138 716 C ATOM 1252 OE1 GLN A 163 36.144 4.079 -14.649 1.00 28.29 O ANISOU 1252 OE1 GLN A 163 3039 3906 3803 -566 -69 575 O ATOM 1253 NE2 GLN A 163 36.610 1.980 -13.930 1.00 26.26 N ANISOU 1253 NE2 GLN A 163 2528 3842 3607 -784 -230 663 N ATOM 1254 N GLU A 164 41.807 2.438 -14.440 1.00 22.91 N ANISOU 1254 N GLU A 164 2642 3124 2937 -890 201 374 N ATOM 1255 CA GLU A 164 42.617 1.221 -14.273 1.00 23.50 C ANISOU 1255 CA GLU A 164 2641 3160 3125 -871 170 313 C ATOM 1256 C GLU A 164 42.678 0.757 -12.819 1.00 21.68 C ANISOU 1256 C GLU A 164 2366 3029 2839 -952 330 229 C ATOM 1257 O GLU A 164 42.595 -0.444 -12.556 1.00 21.89 O ANISOU 1257 O GLU A 164 2438 3113 2766 -754 326 129 O ATOM 1258 CB GLU A 164 44.035 1.437 -14.810 1.00 23.21 C ANISOU 1258 CB GLU A 164 2597 3098 3124 -868 207 319 C ATOM 1259 CG GLU A 164 44.906 0.181 -14.975 1.00 26.98 C ANISOU 1259 CG GLU A 164 3133 3424 3691 -954 152 408 C ATOM 1260 CD GLU A 164 46.356 0.509 -15.435 1.00 27.99 C ANISOU 1260 CD GLU A 164 3254 3464 3916 -845 76 374 C ATOM 1261 OE1 GLU A 164 46.653 1.704 -15.684 1.00 34.35 O ANISOU 1261 OE1 GLU A 164 4279 3660 5109 -1270 -120 406 O ATOM 1262 OE2 GLU A 164 47.200 -0.420 -15.570 1.00 35.79 O ANISOU 1262 OE2 GLU A 164 4532 4108 4958 -773 -35 306 O ATOM 1263 N HIS A 165 42.834 1.711 -11.890 1.00 20.67 N ANISOU 1263 N HIS A 165 2094 2973 2787 -1030 338 206 N ATOM 1264 CA HIS A 165 42.946 1.416 -10.479 1.00 19.66 C ANISOU 1264 CA HIS A 165 1958 2870 2641 -1208 419 157 C ATOM 1265 C HIS A 165 41.649 0.769 -9.948 1.00 20.20 C ANISOU 1265 C HIS A 165 2116 2863 2693 -1158 377 137 C ATOM 1266 O HIS A 165 41.677 -0.239 -9.237 1.00 20.78 O ANISOU 1266 O HIS A 165 2229 2966 2697 -1185 514 119 O ATOM 1267 CB HIS A 165 43.245 2.711 -9.694 1.00 19.21 C ANISOU 1267 CB HIS A 165 1882 2705 2709 -1427 390 274 C ATOM 1268 CG HIS A 165 44.623 3.276 -9.909 1.00 20.23 C ANISOU 1268 CG HIS A 165 1908 2911 2867 -1538 257 327 C ATOM 1269 ND1 HIS A 165 45.140 4.250 -9.086 1.00 22.97 N ANISOU 1269 ND1 HIS A 165 2191 3022 3515 -1738 65 389 N ATOM 1270 CD2 HIS A 165 45.573 3.031 -10.844 1.00 22.07 C ANISOU 1270 CD2 HIS A 165 2426 2907 3052 -1751 181 451 C ATOM 1271 CE1 HIS A 165 46.351 4.596 -9.512 1.00 22.57 C ANISOU 1271 CE1 HIS A 165 2235 3053 3288 -2116 598 600 C ATOM 1272 NE2 HIS A 165 46.646 3.855 -10.570 1.00 22.53 N ANISOU 1272 NE2 HIS A 165 2296 3254 3008 -2222 560 622 N ATOM 1273 N ILE A 166 40.522 1.346 -10.331 1.00 19.59 N ANISOU 1273 N ILE A 166 1952 2826 2663 -1157 429 68 N ATOM 1274 CA ILE A 166 39.225 0.879 -9.893 1.00 19.82 C ANISOU 1274 CA ILE A 166 2011 2773 2744 -1142 280 -19 C ATOM 1275 C ILE A 166 38.881 -0.450 -10.601 1.00 19.73 C ANISOU 1275 C ILE A 166 2050 2701 2743 -1225 255 8 C ATOM 1276 O ILE A 166 38.402 -1.362 -9.964 1.00 20.18 O ANISOU 1276 O ILE A 166 2232 2756 2679 -1190 245 -40 O ATOM 1277 CB ILE A 166 38.187 1.971 -10.143 1.00 20.29 C ANISOU 1277 CB ILE A 166 1992 2851 2863 -1128 280 28 C ATOM 1278 CG1 ILE A 166 38.450 3.222 -9.271 1.00 19.39 C ANISOU 1278 CG1 ILE A 166 1831 2761 2773 -1120 262 126 C ATOM 1279 CG2 ILE A 166 36.764 1.440 -9.969 1.00 19.26 C ANISOU 1279 CG2 ILE A 166 1535 2819 2960 -1279 486 155 C ATOM 1280 CD1 ILE A 166 38.886 3.016 -7.851 1.00 21.93 C ANISOU 1280 CD1 ILE A 166 2450 2544 3336 -1459 -15 211 C ATOM 1281 N ASP A 167 39.168 -0.564 -11.898 1.00 19.13 N ANISOU 1281 N ASP A 167 2044 2612 2612 -1232 361 -85 N ATOM 1282 CA ASP A 167 39.025 -1.860 -12.626 1.00 19.79 C ANISOU 1282 CA ASP A 167 2228 2532 2760 -1305 382 33 C ATOM 1283 C ASP A 167 39.792 -3.008 -11.949 1.00 19.59 C ANISOU 1283 C ASP A 167 2199 2393 2850 -1375 330 -9 C ATOM 1284 O ASP A 167 39.324 -4.165 -11.876 1.00 18.48 O ANISOU 1284 O ASP A 167 2062 2074 2884 -1792 157 -93 O ATOM 1285 CB ASP A 167 39.505 -1.734 -14.086 1.00 20.30 C ANISOU 1285 CB ASP A 167 2289 2704 2717 -1256 480 56 C ATOM 1286 CG ASP A 167 38.599 -0.841 -14.944 1.00 21.51 C ANISOU 1286 CG ASP A 167 2424 3010 2739 -1405 560 165 C ATOM 1287 OD1 ASP A 167 37.463 -0.527 -14.537 1.00 21.97 O ANISOU 1287 OD1 ASP A 167 2058 3068 3219 -2028 739 364 O ATOM 1288 OD2 ASP A 167 39.028 -0.448 -16.052 1.00 28.01 O ANISOU 1288 OD2 ASP A 167 3314 4089 3238 -1305 518 394 O ATOM 1289 N TYR A 168 40.988 -2.696 -11.470 1.00 18.58 N ANISOU 1289 N TYR A 168 2018 2138 2904 -1379 397 19 N ATOM 1290 CA TYR A 168 41.768 -3.665 -10.745 1.00 18.39 C ANISOU 1290 CA TYR A 168 1997 2158 2833 -1333 475 116 C ATOM 1291 C TYR A 168 41.091 -4.044 -9.445 1.00 18.00 C ANISOU 1291 C TYR A 168 1935 2142 2763 -1286 547 141 C ATOM 1292 O TYR A 168 41.100 -5.192 -9.082 1.00 17.48 O ANISOU 1292 O TYR A 168 1976 2008 2655 -1414 560 195 O ATOM 1293 CB TYR A 168 43.183 -3.187 -10.450 1.00 18.62 C ANISOU 1293 CB TYR A 168 1963 2113 2998 -1294 335 -57 C ATOM 1294 CG TYR A 168 43.926 -4.239 -9.670 1.00 19.01 C ANISOU 1294 CG TYR A 168 1846 2180 3195 -1366 467 -26 C ATOM 1295 CD1 TYR A 168 44.364 -5.420 -10.291 1.00 18.43 C ANISOU 1295 CD1 TYR A 168 1468 2059 3475 -1439 556 -113 C ATOM 1296 CD2 TYR A 168 44.160 -4.072 -8.300 1.00 20.05 C ANISOU 1296 CD2 TYR A 168 1728 2355 3534 -1198 297 -14 C ATOM 1297 CE1 TYR A 168 45.034 -6.391 -9.559 1.00 18.61 C ANISOU 1297 CE1 TYR A 168 1545 2011 3515 -1495 439 -213 C ATOM 1298 CE2 TYR A 168 44.803 -5.051 -7.554 1.00 19.66 C ANISOU 1298 CE2 TYR A 168 1511 2227 3728 -1429 379 -104 C ATOM 1299 CZ TYR A 168 45.244 -6.207 -8.190 1.00 18.06 C ANISOU 1299 CZ TYR A 168 1731 1767 3364 -1481 463 -167 C ATOM 1300 OH TYR A 168 45.935 -7.133 -7.437 1.00 18.57 O ANISOU 1300 OH TYR A 168 2012 1787 3255 -1641 405 -288 O ATOM 1301 N PHE A 169 40.570 -3.068 -8.716 1.00 18.86 N ANISOU 1301 N PHE A 169 2091 2303 2771 -1247 587 291 N ATOM 1302 CA PHE A 169 39.819 -3.410 -7.510 1.00 18.06 C ANISOU 1302 CA PHE A 169 1884 2274 2701 -1286 613 438 C ATOM 1303 C PHE A 169 38.647 -4.372 -7.756 1.00 19.33 C ANISOU 1303 C PHE A 169 2067 2310 2966 -1324 444 453 C ATOM 1304 O PHE A 169 38.424 -5.271 -6.939 1.00 19.33 O ANISOU 1304 O PHE A 169 1898 2544 2901 -1365 468 646 O ATOM 1305 CB PHE A 169 39.347 -2.169 -6.723 1.00 17.73 C ANISOU 1305 CB PHE A 169 1907 2263 2565 -1295 734 479 C ATOM 1306 CG PHE A 169 38.461 -2.534 -5.562 1.00 19.01 C ANISOU 1306 CG PHE A 169 2249 2423 2548 -1026 775 450 C ATOM 1307 CD1 PHE A 169 39.019 -2.950 -4.364 1.00 17.92 C ANISOU 1307 CD1 PHE A 169 2353 2026 2426 -1051 846 372 C ATOM 1308 CD2 PHE A 169 37.079 -2.543 -5.705 1.00 17.59 C ANISOU 1308 CD2 PHE A 169 1667 2528 2488 -1133 1003 637 C ATOM 1309 CE1 PHE A 169 38.221 -3.339 -3.323 1.00 18.58 C ANISOU 1309 CE1 PHE A 169 2249 2451 2358 -806 1155 529 C ATOM 1310 CE2 PHE A 169 36.250 -2.937 -4.640 1.00 19.62 C ANISOU 1310 CE2 PHE A 169 2279 2986 2189 -791 1087 649 C ATOM 1311 CZ PHE A 169 36.824 -3.322 -3.461 1.00 19.19 C ANISOU 1311 CZ PHE A 169 2072 2664 2554 -1008 1002 780 C ATOM 1312 N ASP A 170 37.880 -4.161 -8.821 1.00 19.30 N ANISOU 1312 N ASP A 170 1965 2329 3036 -1446 298 416 N ATOM 1313 CA ASP A 170 36.768 -5.070 -9.202 1.00 22.05 C ANISOU 1313 CA ASP A 170 2188 2698 3490 -1238 181 328 C ATOM 1314 C ASP A 170 37.283 -6.473 -9.474 1.00 21.34 C ANISOU 1314 C ASP A 170 2062 2522 3524 -1340 219 220 C ATOM 1315 O ASP A 170 36.622 -7.444 -9.168 1.00 22.49 O ANISOU 1315 O ASP A 170 1910 2742 3893 -1425 172 230 O ATOM 1316 CB ASP A 170 36.033 -4.540 -10.437 1.00 22.59 C ANISOU 1316 CB ASP A 170 2231 2839 3509 -1190 93 312 C ATOM 1317 CG ASP A 170 35.424 -3.167 -10.205 1.00 25.55 C ANISOU 1317 CG ASP A 170 2597 3299 3810 -1152 35 341 C ATOM 1318 OD1 ASP A 170 35.237 -2.786 -9.018 1.00 29.35 O ANISOU 1318 OD1 ASP A 170 2541 4244 4366 -839 256 468 O ATOM 1319 OD2 ASP A 170 35.135 -2.467 -11.206 1.00 25.77 O ANISOU 1319 OD2 ASP A 170 2081 3631 4078 -1623 -244 657 O ATOM 1320 N ALA A 171 38.494 -6.569 -9.996 1.00 21.78 N ANISOU 1320 N ALA A 171 1974 2581 3719 -1296 237 115 N ATOM 1321 CA ALA A 171 39.139 -7.871 -10.278 1.00 22.26 C ANISOU 1321 CA ALA A 171 1932 2674 3850 -1403 328 75 C ATOM 1322 C ALA A 171 39.551 -8.577 -8.982 1.00 22.38 C ANISOU 1322 C ALA A 171 1884 2650 3966 -1444 317 42 C ATOM 1323 O ALA A 171 39.785 -9.786 -8.972 1.00 22.41 O ANISOU 1323 O ALA A 171 1747 2672 4092 -1710 246 11 O ATOM 1324 CB ALA A 171 40.382 -7.655 -11.211 1.00 21.12 C ANISOU 1324 CB ALA A 171 1646 2483 3894 -1588 449 33 C ATOM 1325 N THR A 172 39.722 -7.803 -7.902 1.00 24.17 N ANISOU 1325 N THR A 172 2261 2839 4081 -1288 379 3 N ATOM 1326 CA THR A 172 40.015 -8.385 -6.575 1.00 24.55 C ANISOU 1326 CA THR A 172 2319 2840 4169 -1235 322 41 C ATOM 1327 C THR A 172 38.731 -8.989 -5.983 1.00 25.60 C ANISOU 1327 C THR A 172 2413 2970 4342 -1258 451 65 C ATOM 1328 O THR A 172 38.771 -9.805 -5.059 1.00 24.82 O ANISOU 1328 O THR A 172 2196 2794 4438 -1410 458 262 O ATOM 1329 CB THR A 172 40.715 -7.365 -5.584 1.00 25.38 C ANISOU 1329 CB THR A 172 2476 2965 4199 -1027 334 8 C ATOM 1330 OG1 THR A 172 39.826 -6.305 -5.216 1.00 26.43 O ANISOU 1330 OG1 THR A 172 3065 2920 4057 -906 109 -35 O ATOM 1331 CG2 THR A 172 41.972 -6.768 -6.191 1.00 25.16 C ANISOU 1331 CG2 THR A 172 2638 2814 4106 -1065 179 5 C ATOM 1332 N CYS A 173 37.596 -8.590 -6.539 1.00 26.40 N ANISOU 1332 N CYS A 173 2461 3031 4537 -1356 506 36 N ATOM 1333 CA CYS A 173 36.293 -9.024 -6.026 1.00 28.31 C ANISOU 1333 CA CYS A 173 2712 3310 4732 -1415 642 67 C ATOM 1334 C CYS A 173 35.798 -10.235 -6.781 1.00 29.95 C ANISOU 1334 C CYS A 173 2971 3466 4939 -1435 671 54 C ATOM 1335 O CYS A 173 34.751 -10.819 -6.419 1.00 30.52 O ANISOU 1335 O CYS A 173 2829 3622 5144 -1520 688 92 O ATOM 1336 CB CYS A 173 35.270 -7.913 -6.194 1.00 27.65 C ANISOU 1336 CB CYS A 173 2620 3225 4658 -1406 705 37 C ATOM 1337 SG CYS A 173 35.594 -6.460 -5.234 1.00 30.31 S ANISOU 1337 SG CYS A 173 3068 3535 4911 -1325 787 114 S ATOM 1338 N LYS A 174 36.515 -10.609 -7.839 1.00 31.48 N ANISOU 1338 N LYS A 174 3242 3633 5086 -1451 695 57 N ATOM 1339 CA LYS A 174 36.062 -11.680 -8.751 1.00 33.53 C ANISOU 1339 CA LYS A 174 3611 3915 5214 -1407 649 58 C ATOM 1340 C LYS A 174 36.006 -13.037 -8.053 1.00 34.11 C ANISOU 1340 C LYS A 174 3663 3937 5357 -1457 657 69 C ATOM 1341 O LYS A 174 34.906 -13.539 -7.725 1.00 35.43 O ANISOU 1341 O LYS A 174 3753 4143 5565 -1474 703 136 O ATOM 1342 CB LYS A 174 36.964 -11.748 -9.995 1.00 33.59 C ANISOU 1342 CB LYS A 174 3624 3987 5151 -1359 606 -20 C ATOM 1343 CG LYS A 174 36.284 -12.333 -11.227 1.00 36.86 C ANISOU 1343 CG LYS A 174 4253 4329 5422 -1206 678 126 C ATOM 1344 CD LYS A 174 36.435 -13.848 -11.327 1.00 38.91 C ANISOU 1344 CD LYS A 174 4725 4632 5426 -1211 747 259 C ATOM 1345 CE LYS A 174 36.008 -14.361 -12.703 1.00 40.88 C ANISOU 1345 CE LYS A 174 5095 5032 5402 -1058 815 410 C ATOM 1346 NZ LYS A 174 36.882 -13.792 -13.774 1.00 41.71 N ANISOU 1346 NZ LYS A 174 5187 5355 5305 -898 948 546 N TER 1347 LYS A 174 ATOM 1348 N LYS A 8 30.116 4.721 -21.041 1.00 30.52 N ATOM 1349 CA LYS A 8 31.083 5.674 -21.663 1.00 30.28 C ATOM 1350 C LYS A 8 31.014 5.597 -23.203 1.00 28.36 C ATOM 1351 O LYS A 8 31.205 4.516 -23.803 1.00 29.24 O ATOM 1352 CB LYS A 8 32.486 5.442 -21.131 1.00 30.81 C ATOM 1353 CG LYS A 8 32.483 5.126 -19.614 1.00 35.28 C ATOM 1354 CD LYS A 8 33.816 5.392 -18.913 1.00 40.66 C ATOM 1355 CE LYS A 8 34.746 4.182 -18.968 1.00 45.26 C ATOM 1356 NZ LYS A 8 35.737 4.244 -20.103 1.00 47.28 N ATOM 1357 N PRO A 9 30.681 6.726 -23.845 1.00 26.26 N ANISOU 1357 N PRO B 9 3223 3381 3371 -290 134 31 N ATOM 1358 CA PRO A 9 30.398 6.655 -25.265 1.00 24.75 C ANISOU 1358 CA PRO B 9 3027 3255 3119 -476 188 79 C ATOM 1359 C PRO A 9 31.660 6.630 -26.119 1.00 24.14 C ANISOU 1359 C PRO B 9 2940 3164 3065 -601 204 154 C ATOM 1360 O PRO A 9 32.735 7.031 -25.670 1.00 23.31 O ANISOU 1360 O PRO B 9 2674 3067 3113 -891 267 180 O ATOM 1361 CB PRO A 9 29.623 7.942 -25.515 1.00 24.22 C ANISOU 1361 CB PRO B 9 2998 3159 3042 -389 223 12 C ATOM 1362 CG PRO A 9 30.258 8.911 -24.554 1.00 24.97 C ANISOU 1362 CG PRO B 9 2935 3313 3236 -341 111 16 C ATOM 1363 CD PRO A 9 30.508 8.096 -23.316 1.00 25.59 C ANISOU 1363 CD PRO B 9 3088 3312 3321 -313 110 -38 C ATOM 1364 N LYS A 10 31.531 6.142 -27.343 1.00 22.60 N ANISOU 1364 N LYS B 10 2827 2974 2783 -784 281 229 N ATOM 1365 CA LYS A 10 32.644 6.215 -28.281 1.00 22.42 C ANISOU 1365 CA LYS B 10 2665 2999 2855 -894 306 299 C ATOM 1366 C LYS A 10 32.977 7.659 -28.635 1.00 22.07 C ANISOU 1366 C LYS B 10 2585 2985 2812 -958 324 280 C ATOM 1367 O LYS A 10 34.152 7.997 -28.896 1.00 22.54 O ANISOU 1367 O LYS B 10 2407 3118 3039 -1105 414 344 O ATOM 1368 CB LYS A 10 32.267 5.457 -29.549 1.00 22.34 C ANISOU 1368 CB LYS B 10 2774 2956 2756 -921 317 295 C ATOM 1369 CG LYS A 10 33.422 5.177 -30.446 1.00 22.87 C ANISOU 1369 CG LYS B 10 2464 3070 3152 -1093 271 259 C ATOM 1370 CD LYS A 10 34.273 4.113 -29.880 1.00 23.38 C ANISOU 1370 CD LYS B 10 2758 2925 3200 -1100 235 340 C ATOM 1371 CE LYS A 10 33.935 2.777 -30.472 1.00 27.48 C ANISOU 1371 CE LYS B 10 3455 3552 3434 -794 94 371 C ATOM 1372 NZ LYS A 10 34.597 1.747 -29.640 1.00 28.67 N ANISOU 1372 NZ LYS B 10 3883 3888 3122 -335 463 736 N ATOM 1373 N PHE A 11 31.945 8.496 -28.675 1.00 20.98 N ANISOU 1373 N PHE B 11 2399 2986 2585 -1010 289 391 N ATOM 1374 CA PHE A 11 32.052 9.901 -29.056 1.00 20.45 C ANISOU 1374 CA PHE B 11 2526 2777 2466 -966 246 402 C ATOM 1375 C PHE A 11 30.768 10.620 -28.680 1.00 20.84 C ANISOU 1375 C PHE B 11 2747 2666 2504 -1022 242 386 C ATOM 1376 O PHE A 11 29.767 9.985 -28.377 1.00 22.11 O ANISOU 1376 O PHE B 11 2956 2769 2674 -851 235 414 O ATOM 1377 CB PHE A 11 32.337 10.047 -30.581 1.00 19.82 C ANISOU 1377 CB PHE B 11 2365 2931 2234 -965 362 473 C ATOM 1378 CG PHE A 11 31.385 9.252 -31.465 1.00 20.49 C ANISOU 1378 CG PHE B 11 2628 3040 2117 -836 430 447 C ATOM 1379 CD1 PHE A 11 30.066 9.689 -31.677 1.00 22.09 C ANISOU 1379 CD1 PHE B 11 2889 3270 2233 -836 186 543 C ATOM 1380 CD2 PHE A 11 31.779 8.052 -32.034 1.00 21.50 C ANISOU 1380 CD2 PHE B 11 2838 3107 2223 -920 316 561 C ATOM 1381 CE1 PHE A 11 29.175 8.961 -32.466 1.00 21.22 C ANISOU 1381 CE1 PHE B 11 2621 3105 2335 -1101 592 655 C ATOM 1382 CE2 PHE A 11 30.886 7.309 -32.852 1.00 18.95 C ANISOU 1382 CE2 PHE B 11 1909 3070 2218 -1392 690 1081 C ATOM 1383 CZ PHE A 11 29.590 7.766 -33.063 1.00 20.42 C ANISOU 1383 CZ PHE B 11 2633 2920 2206 -890 494 1002 C ATOM 1384 N LEU A 12 30.785 11.946 -28.756 1.00 21.34 N ANISOU 1384 N LEU B 12 2958 2554 2596 -1021 156 245 N ATOM 1385 CA LEU A 12 29.685 12.783 -28.308 1.00 19.99 C ANISOU 1385 CA LEU B 12 2702 2303 2590 -1082 269 201 C ATOM 1386 C LEU A 12 28.320 12.415 -28.835 1.00 20.53 C ANISOU 1386 C LEU B 12 2858 2278 2665 -1109 156 180 C ATOM 1387 O LEU A 12 28.128 12.281 -30.039 1.00 20.55 O ANISOU 1387 O LEU B 12 2869 2360 2578 -1214 187 261 O ATOM 1388 CB LEU A 12 29.964 14.233 -28.676 1.00 20.92 C ANISOU 1388 CB LEU B 12 2826 2371 2751 -1076 266 241 C ATOM 1389 CG LEU A 12 28.977 15.380 -28.399 1.00 19.79 C ANISOU 1389 CG LEU B 12 2594 2393 2532 -1203 432 58 C ATOM 1390 CD1 LEU A 12 28.651 15.496 -26.925 1.00 20.76 C ANISOU 1390 CD1 LEU B 12 2725 2509 2652 -1461 348 182 C ATOM 1391 CD2 LEU A 12 29.616 16.659 -28.923 1.00 19.17 C ANISOU 1391 CD2 LEU B 12 2820 1969 2493 -1112 406 181 C ATOM 1392 N GLU A 13 27.386 12.273 -27.902 1.00 20.19 N ANISOU 1392 N GLU B 13 2600 2239 2831 -1171 221 146 N ATOM 1393 CA GLU A 13 25.976 11.984 -28.197 1.00 22.44 C ANISOU 1393 CA GLU B 13 2825 2645 3056 -1111 160 218 C ATOM 1394 C GLU A 13 25.043 13.039 -27.612 1.00 22.43 C ANISOU 1394 C GLU B 13 2682 2833 3007 -1194 202 231 C ATOM 1395 O GLU A 13 25.209 13.494 -26.468 1.00 22.45 O ANISOU 1395 O GLU B 13 2527 2978 3025 -1292 237 224 O ATOM 1396 CB GLU A 13 25.605 10.626 -27.619 1.00 22.76 C ANISOU 1396 CB GLU B 13 2816 2627 3204 -1118 169 208 C ATOM 1397 CG GLU A 13 26.406 9.467 -28.162 1.00 25.22 C ANISOU 1397 CG GLU B 13 3176 2886 3517 -1055 147 316 C ATOM 1398 CD GLU A 13 26.075 8.149 -27.437 1.00 25.70 C ANISOU 1398 CD GLU B 13 3216 2878 3671 -1033 144 209 C ATOM 1399 OE1 GLU A 13 25.013 8.057 -26.776 1.00 30.19 O ANISOU 1399 OE1 GLU B 13 3795 3582 4093 -753 171 349 O ATOM 1400 OE2 GLU A 13 26.890 7.207 -27.524 1.00 31.24 O ANISOU 1400 OE2 GLU B 13 3789 3422 4656 -896 -199 99 O ATOM 1401 N TYR A 14 24.030 13.430 -28.371 1.00 23.05 N ANISOU 1401 N TYR B 14 2852 2898 3005 -1139 240 292 N ATOM 1402 CA TYR A 14 23.091 14.410 -27.841 1.00 23.39 C ANISOU 1402 CA TYR B 14 2968 2865 3054 -1231 257 235 C ATOM 1403 C TYR A 14 21.691 13.811 -27.722 1.00 23.70 C ANISOU 1403 C TYR B 14 2985 2887 3130 -1241 228 189 C ATOM 1404 O TYR A 14 21.283 12.970 -28.537 1.00 25.22 O ANISOU 1404 O TYR B 14 3203 3144 3235 -1033 197 136 O ATOM 1405 CB TYR A 14 22.996 15.636 -28.742 1.00 21.83 C ANISOU 1405 CB TYR B 14 2884 2474 2936 -1538 199 286 C ATOM 1406 CG TYR A 14 24.133 16.639 -28.659 1.00 20.52 C ANISOU 1406 CG TYR B 14 2715 2332 2748 -1808 395 399 C ATOM 1407 CD1 TYR A 14 24.959 16.839 -29.738 1.00 22.04 C ANISOU 1407 CD1 TYR B 14 3318 2183 2871 -1836 311 399 C ATOM 1408 CD2 TYR A 14 24.345 17.401 -27.492 1.00 20.68 C ANISOU 1408 CD2 TYR B 14 2845 2080 2931 -2098 336 311 C ATOM 1409 CE1 TYR A 14 26.005 17.766 -29.670 1.00 20.36 C ANISOU 1409 CE1 TYR B 14 2560 2510 2665 -2141 348 473 C ATOM 1410 CE2 TYR A 14 25.381 18.351 -27.411 1.00 19.16 C ANISOU 1410 CE2 TYR B 14 2692 2037 2550 -1977 325 374 C ATOM 1411 CZ TYR A 14 26.193 18.514 -28.514 1.00 18.82 C ANISOU 1411 CZ TYR B 14 2571 2128 2450 -1963 370 360 C ATOM 1412 OH TYR A 14 27.199 19.437 -28.455 1.00 20.14 O ANISOU 1412 OH TYR B 14 2585 2418 2648 -2192 40 461 O ATOM 1413 N LYS A 15 20.971 14.263 -26.700 1.00 24.21 N ANISOU 1413 N LYS B 15 2973 2966 3258 -1096 249 153 N ATOM 1414 CA LYS A 15 19.535 14.027 -26.504 1.00 23.65 C ANISOU 1414 CA LYS B 15 2856 2829 3299 -1208 278 234 C ATOM 1415 C LYS A 15 18.912 15.364 -26.118 1.00 23.32 C ANISOU 1415 C LYS B 15 2718 2920 3221 -1243 287 319 C ATOM 1416 O LYS A 15 19.654 16.308 -25.741 1.00 21.87 O ANISOU 1416 O LYS B 15 2595 2694 3018 -1373 230 287 O ATOM 1417 CB LYS A 15 19.296 13.022 -25.389 1.00 24.86 C ANISOU 1417 CB LYS B 15 3109 2914 3421 -1010 295 208 C ATOM 1418 CG LYS A 15 19.399 11.567 -25.829 1.00 27.53 C ANISOU 1418 CG LYS B 15 3314 3045 4098 -1151 389 350 C ATOM 1419 CD LYS A 15 19.390 10.644 -24.620 1.00 32.11 C ANISOU 1419 CD LYS B 15 3834 3337 5027 -848 711 547 C ATOM 1420 CE LYS A 15 19.533 9.161 -25.045 1.00 35.39 C ANISOU 1420 CE LYS B 15 4113 3672 5662 -628 772 403 C ATOM 1421 NZ LYS A 15 20.924 8.625 -24.814 1.00 35.49 N ANISOU 1421 NZ LYS B 15 3815 3543 6126 -831 981 579 N ATOM 1422 N THR A 16 17.578 15.470 -26.227 1.00 22.65 N ANISOU 1422 N THR B 16 2522 2946 3137 -1387 316 385 N ATOM 1423 CA THR A 16 16.875 16.682 -25.795 1.00 23.23 C ANISOU 1423 CA THR B 16 2377 3171 3276 -1489 398 548 C ATOM 1424 C THR A 16 15.634 16.383 -24.972 1.00 24.13 C ANISOU 1424 C THR B 16 2444 3290 3434 -1439 297 507 C ATOM 1425 O THR A 16 15.113 15.255 -24.997 1.00 25.95 O ANISOU 1425 O THR B 16 2591 3466 3800 -1426 246 476 O ATOM 1426 CB THR A 16 16.460 17.588 -26.953 1.00 23.33 C ANISOU 1426 CB THR B 16 2417 3246 3199 -1451 342 481 C ATOM 1427 OG1 THR A 16 15.551 16.888 -27.793 1.00 22.90 O ANISOU 1427 OG1 THR B 16 1948 3386 3365 -2026 678 608 O ATOM 1428 CG2 THR A 16 17.648 18.001 -27.761 1.00 20.60 C ANISOU 1428 CG2 THR B 16 1941 2843 3043 -1764 640 709 C ATOM 1429 N CYS A 17 15.178 17.383 -24.222 1.00 24.29 N ANISOU 1429 N CYS B 17 2480 3352 3393 -1454 214 615 N ATOM 1430 CA CYS A 17 13.921 17.256 -23.481 1.00 24.23 C ANISOU 1430 CA CYS B 17 2443 3419 3343 -1412 135 534 C ATOM 1431 C CYS A 17 13.325 18.621 -23.289 1.00 24.40 C ANISOU 1431 C CYS B 17 2510 3504 3257 -1284 100 468 C ATOM 1432 O CYS A 17 14.005 19.550 -22.837 1.00 23.75 O ANISOU 1432 O CYS B 17 2455 3305 3261 -1350 51 369 O ATOM 1433 CB CYS A 17 14.135 16.606 -22.118 1.00 24.02 C ANISOU 1433 CB CYS B 17 2447 3381 3298 -1496 190 588 C ATOM 1434 SG CYS A 17 12.589 16.204 -21.244 1.00 25.62 S ANISOU 1434 SG CYS B 17 2615 3469 3647 -1677 82 807 