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*** HYDROLASE 19-APR-17 5XH3 ***elNémo ID: 230128025737104784Job options:ID = 230128025737104784 JOBID = HYDROLASE 19-APR-17 5XH3 USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER HYDROLASE 19-APR-17 5XH3 TITLE CRYSTAL STRUCTURE OF A NOVEL PET HYDROLASE R103G/S131A MUTANT IN TITLE 2 COMPLEX WITH HEMT FROM IDEONELLA SAKAIENSIS 201-F6 COMPND MOL_ID: 1; COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: PETASE; COMPND 5 EC: 3.1.1.101; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS (STRAIN 201-F6); SOURCE 3 ORGANISM_TAXID: 1547922; SOURCE 4 STRAIN: 201-F6; SOURCE 5 GENE: ISF6_4831; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET32A KEYWDS POLY(ETHYLENE TEREPHTHALATE) HYDROLASE, SUBSTRATE BINDING, INHIBITOR, KEYWDS 2 HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR X.HAN,W.D.LIU,Y.Y.ZHENG,C.C.CHEN,R.T.GUO REVDAT 2 27-DEC-17 5XH3 1 JRNL REVDAT 1 20-DEC-17 5XH3 0 JRNL AUTH X.HAN,W.LIU,J.W.HUANG,J.MA,Y.ZHENG,T.P.KO,L.XU,Y.S.CHENG, JRNL AUTH 2 C.C.CHEN,R.T.GUO JRNL TITL STRUCTURAL INSIGHT INTO CATALYTIC MECHANISM OF PET HYDROLASE JRNL REF NAT COMMUN V. 8 2106 2017 JRNL REFN ESSN 2041-1723 JRNL PMID 29235460 JRNL DOI 10.1038/S41467-017-02255-Z REMARK 2 REMARK 2 RESOLUTION. 1.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0158 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 51930 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) : 0.119 REMARK 3 R VALUE (WORKING SET) : 0.118 REMARK 3 FREE R VALUE : 0.146 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 2691 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) : 1.30 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.33 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3707 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.42 REMARK 3 BIN R VALUE (WORKING SET) : 0.1930 REMARK 3 BIN FREE R VALUE SET COUNT : 187 REMARK 3 BIN FREE R VALUE : 0.2190 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1911 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 32 REMARK 3 SOLVENT ATOMS : 244 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.68 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.51000 REMARK 3 B22 (A**2) : 0.25000 REMARK 3 B33 (A**2) : 0.26000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.041 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.040 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.023 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.208 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.978 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.973 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2013 ; 0.010 ; 0.020 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2751 ; 1.502 ; 1.951 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 272 ; 6.670 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 76 ;33.290 ;23.684 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 290 ;11.022 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;15.206 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 302 ; 0.126 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1561 ; 0.017 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): 2013 ; 8.524 ; 3.000 REMARK 3 SPHERICITY; FREE ATOMS (A**2): 171 ;26.477 ; 5.000 REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2036 ; 9.511 ; 5.000 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 : NULL 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 USED IF PRESENT IN REMARK 3 THE INPUT U VALUES : REFINED INDIVIDUALLY REMARK 4 REMARK 4 5XH3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-APR-17. REMARK 100 THE DEPOSITION ID IS D_1300003519. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-APR-17 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSRRC REMARK 200 BEAMLINE : TPS 05A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9998 REMARK 200 MONOCHROMATOR : LN2 COOLED SI(111) DOUBLE REMARK 200 CRYSTAL MONOCHROMATOR REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300-HS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000, HKL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54696 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300 REMARK 200 RESOLUTION RANGE LOW (A) : 25.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 6.900 REMARK 200 R MERGE (I) : 0.05000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.35 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2 REMARK 200 DATA REDUNDANCY IN SHELL : 5.90 REMARK 200 R MERGE FOR SHELL (I) : 0.34300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 4WFI REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 38.96 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, NACL, HEPES, PH 7.5, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 25.44850 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.05400 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.64100 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.05400 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.44850 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 25.64100 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 160 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 9460 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL 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 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 HOH A 616 O HOH A 623 2.03 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH A 623 O HOH A 629 2455 1.86 REMARK 500 O HOH A 487 O HOH A 560 3545 1.97 REMARK 500 O HOH A 639 O HOH A 642 2455 2.07 REMARK 500 O HOH A 601 O HOH A 605 4455 2.13 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 ASN A 44 35.22 -145.61 REMARK 500 THR A 59 -14.03 75.90 REMARK 500 ALA A 131 -122.15 66.84 REMARK 500 SER A 185 -88.77 -130.30 REMARK 500 SER A 185 -86.79 -131.66 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 856 A 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 304 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5XH2 RELATED DB: PDB DBREF1 5XH3 A 1 261 UNP PETH_IDESA DBREF2 5XH3 A A0A0K8P6T7 30 290 SEQADV 5XH3 GLY A 103 UNP A0A0K8P6T ARG 132 ENGINEERED MUTATION SEQADV 5XH3 ALA A 131 UNP A0A0K8P6T SER 160 ENGINEERED MUTATION SEQRES 1 A 261 ASN PRO TYR ALA ARG GLY PRO ASN PRO THR ALA ALA SER SEQRES 2 A 261 LEU GLU ALA SER ALA GLY PRO PHE THR VAL ARG SER PHE SEQRES 3 A 261 THR VAL SER ARG PRO SER GLY TYR GLY ALA GLY THR VAL SEQRES 4 A 261 TYR TYR PRO THR ASN ALA GLY GLY THR VAL GLY ALA ILE SEQRES 5 A 261 ALA ILE VAL PRO GLY TYR THR ALA ARG GLN SER SER ILE SEQRES 6 A 261 LYS TRP TRP GLY PRO ARG LEU ALA SER HIS GLY PHE VAL SEQRES 7 A 261 VAL ILE THR ILE ASP THR ASN SER THR LEU ASP GLN PRO SEQRES 8 A 261 SER SER ARG SER SER GLN GLN MET ALA ALA LEU GLY GLN SEQRES 9 A 261 VAL ALA SER LEU ASN GLY THR SER SER SER PRO ILE TYR SEQRES 10 A 261 GLY LYS VAL ASP THR ALA ARG MET GLY VAL MET GLY TRP SEQRES 11 A 261 ALA MET GLY GLY GLY GLY SER LEU ILE SER ALA ALA ASN SEQRES 12 A 261 ASN PRO SER LEU LYS ALA ALA ALA PRO GLN ALA PRO TRP SEQRES 13 A 261 ASP SER SER THR ASN PHE SER SER VAL THR VAL PRO THR SEQRES 14 A 261 LEU ILE PHE ALA CYS GLU ASN ASP SER ILE ALA PRO VAL SEQRES 15 A 261 ASN SER SER ALA LEU PRO ILE TYR ASP SER MET SER ARG SEQRES 16 A 261 ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY GLY SER HIS SEQRES 17 A 261 SER CYS ALA ASN SER GLY ASN SER ASN GLN ALA LEU ILE SEQRES 18 A 261 GLY LYS LYS GLY VAL ALA TRP MET LYS ARG PHE MET ASP SEQRES 19 A 261 ASN ASP THR ARG TYR SER THR PHE ALA CYS GLU ASN PRO SEQRES 20 A 261 ASN SER THR ARG VAL SER ASP PHE ARG THR ALA ASN CYS SEQRES 21 A 261 SER HET 856 A 301 16 HET SO4 A 302 5 HET SO4 A 303 5 HET GOL A 304 6 HETNAM 856 O 4-(2-HYDROXYETHYL) O 1-METHYL BENZENE-1,4- HETNAM 2 856 DICARBOXYLATE HETNAM SO4 SULFATE ION HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 2 856 C11 H12 O5 FORMUL 3 SO4 2(O4 S 2-) FORMUL 5 GOL C3 H8 O3 FORMUL 6 HOH *244(H2 O) HELIX 1 AA1 THR A 10 ALA A 16 1 7 HELIX 2 AA2 ARG A 61 LYS A 66 5 6 HELIX 3 AA3 TRP A 67 SER A 74 1 8 HELIX 4 AA4 GLN A 90 GLY A 110 1 21 HELIX 5 AA5 ALA A 131 ASN A 144 1 14 HELIX 6 AA6 PRO A 181 SER A 184 5 4 HELIX 7 AA7 SER A 185 MET A 193 1 9 HELIX 8 AA8 ASN A 217 ASP A 234 1 18 HELIX 9 AA9 ASP A 236 ARG A 238 5 3 HELIX 10 AB1 TYR A 239 GLU A 245 1 7 SHEET 1 AA1 6 VAL A 23 THR A 27 0 SHEET 2 AA1 6 ALA A 36 PRO A 42 -1 O VAL A 39 N PHE A 26 SHEET 3 AA1 6 VAL A 78 ASP A 83 -1 O VAL A 79 N TYR A 40 SHEET 4 AA1 6 VAL A 49 VAL A 55 1 N ILE A 54 O ILE A 80 SHEET 5 AA1 6 VAL A 120 GLY A 129 1 O ASP A 121 N VAL A 49 SHEET 6 AA1 6 ALA A 149 ALA A 150 1 O ALA A 149 N VAL A 127 SHEET 1 AA2 3 THR A 169 CYS A 174 0 SHEET 2 AA2 3 LYS A 198 ILE A 203 1 O GLN A 199 N ILE A 171 SHEET 3 AA2 3 VAL A 252 ALA A 258 -1 O ASP A 254 N GLU A 202 SSBOND 1 CYS A 174 CYS A 210 1555 1555 2.04 SSBOND 2 CYS A 244 CYS A 260 1555 1555 2.08 SITE 1 AC1 13 SER A 32 GLY A 57 TYR A 58 GLN A 104 SITE 2 AC1 13 SER A 107 TRP A 130 ALA A 131 MET A 132 SITE 3 AC1 13 TRP A 156 ILE A 179 HIS A 208 HOH A 617 SITE 4 AC1 13 HOH A 630 SITE 1 AC2 4 TYR A 3 ARG A 124 LYS A 148 ASN A 235 SITE 1 AC3 4 ASN A 183 SER A 249 THR A 250 HOH A 401 SITE 1 AC4 6 THR A 59 SER A 95 MET A 99 ASN A 143 SITE 2 AC4 6 ASN A 144 HOH A 433 CRYST1 50.897 51.282 84.108 90.00 90.00 90.00 P 21 21 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.019648 0.000000 0.000000 0.00000 SCALE2 0.000000 0.019500 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011889 0.00000 ATOM 1 N ASN A 1 10.287 10.947 12.500 1.00 24.26 N ANISOU 1 N ASN A 1 2465 3821 2929 -1167 596 -1881 N ATOM 2 CA ASN A 1 9.479 9.890 11.823 1.00 17.98 C ANISOU 2 CA ASN A 1 2103 2614 2115 -448 -98 -1202 C ATOM 3 C ASN A 1 9.495 10.042 10.301 1.00 15.51 C ANISOU 3 C ASN A 1 1302 2009 2581 -670 -95 -517 C ATOM 4 O ASN A 1 8.855 10.945 9.740 1.00 19.43 O ANISOU 4 O ASN A 1 1763 2127 3492 -631 29 -552 O ATOM 5 CB ASN A 1 8.047 10.028 12.320 1.00 16.79 C ANISOU 5 CB ASN A 1 1661 2263 2455 -743 216 -1209 C ATOM 6 CG ASN A 1 7.154 8.882 11.864 1.00 14.25 C ANISOU 6 CG ASN A 1 1842 1480 2089 -523 203 -834 C ATOM 7 OD1 ASN A 1 6.016 8.731 12.328 1.00 20.11 O ANISOU 7 OD1 ASN A 1 1840 2881 2920 -745 539 -742 O ATOM 8 ND2 ASN A 1 7.658 8.070 10.981 1.00 10.68 N ANISOU 8 ND2 ASN A 1 1001 1596 1460 -303 -133 -561 N ATOM 9 N PRO A 2 10.199 9.137 9.602 1.00 15.42 N ANISOU 9 N PRO A 2 1506 2065 2287 -531 -11 -612 N ATOM 10 CA PRO A 2 10.263 9.228 8.132 1.00 15.96 C ANISOU 10 CA PRO A 2 1181 2654 2226 -540 -8 -273 C ATOM 11 C PRO A 2 8.934 8.965 7.426 1.00 14.70 C ANISOU 11 C PRO A 2 1601 2093 1889 -788 -97 -234 C ATOM 12 O PRO A 2 8.827 9.215 6.212 1.00 16.30 O ANISOU 12 O PRO A 2 1594 2513 2085 -591 129 165 O ATOM 13 CB PRO A 2 11.268 8.134 7.749 1.00 18.36 C ANISOU 13 CB PRO A 2 1491 2884 2600 -225 -238 -775 C ATOM 14 CG PRO A 2 11.197 7.155 8.874 1.00 17.63 C ANISOU 14 CG PRO A 2 1530 2744 2422 71 -98 -867 C ATOM 15 CD PRO A 2 10.883 7.937 10.124 1.00 18.15 C ANISOU 15 CD PRO A 2 2325 2399 2171 207 -22 -678 C ATOM 16 N TYR A 3 7.945 8.425 8.143 1.00 11.62 N ANISOU 16 N TYR A 3 1320 1489 1606 -607 17 -318 N ATOM 17 CA TYR A 3 6.674 8.042 7.499 1.00 10.69 C ANISOU 17 CA TYR A 3 1175 1396 1490 -402 11 -143 C ATOM 18 C TYR A 3 5.585 9.101 7.646 1.00 10.65 C ANISOU 18 C TYR A 3 1266 1423 1356 -295 -15 -164 C ATOM 19 O TYR A 3 4.474 8.951 7.104 1.00 11.67 O ANISOU 19 O TYR A 3 1335 1672 1424 -325 -175 -171 O ATOM 20 CB TYR A 3 6.179 6.722 8.077 1.00 11.41 C ANISOU 20 CB TYR A 3 1386 1307 1641 -280 -105 0 C ATOM 21 CG TYR A 3 7.246 5.655 8.106 1.00 11.14 C ANISOU 21 CG TYR A 3 1201 1535 1497 -348 -172 -189 C ATOM 22 CD1 TYR A 3 8.044 5.404 6.987 1.00 12.40 C ANISOU 22 CD1 TYR A 3 1214 1644 1852 -304 -255 -353 C ATOM 23 CD2 TYR A 3 7.358 4.809 9.206 1.00 13.33 C ANISOU 23 CD2 TYR A 3 1724 1438 1901 -162 -490 -167 C ATOM 24 CE1 TYR A 3 9.009 4.399 7.013 1.00 13.47 C ANISOU 24 CE1 TYR A 3 1232 1865 2018 -283 -309 -558 C ATOM 25 CE2 TYR A 3 8.315 3.806 9.252 1.00 15.83 C ANISOU 25 CE2 TYR A 3 1939 1900 2174 85 -497 -216 C ATOM 26 CZ TYR A 3 9.133 3.603 8.150 1.00 15.74 C ANISOU 26 CZ TYR A 3 1822 1924 2232 203 -365 -345 C ATOM 27 OH TYR A 3 10.035 2.581 8.175 1.00 20.85 O ANISOU 27 OH TYR A 3 2537 2195 3191 706 -499 -768 O ATOM 28 N ALA A 4 5.827 10.123 8.468 1.00 11.36 N ANISOU 28 N ALA A 4 1514 1428 1373 -405 54 -265 N ATOM 29 CA ALA A 4 4.810 11.121 8.704 1.00 11.71 C ANISOU 29 CA ALA A 4 1745 1471 1232 -310 148 -219 C ATOM 30 C ALA A 4 4.494 11.893 7.425 1.00 10.57 C ANISOU 30 C ALA A 4 1406 1163 1443 -255 181 -116 C ATOM 31 O ALA A 4 5.398 12.428 6.769 1.00 13.49 O ANISOU 31 O ALA A 4 1675 1655 1792 -670 348 -167 O ATOM 32 CB ALA A 4 5.211 12.066 9.851 1.00 14.26 C ANISOU 32 CB ALA A 4 2039 1853 1527 -210 -244 -696 C ATOM 33 N ARG A 5 3.210 11.991 7.099 1.00 10.90 N ANISOU 33 N ARG A 5 1582 1166 1391 -177 -94 -138 N ATOM 34 CA ARG A 5 2.767 12.765 5.941 1.00 10.74 C ANISOU 34 CA ARG A 5 1554 1226 1301 -359 -243 -159 C ATOM 35 C ARG A 5 1.679 13.735 6.316 1.00 10.62 C ANISOU 35 C ARG A 5 1615 1126 1294 -394 91 -81 C ATOM 36 O ARG A 5 0.870 13.417 7.173 1.00 11.41 O ANISOU 36 O ARG A 5 1638 1324 1374 -295 144 -194 O ATOM 37 CB ARG A 5 2.242 11.870 4.821 1.00 11.31 C ANISOU 37 CB ARG A 5 1505 1313 1478 -418 33 -411 C ATOM 38 CG ARG A 5 3.166 10.721 4.441 1.00 11.46 C ANISOU 38 CG ARG A 5 1551 1258 1545 -233 173 -237 C ATOM 39 CD ARG A 5 4.286 11.136 3.480 1.00 12.50 C ANISOU 39 CD ARG A 5 1573 1384 1792 -299 247 -316 C ATOM 40 NE ARG A 5 5.212 10.018 3.249 1.00 11.42 N ANISOU 40 NE ARG A 5 1646 1411 1282 -229 134 -80 N ATOM 41 CZ ARG A 5 6.347 9.813 3.913 1.00 10.83 C ANISOU 41 CZ ARG A 5 1272 1264 1578 -456 123 -285 C ATOM 42 NH1 ARG A 5 6.776 10.702 4.813 1.00 14.40 N ANISOU 42 NH1 ARG A 5 1957 2070 1442 -1003 249 -474 N ATOM 43 NH2 ARG A 5 7.066 8.726 3.705 1.00 12.79 N ANISOU 43 NH2 ARG A 5 1613 1624 1620 -391 183 -138 N ATOM 44 N GLY A 6 1.606 14.875 5.626 1.00 12.34 N ANISOU 44 N GLY A 6 1944 1216 1526 -308 -377 -227 N ATOM 45 CA GLY A 6 0.477 15.759 5.761 1.00 12.62 C ANISOU 45 CA GLY A 6 2104 1363 1326 -243 -158 -162 C ATOM 46 C GLY A 6 0.513 16.652 6.985 1.00 11.90 C ANISOU 46 C GLY A 6 1739 1420 1360 -291 -135 -116 C ATOM 47 O GLY A 6 1.379 16.506 7.862 1.00 12.29 O ANISOU 47 O GLY A 6 2001 1197 1472 -294 -234 -179 O ATOM 48 N PRO A 7 -0.377 17.649 7.010 1.00 13.96 N ANISOU 48 N PRO A 7 1998 1695 1609 -130 -303 -219 N ATOM 49 CA PRO A 7 -0.428 18.610 8.114 1.00 13.65 C ANISOU 49 CA PRO A 7 2318 1305 1562 -7 -208 -99 C ATOM 50 C PRO A 7 -0.866 17.968 9.406 1.00 13.08 C ANISOU 50 C PRO A 7 1654 1403 1911 -66 132 -100 C ATOM 51 O PRO A 7 -1.517 16.922 9.416 1.00 14.27 O ANISOU 51 O PRO A 7 2062 1491 1868 -371 21 -191 O ATOM 52 CB PRO A 7 -1.443 19.670 7.646 1.00 18.76 C ANISOU 52 CB PRO A 7 2948 1822 2358 304 -566 -135 C ATOM 53 CG PRO A 7 -2.163 19.063 6.499 1.00 27.18 C ANISOU 53 CG PRO A 7 3116 4264 2947 1310 -827 -1302 C ATOM 54 CD PRO A 7 -1.398 17.884 5.974 1.00 18.93 C ANISOU 54 CD PRO A 7 2431 2690 2068 146 -360 -473 C ATOM 55 N ASN A 8 -0.641 18.648 10.514 1.00 13.31 N ANISOU 55 N ASN A 8 1775 1464 1818 -42 -143 -159 N ATOM 56 CA ASN A 8 -1.082 18.114 11.792 1.00 14.22 C ANISOU 56 CA ASN A 8 2128 1470 1804 -407 -195 -362 C ATOM 57 C ASN A 8 -2.597 17.965 11.814 1.00 12.29 C ANISOU 57 C ASN A 8 1855 1323 1490 -33 -22 -164 C ATOM 58 O ASN A 8 -3.324 18.848 11.353 1.00 15.32 O ANISOU 58 O ASN A 8 2130 1532 2159 169 -185 -30 O ATOM 59 CB ASN A 8 -0.658 19.044 12.920 1.00 16.25 C ANISOU 59 CB ASN A 8 2338 1670 2163 -18 -564 -649 C ATOM 60 CG ASN A 8 0.842 19.115 13.081 1.00 17.01 C ANISOU 60 CG ASN A 8 2200 2001 2259 -88 -337 -762 C ATOM 61 OD1 ASN A 8 1.595 18.320 12.494 1.00 15.40 O ANISOU 61 OD1 ASN A 8 2220 1528 2104 -239 -383 -429 O ATOM 62 ND2 ASN A 8 1.296 20.154 13.764 1.00 23.03 N ANISOU 62 ND2 ASN A 8 3302 2545 2904 -822 -896 -956 N ATOM 63 N PRO A 9 -3.088 16.827 12.316 1.00 12.62 N ANISOU 63 N PRO A 9 1594 1353 1848 -64 -109 83 N ATOM 64 CA PRO A 9 -4.519 16.554 12.258 1.00 13.11 C ANISOU 64 CA PRO A 9 1679 1434 1866 39 48 56 C ATOM 65 C PRO A 9 -5.312 17.332 13.304 1.00 14.50 C ANISOU 65 C PRO A 9 1645 1889 1972 4 -166 -555 C ATOM 66 O PRO A 9 -4.804 17.615 14.409 1.00 15.67 O ANISOU 66 O PRO A 9 1957 1809 2184 192 -296 -545 O ATOM 67 CB PRO A 9 -4.594 15.041 12.560 1.00 13.22 C ANISOU 67 CB PRO A 9 1782 1243 1997 128 -263 -94 C ATOM 68 CG PRO A 9 -3.382 14.768 13.411 1.00 12.35 C ANISOU 68 CG PRO A 9 1508 1520 1661 44 -123 -36 C ATOM 69 CD PRO A 9 -2.309 15.676 12.831 1.00 11.97 C ANISOU 69 CD PRO A 9 1536 1192 1819 40 -166 -71 C ATOM 70 N THR A 10 -6.572 17.607 12.984 1.00 13.05 N ANISOU 70 N THR A 10 1671 1654 1631 127 -48 -405 N ATOM 71 CA THR A 10 -7.538 18.106 13.967 1.00 13.19 C ANISOU 71 CA THR A 10 1666 1382 1961 129 -86 -314 C ATOM 72 C THR A 10 -8.788 17.253 13.849 1.00 13.33 C ANISOU 72 C THR A 10 1786 1551 1726 -70 71 -251 C ATOM 73 O THR A 10 -8.948 16.494 12.884 1.00 12.25 O ANISOU 73 O THR A 10 1517 1398 1739 193 -55 -314 O ATOM 74 CB THR A 10 -7.920 19.566 13.673 1.00 15.01 C ANISOU 74 CB THR A 10 1852 1416 2436 116 -359 -538 C ATOM 75 OG1 THR A 10 -8.529 19.633 12.378 1.00 15.49 O ANISOU 75 OG1 THR A 10 2121 1489 2275 176 -219 -537 O ATOM 76 CG2 THR A 10 -6.698 20.459 13.735 1.00 17.49 C ANISOU 76 CG2 THR A 10 2107 1641 2894 16 -658 -754 C ATOM 77 N ALA A 11 -9.666 17.333 14.839 1.00 14.13 N ANISOU 77 N ALA A 11 1575 1707 2086 106 127 -386 N ATOM 78 CA ALA A 11 -10.927 16.617 14.718 1.00 14.38 C ANISOU 78 CA ALA A 11 1440 1936 2085 8 115 -240 C ATOM 79 C ALA A 11 -11.635 16.999 13.417 1.00 12.81 C ANISOU 79 C ALA A 11 1449 1690 1725 284 112 -525 C ATOM 80 O ALA A 11 -12.090 16.133 12.679 1.00 12.94 O ANISOU 80 O ALA A 11 1491 1646 1778 103 -48 -624 O ATOM 81 CB ALA A 11 -11.820 16.878 15.914 1.00 17.57 C ANISOU 81 CB ALA A 11 1892 2757 2025 115 499 -290 C ATOM 82 N ALA A 12 -11.714 18.292 13.125 1.00 15.58 N ANISOU 82 N ALA A 12 1940 1760 2219 423 -183 -331 N ATOM 83 CA ALA A 12 -12.345 18.749 11.892 1.00 15.24 C ANISOU 83 CA ALA A 12 2273 1538 1977 560 -435 -409 C ATOM 84 C ALA A 12 -11.685 18.149 10.660 1.00 13.53 C ANISOU 84 C ALA A 12 1824 1308 2006 265 -421 -250 C ATOM 85 O ALA A 12 -12.371 17.721 9.731 1.00 14.35 O ANISOU 85 O ALA A 12 2014 1385 2053 138 -367 -264 O ATOM 86 CB ALA A 12 -12.320 20.279 11.803 1.00 18.65 C ANISOU 86 CB ALA A 12 2607 1387 3090 502 -710 -657 C ATOM 87 N SER A 13 -10.353 18.134 10.616 1.00 13.30 N ANISOU 87 N SER A 13 1718 1214 2118 266 0 26 N ATOM 88 CA SER A 13 -9.687 17.669 9.395 1.00 13.44 C ANISOU 88 CA SER A 13 1837 1150 2118 -219 173 -3 C ATOM 89 C SER A 13 -9.902 16.173 9.183 1.00 11.58 C ANISOU 89 C SER A 13 1797 1215 1387 4 165 -163 C ATOM 90 O SER A 13 -9.960 15.704 8.048 1.00 12.92 O ANISOU 90 O SER A 13 2029 1224 1656 6 56 -8 O ATOM 91 CB SER A 13 -8.200 18.032 9.374 1.00 14.79 C ANISOU 91 CB SER A 13 1802 1513 2304 -227 19 171 C ATOM 92 OG SER A 13 -7.420 17.146 10.171 1.00 14.73 O ANISOU 92 OG SER A 13 1619 1747 2229 -89 -244 -189 O ATOM 93 N LEU A 14 -10.048 15.428 10.277 1.00 10.31 N ANISOU 93 N LEU A 14 1190 955 1771 -17 64 8 N ATOM 94 CA LEU A 14 -10.335 13.983 10.200 1.00 9.39 C ANISOU 94 CA LEU A 14 1070 996 1502 -71 -84 100 C ATOM 95 C LEU A 14 -11.789 13.630 9.969 1.00 9.46 C ANISOU 95 C LEU A 14 1221 1078 1295 20 -273 -11 C ATOM 96 O LEU A 14 -12.069 12.566 9.450 1.00 10.46 O ANISOU 96 O LEU A 14 1324 1200 1451 67 -197 -190 O ATOM 97 CB LEU A 14 -9.828 13.261 11.441 1.00 10.18 C ANISOU 97 CB LEU A 14 1298 1203 1365 185 -230 14 C ATOM 98 CG LEU A 14 -8.308 13.315 11.583 1.00 11.38 C ANISOU 98 CG LEU A 14 1487 1613 1223 364 -100 -558 C ATOM 99 CD1 LEU A 14 -7.842 12.670 12.883 1.00 13.88 C ANISOU 99 CD1 LEU A 14 1760 1401 2110 -88 -604 333 C ATOM 100 CD2 LEU A 14 -7.427 13.113 10.342 1.00 19.80 C ANISOU 100 CD2 LEU A 14 2287 3407 1827 -11 -90 -289 C ATOM 101 N GLU A 15 -12.707 14.519 10.347 1.00 10.29 N ANISOU 101 N GLU A 15 1184 1237 1486 267 29 155 N ATOM 102 CA GLU A 15 -14.142 14.306 10.157 1.00 9.86 C ANISOU 102 CA GLU A 15 1319 1284 1140 138 14 -76 C ATOM 103 C GLU A 15 -14.586 14.736 8.755 1.00 10.26 C ANISOU 103 C GLU A 15 1400 1196 1301 144 -19 137 C ATOM 104 O GLU A 15 -15.648 14.329 8.279 1.00 12.09 O ANISOU 104 O GLU A 15 1373 1618 1602 -18 -67 187 O ATOM 105 CB GLU A 15 -14.931 15.055 11.227 1.00 12.19 C ANISOU 105 CB GLU A 15 1792 1492 1345 317 178 -89 C ATOM 106 CG GLU A 15 -14.775 14.426 12.609 1.00 12.31 C ANISOU 106 CG GLU A 15 1718 1719 1241 419 226 -99 C ATOM 107 CD GLU A 15 -15.231 15.332 13.740 1.00 16.36 C ANISOU 107 CD GLU A 15 2583 1961 1672 723 396 -223 C ATOM 108 OE1 GLU A 15 -15.837 16.383 13.458 1.00 24.83 O ANISOU 108 OE1 GLU A 15 3763 2963 2706 1912 116 -117 O ATOM 109 OE2 GLU A 15 -14.926 14.987 14.901 1.00 18.23 O ANISOU 109 OE2 GLU A 15 2746 2550 1631 1071 170 -164 O ATOM 110 N ALA A 16 -13.776 15.578 8.092 1.00 11.50 N ANISOU 110 N ALA A 16 1601 1252 1514 264 46 260 N ATOM 111 CA ALA A 16 -14.128 16.073 6.761 1.00 11.87 C ANISOU 111 CA ALA A 16 1574 1468 1467 5 -99 187 C ATOM 112 C ALA A 16 -14.275 14.924 5.777 1.00 11.16 C ANISOU 112 C ALA A 16 1223 1496 1519 78 -232 190 C ATOM 113 O ALA A 16 -13.621 13.890 5.894 1.00 12.81 O