S ATOM 1435 N VAL A 18 12.074 18.762 -23.696 1.00 24.40 N ANISOU 1435 N VAL B 18 2486 3605 3177 -1223 44 415 N ATOM 1436 CA VAL A 18 11.291 19.921 -23.319 1.00 25.57 C ANISOU 1436 CA VAL B 18 2704 3917 3093 -1035 0 310 C ATOM 1437 C VAL A 18 10.441 19.505 -22.141 1.00 25.54 C ANISOU 1437 C VAL B 18 2611 3925 3168 -1092 55 275 C ATOM 1438 O VAL A 18 9.680 18.537 -22.214 1.00 26.12 O ANISOU 1438 O VAL B 18 2666 4015 3244 -1077 -41 192 O ATOM 1439 CB VAL A 18 10.373 20.401 -24.466 1.00 26.75 C ANISOU 1439 CB VAL B 18 2830 4055 3279 -951 -33 293 C ATOM 1440 CG1 VAL A 18 9.574 21.680 -24.049 1.00 26.74 C ANISOU 1440 CG1 VAL B 18 3075 3851 3232 -939 40 180 C ATOM 1441 CG2 VAL A 18 11.203 20.641 -25.716 1.00 26.13 C ANISOU 1441 CG2 VAL B 18 2795 4209 2922 -1053 -15 257 C ATOM 1442 N GLY A 19 10.568 20.227 -21.037 1.00 24.92 N ANISOU 1442 N GLY B 19 2449 3968 3052 -1099 72 286 N ATOM 1443 CA GLY A 19 9.702 19.924 -19.898 1.00 24.17 C ANISOU 1443 CA GLY B 19 2297 3876 3007 -1323 179 328 C ATOM 1444 C GLY A 19 10.234 20.538 -18.629 1.00 24.51 C ANISOU 1444 C GLY B 19 2265 3921 3125 -1311 199 344 C ATOM 1445 O GLY A 19 11.344 21.130 -18.631 1.00 23.46 O ANISOU 1445 O GLY B 19 2232 3705 2974 -1531 129 387 O ATOM 1446 N ASP A 20 9.452 20.383 -17.556 1.00 23.82 N ANISOU 1446 N ASP B 20 2165 3812 3073 -1375 276 365 N ATOM 1447 CA ASP A 20 9.898 20.796 -16.236 1.00 24.25 C ANISOU 1447 CA ASP B 20 1974 3842 3394 -1418 443 409 C ATOM 1448 C ASP A 20 10.935 19.796 -15.702 1.00 23.24 C ANISOU 1448 C ASP B 20 1886 3709 3233 -1436 492 496 C ATOM 1449 O ASP A 20 11.161 18.708 -16.287 1.00 21.73 O ANISOU 1449 O ASP B 20 1526 3570 3158 -1587 572 506 O ATOM 1450 CB ASP A 20 8.719 21.073 -15.268 1.00 25.13 C ANISOU 1450 CB ASP B 20 2085 3890 3570 -1432 356 352 C ATOM 1451 CG ASP A 20 7.924 19.842 -14.917 1.00 27.47 C ANISOU 1451 CG ASP B 20 1939 4233 4264 -1461 509 333 C ATOM 1452 OD1 ASP A 20 8.490 18.724 -14.916 1.00 30.82 O ANISOU 1452 OD1 ASP B 20 2218 4558 4934 -1589 397 -57 O ATOM 1453 OD2 ASP A 20 6.709 19.999 -14.598 1.00 30.64 O ANISOU 1453 OD2 ASP B 20 1914 4482 5243 -2067 554 322 O ATOM 1454 N LEU A 21 11.608 20.197 -14.635 1.00 23.40 N ANISOU 1454 N LEU B 21 1971 3711 3208 -1359 599 550 N ATOM 1455 CA LEU A 21 12.707 19.407 -14.093 1.00 23.37 C ANISOU 1455 CA LEU B 21 2088 3547 3243 -1314 593 542 C ATOM 1456 C LEU A 21 12.330 17.945 -13.817 1.00 22.58 C ANISOU 1456 C LEU B 21 1961 3418 3198 -1435 755 560 C ATOM 1457 O LEU A 21 13.080 17.039 -14.167 1.00 23.10 O ANISOU 1457 O LEU B 21 2220 3331 3226 -1514 739 734 O ATOM 1458 CB LEU A 21 13.209 20.022 -12.806 1.00 22.71 C ANISOU 1458 CB LEU B 21 1999 3453 3173 -1437 575 535 C ATOM 1459 CG LEU A 21 14.600 19.515 -12.451 1.00 23.41 C ANISOU 1459 CG LEU B 21 2050 3733 3110 -1129 496 528 C ATOM 1460 CD1 LEU A 21 15.582 19.890 -13.573 1.00 21.67 C ANISOU 1460 CD1 LEU B 21 1799 3491 2944 -1467 674 890 C ATOM 1461 CD2 LEU A 21 15.031 20.131 -11.119 1.00 23.17 C ANISOU 1461 CD2 LEU B 21 2406 3601 2795 -881 341 291 C ATOM 1462 N ALA A 22 11.216 17.722 -13.141 1.00 23.65 N ANISOU 1462 N ALA B 22 1996 3564 3427 -1299 767 442 N ATOM 1463 CA ALA A 22 10.736 16.360 -12.916 1.00 23.16 C ANISOU 1463 CA ALA B 22 1808 3590 3402 -1385 853 507 C ATOM 1464 C ALA A 22 10.687 15.497 -14.192 1.00 22.64 C ANISOU 1464 C ALA B 22 1588 3568 3444 -1386 851 506 C ATOM 1465 O ALA A 22 11.127 14.351 -14.185 1.00 22.86 O ANISOU 1465 O ALA B 22 1253 3823 3609 -1396 1026 498 O ATOM 1466 CB ALA A 22 9.380 16.355 -12.164 1.00 23.11 C ANISOU 1466 CB ALA B 22 1726 3643 3410 -1309 897 414 C ATOM 1467 N VAL A 23 10.149 16.027 -15.280 1.00 23.61 N ANISOU 1467 N VAL B 23 1756 3637 3578 -1387 700 455 N ATOM 1468 CA VAL A 23 10.149 15.243 -16.530 1.00 24.20 C ANISOU 1468 CA VAL B 23 1864 3589 3743 -1335 528 428 C ATOM 1469 C VAL A 23 11.566 15.061 -17.116 1.00 23.30 C ANISOU 1469 C VAL B 23 1747 3529 3577 -1323 410 444 C ATOM 1470 O VAL A 23 11.899 13.977 -17.602 1.00 23.78 O ANISOU 1470 O VAL B 23 1871 3583 3579 -1148 316 419 O ATOM 1471 CB VAL A 23 9.080 15.686 -17.620 1.00 23.68 C ANISOU 1471 CB VAL B 23 1787 3484 3724 -1422 564 478 C ATOM 1472 CG1 VAL A 23 7.812 16.275 -16.995 1.00 23.87 C ANISOU 1472 CG1 VAL B 23 1784 3258 4026 -1588 633 359 C ATOM 1473 CG2 VAL A 23 9.675 16.623 -18.646 1.00 26.06 C ANISOU 1473 CG2 VAL B 23 1961 3714 4225 -1501 525 608 C ATOM 1474 N VAL A 24 12.395 16.100 -17.045 1.00 22.87 N ANISOU 1474 N VAL B 24 1672 3436 3578 -1307 211 404 N ATOM 1475 CA VAL A 24 13.802 16.040 -17.527 1.00 22.07 C ANISOU 1475 CA VAL B 24 1560 3320 3505 -1402 195 417 C ATOM 1476 C VAL A 24 14.598 14.950 -16.790 1.00 22.67 C ANISOU 1476 C VAL B 24 1612 3536 3465 -1277 89 256 C ATOM 1477 O VAL A 24 15.246 14.106 -17.415 1.00 22.57 O ANISOU 1477 O VAL B 24 1567 3697 3310 -1362 50 226 O ATOM 1478 CB VAL A 24 14.480 17.411 -17.376 1.00 21.46 C ANISOU 1478 CB VAL B 24 1328 3274 3550 -1442 164 461 C ATOM 1479 CG1 VAL A 24 16.041 17.327 -17.638 1.00 20.67 C ANISOU 1479 CG1 VAL B 24 1352 2988 3512 -1565 340 776 C ATOM 1480 CG2 VAL A 24 13.804 18.406 -18.327 1.00 21.64 C ANISOU 1480 CG2 VAL B 24 1320 2909 3993 -1640 141 486 C ATOM 1481 N ILE A 25 14.471 14.933 -15.456 1.00 23.45 N ANISOU 1481 N ILE B 25 1827 3576 3505 -1291 -81 180 N ATOM 1482 CA ILE A 25 15.196 13.998 -14.613 1.00 22.99 C ANISOU 1482 CA ILE B 25 1834 3428 3473 -1224 -104 120 C ATOM 1483 C ILE A 25 14.713 12.558 -14.791 1.00 23.85 C ANISOU 1483 C ILE B 25 1918 3620 3521 -1175 -160 11 C ATOM 1484 O ILE A 25 15.529 11.637 -14.842 1.00 23.77 O ANISOU 1484 O ILE B 25 2238 3439 3351 -1275 -117 10 O ATOM 1485 CB ILE A 25 15.149 14.437 -13.124 1.00 23.87 C ANISOU 1485 CB ILE B 25 1930 3494 3646 -1302 -115 98 C ATOM 1486 CG1 ILE A 25 15.939 15.742 -12.931 1.00 23.43 C ANISOU 1486 CG1 ILE B 25 1912 3010 3979 -1325 -91 151 C ATOM 1487 CG2 ILE A 25 15.724 13.350 -12.193 1.00 20.45 C ANISOU 1487 CG2 ILE B 25 1272 3202 3295 -1300 -288 232 C ATOM 1488 CD1 ILE A 25 17.414 15.579 -13.157 1.00 25.77 C ANISOU 1488 CD1 ILE B 25 2560 2601 4629 -1803 -291 78 C ATOM 1489 N ALA A 26 13.393 12.376 -14.866 1.00 24.65 N ANISOU 1489 N ALA B 26 2004 3748 3613 -1210 -184 5 N ATOM 1490 CA ALA A 26 12.791 11.087 -15.172 1.00 25.76 C ANISOU 1490 CA ALA B 26 2093 3932 3761 -1063 -248 -73 C ATOM 1491 C ALA A 26 13.346 10.520 -16.454 1.00 26.09 C ANISOU 1491 C ALA B 26 2116 4018 3776 -1055 -290 -95 C ATOM 1492 O ALA A 26 13.683 9.332 -16.518 1.00 26.96 O ANISOU 1492 O ALA B 26 2221 4024 3998 -1080 -350 -93 O ATOM 1493 CB ALA A 26 11.246 11.199 -15.251 1.00 25.99 C ANISOU 1493 CB ALA B 26 2025 4061 3787 -1050 -280 -76 C ATOM 1494 N LYS A 27 13.449 11.354 -17.482 1.00 25.64 N ANISOU 1494 N LYS B 27 2004 3982 3756 -1102 -293 -146 N ATOM 1495 CA LYS A 27 13.995 10.892 -18.755 1.00 25.82 C ANISOU 1495 CA LYS B 27 1990 4160 3660 -1117 -246 -197 C ATOM 1496 C LYS A 27 15.491 10.541 -18.602 1.00 25.64 C ANISOU 1496 C LYS B 27 2046 4123 3573 -1102 -226 -270 C ATOM 1497 O LYS A 27 15.946 9.477 -19.028 1.00 26.20 O ANISOU 1497 O LYS B 27 2116 4289 3549 -1101 -226 -336 O ATOM 1498 CB LYS A 27 13.777 11.947 -19.823 1.00 25.91 C ANISOU 1498 CB LYS B 27 1984 4240 3621 -1073 -229 -227 C ATOM 1499 CG LYS A 27 14.357 11.587 -21.161 1.00 28.52 C ANISOU 1499 CG LYS B 27 2130 4621 4082 -1219 -39 17 C ATOM 1500 CD LYS A 27 14.317 12.792 -22.061 1.00 29.39 C ANISOU 1500 CD LYS B 27 1935 4805 4426 -1867 354 85 C ATOM 1501 CE LYS A 27 15.090 12.509 -23.339 1.00 34.85 C ANISOU 1501 CE LYS B 27 3171 5339 4731 -1821 9 -153 C ATOM 1502 NZ LYS A 27 14.168 11.832 -24.269 1.00 30.96 N ANISOU 1502 NZ LYS B 27 2172 4829 4762 -2954 0 -362 N ATOM 1503 N ALA A 28 16.224 11.411 -17.929 1.00 25.08 N ANISOU 1503 N ALA B 28 1991 4027 3508 -1223 -264 -333 N ATOM 1504 CA ALA A 28 17.669 11.221 -17.707 1.00 25.45 C ANISOU 1504 CA ALA B 28 2160 3988 3520 -1181 -315 -365 C ATOM 1505 C ALA A 28 17.947 9.934 -16.932 1.00 25.89 C ANISOU 1505 C ALA B 28 2262 3953 3622 -1237 -320 -424 C ATOM 1506 O ALA A 28 18.845 9.174 -17.287 1.00 25.92 O ANISOU 1506 O ALA B 28 2151 4081 3614 -1228 -305 -460 O ATOM 1507 CB ALA A 28 18.251 12.423 -16.963 1.00 24.66 C ANISOU 1507 CB ALA B 28 2073 3900 3394 -1304 -267 -348 C ATOM 1508 N LEU A 29 17.179 9.686 -15.874 1.00 26.81 N ANISOU 1508 N LEU B 29 2390 4006 3788 -1232 -248 -396 N ATOM 1509 CA LEU A 29 17.327 8.436 -15.119 1.00 28.71 C ANISOU 1509 CA LEU B 29 2781 4093 4032 -1197 -203 -383 C ATOM 1510 C LEU A 29 17.165 7.200 -15.997 1.00 29.93 C ANISOU 1510 C LEU B 29 3036 4144 4192 -1168 -203 -382 C ATOM 1511 O LEU A 29 17.856 6.198 -15.807 1.00 30.58 O ANISOU 1511 O LEU B 29 3141 4140 4338 -1215 -86 -303 O ATOM 1512 CB LEU A 29 16.343 8.390 -13.948 1.00 29.30 C ANISOU 1512 CB LEU B 29 2967 4133 4031 -1130 -171 -379 C ATOM 1513 CG LEU A 29 16.783 9.350 -12.842 1.00 29.60 C ANISOU 1513 CG LEU B 29 2969 4182 4095 -1182 -225 -415 C ATOM 1514 CD1 LEU A 29 15.716 9.427 -11.766 1.00 30.95 C ANISOU 1514 CD1 LEU B 29 3127 4298 4333 -1135 49 -266 C ATOM 1515 CD2 LEU A 29 18.131 8.937 -12.248 1.00 30.74 C ANISOU 1515 CD2 LEU B 29 3234 4065 4380 -1215 -265 -336 C ATOM 1516 N ASP A 30 16.259 7.288 -16.965 1.00 31.55 N ANISOU 1516 N ASP B 30 3284 4232 4472 -1213 -255 -479 N ATOM 1517 CA ASP A 30 16.017 6.208 -17.920 1.00 32.73 C ANISOU 1517 CA ASP B 30 3482 4287 4665 -1262 -326 -523 C ATOM 1518 C ASP A 30 17.066 6.056 -19.009 1.00 32.85 C ANISOU 1518 C ASP B 30 3612 4185 4685 -1223 -346 -514 C ATOM 1519 O ASP A 30 17.508 4.935 -19.310 1.00 32.90 O ANISOU 1519 O ASP B 30 3570 4103 4827 -1360 -296 -499 O ATOM 1520 CB ASP A 30 14.668 6.422 -18.565 1.00 33.93 C ANISOU 1520 CB ASP B 30 3690 4428 4774 -1277 -342 -520 C ATOM 1521 CG ASP A 30 13.641 5.493 -18.029 1.00 36.86 C ANISOU 1521 CG ASP B 30 3894 4964 5146 -1420 -386 -605 C ATOM 1522 OD1 ASP A 30 13.588 5.318 -16.783 1.00 40.40 O ANISOU 1522 OD1 ASP B 30 4250 5514 5585 -1491 -332 -517 O ATOM 1523 OD2 ASP A 30 12.913 4.920 -18.865 1.00 42.46 O ANISOU 1523 OD2 ASP B 30 4587 5690 5854 -1658 -635 -812 O ATOM 1524 N GLU A 31 17.451 7.185 -19.607 1.00 32.85 N ANISOU 1524 N GLU B 31 3689 4067 4722 -1196 -358 -494 N ATOM 1525 CA GLU A 31 18.439 7.209 -20.699 1.00 32.45 C ANISOU 1525 CA GLU B 31 3693 4004 4630 -1070 -375 -558 C ATOM 1526 C GLU A 31 19.853 6.943 -20.193 1.00 30.86 C ANISOU 1526 C GLU B 31 3520 3751 4454 -1076 -385 -513 C ATOM 1527 O GLU A 31 20.661 6.304 -20.888 1.00 30.57 O ANISOU 1527 O GLU B 31 3469 3660 4483 -1189 -345 -432 O ATOM 1528 CB GLU A 31 18.452 8.579 -21.419 1.00 32.96 C ANISOU 1528 CB GLU B 31 3747 4049 4726 -1024 -381 -572 C ATOM 1529 CG GLU A 31 17.082 9.182 -21.837 1.00 36.99 C ANISOU 1529 CG GLU B 31 4228 4605 5220 -882 -591 -948 C ATOM 1530 CD GLU A 31 16.413 8.528 -23.045 1.00 41.54 C ANISOU 1530 CD GLU B 31 4591 5489 5703 -620 -682 -1242 C ATOM 1531 OE1 GLU A 31 15.169 8.676 -23.169 1.00 42.99 O ANISOU 1531 OE1 GLU B 31 4774 5668 5890 -598 -773 -1310 O ATOM 1532 OE2 GLU A 31 17.108 7.885 -23.871 1.00 43.68 O ANISOU 1532 OE2 GLU B 31 4896 5815 5884 -543 -630 -1426 O ATOM 1533 N PHE A 32 20.157 7.443 -18.999 1.00 29.37 N ANISOU 1533 N PHE B 32 3383 3541 4233 -1104 -393 -521 N ATOM 1534 CA PHE A 32 21.550 7.466 -18.519 1.00 28.80 C ANISOU 1534 CA PHE B 32 3354 3530 4058 -1018 -374 -567 C ATOM 1535 C PHE A 32 21.803 6.570 -17.330 1.00 29.25 C ANISOU 1535 C PHE B 32 3483 3552 4078 -998 -398 -663 C ATOM 1536 O PHE A 32 22.934 6.114 -17.130 1.00 29.97 O ANISOU 1536 O PHE B 32 3624 3674 4089 -923 -459 -830 O ATOM 1537 CB PHE A 32 21.977 8.887 -18.124 1.00 27.14 C ANISOU 1537 CB PHE B 32 3022 3329 3959 -1124 -368 -554 C ATOM 1538 CG PHE A 32 22.081 9.844 -19.277 1.00 26.19 C ANISOU 1538 CG PHE B 32 2751 3283 3916 -1081 -353 -498 C ATOM 1539 CD1 PHE A 32 22.435 9.393 -20.551 1.00 25.88 C ANISOU 1539 CD1 PHE B 32 2611 3184 4039 -1064 -424 -284 C ATOM 1540 CD2 PHE A 32 21.870 11.211 -19.082 1.00 24.21 C ANISOU 1540 CD2 PHE B 32 2288 3108 3803 -980 -321 -241 C ATOM 1541 CE1 PHE A 32 22.539 10.264 -21.619 1.00 22.65 C ANISOU 1541 CE1 PHE B 32 1674 3110 3820 -1599 175 -112 C ATOM 1542 CE2 PHE A 32 21.999 12.115 -20.158 1.00 23.73 C ANISOU 1542 CE2 PHE B 32 1765 3418 3830 -1078 -371 -434 C ATOM 1543 CZ PHE A 32 22.312 11.637 -21.422 1.00 23.75 C ANISOU 1543 CZ PHE B 32 1792 3309 3920 -1094 24 -230 C ATOM 1544 N LYS A 33 20.778 6.384 -16.499 1.00 29.15 N ANISOU 1544 N LYS B 33 3593 3510 3969 -1124 -337 -591 N ATOM 1545 CA LYS A 33 20.939 5.649 -15.247 1.00 30.09 C ANISOU 1545 CA LYS B 33 3737 3701 3994 -1139 -320 -585 C ATOM 1546 C LYS A 33 21.646 6.583 -14.258 1.00 28.72 C ANISOU 1546 C LYS B 33 3600 3479 3830 -1282 -250 -542 C ATOM 1547 O LYS A 33 21.153 6.789 -13.153 1.00 29.09 O ANISOU 1547 O LYS B 33 3661 3492 3896 -1364 -171 -471 O ATOM 1548 CB LYS A 33 21.547 4.255 -15.512 1.00 30.53 C ANISOU 1548 CB LYS B 33 3778 3742 4077 -1036 -313 -607 C ATOM 1549 CG LYS A 33 22.806 3.918 -14.712 1.00 33.27 C ANISOU 1549 CG LYS B 33 3879 4284 4475 -1076 -142 -694 C ATOM 1550 CD LYS A 33 23.798 3.062 -15.516 1.00 37.58 C ANISOU 1550 CD LYS B 33 4254 4868 5156 -1085 35 -715 C ATOM 1551 CE LYS A 33 25.248 3.257 -15.020 1.00 37.18 C ANISOU 1551 CE LYS B 33 3901 4885 5338 -1361 179 -694 C ATOM 1552 NZ LYS A 33 26.261 2.473 -15.793 1.00 37.89 N ANISOU 1552 NZ LYS B 33 3917 4918 5558 -1461 381 -434 N ATOM 1553 N GLU A 34 22.824 7.084 -14.613 1.00 28.33 N ANISOU 1553 N GLU B 34 3566 3514 3682 -1225 -223 -468 N ATOM 1554 CA GLU A 34 23.599 7.993 -13.743 1.00 26.32 C ANISOU 1554 CA GLU B 34 3160 3340 3498 -1281 -210 -299 C ATOM 1555 C GLU A 34 24.232 9.156 -14.530 1.00 23.69 C ANISOU 1555 C GLU B 34 2852 2962 3185 -1328 -250 -272 C ATOM 1556 O GLU A 34 24.695 8.988 -15.662 1.00 21.83 O ANISOU 1556 O GLU B 34 2574 2717 3000 -1595 -113 -12 O ATOM 1557 CB GLU A 34 24.637 7.158 -12.979 1.00 27.12 C ANISOU 1557 CB GLU B 34 3229 3458 3618 -1225 -207 -384 C ATOM 1558 CG GLU A 34 25.681 6.490 -13.891 1.00 30.32 C ANISOU 1558 CG GLU B 34 3687 3910 3922 -973 -139 -298 C ATOM 1559 CD GLU A 34 26.953 6.060 -13.177 1.00 29.70 C ANISOU 1559 CD GLU B 34 3477 3912 3892 -1132 -77 -291 C ATOM 1560 OE1 GLU A 34 26.935 5.874 -11.930 1.00 33.33 O ANISOU 1560 OE1 GLU B 34 3859 4524 4281 -1017 178 -13 O ATOM 1561 OE2 GLU A 34 27.991 5.911 -13.883 1.00 36.23 O ANISOU 1561 OE2 GLU B 34 4490 4758 4517 -582 127 -306 O ATOM 1562 N PHE A 35 24.224 10.340 -13.936 1.00 21.51 N ANISOU 1562 N PHE B 35 2600 2679 2892 -1312 -279 -119 N ATOM 1563 CA PHE A 35 24.567 11.521 -14.683 1.00 20.11 C ANISOU 1563 CA PHE B 35 2381 2522 2736 -1265 -339 -262 C ATOM 1564 C PHE A 35 24.825 12.683 -13.728 1.00 19.29 C ANISOU 1564 C PHE B 35 2308 2440 2580 -1242 -332 -267 C ATOM 1565 O PHE A 35 24.442 12.640 -12.560 1.00 19.31 O ANISOU 1565 O PHE B 35 2157 2523 2657 -1435 -304 -263 O ATOM 1566 CB PHE A 35 23.417 11.868 -15.661 1.00 19.85 C ANISOU 1566 CB PHE B 35 2343 2531 2667 -1209 -403 -264 C ATOM 1567 CG PHE A 35 22.116 12.096 -14.973 1.00 18.40 C ANISOU 1567 CG PHE B 35 2072 2470 2447 -1310 -243 -182 C ATOM 1568 CD1 PHE A 35 21.802 13.347 -14.444 1.00 18.53 C ANISOU 1568 CD1 PHE B 35 1939 2830 2269 -1299 -350 -321 C ATOM 1569 CD2 PHE A 35 21.210 11.054 -14.816 1.00 21.53 C ANISOU 1569 CD2 PHE B 35 2436 3029 2714 -1204 -646 -640 C ATOM 1570 CE1 PHE A 35 20.583 13.556 -13.771 1.00 19.24 C ANISOU 1570 CE1 PHE B 35 2143 2714 2451 -1184 -368 -357 C ATOM 1571 CE2 PHE A 35 20.005 11.248 -14.145 1.00 18.63 C ANISOU 1571 CE2 PHE B 35 1937 2652 2486 -1386 59 -700 C ATOM 1572 CZ PHE A 35 19.687 12.507 -13.630 1.00 20.42 C ANISOU 1572 CZ PHE B 35 2281 2832 2644 -1248 -214 -301 C ATOM 1573 N CYS A 36 25.464 13.705 -14.260 1.00 18.14 N ANISOU 1573 N CYS B 36 2196 2171 2521 -1391 -190 -211 N ATOM 1574 CA CYS A 36 25.630 14.991 -13.593 1.00 18.32 C ANISOU 1574 CA CYS B 36 2202 2202 2555 -1340 -133 -36 C ATOM 1575 C CYS A 36 24.608 15.988 -14.136 1.00 17.58 C ANISOU 1575 C CYS B 36 2072 2131 2475 -1398 -46 20 C ATOM 1576 O CYS A 36 24.388 16.079 -15.351 1.00 16.78 O ANISOU 1576 O CYS B 36 1943 2001 2431 -1563 -131 200 O ATOM 1577 CB CYS A 36 27.044 15.513 -13.841 1.00 18.16 C ANISOU 1577 CB CYS B 36 2158 2123 2618 -1335 -88 -178 C ATOM 1578 SG CYS A 36 27.289 17.266 -13.469 1.00 20.56 S ANISOU 1578 SG CYS B 36 2392 2352 3066 -1403 -48 -54 S ATOM 1579 N ILE A 37 23.999 16.748 -13.236 1.00 17.47 N ANISOU 1579 N ILE B 37 1980 2140 2515 -1454 32 187 N ATOM 1580 CA ILE A 37 23.087 17.795 -13.649 1.00 16.32 C ANISOU 1580 CA ILE B 37 1884 2034 2283 -1502 160 352 C ATOM 1581 C ILE A 37 23.782 19.127 -13.505 1.00 16.84 C ANISOU 1581 C ILE B 37 2060 2091 2248 -1442 188 406 C ATOM 1582 O ILE A 37 24.477 19.389 -12.510 1.00 15.62 O ANISOU 1582 O ILE B 37 2045 1945 1944 -1609 264 399 O ATOM 1583 CB ILE A 37 21.709 17.722 -12.918 1.00 17.00 C ANISOU 1583 CB ILE B 37 1903 2173 2380 -1428 150 375 C ATOM 1584 CG1 ILE A 37 20.750 18.758 -13.497 1.00 19.19 C ANISOU 1584 CG1 ILE B 37 1869 2791 2630 -1457 463 424 C ATOM 1585 CG2 ILE A 37 21.860 17.826 -11.404 1.00 15.05 C ANISOU 1585 CG2 ILE B 37 1450 2157 2108 -1449 383 44 C ATOM 1586 CD1 ILE A 37 19.311 18.494 -13.146 1.00 22.80 C ANISOU 1586 CD1 ILE B 37 2363 3514 2783 -1951 857 989 C ATOM 1587 N VAL A 38 23.676 19.916 -14.575 1.00 16.06 N ANISOU 1587 N VAL B 38 2068 1887 2145 -1486 214 540 N ATOM 1588 CA VAL A 38 24.278 21.207 -14.592 1.00 16.29 C ANISOU 1588 CA VAL B 38 1913 2012 2264 -1492 289 600 C ATOM 1589 C VAL A 38 23.275 22.234 -14.136 1.00 15.66 C ANISOU 1589 C VAL B 38 1805 2000 2145 -1385 375 624 C ATOM 1590 O VAL A 38 22.147 22.263 -14.617 1.00 16.13 O ANISOU 1590 O VAL B 38 1920 2016 2190 -1318 472 687 O ATOM 1591 CB VAL A 38 24.870 21.572 -15.998 1.00 15.74 C ANISOU 1591 CB VAL B 38 1901 1972 2107 -1478 338 534 C ATOM 1592 CG1 VAL A 38 25.381 23.020 -15.970 1.00 16.76 C ANISOU 1592 CG1 VAL B 38 1814 1934 2619 -1570 20 471 C ATOM 1593 CG2 VAL A 38 25.978 20.614 -16.331 1.00 15.97 C ANISOU 1593 CG2 VAL B 38 1867 1979 2220 -1462 358 545 C ATOM 1594 N ASN A 39 23.690 23.053 -13.180 1.00 16.29 N ANISOU 1594 N ASN B 39 1665 2042 2480 -1382 356 617 N ATOM 1595 CA ASN A 39 22.906 24.181 -12.728 1.00 17.04 C ANISOU 1595 CA ASN B 39 1832 1998 2643 -1439 356 643 C ATOM 1596 C ASN A 39 23.437 25.509 -13.299 1.00 17.00 C ANISOU 1596 C ASN B 39 1695 2021 2743 -1434 299 612 C ATOM 1597 O ASN A 39 24.650 25.791 -13.249 1.00 17.74 O ANISOU 1597 O ASN B 39 1650 2175 2914 -1380 339 659 O ATOM 1598 CB ASN A 39 22.818 24.166 -11.181 1.00 17.23 C ANISOU 1598 CB ASN B 39 1869 1930 2746 -1426 239 552 C ATOM 1599 CG ASN A 39 21.868 25.219 -10.629 1.00 18.04 C ANISOU 1599 CG ASN B 39 1948 2214 2691 -1527 514 690 C ATOM 1600 OD1 ASN A 39 20.942 25.693 -11.323 1.00 19.42 O ANISOU 1600 OD1 ASN B 39 1745 2368 3264 -1587 476 597 O ATOM 1601 ND2 ASN A 39 22.104 25.609 -9.379 1.00 18.15 N ANISOU 1601 ND2 ASN B 39 1941 1961 2995 -1629 150 460 N ATOM 1602 N ALA A 40 22.528 26.308 -13.872 1.00 17.11 N ANISOU 1602 N ALA B 40 1683 2084 2732 -1460 266 637 N ATOM 1603 CA ALA A 40 22.828 27.667 -14.300 1.00 17.69 C ANISOU 1603 CA ALA B 40 1920 2024 2775 -1317 175 474 C ATOM 1604 C ALA A 40 22.835 28.553 -13.060 1.00 18.06 C ANISOU 1604 C ALA B 40 1930 2128 2801 -1249 252 437 C ATOM 1605 O ALA A 40 21.816 29.208 -12.727 1.00 18.06 O ANISOU 1605 O ALA B 40 1854 2053 2955 -1265 181 259 O ATOM 1606 CB ALA A 40 21.782 28.169 -15.284 1.00 18.64 C ANISOU 1606 CB ALA B 40 1947 2220 2915 -1328 261 598 C ATOM 1607 N ALA A 41 23.988 28.584 -12.400 1.00 16.26 N ANISOU 1607 N ALA B 41 1674 1920 2584 -1267 264 535 N ATOM 1608 CA ALA A 41 24.126 29.216 -11.100 1.00 15.72 C ANISOU 1608 CA ALA B 41 1794 1661 2515 -1237 253 518 C ATOM 1609 C ALA A 41 24.597 30.669 -11.165 1.00 16.92 C ANISOU 1609 C ALA B 41 1975 1844 2609 -1106 248 495 C ATOM 1610 O ALA A 41 24.990 31.166 -12.224 1.00 17.26 O ANISOU 1610 O ALA B 41 2101 1731 2725 -1154 264 456 O ATOM 1611 CB ALA A 41 25.071 28.398 -10.265 1.00 15.94 C ANISOU 1611 CB ALA B 41 1698 1817 2539 -1236 238 494 C ATOM 1612 N ASN A 42 24.495 31.367 -10.042 1.00 17.07 N ANISOU 1612 N ASN B 42 1981 1819 2683 -1027 241 475 N ATOM 1613 CA ASN A 42 25.243 32.579 -9.865 1.00 18.05 C ANISOU 1613 CA ASN B 42 2102 1888 2865 -884 216 477 C ATOM 1614 C ASN A 42 26.471 32.295 -8.962 1.00 17.99 C ANISOU 1614 C ASN B 42 2002 1847 2983 -970 153 540 C ATOM 1615 O ASN A 42 26.531 31.249 -8.309 1.00 17.12 O ANISOU 1615 O ASN B 42 1806 1677 3021 -1022 133 604 O ATOM 1616 CB ASN A 42 24.341 33.707 -9.357 1.00 19.01 C ANISOU 1616 CB ASN B 42 2200 2114 2905 -796 289 519 C ATOM 1617 CG ASN A 42 23.735 33.400 -8.033 1.00 18.47 C ANISOU 1617 CG ASN B 42 2182 2055 2780 -821 349 395 C ATOM 1618 OD1 ASN A 42 24.441 33.300 -7.027 1.00 19.23 O ANISOU 1618 OD1 ASN B 42 2164 2017 3125 -932 532 81 O ATOM 1619 ND2 ASN A 42 22.421 33.220 -8.015 1.00 18.86 N ANISOU 1619 ND2 ASN B 42 1874 2590 2700 -626 402 440 N ATOM 1620 N GLU A 43 27.447 33.207 -8.936 1.00 18.36 N ANISOU 1620 N GLU B 43 2026 1889 3058 -1026 179 523 N ATOM 1621 CA GLU A 43 28.732 32.947 -8.266 1.00 17.70 C ANISOU 1621 CA GLU B 43 1861 1689 3173 -1102 246 486 C ATOM 1622 C GLU A 43 28.596 32.768 -6.719 1.00 17.54 C ANISOU 1622 C GLU B 43 1789 1740 3133 -1106 284 506 C ATOM 1623 O GLU A 43 29.488 32.192 -6.075 1.00 17.19 O ANISOU 1623 O GLU B 43 1785 1668 3076 -1219 471 716 O ATOM 1624 CB GLU A 43 29.783 34.010 -8.670 1.00 18.85 C ANISOU 1624 CB GLU B 43 1964 1912 3283 -940 208 438 C ATOM 1625 CG GLU A 43 29.530 35.370 -8.019 1.00 17.74 C ANISOU 1625 CG GLU B 43 2051 1380 3309 -1256 230 481 C ATOM 1626 CD GLU A 43 30.552 36.419 -8.377 1.00 20.23 C ANISOU 1626 CD GLU B 43 2120 2018 3546 -1164 338 325 C ATOM 1627 OE1 GLU A 43 31.555 36.081 -9.038 1.00 22.10 O ANISOU 1627 OE1 GLU B 43 1570 2475 4349 -1653 501 124 O ATOM 1628 OE2 GLU A 43 30.336 37.593 -8.011 1.00 24.10 O ANISOU 1628 OE2 GLU B 43 2663 2344 4148 -1001 620 597 O ATOM 1629 N HIS A 44 27.475 33.235 -6.141 1.00 17.04 N ANISOU 1629 N HIS B 44 1729 1570 3175 -1271 151 389 N ATOM 1630 CA HIS A 44 27.223 33.154 -4.689 1.00 16.63 C ANISOU 1630 CA HIS B 44 1681 1559 3078 -1317 276 247 C ATOM 1631 C HIS A 44 26.368 31.961 -4.355 1.00 17.26 C ANISOU 1631 C HIS B 44 1841 1580 3134 -1276 183 204 C ATOM 1632 O HIS A 44 26.049 31.690 -3.186 1.00 17.72 O ANISOU 1632 O HIS B 44 1788 1688 3256 -1443 316 183 O ATOM 1633 CB HIS A 44 26.644 34.460 -4.131 1.00 17.03 C ANISOU 1633 CB HIS B 44 1670 1672 3126 -1383 229 218 C ATOM 1634 CG HIS A 44 27.693 35.504 -3.893 1.00 19.49 C ANISOU 1634 CG HIS B 44 2376 1583 3444 -1646 441 61 C ATOM 1635 ND1 HIS A 44 28.357 35.619 -2.692 1.00 22.08 N ANISOU 1635 ND1 HIS B 44 2978 1725 3687 -1992 453 -99 N ATOM 1636 CD2 HIS A 44 28.267 36.405 -4.729 1.00 22.12 C ANISOU 1636 CD2 HIS B 44 2752 2126 3524 -1496 860 -54 C ATOM 1637 CE1 HIS A 44 29.279 36.580 -2.787 1.00 21.65 C ANISOU 1637 CE1 HIS B 44 2754 2080 3393 -1943 959 190 C ATOM 1638 NE2 HIS A 44 29.229 37.078 -4.008 1.00 22.02 N ANISOU 1638 NE2 HIS B 44 2803 1839 3722 -1944 910 -123 N ATOM 1639 N MET A 45 26.060 31.213 -5.408 1.00 17.41 N ANISOU 1639 N MET B 45 1899 1538 3177 -1183 120 151 N ATOM 1640 CA MET A 45 25.327 29.971 -5.294 1.00 16.08 C ANISOU 1640 CA MET B 45 1685 1344 3079 -1134 260 292 C ATOM 1641 C MET A 45 23.947 30.149 -4.646 1.00 17.76 C ANISOU 1641 C MET B 45 2011 1503 3233 -1039 132 212 C ATOM 1642 O MET A 45 23.480 29.298 -3.882 1.00 16.86 O ANISOU 1642 O MET B 45 1824 1373 3206 -1266 203 375 O ATOM 1643 CB MET A 45 26.196 28.917 -4.590 1.00 17.00 C ANISOU 1643 CB MET B 45 1807 1575 3076 -973 278 181 C ATOM 1644 CG MET A 45 27.420 28.463 -5.418 1.00 15.01 C ANISOU 1644 CG MET B 45 1348 1543 2809 -941 801 285 C ATOM 1645 SD MET A 45 27.105 27.559 -6.949 1.00 11.67 S ANISOU 1645 SD MET B 45 1098 1416 1920 -922 440 -5 S ATOM 1646 CE MET A 45 28.412 28.298 -8.000 1.00 17.03 C ANISOU 1646 CE MET B 45 1756 1971 2742 -214 627 213 C ATOM 1647 N SER A 46 23.300 31.267 -4.960 1.00 17.41 N ANISOU 1647 N SER B 46 1919 1382 3314 -1010 97 189 N ATOM 1648 CA SER A 46 21.968 31.553 -4.440 1.00 19.31 C ANISOU 1648 CA SER B 46 2270 1531 3533 -838 47 9 C ATOM 1649 C SER A 46 20.886 31.097 -5.413 1.00 18.59 C ANISOU 1649 C SER B 46 2085 1535 3441 -874 25 55 C ATOM 1650 O SER A 46 20.776 31.619 -6.522 1.00 19.54 O ANISOU 1650 O SER B 46 2102 1681 3639 -910 -9 -36 O ATOM 1651 CB SER A 46 21.817 33.047 -4.147 1.00 19.61 C ANISOU 1651 CB SER B 46 2286 1554 3611 -926 183 70 C ATOM 1652 OG SER A 46 20.802 33.279 -3.186 1.00 21.28 O ANISOU 1652 OG SER B 46 2535 1518 4033 -396 28 -88 O ATOM 1653 N HIS A 47 20.090 30.121 -4.990 1.00 19.54 N ANISOU 1653 N HIS B 47 2226 1738 3460 -921 -12 22 N ATOM 1654 CA HIS A 47 19.354 29.275 -5.921 1.00 20.05 C ANISOU 1654 CA HIS B 47 2237 1888 3494 -885 -58 54 C ATOM 1655 C HIS A 47 17.868 29.615 -5.969 1.00 20.99 C ANISOU 1655 C HIS B 47 2336 1951 3686 -852 -30 129 C ATOM 1656 O HIS A 47 17.023 28.729 -6.096 1.00 21.29 O ANISOU 1656 O HIS B 47 2235 2035 3818 -927 -129 82 O ATOM 1657 CB HIS A 47 19.581 27.797 -5.597 1.00 18.56 C ANISOU 1657 CB HIS B 47 1976 1686 3387 -967 -55 32 C ATOM 1658 CG HIS A 47 21.014 27.373 -5.678 1.00 19.77 C ANISOU 1658 CG HIS B 47 2475 1884 3152 -807 -120 -70 C ATOM 1659 ND1 HIS A 47 21.831 27.709 -6.737 1.00 16.56 N ANISOU 1659 ND1 HIS B 47 2234 1701 2356 -938 -80 -99 N ATOM 1660 CD2 HIS A 47 21.777 26.641 -4.832 1.00 18.12 C ANISOU 1660 CD2 HIS B 47 2471 1561 2850 -842 -91 -46 C ATOM 1661 CE1 HIS A 47 23.035 27.202 -6.540 1.00 17.13 C ANISOU 1661 CE1 HIS B 47 2626 1732 2150 -705 -164 6 C ATOM 1662 NE2 HIS A 47 23.029 26.550 -5.391 1.00 20.20 N ANISOU 1662 NE2 HIS B 47 2602 1818 3254 -624 -84 4 N ATOM 1663 N GLY A 48 17.557 30.903 -5.865 1.00 22.75 N ANISOU 1663 N GLY B 48 2449 2331 3861 -783 25 265 N ATOM 1664 CA GLY A 48 16.208 31.339 -5.559 1.00 22.94 C ANISOU 1664 CA GLY B 48 2351 2516 3848 -781 61 349 C ATOM 1665 C GLY A 48 15.253 31.314 -6.736 1.00 23.16 C ANISOU 1665 C GLY B 48 2318 2559 3921 -823 75 416 C ATOM 1666 O GLY A 48 14.038 31.411 -6.564 1.00 24.17 O ANISOU 1666 O GLY B 48 2302 2742 4138 -850 183 533 O ATOM 1667 N GLY A 49 15.806 31.183 -7.937 1.00 22.68 N ANISOU 1667 N GLY B 49 2185 2616 3814 -875 145 478 N ATOM 1668 CA GLY A 49 15.067 31.473 -9.152 1.00 22.80 C ANISOU 1668 CA GLY B 49 2269 2708 3683 -842 96 584 C ATOM 1669 C GLY A 49 15.421 30.530 -10.285 1.00 22.49 C ANISOU 1669 C GLY B 49 2246 2755 3541 -870 100 612 C ATOM 1670 O GLY A 49 16.488 29.916 -10.284 1.00 22.26 O ANISOU 1670 O GLY B 49 2248 2624 3582 -1044 139 729 O ATOM 1671 N GLY A 50 14.521 30.415 -11.256 1.00 23.65 N ANISOU 1671 N GLY B 50 2398 3021 3563 -779 92 539 N ATOM 1672 CA GLY A 50 14.824 29.706 -12.515 1.00 23.82 C ANISOU 1672 CA GLY B 50 2450 3234 3366 -776 96 503 C ATOM 1673 C GLY A 50 15.119 28.225 -12.339 1.00 23.71 C ANISOU 1673 C GLY B 50 2452 3282 3274 -820 92 525 C ATOM 1674 O GLY A 50 14.572 27.610 -11.447 1.00 23.95 O ANISOU 1674 O GLY B 50 2451 3460 3188 -784 186 546 O ATOM 1675 N VAL A 51 15.975 27.650 -13.185 1.00 24.02 N ANISOU 1675 N VAL B 51 2460 3425 3241 -834 92 511 N ATOM 1676 CA VAL A 51 16.370 26.243 -13.015 1.00 24.18 C ANISOU 1676 CA VAL B 51 2459 3439 3290 -900 159 495 C ATOM 1677 C VAL A 51 17.093 26.029 -11.699 1.00 23.28 C ANISOU 1677 C VAL B 51 2329 3352 3164 -887 177 466 C ATOM 1678 O VAL A 51 17.020 24.947 -11.145 1.00 22.38 O ANISOU 1678 O VAL B 51 2368 3131 3004 -879 211 489 O ATOM 1679 CB VAL A 51 17.323 25.663 -14.082 1.00 25.47 C ANISOU 1679 CB VAL B 51 2654 3644 3378 -925 73 422 C ATOM 1680 CG1 VAL A 51 16.651 24.584 -14.929 1.00 26.86 C ANISOU 1680 CG1 VAL B 51 2699 3624 3880 -1052 164 400 C ATOM 1681 CG2 VAL A 51 18.019 26.749 -14.890 1.00 26.75 C ANISOU 1681 CG2 VAL B 51 2924 3473 3767 -1072 264 677 C ATOM 1682 N ALA A 52 17.817 27.050 -11.234 1.00 22.45 N ANISOU 1682 N ALA B 52 2238 3225 3066 -880 243 423 N ATOM 1683 CA ALA A 52 18.537 26.950 -9.981 1.00 21.29 C ANISOU 1683 CA ALA B 52 2038 3043 3005 -901 311 440 C ATOM 1684 C ALA A 52 17.539 26.606 -8.870 1.00 20.21 C ANISOU 1684 C ALA B 52 1814 2873 2989 -985 384 477 C ATOM 1685 O ALA A 52 17.771 25.666 -8.090 1.00 21.04 O ANISOU 1685 O ALA B 52 1929 2959 3103 -955 386 433 O ATOM 1686 CB ALA A 52 19.286 28.238 -9.689 1.00 21.54 C ANISOU 1686 CB ALA B 52 2049 3164 2968 -897 292 452 C ATOM 1687 N LYS A 53 16.423 27.326 -8.820 1.00 19.78 N ANISOU 1687 N LYS B 53 1789 2719 3006 -1086 370 465 N ATOM 1688 CA LYS A 53 15.346 27.003 -7.861 1.00 18.69 C ANISOU 1688 CA LYS B 53 1435 2570 3097 -1192 426 364 C ATOM 1689 C LYS A 53 14.740 25.606 -8.032 1.00 18.98 C ANISOU 1689 C LYS B 53 1585 2504 3119 -1119 325 278 C ATOM 1690 O LYS A 53 14.453 24.881 -7.032 1.00 17.37 O ANISOU 1690 O LYS B 53 1244 2414 2939 -1343 404 379 O ATOM 1691 CB LYS A 53 14.222 28.032 -7.929 1.00 19.57 C ANISOU 1691 CB LYS B 53 1572 2645 3217 -1181 406 293 C ATOM 1692 CG LYS A 53 13.130 27.776 -6.886 1.00 18.57 C ANISOU 1692 CG LYS B 53 1165 2572 3317 -1353 474 233 C ATOM 1693 CD LYS A 53 11.979 28.771 -7.060 1.00 24.28 C ANISOU 1693 CD LYS B 53 1792 3318 4115 -1130 333 -55 C ATOM 1694 CE LYS A 53 10.822 28.525 -6.041 1.00 23.07 C ANISOU 1694 CE LYS B 53 1491 2817 4457 -1761 367 -37 C ATOM 1695 NZ LYS A 53 10.017 27.293 -6.347 1.00 28.12 N ANISOU 1695 NZ LYS B 53 2574 3200 4908 -1439 81 -247 N ATOM 1696 N ALA A 54 14.472 25.257 -9.287 1.00 18.16 N ANISOU 1696 N ALA B 54 1470 2395 3034 -1154 276 294 N ATOM 1697 CA ALA A 54 13.993 23.927 -9.608 1.00 17.77 C ANISOU 1697 CA ALA B 54 1271 2328 3150 -1236 193 220 C ATOM 1698 C ALA A 54 14.927 22.868 -9.030 1.00 18.11 C ANISOU 1698 C ALA B 54 1329 2330 3219 -1303 162 210 C ATOM 1699 O ALA A 54 14.487 21.945 -8.347 1.00 18.34 O ANISOU 1699 O ALA B 54 1199 2412 3355 -1408 108 281 O ATOM 1700 CB ALA A 54 13.811 23.768 -11.129 1.00 18.35 C ANISOU 1700 CB ALA B 54 1393 2340 3238 -1255 296 240 C ATOM 1701 N ILE A 55 16.230 23.043 -9.243 1.00 16.71 N ANISOU 1701 N ILE B 55 1124 2170 3055 -1276 152 134 N ATOM 1702 CA ILE A 55 17.220 22.095 -8.777 1.00 17.58 C ANISOU 1702 CA ILE B 55 1350 2154 3174 -1304 102 135 C ATOM 1703 C ILE A 55 17.327 22.057 -7.271 1.00 17.07 C ANISOU 1703 C ILE B 55 1279 2112 3093 -1313 295 263 C ATOM 1704 O ILE A 55 17.396 20.977 -6.722 1.00 18.01 O ANISOU 1704 O ILE B 55 1683 1965 3193 -1095 153 144 O ATOM 1705 CB ILE A 55 18.648 22.468 -9.330 1.00 16.78 C ANISOU 1705 CB ILE B 55 1300 2051 3023 -1340 214 195 C ATOM 1706 CG1 ILE A 55 18.671 22.411 -10.852 1.00 20.84 C ANISOU 1706 CG1 ILE B 55 1980 2027 3911 -1455 -291 185 C ATOM 1707 CG2 ILE A 55 19.756 21.556 -8.726 1.00 16.78 C ANISOU 1707 CG2 ILE B 55 1275 2049 3050 -1354 -146 248 C ATOM 1708 CD1 ILE A 55 18.192 21.170 -11.408 1.00 23.67 C ANISOU 1708 CD1 ILE B 55 2139 2780 4071 -1407 -616 -302 C ATOM 1709 N ALA A 56 17.415 23.235 -6.624 1.00 16.75 N ANISOU 1709 N ALA B 56 1190 2145 3026 -1248 345 213 N ATOM 1710 CA ALA A 56 17.547 23.358 -5.178 1.00 17.61 C ANISOU 1710 CA ALA B 56 1211 2327 3153 -1329 416 212 C ATOM 1711 C ALA A 56 16.331 22.719 -4.523 1.00 18.12 C ANISOU 1711 C ALA B 56 1249 2379 3256 -1379 391 245 C ATOM 1712 O ALA A 56 16.421 21.992 -3.518 1.00 19.15 O ANISOU 1712 O ALA B 56 1214 2698 3362 -1429 325 134 O ATOM 1713 CB ALA A 56 17.598 24.819 -4.789 1.00 17.61 C ANISOU 1713 CB ALA B 56 1313 2302 3075 -1369 407 339 C ATOM 1714 N ASP A 57 15.172 22.994 -5.092 1.00 18.06 N ANISOU 1714 N ASP B 57 1198 2379 3284 -1301 528 121 N ATOM 1715 CA ASP A 57 13.944 22.409 -4.512 1.00 18.75 C ANISOU 1715 CA ASP B 57 1484 2181 3458 -1432 467 344 C ATOM 1716 C ASP A 57 13.896 20.896 -4.673 1.00 19.30 C ANISOU 1716 C ASP B 57 1551 2261 3518 -1393 480 319 C ATOM 1717 O ASP A 57 13.322 20.181 -3.819 1.00 19.89 O ANISOU 1717 O ASP B 57 1789 2243 3524 -1406 594 482 O ATOM 1718 CB ASP A 57 12.721 23.025 -5.164 1.00 18.82 C ANISOU 1718 CB ASP B 57 1422 2243 3485 -1421 513 262 C ATOM 1719 CG ASP A 57 12.380 24.387 -4.604 1.00 20.77 C ANISOU 1719 CG ASP B 57 1759 2339 3792 -1652 391 539 C ATOM 1720 OD1 ASP A 57 12.785 24.708 -3.470 1.00 23.51 O ANISOU 1720 OD1 ASP B 57 2360 2403 4169 -2038 476 361 O ATOM 1721 OD2 ASP A 57 11.661 25.125 -5.296 1.00 23.82 O ANISOU 1721 OD2 ASP B 57 2364 2303 4384 -1915 331 827 O ATOM 1722 N PHE A 58 14.450 20.403 -5.770 1.00 19.19 N ANISOU 1722 N PHE B 58 1495 2239 3557 -1425 372 368 N ATOM 1723 CA PHE A 58 14.477 18.960 -6.054 1.00 19.48 C ANISOU 1723 CA PHE B 58 1525 2242 3631 -1413 200 356 C ATOM 1724 C PHE A 58 15.470 18.204 -5.146 1.00 19.67 C ANISOU 1724 C PHE B 58 1592 2317 3562 -1398 176 464 C ATOM 1725 O PHE A 58 15.153 17.161 -4.584 1.00 19.98 O ANISOU 1725 O PHE B 58 1608 2268 3715 -1591 81 612 O ATOM 1726 CB PHE A 58 14.872 18.732 -7.518 1.00 20.24 C ANISOU 1726 CB PHE B 58 1602 2325 3760 -1447 99 234 C ATOM 1727 CG PHE A 58 14.653 17.302 -7.979 1.00 21.08 C ANISOU 1727 CG PHE B 58 1770 2160 4079 -1679 186 215 C ATOM 1728 CD1 PHE A 58 13.414 16.929 -8.464 1.00 25.89 C ANISOU 1728 CD1 PHE B 58 2216 2949 4670 -1710 263 -53 C ATOM 1729 CD2 PHE A 58 15.665 16.349 -7.887 1.00 22.48 C ANISOU 1729 CD2 PHE B 58 1732 2376 4433 -1762 193 73 C ATOM 1730 CE1 PHE A 58 13.171 15.600 -8.881 1.00 24.11 C ANISOU 1730 CE1 PHE B 58 2204 2107 4848 -1890 552 -211 C ATOM 1731 CE2 PHE A 58 15.474 15.021 -8.310 1.00 23.34 C ANISOU 1731 CE2 PHE B 58 1651 2799 4415 -1687 199 -76 C ATOM 1732 CZ PHE A 58 14.202 14.632 -8.782 1.00 23.39 C ANISOU 1732 CZ PHE B 58 1784 2513 4587 -1842 282 97 C ATOM 1733 N CYS A 59 16.670 18.752 -5.018 1.00 18.98 N ANISOU 1733 N CYS B 59 1400 2416 3393 -1274 145 484 N ATOM 1734 CA CYS A 59 17.783 18.152 -4.260 1.00 19.29 C ANISOU 1734 CA CYS B 59 1397 2574 3358 -1220 212 464 C ATOM 1735 C CYS A 59 17.734 18.436 -2.771 1.00 18.52 C ANISOU 1735 C CYS B 59 1338 2397 3302 -1262 160 501 C ATOM 1736 O CYS A 59 18.231 17.643 -1.965 1.00 18.45 O ANISOU 1736 O CYS B 59 1316 2270 3423 -1325 312 668 O ATOM 1737 CB CYS A 59 19.106 18.682 -4.813 1.00 17.98 C ANISOU 1737 CB CYS B 59 1311 2313 3205 -1406 205 472 C ATOM 1738 SG CYS A 59 19.425 18.141 -6.497 1.00 20.10 S ANISOU 1738 SG CYS B 59 1358 2985 3293 -1420 402 436 S ATOM 1739 N GLY A 60 17.212 19.611 -2.419 1.00 18.10 N ANISOU 1739 N GLY B 60 1238 2382 3255 -1206 201 397 N ATOM 1740 CA GLY A 60 16.853 19.903 -1.050 1.00 18.34 C ANISOU 1740 CA GLY B 60 1568 2294 3106 -1157 176 407 C ATOM 1741 C GLY A 60 17.823 20.668 -0.182 1.00 18.02 C ANISOU 1741 C GLY B 60 1741 2058 3044 -1090 272 370 C ATOM 1742 O GLY A 60 18.853 21.204 -0.676 1.00 18.05 O ANISOU 1742 O GLY B 60 1760 1965 3134 -1150 150 396 O ATOM 1743 N PRO A 61 17.513 20.719 1.129 1.00 18.17 N ANISOU 1743 N PRO B 61 1937 2024 2941 -1079 295 375 N ATOM 1744 CA PRO A 61 18.227 21.586 2.064 1.00 18.52 C ANISOU 1744 CA PRO B 61 2051 2123 2860 -990 296 346 C ATOM 1745 C PRO A 61 19.707 21.266 2.194 1.00 18.70 C ANISOU 1745 C PRO B 61 2147 2090 2867 -941 345 399 C ATOM 1746 O PRO A 61 20.506 22.199 2.402 1.00 19.45 O ANISOU 1746 O PRO B 61 2252 2219 2919 -712 221 370 O ATOM 1747 CB PRO A 61 17.514 21.328 3.406 1.00 19.00 C ANISOU 1747 CB PRO B 61 2006 2301 2911 -1141 372 323 C ATOM 1748 CG PRO A 61 16.220 20.678 3.084 1.00 19.80 C ANISOU 1748 CG PRO B 61 2087 2328 3106 -1164 263 233 C ATOM 1749 CD PRO A 61 16.417 19.960 1.793 1.00 17.99 C ANISOU 1749 CD PRO B 61 1911 1987 2936 -1082 390 233 C ATOM 1750 N ASP A 62 20.080 19.974 2.083 1.00 18.47 N ANISOU 1750 N ASP B 62 2225 2076 2714 -853 422 400 N ATOM 1751 CA ASP A 62 21.505 19.596 2.202 1.00 18.02 C ANISOU 1751 CA ASP B 62 2221 1950 2674 -1000 486 479 C ATOM 1752 C ASP A 62 22.320 20.157 1.070 1.00 17.58 C ANISOU 1752 C ASP B 62 2152 1959 2566 -997 421 447 C ATOM 1753 O ASP A 62 23.459 20.529 1.263 1.00 17.24 O ANISOU 1753 O ASP B 62 2294 1886 2370 -1220 631 586 O ATOM 1754 CB ASP A 62 21.702 18.069 2.278 1.00 18.41 C ANISOU 1754 CB ASP B 62 2264 2068 2660 -1014 599 486 C ATOM 1755 CG ASP A 62 21.197 17.483 3.591 1.00 19.67 C ANISOU 1755 CG ASP B 62 2447 2133 2893 -1275 605 553 C ATOM 1756 OD1 ASP A 62 21.182 18.191 4.625 1.00 21.82 O ANISOU 1756 OD1 ASP B 62 2394 2687 3207 -1470 922 529 O ATOM 1757 OD2 ASP A 62 20.814 16.315 3.591 1.00 23.78 O ANISOU 1757 OD2 ASP B 62 3465 2381 3187 -1326 1031 982 O ATOM 1758 N PHE A 63 21.721 20.167 -0.118 1.00 18.46 N ANISOU 1758 N PHE B 63 2240 2040 2733 -1026 376 432 N ATOM 1759 CA PHE A 63 22.332 20.726 -1.312 1.00 16.95 C ANISOU 1759 CA PHE B 63 1916 1717 2806 -1246 286 434 C ATOM 1760 C PHE A 63 22.450 22.226 -1.135 1.00 18.20 C ANISOU 1760 C PHE B 63 2098 1903 2912 -1196 237 348 C ATOM 1761 O PHE A 63 23.541 22.744 -1.276 1.00 17.90 O ANISOU 1761 O PHE B 63 1986 1696 3117 -1419 270 334 O ATOM 1762 CB PHE A 63 21.533 20.365 -2.562 1.00 16.99 C ANISOU 1762 CB PHE B 63 1824 1830 2798 -1183 275 478 C ATOM 1763 CG PHE A 63 21.825 21.224 -3.752 1.00 15.87 C ANISOU 1763 CG PHE B 63 1581 1556 2890 -1190 93 463 C ATOM 1764 CD1 PHE A 63 23.042 21.110 -4.436 1.00 16.29 C ANISOU 1764 CD1 PHE B 63 1590 1863 2734 -1301 248 639 C ATOM 1765 CD2 PHE A 63 20.897 22.171 -4.183 1.00 17.01 C ANISOU 1765 CD2 PHE B 63 1601 1741 3118 -1397 52 280 C ATOM 1766 CE1 PHE A 63 23.308 21.889 -5.554 1.00 16.17 C ANISOU 1766 CE1 PHE B 63 1533 1836 2772 -1346 -57 708 C ATOM 1767 CE2 PHE A 63 21.156 22.973 -5.298 1.00 14.37 C ANISOU 1767 CE2 PHE B 63 1775 1359 2322 -1198 318 320 C ATOM 1768 CZ PHE A 63 22.369 22.831 -5.977 1.00 16.69 C ANISOU 1768 CZ PHE B 63 1848 1509 2982 -1340 232 396 C ATOM 1769 N VAL A 64 21.343 22.899 -0.824 1.00 17.86 N ANISOU 1769 N VAL B 64 2145 1827 2811 -1203 240 281 N ATOM 1770 CA VAL A 64 21.348 24.348 -0.550 1.00 17.44 C ANISOU 1770 CA VAL B 64 2038 1870 2716 -1425 146 307 C ATOM 1771 C VAL A 64 22.408 24.725 0.482 1.00 17.41 C ANISOU 1771 C VAL B 64 2148 1922 2544 -1339 210 242 C ATOM 1772 O VAL A 64 23.213 25.641 0.257 1.00 16.23 O ANISOU 1772 O VAL B 64 1750 2016 2400 -1515 368 313 O ATOM 1773 CB VAL A 64 19.936 24.809 -0.111 1.00 18.41 C ANISOU 1773 CB VAL B 64 2244 1948 2803 -1291 155 263 C ATOM 1774 CG1 VAL A 64 19.920 26.237 0.338 1.00 18.20 C ANISOU 1774 CG1 VAL B 64 2116 1718 3082 -1604 -30 328 C ATOM 1775 CG2 VAL A 64 18.925 24.578 -1.245 1.00 17.00 C ANISOU 1775 CG2 VAL B 64 2177 1711 2569 -1671 -227 315 C ATOM 1776 N GLU A 65 22.438 24.017 1.604 1.00 16.48 N ANISOU 1776 N GLU B 65 1978 1819 2462 -1365 267 201 N ATOM 1777 CA GLU A 65 23.402 24.342 2.663 1.00 17.76 C ANISOU 1777 CA GLU B 65 2125 2031 2592 -1228 235 156 C ATOM 1778 C GLU A 65 24.840 24.055 2.224 1.00 16.74 C ANISOU 1778 C GLU B 65 2019 1813 2525 -1189 225 101 C ATOM 1779 O GLU A 65 25.756 24.789 2.571 1.00 17.76 O ANISOU 1779 O GLU B 65 2045 2152 2549 -931 152 -50 O ATOM 1780 CB GLU A 65 23.065 23.564 3.938 1.00 17.78 C ANISOU 1780 CB GLU B 65 2219 2042 2493 -1334 158 195 C ATOM 1781 CG GLU A 65 23.924 23.958 5.094 1.00 22.82 C ANISOU 1781 CG GLU B 65 2365 2893 3409 -1688 155 297 C ATOM 1782 CD GLU A 65 23.538 23.312 6.389 1.00 27.14 C ANISOU 1782 CD GLU B 65 2785 3568 3959 -2493 204 378 C ATOM 1783 OE1 GLU A 65 22.749 22.344 6.357 1.00 30.73 O ANISOU 1783 OE1 GLU B 65 3624 3479 4571 -3203 338 560 O ATOM 1784 OE2 GLU A 65 24.012 23.788 7.450 1.00 30.20 O ANISOU 1784 OE2 GLU B 65 2721 4569 4184 -2472 124 364 O ATOM 1785 N TYR A 66 25.036 22.969 1.469 1.00 17.20 N ANISOU 1785 N TYR B 66 2113 1915 2507 -1038 213 -9 N ATOM 1786 CA TYR A 66 26.365 22.634 0.953 1.00 16.34 C ANISOU 1786 CA TYR B 66 1900 1765 2541 -1043 120 54 C ATOM 1787 C TYR A 66 26.947 23.833 0.173 1.00 16.38 C ANISOU 1787 C TYR B 66 2075 1607 2541 -992 73 46 C ATOM 1788 O TYR A 66 28.106 24.215 0.365 1.00 16.69 O ANISOU 1788 O TYR B 66 2059 1604 2677 -842 -35 121 O ATOM 1789 CB TYR A 66 26.371 21.359 0.059 1.00 14.92 C ANISOU 1789 CB TYR B 66 1743 1669 2257 -1074 166 -3 C ATOM 1790 CG TYR A 66 27.782 20.984 -0.346 1.00 16.06 C ANISOU 1790 CG TYR B 66 1881 2029 2192 -1120 31 104 C ATOM 1791 CD1 TYR A 66 28.509 20.036 0.370 1.00 15.72 C ANISOU 1791 CD1 TYR B 66 1632 1795 2545 -841 294 -17 C ATOM 1792 CD2 TYR A 66 28.428 21.645 -1.404 1.00 12.15 C ANISOU 1792 CD2 TYR B 66 1374 1586 1654 -1146 584 -176 C ATOM 1793 