ANISOU 113 O ALA A 16 1849 1276 1742 96 -299 -2 O ATOM 114 CB ALA A 16 -13.040 17.020 6.265 1.00 13.25 C ANISOU 114 CB ALA A 16 1675 1431 1927 4 374 95 C ATOM 115 N SER A 17 -15.039 15.150 4.718 1.00 11.76 N ANISOU 115 N SER A 17 1191 1843 1434 65 -109 32 N ATOM 116 CA SER A 17 -15.164 14.170 3.662 1.00 13.58 C ANISOU 116 CA SER A 17 1436 2286 1436 -263 -34 -277 C ATOM 117 C SER A 17 -13.845 13.854 2.967 1.00 12.01 C ANISOU 117 C SER A 17 1278 1740 1544 18 -189 115 C ATOM 118 O SER A 17 -13.660 12.753 2.459 1.00 17.42 O ANISOU 118 O SER A 17 2734 1772 2112 26 255 -99 O ATOM 119 CB SER A 17 -16.159 14.693 2.607 1.00 17.69 C ANISOU 119 CB SER A 17 1227 3789 1705 -185 -484 -43 C ATOM 120 OG SER A 17 -17.467 14.718 3.131 1.00 27.46 O ANISOU 120 OG SER A 17 2821 4804 2806 71 395 -408 O ATOM 121 N ALA A 18 -12.969 14.839 2.849 1.00 12.15 N ANISOU 121 N ALA A 18 1116 1699 1798 17 147 -96 N ATOM 122 CA ALA A 18 -11.688 14.613 2.198 1.00 15.10 C ANISOU 122 CA ALA A 18 1325 2450 1962 -295 230 -371 C ATOM 123 C ALA A 18 -10.549 15.135 3.040 1.00 12.71 C ANISOU 123 C ALA A 18 1379 1271 2179 -41 55 -352 C ATOM 124 O ALA A 18 -10.647 16.205 3.666 1.00 12.89 O ANISOU 124 O ALA A 18 1425 1601 1871 78 87 -116 O ATOM 125 CB ALA A 18 -11.683 15.284 0.851 1.00 20.64 C ANISOU 125 CB ALA A 18 1761 4415 1663 -876 114 -121 C ATOM 126 N GLY A 19 -9.443 14.405 3.003 1.00 11.80 N ANISOU 126 N GLY A 19 1443 1275 1765 -40 389 -65 N ATOM 127 CA GLY A 19 -8.216 14.854 3.596 1.00 10.72 C ANISOU 127 CA GLY A 19 1312 1020 1740 -66 106 218 C ATOM 128 C GLY A 19 -7.465 15.820 2.697 1.00 10.34 C ANISOU 128 C GLY A 19 1415 1193 1320 59 191 -56 C ATOM 129 O GLY A 19 -7.995 16.332 1.702 1.00 12.67 O ANISOU 129 O GLY A 19 1720 1422 1672 136 15 144 O ATOM 130 N PRO A 20 -6.213 16.103 3.054 1.00 9.84 N ANISOU 130 N PRO A 20 1415 941 1379 2 138 2 N ATOM 131 CA PRO A 20 -5.457 17.174 2.407 1.00 12.22 C ANISOU 131 CA PRO A 20 1923 1285 1434 -288 313 -80 C ATOM 132 C PRO A 20 -4.943 16.834 1.011 1.00 10.43 C ANISOU 132 C PRO A 20 1536 1049 1377 -363 260 56 C ATOM 133 O PRO A 20 -4.594 17.753 0.279 1.00 13.55 O ANISOU 133 O PRO A 20 2284 1111 1750 -337 618 235 O ATOM 134 CB PRO A 20 -4.273 17.364 3.354 1.00 16.03 C ANISOU 134 CB PRO A 20 2071 2009 2009 -721 -20 -246 C ATOM 135 CG PRO A 20 -4.098 16.043 4.011 1.00 17.55 C ANISOU 135 CG PRO A 20 1817 2530 2318 -611 51 -284 C ATOM 136 CD PRO A 20 -5.503 15.541 4.212 1.00 12.94 C ANISOU 136 CD PRO A 20 1529 1936 1451 -22 -158 -239 C ATOM 137 N PHE A 21 -4.856 15.560 0.638 1.00 9.84 N ANISOU 137 N PHE A 21 1506 1111 1119 -52 23 -115 N ATOM 138 CA PHE A 21 -4.221 15.189 -0.629 1.00 9.55 C ANISOU 138 CA PHE A 21 1227 1040 1360 -70 220 103 C ATOM 139 C PHE A 21 -5.260 15.003 -1.718 1.00 9.59 C ANISOU 139 C PHE A 21 1356 976 1309 -79 288 -45 C ATOM 140 O PHE A 21 -6.368 14.515 -1.475 1.00 11.10 O ANISOU 140 O PHE A 21 1403 1459 1355 -226 73 188 O ATOM 141 CB PHE A 21 -3.361 13.933 -0.451 1.00 9.75 C ANISOU 141 CB PHE A 21 1216 962 1524 -227 -112 71 C ATOM 142 CG PHE A 21 -2.251 14.111 0.565 1.00 9.06 C ANISOU 142 CG PHE A 21 1139 1111 1192 -114 131 -83 C ATOM 143 CD1 PHE A 21 -1.359 15.173 0.488 1.00 13.52 C ANISOU 143 CD1 PHE A 21 1646 1730 1761 -695 -7 48 C ATOM 144 CD2 PHE A 21 -2.132 13.240 1.638 1.00 13.21 C ANISOU 144 CD2 PHE A 21 1641 1747 1627 -319 -248 583 C ATOM 145 CE1 PHE A 21 -0.345 15.334 1.437 1.00 14.33 C ANISOU 145 CE1 PHE A 21 2013 1592 1839 -329 -306 86 C ATOM 146 CE2 PHE A 21 -1.117 13.384 2.573 1.00 14.14 C ANISOU 146 CE2 PHE A 21 1706 2019 1646 -558 -131 399 C ATOM 147 CZ PHE A 21 -0.234 14.451 2.493 1.00 11.87 C ANISOU 147 CZ PHE A 21 1518 1609 1382 -193 144 -240 C ATOM 148 N THR A 22 -4.830 15.252 -2.944 1.00 9.96 N ANISOU 148 N THR A 22 1642 952 1189 -112 137 11 N ATOM 149 CA THR A 22 -5.655 15.019 -4.115 1.00 11.58 C ANISOU 149 CA THR A 22 1951 1017 1431 -104 -6 106 C ATOM 150 C THR A 22 -5.583 13.544 -4.491 1.00 9.56 C ANISOU 150 C THR A 22 1225 1043 1362 -71 -95 10 C ATOM 151 O THR A 22 -4.524 12.943 -4.428 1.00 10.75 O ANISOU 151 O THR A 22 1464 1055 1562 -99 108 263 O ATOM 152 CB THR A 22 -5.144 15.903 -5.268 1.00 13.99 C ANISOU 152 CB THR A 22 2545 1298 1470 -470 160 292 C ATOM 153 OG1 THR A 22 -5.319 17.268 -4.892 1.00 15.84 O ANISOU 153 OG1 THR A 22 2901 1209 1907 -419 -139 376 O ATOM 154 CG2 THR A 22 -5.921 15.677 -6.546 1.00 17.83 C ANISOU 154 CG2 THR A 22 3372 2058 1343 -475 -257 523 C ATOM 155 N VAL A 23 -6.717 12.985 -4.874 1.00 11.12 N ANISOU 155 N VAL A 23 1507 1220 1496 -205 -231 -28 N ATOM 156 CA VAL A 23 -6.835 11.561 -5.133 1.00 10.13 C ANISOU 156 CA VAL A 23 1541 1098 1210 -280 -155 132 C ATOM 157 C VAL A 23 -7.135 11.349 -6.606 1.00 10.68 C ANISOU 157 C VAL A 23 1429 1389 1239 -37 75 82 C ATOM 158 O VAL A 23 -8.053 11.984 -7.162 1.00 11.65 O ANISOU 158 O VAL A 23 1707 1367 1350 110 -314 -62 O ATOM 159 CB VAL A 23 -7.940 10.939 -4.248 1.00 10.69 C ANISOU 159 CB VAL A 23 1708 1342 1009 -352 1 162 C ATOM 160 CG1 VAL A 23 -8.164 9.467 -4.590 1.00 12.08 C ANISOU 160 CG1 VAL A 23 1992 1282 1314 -350 -26 105 C ATOM 161 CG2 VAL A 23 -7.570 11.116 -2.780 1.00 12.53 C ANISOU 161 CG2 VAL A 23 2309 1407 1042 -178 -68 125 C ATOM 162 N ARG A 24 -6.509 10.333 -7.175 1.00 9.62 N ANISOU 162 N ARG A 24 1486 1046 1123 -131 -48 120 N ATOM 163 CA ARG A 24 -6.894 9.797 -8.480 1.00 10.77 C ANISOU 163 CA ARG A 24 1758 1226 1108 -394 -113 -1 C ATOM 164 C ARG A 24 -7.039 8.289 -8.331 1.00 9.68 C ANISOU 164 C ARG A 24 1526 1093 1057 26 -335 86 C ATOM 165 O ARG A 24 -6.681 7.715 -7.297 1.00 10.13 O ANISOU 165 O ARG A 24 1429 1192 1225 -41 -176 253 O ATOM 166 CB ARG A 24 -5.839 10.148 -9.542 1.00 12.40 C ANISOU 166 CB ARG A 24 2070 1439 1203 -182 90 172 C ATOM 167 CG ARG A 24 -5.761 11.644 -9.842 1.00 15.93 C ANISOU 167 CG ARG A 24 2711 1514 1825 -194 -9 457 C ATOM 168 CD ARG A 24 -6.989 12.163 -10.546 1.00 22.10 C ANISOU 168 CD ARG A 24 3549 2195 2650 -112 -167 982 C ATOM 169 NE ARG A 24 -6.862 13.597 -10.839 1.00 29.78 N ANISOU 169 NE ARG A 24 5403 2339 3574 -212 -401 637 N ATOM 170 CZ ARG A 24 -7.318 14.568 -10.048 1.00 35.23 C ANISOU 170 CZ ARG A 24 7833 2396 3155 -130 -98 625 C ATOM 171 NH1 ARG A 24 -7.925 14.274 -8.898 1.00 27.95 N ANISOU 171 NH1 ARG A 24 4686 2743 3190 144 -684 859 N ATOM 172 NH2 ARG A 24 -7.172 15.828 -10.397 1.00 38.73 N ANISOU 172 NH2 ARG A 24 7517 2594 4604 -1227 -2196 974 N ATOM 173 N SER A 25 -7.607 7.646 -9.344 1.00 10.14 N ANISOU 173 N SER A 25 1636 1098 1117 -128 -334 63 N ATOM 174 CA SER A 25 -7.832 6.214 -9.299 1.00 10.37 C ANISOU 174 CA SER A 25 1813 1051 1073 -355 -46 195 C ATOM 175 C SER A 25 -7.721 5.560 -10.661 1.00 11.17 C ANISOU 175 C SER A 25 1827 1304 1111 -150 -336 90 C ATOM 176 O SER A 25 -7.803 6.246 -11.699 1.00 13.56 O ANISOU 176 O SER A 25 2408 1474 1267 -141 -408 250 O ATOM 177 CB SER A 25 -9.198 5.912 -8.695 1.00 12.24 C ANISOU 177 CB SER A 25 1332 1410 1908 293 -93 298 C ATOM 178 OG SER A 25 -10.233 6.326 -9.557 1.00 15.10 O ANISOU 178 OG SER A 25 1747 2148 1839 137 -242 150 O ATOM 179 N PHE A 26 -7.487 4.253 -10.669 1.00 10.00 N ANISOU 179 N PHE A 26 1652 1168 977 -134 -78 -10 N ATOM 180 CA PHE A 26 -7.510 3.496 -11.909 1.00 10.93 C ANISOU 180 CA PHE A 26 1668 1336 1149 -124 -98 -82 C ATOM 181 C PHE A 26 -8.022 2.100 -11.631 1.00 10.51 C ANISOU 181 C PHE A 26 1952 1151 889 -54 -274 134 C ATOM 182 O PHE A 26 -7.974 1.631 -10.500 1.00 9.70 O ANISOU 182 O PHE A 26 1418 1410 855 -181 -133 201 O ATOM 183 CB PHE A 26 -6.117 3.476 -12.590 1.00 11.85 C ANISOU 183 CB PHE A 26 1673 1682 1145 -159 -101 -11 C ATOM 184 CG PHE A 26 -5.024 2.845 -11.774 1.00 11.68 C ANISOU 184 CG PHE A 26 1456 1764 1218 -229 0 -62 C ATOM 185 CD1 PHE A 26 -4.256 3.606 -10.888 1.00 13.09 C ANISOU 185 CD1 PHE A 26 1775 1954 1243 -688 3 323 C ATOM 186 CD2 PHE A 26 -4.745 1.492 -11.907 1.00 12.80 C ANISOU 186 CD2 PHE A 26 1713 1982 1167 -149 402 9 C ATOM 187 CE1 PHE A 26 -3.230 3.013 -10.166 1.00 13.76 C ANISOU 187 CE1 PHE A 26 1791 2308 1128 -336 220 -40 C ATOM 188 CE2 PHE A 26 -3.727 0.894 -11.180 1.00 13.69 C ANISOU 188 CE2 PHE A 26 1444 2329 1428 -405 112 -60 C ATOM 189 CZ PHE A 26 -2.961 1.671 -10.305 1.00 13.14 C ANISOU 189 CZ PHE A 26 1697 2129 1165 -474 94 223 C ATOM 190 N THR A 27 -8.402 1.413 -12.700 1.00 11.97 N ANISOU 190 N THR A 27 2024 1257 1264 -389 -498 3 N ATOM 191 CA THR A 27 -8.870 0.030 -12.640 1.00 11.20 C ANISOU 191 CA THR A 27 1899 1094 1261 -201 -468 59 C ATOM 192 C THR A 27 -7.665 -0.856 -12.897 1.00 10.90 C ANISOU 192 C THR A 27 1487 1514 1138 -161 -365 274 C ATOM 193 O THR A 27 -6.865 -0.570 -13.783 1.00 13.65 O ANISOU 193 O THR A 27 1880 1835 1472 -579 -233 302 O ATOM 194 CB THR A 27 -9.911 -0.204 -13.756 1.00 11.84 C ANISOU 194 CB THR A 27 1694 1280 1524 -264 -191 -68 C ATOM 195 OG1 THR A 27 -11.016 0.625 -13.461 1.00 15.45 O ANISOU 195 OG1 THR A 27 1880 2037 1949 4 -279 61 O ATOM 196 CG2 THR A 27 -10.358 -1.677 -13.785 1.00 12.84 C ANISOU 196 CG2 THR A 27 1739 1417 1719 -289 -53 -158 C ATOM 197 N VAL A 28 -7.541 -1.966 -12.168 1.00 9.91 N ANISOU 197 N VAL A 28 1517 1197 1049 8 -318 202 N ATOM 198 CA VAL A 28 -6.450 -2.921 -12.429 1.00 10.00 C ANISOU 198 CA VAL A 28 1265 1411 1124 -186 -236 359 C ATOM 199 C VAL A 28 -6.724 -3.716 -13.714 1.00 11.85 C ANISOU 199 C VAL A 28 1367 2205 929 -112 -182 220 C ATOM 200 O VAL A 28 -7.805 -4.307 -13.868 1.00 11.65 O ANISOU 200 O VAL A 28 1382 2002 1039 -1 -122 44 O ATOM 201 CB VAL A 28 -6.303 -3.879 -11.227 1.00 9.73 C ANISOU 201 CB VAL A 28 1493 1261 943 -89 -305 118 C ATOM 202 CG1 VAL A 28 -5.231 -4.923 -11.519 1.00 11.73 C ANISOU 202 CG1 VAL A 28 1740 1651 1064 405 -213 220 C ATOM 203 CG2 VAL A 28 -5.942 -3.067 -9.979 1.00 10.94 C ANISOU 203 CG2 VAL A 28 1598 1529 1027 -124 -357 -78 C ATOM 204 N SER A 29 -5.801 -3.681 -14.674 1.00 13.40 N ANISOU 204 N SER A 29 1761 2357 973 208 -83 236 N ATOM 205 CA SER A 29 -6.024 -4.452 -15.937 1.00 13.74 C ANISOU 205 CA SER A 29 1387 2760 1071 203 -45 141 C ATOM 206 C SER A 29 -6.145 -5.952 -15.741 1.00 18.25 C ANISOU 206 C SER A 29 1605 2966 2363 223 670 -1020 C ATOM 207 O SER A 29 -7.044 -6.591 -16.296 1.00 17.86 O ANISOU 207 O SER A 29 2068 3185 1532 467 -286 -1056 O ATOM 208 CB SER A 29 -4.938 -4.181 -16.973 1.00 15.76 C ANISOU 208 CB SER A 29 2195 3033 758 -284 184 54 C ATOM 209 OG SER A 29 -5.192 -4.978 -18.154 1.00 16.35 O ANISOU 209 OG SER A 29 2207 2705 1298 -63 -169 -37 O ATOM 210 N ARG A 30 -5.112 -6.556 -15.152 1.00 13.38 N ANISOU 210 N ARG A 30 1409 2626 1046 95 88 95 N ATOM 211 CA ARG A 30 -5.087 -8.001 -14.986 1.00 14.63 C ANISOU 211 CA ARG A 30 1716 2648 1194 20 69 -185 C ATOM 212 C ARG A 30 -4.940 -8.264 -13.515 1.00 13.09 C ANISOU 212 C ARG A 30 1562 2466 945 -135 -148 -542 C ATOM 213 O ARG A 30 -3.827 -8.421 -13.025 1.00 11.01 O ANISOU 213 O ARG A 30 1370 1723 1090 -197 7 -205 O ATOM 214 CB ARG A 30 -3.888 -8.609 -15.733 1.00 18.02 C ANISOU 214 CB ARG A 30 2148 3198 1499 356 287 -744 C ATOM 215 CG ARG A 30 -3.948 -8.418 -17.232 1.00 21.47 C ANISOU 215 CG ARG A 30 2822 3261 2071 -191 404 -183 C ATOM 216 CD ARG A 30 -3.025 -7.284 -17.676 1.00 21.80 C ANISOU 216 CD ARG A 30 2385 2849 3047 -111 -486 202 C ATOM 217 NE ARG A 30 -1.613 -7.702 -17.604 1.00 23.25 N ANISOU 217 NE ARG A 30 2165 4224 2444 -399 324 -696 N ATOM 218 CZ ARG A 30 -0.590 -6.985 -18.058 1.00 26.98 C ANISOU 218 CZ ARG A 30 2549 3561 4141 687 -30 849 C ATOM 219 NH1 ARG A 30 0.654 -7.424 -17.870 1.00 23.66 N ANISOU 219 NH1 ARG A 30 2350 3352 3286 -200 -115 1005 N ATOM 220 NH2 ARG A 30 -0.823 -5.973 -18.887 1.00 29.98 N ANISOU 220 NH2 ARG A 30 5559 3001 2831 1443 -1771 -311 N ATOM 221 N PRO A 31 -6.070 -8.350 -12.797 1.00 13.67 N ANISOU 221 N PRO A 31 1281 2326 1587 -300 -58 -576 N ATOM 222 CA PRO A 31 -5.950 -8.745 -11.382 1.00 12.79 C ANISOU 222 CA PRO A 31 1142 2314 1403 -257 64 -249 C ATOM 223 C PRO A 31 -5.157 -10.039 -11.161 1.00 11.09 C ANISOU 223 C PRO A 31 1725 1433 1056 -296 259 -378 C ATOM 224 O PRO A 31 -5.400 -11.056 -11.829 1.00 17.29 O ANISOU 224 O PRO A 31 2723 1674 2172 -724 776 -979 O ATOM 225 CB PRO A 31 -7.411 -8.945 -10.945 1.00 14.80 C ANISOU 225 CB PRO A 31 1532 2228 1862 -22 620 -668 C ATOM 226 CG PRO A 31 -8.141 -8.061 -11.869 1.00 15.03 C ANISOU 226 CG PRO A 31 1899 1699 2109 445 777 121 C ATOM 227 CD PRO A 31 -7.477 -8.221 -13.199 1.00 15.59 C ANISOU 227 CD PRO A 31 1791 2817 1315 47 -267 -782 C ATOM 228 N SER A 32 -4.309 -10.040 -10.163 1.00 12.81 N ANISOU 228 N SER A 32 1534 1597 1735 -139 482 47 N ATOM 229 CA SER A 32 -3.434 -11.158 -9.875 1.00 15.95 C ANISOU 229 CA SER A 32 1854 1396 2809 161 201 -296 C ATOM 230 C SER A 32 -4.120 -11.951 -8.793 1.00 13.90 C ANISOU 230 C SER A 32 1551 1859 1868 351 72 -306 C ATOM 231 O SER A 32 -3.934 -11.650 -7.622 1.00 20.87 O ANISOU 231 O SER A 32 1879 3255 2795 412 -359 -963 O ATOM 232 CB SER A 32 -2.091 -10.589 -9.312 1.00 22.55 C ANISOU 232 CB SER A 32 1667 3038 3863 846 -991 -719 C ATOM 233 OG SER A 32 -1.270 -11.622 -8.767 1.00 27.14 O ANISOU 233 OG SER A 32 3346 3278 3688 367 -167 -663 O ATOM 234 N GLY A 33 -5.050 -12.849 -9.153 1.00 11.45 N ANISOU 234 N GLY A 33 1492 1345 1513 15 497 -93 N ATOM 235 CA GLY A 33 -5.548 -13.784 -8.131 1.00 15.09 C ANISOU 235 CA GLY A 33 1542 1930 2260 462 935 468 C ATOM 236 C GLY A 33 -6.790 -13.285 -7.414 1.00 12.82 C ANISOU 236 C GLY A 33 1374 1850 1646 470 624 756 C ATOM 237 O GLY A 33 -7.197 -13.890 -6.440 1.00 20.44 O ANISOU 237 O GLY A 33 2159 3052 2554 966 1202 1760 O ATOM 238 N TYR A 34 -7.464 -12.280 -7.963 1.00 10.05 N ANISOU 238 N TYR A 34 1166 1184 1466 98 156 -9 N ATOM 239 CA TYR A 34 -8.738 -11.821 -7.398 1.00 9.78 C ANISOU 239 CA TYR A 34 1283 1085 1346 153 113 -10 C ATOM 240 C TYR A 34 -9.588 -11.342 -8.563 1.00 9.52 C ANISOU 240 C TYR A 34 1274 1119 1223 -50 156 -61 C ATOM 241 O TYR A 34 -9.164 -11.417 -9.709 1.00 11.42 O ANISOU 241 O TYR A 34 1483 1662 1192 40 256 21 O ATOM 242 CB TYR A 34 -8.522 -10.749 -6.293 1.00 9.46 C ANISOU 242 CB TYR A 34 1279 1210 1102 -69 96 40 C ATOM 243 CG TYR A 34 -7.730 -9.554 -6.764 1.00 8.22 C ANISOU 243 CG TYR A 34 1150 1101 873 30 79 -202 C ATOM 244 CD1 TYR A 34 -6.328 -9.593 -6.807 1.00 8.71 C ANISOU 244 CD1 TYR A 34 1017 1292 998 -120 53 -79 C ATOM 245 CD2 TYR A 34 -8.376 -8.378 -7.150 1.00 8.78 C ANISOU 245 CD2 TYR A 34 1466 1026 843 -49 227 -137 C ATOM 246 CE1 TYR A 34 -5.601 -8.504 -7.284 1.00 8.10 C ANISOU 246 CE1 TYR A 34 1176 983 918 50 -86 -216 C ATOM 247 CE2 TYR A 34 -7.653 -7.295 -7.623 1.00 8.36 C ANISOU 247 CE2 TYR A 34 1045 1037 1092 -15 189 -311 C ATOM 248 CZ TYR A 34 -6.270 -7.383 -7.730 1.00 8.66 C ANISOU 248 CZ TYR A 34 1234 1095 958 22 43 -194 C ATOM 249 OH TYR A 34 -5.579 -6.291 -8.197 1.00 9.11 O ANISOU 249 OH TYR A 34 1285 1046 1130 -114 14 -182 O ATOM 250 N GLY A 35 -10.792 -10.864 -8.294 1.00 9.18 N ANISOU 250 N GLY A 35 1053 1174 1259 -109 76 -49 N ATOM 251 CA GLY A 35 -11.763 -10.625 -9.363 1.00 9.82 C ANISOU 251 CA GLY A 35 1416 1156 1159 -52 45 -10 C ATOM 252 C GLY A 35 -11.555 -9.344 -10.159 1.00 8.30 C ANISOU 252 C GLY A 35 1092 1069 989 -224 200 -75 C ATOM 253 O GLY A 35 -11.467 -9.348 -11.382 1.00 10.72 O ANISOU 253 O GLY A 35 1656 1398 1019 -164 -54 -115 O ATOM 254 N ALA A 36 -11.423 -8.239 -9.447 1.00 7.89 N ANISOU 254 N ALA A 36 1040 793 1165 1 -26 -114 N ATOM 255 CA ALA A 36 -11.261 -6.923 -10.066 1.00 7.62 C ANISOU 255 CA ALA A 36 1136 810 947 15 -142 -42 C ATOM 256 C ALA A 36 -10.755 -5.992 -8.966 1.00 7.06 C ANISOU 256 C ALA A 36 968 892 820 -12 24 -38 C ATOM 257 O ALA A 36 -10.881 -6.296 -7.778 1.00 7.77 O ANISOU 257 O ALA A 36 1061 1064 827 -74 79 -71 O ATOM 258 CB ALA A 36 -12.599 -6.391 -10.605 1.00 9.62 C ANISOU 258 CB ALA A 36 1020 1411 1221 79 -73 116 C ATOM 259 N GLY A 37 -10.162 -4.872 -9.361 1.00 8.16 N ANISOU 259 N GLY A 37 1181 1000 916 -127 1 -173 N ATOM 260 CA GLY A 37 -9.693 -3.934 -8.372 1.00 9.06 C ANISOU 260 CA GLY A 37 1666 763 1012 -114 -107 -139 C ATOM 261 C GLY A 37 -9.709 -2.515 -8.851 1.00 7.34 C ANISOU 261 C GLY A 37 972 938 878 -208 165 118 C ATOM 262 O GLY A 37 -9.542 -2.252 -10.051 1.00 9.83 O ANISOU 262 O GLY A 37 1499 1291 944 -45 195 91 O ATOM 263 N THR A 38 -9.862 -1.589 -7.908 1.00 7.65 N ANISOU 263 N THR A 38 1062 856 988 -146 -125 -59 N ATOM 264 CA THR A 38 -9.669 -0.168 -8.162 1.00 7.89 C ANISOU 264 CA THR A 38 1087 975 936 -64 -196 105 C ATOM 265 C THR A 38 -8.620 0.328 -7.187 1.00 7.54 C ANISOU 265 C THR A 38 977 1011 876 -162 -235 350 C ATOM 266 O THR A 38 -8.674 0.023 -5.986 1.00 8.13 O ANISOU 266 O THR A 38 1067 1187 834 -192 -150 204 O ATOM 267 CB THR A 38 -10.950 0.640 -7.902 1.00 8.34 C ANISOU 267 CB THR A 38 877 1009 1282 -225 -173 -34 C ATOM 268 OG1 THR A 38 -12.023 0.087 -8.669 1.00 9.20 O ANISOU 268 OG1 THR A 38 1071 1330 1094 -194 -170 -60 O ATOM 269 CG2 THR A 38 -10.749 2.112 -8.291 1.00 9.60 C ANISOU 269 CG2 THR A 38 1476 901 1268 25 45 162 C ATOM 270 N VAL A 39 -7.613 1.026 -7.719 1.00 7.72 N ANISOU 270 N VAL A 39 1041 1046 844 -233 -144 84 N ATOM 271 CA VAL A 39 -6.544 1.604 -6.893 1.00 7.32 C ANISOU 271 CA VAL A 39 954 1035 790 -273 -16 42 C ATOM 272 C VAL A 39 -6.781 3.102 -6.780 1.00 7.48 C ANISOU 272 C VAL A 39 1019 985 836 -174 -156 7 C ATOM 273 O VAL A 39 -6.879 3.794 -7.793 1.00 10.21 O ANISOU 273 O VAL A 39 1736 1203 939 -149 -271 157 O ATOM 274 CB VAL A 39 -5.163 1.330 -7.525 1.00 8.20 C ANISOU 274 CB VAL A 39 842 1278 993 -152 -89 92 C ATOM 275 CG1 VAL A 39 -4.072 2.031 -6.723 1.00 9.99 C ANISOU 275 CG1 VAL A 39 1084 1553 1158 -328 -240 44 C ATOM 276 CG2 VAL A 39 -4.921 -0.181 -7.509 1.00 10.62 C ANISOU 276 CG2 VAL A 39 1396 1228 1410 -142 -65 119 C ATOM 277 N TYR A 40 -6.827 3.598 -5.546 1.00 6.72 N ANISOU 277 N TYR A 40 925 816 810 -72 -91 -58 N ATOM 278 CA TYR A 40 -6.926 5.027 -5.225 1.00 7.85 C ANISOU 278 CA TYR A 40 1022 992 968 -11 -76 -190 C ATOM 279 C TYR A 40 -5.571 5.457 -4.661 1.00 7.56 C ANISOU 279 C TYR A 40 1090 691 1091 -111 -178 -31 C ATOM 280 O TYR A 40 -4.971 4.743 -3.868 1.00 8.16 O ANISOU 280 O TYR A 40 1201 1024 875 -121 -199 242 O ATOM 281 CB TYR A 40 -7.990 5.256 -4.149 1.00 7.77 C ANISOU 281 CB TYR A 40 958 1036 955 -202 -22 -59 C ATOM 282 CG TYR A 40 -9.376 4.825 -4.584 1.00 7.32 C ANISOU 282 CG TYR A 40 925 949 907 -209 -13 -11 C ATOM 283 CD1 TYR A 40 -9.793 3.499 -4.468 1.00 8.77 C ANISOU 283 CD1 TYR A 40 1126 1164 1041 -394 109 116 C ATOM 284 CD2 TYR A 40 -10.261 5.751 -5.125 1.00 8.83 C ANISOU 284 CD2 TYR A 40 1056 1204 1092 -80 -177 -58 C ATOM 285 CE1 TYR A 40 -11.075 3.119 -4.872 1.00 7.99 C ANISOU 285 CE1 TYR A 40 1017 1057 962 -230 84 105 C ATOM 286 CE2 TYR A 40 -11.535 5.390 -5.556 1.00 10.14 C ANISOU 286 CE2 TYR A 40 1230 1301 1321 -244 -282 -34 C ATOM 287 CZ TYR A 40 -11.942 4.078 -5.382 1.00 8.97 C ANISOU 287 CZ TYR A 40 895 1144 1370 -72 8 117 C ATOM 288 OH TYR A 40 -13.175 3.703 -5.816 1.00 11.95 O ANISOU 288 OH TYR A 40 1182 1673 1684 -166 -201 -11 O ATOM 289 N TYR A 41 -5.096 6.643 -5.057 1.00 8.55 N ANISOU 289 N TYR A 41 1157 918 1173 -268 -51 43 N ATOM 290 CA TYR A 41 -3.775 7.062 -4.618 1.00 8.92 C ANISOU 290 CA TYR A 41 1087 962 1339 -190 67 -134 C ATOM 291 C TYR A 41 -3.719 8.569 -4.546 1.00 8.22 C ANISOU 291 C TYR A 41 1025 963 1135 -141 -47 213 C ATOM 292 O TYR A 41 -4.446 9.279 -5.272 1.00 8.84 O ANISOU 292 O TYR A 41 1181 994 1183 -156 -119 146 O ATOM 293 CB TYR A 41 -2.690 6.511 -5.560 1.00 10.14 C ANISOU 293 CB TYR A 41 1339 1368 1146 -25 151 16 C ATOM 294 CG TYR A 41 -2.776 7.061 -6.974 1.00 9.65 C ANISOU 294 CG TYR A 41 1157 1170 1338 -223 -18 64 C ATOM 295 CD1 TYR A 41 -3.617 6.494 -7.926 1.00 11.49 C ANISOU 295 CD1 TYR A 41 1261 2000 1102 55 -77 89 C ATOM 296 CD2 TYR A 41 -1.991 8.148 -7.342 1.00 11.39 C ANISOU 296 CD2 TYR A 41 1451 1383 1492 -130 331 232 C ATOM 297 CE1 TYR A 41 -3.686 7.017 -9.214 1.00 12.34 C ANISOU 297 CE1 TYR A 41 1654 1729 1303 85 -142 303 C ATOM 298 CE2 TYR A 41 -2.066 8.693 -8.624 1.00 13.13 C ANISOU 298 CE2 TYR A 41 1832 1598 1557 295 380 391 C ATOM 299 CZ TYR A 41 -2.934 8.129 -9.545 1.00 13.24 C ANISOU 299 CZ TYR A 41 1963 1783 1284 166 108 297 C ATOM 300 OH TYR A 41 -2.996 8.611 -10.844 1.00 18.34 O ANISOU 300 OH TYR A 41 2885 2689 1394 447 410 717 O ATOM 301 N PRO A 42 -2.840 9.087 -3.671 1.00 8.37 N ANISOU 301 N PRO A 42 1136 894 1150 -172 -115 219 N ATOM 302 CA PRO A 42 -2.652 10.533 -3.587 1.00 9.30 C ANISOU 302 CA PRO A 42 1187 1158 1186 -463 15 37 C ATOM 303 C PRO A 42 -1.663 10.971 -4.655 1.00 9.29 C ANISOU 303 C PRO A 42 1083 1040 1407 -271 4 46 C ATOM 304 O PRO A 42 -0.647 10.305 -4.892 1.00 10.41 O ANISOU 304 O PRO A 42 1351 1112 1491 -310 183 92 O ATOM 305 CB PRO A 42 -2.078 10.716 -2.181 1.00 9.60 C ANISOU 305 CB PRO A 42 1363 1044 1240 -139 -221 191 C ATOM 306 CG PRO A 42 -1.292 9.448 -1.953 1.00 9.78 C ANISOU 306 CG PRO A 42 1389 1082 1243 -60 -245 -303 C ATOM 307 CD PRO A 42 -2.029 8.347 -2.696 1.00 9.70 C ANISOU 307 CD PRO A 42 1432 1093 1160 -294 -418 106 C ATOM 308 N THR A 43 -1.938 12.125 -5.239 1.00 9.94 N ANISOU 308 N THR A 43 1551 1005 1220 -380 117 133 N ATOM 309 CA THR A 43 -1.053 12.627 -6.291 1.00 11.15 C ANISOU 309 CA THR A 43 1616 1353 1265 -335 84 300 C ATOM 310 C THR A 43 0.021 13.550 -5.718 1.00 10.98 C ANISOU 310 C THR A 43 1443 1490 1236 -390 268 33 C ATOM 311 O THR A 43 0.956 13.910 -6.431 1.00 13.94 O ANISOU 311 O THR A 43 1927 