CE1 TYR A 66 29.851 19.762 0.036 1.00 15.49 C ANISOU 1793 CE1 TYR B 66 1533 1875 2474 -1419 193 116 C ATOM 1794 CE2 TYR A 66 29.745 21.368 -1.741 1.00 14.27 C ANISOU 1794 CE2 TYR B 66 1794 1354 2272 -1286 -126 -126 C ATOM 1795 CZ TYR A 66 30.430 20.424 -1.033 1.00 15.28 C ANISOU 1795 CZ TYR B 66 1613 1896 2298 -1265 17 -201 C ATOM 1796 OH TYR A 66 31.703 20.133 -1.393 1.00 17.15 O ANISOU 1796 OH TYR B 66 1585 2281 2649 -1596 159 330 O ATOM 1797 N CYS A 67 26.143 24.376 -0.738 1.00 16.71 N ANISOU 1797 N CYS B 67 2121 1677 2552 -996 31 -61 N ATOM 1798 CA CYS A 67 26.552 25.485 -1.635 1.00 17.07 C ANISOU 1798 CA CYS B 67 2167 1685 2632 -1195 31 -44 C ATOM 1799 C CYS A 67 26.805 26.770 -0.856 1.00 17.61 C ANISOU 1799 C CYS B 67 2111 1838 2740 -1142 81 -137 C ATOM 1800 O CYS A 67 27.810 27.460 -1.069 1.00 19.52 O ANISOU 1800 O CYS B 67 2451 2147 2817 -1060 133 -185 O ATOM 1801 CB CYS A 67 25.429 25.754 -2.655 1.00 15.73 C ANISOU 1801 CB CYS B 67 1946 1510 2520 -1333 148 44 C ATOM 1802 SG CYS A 67 25.329 24.482 -3.889 1.00 17.14 S ANISOU 1802 SG CYS B 67 1819 1673 3018 -1454 167 283 S ATOM 1803 N ALA A 68 25.864 27.076 0.045 1.00 18.41 N ANISOU 1803 N ALA B 68 2087 2071 2835 -1069 -6 -216 N ATOM 1804 CA ALA A 68 25.968 28.227 0.973 1.00 17.52 C ANISOU 1804 CA ALA B 68 1771 1941 2944 -1150 -64 -168 C ATOM 1805 C ALA A 68 27.283 28.167 1.789 1.00 17.13 C ANISOU 1805 C ALA B 68 1462 1959 3086 -1232 -59 -143 C ATOM 1806 O ALA A 68 28.073 29.153 1.831 1.00 17.33 O ANISOU 1806 O ALA B 68 1521 1772 3289 -1374 -99 21 O ATOM 1807 CB ALA A 68 24.754 28.205 1.918 1.00 17.43 C ANISOU 1807 CB ALA B 68 1681 2093 2847 -1160 -29 -256 C ATOM 1808 N ASP A 69 27.533 27.011 2.410 1.00 16.73 N ANISOU 1808 N ASP B 69 1282 1902 3172 -1300 -19 -104 N ATOM 1809 CA ASP A 69 28.690 26.812 3.288 1.00 18.73 C ANISOU 1809 CA ASP B 69 1845 2060 3212 -1117 -4 -120 C ATOM 1810 C ASP A 69 30.030 26.961 2.519 1.00 18.24 C ANISOU 1810 C ASP B 69 1667 2037 3225 -1183 -66 -147 C ATOM 1811 O ASP A 69 31.037 27.481 3.024 1.00 19.24 O ANISOU 1811 O ASP B 69 1715 2288 3306 -1090 -87 -12 O ATOM 1812 CB ASP A 69 28.576 25.453 3.977 1.00 19.36 C ANISOU 1812 CB ASP B 69 1872 2193 3288 -1125 25 -151 C ATOM 1813 CG ASP A 69 27.558 25.439 5.136 1.00 21.95 C ANISOU 1813 CG ASP B 69 2336 2396 3607 -1246 -39 -290 C ATOM 1814 OD1 ASP A 69 27.022 26.510 5.516 1.00 23.97 O ANISOU 1814 OD1 ASP B 69 2086 2999 4022 -1262 -18 -298 O ATOM 1815 OD2 ASP A 69 27.287 24.322 5.674 1.00 28.58 O ANISOU 1815 OD2 ASP B 69 3646 3501 3712 -1117 -12 -253 O ATOM 1816 N TYR A 70 30.027 26.506 1.275 1.00 18.08 N ANISOU 1816 N TYR B 70 1661 2031 3178 -1152 -7 -62 N ATOM 1817 CA TYR A 70 31.217 26.436 0.480 1.00 18.42 C ANISOU 1817 CA TYR B 70 1815 2020 3162 -1083 50 -84 C ATOM 1818 C TYR A 70 31.632 27.870 0.076 1.00 17.69 C ANISOU 1818 C TYR B 70 1676 1889 3156 -1235 73 0 C ATOM 1819 O TYR A 70 32.805 28.278 0.184 1.00 19.32 O ANISOU 1819 O TYR B 70 1946 2151 3242 -945 -18 2 O ATOM 1820 CB TYR A 70 30.964 25.527 -0.751 1.00 17.71 C ANISOU 1820 CB TYR B 70 1691 1961 3075 -1222 33 -202 C ATOM 1821 CG TYR A 70 32.238 25.205 -1.512 1.00 18.47 C ANISOU 1821 CG TYR B 70 1872 2134 3010 -985 -78 -417 C ATOM 1822 CD1 TYR A 70 32.880 23.963 -1.374 1.00 17.10 C ANISOU 1822 CD1 TYR B 70 1791 1740 2963 -1286 -249 -547 C ATOM 1823 CD2 TYR A 70 32.818 26.154 -2.347 1.00 17.63 C ANISOU 1823 CD2 TYR B 70 1883 1608 3207 -1023 0 -366 C ATOM 1824 CE1 TYR A 70 34.069 23.681 -2.073 1.00 18.15 C ANISOU 1824 CE1 TYR B 70 1729 2098 3070 -1206 -93 -429 C ATOM 1825 CE2 TYR A 70 34.025 25.897 -3.044 1.00 19.36 C ANISOU 1825 CE2 TYR B 70 1867 2299 3188 -917 -372 -480 C ATOM 1826 CZ TYR A 70 34.625 24.653 -2.910 1.00 19.68 C ANISOU 1826 CZ TYR B 70 1820 2473 3184 -919 -210 -531 C ATOM 1827 OH TYR A 70 35.788 24.387 -3.604 1.00 22.02 O ANISOU 1827 OH TYR B 70 2047 3118 3200 -964 244 -72 O ATOM 1828 N VAL A 71 30.652 28.624 -0.409 1.00 17.53 N ANISOU 1828 N VAL B 71 1636 1805 3218 -1301 204 41 N ATOM 1829 CA VAL A 71 30.842 30.020 -0.777 1.00 18.76 C ANISOU 1829 CA VAL B 71 1920 1903 3304 -1249 77 -24 C ATOM 1830 C VAL A 71 31.215 30.823 0.469 1.00 18.88 C ANISOU 1830 C VAL B 71 1898 1872 3403 -1320 54 -5 C ATOM 1831 O VAL A 71 32.004 31.738 0.389 1.00 20.43 O ANISOU 1831 O VAL B 71 2118 2103 3542 -1275 -1 -35 O ATOM 1832 CB VAL A 71 29.569 30.582 -1.435 1.00 18.25 C ANISOU 1832 CB VAL B 71 1799 1855 3279 -1293 136 4 C ATOM 1833 CG1 VAL A 71 29.617 32.081 -1.540 1.00 19.75 C ANISOU 1833 CG1 VAL B 71 2103 1968 3432 -1252 106 223 C ATOM 1834 CG2 VAL A 71 29.313 29.904 -2.801 1.00 17.80 C ANISOU 1834 CG2 VAL B 71 1431 2177 3154 -1491 261 -10 C ATOM 1835 N LYS A 72 30.631 30.503 1.620 1.00 18.67 N ANISOU 1835 N LYS B 72 1817 1804 3471 -1410 25 0 N ATOM 1836 CA LYS A 72 31.073 31.166 2.837 1.00 19.89 C ANISOU 1836 CA LYS B 72 1943 1985 3628 -1437 103 49 C ATOM 1837 C LYS A 72 32.556 30.928 3.173 1.00 19.67 C ANISOU 1837 C LYS B 72 1766 2040 3667 -1523 118 28 C ATOM 1838 O LYS A 72 33.220 31.831 3.685 1.00 19.73 O ANISOU 1838 O LYS B 72 1979 1728 3787 -1577 242 115 O ATOM 1839 CB LYS A 72 30.220 30.778 4.016 1.00 19.00 C ANISOU 1839 CB LYS B 72 1847 1916 3456 -1608 99 102 C ATOM 1840 CG LYS A 72 30.625 31.449 5.331 1.00 21.25 C ANISOU 1840 CG LYS B 72 2289 1947 3836 -1790 433 263 C ATOM 1841 CD LYS A 72 29.791 30.818 6.461 1.00 24.21 C ANISOU 1841 CD LYS B 72 2947 2486 3765 -1655 620 184 C ATOM 1842 CE LYS A 72 30.223 31.365 7.825 1.00 27.60 C ANISOU 1842 CE LYS B 72 3391 2501 4593 -1677 173 -85 C ATOM 1843 NZ LYS A 72 30.289 32.844 7.812 1.00 30.22 N ANISOU 1843 NZ LYS B 72 3774 2703 5003 -1477 87 -435 N ATOM 1844 N LYS A 73 33.036 29.697 2.969 1.00 19.59 N ANISOU 1844 N LYS B 73 1639 2101 3702 -1595 166 -1 N ATOM 1845 CA LYS A 73 34.443 29.371 3.238 1.00 20.92 C ANISOU 1845 CA LYS B 73 1869 2285 3793 -1582 244 6 C ATOM 1846 C LYS A 73 35.376 29.916 2.146 1.00 20.59 C ANISOU 1846 C LYS B 73 1776 2271 3775 -1694 187 -23 C ATOM 1847 O LYS A 73 36.417 30.514 2.444 1.00 20.87 O ANISOU 1847 O LYS B 73 1583 2641 3705 -1753 343 55 O ATOM 1848 CB LYS A 73 34.616 27.856 3.372 1.00 20.93 C ANISOU 1848 CB LYS B 73 1788 2221 3941 -1613 185 -11 C ATOM 1849 CG LYS A 73 36.012 27.449 3.863 1.00 23.20 C ANISOU 1849 CG LYS B 73 2295 2424 4095 -1591 279 16 C ATOM 1850 CD LYS A 73 36.243 25.949 3.848 1.00 22.52 C ANISOU 1850 CD LYS B 73 2064 2372 4120 -1637 309 -31 C ATOM 1851 CE LYS A 73 35.392 25.240 4.887 1.00 24.10 C ANISOU 1851 CE LYS B 73 2168 2395 4594 -2013 324 -13 C ATOM 1852 NZ LYS A 73 35.734 23.771 4.938 1.00 26.44 N ANISOU 1852 NZ LYS B 73 2148 2918 4976 -1888 82 -154 N ATOM 1853 N HIS A 74 35.007 29.711 0.882 1.00 19.88 N ANISOU 1853 N HIS B 74 1714 2198 3640 -1664 149 7 N ATOM 1854 CA HIS A 74 35.975 29.842 -0.203 1.00 19.97 C ANISOU 1854 CA HIS B 74 1823 2090 3674 -1519 142 40 C ATOM 1855 C HIS A 74 35.765 31.023 -1.076 1.00 19.62 C ANISOU 1855 C HIS B 74 1847 2009 3598 -1521 146 10 C ATOM 1856 O HIS A 74 36.510 31.189 -2.023 1.00 20.49 O ANISOU 1856 O HIS B 74 1928 2015 3839 -1551 173 -30 O ATOM 1857 CB HIS A 74 35.942 28.635 -1.144 1.00 19.27 C ANISOU 1857 CB HIS B 74 1696 2007 3618 -1589 60 54 C ATOM 1858 CG HIS A 74 36.352 27.354 -0.499 1.00 21.10 C ANISOU 1858 CG HIS B 74 1828 2226 3961 -1535 54 276 C ATOM 1859 ND1 HIS A 74 37.659 27.048 -0.212 1.00 21.32 N ANISOU 1859 ND1 HIS B 74 1920 2201 3980 -1739 -31 737 N ATOM 1860 CD2 HIS A 74 35.621 26.287 -0.107 1.00 21.17 C ANISOU 1860 CD2 HIS B 74 1787 2356 3899 -1733 106 604 C ATOM 1861 CE1 HIS A 74 37.718 25.841 0.325 1.00 23.71 C ANISOU 1861 CE1 HIS B 74 1993 2828 4187 -1656 -63 782 C ATOM 1862 NE2 HIS A 74 36.494 25.356 0.391 1.00 20.45 N ANISOU 1862 NE2 HIS B 74 1544 2521 3705 -1598 70 908 N ATOM 1863 N GLY A 75 34.696 31.770 -0.838 1.00 20.03 N ANISOU 1863 N GLY B 75 1863 2157 3587 -1383 51 22 N ATOM 1864 CA GLY A 75 34.371 32.914 -1.671 1.00 18.21 C ANISOU 1864 CA GLY B 75 1654 1954 3309 -1514 174 256 C ATOM 1865 C GLY A 75 33.465 32.454 -2.806 1.00 18.17 C ANISOU 1865 C GLY B 75 1663 1852 3386 -1456 118 193 C ATOM 1866 O GLY A 75 33.214 31.243 -2.968 1.00 18.64 O ANISOU 1866 O GLY B 75 1565 2191 3324 -1563 170 275 O ATOM 1867 N PRO A 76 32.956 33.414 -3.587 1.00 18.04 N ANISOU 1867 N PRO B 76 1675 1801 3376 -1468 115 196 N ATOM 1868 CA PRO A 76 32.231 33.120 -4.823 1.00 17.85 C ANISOU 1868 CA PRO B 76 1690 1727 3364 -1424 122 182 C ATOM 1869 C PRO A 76 32.974 32.210 -5.833 1.00 17.87 C ANISOU 1869 C PRO B 76 1768 1772 3250 -1326 221 177 C ATOM 1870 O PRO A 76 34.224 32.181 -5.903 1.00 17.19 O ANISOU 1870 O PRO B 76 1585 1739 3206 -1395 140 122 O ATOM 1871 CB PRO A 76 31.881 34.496 -5.398 1.00 18.36 C ANISOU 1871 CB PRO B 76 1977 1639 3359 -1423 85 214 C ATOM 1872 CG PRO A 76 32.650 35.506 -4.557 1.00 18.25 C ANISOU 1872 CG PRO B 76 1785 1835 3314 -1535 116 248 C ATOM 1873 CD PRO A 76 33.029 34.863 -3.280 1.00 18.10 C ANISOU 1873 CD PRO B 76 1636 1712 3529 -1414 81 128 C ATOM 1874 N GLN A 77 32.196 31.407 -6.543 1.00 17.25 N ANISOU 1874 N GLN B 77 1589 1805 3159 -1399 307 174 N ATOM 1875 CA GLN A 77 32.730 30.396 -7.446 1.00 17.88 C ANISOU 1875 CA GLN B 77 1708 1830 3256 -1443 408 241 C ATOM 1876 C GLN A 77 32.086 30.549 -8.807 1.00 17.95 C ANISOU 1876 C GLN B 77 1771 1869 3178 -1474 483 244 C ATOM 1877 O GLN A 77 30.884 30.797 -8.898 1.00 19.01 O ANISOU 1877 O GLN B 77 2097 1997 3128 -1376 664 340 O ATOM 1878 CB GLN A 77 32.467 28.964 -6.939 1.00 18.06 C ANISOU 1878 CB GLN B 77 1713 1832 3314 -1456 406 208 C ATOM 1879 CG GLN A 77 32.952 28.644 -5.545 1.00 18.52 C ANISOU 1879 CG GLN B 77 1723 1820 3491 -1507 195 55 C ATOM 1880 CD GLN A 77 34.486 28.688 -5.408 1.00 19.37 C ANISOU 1880 CD GLN B 77 1800 1859 3701 -1514 575 70 C ATOM 1881 OE1 GLN A 77 35.206 28.130 -6.210 1.00 21.60 O ANISOU 1881 OE1 GLN B 77 2085 2064 4056 -1780 591 -30 O ATOM 1882 NE2 GLN A 77 34.961 29.310 -4.355 1.00 21.62 N ANISOU 1882 NE2 GLN B 77 1970 1908 4334 -1550 31 -143 N ATOM 1883 N GLN A 78 32.878 30.353 -9.861 1.00 18.86 N ANISOU 1883 N GLN B 78 1977 1906 3282 -1579 495 315 N ATOM 1884 CA GLN A 78 32.379 30.351 -11.235 1.00 18.97 C ANISOU 1884 CA GLN B 78 2085 1864 3258 -1584 556 345 C ATOM 1885 C GLN A 78 31.971 28.927 -11.656 1.00 19.51 C ANISOU 1885 C GLN B 78 2101 2040 3269 -1482 415 263 C ATOM 1886 O GLN A 78 31.202 28.746 -12.606 1.00 19.94 O ANISOU 1886 O GLN B 78 2348 1928 3298 -1445 355 147 O ATOM 1887 CB GLN A 78 33.442 31.018 -12.182 1.00 19.66 C ANISOU 1887 CB GLN B 78 2056 1940 3473 -1619 544 352 C ATOM 1888 CG GLN A 78 33.922 32.379 -11.672 1.00 22.45 C ANISOU 1888 CG GLN B 78 2542 2273 3714 -1664 434 397 C ATOM 1889 CD GLN A 78 32.796 33.340 -11.277 1.00 25.71 C ANISOU 1889 CD GLN B 78 3185 2483 4099 -1799 234 697 C ATOM 1890 OE1 GLN A 78 31.805 33.490 -12.001 1.00 27.87 O ANISOU 1890 OE1 GLN B 78 3969 2309 4309 -1786 285 1297 O ATOM 1891 NE2 GLN A 78 32.938 33.983 -10.115 1.00 24.27 N ANISOU 1891 NE2 GLN B 78 3370 1871 3980 -2131 342 536 N ATOM 1892 N LYS A 79 32.455 27.931 -10.906 1.00 18.16 N ANISOU 1892 N LYS B 79 1947 1863 3089 -1542 432 356 N ATOM 1893 CA LYS A 79 32.126 26.527 -11.121 1.00 18.48 C ANISOU 1893 CA LYS B 79 1920 2088 3013 -1546 330 372 C ATOM 1894 C LYS A 79 32.183 25.884 -9.761 1.00 17.99 C ANISOU 1894 C LYS B 79 1868 2122 2844 -1502 273 400 C ATOM 1895 O LYS A 79 33.128 26.146 -9.020 1.00 17.69 O ANISOU 1895 O LYS B 79 1584 2315 2820 -1598 152 421 O ATOM 1896 CB LYS A 79 33.110 25.841 -12.048 1.00 18.59 C ANISOU 1896 CB LYS B 79 1935 1892 3234 -1573 311 407 C ATOM 1897 CG LYS A 79 33.111 24.307 -11.923 1.00 22.04 C ANISOU 1897 CG LYS B 79 2186 2584 3602 -1567 330 419 C ATOM 1898 CD LYS A 79 34.012 23.660 -12.899 1.00 26.10 C ANISOU 1898 CD LYS B 79 2616 3071 4230 -1342 155 441 C ATOM 1899 CE LYS A 79 34.050 22.166 -12.723 1.00 28.23 C ANISOU 1899 CE LYS B 79 2914 3197 4615 -1218 101 429 C ATOM 1900 NZ LYS A 79 34.711 21.563 -13.929 1.00 28.96 N ANISOU 1900 NZ LYS B 79 1821 4218 4964 -1264 200 195 N ATOM 1901 N LEU A 80 31.159 25.087 -9.400 1.00 16.67 N ANISOU 1901 N LEU B 80 1484 2246 2600 -1511 188 335 N ATOM 1902 CA LEU A 80 31.222 24.342 -8.138 1.00 16.09 C ANISOU 1902 CA LEU B 80 1431 2174 2507 -1424 178 447 C ATOM 1903 C LEU A 80 30.498 23.032 -8.251 1.00 15.56 C ANISOU 1903 C LEU B 80 1479 2175 2256 -1432 198 399 C ATOM 1904 O LEU A 80 29.285 23.033 -8.475 1.00 15.11 O ANISOU 1904 O LEU B 80 1357 2211 2172 -1374 169 475 O ATOM 1905 CB LEU A 80 30.640 25.139 -6.978 1.00 16.47 C ANISOU 1905 CB LEU B 80 1406 2339 2513 -1480 195 390 C ATOM 1906 CG LEU A 80 30.624 24.459 -5.604 1.00 16.40 C ANISOU 1906 CG LEU B 80 1217 2457 2555 -1291 -48 511 C ATOM 1907 CD1 LEU A 80 32.059 24.231 -5.067 1.00 17.81 C ANISOU 1907 CD1 LEU B 80 1523 2526 2717 -1118 565 1189 C ATOM 1908 CD2 LEU A 80 29.694 25.206 -4.566 1.00 16.72 C ANISOU 1908 CD2 LEU B 80 1425 2326 2599 -1347 228 627 C ATOM 1909 N VAL A 81 31.236 21.933 -8.079 1.00 14.85 N ANISOU 1909 N VAL B 81 1570 2137 1934 -1437 251 443 N ATOM 1910 CA VAL A 81 30.653 20.614 -8.209 1.00 14.75 C ANISOU 1910 CA VAL B 81 1719 2126 1759 -1362 180 421 C ATOM 1911 C VAL A 81 30.233 20.196 -6.782 1.00 14.15 C ANISOU 1911 C VAL B 81 1554 2135 1687 -1429 266 365 C ATOM 1912 O VAL A 81 31.008 20.268 -5.851 1.00 14.62 O ANISOU 1912 O VAL B 81 1460 2265 1829 -1484 113 400 O ATOM 1913 CB VAL A 81 31.704 19.657 -8.823 1.00 14.76 C ANISOU 1913 CB VAL B 81 1840 2181 1586 -1257 367 493 C ATOM 1914 CG1 VAL A 81 31.189 18.187 -8.796 1.00 14.61 C ANISOU 1914 CG1 VAL B 81 1574 2206 1768 -1583 79 194 C ATOM 1915 CG2 VAL A 81 32.120 20.103 -10.252 1.00 14.40 C ANISOU 1915 CG2 VAL B 81 1615 2279 1576 -1559 160 377 C ATOM 1916 N THR A 82 28.994 19.763 -6.580 1.00 14.02 N ANISOU 1916 N THR B 82 1490 2072 1763 -1432 199 255 N ATOM 1917 CA THR A 82 28.544 19.549 -5.206 1.00 14.39 C ANISOU 1917 CA THR B 82 1656 2001 1808 -1522 184 185 C ATOM 1918 C THR A 82 27.838 18.201 -5.169 1.00 14.32 C ANISOU 1918 C THR B 82 1642 2028 1770 -1495 255 218 C ATOM 1919 O THR A 82 27.485 17.699 -6.212 1.00 15.57 O ANISOU 1919 O THR B 82 1676 2092 2145 -1536 308 240 O ATOM 1920 CB THR A 82 27.464 20.597 -4.764 1.00 15.98 C ANISOU 1920 CB THR B 82 1919 2148 2003 -1480 138 229 C ATOM 1921 OG1 THR A 82 26.285 20.425 -5.554 1.00 15.45 O ANISOU 1921 OG1 THR B 82 1847 2209 1813 -1763 27 68 O ATOM 1922 CG2 THR A 82 27.946 22.030 -4.923 1.00 15.75 C ANISOU 1922 CG2 THR B 82 1854 2082 2047 -1653 236 216 C ATOM 1923 N PRO A 83 27.629 17.645 -3.969 1.00 14.34 N ANISOU 1923 N PRO B 83 1641 1935 1871 -1458 232 242 N ATOM 1924 CA PRO A 83 26.654 16.554 -3.902 1.00 14.33 C ANISOU 1924 CA PRO B 83 1616 1868 1960 -1429 205 225 C ATOM 1925 C PRO A 83 25.275 16.962 -4.414 1.00 14.66 C ANISOU 1925 C PRO B 83 1630 1829 2109 -1302 136 275 C ATOM 1926 O PRO A 83 24.916 18.160 -4.366 1.00 15.68 O ANISOU 1926 O PRO B 83 1630 1958 2369 -1505 176 162 O ATOM 1927 CB PRO A 83 26.574 16.236 -2.404 1.00 13.57 C ANISOU 1927 CB PRO B 83 1686 1842 1626 -1458 190 184 C ATOM 1928 CG PRO A 83 27.107 17.455 -1.679 1.00 14.50 C ANISOU 1928 CG PRO B 83 1674 2018 1814 -1510 308 162 C ATOM 1929 CD PRO A 83 28.194 17.965 -2.647 1.00 13.98 C ANISOU 1929 CD PRO B 83 1639 1917 1756 -1439 256 230 C ATOM 1930 N SER A 84 24.512 15.972 -4.896 1.00 13.73 N ANISOU 1930 N SER B 84 1606 1630 1981 -1294 205 289 N ATOM 1931 CA SER A 84 23.122 16.166 -5.342 1.00 13.13 C ANISOU 1931 CA SER B 84 1426 1671 1889 -1182 248 346 C ATOM 1932 C SER A 84 22.144 15.689 -4.248 1.00 14.03 C ANISOU 1932 C SER B 84 1502 1701 2124 -1253 242 346 C ATOM 1933 O SER A 84 21.002 16.189 -4.156 1.00 14.78 O ANISOU 1933 O SER B 84 1571 1927 2116 -1282 427 440 O ATOM 1934 CB SER A 84 22.853 15.329 -6.589 1.00 13.49 C ANISOU 1934 CB SER B 84 1316 1605 2202 -1079 270 420 C ATOM 1935 OG SER A 84 23.033 13.964 -6.255 1.00 14.83 O ANISOU 1935 OG SER B 84 1256 1935 2443 -1298 -32 90 O ATOM 1936 N PHE A 85 22.625 14.730 -3.440 1.00 14.37 N ANISOU 1936 N PHE B 85 1659 1730 2072 -1296 297 427 N ATOM 1937 CA PHE A 85 21.824 13.970 -2.441 1.00 14.94 C ANISOU 1937 CA PHE B 85 1631 1754 2290 -1354 201 387 C ATOM 1938 C PHE A 85 20.622 13.273 -3.070 1.00 15.93 C ANISOU 1938 C PHE B 85 1780 1862 2409 -1194 260 403 C ATOM 1939 O PHE A 85 19.604 13.140 -2.425 1.00 16.06 O ANISOU 1939 O PHE B 85 1696 1918 2487 -1390 309 540 O ATOM 1940 CB PHE A 85 21.411 14.854 -1.243 1.00 15.51 C ANISOU 1940 CB PHE B 85 1642 1845 2404 -1400 170 448 C ATOM 1941 CG PHE A 85 22.580 15.583 -0.581 1.00 16.74 C ANISOU 1941 CG PHE B 85 1878 1781 2700 -1494 47 503 C ATOM 1942 CD1 PHE A 85 23.352 14.939 0.387 1.00 16.93 C ANISOU 1942 CD1 PHE B 85 2019 2061 2349 -1629 217 557 C ATOM 1943 CD2 PHE A 85 22.898 16.891 -0.925 1.00 18.13 C ANISOU 1943 CD2 PHE B 85 1875 2058 2954 -1517 106 739 C ATOM 1944 CE1 PHE A 85 24.390 15.556 1.023 1.00 17.95 C ANISOU 1944 CE1 PHE B 85 1970 2458 2391 -1480 -24 579 C ATOM 1945 CE2 PHE A 85 23.990 17.544 -0.277 1.00 17.58 C ANISOU 1945 CE2 PHE B 85 1873 1960 2845 -1590 -24 637 C ATOM 1946 CZ PHE A 85 24.722 16.872 0.688 1.00 17.69 C ANISOU 1946 CZ PHE B 85 1890 2061 2770 -1674 -36 527 C ATOM 1947 N VAL A 86 20.765 12.850 -4.332 1.00 15.47 N ANISOU 1947 N VAL B 86 1795 1832 2251 -1269 178 336 N ATOM 1948 CA VAL A 86 19.715 12.169 -5.072 1.00 16.05 C ANISOU 1948 CA VAL B 86 1839 1839 2421 -1306 285 283 C ATOM 1949 C VAL A 86 20.320 10.939 -5.730 1.00 16.46 C ANISOU 1949 C VAL B 86 2016 1808 2431 -1340 380 221 C ATOM 1950 O VAL A 86 21.332 11.034 -6.419 1.00 17.10 O ANISOU 1950 O VAL B 86 2215 1736 2543 -1353 365 45 O ATOM 1951 CB VAL A 86 19.072 13.088 -6.138 1.00 15.05 C ANISOU 1951 CB VAL B 86 1561 1713 2441 -1347 169 219 C ATOM 1952 CG1 VAL A 86 17.953 12.303 -6.957 1.00 15.64 C ANISOU 1952 CG1 VAL B 86 1592 1874 2474 -1410 282 245 C ATOM 1953 CG2 VAL A 86 18.502 14.338 -5.449 1.00 15.90 C ANISOU 1953 CG2 VAL B 86 1566 1848 2624 -1420 149 212 C ATOM 1954 N LYS A 87 19.723 9.776 -5.507 1.00 16.68 N ANISOU 1954 N LYS B 87 2030 1956 2350 -1437 436 337 N ATOM 1955 CA LYS A 87 20.151 8.565 -6.237 1.00 17.42 C ANISOU 1955 CA LYS B 87 2181 2069 2367 -1369 459 436 C ATOM 1956 C LYS A 87 20.141 8.716 -7.783 1.00 18.00 C ANISOU 1956 C LYS B 87 2226 2157 2454 -1348 482 384 C ATOM 1957 O LYS A 87 19.156 9.190 -8.417 1.00 17.95 O ANISOU 1957 O LYS B 87 2266 2331 2222 -1321 603 519 O ATOM 1958 CB LYS A 87 19.349 7.335 -5.818 1.00 17.72 C ANISOU 1958 CB LYS B 87 1967 2224 2540 -1364 415 414 C ATOM 1959 CG LYS A 87 19.352 7.061 -4.324 1.00 18.27 C ANISOU 1959 CG LYS B 87 2250 2232 2459 -1304 382 636 C ATOM 1960 CD LYS A 87 20.775 6.921 -3.764 1.00 19.13 C ANISOU 1960 CD LYS B 87 1984 2661 2620 -1839 144 880 C ATOM 1961 CE LYS A 87 20.856 6.349 -2.341 1.00 20.34 C ANISOU 1961 CE LYS B 87 1742 2876 3110 -1629 -4 473 C ATOM 1962 NZ LYS A 87 22.316 6.457 -1.909 1.00 21.28 N ANISOU 1962 NZ LYS B 87 1316 3338 3430 -1712 262 586 N ATOM 1963 N GLY A 88 21.229 8.280 -8.390 1.00 16.74 N ANISOU 1963 N GLY B 88 1955 1985 2419 -1505 568 387 N ATOM 1964 CA GLY A 88 21.339 8.369 -9.839 1.00 17.49 C ANISOU 1964 CA GLY B 88 2156 1964 2522 -1406 434 411 C ATOM 1965 C GLY A 88 21.993 9.672 -10.304 1.00 17.54 C ANISOU 1965 C GLY B 88 2143 2004 2515 -1389 412 405 C ATOM 1966 O GLY A 88 22.484 9.743 -11.410 1.00 18.87 O ANISOU 1966 O GLY B 88 2208 2295 2663 -1375 328 348 O ATOM 1967 N ILE A 89 21.934 10.726 -9.481 1.00 17.43 N ANISOU 1967 N ILE B 89 2114 1873 2636 -1281 217 415 N ATOM 1968 CA ILE A 89 22.546 11.999 -9.845 1.00 17.16 C ANISOU 1968 CA ILE B 89 2075 1833 2609 -1182 265 507 C ATOM 1969 C ILE A 89 23.906 12.062 -9.135 1.00 16.96 C ANISOU 1969 C ILE B 89 2063 1878 2500 -1048 263 368 C ATOM 1970 O ILE A 89 23.989 12.225 -7.900 1.00 17.08 O ANISOU 1970 O ILE B 89 2181 1863 2443 -947 196 426 O ATOM 1971 CB ILE A 89 21.650 13.224 -9.499 1.00 17.44 C ANISOU 1971 CB ILE B 89 2083 1860 2684 -1169 250 582 C ATOM 1972 CG1 ILE A 89 20.207 13.002 -9.991 1.00 18.88 C ANISOU 1972 CG1 ILE B 89 2353 1977 2840 -1167 98 491 C ATOM 1973 CG2 ILE A 89 22.196 14.515 -10.140 1.00 17.13 C ANISOU 1973 CG2 ILE B 89 1972 1659 2877 -1416 234 593 C ATOM 1974 CD1 ILE A 89 19.309 14.231 -9.937 1.00 17.47 C ANISOU 1974 CD1 ILE B 89 2030 1860 2748 -1273 289 687 C ATOM 1975 N GLN A 90 24.965 11.938 -9.935 1.00 16.42 N ANISOU 1975 N GLN B 90 2082 1689 2467 -1012 300 225 N ATOM 1976 CA GLN A 90 26.325 11.786 -9.434 1.00 15.39 C ANISOU 1976 CA GLN B 90 1872 1653 2321 -1141 248 67 C ATOM 1977 C GLN A 90 26.758 13.010 -8.662 1.00 15.82 C ANISOU 1977 C GLN B 90 1893 1749 2367 -1136 266 113 C ATOM 1978 O GLN A 90 27.496 12.898 -7.692 1.00 16.97 O ANISOU 1978 O GLN B 90 2103 1916 2429 -1263 91 165 O ATOM 1979 CB GLN A 90 27.305 11.589 -10.602 1.00 14.94 C ANISOU 1979 CB GLN B 90 2046 1432 2197 -1072 189 -42 C ATOM 1980 CG GLN A 90 27.202 10.175 -11.226 1.00 17.84 C ANISOU 1980 CG GLN B 90 2366 1780 2630 -1041 390 78 C ATOM 1981 CD GLN A 90 28.062 10.058 -12.452 1.00 19.08 C ANISOU 1981 CD GLN B 90 2632 2298 2318 -781 558 217 C ATOM 1982 OE1 GLN A 90 27.667 10.472 -13.547 1.00 20.54 O ANISOU 1982 OE1 GLN B 90 2735 2877 2190 -819 586 454 O ATOM 1983 NE2 GLN A 90 29.254 9.530 -12.277 1.00 19.09 N ANISOU 1983 NE2 GLN B 90 2491 2160 2602 -893 534 453 N ATOM 1984 N CYS A 91 26.312 14.170 -9.120 1.00 15.65 N ANISOU 1984 N CYS B 91 1726 1846 2374 -1221 306 191 N ATOM 1985 CA CYS A 91 26.691 15.451 -8.539 1.00 15.18 C ANISOU 1985 CA CYS B 91 1512 1835 2419 -1299 455 223 C ATOM 1986 C CYS A 91 25.911 16.544 -9.249 1.00 15.22 C ANISOU 1986 C CYS B 91 1442 1999 2339 -1291 518 236 C ATOM 1987 O CYS A 91 25.302 16.291 -10.314 1.00 15.33 O ANISOU 1987 O CYS B 91 1442 2016 2366 -1350 480 116 O ATOM 1988 CB CYS A 91 28.211 15.678 -8.739 1.00 16.03 C ANISOU 1988 CB CYS B 91 1707 1903 2479 -1265 370 174 C ATOM 1989 SG CYS A 91 28.853 15.553 -10.430 1.00 18.46 S ANISOU 1989 SG CYS B 91 1856 2150 3006 -1645 272 400 S ATOM 1990 N VAL A 92 25.963 17.761 -8.688 1.00 15.05 N ANISOU 1990 N VAL B 92 1390 2016 2311 -1266 508 236 N ATOM 1991 CA VAL A 92 25.518 18.972 -9.384 1.00 15.94 C ANISOU 1991 CA VAL B 92 1573 2075 2406 -1369 510 355 C ATOM 1992 C VAL A 92 26.756 19.799 -9.767 1.00 16.61 C ANISOU 1992 C VAL B 92 1705 2080 2526 -1419 374 386 C ATOM 1993 O VAL A 92 27.593 20.058 -8.919 1.00 16.73 O ANISOU 1993 O VAL B 92 1705 2202 2448 -1531 373 442 O ATOM 1994 CB VAL A 92 24.576 19.832 -8.534 1.00 16.31 C ANISOU 1994 CB VAL B 92 1678 1971 2546 -1418 411 405 C ATOM 1995 CG1 VAL A 92 24.026 20.998 -9.344 1.00 16.51 C ANISOU 1995 CG1 VAL B 92 1789 1970 2510 -1428 611 317 C ATOM 1996 CG2 VAL A 92 23.372 18.913 -7.948 1.00 16.84 C ANISOU 1996 CG2 VAL B 92 1563 2395 2440 -1507 547 264 C ATOM 1997 N ASN A 93 26.856 20.173 -11.041 1.00 15.59 N ANISOU 1997 N ASN B 93 1625 1938 2358 -1401 370 335 N ATOM 1998 CA ASN A 93 27.865 21.117 -11.436 1.00 16.09 C ANISOU 1998 CA ASN B 93 1600 1956 2557 -1336 338 336 C ATOM 1999 C ASN A 93 27.223 22.477 -11.662 1.00 16.31 C ANISOU 1999 C ASN B 93 1620 1985 2591 -1291 262 287 C ATOM 2000 O ASN A 93 26.525 22.676 -12.668 1.00 17.36 O ANISOU 2000 O ASN B 93 1753 2110 2731 -1288 188 240 O ATOM 2001 CB ASN A 93 28.633 20.657 -12.690 1.00 16.24 C ANISOU 2001 CB ASN B 93 1623 1954 2591 -1472 216 289 C ATOM 2002 CG ASN A 93 29.846 21.508 -12.938 1.00 17.07 C ANISOU 2002 CG ASN B 93 1608 2104 2773 -1485 336 369 C ATOM 2003 OD1 ASN A 93 30.116 22.413 -12.152 1.00 18.72 O ANISOU 2003 OD1 ASN B 93 1560 2373 3177 -1620 372 98 O ATOM 2004 ND2 ASN A 93 30.587 21.217 -13.988 1.00 17.44 N ANISOU 2004 ND2 ASN B 93 1451 2367 2808 -1580 108 130 N ATOM 2005 N ASN A 94 27.449 23.392 -10.720 1.00 15.13 N ANISOU 2005 N ASN B 94 1354 1962 2430 -1301 296 249 N ATOM 2006 CA ASN A 94 26.929 24.736 -10.795 1.00 15.28 C ANISOU 2006 CA ASN B 94 1409 1883 2513 -1291 368 220 C ATOM 2007 C ASN A 94 27.910 25.580 -11.613 1.00 16.02 C ANISOU 2007 C ASN B 94 1602 1934 2551 -1220 430 212 C ATOM 2008 O ASN A 94 29.059 25.714 -11.200 1.00 16.68 O ANISOU 2008 O ASN B 94 1604 1886 2845 -1420 281 296 O ATOM 2009 CB ASN A 94 26.816 25.279 -9.377 1.00 15.34 C ANISOU 2009 CB ASN B 94 1425 1909 2494 -1323 340 203 C ATOM 2010 CG ASN A 94 25.913 24.419 -8.463 1.00 16.18 C ANISOU 2010 CG ASN B 94 1541 2108 2499 -1261 317 370 C ATOM 2011 OD1 ASN A 94 24.682 24.567 -8.463 1.00 17.17 O ANISOU 2011 OD1 ASN B 94 1367 2389 2767 -1536 190 -55 O ATOM 2012 ND2 ASN A 94 26.527 23.535 -7.684 1.00 15.57 N ANISOU 2012 ND2 ASN B 94 1441 1748 2726 -1234 361 334 N ATOM 2013 N VAL A 95 27.456 26.132 -12.742 1.00 15.76 N ANISOU 2013 N VAL B 95 1641 1834 2512 -1307 581 247 N ATOM 2014 CA VAL A 95 28.317 26.782 -13.742 1.00 16.96 C ANISOU 2014 CA VAL B 95 1922 1956 2565 -1194 642 169 C ATOM 2015 C VAL A 95 27.716 28.173 -13.881 1.00 18.48 C ANISOU 2015 C VAL B 95 2203 2113 2702 -1160 584 237 C ATOM 2016 O VAL A 95 26.493 28.319 -14.024 1.00 18.86 O ANISOU 2016 O VAL B 95 1988 2239 2936 -1153 595 229 O ATOM 2017 CB VAL A 95 28.351 25.990 -15.109 1.00 15.87 C ANISOU 2017 CB VAL B 95 1817 1764 2447 -1321 726 241 C ATOM 2018 CG1 VAL A 95 29.080 26.782 -16.235 1.00 14.76 C ANISOU 2018 CG1 VAL B 95 1901 1563 2143 -1397 588 -40 C ATOM 2019 CG2 VAL A 95 29.034 24.605 -14.946 1.00 16.48 C ANISOU 2019 CG2 VAL B 95 1734 1947 2579 -1324 796 270 C ATOM 2020 N VAL A 96 28.549 29.190 -13.719 1.00 20.68 N ANISOU 2020 N VAL B 96 2635 2358 2865 -1028 575 149 N ATOM 2021 CA VAL A 96 28.141 30.589 -13.906 1.00 21.14 C ANISOU 2021 CA VAL B 96 2921 2389 2721 -851 648 75 C ATOM 2022 C VAL A 96 28.391 31.083 -15.347 1.00 22.64 C ANISOU 2022 C VAL B 96 3252 2570 2780 -825 624 45 C ATOM 2023 O VAL A 96 29.539 31.280 -15.769 1.00 22.15 O ANISOU 2023 O VAL B 96 3340 2623 2451 -925 770 97 O ATOM 2024 CB VAL A 96 28.853 31.529 -12.886 1.00 20.44 C ANISOU 2024 CB VAL B 96 2862 2269 2633 -859 666 52 C ATOM 2025 CG1 VAL A 96 28.291 32.930 -12.970 1.00 20.51 C ANISOU 2025 CG1 VAL B 96 2670 2278 2842 -1089 758 178 C ATOM 2026 CG2 VAL A 96 28.654 30.998 -11.488 1.00 21.24 C ANISOU 2026 CG2 VAL B 96 2954 2420 2696 -639 734 -80 C ATOM 2027 N GLY A 97 27.310 31.291 -16.083 1.00 24.10 N ANISOU 2027 N GLY B 97 3634 2652 2869 -720 534 25 N ATOM 2028 CA GLY A 97 27.391 31.902 -17.401 1.00 26.76 C ANISOU 2028 CA GLY B 97 4053 2920 3194 -614 588 37 C ATOM 2029 C GLY A 97 27.340 33.427 -17.303 1.00 29.24 C ANISOU 2029 C GLY B 97 4438 3234 3437 -512 540 28 C ATOM 2030 O GLY A 97 27.210 33.986 -16.196 1.00 29.38 O ANISOU 2030 O GLY B 97 4506 3199 3456 -586 569 16 O ATOM 2031 N PRO A 98 27.435 34.124 -18.422 1.00 31.22 N ANISOU 2031 N PRO B 98 4689 3478 3695 -342 435 40 N ATOM 2032 CA PRO A 98 27.458 35.572 -18.360 1.00 32.51 C ANISOU 2032 CA PRO B 98 4864 3630 3857 -278 400 3 C ATOM 2033 C PRO A 98 26.029 36.121 -18.352 1.00 34.94 C ANISOU 2033 C PRO B 98 5091 4021 4164 -235 370 -19 C ATOM 2034 O PRO A 98 25.089 35.405 -18.557 1.00 34.83 O ANISOU 2034 O PRO B 98 5130 3929 4173 -235 379 -83 O ATOM 2035 CB PRO A 98 28.189 35.943 -19.635 1.00 32.53 C ANISOU 2035 CB PRO B 98 4852 3606 3901 -276 413 -44 C ATOM 2036 CG PRO A 98 27.816 34.886 -20.582 1.00 31.45 C ANISOU 2036 CG PRO B 98 4761 3456 3732 -225 348 55 C ATOM 2037 CD PRO A 98 27.572 33.642 -19.797 1.00 30.98 C ANISOU 2037 CD PRO B 98 4617 3487 3666 -363 420 8 C ATOM 2038 N ARG A 99 25.906 37.421 -18.107 1.00 37.47 N ANISOU 2038 N ARG B 99 5282 4414 4539 -139 316 6 N ATOM 2039 CA ARG A 99 24.603 38.075 -18.074 1.00 40.59 C ANISOU 2039 CA ARG B 99 5485 4935 5000 -79 214 6 C ATOM 2040 C ARG A 99 24.464 39.086 -19.206 1.00 42.19 C ANISOU 2040 C ARG B 99 5577 5202 5251 -21 145 23 C ATOM 2041 O ARG A 99 25.460 39.555 -19.758 1.00 43.29 O ANISOU 2041 O ARG B 99 5740 5317 5391 -20 130 37 O ATOM 2042 CB ARG A 99 24.382 38.762 -16.725 1.00 40.67 C ANISOU 2042 CB ARG B 99 5502 4946 5002 -71 229 2 C ATOM 2043 CG ARG A 99 24.225 37.802 -15.557 1.00 41.53 C ANISOU 2043 CG ARG B 99 5508 5057 5215 -177 340 113 C ATOM 2044 CD ARG A 99 24.296 38.535 -14.227 1.00 44.51 C ANISOU 2044 CD ARG B 99 5767 5446 5699 -385 349 215 C ATOM 2045 NE ARG A 99 23.990 37.656 -13.102 1.00 46.36 N ANISOU 2045 NE ARG B 99 5803 5647 6164 -531 528 144 N ATOM 2046 CZ ARG A 99 22.795 37.120 -12.875 1.00 45.65 C ANISOU 2046 CZ ARG B 99 5414 5625 6306 -632 706 226 C ATOM 2047 NH1 ARG A 99 21.786 37.373 -13.698 1.00 46.04 N ANISOU 2047 NH1 ARG B 99 5348 5653 6489 -682 661 409 N ATOM 2048 NH2 ARG A 99 22.608 36.332 -11.826 1.00 44.18 N ANISOU 2048 NH2 ARG B 99 5144 5400 6239 -707 684 120 N ATOM 2049 N HIS A 100 23.224 39.419 -19.548 1.00 44.59 N ATOM 2050 CA HIS A 100 22.739 40.789 -19.433 1.00 46.53 C ATOM 2051 C HIS A 100 23.599 41.749 -20.248 1.00 47.43 C ATOM 2052 O HIS A 100 23.189 42.215 -21.311 1.00 48.54 O ATOM 2053 CB HIS A 100 21.279 40.880 -19.882 1.00 46.89 C ATOM 2054 CG HIS A 100 20.754 42.280 -19.950 1.00 49.78 C ATOM 2055 ND1 HIS A 100 19.519 42.638 -19.453 1.00 51.91 N ATOM 2056 CD2 HIS A 100 21.297 43.412 -20.458 1.00 52.14 C ATOM 2057 CE1 HIS A 100 19.324 43.929 -19.651 1.00 52.76 C ATOM 2058 NE2 HIS A 100 20.388 44.423 -20.259 1.00 53.13 N ATOM 2059 N GLY A 101 24.793 42.040 -19.742 1.00 20.00 N ATOM 2060 CA GLY A 101 26.014 41.774 -20.473 1.00 20.00 C ATOM 2061 C GLY A 101 27.011 42.899 -20.436 1.00 20.00 C ATOM 2062 O GLY A 101 26.757 43.978 -20.879 1.00 20.00 O ATOM 2063 N ASP A 102 28.176 42.612 -19.919 1.00 20.00 N ATOM 2064 CA ASP A 102 28.908 41.443 -20.359 1.00 20.00 C ATOM 2065 C ASP A 102 29.367 41.594 -21.799 1.00 20.00 C ATOM 2066 O ASP A 102 28.587 41.540 -22.719 1.00 50.69 O ATOM 2067 CB ASP A 102 28.108 40.169 -20.113 1.00 20.00 C ATOM 2068 CG ASP A 102 27.970 39.866 -18.649 1.00 20.00 C ATOM 2069 OD1 ASP A 102 28.499 38.854 -18.159 1.00 20.00 O ATOM 2070 OD2 ASP A 102 27.335 40.675 -17.982 1.00 20.00 O ATOM 2071 N SER A 103 30.650 41.835 -21.932 1.00 50.69 N ATOM 2072 CA SER A 103 31.361 41.688 -23.176 1.00 50.63 C ATOM 2073 C SER A 103 31.596 40.235 -23.592 1.00 50.49 C ATOM 2074 O SER A 103 31.400 39.328 -22.821 1.00 50.40 O ATOM 2075 CB SER A 103 32.678 42.411 -23.043 1.00 50.70 C ATOM 2076 OG SER A 103 33.667 41.536 -22.623 1.00 50.70 O ATOM 2077 N ASN A 104 31.931 40.068 -24.854 1.00 50.02 N ATOM 2078 CA ASN A 104 31.885 38.796 -25.517 1.00 49.40 C ATOM 2079 C ASN A 104 31.353 37.632 -24.730 1.00 48.71 C ATOM 2080 O ASN A 104 32.041 36.704 -24.468 1.00 48.49 O ATOM 2081 CB ASN A 104 33.257 38.483 -26.114 1.00 49.89 C ATOM 2082 CG ASN A 104 34.348 38.420 -25.071 1.00 50.26 C ATOM 2083 OD1 ASN A 104 35.320 37.720 -25.233 1.00 50.91 O ATOM 2084 ND2 ASN A 104 34.179 39.157 -24.010 1.00 51.06 N ATOM 2085 N LEU A 105 30.063 37.609 -24.469 1.00 47.66 N ATOM 2086 CA LEU A 105 29.357 36.433 -24.790 1.00 46.44 C ATOM 2087 C LEU A 105 30.147 36.189 -26.022 1.00 45.75 C ATOM 2088 O LEU A 105 30.149 36.985 -26.928 1.00 46.84 O ATOM 2089 CB LEU A 105 27.900 36.754 -25.093 1.00 46.29 C ATOM 2090 CG LEU A 105 27.460 37.995 -24.360 1.00 45.58 C ATOM 2091 CD1 LEU A 105 26.286 38.545 -24.917 1.00 45.76 C ATOM 2092 CD2 LEU A 105 27.320 37.789 -22.897 1.00 45.79 C ATOM 2093 N ARG A 106 30.869 35.106 -26.026 1.00 44.17 N ATOM 2094 CA ARG A 106 30.233 33.906 -26.467 1.00 41.62 C ATOM 2095 C ARG A 106 31.250 33.592 -25.403 1.00 39.63 C ATOM 2096 O ARG A 106 30.923 33.425 -24.220 1.00 38.84 O ATOM 2097 CB ARG A 106 30.038 34.069 -27.987 1.00 42.22 C ATOM 2098 CG ARG A 106 30.718 33.051 -28.892 1.00 42.85 C ATOM 2099 CD ARG A 106 29.747 31.970 -29.300 1.00 43.66 C ATOM 2100 NE ARG A 106 30.399 30.760 -29.802 1.00 44.28 N ATOM 2101 CZ ARG A 106 30.157 30.217 -30.996 1.00 45.58 C ATOM 2102 NH1 ARG A 106 29.285 30.782 -31.824 1.00 45.27 N ATOM 2103 NH2 ARG A 106 30.780 29.102 -31.364 1.00 45.50 N ATOM 2104 N GLU A 107 32.536 33.771 -25.866 1.00 36.83 N ANISOU 2104 N GLU B 107 4741 4579 4673 -336 262 211 N ATOM 2105 CA GLU A 107 33.769 33.087 -25.558 1.00 34.29 C ANISOU 2105 CA GLU B 107 4462 4235 4332 -582 474 413 C ATOM 2106 C GLU A 107 33.506 32.794 -24.093 1.00 32.41 C ANISOU 2106 C GLU B 107 4267 3945 4103 -663 570 470 C ATOM 2107 O GLU A 107 33.878 31.741 -23.617 1.00 31.56 O ANISOU 2107 O GLU B 107 4221 3874 3896 -793 579 537 O ATOM 2108 CB GLU A 107 35.029 33.969 -25.747 1.00 34.99 C ANISOU 2108 CB GLU B 107 4595 4353 4346 -621 519 451 C ATOM 2109 CG GLU A 107 35.464 34.126 -27.224 1.00 36.08 C ANISOU 2109 CG GLU B 107 4559 4499 4649 -1051 774 762 C ATOM 2110 CD GLU A 107 35.433 32.787 -28.011 1.00 38.73 C ANISOU 2110 CD GLU B 107 4878 5081 4755 -1298 936 1251 C ATOM 2111 OE1 GLU A 107 35.811 31.712 -27.449 1.00 34.89 O ANISOU 2111 OE1 GLU B 107 4186 4356 4715 -2226 1629 2358 O ATOM 2112 OE2 GLU A 107 35.016 32.822 -29.191 1.00 38.85 O ANISOU 2112 OE2 GLU B 107 5126 5422 4211 -1296 757 1421 O ATOM 2113 N LYS A 108 32.857 33.732 -23.400 1.00 30.53 N ANISOU 2113 N LYS B 108 4070 3663 3867 -784 683 562 N ATOM 2114 CA LYS A 108 32.390 33.529 -22.031 1.00 29.29 C ANISOU 2114 CA LYS B 108 3901 3421 3807 -884 706 557 C ATOM 2115 C LYS A 108 31.489 32.286 -21.938 1.00 27.61 C ANISOU 2115 C LYS B 108 3707 3159 3623 -913 784 645 C ATOM 2116 O LYS A 108 31.652 31.466 -21.032 1.00 27.43 O ANISOU 2116 O LYS B 108 3582 3178 3662 -855 740 616 O ATOM 2117 CB LYS A 108 31.643 34.770 -21.516 1.00 29.21 C ANISOU 2117 CB LYS B 108 3920 3391 3786 -901 704 514 C ATOM 2118 CG LYS A 108 32.536 35.901 -21.016 1.00 30.29 C ANISOU 2118 CG LYS B 108 4061 3498 3948 -1075 690 502 C ATOM 2119 CD LYS A 108 31.689 37.057 -20.492 1.00 29.08 C ANISOU 2119 CD LYS B 108 3812 3376 3860 -1122 727 515 C ATOM 2120 CE LYS A 108 32.509 38.339 -20.203 1.00 32.00 C ANISOU 2120 CE LYS B 108 4263 3755 4139 -1271 367 492 C ATOM 2121 NZ LYS A 108 33.690 38.075 -19.313 1.00 33.95 N ANISOU 2121 NZ LYS B 108 4808 3948 4142 -1440 -12 340 N ATOM 2122 N LEU A 109 30.563 32.148 -22.885 1.00 25.65 N ANISOU 2122 N LEU B 109 3490 2866 3390 -913 836 771 N ATOM 2123 CA LEU A 109 29.662 30.986 -22.917 1.00 25.75 C ANISOU 2123 CA LEU B 109 3572 2852 3359 -840 878 730 C ATOM 2124 C LEU A 109 30.407 29.682 -23.232 1.00 24.46 C ANISOU 2124 C LEU B 109 3382 2675 3234 -868 930 780 C ATOM 2125 O LEU A 109 30.117 28.644 -22.653 1.00 23.80 O ANISOU 2125 O LEU B 109 3443 2574 3025 -847 1017 871 O ATOM 2126 CB LEU A 109 28.531 31.175 -23.936 1.00 25.96 C ANISOU 2126 CB LEU B 109 3571 2929 3362 -801 851 759 C ATOM 2127 CG LEU A 109 27.063 31.515 -23.629 1.00 26.20 C ANISOU 2127 CG LEU B 109 3744 2863 3348 -876 1090 737 C ATOM 2128 CD1 LEU A 109 26.541 31.077 -22.240 1.00 24.84 C ANISOU 2128 CD1 LEU B 109 4227 2725 2486 -850 1104 373 C ATOM 2129 CD2 LEU A 109 26.818 32.960 -23.841 1.00 24.95 C ANISOU 2129 CD2 LEU B 109 3845 2275 3360 -804 1049 649 C ATOM 2130 N VAL A 110 31.354 29.742 -24.163 1.00 23.28 N ANISOU 2130 N VAL B 110 3336 2471 3037 -939 1055 852 N ATOM 2131 CA VAL A 110 32.210 28.593 -24.472 1.00 22.98 C ANISOU 2131 CA VAL B 110 3192 2467 3071 -1044 1045 834 C ATOM 2132 C VAL A 110 33.001 28.146 -23.256 1.00 21.98 C ANISOU 2132 C VAL B 110 3008 2336 3007 -1123 1015 860 C ATOM 2133 O VAL A 110 33.099 26.950 -22.988 1.00 22.22 O ANISOU 2133 O VAL B 110 2945 2341 3154 -1188 1071 863 O ATOM 2134 CB VAL A 110 33.207 28.879 -25.641 1.00 22.12 C ANISOU 2134 CB VAL B 110 3069 2377 2957 -1095 1095 879 C ATOM 2135 CG1 VAL A 110 34.030 27.637 -25.944 1.00 23.05 C ANISOU 2135 CG1 VAL B 110 3172 2597 2986 -1003 1216 712 C ATOM 2136 CG2 VAL A 110 32.465 29.292 -26.864 1.00 24.13 C ANISOU 2136 CG2 VAL B 110 3462 2442 3263 -1233 894 764 C ATOM 2137 N ALA A 111 33.566 29.103 -22.524 1.00 21.15 N ANISOU 2137 N ALA B 111 2891 2172 2974 -1304 1009 883 N ATOM 2138 CA ALA A 111 34.385 28.792 -21.357 1.00 21.28 C ANISOU 2138 CA ALA B 111 2862 2210 3013 -1296 898 749 C ATOM 2139 C ALA A 111 33.457 28.164 -20.297 1.00 21.27 C ANISOU 2139 C ALA B 111 2733 2320 3026 -1222 888 732 C ATOM 2140 O ALA A 111 33.784 27.154 -19.657 1.00 22.21 O ANISOU 2140 O ALA B 111 2816 2454 3166 -1191 764 727 O ATOM 2141 CB ALA A 111 35.097 30.091 -20.821 1.00 20.33 C ANISOU 2141 CB ALA B 111 2589 2093 3043 -1514 1008 768 C ATOM 2142 N ALA A 112 32.261 28.728 -20.164 1.00 22.32 N ANISOU 2142 N ALA B 112 2909 2489 3079 -1083 873 617 N ATOM 2143 CA ALA A 112 31.226 28.181 -19.256 1.00 22.02 C ANISOU 2143 CA ALA B 112 2908 2543 2912 -1036 840 671 C ATOM 2144 C ALA A 112 30.866 26.732 -19.545 1.00 22.00 C ANISOU 2144 C ALA B 112 2908 2588 2862 -948 758 548 C ATOM 2145 O ALA A 112 30.902 25.892 -18.635 1.00 22.35 O ANISOU 2145 O ALA B 112 2869 2619 3001 -997 759 556 O ATOM 2146 CB ALA A 112 29.964 29.054 -19.270 1.00 21.30 C ANISOU 2146 CB ALA B 112 2742 2522 2828 -1016 946 683 C ATOM 2147 N TYR A 113 30.477 26.438 -20.783 1.00 21.86 N ANISOU 2147 N TYR B 113 2896 2667 2739 -894 757 437 N ATOM 2148 CA TYR A 113 30.159 25.062 -21.169 1.00 21.27 C ANISOU 2148 CA TYR B 113 2691 2725 2666 -960 716 321 C ATOM 2149 C TYR A 113 31.346 24.117 -21.025 1.00 21.28 C ANISOU 2149 C TYR B 113 2736 2694 2654 -997 640 333 C ATOM 2150 O TYR A 113 31.184 23.004 -20.538 1.00 21.49 O ANISOU 2150 O TYR B 113 2631 2592 2941 -1178 603 212 O ATOM 2151 CB TYR A 113 29.558 24.997 -22.579 1.00 21.77 C ANISOU 2151 CB TYR B 113 2674 2846 2748 -873 775 196 C ATOM 2152 CG TYR A 113 28.112 25.434 -22.646 1.00 23.30 C ANISOU 2152 CG TYR B 113 2958 3086 2806 -883 627 117 C ATOM 2153 CD1 TYR A 113 27.750 26.597 -23.320 1.00 24.48 C ANISOU 2153 CD1 TYR B 113 2996 3238 3064 -730 539 15 C ATOM 2154 CD2 TYR A 113 27.104 24.696 -22.009 1.00 25.05 C ANISOU 2154 CD2 TYR B 113 3151 3273 3094 -808 675 -204 C ATOM 2155 CE1 TYR A 113 26.418 27.001 -23.388 1.00 25.02 C ANISOU 2155 CE1 TYR B 113 3028 3447 3029 -638 687 -93 C ATOM 2156 CE2 TYR A 113 25.763 25.096 -22.064 1.00 23.59 C ANISOU 2156 CE2 TYR B 113 2665 3395 2900 -764 561 -136 C ATOM 2157 CZ TYR A 113 25.436 26.257 -22.748 1.00 23.22 C ANISOU 2157 CZ TYR B 113 2777 3142 2904 -819 716 6 C ATOM 2158 OH TYR A 113 24.128 26.664 -22.835 1.00 24.49 O ANISOU 2158 OH TYR B 113 2988 3420 2897 -760 897 156 O ATOM 2159 N LYS A 114 32.554 24.540 -21.407 1.00 21.29 N ANISOU 2159 N LYS B 114 2800 2657 2631 -963 541 309 N ATOM 2160 CA LYS A 114 33.711 23.657 -21.189 1.00 21.52 C ANISOU 2160 CA LYS B 114 2780 2768 2625 -951 509 319 C ATOM 2161 C LYS A 114 33.857 23.218 -19.721 1.00 21.17 C ANISOU 2161 C LYS B 114 2795 2687 2561 -882 456 295 C ATOM 2162 O LYS A 114 34.196 22.054 -19.437 1.00 21.77 O ANISOU 2162 O LYS B 114 2872 2757 2640 -928 485 327 O ATOM 2163 CB LYS A 114 34.994 24.251 -21.728 1.00 21.81 C ANISOU 2163 CB LYS B 114 2868 2714 2703 -973 488 249 C ATOM 2164 CG LYS A 114 35.066 24.180 -23.212 1.00 23.15 C ANISOU 2164 CG LYS B 114 2857 3153 2782 -1287 530 490 C ATOM 2165 CD LYS A 114 36.312 24.813 -23.788 1.00 22.95 C ANISOU 2165 CD LYS B 114 1975 3470 3276 -1940 509 591 C ATOM 2166 CE LYS A 114 36.341 24.613 -25.292 1.00 25.10 C ANISOU 2166 CE LYS B 114 2078 3703 3756 -2093 787 917 C ATOM 2167 NZ LYS A 114 37.486 25.347 -25.937 1.00 30.05 N ANISOU 2167 NZ LYS B 114 2890 4277 4247 -1841 632 863 N ATOM 2168 N SER A 115 33.553 24.134 -18.806 1.00 20.15 N ANISOU 2168 N SER B 115 2627 2578 2447 -906 414 254 N ATOM 2169 CA SER A 115 33.643 23.889 -17.348 1.00 19.26 C ANISOU 2169 CA SER B 115 2376 2487 2455 -1037 424 227 C ATOM 2170 C SER A 115 32.610 22.893 -16.796 1.00 18.22 C ANISOU 2170 C SER B 115 1977 2482 2461 -1098 388 263 C ATOM 2171 O SER A 115 32.697 22.460 -15.644 1.00 18.05 O ANISOU 2171 O SER B 115 1801 2466 2589 -1270 425 272 O ATOM 2172 CB SER A 115 33.611 25.230 -16.582 1.00 18.91 C ANISOU 2172 CB SER B 115 2388 2400 2395 -1038 438 180 C ATOM 2173 OG SER A 115 32.294 25.723 -16.410 1.00 17.52 O ANISOU 2173 OG SER B 115 2084 2208 2362 -1107 193 -27 O ATOM 2174 N VAL A 116 31.660 22.499 -17.633 1.00 18.88 N ANISOU 2174 N VAL B 116 2014 2521 2636 -1150 356 362 N ATOM 2175 CA VAL A 116 30.636 21.503 -17.289 1.00 19.15 C ANISOU 2175 CA VAL B 116 1819 2664 2792 -1123 285 380 C ATOM 2176 C VAL A 116 31.303 20.135 -17.094 1.00 19.83 C ANISOU 2176 C VAL B 116 1991 2751 2792 -1054 189 420 C ATOM 2177 O VAL A 116 30.857 19.316 -16.282 1.00 21.65 O ANISOU 