1845 1522 -735 505 -195 O ATOM 312 CB THR A 43 -1.833 13.420 -7.346 1.00 12.02 C ANISOU 312 CB THR A 43 1921 1204 1441 -69 -237 114 C ATOM 313 OG1 THR A 43 -2.457 14.555 -6.728 1.00 13.75 O ANISOU 313 OG1 THR A 43 2017 1517 1688 20 338 411 O ATOM 314 CG2 THR A 43 -2.869 12.569 -8.006 1.00 14.96 C ANISOU 314 CG2 THR A 43 2053 2022 1607 -780 -435 297 C ATOM 315 N ASN A 44 -0.086 13.905 -4.433 1.00 10.32 N ANISOU 315 N ASN A 44 1589 1041 1292 -587 119 -30 N ATOM 316 CA ASN A 44 0.740 14.966 -3.849 1.00 11.10 C ANISOU 316 CA ASN A 44 1474 1270 1472 -412 106 -136 C ATOM 317 C ASN A 44 1.108 14.692 -2.386 1.00 11.78 C ANISOU 317 C ASN A 44 1419 1468 1585 -598 79 -20 C ATOM 318 O ASN A 44 1.255 15.617 -1.602 1.00 15.47 O ANISOU 318 O ASN A 44 1991 1714 2170 -250 -97 -547 O ATOM 319 CB ASN A 44 0.104 16.349 -4.054 1.00 13.03 C ANISOU 319 CB ASN A 44 1665 1520 1764 -308 231 -30 C ATOM 320 CG ASN A 44 -1.221 16.536 -3.327 1.00 10.97 C ANISOU 320 CG ASN A 44 1438 1147 1581 -409 69 224 C ATOM 321 OD1 ASN A 44 -1.618 17.681 -3.033 1.00 16.51 O ANISOU 321 OD1 ASN A 44 2387 1303 2580 -191 392 -177 O ATOM 322 ND2 ASN A 44 -1.929 15.465 -3.073 1.00 9.61 N ANISOU 322 ND2 ASN A 44 1435 1028 1187 -491 282 29 N ATOM 323 N ALA A 45 1.327 13.429 -2.026 1.00 12.45 N ANISOU 323 N ALA A 45 1656 1497 1578 -220 153 11 N ATOM 324 CA ALA A 45 1.686 13.091 -0.629 1.00 14.99 C ANISOU 324 CA ALA A 45 2307 1741 1645 -155 -437 -238 C ATOM 325 C ALA A 45 3.074 13.524 -0.193 1.00 20.15 C ANISOU 325 C ALA A 45 2638 1762 3254 -301 -166 -225 C ATOM 326 O ALA A 45 3.343 13.626 1.019 1.00 22.17 O ANISOU 326 O ALA A 45 3265 2396 2760 -160 -905 -250 O ATOM 327 CB ALA A 45 1.517 11.618 -0.347 1.00 15.42 C ANISOU 327 CB ALA A 45 2490 1749 1618 -363 -147 -54 C ATOM 328 N GLY A 46 3.992 13.682 -1.136 1.00 17.47 N ANISOU 328 N GLY A 46 1632 1184 3818 -269 233 261 N ATOM 329 CA GLY A 46 5.333 14.174 -0.766 1.00 19.78 C ANISOU 329 CA GLY A 46 2141 1502 3873 -820 -529 423 C ATOM 330 C GLY A 46 6.344 13.145 -0.245 1.00 18.58 C ANISOU 330 C GLY A 46 1886 2130 3041 -679 -89 760 C ATOM 331 O GLY A 46 7.514 13.428 -0.002 1.00 21.78 O ANISOU 331 O GLY A 46 2175 2123 3975 -852 -340 59 O ATOM 332 N GLY A 47 5.936 11.902 -0.187 1.00 14.75 N ANISOU 332 N GLY A 47 1684 1553 2368 -369 515 129 N ATOM 333 CA GLY A 47 6.824 10.786 0.106 1.00 12.11 C ANISOU 333 CA GLY A 47 1247 1390 1964 -601 367 -81 C ATOM 334 C GLY A 47 6.045 9.506 -0.160 1.00 9.73 C ANISOU 334 C GLY A 47 1018 1410 1267 -381 208 83 C ATOM 335 O GLY A 47 4.844 9.546 -0.420 1.00 11.30 O ANISOU 335 O GLY A 47 1162 1579 1549 -308 0 -113 O ATOM 336 N THR A 48 6.723 8.372 -0.106 1.00 9.46 N ANISOU 336 N THR A 48 1156 1126 1310 -275 225 31 N ATOM 337 CA THR A 48 6.033 7.096 -0.284 1.00 10.09 C ANISOU 337 CA THR A 48 1125 1299 1409 -364 301 68 C ATOM 338 C THR A 48 5.046 6.873 0.864 1.00 9.20 C ANISOU 338 C THR A 48 1165 1316 1011 -308 30 -142 C ATOM 339 O THR A 48 5.264 7.324 2.002 1.00 9.89 O ANISOU 339 O THR A 48 1160 1423 1175 -469 112 -138 O ATOM 340 CB THR A 48 7.018 5.920 -0.386 1.00 10.77 C ANISOU 340 CB THR A 48 1382 1494 1215 -148 177 61 C ATOM 341 OG1 THR A 48 7.901 5.920 0.760 1.00 11.44 O ANISOU 341 OG1 THR A 48 1361 1598 1386 -206 142 -48 O ATOM 342 CG2 THR A 48 7.852 6.018 -1.673 1.00 13.80 C ANISOU 342 CG2 THR A 48 1520 2328 1394 -79 399 85 C ATOM 343 N VAL A 49 3.975 6.143 0.569 1.00 8.83 N ANISOU 343 N VAL A 49 990 1040 1323 -336 202 -115 N ATOM 344 CA VAL A 49 2.908 5.899 1.562 1.00 7.72 C ANISOU 344 CA VAL A 49 950 973 1010 -183 48 -9 C ATOM 345 C VAL A 49 2.646 4.401 1.655 1.00 7.52 C ANISOU 345 C VAL A 49 1025 917 914 -160 140 -85 C ATOM 346 O VAL A 49 2.986 3.626 0.752 1.00 7.87 O ANISOU 346 O VAL A 49 929 1060 999 -164 76 -143 O ATOM 347 CB VAL A 49 1.626 6.685 1.225 1.00 7.58 C ANISOU 347 CB VAL A 49 966 887 1027 -97 -134 -159 C ATOM 348 CG1 VAL A 49 1.885 8.184 1.276 1.00 10.42 C ANISOU 348 CG1 VAL A 49 1362 1078 1518 -362 234 -32 C ATOM 349 CG2 VAL A 49 1.036 6.272 -0.132 1.00 9.10 C ANISOU 349 CG2 VAL A 49 1187 1256 1014 -73 -76 4 C ATOM 350 N GLY A 50 2.000 4.004 2.745 1.00 7.31 N ANISOU 350 N GLY A 50 854 982 938 -270 -12 96 N ATOM 351 CA GLY A 50 1.586 2.629 2.893 1.00 8.12 C ANISOU 351 CA GLY A 50 1002 926 1157 -342 -278 -75 C ATOM 352 C GLY A 50 0.395 2.279 2.018 1.00 6.04 C ANISOU 352 C GLY A 50 660 850 784 -92 20 -42 C ATOM 353 O GLY A 50 -0.286 3.163 1.460 1.00 7.62 O ANISOU 353 O GLY A 50 948 865 1079 -99 -195 17 O ATOM 354 N ALA A 51 0.145 0.976 1.889 1.00 6.52 N ANISOU 354 N ALA A 51 816 805 856 -277 0 -70 N ATOM 355 CA ALA A 51 -0.970 0.480 1.062 1.00 6.13 C ANISOU 355 CA ALA A 51 744 847 735 -161 -67 8 C ATOM 356 C ALA A 51 -1.954 -0.317 1.888 1.00 5.79 C ANISOU 356 C ALA A 51 690 809 700 32 -42 -36 C ATOM 357 O ALA A 51 -1.562 -1.047 2.807 1.00 6.62 O ANISOU 357 O ALA A 51 751 882 881 -18 -28 -17 O ATOM 358 CB ALA A 51 -0.456 -0.375 -0.101 1.00 8.69 C ANISOU 358 CB ALA A 51 1200 1164 939 -222 249 -262 C ATOM 359 N ILE A 52 -3.243 -0.178 1.546 1.00 6.14 N ANISOU 359 N ILE A 52 607 904 822 -156 -39 -135 N ATOM 360 CA ILE A 52 -4.327 -0.845 2.276 1.00 5.95 C ANISOU 360 CA ILE A 52 539 908 813 -109 -69 8 C ATOM 361 C ILE A 52 -5.203 -1.570 1.261 1.00 6.23 C ANISOU 361 C ILE A 52 687 808 869 -2 -88 68 C ATOM 362 O ILE A 52 -5.568 -0.982 0.245 1.00 7.16 O ANISOU 362 O ILE A 52 933 935 849 -102 -213 172 O ATOM 363 CB ILE A 52 -5.194 0.197 3.038 1.00 6.60 C ANISOU 363 CB ILE A 52 743 826 937 -205 12 -169 C ATOM 364 CG1 ILE A 52 -4.340 0.980 4.058 1.00 7.23 C ANISOU 364 CG1 ILE A 52 839 919 985 -81 -107 -272 C ATOM 365 CG2 ILE A 52 -6.366 -0.484 3.703 1.00 8.24 C ANISOU 365 CG2 ILE A 52 990 1123 1018 -354 25 -14 C ATOM 366 CD1 ILE A 52 -5.010 2.221 4.612 1.00 8.40 C ANISOU 366 CD1 ILE A 52 978 1113 1097 122 204 -296 C ATOM 367 N ALA A 53 -5.530 -2.833 1.535 1.00 6.18 N ANISOU 367 N ALA A 53 752 796 800 -173 25 13 N ATOM 368 CA ALA A 53 -6.417 -3.615 0.654 1.00 5.47 C ANISOU 368 CA ALA A 53 573 743 763 -65 109 -127 C ATOM 369 C ALA A 53 -7.719 -3.896 1.368 1.00 5.47 C ANISOU 369 C ALA A 53 683 646 747 -48 21 158 C ATOM 370 O ALA A 53 -7.711 -4.345 2.529 1.00 6.20 O ANISOU 370 O ALA A 53 784 857 715 -56 29 132 O ATOM 371 CB ALA A 53 -5.773 -4.918 0.241 1.00 6.90 C ANISOU 371 CB ALA A 53 930 764 925 51 145 15 C ATOM 372 N ILE A 54 -8.824 -3.660 0.666 1.00 5.88 N ANISOU 372 N ILE A 54 562 817 852 -69 -70 -148 N ATOM 373 CA ILE A 54 -10.165 -3.723 1.270 1.00 6.16 C ANISOU 373 CA ILE A 54 550 839 950 40 -106 -41 C ATOM 374 C ILE A 54 -11.064 -4.674 0.498 1.00 6.07 C ANISOU 374 C ILE A 54 792 741 771 -44 95 -34 C ATOM 375 O ILE A 54 -11.132 -4.619 -0.749 1.00 6.87 O ANISOU 375 O ILE A 54 844 996 769 -105 25 19 O ATOM 376 CB ILE A 54 -10.813 -2.315 1.291 1.00 6.08 C ANISOU 376 CB ILE A 54 641 761 907 -10 6 -88 C ATOM 377 CG1 ILE A 54 -9.780 -1.264 1.766 1.00 6.62 C ANISOU 377 CG1 ILE A 54 845 667 1003 -34 -151 13 C ATOM 378 CG2 ILE A 54 -12.065 -2.366 2.168 1.00 6.94 C ANISOU 378 CG2 ILE A 54 691 948 996 -98 140 -27 C ATOM 379 CD1 ILE A 54 -10.398 0.096 2.072 1.00 8.36 C ANISOU 379 CD1 ILE A 54 1098 852 1226 60 37 53 C ATOM 380 N VAL A 55 -11.717 -5.579 1.242 1.00 6.41 N ANISOU 380 N VAL A 55 797 780 855 -148 1 46 N ATOM 381 CA VAL A 55 -12.499 -6.655 0.620 1.00 6.70 C ANISOU 381 CA VAL A 55 720 760 1066 -115 -8 -121 C ATOM 382 C VAL A 55 -13.955 -6.569 1.079 1.00 6.87 C ANISOU 382 C VAL A 55 868 910 830 -148 0 29 C ATOM 383 O VAL A 55 -14.226 -6.339 2.262 1.00 7.92 O ANISOU 383 O VAL A 55 900 1228 882 -268 116 -154 O ATOM 384 CB VAL A 55 -11.937 -8.023 1.009 1.00 8.10 C ANISOU 384 CB VAL A 55 977 998 1103 -96 -266 13 C ATOM 385 CG1 VAL A 55 -12.677 -9.146 0.310 1.00 10.10 C ANISOU 385 CG1 VAL A 55 1311 912 1612 -226 -482 24 C ATOM 386 CG2 VAL A 55 -10.447 -8.100 0.748 1.00 11.79 C ANISOU 386 CG2 VAL A 55 1203 1726 1550 26 276 -163 C ATOM 387 N PRO A 56 -14.914 -6.788 0.164 1.00 6.82 N ANISOU 387 N PRO A 56 677 1063 850 -94 65 -222 N ATOM 388 CA PRO A 56 -16.326 -6.741 0.545 1.00 7.41 C ANISOU 388 CA PRO A 56 642 1265 907 -175 133 18 C ATOM 389 C PRO A 56 -16.789 -7.978 1.300 1.00 7.46 C ANISOU 389 C PRO A 56 775 1037 1021 -74 20 -130 C ATOM 390 O PRO A 56 -16.010 -8.920 1.519 1.00 7.83 O ANISOU 390 O PRO A 56 997 967 1010 -157 -2 -150 O ATOM 391 CB PRO A 56 -17.066 -6.680 -0.806 1.00 9.88 C ANISOU 391 CB PRO A 56 1017 1669 1066 5 -23 215 C ATOM 392 CG PRO A 56 -16.040 -6.450 -1.850 1.00 11.10 C ANISOU 392 CG PRO A 56 980 2109 1125 139 -77 -94 C ATOM 393 CD PRO A 56 -14.745 -6.964 -1.287 1.00 8.35 C ANISOU 393 CD PRO A 56 911 1523 738 -13 -158 -57 C ATOM 394 N GLY A 57 -18.080 -7.977 1.648 1.00 8.31 N ANISOU 394 N GLY A 57 868 1256 1031 -331 45 -146 N ATOM 395 CA GLY A 57 -18.720 -9.139 2.272 1.00 9.90 C ANISOU 395 CA GLY A 57 1177 1270 1314 -519 -87 25 C ATOM 396 C GLY A 57 -19.344 -10.086 1.260 1.00 7.31 C ANISOU 396 C GLY A 57 726 1123 927 -226 31 84 C ATOM 397 O GLY A 57 -19.278 -9.868 0.048 1.00 8.15 O ANISOU 397 O GLY A 57 887 1206 1002 -94 -10 13 O ATOM 398 N TYR A 58 -19.967 -11.140 1.778 1.00 8.13 N ANISOU 398 N TYR A 58 875 974 1239 -319 26 -113 N ATOM 399 CA TYR A 58 -20.636 -12.150 0.969 1.00 7.96 C ANISOU 399 CA TYR A 58 930 1038 1054 -142 -178 -83 C ATOM 400 C TYR A 58 -21.667 -11.477 0.069 1.00 7.35 C ANISOU 400 C TYR A 58 774 809 1208 -61 -42 -38 C ATOM 401 O TYR A 58 -22.465 -10.671 0.539 1.00 8.39 O ANISOU 401 O TYR A 58 827 1176 1183 54 59 -149 O ATOM 402 CB TYR A 58 -21.325 -13.137 1.923 1.00 8.52 C ANISOU 402 CB TYR A 58 1089 914 1233 -296 48 -102 C ATOM 403 CG TYR A 58 -21.745 -14.440 1.285 1.00 7.49 C ANISOU 403 CG TYR A 58 887 907 1051 12 -26 -40 C ATOM 404 CD1 TYR A 58 -20.786 -15.349 0.858 1.00 9.33 C ANISOU 404 CD1 TYR A 58 1094 1160 1290 211 20 -177 C ATOM 405 CD2 TYR A 58 -23.097 -14.809 1.213 1.00 8.52 C ANISOU 405 CD2 TYR A 58 1077 1104 1055 -261 27 28 C ATOM 406 CE1 TYR A 58 -21.156 -16.614 0.404 1.00 9.36 C ANISOU 406 CE1 TYR A 58 1082 1063 1409 63 -78 57 C ATOM 407 CE2 TYR A 58 -23.480 -16.040 0.721 1.00 8.10 C ANISOU 407 CE2 TYR A 58 1099 1018 958 -52 168 -104 C ATOM 408 CZ TYR A 58 -22.501 -16.953 0.360 1.00 8.35 C ANISOU 408 CZ TYR A 58 1139 813 1218 -86 190 111 C ATOM 409 OH TYR A 58 -22.866 -18.204 -0.076 1.00 10.35 O ANISOU 409 OH TYR A 58 1472 922 1538 -209 151 -85 O ATOM 410 N THR A 59 -21.658 -11.853 -1.205 1.00 8.11 N ANISOU 410 N THR A 59 935 964 1182 -182 -149 -166 N ATOM 411 CA THR A 59 -22.521 -11.303 -2.280 1.00 8.49 C ANISOU 411 CA THR A 59 806 1206 1213 -142 -179 -60 C ATOM 412 C THR A 59 -22.100 -9.938 -2.774 1.00 8.89 C ANISOU 412 C THR A 59 1010 1281 1084 -324 -168 69 C ATOM 413 O THR A 59 -22.635 -9.447 -3.768 1.00 10.50 O ANISOU 413 O THR A 59 1340 1283 1365 -318 -145 121 O ATOM 414 CB THR A 59 -24.049 -11.271 -2.004 1.00 8.94 C ANISOU 414 CB THR A 59 914 1244 1239 -276 7 -150 C ATOM 415 OG1 THR A 59 -24.368 -10.122 -1.205 1.00 10.16 O ANISOU 415 OG1 THR A 59 1021 1428 1409 5 89 -146 O ATOM 416 CG2 THR A 59 -24.562 -12.547 -1.360 1.00 11.47 C ANISOU 416 CG2 THR A 59 1445 1267 1645 -374 6 124 C ATOM 417 N ALA A 60 -21.224 -9.259 -2.040 1.00 7.91 N ANISOU 417 N ALA A 60 914 961 1128 -168 34 -182 N ATOM 418 CA ALA A 60 -21.038 -7.817 -2.258 1.00 8.31 C ANISOU 418 CA ALA A 60 1024 957 1177 -112 146 -139 C ATOM 419 C ALA A 60 -19.850 -7.515 -3.178 1.00 8.23 C ANISOU 419 C ALA A 60 780 1121 1226 33 -6 -124 C ATOM 420 O ALA A 60 -18.994 -8.382 -3.438 1.00 7.56 O ANISOU 420 O ALA A 60 805 919 1146 -39 67 142 O ATOM 421 CB ALA A 60 -20.899 -7.092 -0.923 1.00 9.61 C ANISOU 421 CB ALA A 60 1186 1285 1181 -61 123 -387 C ATOM 422 N ARG A 61 -19.809 -6.276 -3.643 1.00 8.66 N ANISOU 422 N ARG A 61 1003 1088 1197 -73 36 -7 N ATOM 423 CA ARG A 61 -18.809 -5.821 -4.585 1.00 8.70 C ANISOU 423 CA ARG A 61 1087 922 1294 -173 58 7 C ATOM 424 C ARG A 61 -18.108 -4.571 -4.057 1.00 8.25 C ANISOU 424 C ARG A 61 856 1148 1130 -52 123 -156 C ATOM 425 O ARG A 61 -18.393 -4.122 -2.935 1.00 8.25 O ANISOU 425 O ARG A 61 1037 1081 1017 -26 39 -81 O ATOM 426 CB ARG A 61 -19.444 -5.590 -5.954 1.00 10.47 C ANISOU 426 CB ARG A 61 1494 1091 1394 -390 -248 -82 C ATOM 427 CG ARG A 61 -19.886 -6.915 -6.585 1.00 11.30 C ANISOU 427 CG ARG A 61 1631 1304 1359 -593 -169 -49 C ATOM 428 CD ARG A 61 -20.534 -6.664 -7.932 1.00 14.93 C ANISOU 428 CD ARG A 61 2644 1641 1387 -704 -603 108 C ATOM 429 NE ARG A 61 -20.747 -7.922 -8.652 1.00 17.73 N ANISOU 429 NE ARG A 61 2822 1897 2016 -1155 -402 -182 N ATOM 430 CZ ARG A 61 -21.758 -8.758 -8.460 1.00 14.78 C ANISOU 430 CZ ARG A 61 2081 1854 1680 -430 -94 -129 C ATOM 431 NH1 ARG A 61 -22.696 -8.475 -7.556 1.00 17.16 N ANISOU 431 NH1 ARG A 61 2017 1971 2532 74 -279 -387 N ATOM 432 NH2 ARG A 61 -21.846 -9.857 -9.215 1.00 17.04 N ANISOU 432 NH2 ARG A 61 2669 2004 1801 -910 -307 -448 N ATOM 433 N GLN A 62 -17.256 -3.979 -4.893 1.00 8.60 N ANISOU 433 N GLN A 62 971 1112 1183 -233 -50 -12 N ATOM 434 CA GLN A 62 -16.489 -2.813 -4.467 1.00 7.90 C ANISOU 434 CA GLN A 62 892 984 1126 -212 145 -260 C ATOM 435 C GLN A 62 -17.404 -1.692 -3.992 1.00 7.98 C ANISOU 435 C GLN A 62 909 1033 1088 0 -149 -92 C ATOM 436 O GLN A 62 -17.022 -0.935 -3.100 1.00 8.54 O ANISOU 436 O GLN A 62 990 1159 1095 -113 -8 -254 O ATOM 437 CB GLN A 62 -15.608 -2.315 -5.608 1.00 8.40 C ANISOU 437 CB GLN A 62 939 1097 1154 41 186 27 C ATOM 438 CG GLN A 62 -14.459 -3.260 -5.897 1.00 8.62 C ANISOU 438 CG GLN A 62 792 1185 1297 -33 149 -2 C ATOM 439 CD GLN A 62 -13.660 -2.783 -7.089 1.00 7.92 C ANISOU 439 CD GLN A 62 1107 965 937 -70 -55 54 C ATOM 440 OE1 GLN A 62 -13.650 -3.426 -8.175 1.00 12.55 O ANISOU 440 OE1 GLN A 62 1895 1640 1230 -4 -14 -389 O ATOM 441 NE2 GLN A 62 -13.043 -1.653 -6.951 1.00 7.27 N ANISOU 441 NE2 GLN A 62 918 1156 686 -182 84 -64 N ATOM 442 N SER A 63 -18.592 -1.552 -4.574 1.00 8.74 N ANISOU 442 N SER A 63 915 1177 1228 104 -68 77 N ATOM 443 CA ASER A 63 -19.454 -0.437 -4.203 0.50 9.70 C ANISOU 443 CA ASER A 63 1035 1380 1270 186 -220 -212 C ATOM 444 CA BSER A 63 -19.457 -0.444 -4.208 0.50 9.70 C ANISOU 444 CA BSER A 63 1043 1369 1273 190 -205 -191 C ATOM 445 C SER A 63 -19.674 -0.355 -2.692 1.00 8.38 C ANISOU 445 C SER A 63 774 1115 1295 135 156 -54 C ATOM 446 O SER A 63 -19.784 0.733 -2.133 1.00 9.80 O ANISOU 446 O SER A 63 1149 1132 1440 49 -30 -231 O ATOM 447 CB ASER A 63 -20.818 -0.549 -4.900 0.50 11.67 C ANISOU 447 CB ASER A 63 966 1867 1599 106 -201 -142 C ATOM 448 CB BSER A 63 -20.811 -0.597 -4.909 0.50 10.82 C ANISOU 448 CB BSER A 63 959 1547 1603 -56 -140 -24 C ATOM 449 OG ASER A 63 -21.399 -1.827 -4.689 0.50 15.54 O ANISOU 449 OG ASER A 63 1582 2339 1981 -256 -318 41 O ATOM 450 OG BSER A 63 -21.695 0.444 -4.558 0.50 16.06 O ANISOU 450 OG BSER A 63 1725 2362 2015 816 -241 -282 O ATOM 451 N SER A 64 -19.820 -1.503 -2.034 1.00 8.05 N ANISOU 451 N SER A 64 760 1191 1107 -8 -130 -27 N ATOM 452 CA SER A 64 -20.128 -1.528 -0.607 1.00 9.01 C ANISOU 452 CA SER A 64 1055 1164 1202 -119 -113 -64 C ATOM 453 C SER A 64 -19.020 -0.901 0.254 1.00 8.05 C ANISOU 453 C SER A 64 833 1096 1130 213 -104 -118 C ATOM 454 O SER A 64 -19.298 -0.393 1.354 1.00 8.53 O ANISOU 454 O SER A 64 999 1051 1189 78 -28 -85 O ATOM 455 CB SER A 64 -20.390 -2.968 -0.154 1.00 8.76 C ANISOU 455 CB SER A 64 940 1135 1250 15 93 -135 C ATOM 456 OG SER A 64 -19.231 -3.781 -0.270 1.00 8.73 O ANISOU 456 OG SER A 64 991 1100 1223 -24 62 -107 O ATOM 457 N ILE A 65 -17.781 -0.906 -0.251 1.00 7.35 N ANISOU 457 N ILE A 65 693 958 1140 136 -124 -139 N ATOM 458 CA ILE A 65 -16.614 -0.483 0.529 1.00 8.52 C ANISOU 458 CA ILE A 65 882 1074 1280 31 -328 -167 C ATOM 459 C ILE A 65 -15.881 0.688 -0.126 1.00 8.16 C ANISOU 459 C ILE A 65 957 1029 1114 -82 -32 -229 C ATOM 460 O ILE A 65 -14.907 1.195 0.436 1.00 9.61 O ANISOU 460 O ILE A 65 976 1159 1516 -36 -165 -231 O ATOM 461 CB ILE A 65 -15.633 -1.654 0.773 1.00 11.35 C ANISOU 461 CB ILE A 65 1085 1341 1884 231 -463 -34 C ATOM 462 CG1 ILE A 65 -15.228 -2.294 -0.609 1.00 17.42 C ANISOU 462 CG1 ILE A 65 2206 1622 2788 951 -962 -1521 C ATOM 463 CG2 ILE A 65 -16.241 -2.577 1.824 1.00 13.86 C ANISOU 463 CG2 ILE A 65 1669 1408 2187 -139 -591 101 C ATOM 464 CD1 ILE A 65 -13.996 -3.127 -0.755 1.00 15.51 C ANISOU 464 CD1 ILE A 65 1070 2852 1970 -210 174 -681 C ATOM 465 N LYS A 66 -16.359 1.149 -1.285 1.00 7.85 N ANISOU 465 N LYS A 66 977 886 1116 -61 -52 -86 N ATOM 466 CA LYS A 66 -15.575 2.098 -2.089 1.00 9.23 C ANISOU 466 CA LYS A 66 1396 892 1219 -143 4 -228 C ATOM 467 C LYS A 66 -15.329 3.427 -1.404 1.00 8.95 C ANISOU 467 C LYS A 66 986 1027 1386 -132 7 -276 C ATOM 468 O LYS A 66 -14.338 4.084 -1.708 1.00 8.73 O ANISOU 468 O LYS A 66 1125 1138 1053 -189 57 -130 O ATOM 469 CB LYS A 66 -16.168 2.274 -3.494 1.00 14.21 C ANISOU 469 CB LYS A 66 2458 1800 1140 -680 -39 -286 C ATOM 470 CG LYS A 66 -17.479 3.022 -3.627 1.00 19.99 C ANISOU 470 CG LYS A 66 3173 2392 2028 -588 -574 -19 C ATOM 471 CD LYS A 66 -17.817 3.214 -5.127 1.00 27.67 C ANISOU 471 CD LYS A 66 5198 3434 1878 -422 -1268 -176 C ATOM 472 CE LYS A 66 -18.976 4.169 -5.367 1.00 50.30 C ANISOU 472 CE LYS A 66 4638 5999 8472 -120 -316 399 C ATOM 473 NZ LYS A 66 -20.133 3.909 -4.464 1.00 62.46 N ANISOU 473 NZ LYS A 66 6866 8520 8344 -871 -347 -4121 N ATOM 474 N TRP A 67 -16.223 3.859 -0.505 1.00 8.03 N ANISOU 474 N TRP A 67 1116 1022 911 57 -36 -148 N ATOM 475 CA TRP A 67 -16.033 5.194 0.090 1.00 7.78 C ANISOU 475 CA TRP A 67 930 1070 956 75 26 -170 C ATOM 476 C TRP A 67 -14.676 5.301 0.798 1.00 6.71 C ANISOU 476 C TRP A 67 964 745 838 22 -61 103 C ATOM 477 O TRP A 67 -14.113 6.388 0.939 1.00 8.34 O ANISOU 477 O TRP A 67 1145 843 1179 -139 0 -31 O ATOM 478 CB TRP A 67 -17.196 5.549 1.042 1.00 8.22 C ANISOU 478 CB TRP A 67 920 1255 946 261 9 96 C ATOM 479 CG TRP A 67 -17.118 4.841 2.381 1.00 8.17 C ANISOU 479 CG TRP A 67 979 994 1131 57 124 31 C ATOM 480 CD1 TRP A 67 -17.463 3.545 2.670 1.00 7.95 C ANISOU 480 CD1 TRP A 67 889 1058 1072 187 70 215 C ATOM 481 CD2 TRP A 67 -16.773 5.457 3.620 1.00 7.59 C ANISOU 481 CD2 TRP A 67 840 936 1108 219 -54 -97 C ATOM 482 NE1 TRP A 67 -17.287 3.301 4.015 1.00 8.00 N ANISOU 482 NE1 TRP A 67 1087 926 1026 98 29 -75 N ATOM 483 CE2 TRP A 67 -16.871 4.463 4.623 1.00 7.92 C ANISOU 483 CE2 TRP A 67 882 1088 1036 255 6 -101 C ATOM 484 CE3 TRP A 67 -16.379 6.750 3.986 1.00 8.94 C ANISOU 484 CE3 TRP A 67 1095 1047 1254 80 -72 -66 C ATOM 485 CZ2 TRP A 67 -16.630 4.734 5.962 1.00 8.43 C ANISOU 485 CZ2 TRP A 67 982 1167 1054 265 -26 9 C ATOM 486 CZ3 TRP A 67 -16.098 7.003 5.334 1.00 9.16 C ANISOU 486 CZ3 TRP A 67 1293 1065 1119 -13 -34 -66 C ATOM 487 CH2 TRP A 67 -16.232 5.999 6.303 1.00 8.89 C ANISOU 487 CH2 TRP A 67 948 1244 1185 118 -117 -19 C ATOM 488 N TRP A 68 -14.175 4.176 1.313 1.00 6.37 N ANISOU 488 N TRP A 68 879 725 813 64 -33 144 N ATOM 489 CA TRP A 68 -12.886 4.166 1.995 1.00 6.90 C ANISOU 489 CA TRP A 68 785 935 902 82 9 239 C ATOM 490 C TRP A 68 -11.743 4.562 1.057 1.00 6.37 C ANISOU 490 C TRP A 68 780 709 931 6 -25 -48 C ATOM 491 O TRP A 68 -10.711 5.005 1.529 1.00 7.93 O ANISOU 491 O TRP A 68 973 923 1117 -195 -42 -90 O ATOM 492 CB TRP A 68 -12.590 2.764 2.543 1.00 7.20 C ANISOU 492 CB TRP A 68 1075 790 869 25 71 113 C ATOM 493 CG TRP A 68 -13.324 2.449 3.805 1.00 6.65 C ANISOU 493 CG TRP A 68 784 796 947 62 -32 71 C ATOM 494 CD1 TRP A 68 -14.213 1.424 4.006 1.00 7.13 C ANISOU 494 CD1 TRP A 68 901 775 1033 146 -28 210 C ATOM 495 CD2 TRP A 68 -13.157 3.099 5.081 1.00 6.85 C ANISOU 495 CD2 TRP A 68 905 824 873 55 -40 39 C ATOM 496 NE1 TRP A 68 -14.588 1.386 5.333 1.00 7.34 N ANISOU 496 NE1 TRP A 68 984 907 897 25 -71 -68 N ATOM 497 CE2 TRP A 68 -13.947 2.391 6.017 1.00 6.66 C ANISOU 497 CE2 TRP A 68 759 915 853 56 11 -119 C ATOM 498 CE3 TRP A 68 -12.364 4.181 5.535 1.00 8.39 C ANISOU 498 CE3 TRP A 68 1083 935 1168 105 -236 -279 C ATOM 499 CZ2 TRP A 68 -13.971 2.712 7.393 1.00 7.50 C ANISOU 499 CZ2 TRP A 68 970 994 884 341 -218 17 C ATOM 500 CZ3 TRP A 68 -12.406 4.521 6.890 1.00 7.94 C ANISOU 500 CZ3 TRP A 68 872 1039 1102 109 -2 -82 C ATOM 501 CH2 TRP A 68 -13.198 3.779 7.812 1.00 7.90 C ANISOU 501 CH2 TRP A 68 860 1023 1118 99 -147 -21 C ATOM 502 N GLY A 69 -11.873 4.316 -0.248 1.00 7.27 N ANISOU 502 N GLY A 69 947 942 873 1 161 -47 N ATOM 503 CA GLY A 69 -10.774 4.567 -1.181 1.00 8.60 C ANISOU 503 CA GLY A 69 1067 995 1204 -330 242 -80 C ATOM 504 C GLY A 69 -10.375 6.032 -1.162 1.00 7.14 C ANISOU 504 C GLY A 69 948 930 831 -87 -53 42 C ATOM 505 O GLY A 69 -9.223 6.364 -0.820 1.00 8.31 O ANISOU 505 O GLY A 69 860 1264 1033 -152 -73 49 O ATOM 506 N PRO A 70 -11.299 6.943 -1.505 1.00 7.67 N ANISOU 506 N PRO A 70 995 901 1018 -88 -49 31 N ATOM 507 CA PRO A 70 -10.906 8.363 -1.484 1.00 9.14 C ANISOU 507 CA PRO A 70 1434 1035 1001 -122 -27 245 C ATOM 508 C PRO A 70 -10.707 8.866 -0.051 1.00 8.21 C ANISOU 508 C PRO A 70 1121 921 1077 -94 -127 96 C ATOM 509 O PRO A 70 -9.819 9.696 0.176 1.00 9.42 O ANISOU 509 O PRO A 70 1163 1060 1353 -108 -71 42 O ATOM 510 CB PRO A 70 -12.113 9.071 -2.140 1.00 11.47 C ANISOU 510 CB PRO A 70 1653 1321 1383 204 -451 45 C ATOM 511 CG PRO A 70 -12.758 7.978 -2.991 1.00 12.33 C ANISOU 511 CG PRO A 70 1975 1150 1556 -308 -371 286 C ATOM 512 CD PRO A 70 -12.581 6.710 -2.208 1.00 9.01 C ANISOU 512 CD PRO A 70 1027 1263 1131 -22 -193 59 C ATOM 513 N