2177 O VAL B 116 2094 3006 3123 -917 49 407 O ATOM 2178 CB VAL A 116 29.579 21.467 -18.447 1.00 19.02 C ANISOU 2178 CB VAL B 116 1724 2626 2875 -1201 277 417 C ATOM 2179 CG1 VAL A 116 28.743 20.156 -18.471 1.00 18.21 C ANISOU 2179 CG1 VAL B 116 1387 2440 3090 -1307 694 479 C ATOM 2180 CG2 VAL A 116 28.713 22.732 -18.386 1.00 18.74 C ANISOU 2180 CG2 VAL B 116 1716 2692 2711 -1252 431 360 C ATOM 2181 N LEU A 117 32.413 19.916 -17.802 1.00 20.51 N ANISOU 2181 N LEU B 117 2199 2826 2765 -854 195 379 N ATOM 2182 CA LEU A 117 33.103 18.626 -17.774 1.00 20.86 C ANISOU 2182 CA LEU B 117 2363 2770 2792 -906 186 317 C ATOM 2183 C LEU A 117 33.747 18.369 -16.420 1.00 20.76 C ANISOU 2183 C LEU B 117 2444 2670 2771 -906 129 346 C ATOM 2184 O LEU A 117 34.414 19.234 -15.863 1.00 21.87 O ANISOU 2184 O LEU B 117 2755 2844 2707 -946 67 333 O ATOM 2185 CB LEU A 117 34.136 18.538 -18.906 1.00 21.74 C ANISOU 2185 CB LEU B 117 2493 2852 2912 -845 138 280 C ATOM 2186 CG LEU A 117 33.422 18.137 -20.210 1.00 23.11 C ANISOU 2186 CG LEU B 117 2714 3049 3014 -878 282 299 C ATOM 2187 CD1 LEU A 117 33.121 19.352 -21.043 1.00 26.82 C ANISOU 2187 CD1 LEU B 117 2887 3670 3633 -818 102 459 C ATOM 2188 CD2 LEU A 117 34.243 17.134 -20.985 1.00 25.30 C ANISOU 2188 CD2 LEU B 117 2642 3447 3522 -1317 556 240 C ATOM 2189 N VAL A 118 33.537 17.182 -15.886 1.00 21.56 N ANISOU 2189 N VAL B 118 2498 2758 2932 -864 137 255 N ATOM 2190 CA VAL A 118 34.102 16.809 -14.593 1.00 20.49 C ANISOU 2190 CA VAL B 118 2414 2551 2819 -864 144 255 C ATOM 2191 C VAL A 118 34.736 15.427 -14.774 1.00 20.79 C ANISOU 2191 C VAL B 118 2516 2523 2858 -845 46 316 C ATOM 2192 O VAL A 118 34.179 14.582 -15.480 1.00 18.95 O ANISOU 2192 O VAL B 118 2303 2212 2685 -891 -10 151 O ATOM 2193 CB VAL A 118 33.034 16.879 -13.425 1.00 21.67 C ANISOU 2193 CB VAL B 118 2636 2593 3004 -821 158 209 C ATOM 2194 CG1 VAL A 118 32.097 18.103 -13.566 1.00 22.37 C ANISOU 2194 CG1 VAL B 118 2541 2953 3004 -811 282 198 C ATOM 2195 CG2 VAL A 118 32.195 15.682 -13.400 1.00 22.04 C ANISOU 2195 CG2 VAL B 118 2471 2831 3072 -1023 610 256 C ATOM 2196 N GLY A 119 35.925 15.212 -14.199 1.00 20.85 N ANISOU 2196 N GLY B 119 2538 2401 2980 -772 -72 345 N ATOM 2197 CA GLY A 119 36.567 13.887 -14.269 1.00 20.58 C ANISOU 2197 CA GLY B 119 2640 2260 2919 -880 -89 436 C ATOM 2198 C GLY A 119 35.680 12.786 -13.682 1.00 20.18 C ANISOU 2198 C GLY B 119 2581 2112 2973 -957 -132 453 C ATOM 2199 O GLY A 119 35.171 12.892 -12.561 1.00 18.94 O ANISOU 2199 O GLY B 119 2387 1962 2847 -945 -164 495 O ATOM 2200 N GLY A 120 35.448 11.743 -14.470 1.00 20.47 N ANISOU 2200 N GLY B 120 2652 2030 3093 -1002 -76 537 N ATOM 2201 CA GLY A 120 34.703 10.571 -13.991 1.00 20.26 C ANISOU 2201 CA GLY B 120 2564 2050 3082 -1176 31 716 C ATOM 2202 C GLY A 120 33.194 10.627 -14.198 1.00 20.17 C ANISOU 2202 C GLY B 120 2558 2127 2977 -1176 62 693 C ATOM 2203 O GLY A 120 32.434 9.817 -13.636 1.00 21.63 O ANISOU 2203 O GLY B 120 2864 2228 3126 -1350 1 721 O ATOM 2204 N VAL A 121 32.746 11.610 -14.965 1.00 18.98 N ANISOU 2204 N VAL B 121 2412 2165 2632 -1180 157 663 N ATOM 2205 CA VAL A 121 31.355 11.731 -15.354 1.00 17.61 C ANISOU 2205 CA VAL B 121 2088 2222 2381 -1093 200 481 C ATOM 2206 C VAL A 121 31.312 11.768 -16.860 1.00 17.04 C ANISOU 2206 C VAL B 121 1980 2106 2389 -1197 271 507 C ATOM 2207 O VAL A 121 32.045 12.520 -17.474 1.00 16.73 O ANISOU 2207 O VAL B 121 1506 2387 2462 -1147 268 404 O ATOM 2208 CB VAL A 121 30.694 13.012 -14.790 1.00 17.91 C ANISOU 2208 CB VAL B 121 2243 2272 2287 -968 166 596 C ATOM 2209 CG1 VAL A 121 29.225 13.055 -15.210 1.00 16.34 C ANISOU 2209 CG1 VAL B 121 1713 2475 2020 -1130 137 394 C ATOM 2210 CG2 VAL A 121 30.802 13.033 -13.266 1.00 18.14 C ANISOU 2210 CG2 VAL B 121 2353 2244 2293 -1022 363 384 C ATOM 2211 N VAL A 122 30.436 10.956 -17.458 1.00 16.08 N ANISOU 2211 N VAL B 122 1740 1918 2452 -1330 393 465 N ATOM 2212 CA VAL A 122 30.318 10.942 -18.915 1.00 16.33 C ANISOU 2212 CA VAL B 122 1752 1806 2646 -1312 492 422 C ATOM 2213 C VAL A 122 28.940 11.412 -19.368 1.00 16.12 C ANISOU 2213 C VAL B 122 1812 1785 2525 -1298 456 432 C ATOM 2214 O VAL A 122 28.814 11.952 -20.451 1.00 17.50 O ANISOU 2214 O VAL B 122 1817 2067 2763 -1364 596 672 O ATOM 2215 CB VAL A 122 30.741 9.592 -19.553 1.00 16.38 C ANISOU 2215 CB VAL B 122 1644 1852 2725 -1330 513 373 C ATOM 2216 CG1 VAL A 122 32.283 9.385 -19.464 1.00 19.86 C ANISOU 2216 CG1 VAL B 122 2124 2250 3171 -1141 442 204 C ATOM 2217 CG2 VAL A 122 30.029 8.445 -18.911 1.00 19.60 C ANISOU 2217 CG2 VAL B 122 2541 1584 3319 -1373 694 560 C ATOM 2218 N ASN A 123 27.910 11.181 -18.541 1.00 15.00 N ANISOU 2218 N ASN B 123 1678 1599 2419 -1201 558 333 N ATOM 2219 CA ASN A 123 26.556 11.669 -18.813 1.00 15.68 C ANISOU 2219 CA ASN B 123 1838 1661 2456 -1257 465 367 C ATOM 2220 C ASN A 123 26.166 12.994 -18.112 1.00 15.83 C ANISOU 2220 C ASN B 123 1938 1747 2327 -1110 480 354 C ATOM 2221 O ASN A 123 26.260 13.123 -16.881 1.00 17.20 O ANISOU 2221 O ASN B 123 2181 1955 2400 -1107 395 364 O ATOM 2222 CB ASN A 123 25.554 10.581 -18.422 1.00 14.76 C ANISOU 2222 CB ASN B 123 1627 1551 2430 -1173 488 352 C ATOM 2223 CG ASN A 123 25.873 9.254 -19.080 1.00 16.81 C ANISOU 2223 CG ASN B 123 1826 1894 2664 -1460 467 370 C ATOM 2224 OD1 ASN A 123 26.238 9.195 -20.258 1.00 19.87 O ANISOU 2224 OD1 ASN B 123 1907 2305 3334 -1776 325 311 O ATOM 2225 ND2 ASN A 123 25.717 8.177 -18.331 1.00 18.25 N ANISOU 2225 ND2 ASN B 123 2684 1239 3008 -1069 -38 335 N ATOM 2226 N TYR A 124 25.676 13.952 -18.898 1.00 16.41 N ANISOU 2226 N TYR B 124 1966 1949 2320 -1168 516 388 N ATOM 2227 CA TYR A 124 25.342 15.298 -18.396 1.00 16.23 C ANISOU 2227 CA TYR B 124 1810 2019 2335 -1258 437 427 C ATOM 2228 C TYR A 124 23.971 15.756 -18.841 1.00 17.22 C ANISOU 2228 C TYR B 124 1958 2263 2319 -1230 446 388 C ATOM 2229 O TYR A 124 23.533 15.502 -19.967 1.00 17.02 O ANISOU 2229 O TYR B 124 2067 2376 2023 -1372 477 433 O ATOM 2230 CB TYR A 124 26.353 16.316 -18.918 1.00 16.90 C ANISOU 2230 CB TYR B 124 1928 2013 2480 -1189 316 508 C ATOM 2231 CG TYR A 124 27.769 16.057 -18.482 1.00 17.25 C ANISOU 2231 CG TYR B 124 1726 2238 2588 -1273 153 531 C ATOM 2232 CD1 TYR A 124 28.303 16.736 -17.394 1.00 17.85 C ANISOU 2232 CD1 TYR B 124 1986 2330 2464 -1240 -24 417 C ATOM 2233 CD2 TYR A 124 28.575 15.117 -19.153 1.00 16.21 C ANISOU 2233 CD2 TYR B 124 1587 1832 2738 -1269 -207 609 C ATOM 2234 CE1 TYR A 124 29.631 16.515 -16.984 1.00 18.84 C ANISOU 2234 CE1 TYR B 124 2032 2231 2895 -833 -31 578 C ATOM 2235 CE2 TYR A 124 29.903 14.884 -18.755 1.00 18.73 C ANISOU 2235 CE2 TYR B 124 2343 1985 2788 -896 -125 673 C ATOM 2236 CZ TYR A 124 30.421 15.594 -17.679 1.00 18.38 C ANISOU 2236 CZ TYR B 124 2021 2278 2684 -1029 -25 526 C ATOM 2237 OH TYR A 124 31.701 15.353 -17.281 1.00 19.35 O ANISOU 2237 OH TYR B 124 1995 2687 2670 -1033 -50 705 O ATOM 2238 N VAL A 125 23.303 16.463 -17.947 1.00 18.09 N ANISOU 2238 N VAL B 125 1921 2424 2527 -1184 315 351 N ATOM 2239 CA VAL A 125 21.990 16.992 -18.194 1.00 18.16 C ANISOU 2239 CA VAL B 125 1857 2496 2544 -1096 278 290 C ATOM 2240 C VAL A 125 22.216 18.493 -18.072 1.00 18.52 C ANISOU 2240 C VAL B 125 1901 2529 2605 -1092 181 311 C ATOM 2241 O VAL A 125 22.555 18.980 -17.005 1.00 19.53 O ANISOU 2241 O VAL B 125 1990 2797 2634 -990 14 100 O ATOM 2242 CB VAL A 125 20.962 16.441 -17.145 1.00 17.08 C ANISOU 2242 CB VAL B 125 1731 2276 2481 -1245 298 368 C ATOM 2243 CG1 VAL A 125 19.687 17.200 -17.216 1.00 16.32 C ANISOU 2243 CG1 VAL B 125 1480 2478 2243 -1216 702 576 C ATOM 2244 CG2 VAL A 125 20.697 14.932 -17.368 1.00 16.23 C ANISOU 2244 CG2 VAL B 125 1237 2421 2508 -1137 337 257 C ATOM 2245 N VAL A 126 22.022 19.215 -19.171 1.00 19.34 N ANISOU 2245 N VAL B 126 1902 2706 2738 -1072 228 312 N ATOM 2246 CA VAL A 126 22.535 20.573 -19.310 1.00 19.54 C ANISOU 2246 CA VAL B 126 2099 2593 2731 -941 184 361 C ATOM 2247 C VAL A 126 21.430 21.521 -19.715 1.00 20.18 C ANISOU 2247 C VAL B 126 2202 2784 2680 -906 189 353 C ATOM 2248 O VAL A 126 20.722 21.245 -20.693 1.00 21.36 O ANISOU 2248 O VAL B 126 2356 2885 2873 -962 73 285 O ATOM 2249 CB VAL A 126 23.654 20.574 -20.416 1.00 19.38 C ANISOU 2249 CB VAL B 126 1952 2620 2789 -995 255 346 C ATOM 2250 CG1 VAL A 126 24.313 21.947 -20.595 1.00 19.42 C ANISOU 2250 CG1 VAL B 126 2160 2298 2919 -872 309 474 C ATOM 2251 CG2 VAL A 126 24.697 19.504 -20.120 1.00 17.93 C ANISOU 2251 CG2 VAL B 126 1987 2150 2674 -932 179 460 C ATOM 2252 N PRO A 127 21.279 22.653 -18.994 1.00 20.21 N ANISOU 2252 N PRO B 127 2287 2860 2529 -804 223 389 N ATOM 2253 CA PRO A 127 20.316 23.667 -19.422 1.00 21.23 C ANISOU 2253 CA PRO B 127 2478 2997 2589 -716 214 408 C ATOM 2254 C PRO A 127 20.948 24.560 -20.468 1.00 22.06 C ANISOU 2254 C PRO B 127 2677 3105 2597 -595 180 486 C ATOM 2255 O PRO A 127 22.172 24.491 -20.677 1.00 22.71 O ANISOU 2255 O PRO B 127 2785 3130 2712 -517 81 452 O ATOM 2256 CB PRO A 127 20.100 24.505 -18.162 1.00 20.99 C ANISOU 2256 CB PRO B 127 2509 2964 2501 -750 234 397 C ATOM 2257 CG PRO A 127 21.384 24.394 -17.410 1.00 18.77 C ANISOU 2257 CG PRO B 127 1985 2723 2422 -849 349 459 C ATOM 2258 CD PRO A 127 22.014 23.070 -17.782 1.00 20.15 C ANISOU 2258 CD PRO B 127 2262 2842 2550 -829 250 393 C ATOM 2259 N VAL A 128 20.142 25.426 -21.080 1.00 23.73 N ANISOU 2259 N VAL B 128 2808 3399 2808 -483 95 505 N ATOM 2260 CA VAL A 128 20.678 26.524 -21.920 1.00 24.29 C ANISOU 2260 CA VAL B 128 2931 3459 2839 -439 104 536 C ATOM 2261 C VAL A 128 21.167 27.621 -20.962 1.00 25.46 C ANISOU 2261 C VAL B 128 3043 3660 2969 -292 120 503 C ATOM 2262 O VAL A 128 20.369 28.268 -20.291 1.00 26.21 O ANISOU 2262 O VAL B 128 3048 3854 3053 -273 115 528 O ATOM 2263 CB VAL A 128 19.595 27.088 -22.867 1.00 24.55 C ANISOU 2263 CB VAL B 128 3034 3435 2859 -421 122 527 C ATOM 2264 CG1 VAL A 128 20.170 28.130 -23.804 1.00 24.19 C ANISOU 2264 CG1 VAL B 128 2921 3323 2946 -446 196 556 C ATOM 2265 CG2 VAL A 128 18.918 25.955 -23.673 1.00 24.49 C ANISOU 2265 CG2 VAL B 128 2949 3523 2832 -528 190 566 C ATOM 2266 N LEU A 129 22.483 27.794 -20.844 1.00 26.00 N ANISOU 2266 N LEU B 129 3128 3782 2966 -296 136 506 N ATOM 2267 CA LEU A 129 23.008 28.745 -19.890 1.00 26.68 C ANISOU 2267 CA LEU B 129 3301 3815 3020 -211 75 407 C ATOM 2268 C LEU A 129 22.672 30.164 -20.303 1.00 27.99 C ANISOU 2268 C LEU B 129 3419 3976 3240 -158 21 300 C ATOM 2269 O LEU A 129 22.715 30.508 -21.490 1.00 28.90 O ANISOU 2269 O LEU B 129 3629 3985 3366 -71 -68 269 O ATOM 2270 CB LEU A 129 24.529 28.584 -19.731 1.00 26.64 C ANISOU 2270 CB LEU B 129 3363 3812 2947 -182 160 412 C ATOM 2271 CG LEU A 129 25.073 27.290 -19.108 1.00 26.82 C ANISOU 2271 CG LEU B 129 3640 3777 2771 -223 229 409 C ATOM 2272 CD1 LEU A 129 26.612 27.184 -19.263 1.00 26.18 C ANISOU 2272 CD1 LEU B 129 3813 3417 2715 -194 197 367 C ATOM 2273 CD2 LEU A 129 24.626 27.146 -17.628 1.00 25.60 C ANISOU 2273 CD2 LEU B 129 3990 3528 2208 -345 669 441 C ATOM 2274 N SER A 130 22.345 30.987 -19.315 1.00 29.26 N ANISOU 2274 N SER B 130 3531 4102 3484 -174 -27 253 N ATOM 2275 CA SER A 130 22.129 32.422 -19.518 1.00 30.75 C ANISOU 2275 CA SER B 130 3738 4193 3752 -155 -75 208 C ATOM 2276 C SER A 130 20.846 32.694 -20.301 1.00 32.12 C ANISOU 2276 C SER B 130 3938 4329 3938 -167 -113 172 C ATOM 2277 O SER A 130 20.754 33.645 -21.077 1.00 32.87 O ANISOU 2277 O SER B 130 4066 4331 4093 -257 -119 134 O ATOM 2278 CB SER A 130 23.355 33.054 -20.189 1.00 30.38 C ANISOU 2278 CB SER B 130 3665 4177 3701 -156 -83 229 C ATOM 2279 OG SER A 130 24.519 32.875 -19.375 1.00 29.41 O ANISOU 2279 OG SER B 130 3433 3944 3793 -182 127 305 O ATOM 2280 N SER A 131 19.841 31.853 -20.101 1.00 34.20 N ANISOU 2280 N SER B 131 4229 4547 4216 -137 -135 145 N ATOM 2281 CA SER A 131 18.610 32.006 -20.874 1.00 36.06 C ANISOU 2281 CA SER B 131 4465 4765 4470 -135 -145 159 C ATOM 2282 C SER A 131 17.465 32.538 -20.007 1.00 37.82 C ANISOU 2282 C SER B 131 4688 4968 4712 -82 -150 141 C ATOM 2283 O SER A 131 16.412 32.933 -20.526 1.00 38.70 O ANISOU 2283 O SER B 131 4684 5146 4875 -99 -214 166 O ATOM 2284 CB SER A 131 18.237 30.702 -21.594 1.00 35.74 C ANISOU 2284 CB SER B 131 4453 4709 4418 -172 -150 143 C ATOM 2285 OG SER A 131 17.738 29.734 -20.686 1.00 35.90 O ANISOU 2285 OG SER B 131 4568 4585 4486 -439 -173 193 O ATOM 2286 N GLY A 132 17.694 32.585 -18.694 1.00 38.88 N ANISOU 2286 N GLY B 132 4887 5070 4814 -61 -101 101 N ATOM 2287 CA GLY A 132 16.659 32.975 -17.743 1.00 40.43 C ANISOU 2287 CA GLY B 132 5115 5170 5074 -19 -41 62 C ATOM 2288 C GLY A 132 16.394 34.467 -17.659 1.00 41.44 C ANISOU 2288 C GLY B 132 5270 5266 5210 3 -19 45 C ATOM 2289 O GLY A 132 16.371 35.161 -18.683 1.00 41.86 O ANISOU 2289 O GLY B 132 5356 5318 5229 34 17 60 O ATOM 2290 N ILE A 133 16.183 34.951 -16.434 1.00 42.35 N ATOM 2291 CA ILE A 133 15.914 36.375 -16.172 1.00 43.19 C ATOM 2292 C ILE A 133 17.206 37.187 -16.151 1.00 43.57 C ATOM 2293 O ILE A 133 17.462 37.957 -17.082 1.00 44.37 O ATOM 2294 CB ILE A 133 15.046 36.590 -14.872 1.00 43.15 C ATOM 2295 CG1 ILE A 133 13.575 36.341 -15.186 1.00 43.38 C ATOM 2296 CG2 ILE A 133 15.179 38.021 -14.324 1.00 43.34 C ATOM 2297 CD1 ILE A 133 12.730 36.010 -13.985 1.00 43.63 C ATOM 2298 N GLY A 135 19.347 37.377 -18.738 1.00 44.76 N ANISOU 2298 N GLY B 135 6022 5827 5155 69 593 598 N ATOM 2299 CA GLY A 135 18.970 36.796 -20.024 1.00 44.77 C ANISOU 2299 CA GLY B 135 5996 5801 5213 85 546 537 C ATOM 2300 C GLY A 135 19.864 37.221 -21.187 1.00 44.58 C ANISOU 2300 C GLY B 135 5933 5781 5224 94 521 523 C ATOM 2301 O GLY A 135 20.161 38.407 -21.353 1.00 45.00 O ANISOU 2301 O GLY B 135 5991 5765 5340 104 518 553 O ATOM 2302 N VAL A 136 20.289 36.237 -21.981 1.00 43.85 N ANISOU 2302 N VAL B 136 5811 5735 5114 115 484 471 N ATOM 2303 CA VAL A 136 21.137 36.430 -23.164 1.00 43.22 C ANISOU 2303 CA VAL B 136 5688 5684 5047 100 422 472 C ATOM 2304 C VAL A 136 20.485 35.612 -24.289 1.00 42.80 C ANISOU 2304 C VAL B 136 5679 5631 4951 124 396 494 C ATOM 2305 O VAL A 136 19.697 34.702 -24.004 1.00 43.15 O ANISOU 2305 O VAL B 136 5687 5653 5055 142 390 465 O ATOM 2306 CB VAL A 136 22.603 35.952 -22.861 1.00 43.33 C ANISOU 2306 CB VAL B 136 5709 5711 5041 89 452 461 C ATOM 2307 CG1 VAL A 136 23.311 35.399 -24.091 1.00 43.18 C ANISOU 2307 CG1 VAL B 136 5609 5636 5161 52 441 409 C ATOM 2308 CG2 VAL A 136 23.419 37.075 -22.193 1.00 43.37 C ANISOU 2308 CG2 VAL B 136 5569 5765 5141 31 472 518 C ATOM 2309 N ASP A 137 20.774 35.933 -25.550 1.00 41.82 N ANISOU 2309 N ASP B 137 5604 5530 4753 125 341 549 N ATOM 2310 CA ASP A 137 20.175 35.176 -26.665 1.00 41.12 C ANISOU 2310 CA ASP B 137 5547 5457 4616 98 312 606 C ATOM 2311 C ASP A 137 20.519 33.682 -26.588 1.00 39.72 C ANISOU 2311 C ASP B 137 5360 5269 4461 103 254 661 C ATOM 2312 O ASP A 137 21.677 33.292 -26.424 1.00 39.62 O ANISOU 2312 O ASP B 137 5310 5253 4488 96 249 623 O ATOM 2313 CB ASP A 137 20.534 35.771 -28.045 1.00 41.57 C ANISOU 2313 CB ASP B 137 5659 5518 4617 64 352 636 C ATOM 2314 CG ASP A 137 19.882 35.011 -29.226 1.00 42.81 C ANISOU 2314 CG ASP B 137 5866 5782 4615 -54 466 682 C ATOM 2315 OD1 ASP A 137 18.942 34.201 -29.036 1.00 45.25 O ANISOU 2315 OD1 ASP B 137 6218 6132 4840 -242 395 598 O ATOM 2316 OD2 ASP A 137 20.313 35.230 -30.373 1.00 44.15 O ANISOU 2316 OD2 ASP B 137 6206 5931 4634 -32 636 789 O ATOM 2317 N PHE A 138 19.485 32.857 -26.698 1.00 38.10 N ANISOU 2317 N PHE B 138 5150 5097 4229 110 201 709 N ATOM 2318 CA PHE A 138 19.638 31.424 -26.562 1.00 36.35 C ANISOU 2318 CA PHE B 138 4966 4854 3989 115 215 743 C ATOM 2319 C PHE A 138 20.380 30.757 -27.708 1.00 35.43 C ANISOU 2319 C PHE B 138 4871 4721 3867 75 177 760 C ATOM 2320 O PHE A 138 21.020 29.733 -27.494 1.00 35.43 O ANISOU 2320 O PHE B 138 4812 4744 3905 71 128 779 O ATOM 2321 CB PHE A 138 18.283 30.749 -26.317 1.00 36.22 C ANISOU 2321 CB PHE B 138 4887 4921 3954 137 225 718 C ATOM 2322 CG PHE A 138 17.391 30.717 -27.517 1.00 35.69 C ANISOU 2322 CG PHE B 138 4870 4882 3808 224 358 845 C ATOM 2323 CD1 PHE A 138 16.510 31.758 -27.768 1.00 35.61 C ANISOU 2323 CD1 PHE B 138 4921 4982 3625 263 362 963 C ATOM 2324 CD2 PHE A 138 17.416 29.625 -28.380 1.00 35.25 C ANISOU 2324 CD2 PHE B 138 4779 4823 3790 329 398 921 C ATOM 2325 CE1 PHE A 138 15.666 31.709 -28.875 1.00 37.32 C ANISOU 2325 CE1 PHE B 138 5291 5080 3809 324 316 680 C ATOM 2326 CE2 PHE A 138 16.592 29.554 -29.476 1.00 34.22 C ANISOU 2326 CE2 PHE B 138 5003 4730 3269 484 299 1014 C ATOM 2327 CZ PHE A 138 15.712 30.600 -29.735 1.00 37.32 C ANISOU 2327 CZ PHE B 138 5227 5166 3784 345 271 720 C ATOM 2328 N LYS A 139 20.287 31.311 -28.918 1.00 34.10 N ANISOU 2328 N LYS B 139 4792 4509 3654 58 192 779 N ATOM 2329 CA LYS A 139 20.995 30.739 -30.065 1.00 33.34 C ANISOU 2329 CA LYS B 139 4783 4337 3548 83 218 771 C ATOM 2330 C LYS A 139 22.507 30.843 -29.882 1.00 32.18 C ANISOU 2330 C LYS B 139 4667 4151 3407 -13 302 769 C ATOM 2331 O LYS A 139 23.241 29.930 -30.230 1.00 31.86 O ANISOU 2331 O LYS B 139 4716 4142 3245 -48 320 818 O ATOM 2332 CB LYS A 139 20.544 31.381 -31.389 1.00 33.06 C ANISOU 2332 CB LYS B 139 4797 4328 3436 107 195 725 C ATOM 2333 CG LYS A 139 19.051 31.184 -31.653 1.00 33.46 C ANISOU 2333 CG LYS B 139 4848 4312 3551 181 194 790 C ATOM 2334 CD LYS A 139 18.614 31.644 -33.037 1.00 34.82 C ANISOU 2334 CD LYS B 139 4949 4525 3756 208 176 719 C ATOM 2335 CE LYS A 139 17.096 31.551 -33.184 1.00 37.52 C ANISOU 2335 CE LYS B 139 5323 4753 4179 252 345 679 C ATOM 2336 NZ LYS A 139 16.384 32.811 -32.749 1.00 39.61 N ANISOU 2336 NZ LYS B 139 5569 4848 4629 354 356 698 N ATOM 2337 N ILE A 140 22.974 31.943 -29.310 1.00 31.43 N ANISOU 2337 N ILE B 140 4537 4016 3387 -162 436 749 N ATOM 2338 CA ILE A 140 24.396 32.049 -29.029 1.00 31.13 C ANISOU 2338 CA ILE B 140 4464 3837 3526 -265 498 695 C ATOM 2339 C ILE A 140 24.857 31.093 -27.930 1.00 29.82 C ANISOU 2339 C ILE B 140 4290 3672 3367 -349 619 720 C ATOM 2340 O ILE A 140 25.945 30.514 -28.042 1.00 29.62 O ANISOU 2340 O ILE B 140 4191 3587 3475 -439 683 799 O ATOM 2341 CB ILE A 140 24.897 33.531 -28.852 1.00 31.72 C ANISOU 2341 CB ILE B 140 4519 3893 3638 -250 472 639 C ATOM 2342 CG1 ILE A 140 26.043 33.619 -27.837 1.00 32.11 C ANISOU 2342 CG1 ILE B 140 4594 3818 3785 -386 418 689 C ATOM 2343 CG2 ILE A 140 23.754 34.476 -28.485 1.00 32.91 C ANISOU 2343 CG2 ILE B 140 4615 4030 3856 -270 541 654 C ATOM 2344 CD1 ILE A 140 26.571 35.046 -27.649 1.00 32.88 C ANISOU 2344 CD1 ILE B 140 4647 4014 3832 -300 511 568 C ATOM 2345 N SER A 141 24.023 30.899 -26.900 1.00 28.40 N ANISOU 2345 N SER B 141 4099 3459 3233 -427 669 725 N ATOM 2346 CA SER A 141 24.305 29.939 -25.843 1.00 26.76 C ANISOU 2346 CA SER B 141 3911 3296 2960 -552 745 729 C ATOM 2347 C SER A 141 24.435 28.518 -26.442 1.00 26.31 C ANISOU 2347 C SER B 141 3874 3223 2899 -560 740 770 C ATOM 2348 O SER A 141 25.438 27.835 -26.238 1.00 26.43 O ANISOU 2348 O SER B 141 3977 3173 2892 -550 787 849 O ATOM 2349 CB SER A 141 23.195 29.996 -24.769 1.00 26.81 C ANISOU 2349 CB SER B 141 3916 3278 2992 -591 730 728 C ATOM 2350 OG SER A 141 23.484 29.125 -23.689 1.00 26.88 O ANISOU 2350 OG SER B 141 3474 3709 3030 -733 679 656 O ATOM 2351 N ILE A 142 23.433 28.111 -27.218 1.00 24.97 N ANISOU 2351 N ILE B 142 3692 2990 2805 -742 763 766 N ATOM 2352 CA ILE A 142 23.406 26.796 -27.859 1.00 24.53 C ANISOU 2352 CA ILE B 142 3612 2874 2833 -793 688 777 C ATOM 2353 C ILE A 142 24.551 26.572 -28.850 1.00 25.15 C ANISOU 2353 C ILE B 142 3651 2802 3103 -847 575 681 C ATOM 2354 O ILE A 142 25.115 25.467 -28.930 1.00 24.46 O ANISOU 2354 O ILE B 142 3613 2454 3225 -977 549 733 O ATOM 2355 CB ILE A 142 22.057 26.576 -28.551 1.00 24.34 C ANISOU 2355 CB ILE B 142 3519 2871 2854 -844 691 756 C ATOM 2356 CG1 ILE A 142 20.952 26.445 -27.495 1.00 24.18 C ANISOU 2356 CG1 ILE B 142 3570 2928 2689 -725 630 896 C ATOM 2357 CG2 ILE A 142 22.115 25.359 -29.452 1.00 25.07 C ANISOU 2357 CG2 ILE B 142 3585 3205 2732 -768 853 740 C ATOM 2358 