ARG A 71 -11.445 8.329 0.924 1.00 8.03 N ANISOU 513 N ARG A 71 1205 1000 843 -40 -124 58 N ATOM 514 CA ARG A 71 -11.322 8.835 2.288 1.00 8.17 C ANISOU 514 CA ARG A 71 915 965 1222 -61 -120 -58 C ATOM 515 C ARG A 71 -9.907 8.576 2.802 1.00 7.69 C ANISOU 515 C ARG A 71 983 781 1156 3 -266 -22 C ATOM 516 O ARG A 71 -9.286 9.464 3.381 1.00 10.01 O ANISOU 516 O ARG A 71 1260 900 1640 -105 -522 -177 O ATOM 517 CB ARG A 71 -12.399 8.239 3.174 1.00 10.30 C ANISOU 517 CB ARG A 71 1264 1584 1065 51 134 29 C ATOM 518 CG ARG A 71 -12.397 8.747 4.619 1.00 10.89 C ANISOU 518 CG ARG A 71 1693 1139 1305 258 95 -222 C ATOM 519 CD ARG A 71 -12.330 10.295 4.729 1.00 13.85 C ANISOU 519 CD ARG A 71 2485 1397 1380 239 334 -297 C ATOM 520 NE ARG A 71 -12.623 10.747 6.114 1.00 12.76 N ANISOU 520 NE ARG A 71 2077 1439 1330 276 245 15 N ATOM 521 CZ ARG A 71 -13.865 10.865 6.577 1.00 12.00 C ANISOU 521 CZ ARG A 71 1581 1521 1454 61 91 152 C ATOM 522 NH1 ARG A 71 -14.909 10.590 5.795 1.00 14.56 N ANISOU 522 NH1 ARG A 71 2272 1672 1585 -327 -77 -91 N ATOM 523 NH2 ARG A 71 -14.090 11.202 7.848 1.00 9.63 N ANISOU 523 NH2 ARG A 71 1232 1273 1152 47 -8 86 N ATOM 524 N LEU A 72 -9.422 7.337 2.693 1.00 7.27 N ANISOU 524 N LEU A 72 911 863 987 107 -56 43 N ATOM 525 CA LEU A 72 -8.072 7.024 3.128 1.00 7.40 C ANISOU 525 CA LEU A 72 948 877 984 90 -4 4 C ATOM 526 C LEU A 72 -7.008 7.606 2.205 1.00 7.48 C ANISOU 526 C LEU A 72 894 952 995 -66 -37 -73 C ATOM 527 O LEU A 72 -6.007 8.152 2.675 1.00 7.86 O ANISOU 527 O LEU A 72 880 928 1177 -138 -147 57 O ATOM 528 CB LEU A 72 -7.886 5.512 3.284 1.00 7.88 C ANISOU 528 CB LEU A 72 1072 770 1148 154 147 97 C ATOM 529 CG LEU A 72 -8.565 4.937 4.537 1.00 8.57 C ANISOU 529 CG LEU A 72 1018 978 1261 63 76 158 C ATOM 530 CD1 LEU A 72 -8.845 3.453 4.343 1.00 10.35 C ANISOU 530 CD1 LEU A 72 1183 912 1836 -122 -56 117 C ATOM 531 CD2 LEU A 72 -7.617 5.135 5.721 1.00 12.13 C ANISOU 531 CD2 LEU A 72 2101 1487 1018 247 -371 232 C ATOM 532 N ALA A 73 -7.196 7.505 0.891 1.00 7.37 N ANISOU 532 N ALA A 73 1021 908 871 -46 27 -22 N ATOM 533 CA ALA A 73 -6.112 7.923 -0.004 1.00 8.08 C ANISOU 533 CA ALA A 73 1063 1035 972 -120 53 19 C ATOM 534 C ALA A 73 -5.852 9.429 0.149 1.00 8.89 C ANISOU 534 C ALA A 73 1084 1098 1195 -78 164 66 C ATOM 535 O ALA A 73 -4.695 9.863 0.066 1.00 9.03 O ANISOU 535 O ALA A 73 1141 1165 1123 -230 -12 42 O ATOM 536 CB ALA A 73 -6.431 7.617 -1.438 1.00 8.83 C ANISOU 536 CB ALA A 73 1269 1226 860 -279 -27 -29 C ATOM 537 N SER A 74 -6.904 10.214 0.454 1.00 7.45 N ANISOU 537 N SER A 74 1214 789 825 -34 -59 42 N ATOM 538 CA SER A 74 -6.743 11.666 0.614 1.00 8.41 C ANISOU 538 CA SER A 74 1383 803 1009 9 -133 -13 C ATOM 539 C SER A 74 -5.996 12.039 1.890 1.00 7.33 C ANISOU 539 C SER A 74 1094 800 890 52 -22 -50 C ATOM 540 O SER A 74 -5.621 13.190 2.046 1.00 9.12 O ANISOU 540 O SER A 74 1333 898 1234 -62 -41 36 O ATOM 541 CB SER A 74 -8.105 12.352 0.599 1.00 8.55 C ANISOU 541 CB SER A 74 1184 992 1069 -70 -40 82 C ATOM 542 OG SER A 74 -8.874 12.012 1.750 1.00 9.86 O ANISOU 542 OG SER A 74 1247 999 1500 19 204 110 O ATOM 543 N HIS A 75 -5.718 11.056 2.755 1.00 8.01 N ANISOU 543 N HIS A 75 1096 939 1007 42 -7 43 N ATOM 544 CA HIS A 75 -4.863 11.285 3.906 1.00 8.10 C ANISOU 544 CA HIS A 75 1127 1047 903 -198 -7 54 C ATOM 545 C HIS A 75 -3.480 10.666 3.750 1.00 9.00 C ANISOU 545 C HIS A 75 1166 1089 1164 6 53 -93 C ATOM 546 O HIS A 75 -2.675 10.759 4.662 1.00 11.56 O ANISOU 546 O HIS A 75 1306 1861 1222 239 -86 -136 O ATOM 547 CB HIS A 75 -5.532 10.753 5.168 1.00 8.61 C ANISOU 547 CB HIS A 75 1185 1096 989 40 254 89 C ATOM 548 CG HIS A 75 -6.658 11.610 5.625 1.00 7.81 C ANISOU 548 CG HIS A 75 1145 888 932 -88 184 -144 C ATOM 549 ND1 HIS A 75 -6.458 12.719 6.423 1.00 8.73 N ANISOU 549 ND1 HIS A 75 1321 992 1001 -107 -110 -237 N ATOM 550 CD2 HIS A 75 -7.989 11.562 5.362 1.00 8.40 C ANISOU 550 CD2 HIS A 75 1132 891 1166 65 80 144 C ATOM 551 CE1 HIS A 75 -7.626 13.289 6.669 1.00 9.92 C ANISOU 551 CE1 HIS A 75 1239 1179 1348 -9 -103 -68 C ATOM 552 NE2 HIS A 75 -8.572 12.603 6.047 1.00 9.41 N ANISOU 552 NE2 HIS A 75 1521 913 1140 -139 -8 166 N ATOM 553 N GLY A 76 -3.189 10.086 2.589 1.00 8.60 N ANISOU 553 N GLY A 76 1125 1007 1136 -179 16 -176 N ATOM 554 CA GLY A 76 -1.820 9.605 2.296 1.00 8.80 C ANISOU 554 CA GLY A 76 1159 993 1189 52 -30 -237 C ATOM 555 C GLY A 76 -1.666 8.098 2.415 1.00 8.13 C ANISOU 555 C GLY A 76 1054 961 1074 -115 -159 -6 C ATOM 556 O GLY A 76 -0.869 7.602 3.211 1.00 8.41 O ANISOU 556 O GLY A 76 1041 1062 1090 -108 -117 -92 O ATOM 557 N PHE A 77 -2.453 7.372 1.611 1.00 8.03 N ANISOU 557 N PHE A 77 1126 976 946 -201 -26 -115 N ATOM 558 CA PHE A 77 -2.370 5.905 1.513 1.00 7.32 C ANISOU 558 CA PHE A 77 980 845 957 -159 82 -162 C ATOM 559 C PHE A 77 -2.683 5.544 0.067 1.00 7.76 C ANISOU 559 C PHE A 77 853 1073 1021 -176 -58 -5 C ATOM 560 O PHE A 77 -3.468 6.235 -0.587 1.00 8.50 O ANISOU 560 O PHE A 77 1166 1054 1009 -24 -137 24 O ATOM 561 CB PHE A 77 -3.416 5.212 2.400 1.00 8.60 C ANISOU 561 CB PHE A 77 1084 1241 941 -186 62 185 C ATOM 562 CG PHE A 77 -3.164 5.425 3.862 1.00 7.94 C ANISOU 562 CG PHE A 77 872 1201 944 -241 -50 104 C ATOM 563 CD1 PHE A 77 -2.142 4.732 4.510 1.00 9.38 C ANISOU 563 CD1 PHE A 77 981 1409 1173 -169 -189 129 C ATOM 564 CD2 PHE A 77 -3.891 6.360 4.566 1.00 9.50 C ANISOU 564 CD2 PHE A 77 1333 1300 975 -103 1 -85 C ATOM 565 CE1 PHE A 77 -1.848 5.003 5.848 1.00 9.55 C ANISOU 565 CE1 PHE A 77 1194 1265 1169 -200 31 77 C ATOM 566 CE2 PHE A 77 -3.611 6.614 5.915 1.00 10.57 C ANISOU 566 CE2 PHE A 77 1370 1640 1004 88 -90 -57 C ATOM 567 CZ PHE A 77 -2.583 5.935 6.538 1.00 9.69 C ANISOU 567 CZ PHE A 77 1200 1450 1029 -125 -124 -100 C ATOM 568 N VAL A 78 -2.116 4.438 -0.398 1.00 7.39 N ANISOU 568 N VAL A 78 919 1016 870 -325 -61 -73 N ATOM 569 CA VAL A 78 -2.602 3.784 -1.622 1.00 7.21 C ANISOU 569 CA VAL A 78 1067 862 809 -193 -50 -85 C ATOM 570 C VAL A 78 -3.612 2.718 -1.212 1.00 7.06 C ANISOU 570 C VAL A 78 945 961 776 -183 -123 94 C ATOM 571 O VAL A 78 -3.322 1.914 -0.331 1.00 9.37 O ANISOU 571 O VAL A 78 1046 1230 1282 -159 -204 538 O ATOM 572 CB VAL A 78 -1.443 3.202 -2.438 1.00 7.91 C ANISOU 572 CB VAL A 78 1016 975 1011 -127 56 -169 C ATOM 573 CG1 VAL A 78 -1.986 2.331 -3.588 1.00 9.81 C ANISOU 573 CG1 VAL A 78 1434 1218 1075 -176 -116 -216 C ATOM 574 CG2 VAL A 78 -0.617 4.358 -3.001 1.00 9.29 C ANISOU 574 CG2 VAL A 78 1226 1247 1053 -381 221 -89 C ATOM 575 N VAL A 79 -4.814 2.771 -1.771 1.00 6.96 N ANISOU 575 N VAL A 79 852 913 878 -140 15 53 N ATOM 576 CA VAL A 79 -5.897 1.895 -1.326 1.00 6.58 C ANISOU 576 CA VAL A 79 896 838 766 -96 -44 -9 C ATOM 577 C VAL A 79 -6.359 1.087 -2.514 1.00 6.41 C ANISOU 577 C VAL A 79 807 860 767 -194 -25 65 C ATOM 578 O VAL A 79 -6.683 1.681 -3.544 1.00 8.29 O ANISOU 578 O VAL A 79 1391 874 883 -187 -230 168 O ATOM 579 CB VAL A 79 -7.087 2.714 -0.755 1.00 7.61 C ANISOU 579 CB VAL A 79 951 922 1016 -35 68 -70 C ATOM 580 CG1 VAL A 79 -8.169 1.742 -0.262 1.00 10.26 C ANISOU 580 CG1 VAL A 79 1118 1380 1397 -264 295 39 C ATOM 581 CG2 VAL A 79 -6.631 3.662 0.358 1.00 9.91 C ANISOU 581 CG2 VAL A 79 1538 1128 1096 -27 -64 -232 C ATOM 582 N ILE A 80 -6.429 -0.236 -2.384 1.00 6.73 N ANISOU 582 N ILE A 80 843 817 894 -179 -175 -83 N ATOM 583 CA ILE A 80 -7.034 -1.056 -3.420 1.00 6.62 C ANISOU 583 CA ILE A 80 854 821 838 -298 4 -112 C ATOM 584 C ILE A 80 -8.308 -1.694 -2.872 1.00 6.43 C ANISOU 584 C ILE A 80 771 959 712 -95 -20 206 C ATOM 585 O ILE A 80 -8.295 -2.339 -1.816 1.00 7.15 O ANISOU 585 O ILE A 80 954 971 789 -48 -19 133 O ATOM 586 CB ILE A 80 -6.045 -2.121 -3.961 1.00 7.30 C ANISOU 586 CB ILE A 80 1051 848 875 0 -178 -35 C ATOM 587 CG1 ILE A 80 -6.676 -2.903 -5.132 1.00 8.62 C ANISOU 587 CG1 ILE A 80 1164 1236 874 -193 74 -133 C ATOM 588 CG2 ILE A 80 -5.484 -3.044 -2.866 1.00 8.64 C ANISOU 588 CG2 ILE A 80 1202 1076 1002 133 -72 130 C ATOM 589 CD1 ILE A 80 -5.677 -3.699 -5.941 1.00 9.39 C ANISOU 589 CD1 ILE A 80 1414 1214 937 114 144 -87 C ATOM 590 N THR A 81 -9.421 -1.439 -3.567 1.00 6.93 N ANISOU 590 N THR A 81 703 1016 911 -85 -69 -13 N ATOM 591 CA THR A 81 -10.682 -2.081 -3.237 1.00 7.19 C ANISOU 591 CA THR A 81 690 869 1171 -166 -81 -104 C ATOM 592 C THR A 81 -10.879 -3.197 -4.242 1.00 6.86 C ANISOU 592 C THR A 81 874 904 828 -204 85 -43 C ATOM 593 O THR A 81 -10.689 -2.979 -5.446 1.00 8.73 O ANISOU 593 O THR A 81 1314 1133 867 -271 40 -5 O ATOM 594 CB THR A 81 -11.863 -1.090 -3.316 1.00 7.30 C ANISOU 594 CB THR A 81 974 990 808 17 -143 37 C ATOM 595 OG1 THR A 81 -11.939 -0.476 -4.618 1.00 8.71 O ANISOU 595 OG1 THR A 81 1044 1258 1006 -81 -151 170 O ATOM 596 CG2 THR A 81 -11.706 0.022 -2.275 1.00 8.59 C ANISOU 596 CG2 THR A 81 1170 1093 998 153 -58 -192 C ATOM 597 N ILE A 82 -11.265 -4.381 -3.778 1.00 6.58 N ANISOU 597 N ILE A 82 843 810 845 -103 -165 -60 N ATOM 598 CA ILE A 82 -11.386 -5.515 -4.702 1.00 7.13 C ANISOU 598 CA ILE A 82 833 857 1017 -40 0 -246 C ATOM 599 C ILE A 82 -12.798 -6.062 -4.818 1.00 7.54 C ANISOU 599 C ILE A 82 848 1096 920 -59 39 -61 C ATOM 600 O ILE A 82 -13.589 -5.991 -3.856 1.00 7.97 O ANISOU 600 O ILE A 82 1000 1087 942 -66 33 -40 O ATOM 601 CB ILE A 82 -10.386 -6.647 -4.381 1.00 6.79 C ANISOU 601 CB ILE A 82 756 809 1014 -35 -5 6 C ATOM 602 CG1 ILE A 82 -10.729 -7.429 -3.100 1.00 8.23 C ANISOU 602 CG1 ILE A 82 1176 901 1049 202 -34 27 C ATOM 603 CG2 ILE A 82 -8.962 -6.096 -4.410 1.00 8.77 C ANISOU 603 CG2 ILE A 82 778 1274 1280 -95 -106 -164 C ATOM 604 CD1 ILE A 82 -9.931 -8.704 -2.947 1.00 10.35 C ANISOU 604 CD1 ILE A 82 1667 1047 1215 450 -153 -16 C ATOM 605 N ASP A 83 -13.053 -6.669 -5.976 1.00 7.16 N ANISOU 605 N ASP A 83 934 964 822 -87 -26 -131 N ATOM 606 CA ASP A 83 -14.073 -7.698 -6.094 1.00 7.62 C ANISOU 606 CA ASP A 83 919 904 1072 -141 -103 -52 C ATOM 607 C ASP A 83 -13.393 -9.051 -6.013 1.00 7.11 C ANISOU 607 C ASP A 83 884 845 972 -110 28 -142 C ATOM 608 O ASP A 83 -12.275 -9.224 -6.531 1.00 8.53 O ANISOU 608 O ASP A 83 910 1165 1164 4 220 -165 O ATOM 609 CB ASP A 83 -14.793 -7.613 -7.429 1.00 9.41 C ANISOU 609 CB ASP A 83 1178 1257 1138 -37 -330 -37 C ATOM 610 CG ASP A 83 -15.668 -6.397 -7.524 1.00 9.40 C ANISOU 610 CG ASP A 83 1144 1330 1096 4 -96 -52 C ATOM 611 OD1 ASP A 83 -16.388 -6.129 -6.544 1.00 11.91 O ANISOU 611 OD1 ASP A 83 1511 1646 1367 159 -1 -84 O ATOM 612 OD2 ASP A 83 -15.544 -5.624 -8.505 1.00 12.74 O ANISOU 612 OD2 ASP A 83 1493 1708 1637 13 -112 162 O ATOM 613 N THR A 84 -14.028 -9.993 -5.337 1.00 7.58 N ANISOU 613 N THR A 84 919 867 1094 -63 61 -36 N ATOM 614 CA THR A 84 -13.484 -11.333 -5.227 1.00 7.83 C ANISOU 614 CA THR A 84 1029 961 985 21 -135 -62 C ATOM 615 C THR A 84 -13.747 -12.158 -6.486 1.00 8.77 C ANISOU 615 C THR A 84 1082 1115 1134 45 -51 37 C ATOM 616 O THR A 84 -14.586 -11.811 -7.330 1.00 8.89 O ANISOU 616 O THR A 84 1119 1254 1004 29 -26 -24 O ATOM 617 CB THR A 84 -14.028 -12.012 -3.961 1.00 8.14 C ANISOU 617 CB THR A 84 970 1044 1077 -86 -30 -88 C ATOM 618 OG1 THR A 84 -15.455 -11.897 -3.943 1.00 8.99 O ANISOU 618 OG1 THR A 84 917 1342 1156 -83 228 -157 O ATOM 619 CG2 THR A 84 -13.487 -11.336 -2.709 1.00 10.26 C ANISOU 619 CG2 THR A 84 1412 1253 1230 -148 -287 -264 C ATOM 620 N ASN A 85 -13.011 -13.256 -6.621 1.00 8.13 N ANISOU 620 N ASN A 85 1046 989 1051 -78 142 -191 N ATOM 621 CA ASN A 85 -13.199 -14.123 -7.774 1.00 9.19 C ANISOU 621 CA ASN A 85 1078 1162 1250 22 -22 -520 C ATOM 622 C ASN A 85 -14.652 -14.557 -7.927 1.00 10.06 C ANISOU 622 C ASN A 85 1020 1652 1150 -93 27 -106 C ATOM 623 O ASN A 85 -15.149 -14.644 -9.051 1.00 12.36 O ANISOU 623 O ASN A 85 1338 2116 1242 -134 -167 -301 O ATOM 624 CB ASN A 85 -12.325 -15.368 -7.638 1.00 9.96 C ANISOU 624 CB ASN A 85 1030 1289 1464 172 97 -261 C ATOM 625 CG ASN A 85 -10.844 -15.071 -7.788 1.00 11.81 C ANISOU 625 CG ASN A 85 1376 1492 1620 -244 -119 -272 C ATOM 626 OD1 ASN A 85 -9.986 -15.672 -7.100 1.00 17.49 O ANISOU 626 OD1 ASN A 85 1738 2198 2708 150 -379 -188 O ATOM 627 ND2 ASN A 85 -10.531 -14.211 -8.690 1.00 11.22 N ANISOU 627 ND2 ASN A 85 1278 1285 1699 -110 487 -333 N ATOM 628 N SER A 86 -15.298 -14.876 -6.807 1.00 8.90 N ANISOU 628 N SER A 86 924 1174 1282 -120 -34 -258 N ATOM 629 CA SER A 86 -16.741 -15.151 -6.780 1.00 9.50 C ANISOU 629 CA SER A 86 945 1327 1336 -30 107 -200 C ATOM 630 C SER A 86 -17.306 -14.301 -5.650 1.00 9.35 C ANISOU 630 C SER A 86 917 1447 1187 31 9 -125 C ATOM 631 O SER A 86 -16.701 -14.214 -4.573 1.00 9.62 O ANISOU 631 O SER A 86 803 1513 1338 -55 -17 -357 O ATOM 632 CB SER A 86 -16.961 -16.644 -6.411 1.00 10.76 C ANISOU 632 CB SER A 86 1008 1110 1970 -171 -15 -325 C ATOM 633 OG SER A 86 -18.293 -16.884 -6.016 1.00 11.39 O ANISOU 633 OG SER A 86 1345 1367 1615 -7 15 -237 O ATOM 634 N THR A 87 -18.515 -13.786 -5.830 1.00 9.30 N ANISOU 634 N THR A 87 797 1253 1484 -95 73 -313 N ATOM 635 CA THR A 87 -19.169 -13.099 -4.727 1.00 9.14 C ANISOU 635 CA THR A 87 1033 1234 1205 204 7 -193 C ATOM 636 C THR A 87 -19.440 -14.032 -3.549 1.00 8.48 C ANISOU 636 C THR A 87 757 1236 1227 -93 -49 -288 C ATOM 637 O THR A 87 -19.782 -13.568 -2.463 1.00 9.75 O ANISOU 637 O THR A 87 829 1527 1346 87 14 -436 O ATOM 638 CB THR A 87 -20.495 -12.410 -5.129 1.00 9.88 C ANISOU 638 CB THR A 87 704 1416 1635 -169 -193 104 C ATOM 639 OG1 THR A 87 -21.424 -13.424 -5.499 1.00 9.97 O ANISOU 639 OG1 THR A 87 959 1325 1502 -161 -114 -232 O ATOM 640 CG2 THR A 87 -20.340 -11.399 -6.268 1.00 10.67 C ANISOU 640 CG2 THR A 87 1114 1454 1484 72 -228 75 C ATOM 641 N LEU A 88 -19.339 -15.349 -3.764 1.00 8.96 N ANISOU 641 N LEU A 88 746 1276 1381 -81 -93 -177 N ATOM 642 CA LEU A 88 -19.703 -16.329 -2.741 1.00 9.54 C ANISOU 642 CA LEU A 88 774 1257 1592 -67 -205 -115 C ATOM 643 C LEU A 88 -18.457 -16.941 -2.088 1.00 8.37 C ANISOU 643 C LEU A 88 966 1142 1071 -47 50 -54 C ATOM 644 O LEU A 88 -18.547 -17.894 -1.325 1.00 9.32 O ANISOU 644 O LEU A 88 976 1100 1465 -93 -50 -135 O ATOM 645 CB LEU A 88 -20.598 -17.425 -3.374 1.00 11.81 C ANISOU 645 CB LEU A 88 1393 1538 1556 -520 -280 142 C ATOM 646 CG LEU A 88 -21.810 -16.871 -4.152 1.00 13.59 C ANISOU 646 CG LEU A 88 1403 1858 1899 -452 -528 114 C ATOM 647 CD1 LEU A 88 -22.651 -17.997 -4.736 1.00 19.73 C ANISOU 647 CD1 LEU A 88 2107 2937 2451 -1710 -891 847 C ATOM 648 CD2 LEU A 88 -22.610 -15.927 -3.252 1.00 15.76 C ANISOU 648 CD2 LEU A 88 864 3350 1774 165 39 730 C ATOM 649 N ASP A 89 -17.305 -16.288 -2.266 1.00 8.84 N ANISOU 649 N ASP A 89 782 1184 1392 -26 -52 -318 N ATOM 650 CA ASP A 89 -16.081 -16.771 -1.588 1.00 8.42 C ANISOU 650 CA ASP A 89 838 1197 1161 -191 -150 39 C ATOM 651 C ASP A 89 -16.191 -16.618 -0.079 1.00 7.62 C ANISOU 651 C ASP A 89 757 919 1219 -135 -103 -123 C ATOM 652 O ASP A 89 -16.813 -15.680 0.416 1.00 9.40 O ANISOU 652 O ASP A 89 1057 988 1525 -125 -3 -151 O ATOM 653 CB ASP A 89 -14.848 -16.007 -2.107 1.00 8.57 C ANISOU 653 CB ASP A 89 848 1206 1199 -218 56 -36 C ATOM 654 CG ASP A 89 -14.475 -16.379 -3.530 1.00 9.55 C ANISOU 654 CG ASP A 89 842 1330 1455 -65 -115 -235 C ATOM 655 OD1 ASP A 89 -14.839 -17.505 -3.969 1.00 11.50 O ANISOU 655 OD1 ASP A 89 1353 1406 1608 -269 76 -366 O ATOM 656 OD2 ASP A 89 -13.876 -15.532 -4.248 1.00 9.72 O ANISOU 656 OD2 ASP A 89 898 1437 1354 -71 -17 -156 O ATOM 657 N GLN A 90 -15.517 -17.509 0.647 1.00 7.63 N ANISOU 657 N GLN A 90 820 972 1107 -185 -226 118 N ATOM 658 CA GLN A 90 -15.522 -17.532 2.092 1.00 8.29 C ANISOU 658 CA GLN A 90 965 1067 1116 -279 -25 107 C ATOM 659 C GLN A 90 -14.343 -16.719 2.663 1.00 7.55 C ANISOU 659 C GLN A 90 789 1018 1058 -33 39 30 C ATOM 660 O GLN A 90 -13.475 -16.281 1.915 1.00 7.99 O ANISOU 660 O GLN A 90 891 944 1201 -190 81 22 O ATOM 661 CB GLN A 90 -15.477 -18.995 2.582 1.00 10.69 C ANISOU 661 CB GLN A 90 1435 955 1672 -323 -108 238 C ATOM 662 CG GLN A 90 -16.693 -19.797 2.136 1.00 13.61 C ANISOU 662 CG GLN A 90 1791 1732 1647 -615 65 -159 C ATOM 663 CD GLN A 90 -17.987 -19.220 2.660 1.00 14.12 C ANISOU 663 CD GLN A 90 1689 1654 2020 -620 -200 362 C ATOM 664 OE1 GLN A 90 -18.943 -18.972 1.887 1.00 21.69 O ANISOU 664 OE1 GLN A 90 2908 2693 2639 -522 -1270 456 O ATOM 665 NE2 GLN A 90 -18.057 -19.034 3.954 1.00 12.35 N ANISOU 665 NE2 GLN A 90 975 1841 1873 -388 -73 127 N ATOM 666 N PRO A 91 -14.284 -16.524 3.994 1.00 8.26 N ANISOU 666 N PRO A 91 1024 956 1157 -175 139 -123 N ATOM 667 CA PRO A 91 -13.239 -15.668 4.557 1.00 8.21 C ANISOU 667 CA PRO A 91 868 1136 1113 -36 -36 -222 C ATOM 668 C PRO A 91 -11.806 -16.067 4.215 1.00 7.34 C ANISOU 668 C PRO A 91 862 758 1169 -71 -53 42 C ATOM 669 O PRO A 91 -10.989 -15.172 3.950 1.00 7.97 O ANISOU 669 O PRO A 91 906 929 1192 -205 34 38 O ATOM 670 CB PRO A 91 -13.511 -15.743 6.072 1.00 8.76 C ANISOU 670 CB PRO A 91 911 1198 1219 -101 186 39 C ATOM 671 CG PRO A 91 -15.019 -15.904 6.142 1.00 8.77 C ANISOU 671 CG PRO A 91 906 1126 1297 -68 113 -10 C ATOM 672 CD PRO A 91 -15.309 -16.873 5.006 1.00 8.54 C ANISOU 672 CD PRO A 91 999 1056 1187 -141 341 -47 C ATOM 673 N SER A 92 -11.454 -17.346 4.249 1.00 7.82 N ANISOU 673 N SER A 92 894 920 1157 111 100 102 N ATOM 674 CA ASER A 92 -10.067 -17.740 3.952 0.50 8.61 C ANISOU 674 CA ASER A 92 915 979 1376 98 121 88 C ATOM 675 CA BSER A 92 -10.070 -17.725 3.967 0.50 8.30 C ANISOU 675 CA BSER A 92 918 890 1343 91 89 70 C ATOM 676 C SER A 92 -9.660 -17.350 2.537 1.00 8.26 C ANISOU 676 C SER A 92 1050 861 1226 64 -38 18 C ATOM 677 O SER A 92 -8.567 -16.810 2.301 1.00 8.95 O ANISOU 677 O SER A 92 1024 1046 1328 -56 55 35 O ATOM 678 CB ASER A 92 -9.880 -19.241 4.167 0.50 12.60 C ANISOU 678 CB ASER A 92 1491 1197 2098 580 632 341 C ATOM 679 CB BSER A 92 -9.863 -19.215 4.226 0.50 11.51 C ANISOU 679 CB BSER A 92 1426 1123 1822 395 322 451 C ATOM 680 OG ASER A 92 -9.903 -19.524 5.547 0.50 15.95 O ANISOU 680 OG ASER A 92 1744 2262 2053 44 589 481 O ATOM 681 OG BSER A 92 -8.535 -19.569 3.930 0.50 13.34 O ANISOU 681 OG BSER A 92 1510 1505 2054 774 248 496 O ATOM 682 N SER A 93 -10.529 -17.625 1.572 1.00 8.39 N ANISOU 682 N SER A 93 1092 1040 1054 85 -79 -81 N ATOM 683 CA SER A 93 -10.289 -17.244 0.191 1.00 7.87 C ANISOU 683 CA SER A 93 1106 835 1049 -193 -141 -156 C ATOM 684 C SER A 93 -10.218 -15.723 0.074 1.00 7.50 C ANISOU 684 C SER A 93 846 842 1160 -26 -34 -109 C ATOM 685 O SER A 93 -9.374 -15.192 -0.659 1.00 8.04 O ANISOU 685 O SER A 93 946 926 1179 -148 3 -116 O ATOM 686 CB SER A 93 -11.431 -17.768 -0.677 1.00 9.95 C ANISOU 686 CB SER A 93 1359 1291 1128 -405 -130 -77 C ATOM 687 OG SER A 93 -11.302 -17.315 -2.004 1.00 12.66 O ANISOU 687 OG SER A 93 2025 1473 1310 -422 -270 -70 O ATOM 688 N ARG A 94 -11.069 -14.999 0.778 1.00 6.81 N ANISOU 688 N ARG A 94 799 786 1001 17 -145 -168 N ATOM 689 CA ARG A 94 -11.046 -13.533 0.787 1.00 7.48 C ANISOU 689 CA ARG A 94 645 849 1347 -88 18 -106 C ATOM 690 C ARG A 94 -9.689 -13.021 1.286 1.00 6.52 C ANISOU 690 C ARG A 94 738 937 800 3 -19 53 C ATOM 691 O ARG A 94 -9.173 -12.104 0.732 1.00 6.84 O ANISOU 691 O ARG A 94 693 938 965 -145 33 23 O ATOM 692 CB ARG A 94 -12.199 -12.954 1.635 1.00 30.00 C ATOM 693 CG ARG A 94 -13.561 -13.133 0.935 1.00 30.00 C ATOM 694 CD ARG A 94 -14.774 -12.612 1.766 1.00 30.00 C ATOM 695 NE ARG A 94 -15.957 -13.102 1.050 1.00 30.00 N ATOM 696 CZ ARG A 94 -16.571 -12.457 0.090 1.00 30.00 C ATOM 697 NH1 ARG A 94 -16.290 -11.209 -0.191 1.00 30.00 N ATOM 698 NH2 ARG A 94 -17.463 -13.123 -0.619 1.00 30.00 N ATOM 699 N SER A 95 -9.179 -13.667 2.320 1.00 6.20 N ANISOU 699 N SER A 95 633 856 865 0 -43 -94 N ATOM 700 CA SER A 95 -7.856 -13.300 2.832 1.00 6.38 C ANISOU 700 CA SER A 95 606 1020 795 5 -88 36 C ATOM 701 C SER A 95 -6.758 -13.529 1.783 1.00 6.13 C ANISOU 701 C SER A 95 683 767 877 29 -56 -61 C ATOM 702 O SER A 95 -5.932 -12.639 1.545 1.00 7.11 O ANISOU 702 O SER A 95 741 996 964 -98 -37 29 O ATOM 703 CB SER A 95 -7.543 -14.111 4.092 1.00 7.38 C ANISOU 703 CB SER A 95 767 984 1050 -106 -289 155 C ATOM 704 OG SER A 95 -6.224 -13.798 4.520 1.00 7.53 O ANISOU 704 OG SER A 95 808 966 1084 -72 -90 -1 O ATOM 705 N SER A 96 -6.763 -14.690 1.121 1.00 7.71 N ANISOU 705 N SER A 96 941 935 1052 161 39 -121 N ATOM 706 CA SER A 96 -5.762 -14.939 0.079 1.00 7.44 C ANISOU 706 CA SER A 96 1031 949 846 -22 142 -45 C ATOM 707 C SER A 96 -5.845 -13.875 -1.002 1.00 7.09 C ANISOU 707 C SER A 96 747 1012 935 34 89 -49 C ATOM 708 O SER A 96 -4.814 -13.402 -1.503 1.00 7.77 O ANISOU 708 O SER A 96 881 1069 999 -132 172 -45 O ATOM 709 CB SER A 96 -5.959 -16.311 -0.525 1.00 9.51 C ANISOU 709 CB SER A 96 1387 781 1444 50 -56 -95 C ATOM 710 OG SER A 96 -5.677 -17.294 0.436 1.00 15.33 O ANISOU 710 OG SER A 96 2224 1630 1968 316 207 404 O ATOM 711 N GLN A 97 -7.063 -13.522 -1.404 1.00 7.08 N ANISOU 711 N GLN A 97 860 867 961 52 -76 -15 N ATOM 712 CA GLN A 97 -7.265 -12.530 -2.454 1.00 6.97 C ANISOU 712 CA GLN A 97 843 959 844 -176 -128 -100 C ATOM 713 C GLN A 97 -6.828 -11.126 -2.020 1.00 6.27 C ANISOU 713 C GLN A 97 669 934 777 -157 -35 -56 C ATOM 714 O GLN A 97 -6.238 -10.372 -2.804 1.00 7.46 O ANISOU 714 O GLN A 97 943 905 984 -202 88 17 O ATOM 715 CB GLN A 97 -8.717 -12.552 -2.903 1.00 7.12 C ANISOU 715 CB GLN A 97 810 1027 866 -167 -131 -161 C ATOM 716 CG GLN A 97 -9.018 -13.861 -3.641 1.00 8.00 C ANISOU 716 CG GLN A 97 887 999 1152 -156 -262 -333 C ATOM 717 CD GLN A 97 -10.480 -13.963 -4.022 1.00 7.22 C ANISOU 717 CD GLN A 97 861 937 945 -88 -34 -78 C ATOM 718 OE1 GLN A 97 -11.237 -14.832 -3.487 1.00 12.14 O ANISOU 718 OE1 GLN A 97 1326 1504 1782 -411 159 84 O ATOM 719 NE2 GLN A 97 -10.891 -13.112 -4.908 1.00 6.71 N ANISOU 719 NE2 GLN A 97 787 807 955 -10 -55 -143 N ATOM 720 N GLN A 98 -7.094 -10.782 -0.765 1.00 6.41 N ANISOU 720 N GLN A 98 782 884 768 55 -42 -151 N ATOM 721 CA GLN A 98 -6.670 -9.520 -0.190 1.00 6.48 C ANISOU 721 CA GLN A 98 722 1069 668 -100 -89 -196 C ATOM 722 C GLN A 98 -5.158 -9.387 -0.218 1.00 6.67 C ANISOU 722 C GLN A 98 837 952 745 -77 -116 102 C ATOM 723 O GLN A 98 -4.609 -8.341 -0.610 1.00 6.67 O ANISOU 723 O GLN A 98 790 897 846 -119 63 -6 O ATOM 724 CB GLN A 98 -7.154 -9.466 1.257 1.00 7.10 C ANISOU 724 CB GLN A 98 829 1044 823 -85 137 -184 C ATOM 725 CG GLN A 98 -6.802 -8.197 2.007 1.00 6.86 C ANISOU 725 CG GLN A 98 831 888 888 -171 58 -105 C ATOM 726 CD GLN A 98 -7.480 -8.179 3.345 1.00 5.62 C ANISOU 726 CD GLN A 98 696 672 766 47 -72 18 C ATOM 727 OE1 GLN A 98 -7.396 -9.167 4.092 1.00 7.44 O ANISOU 727 OE1 GLN A 98 1056 750 1020 162 69 27 O ATOM 728 NE2 GLN A 98 -8.258 -7.138 3.620 1.00 6.33 N ANISOU 728 NE2 GLN A 98 693 803 908 111 -94 -102 N ATOM 729 N MET A 99 -4.469 -10.466 0.153 1.00 6.19 N ANISOU 729 N MET A 99 653 867 830 -79 -113 -23 N ATOM 730 CA MET A 99 -3.003 -10.426 0.146 1.00 6.23 C ANISOU 730 CA MET A 99 593 952 821 2 -7 77 C ATOM 731 C MET A 99 -2.453 -10.426 -1.272 1.00 6.79 C ANISOU 731 C MET A 99 849 770 962 -50 42 -110 C ATOM 732 O MET A 99 -1.428 -9.774 -1.529 1.00 7.81 O ANISOU 732 O MET A 99 822 1052 1092 -105 75 -7 O ATOM 733 CB MET A 99 -2.442 -11.587 0.950 1.00 7.22 C ANISOU 733 CB MET A 99 942 950 849 118 -27 -29 C ATOM 734 CG MET A 99 -2.836 -11.541 2.433 1.00 7.55 C ANISOU 734 CG MET A 99 1000 919 948 36 -62 -51 C ATOM 735 SD MET A 99 -2.540 -9.995 3.279 1.00 7.97 S ANISOU 735 SD MET A 99 860 1139 1027 59 -24 -105 S ATOM 736 CE MET A 99 -0.748 -9.813 3.076 1.00 8.89 C ANISOU 736 CE MET A 99 690 1308 1379 6 84 -258 C ATOM 737 N ALA A 100 -3.114 -11.122 -2.205 1.00 7.00 N ANISOU 737 N ALA A 100 828 908 921 -3 52 -121 N ATOM 738 CA ALA A 100 -2.703 -11.063 -3.602 1.00 7.94 C ANISOU 738 CA ALA A 100 1187 1041 786 -60 68 -118 C ATOM 739 C ALA A 100 -2.834 -9.623 -4.118 1.00 7.29 C ANISOU 739 C ALA A 100 930 1049 789 76 -22 -121 C ATOM 740 O ALA A 100 -2.009 -9.152 -4.897 1.00 8.91 O ANISOU 740 O ALA A 100 1076 1216 1090 -174 239 5 O ATOM 741 CB ALA A 100 -3.544 -12.020 -4.437 1.00 8.93 C ANISOU 741 CB ALA A 100 1135 1075 1180 -258 97 -249 C ATOM 742 N ALA A 101 -3.888 -8.915 -3.699 1.00 6.73 N ANISOU 742 N ALA A 101 829 873 855 -14 -137 -116 N ATOM 743 CA ALA A 101 -4.085 -7.530 -4.121 1.00 7.92 C ANISOU 743 CA ALA A 101 817 928 1263 -112 -126 -43 C ATOM 744 C ALA A 101 -2.974 -6.643 -3.558 1.00 7.39 C ANISOU 744 C ALA A 101 913 951 941 -108 -19 -56 C ATOM 745 O ALA A 101 -2.459 -5.793 -4.276 1.00 7.70 O ANISOU 745 O ALA A 101 868 1079 976 -163 -50 83 O ATOM 746 CB ALA A 101 -5.471 -7.046 -3.674 1.00 9.20 C ANISOU 746 CB ALA A 101 743 1387 1363 -86 -40 -178 C ATOM 747 N LEU A 102 -2.554 -6.869 -2.308 1.00 7.26 N ANISOU 747 N LEU A 102 702 1046 1008 60 -137 -345 N ATOM 748 CA LEU A 102 -1.399 -6.119 -1.782 1.00 6.84 C ANISOU 748 CA LEU A 102 603 1105 887 -4 -79 -81 C ATOM 749 C LEU A 102 -0.138 -6.431 -2.588 1.00 7.07 C ANISOU 749 C LEU A 102 842 907 935 28 -33 -73 C ATOM 750 O LEU A 102 0.652 -5.522 -2.882 1.00 8.32 O ANISOU 750 O LEU A 102 937 1103 1120 -145 5 -31 O ATOM 751 CB LEU A 102 -1.193 -6.422 -0.301 1.00 7.13 C ANISOU 751 CB LEU A 102 700 1174 834 94 -16 -70 C ATOM 752 CG LEU A 102 -2.213 -5.744 0.625 1.00 7.06 C ANISOU 752 CG LEU A 102 912 813 956 156 84 -38 C ATOM 753 CD1 LEU A 102 -2.050 -6.315 2.026 1.00 8.73 C ANISOU 753 CD1 LEU A 102 1096 1354 866 -74 106 -68 C ATOM 754 CD2 LEU A 102 -2.079 -4.230 0.616 1.00 8.50 C ANISOU 754 CD2 LEU A 102 943 915 1369 51 -51 -143 C ATOM 755 N GLY A 103 0.082 -7.708 -2.916 1.00 7.07 N ANISOU 755 N GLY A 103 749 925 1008 90 49 -92 N ATOM 756 CA GLY A 103 1.219 -8.093 -3.756 1.00 8.11 C ANISOU 756 CA GLY A 103 867 1143 1072 169 190 -135 C ATOM 757 C GLY A 103 1.186 -7.363 -5.092 1.00 8.15 C ANISOU 757 C GLY A 103 953 979 1163 41 39 -48 C ATOM 758 O GLY A 103 2.228 -6.893 -5.589 1.00 9.75 O ANISOU 758 O GLY A 103 1141 1332 1228 -268 174 -287 O ATOM 759 N GLN A 104 0.000 -7.239 -5.684 1.00 8.09 N ANISOU 759 N GLN A 104 1134 1081 857 -25 -82 -181 N ATOM 760 CA GLN A 104 -0.113 -6.542 -6.962 1.00 8.02 C ANISOU 760 CA GLN A 104 1113 1106 826 -138 -25 -167 C ATOM 761 C GLN A 104 0.114 -5.036 -6.828 1.00 8.61 C ANISOU 761 C GLN A 104 1095 1132 1043 -254 163 -177 C ATOM 762 O GLN A 104 0.730 -4.410 -7.698 1.00 9.65 O ANISOU 762 O GLN A 104 1283 1317 1063 -345 208 -78 O ATOM 763 CB GLN A 104 -1.428 -6.855 -7.656 1.00 9.09 C ANISOU 763 CB GLN A 104 1172 1568 711 -294 -18 -50 C ATOM 764 CG GLN A 104 -1.481 -6.207 -9.019 1.00 10.54 C ANISOU 764 CG GLN A 104 1510 1578 916 -326 -93 -17 C ATOM 765 CD GLN A 104 -2.462 -6.908 -9.929 1.00 8.77 C ANISOU 765 CD GLN A 104 930 1405 997 -164 -118 -15 C ATOM 766 OE1 GLN A 104 -3.507 -7.370 -9.481 1.00 9.16 O ANISOU 766 OE1 GLN A 104 1039 1179 1259 -115 -12 46 O ATOM 767 NE2 GLN A 104 -2.131 -7.003 -11.214 1.00 11.00 N ANISOU 767 NE2 GLN A 104 1434 1722 1024 -233 45 -85 N ATOM 768 N VAL A 105 -0.319 -4.435 -5.718 1.00 8.08 N ANISOU 768 N VAL A 105 962 1104 1002 -145 -38 -259 N ATOM 769 CA VAL A 105 0.054 -3.049 -5.462 1.00 8.16 C ANISOU 769 CA VAL A 105 847 1142 1111 -192 81 -142 C ATOM 770 C VAL A 105 1.580 -2.912 -5.391 1.00 8.20 C ANISOU 770 C VAL A 105 875 1022 1216 -117 154 86 C ATOM 771 O VAL A 105 2.168 -1.999 -5.989 1.00 8.42 O ANISOU 771 O VAL A 105 947 1105 1146 -190 140 44 O ATOM 772 CB VAL A 105 -0.648 -2.515 -4.182 1.00 8.26 C ANISOU 772 CB VAL A 105 1000 1102 1036 -64 81 -209 C ATOM 773 CG1 VAL A 105 -0.044 -1.191 -3.759 1.00 9.58 C ANISOU 773 CG1 VAL A 105 1212 1147 1278 -289 52 -367 C ATOM 774 CG2 VAL A 105 -2.156 -2.371 -4.439 1.00 10.76 C ANISOU 774 CG2 VAL A 105 868 1687 1530 226 109 -133 C ATOM 775 N ALA A 106 2.232 -3.848 -4.708 1.00 8.44 N ANISOU 775 N ALA A 106 854 1006 1344 -67 2 -240 N ATOM 776 CA ALA A 106 3.699 -3.845 -4.698 1.00 9.86 C ANISOU 776 CA ALA A 106 852 1371 1521 11 -198 -178 C ATOM 777 C ALA A 106 4.275 -3.974 -6.132 1.00 11.11 C ANISOU 777 C ALA A 106 983 1447 1789 14 221 -143 C ATOM 778 O ALA A 106 5.224 -3.242 -6.525 1.00 13.23 O ANISOU 778 O ALA A 106 1085 1489 2450 -109 503 -307 O ATOM 779 CB ALA A 106 4.215 -4.935 -3.765 1.00 11.38 C ANISOU 779 CB ALA A 106 975 1442 1904 -207 -255 19 C ATOM 780 N SER A 107 3.681 -4.825 -6.957 1.00 11.43 N ANISOU 780 N SER A 107 1311 1410 1621 11 497 -307 N ATOM 781 CA SER A 107 4.129 -4.963 -8.361 1.00 12.46 C ANISOU 781 CA SER A 107 1348 1566 1819 -80 539 -433 C ATOM 782 C SER A 107 3.995 -3.649 -9.112 1.00 12.58 C ANISOU 782 C SER A 107 1409 1582 1788 -248 570 -285 C ATOM 783 O SER A 107 4.906 -3.227 -9.857 1.00 14.30 O ANISOU 783 O SER A 107 1674 1830 1929 -558 962 -580 O ATOM 784 CB SER A 107 3.266 -6.017 -9.089 1.00 16.65 C ANISOU 784 CB SER A 107 3061 1646 1616 -623 920 -1103 C ATOM 785 OG SER A 107 3.485 -5.988 -10.514 1.00 22.25 O ANISOU 785 OG SER A 107 3532 2554 2366 -553 823 -589 O ATOM 786 N LEU A 108 2.857 -2.997 -8.935 1.00 11.70 N ANISOU 786 N LEU A 108 1346 1449 1649 -372 405 -385 N ATOM 787 CA LEU A 108 2.593 -1.776 -9.658 1.00 13.07 C ANISOU 787 CA LEU A 108 1460 1692 1813 -402 119 -367 C ATOM 788 C LEU A 108 3.527 -0.669 -9.189 1.00 11.88 C ANISOU 788 C LEU A 108 1611 1717 1184 -394 344 -214 C ATOM 789 O LEU A 108 3.918 0.197 -9.989 1.00 11.95 O ANISOU 789 O LEU A 108 1568 1518 1452 -429 536 -96 O ATOM 790 CB LEU A 108 1.126 -1.390 -9.506 1.00 12.84 C ANISOU 790 CB LEU A 108 1781 1661 1435 -342 2 -192 C ATOM 791 CG LEU A 108 0.151 -2.332 -10.229 1.00 13.76 C ANISOU 791 CG LEU A 108 1840 1998 1389 -756 -162 155 C ATOM 792 CD1 LEU A 108 -1.278 -1.978 -9.844 1.00 16.52 C ANISOU 792 CD1 LEU A 108 1819 2312 2145 -598 -108 -166 C ATOM 793 CD2 LEU A 108 0.374 -2.240 -11.749 1.00 19.43 C ANISOU 793 CD2 LEU A 108 3181 2761 1439 -1404 -258 88 C ATOM 794 N ASN A 109 3.904 -0.698 -7.907 1.00 10.47 N ANISOU 794 N ASN A 109 1221 1332 1422 -392 294 -325 N ATOM 795 CA ASN A 109 4.889 0.258 -7.400 1.00 10.13 C ANISOU 795 CA ASN A 109 1054 1571 1223 -158 199 -211 C ATOM 796 C ASN A 109 6.212 0.152 -8.184 1.00 10.82 C ANISOU 796 C ASN A 109 1439 1226 1447 -88 567 -147 C ATOM 797 O ASN A 109 6.986 1.130 -8.254 1.00 11.68 O ANISOU 797 O ASN A 109 1527 1526 1385 -404 449 -262 O ATOM 798 CB ASN A 109 5.127 0.034 -5.907 1.00 12.09 C ANISOU 798 CB ASN A 109 1811 1573 1208 -341 28 -158 C ATOM 799 CG ASN A 109 6.132 1.019 -5.342 1.00 11.30 C ANISOU 799 CG ASN A 109 1539 1428 1326 -222 263 -91 C ATOM 800 OD1 ASN A 109 5.892 2.216 -5.349 1.00 11.76 O ANISOU 800 OD1 ASN A 109 1747 1410 1309 -349 314 -266 O ATOM 801 ND2 ASN A 109 7.262 0.522 -4.883 1.00 14.11 N ANISOU 801 ND2 ASN A 109 1895 2148 1318 -274 405 -116 N ATOM 802 N GLY A 110 6.517 -1.041 -8.690 1.00 10.74 N ANISOU 802 N GLY A 110 1494 1390 1194 -130 502 -276 N ATOM 803 CA GLY A 110 7.737 -1.275 -9.468 1.00 12.20 C ANISOU 803 CA GLY A 110 1388 1839 1409 -28 436 -182 C ATOM 804 C GLY A 110 7.533 -1.311 -10.968 1.00 12.11 C ANISOU 804 C GLY A 110 1495 1619 1485 47 432 -311 C ATOM 805 O GLY A 110 8.444 -1.675 -11.695 1.00 15.68 O ANISOU 805 O GLY A 110 1954 2249 1752 212 714 -340 O ATOM 806 N THR A 111 6.378 -0.840 -11.435 1.00 12.05 N ANISOU 806 N THR A 111 1727 1823 1026 -442 232 -252 N ATOM 807 CA THR A 111 6.025 -0.885 -12.856 1.00 14.29 C ANISOU 807 CA THR A 111 1724 2330 1375 -476 -9 -288 C ATOM 808 C THR A 111 5.952 0.524 -13.423 1.00 14.11 C ANISOU 808 C THR A 111 1617 2276 1465 -152 373 -186 C ATOM 809 O THR A 111 5.130 1.327 -12.996 1.00 13.58 O ANISOU 809 O THR A 111 1775 2095 1288 -567 214 -148 O ATOM 810 CB THR A 111 4.655 -1.580 -13.023 1.00 14.54 C ANISOU 810 CB THR A 111 1723 2102 1697 -505 78 -382 C ATOM 811 OG1 THR A 111 4.758 -2.931 -12.547 1.00 17.18 O ANISOU 811 OG1 THR A 111 2206 2262 2058 -575 495 -521 O ATOM 812 CG2 THR A 111 4.202 -1.564 -14.486 1.00 17.99 C ANISOU 812 CG2 THR A 111 2508 2822 1503 -666 -69 -746 C ATOM 813 N SER A 112 6.887 0.868 -14.313 1.00 14.39 N ANISOU 813 N SER A 112 1778 2347 1341 -584 473 -268 N ATOM 814 CA SER A 112 7.095 2.272 -14.672 1.00 17.02 C ANISOU 814 CA SER A 112 2142 2323 1998 -408 670 195 C ATOM 815 C SER A 112 5.900 2.916 -15.385 1.00 16.04 C ANISOU 815 C SER A 112 2402 2071 1617 -515 439 -208 C ATOM 816 O SER A 112 5.710 4.127 -15.304 1.00 19.17 O ANISOU 816 O SER A 112 2559 2346 2376 -47 140 79 O ATOM 817 CB SER A 112 8.372 2.445 -15.494 1.00 21.20 C ANISOU 817 CB SER A 112 2522 3363 2170 -1050 957 -418 C ATOM 818 OG SER A 112 8.255 1.720 -16.690 1.00 23.94 O ANISOU 818 OG SER A 112 2771 3810 2515 -520 1092 -532 O ATOM 819 N SER A 113 5.053 2.103 -16.021 1.00 14.76 N ANISOU 819 N SER A 113 1947 2569 1090 -303 412 -28 N ATOM 820 CA SER A 113 3.829 2.622 -16.607 1.00 19.29 C ANISOU 820 CA SER A 113 2336 3311 1681 -221 69 -299 C ATOM 821 C SER A 113 2.656 2.870 -15.655 1.00 17.86 C ANISOU 821 C SER A 113 2240 2976 1566 143 104 181 C ATOM 822 O SER A 113 1.650 3.470 -16.054 1.00 21.75 O ANISOU 822 O SER A 113 2718 3904 1641 -172 -151 489 O ATOM 823 CB SER A 113 3.372 1.703 -17.722 1.00 22.40 C ANISOU 823 CB SER A 113 3480 3396 1635 -1006 437 -703 C ATOM 824 OG SER A 113 3.065 0.429 -17.178 1.00 22.77 O ANISOU 824 OG SER A 113 3292 3173 2185 -905 -19 -189 O ATOM 825 N SER A 114 2.802 2.461 -14.399 1.00 15.02 N ANISOU 825 N SER A 114 1968 2349 1390 -539 181 -139 N ATOM 826 CA SER A 114 1.702 2.596 -13.439 1.00 14.54 C ANISOU 826 CA SER A 114 1772 2203 1548 -275 299 130 C ATOM 827 C SER A 114 1.651 4.009 -12.858 1.00 14.56 C ANISOU 827 C SER A 114 2021 2397 1114 -126 35 203 C ATOM 828 O SER A 114 2.684 4.566 -12.478 1.00 15.43 O ANISOU 828 O SER A 114 1959 2454 1447 -537 243 -61 O ATOM 829 CB SER A 114 1.861 1.593 -12.281 1.00 16.16 C ANISOU 829 CB SER A 114 1353 2177 2607 -115 597 897 C ATOM 830 OG SER A 114 0.755 1.686 -11.399 1.00 15.45 O ANISOU 830 OG SER A 114 1978 2145 1744 -155 177 -114 O ATOM 831 N PRO A 115 0.441 4.504 -12.579 1.00 13.40 N ANISOU 831 N PRO A 115 1771 2010 1309 -328 145 200 N ATOM 832 CA PRO A 115 0.323 5.745 -11.856 1.00 14.87 C ANISOU 832 CA PRO A 115 2129 1868 1653 -119 23 250 C ATOM 833 C PRO A 115 0.915 5.707 -10.444 1.00 13.90 C ANISOU 833 C PRO A 115 1904 1884 1491 -378 287 376 C ATOM 834 O PRO A 115 1.160 6.758 -9.873 1.00 18.48 O ANISOU 834 O PRO A 115 3190 2102 1727 -235 131 -80 O ATOM 835 CB PRO A 115 -1.206 5.985 -11.814 1.00 16.99 C ANISOU 835 CB PRO A 115 2035 2751 1669 39 3 222 C ATOM 836 CG PRO A 115 -1.723 5.266 -13.026 1.00 18.68 C ANISOU 836 CG PRO A 115 2346 3138 1613 187 73 187 C ATOM 837 CD PRO A 115 -0.867 4.034 -13.082 1.00 16.70 C ANISOU 837 CD PRO A 115 1976 2462 1906 -222 -556 326 C ATOM 838 N ILE A 116 1.069 4.526 -9.853 1.00 11.73 N ANISOU 838 N ILE A 116 1500 1798 1158 -183 -68 197 N ATOM 839 CA ILE A 116 1.641 4.423 -8.508 1.00 11.19 C ANISOU 839 CA ILE A 116 1328 1759 1165 -190 -14 93 C ATOM 840 C ILE A 116 3.093 3.982 -8.487 1.00 10.42 C ANISOU 840 C ILE A 116 1167 1753 1039 -323 184 -47 C ATOM 841 O ILE A 116 3.625 3.642 -7.434 1.00 10.73 O ANISOU 841 O ILE A 116 1179 1593 1305 -203 153 -97 O ATOM 842 CB ILE A 116 0.766 3.582 -7.548 1.00 10.68 C ANISOU 842 CB ILE A 116 1262 1274 1521 -21 256 -165 C ATOM 843 CG1 ILE A 116 0.648 2.131 -8.042 1.00 10.34 C ANISOU 843 CG1 ILE A 116 1713 1220 996 -171 -116 44 C ATOM 844 CG2 ILE A 116 -0.587 4.259 -7.313 1.00 11.30 C ANISOU 844 CG2 ILE A 116 1233 1479 1580 113 105 -37 C ATOM 845 CD1 ILE A 116 0.090 1.198 -6.967 1.00 12.28 C ANISOU 845 CD1 ILE A 116 1680 1836 1149 -300 283 161 C ATOM 846 N TYR A 117 3.762 4.083 -9.636 1.00 11.12 N ANISOU 846 N TYR A 117 1416 1538 1269 -313 249 -91 N ATOM 847 CA TYR A 117 5.188 3.777 -9.691 1.00 13.37 C ANISOU 847 CA TYR A 117 1705 2150 1223 -514 416 -378 C ATOM 848 C TYR A 117 5.941 4.640 -8.643 1.00 10.70 C ANISOU 848 C TYR A 117 1313 1581 1172 -271 233 -82 C ATOM 849 O TYR A 117 5.883 5.860 -8.700 1.00 12.50 O ANISOU 849 O TYR A 117 1681 1600 1468 -418 156 -179 O ATOM 850 CB TYR A 117 5.695 4.069 -11.105 1.00 13.15 C ANISOU 850 CB TYR A 117 1650 2067 1279 -349 453 59 C ATOM 851 CG TYR A 117 7.157 3.780 -11.302 1.00 13.22 C ANISOU 851 CG TYR A 117 1577 1816 1629 -614 356 -498 C ATOM 852 CD1 TYR A 117 7.661 2.504 -11.149 1.00 14.34 C ANISOU 852 CD1 TYR A 117 1497 2552 1397 -471 292 -335 C ATOM 853 CD2 TYR A 117 7.986 4.759 -11.839 1.00 18.91 C ANISOU 853 CD2 TYR A 117 1759 2559 2865 -1188 671 -687 C ATOM 854 CE1 TYR A 117 8.966 2.193 -11.479 1.00 15.44 C ANISOU 854 CE1 TYR A 117 1761 2148 1957 -575 484 -695 C ATOM 855 CE2 TYR A 117 9.266 4.459 -12.262 1.00 20.97 C ANISOU 855 CE2 TYR A 117 2093 3114 2757 -890 1144 -436 C ATOM 856 CZ TYR A 117 9.778 3.195 -12.005 1.00 23.33 C ANISOU 856 CZ TYR A 117 1788 2483 4592 -830 1143 -835 C ATOM 857 OH TYR A 117 11.046 2.889 -12.419 1.00 33.87 O ANISOU 857 OH TYR A 117 2228 3796 6843 -1056 2237 -1819 O ATOM 858 N GLY A 118 6.662 3.987 -7.736 1.00 10.89 N ANISOU 858 N GLY A 118 1158 1643 1334 -488 301 -95 N ATOM 859 CA GLY A 118 7.431 4.684 -6.704 1.00 11.85 C ANISOU 859 CA GLY A 118 1262 1921 1318 -451 229 -365 C ATOM 860 C GLY A 118 6.608 5.442 -5.665 1.00 10.88 C ANISOU 860 C GLY A 118 1328 1555 1249 -412 248 -45 C ATOM 861 O GLY A 118 7.159 6.260 -4.937 1.00 14.39 O ANISOU 861 O GLY A 118 1717 2320 1430 -778 44 -415 O ATOM 862 N LYS A 119 5.303 5.187 -5.569 1.00 9.35 N ANISOU 862 N LYS A 119 1213 1363 974 -145 268 10 N ATOM 863 CA LYS A 119 4.481 5.864 -4.565 1.00 9.63 C ANISOU 863 CA LYS A 119 1319 1160 1179 -216 298 -38 C ATOM 864 C LYS A 119 4.319 5.090 -3.273 1.00 9.68 C ANISOU 864 C LYS A 119 1402 1101 1173 -238 83 42 C ATOM 865 O LYS A 119 3.799 5.654 -2.303 1.00 10.80 O ANISOU 865 O LYS A 119 1629 1290 1182 -184 126 -217 O ATOM 866 CB LYS A 119 3.097 6.216 -5.117 1.00 10.76 C ANISOU 866 CB LYS A 119 1484 1386 1216 -25 96 84 C ATOM 867 CG LYS A 119 3.134 7.336 -6.149 1.00 12.38 C ANISOU 867 CG LYS A 119 1764 1371 1566 -230 247 331 C ATOM 868 CD LYS A 119 1.735 7.940 -6.328 1.00 14.02 C ANISOU 868 CD LYS A 119 2130 1425 1769 237 143 383 C ATOM 869 CE LYS A 119 1.729 9.211 -7.159 1.00 15.28 C ANISOU 869 CE LYS A 119 2501 1819 1482 241 181 387 C ATOM 870 NZ LYS A 119 2.121 8.928 -8.553 1.00 22.84 N ANISOU 870 NZ LYS A 119 3372 2835 2471 33 1137 35 N ATOM 871 N VAL A 120 4.657 3.796 -3.286 1.00 8.81 N ANISOU 871 N VAL A 120 1011 1261 1075 -208 46 8 N ATOM 872 CA VAL A 120 4.282 2.909 -2.171 1.00 8.98 C ANISOU 872 CA VAL A 120 1213 1079 1120 -247 -215 10 C ATOM 873 C VAL A 120 5.531 2.492 -1.399 1.00 9.00 C ANISOU 873 C VAL A 120 1118 1216 1085 -148 95 -186 C ATOM 874 O VAL A 120 6.543 2.102 -1.994 1.00 10.45 O ANISOU 874 O VAL A 120 1138 1764 1066 21 90 -49 O ATOM 875 CB VAL A 120 3.605 1.626 -2.707 1.00 8.99 C ANISOU 875 CB VAL A 120 1153 1218 1045 -364 -119 37 C ATOM 876 CG1 VAL A 120 3.177 0.739 -1.543 1.00 9.97 C ANISOU 876 CG1 VAL A 120 1300 1243 1245 -415 114 15 C ATOM 877 CG2 VAL A 120 2.412 1.992 -3.592 1.00 12.84 C ANISOU 877 CG2 VAL A 120 1247 1753 1878 -146 -629 25 C ATOM 878 N ASP A 121 5.437 2.548 -0.075 1.00 8.46 N ANISOU 878 N ASP A 121 1099 1086 1026 -139 -156 -90 N ATOM 879 CA ASP A 121 6.391 1.877 0.787 1.00 7.78 C ANISOU 879 CA ASP A 121 1080 1032 845 -203 -41 -51 C ATOM 880 C ASP A 121 5.853 0.474 1.057 1.00 7.90 C ANISOU 880 C ASP A 121 942 1051 1007 -260 74 -211 C ATOM 881 O ASP A 121 4.910 0.295 1.830 1.00 8.36 O ANISOU 881 O ASP A 121 752 1197 1225 -86 90 -19 O ATOM 882 CB ASP A 121 6.593 2.649 2.090 1.00 8.33 C ANISOU 882 CB ASP A 121 1041 1145 976 4 -24 -222 C ATOM 883 CG ASP A 121 7.604 1.980 2.989 1.00 8.39 C ANISOU 883 CG ASP A 121 819 1194 1174 -202 59 -145 C ATOM 884 OD1 ASP A 121 7.977 0.818 2.744 1.00 10.42 O ANISOU 884 OD1 ASP A 121 1261 1534 1163 -6 -172 -138 O ATOM 885 OD2 ASP A 121 8.066 2.638 3.948 1.00 10.71 O ANISOU 885 OD2 ASP A 121 1212 1670 1187 -180 -15 -472 O ATOM 886 N THR A 122 6.346 -0.513 0.300 1.00 8.55 N ANISOU 886 N THR A 122 1004 1033 1209 44 -133 -204 N ATOM 887 CA THR A 122 5.759 -1.841 0.326 1.00 9.10 C ANISOU 887 CA THR A 122 1224 1039 1195 101 -20 -151 C ATOM 888 C THR A 122 5.970 -2.555 1.650 1.00 8.47 C ANISOU 888 C THR A 122 966 1058 1193 -22 83 -208 C ATOM 889 O THR A 122 5.307 -3.569 1.876 1.00 10.16 O ANISOU 889 O THR A 122 1198 1077 1582 -76 87 -142 O ATOM 890 CB THR A 122 6.294 -2.730 -0.795 1.00 9.65 C ANISOU 890 CB THR A 122 1214 1352 1100 -3 54 -158 C ATOM 891 OG1 THR A 122 7.703 -2.864 -0.625 1.00 12.27 O ANISOU 891 OG1 THR A 122 1395 1559 1707 331 233 -511 O ATOM 892 CG2 THR A 122 6.035 -2.096 -2.143 1.00 11.14 C ANISOU 892 CG2 THR A 122 1646 1456 1129 -56 80 -227 C ATOM 893 N ALA A 123 6.771 -1.991 2.558 1.00 8.29 N ANISOU 893 N ALA A 123 857 1286 1004 78 0 -104 N ATOM 894 CA ALA A 123 6.952 -2.602 3.869 1.00 9.35 C ANISOU 894 CA ALA A 123 739 1603 1207 216 -93 -73 C ATOM 895 C ALA A 123 5.842 -2.182 4.832 1.00 9.76 C ANISOU 895 C ALA A 123 974 1492 1241 156 143 169 C ATOM 896 O ALA A 123 5.843 -2.627 5.982 1.00 14.21 O ANISOU 896 O ALA A 123 1191 2519 1689 396 154 777 O ATOM 897 CB ALA A 123 8.296 -2.178 4.453 1.00 11.56 C ANISOU 897 CB ALA A 123 719 2140 1533 203 -288 -104 C ATOM 898 N ARG A 124 4.942 -1.291 4.417 1.00 7.56 N ANISOU 898 N ARG A 124 731 1037 1104 -20 47 -240 N ATOM 899 CA ARG A 124 3.913 -0.763 5.345 1.00 7.72 C ANISOU 899 CA ARG A 124 754 1037 1140 -72 -46 -285 C ATOM 900 C ARG A 124 2.545 -0.962 4.724 1.00 6.58 C ANISOU 900 C ARG A 124 785 852 861 -84 -46 -44 C ATOM 901 O ARG A 124 2.119 -0.209 3.843 1.00 7.90 O ANISOU 901 O ARG A 124 849 1127 1024 -107 -126 65 O ATOM 902 CB ARG A 124 4.210 0.720 5.677 1.00 8.07 C ANISOU 902 CB ARG A 124 852 1126 1087 -182 -165 -298 C ATOM 903 CG ARG A 124 5.610 0.863 6.269 1.00 9.49 C ANISOU 903 CG ARG A 124 962 1211 1433 -256 -295 -256 C ATOM 904 CD ARG A 124 5.894 2.266 6.777 1.00 8.74 C ANISOU 904 CD ARG A 124 1135 1077 1108 -191 -130 -195 C ATOM 905 NE ARG A 124 5.894 3.267 5.710 1.00 8.50 N ANISOU 905 NE ARG A 124 1050 1086 1091 -179 -170 -257 N ATOM 906 CZ ARG A 124 5.022 4.252 5.574 1.00 8.21 C ANISOU 906 CZ ARG A 124 968 1133 1015 -219 -50 -158 C ATOM 907 NH1 ARG A 124 3.903 4.287 6.317 1.00 9.02 N ANISOU 907 NH1 ARG A 124 937 1263 1226 -272 122 -311 N ATOM 908 NH2 ARG A 124 5.229 5.177 4.641 1.00 8.93 N ANISOU 908 NH2 ARG A 124 1345 1215 833 -255 -110 -155 N ATOM 909 N MET A 125 1.840 -1.997 5.207 1.00 7.79 N ANISOU 909 N MET A 125 820 1009 1129 -200 -91 70 N ATOM 910 CA AMET A 125 0.569 -2.395 4.622 0.50 7.35 C ANISOU 910 CA AMET A 125 824 1107 859 -211 -74 -8 C ATOM 911 CA BMET A 125 0.583 -2.440 4.588 0.50 8.29 C ANISOU 911 CA BMET A 125 858 1361 928 -315 -66 16 C ATOM 912 C MET A 125 -0.479 -2.654 5.665 1.00 7.36 C ANISOU 912 C MET A 125 819 1160 816 -106 -172 127 C ATOM 913 O MET A 125 -0.170 -3.013 6.801 1.00 9.51 O ANISOU 913 O MET A 125 953 1598 1061 -139 -278 326 O ATOM 914 CB AMET A 125 0.754 -3.650 3.797 0.50 6.63 C ANISOU 914 CB AMET A 125 685 1072 