CD1 ILE A 142 19.532 26.514 -28.058 1.00 23.32 C ANISOU 2358 CD1 ILE B 142 3109 2905 2846 -1237 832 840 C ATOM 2359 N ASP A 143 24.917 27.627 -29.586 1.00 24.23 N ANISOU 2359 N ASP B 143 3544 2697 2965 -918 505 695 N ATOM 2360 CA ASP A 143 26.054 27.542 -30.494 1.00 24.34 C ANISOU 2360 CA ASP B 143 3457 2743 3046 -951 404 494 C ATOM 2361 C ASP A 143 27.338 27.315 -29.727 1.00 23.70 C ANISOU 2361 C ASP B 143 3235 2764 3003 -960 412 381 C ATOM 2362 O ASP A 143 28.112 26.430 -30.092 1.00 23.33 O ANISOU 2362 O ASP B 143 3204 2797 2862 -957 436 231 O ATOM 2363 CB ASP A 143 26.155 28.775 -31.400 1.00 25.27 C ANISOU 2363 CB ASP B 143 3588 2819 3192 -945 339 584 C ATOM 2364 CG ASP A 143 25.102 28.763 -32.501 1.00 28.79 C ANISOU 2364 CG ASP B 143 4194 3115 3627 -1029 252 695 C ATOM 2365 OD1 ASP A 143 24.449 27.715 -32.713 1.00 27.95 O ANISOU 2365 OD1 ASP B 143 3552 3070 3994 -1613 440 568 O ATOM 2366 OD2 ASP A 143 24.923 29.803 -33.159 1.00 32.31 O ANISOU 2366 OD2 ASP B 143 4839 3627 3808 -939 275 1157 O ATOM 2367 N ALA A 144 27.523 28.102 -28.653 1.00 22.40 N ANISOU 2367 N ALA B 144 2930 2657 2921 -1094 467 283 N ATOM 2368 CA ALA A 144 28.649 27.987 -27.721 1.00 21.47 C ANISOU 2368 CA ALA B 144 2703 2544 2909 -1261 559 303 C ATOM 2369 C ALA A 144 28.843 26.590 -27.138 1.00 21.82 C ANISOU 2369 C ALA B 144 2636 2630 3022 -1238 597 264 C ATOM 2370 O ALA A 144 29.982 26.118 -27.022 1.00 20.90 O ANISOU 2370 O ALA B 144 2415 2369 3154 -1512 565 176 O ATOM 2371 CB ALA A 144 28.471 28.980 -26.593 1.00 21.20 C ANISOU 2371 CB ALA B 144 2670 2576 2808 -1269 582 223 C ATOM 2372 N MET A 145 27.724 25.974 -26.711 1.00 22.12 N ANISOU 2372 N MET B 145 2648 2715 3040 -1312 597 399 N ATOM 2373 CA MET A 145 27.692 24.605 -26.224 1.00 22.66 C ANISOU 2373 CA MET B 145 2603 2874 3133 -1235 702 559 C ATOM 2374 C MET A 145 28.236 23.566 -27.215 1.00 23.63 C ANISOU 2374 C MET B 145 2796 3092 3090 -1079 627 559 C ATOM 2375 O MET A 145 29.068 22.706 -26.843 1.00 24.38 O ANISOU 2375 O MET B 145 2825 3262 3174 -1045 604 627 O ATOM 2376 CB MET A 145 26.258 24.231 -25.803 1.00 22.01 C ANISOU 2376 CB MET B 145 2424 2852 3088 -1190 667 564 C ATOM 2377 CG MET A 145 26.191 22.917 -25.085 1.00 23.90 C ANISOU 2377 CG MET B 145 2464 3075 3540 -1343 776 588 C ATOM 2378 SD MET A 145 24.535 22.208 -24.764 1.00 21.14 S ANISOU 2378 SD MET B 145 2133 2761 3137 -1615 1017 742 S ATOM 2379 CE MET A 145 24.129 21.661 -26.400 1.00 26.36 C ANISOU 2379 CE MET B 145 2519 3219 4275 -1463 716 468 C ATOM 2380 N ARG A 146 27.722 23.603 -28.446 1.00 24.29 N ANISOU 2380 N ARG B 146 2885 3165 3179 -1018 513 564 N ATOM 2381 CA ARG A 146 28.269 22.823 -29.572 1.00 25.12 C ANISOU 2381 CA ARG B 146 3188 3128 3228 -983 401 465 C ATOM 2382 C ARG A 146 29.801 22.953 -29.741 1.00 25.13 C ANISOU 2382 C ARG B 146 3274 3076 3195 -948 528 503 C ATOM 2383 O ARG A 146 30.508 21.947 -29.873 1.00 24.17 O ANISOU 2383 O ARG B 146 3364 2885 2933 -853 647 349 O ATOM 2384 CB ARG A 146 27.593 23.233 -30.875 1.00 25.26 C ANISOU 2384 CB ARG B 146 3123 3175 3298 -999 308 454 C ATOM 2385 CG ARG A 146 26.203 22.668 -31.059 1.00 28.34 C ANISOU 2385 CG ARG B 146 3701 3411 3655 -1187 23 341 C ATOM 2386 CD ARG A 146 25.980 22.362 -32.562 1.00 31.71 C ANISOU 2386 CD ARG B 146 3945 3952 4150 -1402 -405 628 C ATOM 2387 NE ARG A 146 25.061 21.235 -32.699 1.00 36.53 N ANISOU 2387 NE ARG B 146 4774 4462 4644 -1147 -735 586 N ATOM 2388 CZ ARG A 146 25.417 19.984 -32.953 1.00 36.82 C ANISOU 2388 CZ ARG B 146 4721 4359 4910 -1239 -722 673 C ATOM 2389 NH1 ARG A 146 24.484 19.058 -33.033 1.00 40.54 N ANISOU 2389 NH1 ARG B 146 4973 5046 5383 -1147 -827 673 N ATOM 2390 NH2 ARG A 146 26.686 19.655 -33.133 1.00 38.83 N ANISOU 2390 NH2 ARG B 146 5014 4731 5007 -917 -691 820 N ATOM 2391 N GLU A 147 30.311 24.188 -29.701 1.00 25.52 N ANISOU 2391 N GLU B 147 3397 2940 3357 -978 542 537 N ATOM 2392 CA GLU A 147 31.747 24.426 -29.824 1.00 25.73 C ANISOU 2392 CA GLU B 147 3388 2915 3472 -1141 624 589 C ATOM 2393 C GLU A 147 32.517 23.796 -28.647 1.00 24.67 C ANISOU 2393 C GLU B 147 3288 2810 3273 -1150 647 588 C ATOM 2394 O GLU A 147 33.508 23.102 -28.846 1.00 23.86 O ANISOU 2394 O GLU B 147 2963 2710 3391 -1461 747 645 O ATOM 2395 CB GLU A 147 32.058 25.922 -29.938 1.00 26.48 C ANISOU 2395 CB GLU B 147 3496 3046 3516 -978 669 577 C ATOM 2396 CG GLU A 147 33.412 26.184 -30.591 1.00 28.01 C ANISOU 2396 CG GLU B 147 3674 2998 3969 -1372 717 661 C ATOM 2397 CD GLU A 147 33.991 27.598 -30.337 1.00 29.27 C ANISOU 2397 CD GLU B 147 3780 3333 4007 -1156 599 651 C ATOM 2398 OE1 GLU A 147 33.269 28.619 -30.472 1.00 30.76 O ANISOU 2398 OE1 GLU B 147 4373 3242 4073 -785 713 933 O ATOM 2399 OE2 GLU A 147 35.192 27.664 -29.994 1.00 35.07 O ANISOU 2399 OE2 GLU B 147 4111 4349 4863 -1376 769 852 O ATOM 2400 N ALA A 148 32.020 23.995 -27.426 1.00 24.78 N ANISOU 2400 N ALA B 148 3381 2773 3259 -1163 525 599 N ATOM 2401 CA ALA A 148 32.677 23.497 -26.215 1.00 23.15 C ANISOU 2401 CA ALA B 148 3242 2630 2922 -1225 439 638 C ATOM 2402 C ALA A 148 32.744 21.969 -26.133 1.00 22.53 C ANISOU 2402 C ALA B 148 3203 2498 2858 -1280 432 634 C ATOM 2403 O ALA A 148 33.712 21.411 -25.593 1.00 21.00 O ANISOU 2403 O ALA B 148 2898 2290 2788 -1596 429 575 O ATOM 2404 CB ALA A 148 31.978 24.048 -24.994 1.00 23.28 C ANISOU 2404 CB ALA B 148 3253 2630 2960 -1131 438 569 C ATOM 2405 N PHE A 149 31.704 21.288 -26.647 1.00 22.74 N ANISOU 2405 N PHE B 149 3315 2517 2804 -1261 368 693 N ATOM 2406 CA PHE A 149 31.598 19.831 -26.508 1.00 22.28 C ANISOU 2406 CA PHE B 149 3368 2489 2608 -1197 444 800 C ATOM 2407 C PHE A 149 32.215 19.009 -27.649 1.00 23.33 C ANISOU 2407 C PHE B 149 3501 2566 2796 -1140 426 817 C ATOM 2408 O PHE A 149 32.379 17.795 -27.524 1.00 21.95 O ANISOU 2408 O PHE B 149 3491 2266 2583 -1260 459 916 O ATOM 2409 CB PHE A 149 30.134 19.419 -26.240 1.00 22.14 C ANISOU 2409 CB PHE B 149 3257 2478 2675 -1207 412 854 C ATOM 2410 CG PHE A 149 29.605 19.846 -24.864 1.00 21.81 C ANISOU 2410 CG PHE B 149 3120 2605 2559 -1194 526 862 C ATOM 2411 CD1 PHE A 149 30.478 20.129 -23.803 1.00 22.84 C ANISOU 2411 CD1 PHE B 149 3249 2954 2473 -984 650 1064 C ATOM 2412 CD2 PHE A 149 28.220 19.943 -24.625 1.00 22.21 C ANISOU 2412 CD2 PHE B 149 3039 2906 2492 -874 692 934 C ATOM 2413 CE1 PHE A 149 29.983 20.515 -22.530 1.00 24.77 C ANISOU 2413 CE1 PHE B 149 3318 2935 3157 -1017 472 740 C ATOM 2414 CE2 PHE A 149 27.721 20.315 -23.350 1.00 22.79 C ANISOU 2414 CE2 PHE B 149 3059 2728 2870 -755 236 974 C ATOM 2415 CZ PHE A 149 28.596 20.611 -22.313 1.00 23.01 C ANISOU 2415 CZ PHE B 149 3401 2662 2676 -945 556 887 C ATOM 2416 N LYS A 150 32.555 19.675 -28.754 1.00 23.53 N ANISOU 2416 N LYS B 150 3580 2611 2746 -1121 462 785 N ATOM 2417 CA LYS A 150 33.246 19.059 -29.888 1.00 24.97 C ANISOU 2417 CA LYS B 150 3730 2807 2947 -1043 464 654 C ATOM 2418 C LYS A 150 34.385 18.170 -29.432 1.00 24.81 C ANISOU 2418 C LYS B 150 3647 2894 2885 -1028 446 594 C ATOM 2419 O LYS A 150 35.241 18.611 -28.684 1.00 25.98 O ANISOU 2419 O LYS B 150 3709 3089 3072 -1064 373 431 O ATOM 2420 CB LYS A 150 33.858 20.139 -30.786 1.00 24.97 C ANISOU 2420 CB LYS B 150 3771 2714 3002 -1109 481 741 C ATOM 2421 CG LYS A 150 33.090 20.462 -32.023 1.00 25.98 C ANISOU 2421 CG LYS B 150 4099 2831 2940 -1087 521 581 C ATOM 2422 CD LYS A 150 33.946 21.255 -32.987 1.00 29.88 C ANISOU 2422 CD LYS B 150 4651 3345 3356 -918 636 665 C ATOM 2423 CE LYS A 150 33.148 22.387 -33.608 1.00 31.85 C ANISOU 2423 CE LYS B 150 5215 3592 3294 -985 775 874 C ATOM 2424 NZ LYS A 150 33.604 22.725 -34.965 1.00 32.87 N ANISOU 2424 NZ LYS B 150 5485 3257 3745 -1186 926 1250 N ATOM 2425 N GLY A 151 34.399 16.924 -29.890 1.00 24.34 N ANISOU 2425 N GLY B 151 3576 2850 2820 -923 491 518 N ATOM 2426 CA GLY A 151 35.512 16.039 -29.617 1.00 23.64 C ANISOU 2426 CA GLY B 151 3354 2861 2765 -936 449 494 C ATOM 2427 C GLY A 151 35.447 15.313 -28.300 1.00 23.74 C ANISOU 2427 C GLY B 151 3342 2801 2874 -865 370 396 C ATOM 2428 O GLY A 151 36.290 14.469 -28.047 1.00 24.41 O ANISOU 2428 O GLY B 151 3330 2952 2992 -848 336 391 O ATOM 2429 N CYS A 152 34.435 15.623 -27.478 1.00 22.99 N ANISOU 2429 N CYS B 152 3190 2685 2858 -1009 387 369 N ATOM 2430 CA CYS A 152 34.325 15.088 -26.111 1.00 22.75 C ANISOU 2430 CA CYS B 152 3155 2573 2913 -1008 380 283 C ATOM 2431 C CYS A 152 33.529 13.816 -26.159 1.00 22.07 C ANISOU 2431 C CYS B 152 3148 2422 2815 -878 316 209 C ATOM 2432 O CYS A 152 32.484 13.766 -26.777 1.00 22.76 O ANISOU 2432 O CYS B 152 3360 2333 2955 -840 359 41 O ATOM 2433 CB CYS A 152 33.630 16.082 -25.181 1.00 22.99 C ANISOU 2433 CB CYS B 152 3200 2541 2991 -1108 350 367 C ATOM 2434 SG CYS A 152 34.534 17.598 -24.906 1.00 26.98 S ANISOU 2434 SG CYS B 152 3660 3096 3492 -1266 619 248 S ATOM 2435 N ALA A 153 34.026 12.802 -25.465 1.00 22.30 N ANISOU 2435 N ALA B 153 3133 2503 2837 -825 330 67 N ATOM 2436 CA ALA A 153 33.436 11.491 -25.456 1.00 21.43 C ANISOU 2436 CA ALA B 153 2902 2482 2757 -786 357 141 C ATOM 2437 C ALA A 153 32.470 11.434 -24.251 1.00 20.63 C ANISOU 2437 C ALA B 153 2685 2509 2644 -746 272 81 C ATOM 2438 O ALA A 153 32.780 10.862 -23.200 1.00 20.31 O ANISOU 2438 O ALA B 153 2611 2416 2690 -859 330 60 O ATOM 2439 CB ALA A 153 34.557 10.447 -25.352 1.00 21.92 C ANISOU 2439 CB ALA B 153 2951 2581 2795 -870 359 130 C ATOM 2440 N ILE A 154 31.310 12.065 -24.435 1.00 20.71 N ANISOU 2440 N ILE B 154 2696 2543 2627 -701 160 8 N ATOM 2441 CA ILE A 154 30.294 12.285 -23.398 1.00 19.50 C ANISOU 2441 CA ILE B 154 2323 2569 2515 -642 43 -31 C ATOM 2442 C ILE A 154 28.894 12.199 -23.981 1.00 20.74 C ANISOU 2442 C ILE B 154 2530 2801 2546 -552 -29 -13 C ATOM 2443 O ILE A 154 28.726 12.193 -25.213 1.00 22.51 O ANISOU 2443 O ILE B 154 2823 3103 2628 -479 13 115 O ATOM 2444 CB ILE A 154 30.426 13.679 -22.718 1.00 19.59 C ANISOU 2444 CB ILE B 154 2342 2593 2507 -596 46 -45 C ATOM 2445 CG1 ILE A 154 30.119 14.811 -23.721 1.00 18.02 C ANISOU 2445 CG1 ILE B 154 2071 2231 2543 -486 -105 -112 C ATOM 2446 CG2 ILE A 154 31.812 13.828 -22.070 1.00 17.45 C ANISOU 2446 CG2 ILE B 154 1846 2283 2499 -1071 -343 -246 C ATOM 2447 CD1 ILE A 154 30.112 16.230 -23.094 1.00 20.18 C ANISOU 2447 CD1 ILE B 154 2253 2696 2718 -526 32 -150 C ATOM 2448 N ARG A 155 27.897 12.116 -23.102 1.00 19.91 N ANISOU 2448 N ARG B 155 2213 2790 2563 -558 -41 14 N ATOM 2449 CA ARG A 155 26.477 12.218 -23.501 1.00 20.05 C ANISOU 2449 CA ARG B 155 2149 2858 2610 -531 -130 25 C ATOM 2450 C ARG A 155 25.835 13.435 -22.867 1.00 20.23 C ANISOU 2450 C ARG B 155 2051 2988 2645 -605 -87 28 C ATOM 2451 O ARG A 155 25.983 13.667 -21.672 1.00 19.94 O ANISOU 2451 O ARG B 155 1950 3088 2536 -597 -79 122 O ATOM 2452 CB ARG A 155 25.709 10.972 -23.110 1.00 19.94 C ANISOU 2452 CB ARG B 155 2025 2942 2608 -523 -157 -46 C ATOM 2453 CG ARG A 155 26.393 9.712 -23.537 1.00 20.37 C ANISOU 2453 CG ARG B 155 2297 2878 2563 -431 -99 -123 C ATOM 2454 CD ARG A 155 25.527 8.542 -23.242 1.00 21.34 C ANISOU 2454 CD ARG B 155 2284 2883 2940 -694 164 -321 C ATOM 2455 NE ARG A 155 26.115 7.269 -23.638 1.00 21.76 N ANISOU 2455 NE ARG B 155 2350 2919 2998 -1191 240 -355 N ATOM 2456 CZ ARG A 155 26.887 6.510 -22.869 1.00 22.23 C ANISOU 2456 CZ ARG B 155 2435 2730 3281 -1267 181 -519 C ATOM 2457 NH1 ARG A 155 27.230 6.911 -21.641 1.00 22.03 N ANISOU 2457 NH1 ARG B 155 2822 2174 3372 -1726 310 -475 N ATOM 2458 NH2 ARG A 155 27.339 5.352 -23.346 1.00 21.72 N ANISOU 2458 NH2 ARG B 155 2666 2424 3160 -1658 380 -849 N ATOM 2459 N VAL A 156 25.138 14.229 -23.680 1.00 20.36 N ANISOU 2459 N VAL B 156 2006 2959 2770 -675 -109 3 N ATOM 2460 CA VAL A 156 24.529 15.468 -23.213 1.00 20.53 C ANISOU 2460 CA VAL B 156 2048 2920 2830 -700 -61 -16 C ATOM 2461 C VAL A 156 23.049 15.440 -23.527 1.00 21.06 C ANISOU 2461 C VAL B 156 2135 3050 2814 -665 -55 -27 C ATOM 2462 O VAL A 156 22.681 15.297 -24.695 1.00 21.45 O ANISOU 2462 O VAL B 156 2068 3316 2763 -651 -14 36 O ATOM 2463 CB VAL A 156 25.163 16.695 -23.909 1.00 20.41 C ANISOU 2463 CB VAL B 156 1973 2886 2893 -667 -42 -38 C ATOM 2464 CG1 VAL A 156 24.428 17.991 -23.538 1.00 19.95 C ANISOU 2464 CG1 VAL B 156 2226 2779 2572 -833 -6 127 C ATOM 2465 CG2 VAL A 156 26.654 16.752 -23.592 1.00 21.36 C ANISOU 2465 CG2 VAL B 156 2369 2769 2975 -708 -192 -203 C ATOM 2466 N LEU A 157 22.218 15.479 -22.479 1.00 20.73 N ANISOU 2466 N LEU B 157 2241 2884 2751 -736 -17 -93 N ATOM 2467 CA LEU A 157 20.813 15.776 -22.608 1.00 20.52 C ANISOU 2467 CA LEU B 157 2177 2853 2764 -819 23 -44 C ATOM 2468 C LEU A 157 20.555 17.271 -22.394 1.00 20.82 C ANISOU 2468 C LEU B 157 2326 2867 2717 -791 29 61 C ATOM 2469 O LEU A 157 20.605 17.768 -21.262 1.00 21.68 O ANISOU 2469 O LEU B 157 2486 2803 2948 -664 -46 -59 O ATOM 2470 CB LEU A 157 20.003 14.937 -21.596 1.00 20.12 C ANISOU 2470 CB LEU B 157 2160 2797 2685 -837 11 -146 C ATOM 2471 CG LEU A 157 18.485 15.173 -21.455 1.00 23.56 C ANISOU 2471 CG LEU B 157 2672 3320 2959 -835 -20 -74 C ATOM 2472 CD1 LEU A 157 17.781 15.170 -22.768 1.00 26.65 C ANISOU 2472 CD1 LEU B 157 2952 3726 3446 -459 213 -196 C ATOM 2473 CD2 LEU A 157 17.853 14.112 -20.522 1.00 20.85 C ANISOU 2473 CD2 LEU B 157 1942 2948 3030 -1130 119 101 C ATOM 2474 N LEU A 158 20.253 17.986 -23.471 1.00 21.57 N ANISOU 2474 N LEU B 158 2484 2919 2791 -771 61 172 N ATOM 2475 CA LEU A 158 19.939 19.411 -23.354 1.00 22.06 C ANISOU 2475 CA LEU B 158 2700 3009 2670 -751 160 300 C ATOM 2476 C LEU A 158 18.462 19.608 -23.011 1.00 22.16 C ANISOU 2476 C LEU B 158 2698 3082 2640 -781 192 364 C ATOM 2477 O LEU A 158 17.576 19.039 -23.673 1.00 22.79 O ANISOU 2477 O LEU B 158 2989 2942 2725 -880 242 315 O ATOM 2478 CB LEU A 158 20.289 20.180 -24.643 1.00 22.11 C ANISOU 2478 CB LEU B 158 2673 3043 2683 -786 174 360 C ATOM 2479 CG LEU A 158 19.759 21.618 -24.653 1.00 22.19 C ANISOU 2479 CG LEU B 158 2879 3049 2501 -887 179 489 C ATOM 2480 CD1 LEU A 158 20.669 22.531 -23.821 1.00 23.11 C ANISOU 2480 CD1 LEU B 158 2746 3490 2542 -1024 133 476 C ATOM 2481 CD2 LEU A 158 19.609 22.163 -26.096 1.00 22.91 C ANISOU 2481 CD2 LEU B 158 2822 3219 2664 -678 108 376 C ATOM 2482 N PHE A 159 18.173 20.430 -22.000 1.00 21.95 N ANISOU 2482 N PHE B 159 2649 3084 2606 -809 219 388 N ATOM 2483 CA PHE A 159 16.771 20.555 -21.585 1.00 22.28 C ANISOU 2483 CA PHE B 159 2565 3277 2624 -742 261 427 C ATOM 2484 C PHE A 159 16.297 21.983 -21.439 1.00 22.96 C ANISOU 2484 C PHE B 159 2617 3399 2706 -698 234 585 C ATOM 2485 O PHE A 159 17.098 22.861 -21.151 1.00 22.68 O ANISOU 2485 O PHE B 159 2664 3306 2646 -770 302 686 O ATOM 2486 CB PHE A 159 16.498 19.741 -20.299 1.00 22.04 C ANISOU 2486 CB PHE B 159 2507 3352 2513 -806 199 317 C ATOM 2487 CG PHE A 159 17.065 20.360 -19.040 1.00 22.49 C ANISOU 2487 CG PHE B 159 2488 3595 2462 -949 281 153 C ATOM 2488 CD1 PHE A 159 16.285 21.207 -18.248 1.00 22.55 C ANISOU 2488 CD1 PHE B 159 2190 3512 2864 -1176 13 -28 C ATOM 2489 CD2 PHE A 159 18.386 20.090 -18.646 1.00 20.86 C ANISOU 2489 CD2 PHE B 159 2198 3632 2095 -920 -3 55 C ATOM 2490 CE1 PHE A 159 16.815 21.776 -17.061 1.00 22.83 C ANISOU 2490 CE1 PHE B 159 2502 3601 2569 -1110 -49 -92 C ATOM 2491 CE2 PHE A 159 18.923 20.652 -17.475 1.00 22.89 C ANISOU 2491 CE2 PHE B 159 2397 3743 2556 -985 195 -67 C ATOM 2492 CZ PHE A 159 18.141 21.491 -16.685 1.00 22.93 C ANISOU 2492 CZ PHE B 159 2475 3674 2560 -892 168 -16 C ATOM 2493 N SER A 160 14.988 22.200 -21.618 1.00 23.25 N ANISOU 2493 N SER B 160 2472 3501 2858 -640 326 724 N ATOM 2494 CA SER A 160 14.408 23.539 -21.535 1.00 25.30 C ANISOU 2494 CA SER B 160 2584 3897 3129 -492 267 627 C ATOM 2495 C SER A 160 12.885 23.449 -21.383 1.00 26.44 C ANISOU 2495 C SER B 160 2621 4072 3353 -370 185 547 C ATOM 2496 O SER A 160 12.263 22.474 -21.806 1.00 26.67 O ANISOU 2496 O SER B 160 2478 4185 3469 -402 253 591 O ATOM 2497 CB SER A 160 14.811 24.381 -22.778 1.00 25.55 C ANISOU 2497 CB SER B 160 2718 3767 3222 -495 146 686 C ATOM 2498 OG SER A 160 14.295 25.706 -22.710 1.00 27.05 O ANISOU 2498 OG SER B 160 3099 3894 3285 -624 168 618 O ATOM 2499 N LEU A 161 12.294 24.454 -20.749 1.00 27.76 N ANISOU 2499 N LEU B 161 2692 4403 3449 -267 152 462 N ATOM 2500 CA LEU A 161 10.828 24.597 -20.754 1.00 28.81 C ANISOU 2500 CA LEU B 161 2761 4618 3564 -266 121 353 C ATOM 2501 C LEU A 161 10.327 25.046 -22.132 1.00 29.40 C ANISOU 2501 C LEU B 161 2793 4769 3606 -242 7 317 C ATOM 2502 O LEU A 161 9.164 24.838 -22.483 1.00 29.83 O ANISOU 2502 O LEU B 161 2716 4922 3696 -276 98 388 O ATOM 2503 CB LEU A 161 10.397 25.617 -19.699 1.00 29.41 C ANISOU 2503 CB LEU B 161 2831 4710 3633 -303 129 322 C ATOM 2504 CG LEU A 161 10.450 25.169 -18.241 1.00 28.95 C ANISOU 2504 CG LEU B 161 2839 4590 3568 -398 223 376 C ATOM 2505 CD1 LEU A 161 10.259 26.375 -17.335 1.00 28.46 C ANISOU 2505 CD1 LEU B 161 2595 4469 3750 -750 400 381 C ATOM 2506 CD2 LEU A 161 9.383 24.113 -17.984 1.00 29.10 C ANISOU 2506 CD2 LEU B 161 2920 4368 3765 -414 357 325 C ATOM 2507 N SER A 162 11.223 25.644 -22.912 1.00 29.73 N ANISOU 2507 N SER B 162 2909 4792 3595 -214 -55 303 N ATOM 2508 CA SER A 162 10.895 26.232 -24.200 1.00 30.72 C ANISOU 2508 CA SER B 162 3091 4926 3651 -217 -149 213 C ATOM 2509 C SER A 162 11.116 25.288 -25.400 1.00 31.69 C ANISOU 2509 C SER B 162 3249 5024 3766 -143 -246 194 C ATOM 2510 O SER A 162 12.259 24.944 -25.746 1.00 31.33 O ANISOU 2510 O SER B 162 3159 5042 3702 -174 -220 213 O ATOM 2511 CB SER A 162 11.704 27.526 -24.380 1.00 30.64 C ANISOU 2511 CB SER B 162 3044 4939 3657 -257 -197 287 C ATOM 2512 OG SER A 162 11.676 27.984 -25.721 1.00 30.76 O ANISOU 2512 OG SER B 162 2987 5015 3683 -361 77 157 O ATOM 2513 N GLN A 163 10.016 24.907 -26.058 1.00 32.34 N ANISOU 2513 N GLN B 163 3389 5057 3840 -148 -264 108 N ATOM 2514 CA GLN A 163 10.091 24.206 -27.343 1.00 33.37 C ANISOU 2514 CA GLN B 163 3626 5143 3910 -113 -361 96 C ATOM 2515 C GLN A 163 10.998 24.937 -28.357 1.00 33.61 C ANISOU 2515 C GLN B 163 3699 5137 3931 -67 -354 105 C ATOM 2516 O GLN A 163 11.694 24.314 -29.145 1.00 33.86 O ANISOU 2516 O GLN B 163 3657 5248 3960 -28 -366 102 O ATOM 2517 CB GLN A 163 8.686 23.999 -27.925 1.00 33.69 C ANISOU 2517 CB GLN B 163 3666 5190 3944 -135 -318 21 C ATOM 2518 CG GLN A 163 8.632 22.958 -29.048 1.00 35.89 C ANISOU 2518 CG GLN B 163 4062 5491 4080 -168 -369 -28 C ATOM 2519 CD GLN A 163 8.988 21.557 -28.581 1.00 37.77 C ANISOU 2519 CD GLN B 163 4409 5794 4148 -257 -334 -120 C ATOM 2520 OE1 GLN A 163 8.429 21.053 -27.606 1.00 40.92 O ANISOU 2520 OE1 GLN B 163 4942 6233 4373 -392 -272 -177 O ATOM 2521 NE2 GLN A 163 9.919 20.918 -29.281 1.00 40.08 N ANISOU 2521 NE2 GLN B 163 4813 5962 4454 -147 -507 -212 N ATOM 2522 N GLU A 164 10.981 26.263 -28.307 1.00 34.06 N ANISOU 2522 N GLU B 164 3804 5114 4023 -147 -352 186 N ATOM 2523 CA GLU A 164 11.732 27.113 -29.229 1.00 34.50 C ANISOU 2523 CA GLU B 164 4005 5128 3974 -104 -379 211 C ATOM 2524 C GLU A 164 13.234 26.825 -29.154 1.00 33.55 C ANISOU 2524 C GLU B 164 3828 5043 3876 -118 -449 221 C ATOM 2525 O GLU A 164 13.910 26.728 -30.181 1.00 33.57 O ANISOU 2525 O GLU B 164 3969 5060 3726 -41 -454 278 O ATOM 2526 CB GLU A 164 11.468 28.584 -28.898 1.00 34.60 C ANISOU 2526 CB GLU B 164 4045 5065 4034 -139 -361 287 C ATOM 2527 CG GLU A 164 11.136 29.405 -30.101 1.00 37.97 C ANISOU 2527 CG GLU B 164 4735 5278 4410 -269 -209 294 C ATOM 2528 CD GLU A 164 11.651 30.832 -30.000 1.00 41.16 C ANISOU 2528 CD GLU B 164 5481 5477 4682 -429 2 251 C ATOM 2529 OE1 GLU A 164 11.527 31.456 -28.915 1.00 43.30 O ANISOU 2529 OE1 GLU B 164 5831 5742 4876 -485 208 300 O ATOM 2530 OE2 GLU A 164 12.182 31.324 -31.019 1.00 42.41 O ANISOU 2530 OE2 GLU B 164 5801 5481 4830 -366 154 379 O ATOM 2531 N HIS A 165 13.739 26.670 -27.931 1.00 33.16 N ANISOU 2531 N HIS B 165 3769 5019 3809 -124 -488 233 N ATOM 2532 CA HIS A 165 15.166 26.405 -27.675 1.00 32.84 C ANISOU 2532 CA HIS B 165 3641 5028 3808 -99 -573 173 C ATOM 2533 C HIS A 165 15.575 25.019 -28.184 1.00 32.78 C ANISOU 2533 C HIS B 165 3608 5061 3786 -114 -612 131 