761 -337 139 41 C ATOM 915 CB BMET A 125 0.766 -3.740 3.770 0.50 11.04 C ANISOU 915 CB BMET A 125 1497 1360 1337 -354 37 -135 C ATOM 916 CG AMET A 125 1.487 -3.310 2.541 0.50 4.41 C ANISOU 916 CG AMET A 125 574 692 408 -200 -114 -63 C ATOM 917 CG BMET A 125 1.936 -3.750 2.787 0.50 13.78 C ANISOU 917 CG BMET A 125 1360 2014 1859 341 -61 291 C ATOM 918 SD AMET A 125 1.760 -4.796 1.596 0.50 4.23 S ANISOU 918 SD AMET A 125 420 498 689 3 -49 -68 S ATOM 919 SD BMET A 125 1.812 -2.655 1.367 0.50 18.00 S ANISOU 919 SD BMET A 125 2784 1852 2203 481 -13 -145 S ATOM 920 CE AMET A 125 2.164 -4.082 0.002 0.50 5.66 C ANISOU 920 CE AMET A 125 374 1174 601 196 -83 -46 C ATOM 921 CE BMET A 125 1.681 -3.836 0.031 0.50 20.35 C ANISOU 921 CE BMET A 125 2628 2064 3041 -483 -450 -983 C ATOM 922 N GLY A 126 -1.730 -2.511 5.242 1.00 7.22 N ANISOU 922 N GLY A 126 656 1101 984 -170 -52 -22 N ATOM 923 CA GLY A 126 -2.871 -2.675 6.131 1.00 7.76 C ANISOU 923 CA GLY A 126 859 1187 902 -386 1 35 C ATOM 924 C GLY A 126 -3.997 -3.401 5.422 1.00 6.24 C ANISOU 924 C GLY A 126 774 880 715 6 51 10 C ATOM 925 O GLY A 126 -4.040 -3.456 4.181 1.00 6.83 O ANISOU 925 O GLY A 126 708 1030 856 -134 -48 90 O ATOM 926 N VAL A 127 -4.942 -3.901 6.225 1.00 6.06 N ANISOU 926 N VAL A 127 666 816 819 -103 -20 7 N ATOM 927 CA VAL A 127 -6.068 -4.681 5.709 1.00 6.11 C ANISOU 927 CA VAL A 127 620 747 952 -76 -63 -45 C ATOM 928 C VAL A 127 -7.381 -4.252 6.312 1.00 5.92 C ANISOU 928 C VAL A 127 650 915 684 -29 -51 -8 C ATOM 929 O VAL A 127 -7.466 -3.972 7.524 1.00 7.06 O ANISOU 929 O VAL A 127 853 1007 820 103 -77 -54 O ATOM 930 CB VAL A 127 -5.856 -6.197 5.947 1.00 6.10 C ANISOU 930 CB VAL A 127 793 737 787 61 104 80 C ATOM 931 CG1 VAL A 127 -4.779 -6.740 5.020 1.00 7.11 C ANISOU 931 CG1 VAL A 127 847 922 930 232 79 -118 C ATOM 932 CG2 VAL A 127 -5.543 -6.533 7.410 1.00 7.23 C ANISOU 932 CG2 VAL A 127 843 1020 883 -65 -111 47 C ATOM 933 N MET A 128 -8.393 -4.127 5.462 1.00 5.70 N ANISOU 933 N MET A 128 650 695 818 106 -60 13 N ATOM 934 CA MET A 128 -9.752 -3.771 5.906 1.00 6.25 C ANISOU 934 CA MET A 128 621 786 968 -8 33 -37 C ATOM 935 C MET A 128 -10.756 -4.620 5.135 1.00 5.89 C ANISOU 935 C MET A 128 612 900 722 16 -22 12 C ATOM 936 O MET A 128 -10.428 -5.205 4.103 1.00 6.46 O ANISOU 936 O MET A 128 772 845 837 -14 -20 44 O ATOM 937 CB MET A 128 -10.042 -2.285 5.650 1.00 6.78 C ANISOU 937 CB MET A 128 822 721 1029 38 -114 -40 C ATOM 938 CG MET A 128 -9.127 -1.395 6.503 1.00 6.82 C ANISOU 938 CG MET A 128 880 657 1051 -1 -111 48 C ATOM 939 SD MET A 128 -9.327 0.371 6.153 1.00 7.84 S ANISOU 939 SD MET A 128 876 883 1218 0 -53 74 S ATOM 940 CE MET A 128 -11.003 0.633 6.729 1.00 8.54 C ANISOU 940 CE MET A 128 883 1118 1240 190 78 19 C ATOM 941 N GLY A 129 -12.008 -4.637 5.578 1.00 6.22 N ANISOU 941 N GLY A 129 611 884 865 -75 -48 -46 N ATOM 942 CA GLY A 129 -13.002 -5.385 4.838 1.00 6.95 C ANISOU 942 CA GLY A 129 619 1065 954 -196 -36 -34 C ATOM 943 C GLY A 129 -14.257 -5.564 5.639 1.00 6.54 C ANISOU 943 C GLY A 129 766 960 758 -56 15 -87 C ATOM 944 O GLY A 129 -14.241 -5.472 6.866 1.00 7.01 O ANISOU 944 O GLY A 129 809 1095 758 -6 68 -94 O ATOM 945 N TRP A 130 -15.337 -5.859 4.918 1.00 6.60 N ANISOU 945 N TRP A 130 638 923 944 -112 14 -198 N ATOM 946 CA TRP A 130 -16.658 -5.956 5.523 1.00 6.33 C ANISOU 946 CA TRP A 130 601 857 945 -80 85 159 C ATOM 947 C TRP A 130 -17.103 -7.399 5.682 1.00 6.14 C ANISOU 947 C TRP A 130 613 834 883 87 16 -123 C ATOM 948 O TRP A 130 -17.051 -8.176 4.721 1.00 7.56 O ANISOU 948 O TRP A 130 875 984 1012 13 27 -223 O ATOM 949 CB TRP A 130 -17.637 -5.215 4.607 1.00 8.10 C ANISOU 949 CB TRP A 130 672 1418 986 204 39 -19 C ATOM 950 CG TRP A 130 -19.093 -5.325 5.026 1.00 7.45 C ANISOU 950 CG TRP A 130 712 1036 1079 4 17 -121 C ATOM 951 CD1 TRP A 130 -19.596 -5.305 6.309 1.00 8.11 C ANISOU 951 CD1 TRP A 130 780 1073 1227 -26 98 -29 C ATOM 952 CD2 TRP A 130 -20.211 -5.444 4.150 1.00 7.42 C ANISOU 952 CD2 TRP A 130 857 1119 843 87 -25 -90 C ATOM 953 NE1 TRP A 130 -20.979 -5.409 6.273 1.00 7.91 N ANISOU 953 NE1 TRP A 130 705 1097 1204 32 41 -80 N ATOM 954 CE2 TRP A 130 -21.375 -5.488 4.957 1.00 8.04 C ANISOU 954 CE2 TRP A 130 785 1228 1041 -100 -18 -78 C ATOM 955 CE3 TRP A 130 -20.351 -5.450 2.751 1.00 8.81 C ANISOU 955 CE3 TRP A 130 1205 1089 1051 149 -165 -122 C ATOM 956 CZ2 TRP A 130 -22.676 -5.570 4.395 1.00 9.30 C ANISOU 956 CZ2 TRP A 130 915 1357 1259 -15 -238 -122 C ATOM 957 CZ3 TRP A 130 -21.631 -5.528 2.199 1.00 9.14 C ANISOU 957 CZ3 TRP A 130 1128 1138 1207 185 -176 -184 C ATOM 958 CH2 TRP A 130 -22.777 -5.581 3.019 1.00 11.35 C ANISOU 958 CH2 TRP A 130 1491 1551 1268 -107 60 -334 C ATOM 959 N ALA A 131 -17.519 -7.779 6.898 1.00 7.27 N ANISOU 959 N ALA A 131 871 854 1037 -54 111 37 N ATOM 960 CA ALA A 131 -18.285 -9.018 7.109 1.00 8.00 C ANISOU 960 CA ALA A 131 642 932 1463 -5 92 -244 C ATOM 961 C ALA A 131 -17.357 -10.201 6.792 1.00 6.83 C ANISOU 961 C ALA A 131 849 850 895 -17 89 -201 C ATOM 962 O ALA A 131 -16.318 -10.297 7.452 1.00 8.05 O ANISOU 962 O ALA A 131 770 1132 1157 -29 6 -75 O ATOM 963 CB ALA A 131 -19.575 -9.005 6.304 1.00 8.57 C ANISOU 963 CB ALA A 131 839 1203 1213 -164 -14 -304 C ATOM 964 N MET A 132 -17.670 -11.101 5.862 1.00 7.03 N ANISOU 964 N MET A 132 870 724 1076 -42 172 -184 N ATOM 965 CA MET A 132 -16.699 -12.156 5.574 1.00 7.95 C ANISOU 965 CA MET A 132 866 852 1302 -75 140 -330 C ATOM 966 C MET A 132 -15.363 -11.550 5.135 1.00 7.38 C ANISOU 966 C MET A 132 823 931 1047 -21 -61 -116 C ATOM 967 O MET A 132 -14.333 -12.203 5.306 1.00 8.37 O ANISOU 967 O MET A 132 799 1032 1347 -47 23 -240 O ATOM 968 CB MET A 132 -17.214 -13.114 4.494 1.00 8.90 C ANISOU 968 CB MET A 132 897 1141 1344 -210 91 -426 C ATOM 969 CG MET A 132 -18.251 -14.085 5.009 1.00 10.46 C ANISOU 969 CG MET A 132 1088 1146 1737 -293 155 -351 C ATOM 970 SD MET A 132 -18.642 -15.245 3.669 1.00 12.06 S ANISOU 970 SD MET A 132 1214 1291 2076 -101 -193 -601 S ATOM 971 CE MET A 132 -20.071 -16.114 4.338 1.00 16.10 C ANISOU 971 CE MET A 132 1470 1486 3159 -670 -43 -716 C ATOM 972 N GLY A 133 -15.369 -10.383 4.486 1.00 6.86 N ANISOU 972 N GLY A 133 652 1097 855 -173 -16 -142 N ATOM 973 CA GLY A 133 -14.127 -9.699 4.132 1.00 7.73 C ANISOU 973 CA GLY A 133 743 1037 1156 -209 57 -260 C ATOM 974 C GLY A 133 -13.400 -9.136 5.350 1.00 7.07 C ANISOU 974 C GLY A 133 794 899 992 -145 2 -98 C ATOM 975 O GLY A 133 -12.185 -8.894 5.303 1.00 7.19 O ANISOU 975 O GLY A 133 730 988 1013 -59 -113 -26 O ATOM 976 N GLY A 134 -14.150 -8.863 6.418 1.00 7.10 N ANISOU 976 N GLY A 134 909 896 890 -2 -106 -143 N ATOM 977 CA GLY A 134 -13.592 -8.500 7.698 1.00 7.56 C ANISOU 977 CA GLY A 134 1081 929 859 36 -74 -88 C ATOM 978 C GLY A 134 -12.957 -9.706 8.372 1.00 6.56 C ANISOU 978 C GLY A 134 704 856 933 -54 -20 -43 C ATOM 979 O GLY A 134 -11.835 -9.627 8.903 1.00 7.69 O ANISOU 979 O GLY A 134 844 1055 1022 -21 -63 -24 O ATOM 980 N GLY A 135 -13.650 -10.855 8.331 1.00 7.22 N ANISOU 980 N GLY A 135 960 857 925 -128 74 3 N ATOM 981 CA GLY A 135 -12.998 -12.093 8.777 1.00 8.33 C ANISOU 981 CA GLY A 135 963 1013 1186 -39 161 50 C ATOM 982 C GLY A 135 -11.736 -12.340 7.957 1.00 7.31 C ANISOU 982 C GLY A 135 756 895 1126 -36 -47 -78 C ATOM 983 O GLY A 135 -10.700 -12.736 8.498 1.00 8.05 O ANISOU 983 O GLY A 135 885 954 1216 -3 -147 79 O ATOM 984 N GLY A 136 -11.817 -12.151 6.643 1.00 7.51 N ANISOU 984 N GLY A 136 983 854 1014 -84 86 -211 N ATOM 985 CA GLY A 136 -10.630 -12.330 5.804 1.00 7.72 C ANISOU 985 CA GLY A 136 785 954 1195 -123 43 -104 C ATOM 986 C GLY A 136 -9.495 -11.401 6.210 1.00 7.26 C ANISOU 986 C GLY A 136 878 845 1035 57 -175 5 C ATOM 987 O GLY A 136 -8.328 -11.817 6.198 1.00 7.03 O ANISOU 987 O GLY A 136 766 916 988 60 -30 -24 O ATOM 988 N SER A 137 -9.801 -10.172 6.633 1.00 6.60 N ANISOU 988 N SER A 137 838 815 854 -98 97 -105 N ATOM 989 CA SER A 137 -8.744 -9.259 7.066 1.00 6.71 C ANISOU 989 CA SER A 137 823 717 1009 -83 -136 -76 C ATOM 990 C SER A 137 -8.069 -9.723 8.358 1.00 6.84 C ANISOU 990 C SER A 137 821 827 951 -44 68 24 C ATOM 991 O SER A 137 -6.847 -9.595 8.507 1.00 7.18 O ANISOU 991 O SER A 137 766 965 995 65 -82 59 O ATOM 992 CB SER A 137 -9.356 -7.883 7.340 1.00 6.27 C ANISOU 992 CB SER A 137 879 787 714 -21 -11 -7 C ATOM 993 OG SER A 137 -9.896 -7.312 6.155 1.00 6.64 O ANISOU 993 OG SER A 137 892 842 786 42 -24 32 O ATOM 994 N LEU A 138 -8.850 -10.308 9.264 1.00 7.01 N ANISOU 994 N LEU A 138 1003 778 881 6 5 110 N ATOM 995 CA LEU A 138 -8.303 -10.873 10.496 1.00 7.40 C ANISOU 995 CA LEU A 138 954 1000 857 45 21 102 C ATOM 996 C LEU A 138 -7.451 -12.113 10.239 1.00 6.90 C ANISOU 996 C LEU A 138 850 821 951 -109 3 28 C ATOM 997 O LEU A 138 -6.371 -12.253 10.831 1.00 7.80 O ANISOU 997 O LEU A 138 820 1089 1053 46 6 65 O ATOM 998 CB LEU A 138 -9.438 -11.191 11.460 1.00 8.80 C ANISOU 998 CB LEU A 138 1260 1065 1019 70 362 22 C ATOM 999 CG LEU A 138 -10.201 -9.961 11.977 1.00 9.55 C ANISOU 999 CG LEU A 138 1204 1019 1405 201 193 -30 C ATOM 1000 CD1 LEU A 138 -11.625 -10.351 12.423 1.00 12.79 C ANISOU 1000 CD1 LEU A 138 1319 1689 1852 263 423 169 C ATOM 1001 CD2 LEU A 138 -9.464 -9.364 13.167 1.00 13.56 C ANISOU 1001 CD2 LEU A 138 1582 1913 1655 139 -290 -486 C ATOM 1002 N ILE A 139 -7.855 -12.938 9.275 1.00 6.78 N ANISOU 1002 N ILE A 139 877 816 879 37 69 64 N ATOM 1003 CA ILE A 139 -7.031 -14.071 8.851 1.00 6.95 C ANISOU 1003 CA ILE A 139 993 712 936 -52 184 -58 C ATOM 1004 C ILE A 139 -5.733 -13.562 8.218 1.00 7.28 C ANISOU 1004 C ILE A 139 864 950 950 41 -35 75 C ATOM 1005 O ILE A 139 -4.631 -14.057 8.523 1.00 7.58 O ANISOU 1005 O ILE A 139 851 890 1138 33 -84 -17 O ATOM 1006 CB ILE A 139 -7.836 -14.941 7.849 1.00 7.56 C ANISOU 1006 CB ILE A 139 971 785 1113 -36 204 -57 C ATOM 1007 CG1 ILE A 139 -9.008 -15.620 8.561 1.00 8.47 C ANISOU 1007 CG1 ILE A 139 1014 984 1219 -247 47 80 C ATOM 1008 CG2 ILE A 139 -6.942 -16.004 7.205 1.00 9.18 C ANISOU 1008 CG2 ILE A 139 1215 971 1301 62 138 -98 C ATOM 1009 CD1 ILE A 139 -10.014 -16.279 7.614 1.00 9.26 C ANISOU 1009 CD1 ILE A 139 1117 1029 1370 -211 -148 26 C ATOM 1010 N SER A 140 -5.832 -12.504 7.406 1.00 6.43 N ANISOU 1010 N SER A 140 814 764 863 -82 85 8 N ATOM 1011 CA SER A 140 -4.625 -11.922 6.804 1.00 6.55 C ANISOU 1011 CA SER A 140 757 893 837 -142 -22 86 C ATOM 1012 C SER A 140 -3.659 -11.458 7.889 1.00 6.62 C ANISOU 1012 C SER A 140 793 882 841 51 -74 -44 C ATOM 1013 O SER A 140 -2.437 -11.705 7.794 1.00 7.30 O ANISOU 1013 O SER A 140 761 1033 980 192 -13 72 O ATOM 1014 CB SER A 140 -4.969 -10.732 5.905 1.00 6.86 C ANISOU 1014 CB SER A 140 933 846 826 13 -138 30 C ATOM 1015 OG SER A 140 -5.616 -11.191 4.720 1.00 6.67 O ANISOU 1015 OG SER A 140 825 884 824 26 -13 -103 O ATOM 1016 N ALA A 141 -4.194 -10.769 8.892 1.00 6.35 N ANISOU 1016 N ALA A 141 867 716 828 -4 35 -107 N ATOM 1017 CA ALA A 141 -3.373 -10.268 9.989 1.00 7.59 C ANISOU 1017 CA ALA A 141 987 981 912 87 -35 -117 C ATOM 1018 C ALA A 141 -2.759 -11.434 10.768 1.00 7.64 C ANISOU 1018 C ALA A 141 880 1013 1009 -5 -122 51 C ATOM 1019 O ALA A 141 -1.589 -11.350 11.153 1.00 8.92 O ANISOU 1019 O ALA A 141 956 1207 1226 119 -110 189 O ATOM 1020 CB ALA A 141 -4.229 -9.412 10.915 1.00 8.25 C ANISOU 1020 CB ALA A 141 1121 1062 949 165 -92 -181 C ATOM 1021 N ALA A 142 -3.537 -12.470 11.076 1.00 7.48 N ANISOU 1021 N ALA A 142 1170 862 806 169 -77 70 N ATOM 1022 CA ALA A 142 -2.999 -13.635 11.789 1.00 8.90 C ANISOU 1022 CA ALA A 142 1217 911 1250 187 41 290 C ATOM 1023 C ALA A 142 -1.836 -14.260 11.007 1.00 9.01 C ANISOU 1023 C ALA A 142 1010 1204 1207 112 -140 230 C ATOM 1024 O ALA A 142 -0.848 -14.716 11.583 1.00 10.85 O ANISOU 1024 O ALA A 142 1498 1398 1224 387 -310 53 O ATOM 1025 CB ALA A 142 -4.088 -14.668 11.991 1.00 10.26 C ANISOU 1025 CB ALA A 142 1427 1187 1282 40 263 318 C ATOM 1026 N ASN A 143 -1.998 -14.387 9.691 1.00 8.03 N ANISOU 1026 N ASN A 143 1111 968 970 94 153 108 N ATOM 1027 CA ASN A 143 -1.015 -15.091 8.877 1.00 8.66 C ANISOU 1027 CA ASN A 143 1160 865 1263 90 82 -144 C ATOM 1028 C ASN A 143 0.172 -14.206 8.492 1.00 7.90 C ANISOU 1028 C ASN A 143 947 857 1197 186 -9 -107 C ATOM 1029 O ASN A 143 1.207 -14.735 8.072 1.00 9.40 O ANISOU 1029 O ASN A 143 980 1081 1510 184 70 -59 O ATOM 1030 CB ASN A 143 -1.646 -15.647 7.592 1.00 9.11 C ANISOU 1030 CB ASN A 143 1156 1043 1262 14 -23 -226 C ATOM 1031 CG ASN A 143 -2.573 -16.820 7.840 1.00 11.58 C ANISOU 1031 CG ASN A 143 1431 1216 1754 70 -132 8 C ATOM 1032 OD1 ASN A 143 -3.521 -17.075 7.038 1.00 15.85 O ANISOU 1032 OD1 ASN A 143 1659 1666 2696 274 -452 -363 O ATOM 1033 ND2 ASN A 143 -2.241 -17.611 8.823 1.00 13.72 N ANISOU 1033 ND2 ASN A 143 2120 1364 1728 -505 -261 227 N ATOM 1034 N ASN A 144 0.024 -12.883 8.582 1.00 7.33 N ANISOU 1034 N ASN A 144 941 832 1013 85 -27 67 N ATOM 1035 CA ASN A 144 1.072 -11.969 8.134 1.00 7.62 C ANISOU 1035 CA ASN A 144 1093 883 916 -149 -45 79 C ATOM 1036 C ASN A 144 1.250 -10.915 9.202 1.00 7.74 C ANISOU 1036 C ASN A 144 913 1079 949 -22 -123 -95 C ATOM 1037 O ASN A 144 0.802 -9.774 9.044 1.00 8.59 O ANISOU 1037 O ASN A 144 944 1110 1206 6 -3 -12 O ATOM 1038 CB ASN A 144 0.686 -11.330 6.784 1.00 7.90 C ANISOU 1038 CB ASN A 144 1047 995 960 101 -105 43 C ATOM 1039 CG ASN A 144 0.487 -12.387 5.713 1.00 7.26 C ANISOU 1039 CG ASN A 144 828 928 1000 89 -10 -8 C ATOM 1040 OD1 ASN A 144 1.451 -12.869 5.098 1.00 9.29 O ANISOU 1040 OD1 ASN A 144 957 1326 1246 202 59 -156 O ATOM 1041 ND2 ASN A 144 -0.765 -12.795 5.512 1.00 7.88 N ANISOU 1041 ND2 ASN A 144 766 1144 1081 -29 -31 239 N ATOM 1042 N PRO A 145 1.980 -11.267 10.280 1.00 7.52 N ANISOU 1042 N PRO A 145 810 1020 1027 104 -54 -26 N ATOM 1043 CA PRO A 145 2.075 -10.358 11.423 1.00 8.18 C ANISOU 1043 CA PRO A 145 1037 1225 844 37 -83 -39 C ATOM 1044 C PRO A 145 2.879 -9.102 11.130 1.00 8.22 C ANISOU 1044 C PRO A 145 953 1246 922 61 -124 60 C ATOM 1045 O PRO A 145 2.918 -8.191 11.978 1.00 9.75 O ANISOU 1045 O PRO A 145 1268 1396 1039 9 -71 -147 O ATOM 1046 CB PRO A 145 2.746 -11.210 12.510 1.00 10.34 C ANISOU 1046 CB PRO A 145 1566 1460 900 396 -81 150 C ATOM 1047 CG PRO A 145 3.440 -12.311 11.764 1.00 12.09 C ANISOU 1047 CG PRO A 145 1944 1371 1278 452 -467 -211 C ATOM 1048 CD PRO A 145 2.546 -12.587 10.583 1.00 10.17 C ANISOU 1048 CD PRO A 145 1487 1158 1216 426 -384 -16 C ATOM 1049 N SER A 146 3.562 -9.025 9.982 1.00 7.71 N ANISOU 1049 N SER A 146 684 1096 1148 90 59 117 N ATOM 1050 CA ASER A 146 4.242 -7.771 9.656 0.50 7.78 C ANISOU 1050 CA ASER A 146 744 1073 1137 76 27 215 C ATOM 1051 CA BSER A 146 4.254 -7.789 9.607 0.50 7.43 C ANISOU 1051 CA BSER A 146 674 1067 1080 79 59 153 C ATOM 1052 C SER A 146 3.307 -6.732 9.046 1.00 7.33 C ANISOU 1052 C SER A 146 835 1025 925 -11 -196 66 C ATOM 1053 O SER A 146 3.710 -5.574 8.882 1.00 8.69 O ANISOU 1053 O SER A 146 1016 1097 1188 -68 -86 73 O ATOM 1054 CB ASER A 146 5.445 -7.984 8.739 0.50 11.56 C ANISOU 1054 CB ASER A 146 1056 1824 1511 27 316 36 C ATOM 1055 CB BSER A 146 5.376 -8.051 8.597 0.50 9.08 C ANISOU 1055 CB BSER A 146 1019 1599 829 201 99 189 C ATOM 1056 OG ASER A 146 5.019 -8.330 7.439 0.50 15.03 O ANISOU 1056 OG ASER A 146 1469 2537 1702 15 277 15 O ATOM 1057 OG BSER A 146 6.428 -8.798 9.190 0.50 9.42 O ANISOU 1057 OG BSER A 146 794 1209 1576 363 163 -156 O ATOM 1058 N LEU A 147 2.046 -7.100 8.761 1.00 7.65 N ANISOU 1058 N LEU A 147 731 1219 954 195 -122 -33 N ATOM 1059 CA LEU A 147 1.056 -6.067 8.467 1.00 7.29 C ANISOU 1059 CA LEU A 147 857 848 1064 47 -40 -124 C ATOM 1060 C LEU A 147 1.037 -5.058 9.614 1.00 6.77 C ANISOU 1060 C LEU A 147 831 936 805 -71 7 27 C ATOM 1061 O LEU A 147 1.177 -5.432 10.780 1.00 8.48 O ANISOU 1061 O LEU A 147 1153 1111 956 -49 29 53 O ATOM 1062 CB LEU A 147 -0.346 -6.687 8.306 1.00 6.97 C ANISOU 1062 CB LEU A 147 859 898 892 -75 -150 -234 C ATOM 1063 CG LEU A 147 -0.545 -7.425 6.982 1.00 6.53 C ANISOU 1063 CG LEU A 147 816 965 699 -41 -68 -47 C ATOM 1064 CD1 LEU A 147 -1.788 -8.307 7.021 1.00 7.87 C ANISOU 1064 CD1 LEU A 147 668 1151 1171 -162 -84 -38 C ATOM 1065 CD2 LEU A 147 -0.613 -6.448 5.819 1.00 8.13 C ANISOU 1065 CD2 LEU A 147 1143 1024 919 -139 -176 65 C ATOM 1066 N LYS A 148 0.854 -3.789 9.290 1.00 7.09 N ANISOU 1066 N LYS A 148 772 887 1032 25 -32 -250 N ATOM 1067 CA LYS A 148 0.939 -2.756 10.319 1.00 7.55 C ANISOU 1067 CA LYS A 148 966 1055 846 -96 -79 -196 C ATOM 1068 C LYS A 148 -0.363 -2.410 10.983 1.00 6.63 C ANISOU 1068 C LYS A 148 764 947 808 33 -171 -110 C ATOM 1069 O LYS A 148 -0.359 -1.880 12.103 1.00 7.70 O ANISOU 1069 O LYS A 148 935 1160 829 41 -133 -106 O ATOM 1070 CB LYS A 148 1.622 -1.518 9.763 1.00 10.41 C ANISOU 1070 CB LYS A 148 1527 1240 1185 -396 440 -372 C ATOM 1071 CG LYS A 148 3.093 -1.880 9.479 1.00 19.59 C ANISOU 1071 CG LYS A 148 2264 2164 3014 -447 2088 -1072 C ATOM 1072 CD LYS A 148 4.090 -0.778 9.392 1.00 19.37 C ANISOU 1072 CD LYS A 148 1738 2917 2703 -251 -94 -1507 C ATOM 1073 CE LYS A 148 4.266 -0.056 10.715 1.00 17.13 C ANISOU 1073 CE LYS A 148 1538 2542 2428 220 203 -1161 C ATOM 1074 NZ LYS A 148 4.940 1.201 10.432 1.00 20.36 N ANISOU 1074 NZ LYS A 148 2811 2496 2429 230 -137 -74 N ATOM 1075 N ALA A 149 -1.485 -2.710 10.328 1.00 6.85 N ANISOU 1075 N ALA A 149 584 1024 994 113 -56 -21 N ATOM 1076 CA ALA A 149 -2.792 -2.350 10.910 1.00 7.19 C ANISOU 1076 CA ALA A 149 757 849 1123 39 -4 -150 C ATOM 1077 C ALA A 149 -3.895 -3.130 10.229 1.00 6.13 C ANISOU 1077 C ALA A 149 765 954 608 -9 -19 -7 C ATOM 1078 O ALA A 149 -3.789 -3.485 9.046 1.00 7.31 O ANISOU 1078 O ALA A 149 921 1128 727 -24 -35 -68 O ATOM 1079 CB ALA A 149 -3.072 -0.855 10.790 1.00 8.47 C ANISOU 1079 CB ALA A 149 1152 841 1223 99 -118 -103 C ATOM 1080 N ALA A 150 -4.974 -3.339 10.972 1.00 6.22 N ANISOU 1080 N ALA A 150 687 1000 675 -15 -33 -13 N ATOM 1081 CA ALA A 150 -6.190 -3.961 10.446 1.00 6.17 C ANISOU 1081 CA ALA A 150 590 905 847 15 -50 -11 C ATOM 1082 C ALA A 150 -7.379 -3.169 10.977 1.00 6.62 C ANISOU 1082 C ALA A 150 787 1013 715 146 -80 43 C ATOM 1083 O ALA A 150 -7.388 -2.745 12.143 1.00 7.38 O ANISOU 1083 O ALA A 150 818 1151 835 35 -76 -149 O ATOM 1084 CB ALA A 150 -6.288 -5.421 10.889 1.00 7.85 C ANISOU 1084 CB ALA A 150 1001 946 1034 108 -30 170 C ATOM 1085 N ALA A 151 -8.388 -2.964 10.130 1.00 6.68 N ANISOU 1085 N ALA A 151 537 1028 972 33 -72 88 N ATOM 1086 CA ALA A 151 -9.611 -2.268 10.603 1.00 6.71 C ANISOU 1086 CA ALA A 151 585 798 1165 42 2 -10 C ATOM 1087 C ALA A 151 -10.835 -2.839 9.900 1.00 6.36 C ANISOU 1087 C ALA A 151 722 877 817 -9 95 54 C ATOM 1088 O ALA A 151 -11.501 -2.140 9.126 1.00 7.89 O ANISOU 1088 O ALA A 151 939 1193 865 64 -111 134 O ATOM 1089 CB ALA A 151 -9.505 -0.754 10.404 1.00 7.79 C ANISOU 1089 CB ALA A 151 1003 820 1136 -142 -8 13 C ATOM 1090 N PRO A 152 -11.173 -4.099 10.214 1.00 6.28 N ANISOU 1090 N PRO A 152 786 883 715 8 -33 41 N ATOM 1091 CA PRO A 152 -12.386 -4.713 9.627 1.00 7.22 C ANISOU 1091 CA PRO A 152 688 855 1200 7 29 -141 C ATOM 1092 C PRO A 152 -13.686 -4.112 10.175 1.00 6.15 C ANISOU 1092 C PRO A 152 776 814 743 -28 10 -120 C ATOM 1093 O PRO A 152 -13.701 -3.501 11.261 1.00 7.58 O ANISOU 1093 O PRO A 152 838 1076 966 -17 -12 -239 O ATOM 1094 CB PRO A 152 -12.255 -6.165 10.066 1.00 8.10 C ANISOU 1094 CB PRO A 152 1081 760 1236 156 -176 -181 C ATOM 1095 CG PRO A 152 -11.539 -6.075 11.392 1.00 9.12 C ANISOU 1095 CG PRO A 152 1319 1112 1033 -205 -118 79 C ATOM 1096 CD PRO A 152 -10.518 -4.979 11.187 1.00 7.84 C ANISOU 1096 CD PRO A 152 1059 808 1112 65 -148 176 C ATOM 1097 N GLN A 153 -14.777 -4.299 9.419 1.00 6.26 N ANISOU 1097 N GLN A 153 723 760 893 4 -92 -75 N ATOM 1098 CA GLN A 153 -16.071 -3.759 9.825 1.00 6.44 C ANISOU 1098 CA GLN A 153 602 813 1030 14 18 103 C ATOM 1099 C GLN A 153 -17.113 -4.851 9.771 1.00 6.45 C ANISOU 1099 C GLN A 153 804 887 760 -52 48 -75 C ATOM 1100 O GLN A 153 -17.175 -5.628 8.812 1.00 7.15 O ANISOU 1100 O GLN A 153 905 942 867 -86 90 -88 O ATOM 1101 CB GLN A 153 -16.484 -2.568 8.955 1.00 6.95 C ANISOU 1101 CB GLN A 153 784 1067 789 84 4 131 C ATOM 1102 CG GLN A 153 -16.667 -2.898 7.466 1.00 7.41 C ANISOU 1102 CG GLN A 153 962 896 956 -21 -9 -7 C ATOM 1103 CD GLN A 153 -16.609 -1.655 6.598 1.00 7.49 C ANISOU 1103 CD GLN A 153 865 1066 912 120 -100 66 C ATOM 1104 OE1 GLN A 153 -15.651 -0.884 6.707 1.00 7.74 O ANISOU 1104 OE1 GLN A 153 826 963 1148 63 44 117 O ATOM 1105 NE2 GLN A 153 -17.648 -1.414 5.772 1.00 8.13 N ANISOU 1105 NE2 GLN A 153 872 1132 1083 243 -160 -63 N ATOM 1106 N ALA A 154 -17.914 -4.930 10.840 1.00 7.75 N ANISOU 1106 N ALA A 154 805 1166 972 -99 260 79 N ATOM 1107 CA ALA A 154 -18.957 -5.955 10.995 1.00 8.35 C ANISOU 1107 CA ALA A 154 769 1149 1252 -110 129 6 C ATOM 1108 C ALA A 154 -18.405 -7.338 10.632 1.00 8.48 C ANISOU 1108 C ALA A 154 1085 1150 988 -153 153 -83 C ATOM 1109 O ALA A 154 -19.013 -8.085 9.862 1.00 8.96 O ANISOU 1109 O ALA A 154 1104 1207 1091 -292 239 -287 O ATOM 1110 CB ALA A 154 -20.200 -5.625 10.183 1.00 9.11 C ANISOU 1110 CB ALA A 154 996 1368 1096 -99 -16 -209 C ATOM 1111 N PRO A 155 -17.245 -7.703 11.215 1.00 8.63 N ANISOU 1111 N PRO A 155 1205 1165 906 -108 62 -120 N ATOM 1112 CA PRO A 155 -16.589 -8.938 10.770 1.00 8.87 C ANISOU 1112 CA PRO A 155 1145 1008 1215 -223 226 -15 C ATOM 1113 C PRO