C ATOM 2534 O HIS A 165 16.603 24.867 -28.853 1.00 32.26 O ANISOU 2534 O HIS B 165 3473 5105 3678 -157 -624 99 O ATOM 2535 CB HIS A 165 15.457 26.501 -26.172 1.00 32.68 C ANISOU 2535 CB HIS B 165 3649 4974 3792 -148 -590 151 C ATOM 2536 CG HIS A 165 15.269 27.869 -25.590 1.00 33.02 C ANISOU 2536 CG HIS B 165 3601 5039 3905 -54 -595 130 C ATOM 2537 ND1 HIS A 165 15.529 28.149 -24.266 1.00 33.31 N ANISOU 2537 ND1 HIS B 165 3502 5089 4063 -134 -406 -7 N ATOM 2538 CD2 HIS A 165 14.881 29.039 -26.149 1.00 34.73 C ANISOU 2538 CD2 HIS B 165 3862 5151 4182 -13 -529 48 C ATOM 2539 CE1 HIS A 165 15.291 29.425 -24.029 1.00 32.99 C ANISOU 2539 CE1 HIS B 165 3469 5055 4008 -206 -575 -72 C ATOM 2540 NE2 HIS A 165 14.905 29.991 -25.156 1.00 33.42 N ANISOU 2540 NE2 HIS B 165 3652 5135 3910 -130 -706 -20 N ATOM 2541 N ILE A 166 14.753 24.011 -27.875 1.00 32.94 N ANISOU 2541 N ILE B 166 3630 5073 3810 -79 -611 148 N ATOM 2542 CA ILE A 166 15.015 22.651 -28.352 1.00 33.62 C ANISOU 2542 CA ILE B 166 3642 5189 3942 -81 -617 136 C ATOM 2543 C ILE A 166 14.984 22.540 -29.886 1.00 34.04 C ANISOU 2543 C ILE B 166 3655 5251 4027 -63 -617 108 C ATOM 2544 O ILE A 166 15.846 21.869 -30.472 1.00 34.26 O ANISOU 2544 O ILE B 166 3650 5271 4095 -135 -608 27 O ATOM 2545 CB ILE A 166 14.090 21.598 -27.679 1.00 33.88 C ANISOU 2545 CB ILE B 166 3744 5167 3959 -105 -621 147 C ATOM 2546 CG1 ILE A 166 14.317 21.564 -26.148 1.00 34.69 C ANISOU 2546 CG1 ILE B 166 3809 5228 4144 -87 -611 273 C ATOM 2547 CG2 ILE A 166 14.282 20.229 -28.304 1.00 33.17 C ANISOU 2547 CG2 ILE B 166 3546 5066 3988 -45 -668 97 C ATOM 2548 CD1 ILE A 166 15.782 21.557 -25.654 1.00 35.13 C ANISOU 2548 CD1 ILE B 166 3934 5107 4307 -46 -760 381 C ATOM 2549 N ASP A 167 14.007 23.196 -30.523 1.00 34.36 N ANISOU 2549 N ASP B 167 3637 5343 4075 -8 -639 139 N ATOM 2550 CA ASP A 167 13.923 23.235 -31.988 1.00 34.44 C ANISOU 2550 CA ASP B 167 3605 5406 4074 30 -574 152 C ATOM 2551 C ASP A 167 15.199 23.779 -32.623 1.00 34.31 C ANISOU 2551 C ASP B 167 3622 5347 4066 35 -536 124 C ATOM 2552 O ASP A 167 15.691 23.207 -33.592 1.00 34.47 O ANISOU 2552 O ASP B 167 3632 5418 4046 39 -532 168 O ATOM 2553 CB ASP A 167 12.730 24.080 -32.457 1.00 35.27 C ANISOU 2553 CB ASP B 167 3695 5552 4154 25 -624 167 C ATOM 2554 CG ASP A 167 11.380 23.361 -32.294 1.00 35.87 C ANISOU 2554 CG ASP B 167 3644 5717 4265 42 -613 239 C ATOM 2555 OD1 ASP A 167 11.350 22.155 -31.981 1.00 37.11 O ANISOU 2555 OD1 ASP B 167 3918 5669 4513 116 -815 256 O ATOM 2556 OD2 ASP A 167 10.342 24.022 -32.491 1.00 38.86 O ANISOU 2556 OD2 ASP B 167 3955 6444 4365 91 -731 369 O ATOM 2557 N TYR A 168 15.731 24.873 -32.080 1.00 34.10 N ANISOU 2557 N TYR B 168 3598 5281 4075 6 -490 120 N ATOM 2558 CA TYR A 168 16.963 25.455 -32.617 1.00 34.03 C ANISOU 2558 CA TYR B 168 3641 5164 4124 -11 -487 96 C ATOM 2559 C TYR A 168 18.149 24.485 -32.494 1.00 34.67 C ANISOU 2559 C TYR B 168 3730 5144 4297 -31 -469 77 C ATOM 2560 O TYR A 168 18.981 24.379 -33.403 1.00 34.49 O ANISOU 2560 O TYR B 168 3642 5049 4410 -91 -466 69 O ATOM 2561 CB TYR A 168 17.284 26.812 -31.985 1.00 33.44 C ANISOU 2561 CB TYR B 168 3624 5154 3926 -56 -504 52 C ATOM 2562 CG TYR A 168 18.589 27.374 -32.490 1.00 32.77 C ANISOU 2562 CG TYR B 168 3604 5126 3721 -111 -506 105 C ATOM 2563 CD1 TYR A 168 18.654 28.073 -33.690 1.00 32.70 C ANISOU 2563 CD1 TYR B 168 3521 5175 3726 -116 -569 117 C ATOM 2564 CD2 TYR A 168 19.782 27.159 -31.783 1.00 32.99 C ANISOU 2564 CD2 TYR B 168 3766 5135 3631 -167 -592 49 C ATOM 2565 CE1 TYR A 168 19.876 28.564 -34.167 1.00 31.65 C ANISOU 2565 CE1 TYR B 168 3486 4988 3548 -301 -440 184 C ATOM 2566 CE2 TYR A 168 20.994 27.642 -32.247 1.00 31.21 C ANISOU 2566 CE2 TYR B 168 3475 4924 3457 -234 -504 134 C ATOM 2567 CZ TYR A 168 21.035 28.345 -33.436 1.00 32.36 C ANISOU 2567 CZ TYR B 168 3613 5118 3562 -283 -494 75 C ATOM 2568 OH TYR A 168 22.254 28.822 -33.891 1.00 33.86 O ANISOU 2568 OH TYR B 168 3969 5382 3512 -251 -536 89 O ATOM 2569 N PHE A 169 18.206 23.762 -31.383 1.00 35.33 N ANISOU 2569 N PHE B 169 3815 5142 4467 -4 -461 57 N ATOM 2570 CA PHE A 169 19.225 22.743 -31.232 1.00 36.53 C ANISOU 2570 CA PHE B 169 4002 5158 4716 15 -440 54 C ATOM 2571 C PHE A 169 19.050 21.565 -32.205 1.00 37.70 C ANISOU 2571 C PHE B 169 4151 5289 4884 35 -447 -21 C ATOM 2572 O PHE A 169 20.032 21.062 -32.748 1.00 37.74 O ANISOU 2572 O PHE B 169 4044 5323 4970 -23 -505 -61 O ATOM 2573 CB PHE A 169 19.316 22.235 -29.798 1.00 36.01 C ANISOU 2573 CB PHE B 169 3905 5072 4706 26 -407 111 C ATOM 2574 CG PHE A 169 20.397 21.227 -29.613 1.00 35.94 C ANISOU 2574 CG PHE B 169 3965 4846 4844 16 -365 273 C ATOM 2575 CD1 PHE A 169 21.729 21.631 -29.512 1.00 34.53 C ANISOU 2575 CD1 PHE B 169 3725 4615 4780 -15 -395 434 C ATOM 2576 CD2 PHE A 169 20.106 19.870 -29.622 1.00 36.80 C ANISOU 2576 CD2 PHE B 169 4045 4931 5005 -19 -197 541 C ATOM 2577 CE1 PHE A 169 22.733 20.709 -29.384 1.00 33.39 C ANISOU 2577 CE1 PHE B 169 3516 4465 4706 42 -373 474 C ATOM 2578 CE2 PHE A 169 21.116 18.932 -29.479 1.00 34.92 C ANISOU 2578 CE2 PHE B 169 3657 4605 5003 188 -266 670 C ATOM 2579 CZ PHE A 169 22.424 19.353 -29.361 1.00 35.24 C ANISOU 2579 CZ PHE B 169 3726 4730 4931 147 -405 490 C ATOM 2580 N ASP A 170 17.809 21.121 -32.407 1.00 39.55 N ANISOU 2580 N ASP B 170 4403 5514 5109 97 -496 -75 N ATOM 2581 CA ASP A 170 17.520 19.973 -33.287 1.00 41.53 C ANISOU 2581 CA ASP B 170 4657 5739 5383 110 -441 -168 C ATOM 2582 C ASP A 170 17.884 20.239 -34.748 1.00 42.46 C ANISOU 2582 C ASP B 170 4766 5861 5507 121 -384 -181 C ATOM 2583 O ASP A 170 18.266 19.321 -35.476 1.00 43.07 O ANISOU 2583 O ASP B 170 4815 5878 5672 95 -348 -216 O ATOM 2584 CB ASP A 170 16.043 19.559 -33.196 1.00 41.81 C ANISOU 2584 CB ASP B 170 4677 5790 5418 113 -440 -198 C ATOM 2585 CG ASP A 170 15.747 18.697 -31.982 1.00 43.10 C ANISOU 2585 CG ASP B 170 4876 5840 5657 150 -530 -244 C ATOM 2586 OD1 ASP A 170 16.696 18.098 -31.424 1.00 45.71 O ANISOU 2586 OD1 ASP B 170 5346 6060 5960 162 -534 -443 O ATOM 2587 OD2 ASP A 170 14.560 18.611 -31.583 1.00 45.80 O ANISOU 2587 OD2 ASP B 170 5390 5999 6011 228 -636 -424 O ATOM 2588 N ALA A 171 17.758 21.492 -35.174 1.00 43.19 N ANISOU 2588 N ALA B 171 4803 5990 5617 128 -406 -173 N ATOM 2589 CA ALA A 171 18.143 21.881 -36.521 1.00 44.16 C ANISOU 2589 CA ALA B 171 4912 6166 5701 111 -370 -183 C ATOM 2590 C ALA A 171 19.670 21.891 -36.618 1.00 45.05 C ANISOU 2590 C ALA B 171 5059 6288 5767 90 -390 -217 C ATOM 2591 O ALA A 171 20.250 21.673 -37.689 1.00 44.69 O ANISOU 2591 O ALA B 171 4996 6311 5672 75 -340 -222 O ATOM 2592 CB ALA A 171 17.573 23.265 -36.849 1.00 44.36 C ANISOU 2592 CB ALA B 171 4911 6185 5759 127 -390 -164 C ATOM 2593 N THR A 172 20.293 22.101 -35.461 1.00 46.05 N ANISOU 2593 N THR B 172 5210 6446 5840 48 -385 -258 N ATOM 2594 CA THR A 172 21.732 22.277 -35.307 1.00 46.92 C ANISOU 2594 CA THR B 172 5369 6529 5928 27 -389 -270 C ATOM 2595 C THR A 172 22.432 20.916 -35.398 1.00 47.65 C ANISOU 2595 C THR B 172 5491 6608 6006 55 -403 -292 C ATOM 2596 O THR A 172 23.601 20.837 -35.797 1.00 48.39 O ANISOU 2596 O THR B 172 5616 6699 6071 26 -461 -283 O ATOM 2597 CB THR A 172 22.006 23.011 -33.944 1.00 46.89 C ANISOU 2597 CB THR B 172 5346 6544 5924 -19 -382 -268 C ATOM 2598 OG1 THR A 172 22.777 24.200 -34.146 1.00 47.58 O ANISOU 2598 OG1 THR B 172 5465 6649 5962 -94 -362 -230 O ATOM 2599 CG2 THR A 172 22.647 22.106 -32.894 1.00 45.83 C ANISOU 2599 CG2 THR B 172 5169 6396 5848 -43 -349 -261 C ATOM 2600 N CYS A 173 21.697 19.856 -35.048 1.00 48.38 N ANISOU 2600 N CYS B 173 5640 6634 6108 62 -422 -330 N ATOM 2601 CA CYS A 173 22.178 18.473 -35.109 1.00 49.28 C ANISOU 2601 CA CYS B 173 5790 6677 6254 97 -418 -324 C ATOM 2602 C CYS A 173 22.180 17.903 -36.527 1.00 49.01 C ANISOU 2602 C CYS B 173 5792 6634 6192 80 -435 -385 C ATOM 2603 O CYS A 173 21.225 18.088 -37.280 1.00 49.01 O ANISOU 2603 O CYS B 173 5772 6617 6232 77 -376 -441 O ATOM 2604 CB CYS A 173 21.341 17.575 -34.194 1.00 49.47 C ANISOU 2604 CB CYS B 173 5853 6690 6253 100 -445 -354 C ATOM 2605 SG CYS A 173 21.657 17.788 -32.421 1.00 53.24 S ANISOU 2605 SG CYS B 173 6330 6966 6930 182 -442 -196 S TER 2606 CYS B 173 HETATM 2607 O HOH A 175 41.072 15.387 -7.638 1.00 13.66 O HETATM 2608 O HOH A 176 51.275 8.850 -3.074 1.00 13.04 O HETATM 2609 O HOH A 177 45.453 25.339 14.848 1.00 25.87 O HETATM 2610 O HOH A 178 41.391 6.754 17.058 1.00 23.42 O HETATM 2611 O HOH A 179 43.513 6.902 -5.295 1.00 19.32 O HETATM 2612 O HOH A 180 56.079 -0.804 -6.333 1.00 18.56 O HETATM 2613 O HOH A 181 51.548 -13.576 -1.419 1.00 20.47 O HETATM 2614 O HOH A 182 58.315 9.756 -4.056 1.00 20.27 O HETATM 2615 O HOH A 183 51.030 9.039 1.913 1.00 20.99 O HETATM 2616 O HOH A 184 35.895 20.251 -9.214 1.00 21.36 O HETATM 2617 O HOH A 185 46.397 12.123 15.321 1.00 18.18 O HETATM 2618 O HOH A 186 46.807 22.661 15.212 1.00 26.99 O HETATM 2619 O HOH A 187 25.354 13.310 -4.021 1.00 19.54 O HETATM 2620 O HOH A 188 53.350 1.856 7.341 1.00 20.41 O HETATM 2621 O HOH A 189 50.743 16.136 2.494 1.00 23.28 O HETATM 2622 O HOH A 190 29.145 18.702 3.530 1.00 20.72 O HETATM 2623 O HOH A 191 31.516 7.002 10.125 1.00 21.30 O HETATM 2624 O HOH A 192 37.305 18.186 -7.434 1.00 19.16 O HETATM 2625 O HOH A 193 39.292 -6.731 2.383 1.00 22.00 O HETATM 2626 O HOH A 194 41.287 16.273 -10.481 1.00 26.12 O HETATM 2627 O HOH A 195 59.658 6.226 2.270 1.00 18.46 O HETATM 2628 O HOH A 196 56.941 12.057 4.094 1.00 20.69 O HETATM 2629 O HOH A 197 30.260 1.277 -5.720 1.00 27.38 O HETATM 2630 O HOH A 198 34.828 22.850 2.140 1.00 28.02 O HETATM 2631 O HOH A 199 49.266 0.346 11.656 1.00 22.37 O HETATM 2632 O HOH A 200 40.259 12.134 -6.963 1.00 24.16 O HETATM 2633 O HOH A 201 45.182 16.262 15.504 1.00 22.98 O HETATM 2634 O HOH A 202 39.118 10.590 -13.680 1.00 27.34 O HETATM 2635 O HOH A 203 40.139 -9.966 0.347 1.00 28.35 O HETATM 2636 O HOH A 204 33.007 18.315 10.352 1.00 27.49 O HETATM 2637 O HOH A 205 44.108 9.246 -8.532 1.00 25.29 O HETATM 2638 O HOH A 206 37.403 -9.076 2.290 1.00 20.50 O HETATM 2639 O HOH A 207 31.414 -5.076 -0.588 1.00 25.73 O HETATM 2640 O HOH A 208 44.736 -8.921 -0.503 1.00 27.38 O HETATM 2641 O HOH A 209 31.177 17.517 -3.742 1.00 25.11 O HETATM 2642 O HOH A 210 44.165 2.469 13.317 1.00 31.17 O HETATM 2643 O HOH A 211 57.020 7.317 3.287 1.00 22.31 O HETATM 2644 O HOH A 212 26.277 3.852 4.679 1.00 30.79 O HETATM 2645 O HOH A 213 45.730 17.907 -6.990 1.00 24.25 O HETATM 2646 O HOH A 214 47.760 8.191 -3.049 1.00 29.08 O HETATM 2647 O HOH A 215 57.458 14.362 15.406 1.00 31.80 O HETATM 2648 O HOH A 216 26.086 5.467 7.120 1.00 32.57 O HETATM 2649 O HOH A 217 28.970 -5.467 12.743 1.00 31.23 O HETATM 2650 O HOH A 218 35.446 -4.908 13.005 1.00 29.79 O HETATM 2651 O HOH A 219 35.706 18.310 11.395 1.00 33.74 O HETATM 2652 O HOH A 220 30.336 22.368 5.715 1.00 23.62 O HETATM 2653 O HOH A 221 61.740 -6.533 1.498 1.00 39.35 O HETATM 2654 O HOH A 222 49.518 22.982 6.068 1.00 33.87 O HETATM 2655 O HOH A 223 57.159 11.311 12.855 1.00 36.83 O HETATM 2656 O HOH A 224 29.349 21.427 3.804 1.00 26.17 O HETATM 2657 O HOH A 225 46.392 14.572 17.211 1.00 31.98 O HETATM 2658 O HOH A 226 51.825 -4.751 8.590 1.00 26.87 O HETATM 2659 O HOH A 227 34.906 -8.320 -2.388 1.00 29.99 O HETATM 2660 O HOH A 228 59.385 3.227 4.477 1.00 34.81 O HETATM 2661 O HOH A 229 51.054 2.482 -9.719 1.00 35.32 O HETATM 2662 O HOH A 230 52.935 10.295 13.748 1.00 31.67 O HETATM 2663 O HOH A 232 50.824 12.291 -6.077 1.00 27.48 O HETATM 2664 O HOH A 233 46.823 9.462 -5.064 1.00 27.63 O HETATM 2665 O HOH A 234 49.096 13.369 -2.304 1.00 29.84 O HETATM 2666 O HOH A 235 33.397 2.935 -9.919 1.00 26.40 O HETATM 2667 O HOH A 236 56.481 0.254 -9.364 1.00 36.27 O HETATM 2668 O HOH A 237 56.738 -7.180 4.071 1.00 30.28 O HETATM 2669 O HOH A 238 58.512 -0.931 -4.568 1.00 29.03 O HETATM 2670 O HOH A 239 50.380 5.061 9.748 1.00 24.62 O HETATM 2671 O HOH A 240 32.258 24.027 5.469 1.00 32.83 O HETATM 2672 O HOH A 241 50.690 4.912 12.422 1.00 41.91 O HETATM 2673 O HOH A 242 26.095 14.757 7.532 1.00 37.89 O HETATM 2674 O HOH A 243 33.441 -1.116 13.024 1.00 30.91 O HETATM 2675 O HOH A 244 57.274 4.101 -9.757 1.00 32.61 O HETATM 2676 O HOH A 245 25.916 16.026 5.109 1.00 33.42 O HETATM 2677 O HOH A 246 34.823 15.095 16.632 1.00 32.53 O HETATM 2678 O HOH A 247 23.765 4.832 1.974 1.00 30.54 O HETATM 2679 O HOH A 249 56.612 3.618 5.705 1.00 26.54 O HETATM 2680 O HOH A 250 49.732 -4.176 10.283 1.00 30.51 O HETATM 2681 O HOH A 251 44.160 9.609 -4.985 1.00 23.30 O HETATM 2682 O HOH A 252 26.601 17.956 3.366 1.00 26.34 O HETATM 2683 O HOH A 253 42.870 11.043 -6.837 1.00 36.38 O HETATM 2684 O HOH A 254 63.150 1.650 3.370 1.00 37.47 O HETATM 2685 O HOH A 255 47.982 11.736 -5.494 1.00 32.01 O HETATM 2686 O HOH A 256 40.804 7.084 -15.944 1.00 33.10 O HETATM 2687 O HOH A 257 57.646 10.917 10.361 1.00 39.29 O HETATM 2688 O HOH A 258 52.188 27.813 14.954 1.00 41.08 O HETATM 2689 O HOH A 259 55.022 -4.130 -9.119 1.00 30.53 O HETATM 2690 O HOH A 260 27.744 1.144 15.329 1.00 36.76 O HETATM 2691 O HOH A 261 45.966 21.184 17.368 1.00 28.03 O HETATM 2692 O HOH A 262 35.898 18.982 -11.575 1.00 33.64 O HETATM 2693 O HOH A 263 26.444 13.220 4.694 1.00 32.98 O HETATM 2694 O HOH A 264 50.304 7.848 -0.593 1.00 30.35 O HETATM 2695 O HOH A 265 47.384 7.503 -7.424 1.00 28.43 O HETATM 2696 O HOH A 266 21.002 12.131 1.382 1.00 35.90 O HETATM 2697 O HOH A 267 50.007 -6.188 -1.273 1.00 31.93 O HETATM 2698 O HOH A 268 33.024 5.531 -10.607 1.00 31.94 O HETATM 2699 O HOH A 269 25.056 -3.061 12.393 1.00 33.61 O HETATM 2700 O HOH A 270 45.387 28.725 6.158 1.00 35.78 O HETATM 2701 O HOH A 271 41.865 -10.388 -3.964 1.00 33.83 O HETATM 2702 O HOH A 272 24.815 13.937 13.603 1.00 37.87 O HETATM 2703 O HOH A 273 54.363 14.309 -0.960 1.00 29.30 O HETATM 2704 O HOH A 274 36.141 -9.441 4.938 1.00 36.11 O HETATM 2705 O HOH A 275 49.185 22.556 3.206 1.00 37.25 O HETATM 2706 O HOH A 276 47.736 4.158 14.057 1.00 39.19 O HETATM 2707 O HOH A 277 36.459 6.304 -16.254 1.00 40.12 O HETATM 2708 O HOH A 278 44.989 6.776 -7.474 1.00 31.00 O HETATM 2709 O HOH A 279 63.122 3.401 -1.439 1.00 47.45 O HETATM 2710 O HOH A 280 23.354 11.946 3.283 1.00 41.87 O HETATM 2711 O HOH A 281 42.029 26.489 11.763 1.00 35.47 O HETATM 2712 O HOH A 282 29.221 -6.547 3.099 1.00 33.14 O HETATM 2713 O HOH A 283 56.465 -3.448 -7.105 1.00 35.84 O HETATM 2714 O HOH A 284 43.232 25.493 1.488 1.00 36.96 O HETATM 2715 O HOH A 285 46.806 24.202 -3.026 1.00 37.85 O HETATM 2716 O HOH A 286 49.623 4.890 -10.006 1.00 34.83 O HETATM 2717 O HOH A 287 46.982 12.385 -8.095 1.00 33.29 O HETATM 2718 O HOH A 288 55.559 -1.658 -11.433 1.00 49.72 O HETATM 2719 O HOH A 289 44.198 13.680 -7.065 1.00 33.87 O HETATM 2720 O HOH A 290 48.359 21.015 19.219 1.00 30.25 O HETATM 2721 O HOH A 291 43.098 25.027 13.960 1.00 32.59 O HETATM 2722 O HOH A 292 48.498 8.714 -9.486 1.00 38.01 O HETATM 2723 O HOH A 293 33.029 -9.980 4.809 1.00 42.00 O HETATM 2724 O HOH A 294 52.364 12.976 -0.792 1.00 34.54 O HETATM 2725 O HOH A 295 40.877 24.307 15.497 1.00 26.56 O HETATM 2726 O HOH B 175 34.235 22.046 -7.547 1.00 14.95 O HETATM 2727 O HOH B 176 11.350 23.262 -13.904 1.00 18.90 O HETATM 2728 O HOH B 177 27.256 35.430 -10.757 1.00 18.21 O HETATM 2729 O HOH B 178 34.998 21.606 -4.674 1.00 19.66 O HETATM 2730 O HOH B 179 30.207 22.871 1.680 1.00 18.50 O HETATM 2731 O HOH B 180 17.514 11.736 -1.942 1.00 21.87 O HETATM 2732 O HOH B 181 28.459 9.721 -15.955 1.00 20.21 O HETATM 2733 O HOH B 182 29.218 20.000 -30.423 1.00 24.39 O HETATM 2734 O HOH B 183 32.592 27.986 -15.121 1.00 24.84 O HETATM 2735 O HOH B 184 32.732 20.745 -3.628 1.00 20.56 O HETATM 2736 O HOH B 185 30.181 18.114 -32.437 1.00 26.14 O HETATM 2737 O HOH B 186 33.053 13.312 -29.600 1.00 23.76 O HETATM 2738 O HOH B 187 24.843 20.184 3.542 1.00 22.23 O HETATM 2739 O HOH B 188 25.214 16.257 -33.804 1.00 30.05 O HETATM 2740 O HOH B 189 22.645 30.021 -8.257 1.00 19.38 O HETATM 2741 O HOH B 190 36.323 26.844 -18.974 1.00 24.56 O HETATM 2742 O HOH B 191 27.107 31.724 1.337 1.00 22.78 O HETATM 2743 O HOH B 192 29.335 11.036 -7.514 1.00 19.85 O HETATM 2744 O HOH B 193 15.803 27.682 -3.658 1.00 28.45 O HETATM 2745 O HOH B 194 28.536 34.423 1.015 1.00 25.78 O HETATM 2746 O HOH B 195 20.262 29.014 -2.118 1.00 23.85 O HETATM 2747 O HOH B 196 17.706 14.953 -1.573 1.00 23.36 O HETATM 2748 O HOH B 197 11.969 27.511 -11.025 1.00 23.65 O HETATM 2749 O HOH B 198 13.372 21.307 -0.534 1.00 29.13 O HETATM 2750 O HOH B 199 29.049 13.385 -32.256 1.00 30.81 O HETATM 2751 O HOH B 200 25.314 11.206 -5.476 1.00 32.41 O HETATM 2752 O HOH B 201 8.578 27.607 -26.932 1.00 35.86 O HETATM 2753 O HOH B 202 35.253 24.975 -7.347 1.00 37.55 O HETATM 2754 O HOH B 203 19.069 29.783 -12.492 1.00 25.16 O HETATM 2755 O HOH B 204 31.610 27.050 5.683 1.00 24.38 O HETATM 2756 O HOH B 205 28.231 7.077 -16.094 1.00 32.55 O HETATM 2757 O HOH B 206 25.106 35.201 -12.644 1.00 25.03 O HETATM 2758 O HOH B 207 38.112 28.771 -4.286 1.00 28.77 O HETATM 2759 O HOH B 208 13.688 26.471 -19.266 1.00 31.38 O HETATM 2760 O HOH B 209 9.520 19.694 -11.687 1.00 31.67 O HETATM 2761 O HOH B 210 13.164 22.490 -16.907 1.00 33.13 O HETATM 2762 O HOH B 211 30.265 9.169 -9.514 1.00 24.55 O HETATM 2763 O HOH B 212 10.392 24.339 -7.372 1.00 33.11 O HETATM 2764 O HOH B 213 11.487 30.335 -10.895 1.00 24.95 O HETATM 2765 O HOH B 214 36.252 30.945 -24.455 1.00 29.04 O HETATM 2766 O HOH B 215 32.539 32.016 -18.600 1.00 28.31 O HETATM 2767 O HOH B 216 26.880 21.966 4.141 1.00 27.87 O HETATM 2768 O HOH B 217 15.790 23.094 -0.644 1.00 28.43 O HETATM 2769 O HOH B 218 26.315 11.619 -31.687 1.00 25.22 O HETATM 2770 O HOH B 219 17.302 30.058 -15.119 1.00 29.14 O HETATM 2771 O HOH B 220 34.795 11.706 -21.271 1.00 30.95 O HETATM 2772 O HOH B 221 17.744 28.503 -1.764 1.00 33.61 O HETATM 2773 O HOH B 222 15.149 25.320 -2.248 1.00 29.79 O HETATM 2774 O HOH B 223 35.730 21.215 -16.944 1.00 30.76 O HETATM 2775 O HOH B 224 18.690 32.378 -8.176 1.00 33.83 O HETATM 2776 O HOH B 225 31.954 33.001 -14.390 1.00 36.44 O HETATM 2777 O HOH B 226 16.496 8.876 -7.941 1.00 38.17 O HETATM 2778 O HOH B 227 39.584 28.726 -0.308 1.00 44.16 O HETATM 2779 O HOH B 228 11.894 21.380 -8.927 1.00 32.09 O HETATM 2780 O HOH B 229 18.809 17.684 0.820 1.00 25.81 O HETATM 2781 O HOH B 230 16.468 16.626 1.602 1.00 30.62 O HETATM 2782 O HOH B 231 39.792 20.311 -4.234 1.00 25.56 O HETATM 2783 O HOH B 232 17.245 25.421 -20.364 1.00 28.60 O HETATM 2784 O HOH B 233 36.569 32.941 -4.398 1.00 31.39 O HETATM 2785 O HOH B 234 23.716 13.042 -31.166 1.00 27.45 O HETATM 2786 O HOH B 235 18.181 18.494 -37.858 1.00 39.98 O HETATM 2787 O HOH B 236 28.947 39.836 -27.060 1.00 39.08 O HETATM 2788 O HOH B 237 37.404 33.234 0.727 1.00 36.60 O HETATM 2789 O HOH B 238 24.675 30.859 -14.918 1.00 30.27 O HETATM 2790 O HOH B 239 36.180 11.201 -16.929 1.00 39.58 O HETATM 2791 O HOH B 240 26.971 5.271 -18.648 1.00 32.73 O HETATM 2792 O HOH B 241 10.823 16.815 -25.250 1.00 29.82 O HETATM 2793 O HOH B 242 12.880 7.504 -14.834 1.00 36.51 O HETATM 2794 O HOH B 243 15.490 32.689 -14.812 1.00 35.86 O HETATM 2795 O HOH B 244 4.904 18.824 -16.057 1.00 40.62 O HETATM 2796 O HOH B 245 36.027 14.137 -23.109 1.00 32.39 O HETATM 2797 O HOH B 246 13.625 35.992 -19.112 1.00 47.22 O HETATM 2798 O HOH B 247 11.773 9.046 -12.409 1.00 39.09 O HETATM 2799 O HOH B 248 37.242 19.717 -4.826 1.00 25.73 O HETATM 2800 O HOH B 249 35.376 11.478 -28.932 1.00 30.98 O HETATM 2801 O HOH B 250 21.972 17.017 7.179 1.00 38.97 O HETATM 2802 O HOH B 251 17.643 6.090 -9.017 1.00 38.89 O HETATM 2803 O HOH B 252 26.446 31.709 -33.993 1.00 41.18 O HETATM 2804 O HOH B 253 13.814 27.849 -32.703 1.00 35.03 O HETATM 2805 O HOH B 254 10.059 12.318 -18.497 1.00 32.92 O HETATM 2806 O HOH B 255 35.272 33.186 -8.194 1.00 35.04 O HETATM 2807 O HOH B 256 13.978 21.654 -35.335 1.00 44.99 O HETATM 2808 O HOH B 257 20.530 20.645 5.755 1.00 38.76 O MASTER 348 0 0 12 12 0 0 6 2806 2 0 28 END