A 155 -17.357 -10.200 11.122 1.00 10.03 C ANISOU 1113 C PRO A 155 1427 1103 1280 -311 495 -110 C ATOM 1114 O PRO A 155 -18.091 -10.262 12.119 1.00 11.48 O ANISOU 1114 O PRO A 155 1610 1194 1558 -92 646 -63 O ATOM 1115 CB PRO A 155 -15.267 -8.931 11.542 1.00 9.74 C ANISOU 1115 CB PRO A 155 1326 1277 1098 36 -14 -34 C ATOM 1116 CG PRO A 155 -15.591 -8.130 12.801 1.00 10.47 C ANISOU 1116 CG PRO A 155 1602 1210 1165 257 -148 -81 C ATOM 1117 CD PRO A 155 -16.474 -7.002 12.263 1.00 9.99 C ANISOU 1117 CD PRO A 155 1455 1262 1077 157 -335 -97 C ATOM 1118 N TRP A 156 -17.115 -11.233 10.319 1.00 11.61 N ANISOU 1118 N TRP A 156 1788 995 1626 -264 541 -196 N ATOM 1119 CA TRP A 156 -17.567 -12.562 10.646 1.00 13.89 C ANISOU 1119 CA TRP A 156 1878 1135 2263 -394 566 15 C ATOM 1120 C TRP A 156 -16.549 -13.560 10.168 1.00 13.19 C ANISOU 1120 C TRP A 156 2231 1230 1547 -104 469 -71 C ATOM 1121 O TRP A 156 -15.986 -13.422 9.097 1.00 11.65 O ANISOU 1121 O TRP A 156 1531 1188 1707 -282 301 -117 O ATOM 1122 CB TRP A 156 -18.897 -12.849 9.985 1.00 16.13 C ANISOU 1122 CB TRP A 156 1624 1959 2543 -169 554 -411 C ATOM 1123 CG TRP A 156 -19.370 -14.241 10.305 1.00 16.80 C ANISOU 1123 CG TRP A 156 1748 2141 2493 -775 847 -655 C ATOM 1124 CD1 TRP A 156 -20.082 -14.655 11.412 1.00 21.74 C ANISOU 1124 CD1 TRP A 156 2326 2834 3098 -1124 1393 -449 C ATOM 1125 CD2 TRP A 156 -19.090 -15.422 9.530 1.00 16.77 C ANISOU 1125 CD2 TRP A 156 2240 1726 2404 -452 584 -427 C ATOM 1126 NE1 TRP A 156 -20.241 -16.023 11.363 1.00 27.58 N ANISOU 1126 NE1 TRP A 156 4759 2861 2858 -1537 777 -703 N ATOM 1127 CE2 TRP A 156 -19.638 -16.515 10.224 1.00 20.35 C ANISOU 1127 CE2 TRP A 156 2665 1954 3112 -1440 782 -660 C ATOM 1128 CE3 TRP A 156 -18.343 -15.663 8.353 1.00 18.65 C ANISOU 1128 CE3 TRP A 156 2395 2350 2341 -563 289 -732 C ATOM 1129 CZ2 TRP A 156 -19.398 -17.839 9.831 1.00 23.68 C ANISOU 1129 CZ2 TRP A 156 2954 2699 3345 -1505 507 -991 C ATOM 1130 CZ3 TRP A 156 -18.251 -16.966 7.872 1.00 21.50 C ANISOU 1130 CZ3 TRP A 156 2378 2315 3474 -825 380 -459 C ATOM 1131 CH2 TRP A 156 -18.758 -18.046 8.628 1.00 21.92 C ANISOU 1131 CH2 TRP A 156 3320 2037 2969 -301 47 -266 C ATOM 1132 N ASP A 157 -16.350 -14.596 10.980 1.00 15.34 N ANISOU 1132 N ASP A 157 2440 1684 1703 161 -23 68 N ATOM 1133 CA ASP A 157 -15.646 -15.810 10.570 1.00 14.49 C ANISOU 1133 CA ASP A 157 2414 1137 1954 -82 64 310 C ATOM 1134 C ASP A 157 -16.320 -16.936 11.350 1.00 16.41 C ANISOU 1134 C ASP A 157 3056 1455 1725 -817 -23 -237 C ATOM 1135 O ASP A 157 -17.012 -16.695 12.354 1.00 18.81 O ANISOU 1135 O ASP A 157 3342 1750 2055 -991 396 31 O ATOM 1136 CB ASP A 157 -14.162 -15.719 10.912 1.00 16.44 C ANISOU 1136 CB ASP A 157 2710 1775 1762 -148 -124 175 C ATOM 1137 CG ASP A 157 -13.354 -16.885 10.349 1.00 24.67 C ANISOU 1137 CG ASP A 157 3804 3074 2495 1451 -780 -767 C ATOM 1138 OD1 ASP A 157 -13.219 -16.988 9.119 1.00 25.37 O ANISOU 1138 OD1 ASP A 157 3093 3804 2741 850 68 136 O ATOM 1139 OD2 ASP A 157 -12.733 -17.618 11.136 1.00 31.34 O ANISOU 1139 OD2 ASP A 157 5347 3586 2971 1272 -927 -504 O ATOM 1140 N SER A 158 -16.261 -18.146 10.823 1.00 20.19 N ANISOU 1140 N SER A 158 4402 1289 1978 -892 3 -144 N ATOM 1141 CA SER A 158 -16.854 -19.283 11.552 1.00 20.54 C ANISOU 1141 CA SER A 158 4145 1552 2107 -1336 -381 20 C ATOM 1142 C SER A 158 -16.092 -19.605 12.848 1.00 24.38 C ANISOU 1142 C SER A 158 3886 3092 2283 -520 -63 331 C ATOM 1143 O SER A 158 -16.668 -20.182 13.773 1.00 26.16 O ANISOU 1143 O SER A 158 3836 3216 2885 -1582 -866 922 O ATOM 1144 CB SER A 158 -16.956 -20.515 10.653 1.00 23.19 C ANISOU 1144 CB SER A 158 4615 1632 2563 -572 80 66 C ATOM 1145 OG SER A 158 -15.691 -20.849 10.121 1.00 30.09 O ANISOU 1145 OG SER A 158 5773 1948 3712 -218 564 -861 O ATOM 1146 N SER A 159 -14.852 -19.122 12.967 1.00 20.79 N ANISOU 1146 N SER A 159 4180 1735 1982 -63 108 11 N ATOM 1147 CA SER A 159 -14.140 -19.124 14.256 1.00 20.70 C ANISOU 1147 CA SER A 159 3148 2228 2488 -394 59 -496 C ATOM 1148 C SER A 159 -14.043 -17.705 14.796 1.00 16.38 C ANISOU 1148 C SER A 159 2798 1500 1924 -691 -68 256 C ATOM 1149 O SER A 159 -13.805 -16.775 14.040 1.00 21.80 O ANISOU 1149 O SER A 159 3873 2239 2170 -1324 -241 496 O ATOM 1150 CB SER A 159 -12.724 -19.678 14.084 1.00 27.98 C ANISOU 1150 CB SER A 159 3052 3532 4047 -349 -451 330 C ATOM 1151 OG SER A 159 -11.995 -19.596 15.305 1.00 31.52 O ANISOU 1151 OG SER A 159 3606 3901 4468 51 83 -147 O ATOM 1152 N THR A 160 -14.161 -17.529 16.105 1.00 14.47 N ANISOU 1152 N THR A 160 2241 1372 1883 -258 -32 10 N ATOM 1153 CA THR A 160 -14.014 -16.196 16.680 1.00 15.21 C ANISOU 1153 CA THR A 160 2108 1490 2178 -394 -42 -137 C ATOM 1154 C THR A 160 -12.676 -16.042 17.420 1.00 15.59 C ANISOU 1154 C THR A 160 2190 1798 1933 138 -476 187 C ATOM 1155 O THR A 160 -12.385 -14.990 18.006 1.00 16.61 O ANISOU 1155 O THR A 160 2223 1774 2312 -211 -169 -56 O ATOM 1156 CB THR A 160 -15.172 -15.824 17.640 1.00 18.56 C ANISOU 1156 CB THR A 160 2106 2474 2471 -118 -85 -122 C ATOM 1157 OG1 THR A 160 -15.281 -16.798 18.687 1.00 21.67 O ANISOU 1157 OG1 THR A 160 2633 2725 2875 -603 579 157 O ATOM 1158 CG2 THR A 160 -16.501 -15.687 16.897 1.00 23.88 C ANISOU 1158 CG2 THR A 160 1972 2747 4353 -168 -689 -1045 C ATOM 1159 N ASN A 161 -11.871 -17.098 17.443 1.00 14.58 N ANISOU 1159 N ASN A 161 1926 1545 2067 -292 26 375 N ATOM 1160 CA ASN A 161 -10.612 -17.064 18.192 1.00 14.75 C ANISOU 1160 CA ASN A 161 1991 1439 2175 -305 -197 772 C ATOM 1161 C ASN A 161 -9.477 -16.486 17.356 1.00 14.07 C ANISOU 1161 C ASN A 161 2015 1548 1780 11 -113 292 C ATOM 1162 O ASN A 161 -8.881 -17.185 16.515 1.00 15.65 O ANISOU 1162 O ASN A 161 2381 1395 2169 -285 82 -7 O ATOM 1163 CB ASN A 161 -10.255 -18.492 18.657 1.00 19.12 C ANISOU 1163 CB ASN A 161 2777 1610 2876 33 -611 1020 C ATOM 1164 CG ASN A 161 -8.925 -18.571 19.386 1.00 19.31 C ANISOU 1164 CG ASN A 161 2757 1602 2979 -382 -686 952 C ATOM 1165 OD1 ASN A 161 -8.563 -19.657 19.866 1.00 33.06 O ANISOU 1165 OD1 ASN A 161 4126 2210 6222 -666 -2156 2146 O ATOM 1166 ND2 ASN A 161 -8.329 -17.436 19.690 1.00 17.43 N ANISOU 1166 ND2 ASN A 161 2366 1742 2512 -272 -547 1325 N ATOM 1167 N PHE A 162 -9.239 -15.191 17.542 1.00 12.02 N ANISOU 1167 N PHE A 162 1599 1445 1522 -219 -302 587 N ATOM 1168 CA PHE A 162 -8.166 -14.506 16.848 1.00 10.94 C ANISOU 1168 CA PHE A 162 1497 1167 1491 -32 -157 469 C ATOM 1169 C PHE A 162 -7.099 -14.081 17.836 1.00 11.90 C ANISOU 1169 C PHE A 162 1530 1418 1573 212 -149 538 C ATOM 1170 O PHE A 162 -6.392 -13.078 17.628 1.00 11.07 O ANISOU 1170 O PHE A 162 1511 1355 1339 -61 -97 431 O ATOM 1171 CB PHE A 162 -8.719 -13.335 16.015 1.00 10.77 C ANISOU 1171 CB PHE A 162 1731 1155 1205 144 -281 170 C ATOM 1172 CG PHE A 162 -9.361 -13.810 14.725 1.00 10.18 C ANISOU 1172 CG PHE A 162 1387 1125 1354 -128 -66 162 C ATOM 1173 CD1 PHE A 162 -8.576 -14.088 13.623 1.00 11.90 C ANISOU 1173 CD1 PHE A 162 1873 1269 1377 -77 231 30 C ATOM 1174 CD2 PHE A 162 -10.723 -14.064 14.651 1.00 11.98 C ANISOU 1174 CD2 PHE A 162 1694 1366 1491 -410 -193 101 C ATOM 1175 CE1 PHE A 162 -9.127 -14.611 12.472 1.00 12.57 C ANISOU 1175 CE1 PHE A 162 1819 1305 1649 -60 -49 201 C ATOM 1176 CE2 PHE A 162 -11.294 -14.547 13.500 1.00 15.53 C ANISOU 1176 CE2 PHE A 162 1903 2254 1743 -477 -279 115 C ATOM 1177 CZ PHE A 162 -10.492 -14.827 12.396 1.00 14.61 C ANISOU 1177 CZ PHE A 162 2051 1590 1910 -263 -149 85 C ATOM 1178 N SER A 163 -6.839 -14.953 18.814 1.00 12.16 N ANISOU 1178 N SER A 163 1695 1498 1425 98 -279 582 N ATOM 1179 CA SER A 163 -5.726 -14.712 19.721 1.00 13.38 C ANISOU 1179 CA SER A 163 1761 1830 1492 134 -202 686 C ATOM 1180 C SER A 163 -4.382 -14.762 18.982 1.00 12.10 C ANISOU 1180 C SER A 163 1705 1201 1690 -65 -210 476 C ATOM 1181 O SER A 163 -3.376 -14.283 19.516 1.00 14.22 O ANISOU 1181 O SER A 163 1871 1683 1846 -4 -229 76 O ATOM 1182 CB SER A 163 -5.754 -15.713 20.884 1.00 13.66 C ANISOU 1182 CB SER A 163 1928 1597 1664 -224 -272 664 C ATOM 1183 OG SER A 163 -5.644 -17.034 20.396 1.00 19.23 O ANISOU 1183 OG SER A 163 2837 1826 2641 28 -870 876 O ATOM 1184 N SER A 164 -4.384 -15.290 17.748 1.00 12.69 N ANISOU 1184 N SER A 164 1930 1232 1657 292 -57 281 N ATOM 1185 CA SER A 164 -3.209 -15.278 16.877 1.00 14.32 C ANISOU 1185 CA SER A 164 2561 1166 1714 243 326 281 C ATOM 1186 C SER A 164 -2.799 -13.878 16.400 1.00 13.81 C ANISOU 1186 C SER A 164 1693 1289 2266 249 281 221 C ATOM 1187 O SER A 164 -1.716 -13.724 15.837 1.00 15.58 O ANISOU 1187 O SER A 164 1922 1675 2320 378 278 158 O ATOM 1188 CB SER A 164 -3.444 -16.146 15.609 1.00 17.42 C ANISOU 1188 CB SER A 164 3057 1296 2264 224 100 -258 C ATOM 1189 OG SER A 164 -4.703 -15.793 15.038 1.00 23.68 O ANISOU 1189 OG SER A 164 4196 2665 2134 -312 -302 -8 O ATOM 1190 N VAL A 165 -3.702 -12.893 16.483 1.00 10.70 N ANISOU 1190 N VAL A 165 1556 1121 1386 72 -28 208 N ATOM 1191 CA VAL A 165 -3.452 -11.601 15.820 1.00 10.09 C ANISOU 1191 CA VAL A 165 1274 1057 1501 15 -12 53 C ATOM 1192 C VAL A 165 -2.606 -10.690 16.684 1.00 8.86 C ANISOU 1192 C VAL A 165 1133 1135 1096 79 36 28 C ATOM 1193 O VAL A 165 -2.990 -10.318 17.797 1.00 11.44 O ANISOU 1193 O VAL A 165 1557 1552 1236 -37 337 153 O ATOM 1194 CB VAL A 165 -4.796 -10.923 15.462 1.00 10.03 C ANISOU 1194 CB VAL A 165 1142 1194 1474 17 -55 124 C ATOM 1195 CG1 VAL A 165 -4.559 -9.508 14.939 1.00 10.53 C ANISOU 1195 CG1 VAL A 165 1515 1078 1408 -40 23 252 C ATOM 1196 CG2 VAL A 165 -5.544 -11.771 14.453 1.00 11.92 C ANISOU 1196 CG2 VAL A 165 1725 1411 1391 -2 107 -110 C ATOM 1197 N THR A 166 -1.465 -10.255 16.145 1.00 9.33 N ANISOU 1197 N THR A 166 1149 1075 1318 137 92 157 N ATOM 1198 CA THR A 166 -0.592 -9.364 16.883 1.00 8.32 C ANISOU 1198 CA THR A 166 1117 1035 1009 116 -22 152 C ATOM 1199 C THR A 166 -0.571 -7.971 16.252 1.00 8.90 C ANISOU 1199 C THR A 166 1093 1175 1111 -161 24 231 C ATOM 1200 O THR A 166 0.143 -7.089 16.690 1.00 11.13 O ANISOU 1200 O THR A 166 1527 1350 1351 -238 -289 217 O ATOM 1201 CB THR A 166 0.836 -9.916 16.961 1.00 12.06 C ANISOU 1201 CB THR A 166 1441 1759 1381 624 146 378 C ATOM 1202 OG1 THR A 166 1.366 -10.059 15.647 1.00 12.16 O ANISOU 1202 OG1 THR A 166 1375 1586 1656 189 178 24 O ATOM 1203 CG2 THR A 166 0.858 -11.294 17.644 1.00 15.30 C ANISOU 1203 CG2 THR A 166 1640 1966 2206 751 298 770 C ATOM 1204 N VAL A 167 -1.320 -7.812 15.174 1.00 8.30 N ANISOU 1204 N VAL A 167 983 1133 1036 309 0 314 N ATOM 1205 CA VAL A 167 -1.375 -6.567 14.405 1.00 7.60 C ANISOU 1205 CA VAL A 167 1011 992 882 108 -6 183 C ATOM 1206 C VAL A 167 -2.387 -5.620 15.077 1.00 7.34 C ANISOU 1206 C VAL A 167 945 870 972 74 18 63 C ATOM 1207 O VAL A 167 -3.461 -6.072 15.475 1.00 7.84 O ANISOU 1207 O VAL A 167 996 1076 904 77 -26 35 O ATOM 1208 CB VAL A 167 -1.880 -6.895 12.988 1.00 7.46 C ANISOU 1208 CB VAL A 167 1242 770 821 118 -41 -25 C ATOM 1209 CG1 VAL A 167 -2.104 -5.624 12.139 1.00 8.21 C ANISOU 1209 CG1 VAL A 167 1307 958 852 115 -88 212 C ATOM 1210 CG2 VAL A 167 -0.893 -7.841 12.316 1.00 8.35 C ANISOU 1210 CG2 VAL A 167 1124 1002 1046 125 69 -39 C ATOM 1211 N PRO A 168 -2.068 -4.320 15.213 1.00 7.38 N ANISOU 1211 N PRO A 168 798 1040 964 104 -41 -83 N ATOM 1212 CA PRO A 168 -3.041 -3.371 15.768 1.00 7.12 C ANISOU 1212 CA PRO A 168 727 914 1061 46 -71 -21 C ATOM 1213 C PRO A 168 -4.364 -3.441 15.013 1.00 7.68 C ANISOU 1213 C PRO A 168 883 1208 826 166 -40 91 C ATOM 1214 O PRO A 168 -4.405 -3.140 13.808 1.00 7.59 O ANISOU 1214 O PRO A 168 910 1182 792 64 -78 49 O ATOM 1215 CB PRO A 168 -2.353 -2.012 15.561 1.00 8.54 C ANISOU 1215 CB PRO A 168 794 1067 1381 -148 -254 41 C ATOM 1216 CG PRO A 168 -0.889 -2.349 15.682 1.00 8.50 C ANISOU 1216 CG PRO A 168 869 1105 1254 118 -41 -128 C ATOM 1217 CD PRO A 168 -0.777 -3.670 14.946 1.00 8.33 C ANISOU 1217 CD PRO A 168 929 927 1308 -82 5 -98 C ATOM 1218 N THR A 169 -5.454 -3.706 15.732 1.00 7.18 N ANISOU 1218 N THR A 169 762 1007 959 92 -41 -93 N ATOM 1219 CA THR A 169 -6.727 -4.018 15.072 1.00 7.04 C ANISOU 1219 CA THR A 169 809 970 896 30 -17 0 C ATOM 1220 C THR A 169 -7.884 -3.226 15.665 1.00 6.71 C ANISOU 1220 C THR A 169 881 873 794 -24 -41 46 C ATOM 1221 O THR A 169 -8.151 -3.321 16.866 1.00 7.96 O ANISOU 1221 O THR A 169 1054 1242 728 124 13 -8 O ATOM 1222 CB THR A 169 -7.029 -5.527 15.162 1.00 7.64 C ANISOU 1222 CB THR A 169 907 983 1010 -43 -44 4 C ATOM 1223 OG1 THR A 169 -6.046 -6.246 14.438 1.00 8.36 O ANISOU 1223 OG1 THR A 169 1147 970 1057 174 12 3 O ATOM 1224 CG2 THR A 169 -8.396 -5.855 14.549 1.00 8.96 C ANISOU 1224 CG2 THR A 169 967 1240 1196 -126 -236 15 C ATOM 1225 N LEU A 170 -8.536 -2.434 14.824 1.00 6.81 N ANISOU 1225 N LEU A 170 768 988 831 153 -2 22 N ATOM 1226 CA LEU A 170 -9.753 -1.716 15.151 1.00 7.25 C ANISOU 1226 CA LEU A 170 763 998 992 82 12 84 C ATOM 1227 C LEU A 170 -10.927 -2.472 14.537 1.00 7.10 C ANISOU 1227 C LEU A 170 904 930 862 14 154 -60 C ATOM 1228 O LEU A 170 -10.951 -2.694 13.312 1.00 8.43 O ANISOU 1228 O LEU A 170 1115 1303 783 -113 24 -80 O ATOM 1229 CB LEU A 170 -9.662 -0.292 14.548 1.00 7.68 C ANISOU 1229 CB LEU A 170 1031 827 1059 178 -106 54 C ATOM 1230 CG LEU A 170 -10.964 0.530 14.438 1.00 7.51 C ANISOU 1230 CG LEU A 170 932 823 1096 190 193 10 C ATOM 1231 CD1 LEU A 170 -11.647 0.751 15.789 1.00 9.66 C ANISOU 1231 CD1 LEU A 170 1325 1357 988 73 20 -72 C ATOM 1232 CD2 LEU A 170 -10.627 1.882 13.774 1.00 9.00 C ANISOU 1232 CD2 LEU A 170 1086 996 1335 185 -41 163 C ATOM 1233 N ILE A 171 -11.889 -2.865 15.361 1.00 7.53 N ANISOU 1233 N ILE A 171 766 1094 1001 -50 57 -66 N ATOM 1234 CA ILE A 171 -13.086 -3.536 14.875 1.00 7.99 C ANISOU 1234 CA ILE A 171 815 1072 1147 -81 -3 -139 C ATOM 1235 C ILE A 171 -14.242 -2.539 14.921 1.00 7.81 C ANISOU 1235 C ILE A 171 964 1056 947 41 45 -152 C ATOM 1236 O ILE A 171 -14.653 -2.087 15.993 1.00 9.24 O ANISOU 1236 O ILE A 171 1077 1389 1043 134 48 -271 O ATOM 1237 CB ILE A 171 -13.415 -4.752 15.751 1.00 9.94 C ANISOU 1237 CB ILE A 171 851 1058 1868 -68 -114 103 C ATOM 1238 CG1 ILE A 171 -12.318 -5.811 15.516 1.00 16.35 C ANISOU 1238 CG1 ILE A 171 1018 1734 3457 -205 82 661 C ATOM 1239 CG2 ILE A 171 -14.806 -5.325 15.443 1.00 12.04 C ANISOU 1239 CG2 ILE A 171 1112 1454 2007 -169 -76 -6 C ATOM 1240 CD1 ILE A 171 -12.435 -7.020 16.377 1.00 17.88 C ANISOU 1240 CD1 ILE A 171 2257 2064 2469 159 -174 506 C ATOM 1241 N PHE A 172 -14.761 -2.184 13.750 1.00 7.80 N ANISOU 1241 N PHE A 172 930 1013 1018 22 71 -64 N ATOM 1242 CA PHE A 172 -16.057 -1.519 13.687 1.00 7.94 C ANISOU 1242 CA PHE A 172 868 1021 1125 -55 56 27 C ATOM 1243 C PHE A 172 -17.151 -2.563 13.788 1.00 7.60 C ANISOU 1243 C PHE A 172 718 1137 1031 -3 12 -282 C ATOM 1244 O PHE A 172 -17.099 -3.582 13.116 1.00 9.04 O ANISOU 1244 O PHE A 172 1072 1233 1128 -81 119 -286 O ATOM 1245 CB PHE A 172 -16.206 -0.768 12.341 1.00 8.22 C ANISOU 1245 CB PHE A 172 1094 1028 999 -122 -142 105 C ATOM 1246 CG PHE A 172 -15.226 0.360 12.141 1.00 7.90 C ANISOU 1246 CG PHE A 172 946 956 1100 160 12 103 C ATOM 1247 CD1 PHE A 172 -15.351 1.553 12.856 1.00 8.74 C ANISOU 1247 CD1 PHE A 172 1079 994 1246 16 -336 127 C ATOM 1248 CD2 PHE A 172 -14.156 0.228 11.246 1.00 9.22 C ANISOU 1248 CD2 PHE A 172 938 1316 1249 -106 -42 190 C ATOM 1249 CE1 PHE A 172 -14.462 2.600 12.652 1.00 10.33 C ANISOU 1249 CE1 PHE A 172 1344 1170 1411 -40 -361 119 C ATOM 1250 CE2 PHE A 172 -13.322 1.293 10.993 1.00 10.83 C ANISOU 1250 CE2 PHE A 172 1480 1463 1169 -159 -130 282 C ATOM 1251 CZ PHE A 172 -13.447 2.457 11.731 1.00 11.07 C ANISOU 1251 CZ PHE A 172 1519 1227 1458 30 -307 395 C ATOM 1252 N ALA A 173 -18.164 -2.257 14.581 1.00 8.25 N ANISOU 1252 N ALA A 173 788 1218 1126 -57 180 40 N ATOM 1253 CA ALA A 173 -19.278 -3.177 14.755 1.00 8.84 C ANISOU 1253 CA ALA A 173 983 1202 1171 -108 205 23 C ATOM 1254 C ALA A 173 -20.564 -2.378 14.590 1.00 8.54 C ANISOU 1254 C ALA A 173 1081 970 1193 -45 253 -285 C ATOM 1255 O ALA A 173 -20.570 -1.155 14.721 1.00 8.56 O ANISOU 1255 O ALA A 173 999 1049 1204 6 69 -122 O ATOM 1256 CB ALA A 173 -19.219 -3.849 16.121 1.00 10.82 C ANISOU 1256 CB ALA A 173 1228 1305 1576 -61 278 371 C ATOM 1257 N CYS A 174 -21.659 -3.083 14.359 1.00 9.24 N ANISOU 1257 N CYS A 174 933 1364 1212 6 108 57 N ATOM 1258 CA CYS A 174 -22.946 -2.415 14.075 1.00 9.35 C ANISOU 1258 CA CYS A 174 945 1594 1013 69 28 52 C ATOM 1259 C CYS A 174 -23.967 -2.980 15.068 1.00 9.21 C ANISOU 1259 C CYS A 174 1043 1159 1294 -33 38 -108 C ATOM 1260 O CYS A 174 -24.247 -4.178 15.066 1.00 9.80 O ANISOU 1260 O CYS A 174 1050 1316 1356 -57 176 -45 O ATOM 1261 CB CYS A 174 -23.358 -2.717 12.623 1.00 9.93 C ANISOU 1261 CB CYS A 174 843 1800 1127 -118 122 -4 C ATOM 1262 SG CYS A 174 -22.159 -2.111 11.415 1.00 10.61 S ANISOU 1262 SG CYS A 174 1191 1528 1310 8 59 -97 S ATOM 1263 N GLU A 175 -24.497 -2.132 15.948 1.00 9.86 N ANISOU 1263 N GLU A 175 1241 1245 1259 -42 310 -99 N ATOM 1264 CA GLU A 175 -25.215 -2.610 17.133 1.00 10.13 C ANISOU 1264 CA GLU A 175 1249 1377 1223 -107 238 -131 C ATOM 1265 C GLU A 175 -26.287 -3.637 16.794 1.00 10.24 C ANISOU 1265 C GLU A 175 1284 1413 1191 -4 272 47 C ATOM 1266 O GLU A 175 -26.422 -4.648 17.479 1.00 12.30 O ANISOU 1266 O GLU A 175 1391 1688 1594 -85 399 70 O ATOM 1267 CB GLU A 175 -25.856 -1.436 17.861 1.00 11.03 C ANISOU 1267 CB GLU A 175 1223 1611 1357 25 349 -123 C ATOM 1268 CG GLU A 175 -26.548 -1.898 19.146 1.00 12.07 C ANISOU 1268 CG GLU A 175 1666 1491 1429 -80 311 -42 C ATOM 1269 CD GLU A 175 -27.205 -0.765 19.904 1.00 15.01 C ANISOU 1269 CD GLU A 175 2051 1957 1695 394 413 -164 C ATOM 1270 OE1 GLU A 175 -27.610 0.233 19.276 1.00 15.49 O ANISOU 1270 OE1 GLU A 175 1921 2195 1768 317 570 -95 O ATOM 1271 OE2 GLU A 175 -27.328 -0.892 21.135 1.00 18.56 O ANISOU 1271 OE2 GLU A 175 2763 2599 1688 218 757 -21 O ATOM 1272 N ASN A 176 -27.083 -3.331 15.775 1.00 11.08 N ANISOU 1272 N ASN A 176 921 1797 1490 51 201 -201 N ATOM 1273 CA ASN A 176 -28.282 -4.115 15.460 1.00 11.63 C ANISOU 1273 CA ASN A 176 955 1884 1580 -63 -54 -457 C ATOM 1274 C ASN A 176 -28.030 -5.069 14.311 1.00 12.57 C ANISOU 1274 C ASN A 176 1140 2092 1541 20 17 -467 C ATOM 1275 O ASN A 176 -28.951 -5.516 13.655 1.00 16.41 O ANISOU 1275 O ASN A 176 1321 2421 2490 114 -95 -1147 O ATOM 1276 CB ASN A 176 -29.451 -3.178 15.140 1.00 13.99 C ANISOU 1276 CB ASN A 176 1177 2095 2041 178 186 -248 C ATOM 1277 CG ASN A 176 -29.945 -2.437 16.357 1.00 17.68 C ANISOU 1277 CG ASN A 176 1848 2568 2299 -105 330 -235 C ATOM 1278 OD1 ASN A 176 -29.685 -2.844 17.481 1.00 23.17 O ANISOU 1278 OD1 ASN A 176 2301 3866 2633 453 803 -723 O ATOM 1279 ND2 ASN A 176 -30.748 -1.404 16.132 1.00 25.91 N ANISOU 1279 ND2 ASN A 176 2742 2861 4239 572 606 -227 N ATOM 1280 N ASP A 177 -26.769 -5.432 14.094 1.00 11.96 N ANISOU 1280 N ASP A 177 1207 1769 1567 75 320 -216 N ATOM 1281 CA ASP A 177 -26.434 -6.367 13.015 1.00 10.61 C ANISOU 1281 CA ASP A 177 879 1433 1717 -124 422 -202 C ATOM 1282 C ASP A 177 -27.177 -7.698 13.217 1.00 11.44 C ANISOU 1282 C ASP A 177 1238 1689 1417 -257 314 -195 C ATOM 1283 O ASP A 177 -27.002 -8.376 14.260 1.00 13.10 O ANISOU 1283 O ASP A 177 1283 1772 1922 -302 126 -61 O ATOM 1284 CB ASP A 177 -24.935 -6.621 13.073 1.00 10.88 C ANISOU 1284 CB ASP A 177 977 1753 1403 -65 218 -279 C ATOM 1285 CG ASP A 177 -24.388 -7.187 11.781 1.00 10.47 C ANISOU 1285 CG ASP A 177 1277 1271 1429 -183 274 -304 C ATOM 1286 OD1 ASP A 177 -25.064 -8.034 11.166 1.00 11.03 O ANISOU 1286 OD1 ASP A 177 1068 1455 1666 -210 78 -220 O ATOM 1287 OD2 ASP A 177 -23.227 -6.845 11.423 1.00 10.69 O ANISOU 1287 OD2 ASP A 177 1079 1516 1466 -223 188 -166 O ATOM 1288 N SER A 178 -27.970 -8.102 12.212 1.00 12.74 N ANISOU 1288 N SER A 178 1169 1787 1884 -285 225 -506 N ATOM 1289 CA ASER A 178 -28.701 -9.365 12.274 0.50 14.24 C ANISOU 1289 CA ASER A 178 1276 1835 2299 -447 259 -505 C ATOM 1290 CA BSER A 178 -28.704 -9.368 12.271 0.50 14.28 C ANISOU 1290 CA BSER A 178 1275 1838 2311 -447 266 -511 C ATOM 1291 C SER A 178 -28.033 -10.471 11.454 1.00 12.73 C ANISOU 1291 C SER A 178 1593 1620 1624 -435 85 -334 C ATOM 1292 O SER A 178 -28.472 -11.612 11.461 1.00 15.65 O ANISOU 1292 O SER A 178 2194 1596 2154 -671 304 -550 O ATOM 1293 CB ASER A 178 -30.140 -9.166 11.785 0.50 19.56 C ANISOU 1293 CB ASER A 178 1381 2736 3315 -358 3 -343 C ATOM 1294 CB BSER A 178 -30.145 -9.190 11.772 0.50 18.60 C ANISOU 1294 CB BSER A 178 1409 2723 2935 -277 78 -230 C ATOM 1295 OG ASER A 178 -30.168 -8.938 10.383 0.50 22.87 O ANISOU 1295 OG ASER A 178 1757 3348 3582 -323 -443 -225 O ATOM 1296 OG BSER A 178 -30.846 -8.212 12.513 0.50 20.19 O ANISOU 1296 OG BSER A 178 1463 3014 3194 -237 -77 -750 O ATOM 1297 N ILE A 179 -27.031 -10.095 10.678 1.00 12.30 N ANISOU 1297 N ILE A 179 1366 1464 1843 -174 86 -52 N ATOM 1298 CA ILE A 179 -26.342 -11.029 9.787 1.00 11.76 C ANISOU 1298 CA ILE A 179 1356 1477 1634 -336 -37 -124 C ATOM 1299 C ILE A 179 -25.101 -11.604 10.468 1.00 12.10 C ANISOU 1299 C ILE A 179 1403 1510 1682 -125 -72 -235 C ATOM 1300 O ILE A 179 -24.871 -12.822 10.427 1.00 14.47 O ANISOU 1300 O ILE A 179 1889 1500 2107 -161 -357 -312 O ATOM 1301 CB ILE A 179 -25.914 -10.319 8.506 1.00 12.75 C ANISOU 1301 CB ILE A 179 1703 1715 1424 100 75 31 C ATOM 1302 CG1 ILE A 179 -27.133 -9.756 7.776 1.00 22.20 C ANISOU 1302 CG1 ILE A 179 2407 2537 3489 919 -144 18 C ATOM 1303 CG2 ILE A 179 -25.041 -11.212 7.635 1.00 15.70 C ANISOU 1303 CG2 ILE A 179 2661 1558 1744 -175 558 -266 C ATOM 1304 CD1 ILE A 179 -27.892 -10.823 7.062 1.00 28.61 C ANISOU 1304 CD1 ILE A 179 3228 3647 3995 -667 -752 604 C ATOM 1305 N ALA A 180 -24.319 -10.724 11.110 1.00 11.94 N ANISOU 1305 N ALA A 180 1369 1832 1335 -225 -128 -232 N ATOM 1306 CA ALA A 180 -23.187 -11.142 11.925 1.00 12.74 C ANISOU 1306 CA ALA A 180 1298 1893 1649 -205 -61 -363 C ATOM 1307 C ALA A 180 -23.330 -10.516 13.304 1.00 12.09 C ANISOU 1307 C ALA A 180 1511 1536 1545 -124 -86 -107 C ATOM 1308 O ALA A 180 -22.743 -9.472 13.579 1.00 11.23 O ANISOU 1308 O ALA A 180 1360 1482 1422 -126 66 -194 O ATOM 1309 CB ALA A 180 -21.869 -10.728 11.251 1.00 14.82 C ANISOU 1309 CB ALA A 180 1428 2500 1703 73 325 -330 C ATOM 1310 N PRO A 181 -24.248 -11.056 14.117 1.00 11.66 N ANISOU 1310 N PRO A 181 1421 1509 1500 -256 -12 -265 N ATOM 1311 CA PRO A 181 -24.582 -10.403 15.383 1.00 13.61 C ANISOU 1311 CA PRO A 181 1489 1966 1716 -564 102 -511 C ATOM 1312 C PRO A 181 -23.332 -10.103 16.194 1.00 11.48 C ANISOU 1312 C PRO A 181 1627 1528 1204 -140 122 6 C ATOM 1313 O PRO A 181 -22.437 -10.954 16.318 1.00 12.64 O ANISOU 1313 O PRO A 181 1452 1779 1570 -9 62 -79 O ATOM 1314 CB PRO A 181 -25.470 -11.446 16.081 1.00 15.09 C ANISOU 1314 CB PRO A 181 1778 2072 1880 -552 272 -255 C ATOM 1315 CG PRO A 181 -26.137 -12.165 14.947 1.00 17.64 C ANISOU 1315 CG PRO A 181 1890 2098 2713 -486 232 -468 C ATOM 1316 CD PRO A 181 -25.053 -12.278 13.907 1.00 14.91 C ANISOU 1316 CD PRO A 181 1749 1772 2144 -561 54 -764 C ATOM 1317 N VAL A 182 -23.320 -8.938 16.822 1.00 10.39 N ANISOU 1317 N VAL A 182 1245 1554 1148 -254 77 -110 N ATOM 1318 CA VAL A 182 -22.163 -8.509 17.579 1.00 10.88 C ANISOU 1318 CA VAL A 182 1189 1556 1388 -31 36 -118 C ATOM 1319 C VAL A 182 -21.805 -9.517 18.668 1.00 10.98 C ANISOU 1319 C VAL A 182 1299 1745 1125 -242 165 6 C ATOM 1320 O VAL A 182 -20.643 -9.849 18.856 1.00 12.40 O ANISOU 1320 O VAL A 182 1313 1642 1756 -297 138 208 O ATOM 1321 CB VAL A 182 -22.403 -7.118 18.168 1.00 11.76 C ANISOU 1321 CB VAL A 182 1640 1405 1422 -118 -200 -57 C ATOM 1322 CG1 VAL A 182 -21.289 -6.775 19.138 1.00 15.30 C ANISOU 1322 CG1 VAL A 182 1741 1817 2255 -113 -498 -383 C ATOM 1323 CG2 VAL A 182 -22.521 -6.072 17.044 1.00 14.79 C ANISOU 1323 CG2 VAL A 182 2054 1606 1960 -49 231 241 C ATOM 1324 N ASN A 183 -22.800 -10.079 19.353 1.00 11.88 N ANISOU 1324 N ASN A 183 1499 1696 1316 -229 279 124 N ATOM 1325 CA ASN A 183 -22.500 -10.924 20.503 1.00 12.96 C ANISOU 1325 CA ASN A 183 1701 1996 1225 -212 418 318 C ATOM 1326 C ASN A 183 -21.924 -12.283 20.127 1.00 13.63 C ANISOU 1326 C ASN A 183 1328 2074 1776 26 313 217 C ATOM 1327 O ASN A 183 -21.340 -12.978 20.978 1.00 16.63 O ANISOU 1327 O ASN A 183 2087 2156 2074 -80 282 607 O ATOM 1328 CB ASN A 183 -23.728 -11.103 21.391 1.00 15.66 C ANISOU 1328 CB ASN A 183 2058 2123 1768 -157 884 27 C ATOM 1329 CG ASN A 183 -23.991 -9.887 22.208 1.00 19.45 C ANISOU 1329 CG ASN A 183 2350 2544 2495 -694 548 -769 C ATOM 1330 OD1 ASN A 183 -23.074 -9.124 22.461 1.00 26.79 O ANISOU 1330 OD1 ASN A 183 3770 2852 3555 -1518 723 -586 O ATOM 1331 ND2 ASN A 183 -25.216 -9.736 22.697 1.00 24.27 N ANISOU 1331 ND2 ASN A 183 2615 3568 3039 -191 1186 -511 N ATOM 1332 N SER A 184 -22.132 -12.704 18.881 1.00 14.06 N ANISOU 1332 N SER A 184 1511 1764 2066 -506 503 98 N ATOM 1333 CA SER A 184 -21.554 -13.969 18.427 1.00 13.98 C ANISOU 1333 CA SER A 184 1516 1629 2167 -448 397 40 C ATOM 1334 C SER A 184 -20.391 -13.804 17.448 1.00 13.35 C ANISOU 1334 C SER A 184 1731 1455 1885 -277 309 198 C ATOM 1335 O SER A 184 -19.781 -14.791 17.057 1.00 15.31 O ANISOU 1335 O SER A 184 1702 1539 2575 -378 506 196 O ATOM 1336 CB SER A 184 -22.627 -14.843 17.787 1.00 15.73 C ANISOU 1336 CB SER A 184 1882 2104 1990 -538 194 94 C ATOM 1337 OG SER A 184 -23.136 -14.162 16.655 1.00 18.75 O ANISOU 1337 OG SER A 184 2566 2182 2372 -424 -295 96 O ATOM 1338 N SER A 185 -20.104 -12.570 17.035 1.00 10.83 N ANISOU 1338 N SER A 185 1174 1488 1452 -268 104 214 N ATOM 1339 CA ASER A 185 -19.141 -12.316 15.979 0.50 12.27 C ANISOU 1339 CA ASER A 185 1637 1422 1601 -543 312 -118 C ATOM 1340 CA BSER A 185 -19.108 -12.336 15.989 0.50 11.35 C ANISOU 1340 CA BSER A 185 1538 1365 1410 -443 187 -15 C ATOM 1341 C SER A 185 -18.124 -11.244 16.404 1.00 10.39 C ANISOU 1341 C SER A 185 1301 1265 1379 -117 161 -122 C ATOM 1342 O SER A 185 -17.098 -11.539 17.011 1.00 11.25 O ANISOU 1342 O SER A 185 1449 1465 1360 -112 134 224 O ATOM 1343 CB ASER A 185 -19.892 -11.915 14.690 0.50 16.07 C ANISOU 1343 CB ASER A 185 1961 2840 1305 -2200 14 -317 C ATOM 1344 CB BSER A 185 -19.787 -12.035 14.635 0.50 15.80 C ANISOU 1344 CB BSER A 185 2467 2542 992 -870 303 -122 C ATOM 1345 OG ASER A 185 -19.059 -12.125 13.584 0.50 22.70 O ANISOU 1345 OG ASER A 185 2745 2742 3134 -721 1004 -828 O ATOM 1346 OG BSER A 185 -20.865 -12.928 14.425 0.50 15.23 O ANISOU 1346 OG BSER A 185 2235 1784 1767 -211 43 261 O ATOM 1347 N ALA A 186 -18.452 -9.979 16.148 1.00 10.27 N ANISOU 1347 N ALA A 186 1390 1164 1346 -167 153 -3 N ATOM 1348 CA ALA A 186 -17.468 -8.924 16.381 1.00 10.23 C ANISOU 1348 CA ALA A 186 1339 1430 1117 -324 -128 40 C ATOM 1349 C ALA A 186 -16.942 -8.899 17.816 1.00 9.61 C ANISOU 1349 C ALA A 186 1049 1398 1202 -48 106 147 C ATOM 1350 O ALA A 186 -15.747 -8.705 18.015 1.00 10.03 O ANISOU 1350 O ALA A 186 1156 1503 1152 -152 -84 289 O ATOM 1351 CB ALA A 186 -18.048 -7.566 16.008 1.00 10.86 C ANISOU 1351 CB ALA A 186 1290 1384 1451 -264 -136 303 C ATOM 1352 N LEU A 187 -17.820 -9.025 18.821 1.00 10.80 N ANISOU 1352 N LEU A 187 1448 1710 947 -293 126 118 N ATOM 1353 CA LEU A 187 -17.335 -8.887 20.196 1.00 10.66 C ANISOU 1353 CA LEU A 187 1185 1796 1069 -24 -1 194 C ATOM 1354 C LEU A 187 -16.462 -10.048 20.677 1.00 10.87 C ANISOU 1354 C LEU A 187 1438 1461 1228 -232 59 53 C ATOM 1355 O LEU A 187 -15.364 -9.803 21.183 1.00 11.24 O ANISOU 1355 O LEU A 187 1244 1816 1209 -172 -47 296 O ATOM 1356 CB LEU A 187 -18.458 -8.557 21.172 1.00 12.91 C ANISOU 1356 CB LEU A 187 1414 2382 1109 -200 173 13 C ATOM 1357 CG LEU A 187 -18.037 -8.309 22.627 1.00 13.02 C ANISOU 1357 CG LEU A 187 1540 2230 1173 -159 151 -107 C ATOM 1358 CD1 LEU A 187 -17.025 -7.165 22.743 1.00 14.92 C ANISOU 1358 CD1 LEU A 187 1983 2090 1596 -381 -39 -273 C ATOM 1359 CD2 LEU A 187 -19.287 -8.018 23.471 1.00 18.94 C ANISOU 1359 CD2 LEU A 187 1981 3383 1832 205 682 -154 C ATOM 1360 N PRO A 188 -16.872 -11.305 20.415 1.00 10.77 N ANISOU 1360 N PRO A 188 1429 1493 1168 -190 -24 267 N ATOM 1361 CA PRO A 188 -15.957 -12.383 20.802 1.00 11.18 C ANISOU 1361 CA PRO A 188 1453 1642 1153 -305 131 351 C ATOM 1362 C PRO A 188 -14.643 -12.329 20.021 1.00 11.13 C ANISOU 1362 C PRO A 188 1335 1570 1324 113 164 336 C ATOM 1363 O PRO A 188 -13.574 -12.632 20.573 1.00 11.65 O ANISOU 1363 O PRO A 188 1440 1626 1357 -144 -29 443 O ATOM 1364 CB PRO A 188 -16.722 -13.676 20.486 1.00 15.04 C ANISOU 1364 CB PRO A 188 1793 1995 1926 -299 36 161 C ATOM 1365 CG PRO A 188 -18.091 -13.278 20.128 1.00 20.21 C ANISOU 1365 CG PRO A 188 2437 1657 3584 -221 -1068 264 C ATOM 1366 CD PRO A 188 -18.217 -11.787 20.069 1.00 13.09 C ANISOU 1366 CD PRO A 188 1905 1569 1497 -587 -144 327 C ATOM 1367 N ILE A 189 -14.688 -11.921 18.756 1.00 11.20 N ANISOU 1367 N ILE A 189 1532 1581 1141 -373 230 102 N ATOM 1368 CA ILE A 189 -13.423 -11.689 18.034 1.00 10.92 C ANISOU 1368 CA ILE A 189 1372 1536 1238 -482 1 384 C ATOM 1369 C ILE A 189 -12.542 -10.669 18.754 1.00 9.46 C ANISOU 1369 C ILE A 189 1168 1303 1123 -45 193 130 C ATOM 1370 O ILE A 189 -11.338 -10.910 19.009 1.00 10.44 O ANISOU 1370 O ILE A 189 1194 1490 1280 -33 -9 271 O ATOM 1371 CB ILE A 189 -13.704 -11.218 16.584 1.00 9.87 C ANISOU 1371 CB ILE A 189 1303 1432 1011 -197 86 269 C ATOM 1372 CG1 ILE A 189 -14.248 -12.392 15.752 1.00 10.89 C ANISOU 1372 CG1 ILE A 189 1551 1565 1020 -125 -48 87 C ATOM 1373 CG2 ILE A 189 -12.433 -10.701 15.919 1.00 12.26 C ANISOU 1373 CG2 ILE A 189 1506 1833 1319 -442 282 367 C ATOM 1374 CD1 ILE A 189 -14.846 -11.976 14.414 1.00 12.93 C ANISOU 1374 CD1 ILE A 189 1544 2039 1330 -71 -95 345 C ATOM 1375 N TYR A 190 -13.127 -9.521 19.095 1.00 9.34 N ANISOU 1375 N TYR A 190 1288 1183 1075 -174 60 228 N ATOM 1376 CA TYR A 190 -12.385 -8.488 19.800 1.00 9.63 C ANISOU 1376 CA TYR A 190 1269 1255 1132 -65 -141 122 C ATOM 1377 C TYR A 190 -11.802 -9.054 21.091 1.00 10.31 C ANISOU 1377 C TYR A 190 1269 1430 1218 -198 -5 248 C ATOM 1378 O TYR A 190 -10.632 -8.835 21.408 1.00 10.42 O ANISOU 1378 O TYR A 190 1146 1499 1312 -79 -143 239 O ATOM 1379 CB TYR A 190 -13.297 -7.301 20.097 1.00 10.27 C ANISOU 1379 CB TYR A 190 1359 1250 1293 -112 20 79 C ATOM 1380 CG TYR A 190 -12.621 -6.254 20.955 1.00 9.62 C ANISOU 1380 CG TYR A 190 1211 1133 1311 -41 67 -12 C ATOM 1381 CD1 TYR A 190 -11.748 -5.330 20.388 1.00 10.48 C ANISOU 1381 CD1 TYR A 190 1038 1275 1666 142 -122 298 C ATOM 1382 CD2 TYR A 190 -12.824 -6.214 22.325 1.00 11.17 C ANISOU 1382 CD2 TYR A 190 1579 1228 1436 -105 -216 312 C ATOM 1383 CE1 TYR A 190 -11.094 -4.405 21.169 1.00 10.16 C ANISOU 1383 CE1 TYR A 190 1233 1300 1324 96 42 72 C ATOM 1384 CE2 TYR A 190 -12.149 -5.304 23.125 1.00 11.23 C ANISOU 1384 CE2 TYR A 190 1483 1216 1567 -94 69 -18 C ATOM 1385 CZ TYR A 190 -11.291 -4.393 22.533 1.00 10.36 C ANISOU 1385 CZ TYR A 190 1223 1417 1296 -105 -58 89 C ATOM 1386 OH TYR A 190 -10.624 -3.470 23.303 1.00 12.68 O ANISOU 1386 OH TYR A 190 1369 1533 1913 -23 -224 -185 O ATOM 1387 N ASP A 191 -12.619 -9.746 21.864 1.00 10.57 N ANISOU 1387 N ASP A 191 1466 1524 1026 -100 76 330 N ATOM 1388 CA ASP A 191 -12.182 -10.213 23.166 1.00 12.41 C ANISOU 1388 CA ASP A 191 1786 1787 1140 -3 -3 543 C ATOM 1389 C ASP A 191 -11.045 -11.221 23.081 1.00 13.36 C ANISOU 1389 C ASP A 191 1935 1728 1414 -31 -198 461 C ATOM 1390 O ASP A 191 -10.250 -11.343 24.018 1.00 16.01 O ANISOU 1390 O ASP A 191 2000 2721 1361 423 -295 300 O ATOM 1391 CB ASP A 191 -13.378 -10.831 23.885 1.00 14.93 C ANISOU 1391 CB ASP A 191 1859 2363 1450 -118 368 520 C ATOM 1392 CG ASP A 191 -14.271 -9.784 24.530 1.00 17.12 C ANISOU 1392 CG ASP A 191 2289 2414 1798 46 -377 508 C ATOM 1393 OD1 ASP A 191 -13.771 -8.666 24.803 1.00 20.41 O ANISOU 1393 OD1 ASP A 191 3132 2476 2146 242 721 -6 O ATOM 1394 OD2 ASP A 191 -15.401 -10.145 24.933 1.00 21.30 O ANISOU 1394 OD2 ASP A 191 2218 3486 2386 256 198 499 O ATOM 1395 N SER A 192 -10.971 -11.960 21.973 1.00 11.59 N ANISOU 1395 N SER A 192 1796 1255 1351 36 -7 509 N ATOM 1396 CA SER A 192 -9.965 -13.005 21.816 1.00 11.77 C ANISOU 1396 CA SER A 192 1848 1452 1171 -129 -81 521 C ATOM 1397 C SER A 192 -8.549 -12.459 21.690 1.00 11.51 C ANISOU 1397 C SER A 192 1597 1331 1444 -52 -142 531 C ATOM 1398 O SER A 192 -7.578 -13.201 21.885 1.00 13.09 O ANISOU 1398 O SER A 192 1647 1581 1746 -37 -293 576 O ATOM 1399 CB SER A 192 -10.285 -13.898 20.603 1.00 12.63 C ANISOU 1399 CB SER A 192 2081 1243 1473 -152 -157 480 C ATOM 1400 OG SER A 192 -10.014 -13.252 19.365 1.00 11.61 O ANISOU 1400 OG SER A 192 1770 1271 1370 -228 -184 348 O ATOM 1401 N MET A 193 -8.421 -11.217 21.242 1.00 10.76 N ANISOU 1401 N MET A 193 1644 1180 1262 -100 -171 303 N ATOM 1402 CA MET A 193 -7.100 -10.691 20.864 1.00 10.44 C ANISOU 1402 CA MET A 193 1493 1270 1202 -223 -274 200 C ATOM 1403 C MET A 193 -6.358 -10.149 22.067 1.00 10.43 C ANISOU 1403 C MET A 193 1283 1371 1308 -48 -169 41 C ATOM 1404 O MET A 193 -6.870 -9.286 22.758 1.00 12.63 O ANISOU 1404 O MET A 193 1450 1588 1759 240 -307 -10 O ATOM 1405 CB MET A 193 -7.269 -9.557 19.836 1.00 10.68 C ANISOU 1405 CB MET A 193 1519 1500 1035 -6 -445 367 C ATOM 1406 CG MET A 193 -7.740 -10.085 18.483 1.00 10.12 C ANISOU 1406 CG MET A 193 1501 1274 1069 -2 -129 157 C ATOM 1407 SD MET A 193 -7.798 -8.835 17.195 1.00 10.60 S ANISOU 1407 SD MET A 193 1278 1549 1199 -54 -95 198 S ATOM 1408 CE MET A 193 -9.082 -7.766 17.830 1.00 13.92 C ANISOU 1408 CE MET A 193 1533 2240 1516 568 331 349 C ATOM 1409 N SER A 194 -5.192 -10.720 22.365 1.00 11.16 N ANISOU 1409 N SER A 194 1353 1528 1357 -15 -422 111 N ATOM 1410 CA SER A 194 -4.530 -10.481 23.635 1.00 10.58 C ANISOU 1410 CA SER A 194 1676 1272 1069 -114 -437 484 C ATOM 1411 C SER A 194 -3.176 -9.812 23.522 1.00 10.64 C ANISOU 1411 C SER A 194 1567 1172 1304 294 -205 53 C ATOM 1412 O SER A 194 -2.636 -9.343 24.531 1.00 12.52 O ANISOU 1412 O SER A 194 1816 1680 1260 -27 -350 260 O ATOM 1413 CB SER A 194 -4.291 -11.824 24.306 1.00 12.49 C ANISOU 1413 CB SER A 194 1758 1248 1740 53 -70 498 C ATOM 1414 OG SER A 194 -3.470 -12.596 23.447 1.00 15.19 O ANISOU 1414 OG SER A 194 1764 1816 2190 292 -156 354 O ATOM 1415 N ARG A 195 -2.588 -9.820 22.330 1.00 10.37 N ANISOU 1415 N ARG A 195 1484 1281 1176 103 -184 259 N ATOM 1416 CA ARG A 195 -1.202 -9.407 22.150 1.00 12.97 C ANISOU 1416 CA ARG A 195 1671 1564 1692 419 157 402 C ATOM 1417 C ARG A 195 -1.054 -8.088 21.421 1.00 14.38 C ANISOU 1417 C ARG A 195 1665 1784 2014 365 73 736 C ATOM 1418 O ARG A 195 0.051 -7.655 21.153 1.00 22.32 O ANISOU 1418 O ARG A 195 1908 2402 4169 520 269 1605 O ATOM 1419 CB ARG A 195 -0.408 -10.480 21.394 1.00 14.81 C ANISOU 1419 CB ARG A 195 2418 1588 1619 677 372 503 C ATOM 1420 CG ARG A 195 -0.008 -11.627 22.315 1.00 16.80 C ANISOU 1420 CG ARG A 195 2674 1737 1973 667 416 890 C ATOM 1421 CD ARG A 195 0.913 -12.663 21.634 1.00 18.38 C ANISOU 1421 CD ARG A 195 1457 2064 3459 293 -28 344 C ATOM 1422 NE ARG A 195 0.111 -13.400 20.659 1.00 18.16 N ANISOU 1422 NE ARG A 195 3936 1591 1370 174 -705 253 N ATOM 1423 CZ ARG A 195 0.550 -14.194 19.684 1.00 14.94 C ANISOU 1423 CZ ARG A 195 2268 1609 1799 311 -227 624 C ATOM 1424 NH1 ARG A 195 1.841 -14.362 19.413 1.00 16.97 N ANISOU 1424 NH1 ARG A 195 2493 1957 1997 287 100 547 N ATOM 1425 NH2 ARG A 195 -0.341 -14.908 19.024 1.00 18.29 N ANISOU 1425 NH2 ARG A 195 2586 2058 2305 130 -329 320 N ATOM 1426 N ASN A 196 -2.150 -7.416 21.126 1.00 9.79 N ANISOU 1426 N ASN A 196 1398 1167 1153 340 -158 211 N ATOM 1427 CA ASN A 196 -2.102 -6.270 20.239 1.00 9.21 C ANISOU 1427 CA ASN A 196 1352 1250 895 136 -41 129 C ATOM 1428 C ASN A 196 -2.735 -5.014 20.828 1.00 9.51 C ANISOU 1428 C ASN A 196 1338 1201 1073 173 -105 221 C ATOM 1429 O ASN A 196 -3.577 -5.079 21.750 1.00 10.04 O ANISOU 1429 O ASN A 196 1403 1281 1131 92 -21 118 O ATOM 1430 CB ASN A 196 -2.753 -6.584 18.874 1.00 9.73 C ANISOU 1430 CB ASN A 196 1199 1522 974 112 -282 -8 C ATOM 1431 CG ASN A 196 -4.194 -7.055 18.975 1.00 9.65 C ANISOU 1431 CG ASN A 196 1264 1275 1126 27 -140 244 C ATOM 1432 OD1 ASN A 196 -4.707 -7.431 20.066 1.00 11.03 O ANISOU 1432 OD1 ASN A 196 1505 1599 1086 -50 -181 129 O ATOM 1433 ND2 ASN A 196 -4.882 -7.047 17.822 1.00 9.87 N ANISOU 1433 ND2 ASN A 196 1430 1278 1040 213 -74 114 N ATOM 1434 N ALA A 197 -2.372 -3.864 20.269 1.00 8.34 N ANISOU 1434 N ALA A 197 1018 1121 1029 78 -283 144 N ATOM 1435 CA ALA A 197 -3.244 -2.696 20.348 1.00 8.27 C ANISOU 1435 CA ALA A 197 938 1140 1064 56 -148 53 C ATOM 1436 C ALA A 197 -4.563 -3.035 19.658 1.00 7.39 C ANISOU 1436 C ALA A 197 895 1116 796 -4 -44 31 C ATOM 1437 O ALA A 197 -4.569 -3.585 18.555 1.00 8.08 O ANISOU 1437 O ALA A 197 1068 1197 806 99 -93 -46 O ATOM 1438 CB ALA A 197 -2.582 -1.546 19.644 1.00 9.71 C ANISOU 1438 CB ALA A 197 1421 1097 1169 -96 166 184 C ATOM 1439 N LYS A 198 -5.680 -2.740 20.297 1.00 7.82 N ANISOU 1439 N LYS A 198 890 1197 881 78 -51 63 N ATOM 1440 CA LYS A 198 -6.962 -3.097 19.707 1.00 7.67 C ANISOU 1440 CA LYS A 198 860 961 1091 70 -95 2 C ATOM 1441 C LYS A 198 -8.049 -2.122 20.146 1.00 7.65 C ANISOU 1441 C LYS A 198 969 1118 818 137 -54 -7 C ATOM 1442 O LYS A 198 -7.948 -1.458 21.187 1.00 8.60 O ANISOU 1442 O LYS A 198 1069 1276 923 75 -47 -98 O ATOM 1443 CB LYS A 198 -7.392 -4.531 20.075 1.00 8.71 C ANISOU 1443 CB LYS A 198 1404 995 909 152 -9 74 C ATOM 1444 CG LYS A 198 -7.582 -4.804 21.558 1.00 8.75 C ANISOU 1444 CG LYS A 198 1372 1106 846 -47 15 112 C ATOM 1445 CD LYS A 198 -8.131 -6.205 21.812 1.00 8.85 C ANISOU 1445 CD LYS A 198 1285 1096 981 63 116 174 C ATOM 1446 CE LYS A 198 -8.499 -6.392 23.287 1.00 10.24 C ANISOU 1446 CE LYS A 198 1718 1200 972 -90 25 72 C ATOM 1447 NZ LYS A 198 -9.078 -7.745 23.527 1.00 10.68 N ANISOU 1447 NZ LYS A 198 1473 1201 1382 -282 -26 119 N ATOM 1448 N GLN A 199 -9.122 -2.072 19.370 1.00 7.81 N ANISOU 1448 N GLN A 199 910 1048 1009 127 -45 -6 N ATOM 1449 CA GLN A 199 -10.217 -1.181 19.683 1.00 7.55 C ANISOU 1449 CA GLN A 199 852 992 1023 85 -36 114 C ATOM 1450 C GLN A 199 -11.490 -1.776 19.112 1.00 7.73 C ANISOU 1450 C GLN A 199 1096 915 925 61 -55 -85 C ATOM 1451 O GLN A 199 -11.473 -2.457 18.095 1.00 8.39 O ANISOU 1451 O GLN A 199 1204 1081 901 127 -65 -53 O ATOM 1452 CB GLN A 199 -9.932 0.223 19.108 1.00 8.14 C ANISOU 1452 CB GLN A 199 1093 1043 956 118 68 91 C ATOM 1453 CG GLN A 199 -10.931 1.292 19.532 1.00 8.69 C ANISOU 1453 CG GLN A 199 1098 1063 1137 16 104 -96 C ATOM 1454 CD GLN A 199 -10.326 2.672 19.418 1.00 7.78 C ANISOU 1454 CD GLN A 199 1143 911 901 68 108 -3 C ATOM 1455 OE1 GLN A 199 -9.345 3.022 20.158 1.00 10.91 O ANISOU 1455 OE1 GLN A 199 1298 1503 1344 -107 -205 -90 O ATOM 1456 NE2 GLN A 199 -10.877 3.475 18.551 1.00 6.45 N ANISOU 1456 NE2 GLN A 199 952 788 708 -34 10 -108 N ATOM 1457 N PHE A 200 -12.602 -1.444 19.759 1.00 8.32 N ANISOU 1457 N PHE A 200 907 1204 1050 29 34 -8 N ATOM 1458 CA PHE A 200 -13.939 -1.926 19.399 1.00 8.34 C ANISOU 1458 CA PHE A 200 956 1090 1122 -23 -40 129 C ATOM 1459 C PHE A 200 -14.854 -0.710 19.373 1.00 7.64 C ANISOU 1459 C PHE A 200 1106 992 804 55 55 -99 C ATOM 1460 O PHE A 200 -14.936 0.029 20.356 1.00 9.15 O ANISOU 1460 O PHE A 200 1130 1378 968 -35 -26 -242 O ATOM 1461 CB PHE A 200 -14.445 -2.905 20.476 1.00 9.83 C ANISOU 1461 CB PHE A 200 1102 1419 1211 -272 -105 374 C ATOM 1462 CG PHE A 200 -15.780 -3.537 20.163 1.00 9.31 C ANISOU 1462 CG PHE A 200 1256 1193 1084 -7 -5 93 C ATOM 1463 CD1 PHE A 200 -15.868 -4.595 19.263 1.00 11.48 C ANISOU 1463 CD1 PHE A 200 1739 1323 1297 -200 -292 195 C ATOM 1464 CD2 PHE A 200 -16.947 -3.101 20.794 1.00 11.42 C ANISOU 1464 CD2 PHE A 200 1033 1595 1710 -52 12 129 C ATOM 1465 CE1 PHE A 200 -17.101 -5.194 18.989 1.00 12.58 C ANISOU 1465 CE1 PHE A 200 1663 1578 1538 -252 -353 156 C ATOM 1466 CE2 PHE A 200 -18.177 -3.718 20.544 1.00 12.83 C ANISOU 1466 CE2 PHE A 200 1341 1697 1837 -302 -184 65 C ATOM 1467 CZ PHE A 200 -18.241 -4.744 19.620 1.00 13.07 C ANISOU 1467 CZ PHE A 200 1400 1639 1927 -210 -239 226 C ATOM 1468 N LEU A 201 -15.464 -0.427 18.228 1.00 7.88 N ANISOU 1468 N LEU A 201 889 1139 963 107 -44 65 N ATOM 1469 CA LEU A 201 -16.319 0.747 18.075 1.00 9.12 C ANISOU 1469 CA LEU A 201 1055 1079 1328 49 -152 16 C ATOM 1470 C LEU A 201 -17.612 0.298 17.455 1.00 8.35 C ANISOU 1470 C LEU A 201 1086 1115 969 -55 -68 -226 C ATOM 1471 O LEU A 201 -17.678 0.007 16.262 1.00 9.02 O ANISOU 1471 O LEU A 201 1180 1201 1043 124 -33 -197 O ATOM 1472 CB LEU A 201 -15.614 1.785 17.175 1.00 10.35 C ANISOU 1472 CB LEU A 201 1334 948 1649 78 -34 -100 C ATOM 1473 CG LEU A 201 -16.304 3.143 17.104 1.00 13.30 C ANISOU 1473 CG LEU A 201 1772 1142 2138 355 83 78 C ATOM 1474 CD1 LEU A 201 -17.691 3.238 16.495 1.00 21.88 C ANISOU 1474 CD1 LEU A 201 2909 2389 3014 420 -460 -485 C ATOM 1475 CD2 LEU A 201 -16.066 4.019 18.300 1.00 22.66 C ANISOU 1475 CD2 LEU A 201 3296 2126 3184 385 130 242 C ATOM 1476 N GLU A 202 -18.645 0.238 18.288 1.00 9.53 N ANISOU 1476 N GLU A 202 1056 1323 1243 122 118 -114 N ATOM 1477 CA GLU A 202 -19.960 -0.220 17.833 1.00 9.46 C ANISOU 1477 CA GLU A 202 999 1243 1352 22 77 10 C ATOM 1478 C GLU A 202 -20.896 0.956 17.573 1.00 9.13 C ANISOU 1478 C GLU A 202 1113 1308 1045 133 262 -75 C ATOM 1479 O GLU A 202 -21.084 1.810 18.445 1.00 10.00 O ANISOU 1479 O GLU A 202 1152 1488 1160 36 215 -330 O ATOM 1480 CB GLU A 202 -20.580 -1.131 18.872 1.00 10.26 C ANISOU 1480 CB GLU A 202 1259 1426 1211 0 46 95 C ATOM 1481 CG GLU A 202 -21.910 -1.737 18.474 1.00 11.52 C ANISOU 1481 CG GLU A 202 1247 1676 1451 -234 41 47 C ATOM 1482 CD GLU A 202 -22.570 -2.451 19.642 1.00 12.45 C ANISOU 1482 CD GLU A 202 1757 1444 1529 -56 152 44 C ATOM 1483 OE1 GLU A 202 -22.348 -3.658 19.788 1.00 17.80 O ANISOU 1483 OE1 GLU A 202 2757 1661 2345 -102 573 55 O ATOM 1484 OE2 GLU A 202 -23.184 -1.781 20.500 1.00 14.22 O ANISOU 1484 OE2 GLU A 202 1748 1927 1728 -40 396 14 O ATOM 1485 N ILE A 203 -21.425 1.038 16.355 1.00 9.59 N ANISOU 1485 N ILE A 203 1042 1440 1162 124 24 112 N ATOM 1486 CA ILE A 203 -22.279 2.133 15.941 1.00 9.51 C ANISOU 1486 CA ILE A 203 1154 1328 1131 73 43 19 C ATOM 1487 C ILE A 203 -23.706 1.909 16.433 1.00 8.77 C ANISOU 1487 C ILE A 203 1024 999 1308 147 -44 -52 C ATOM 1488 O ILE A 203 -24.320 0.860 16.181 1.00 10.15 O ANISOU 1488 O ILE A 203 1136 1378 1341 103 100 -82 O ATOM 1489 CB ILE A 203 -22.268 2.261 14.405 1.00 11.01 C ANISOU 1489 CB ILE A 203 1363 1709 1110 121 134 25 C ATOM 1490 CG1 ILE A 203 -20.842 2.626 13.938 1.00 12.59 C ANISOU 1490 CG1 ILE A 203 1740 1567 1473 -261 393 -188 C ATOM 1491 CG2 ILE A 203 -23.297 3.311 13.949 1.00 13.33 C ANISOU 1491 CG2 ILE A 203 1927 1642 1494 236 -335 122 C ATOM 1492 CD1 ILE A 203 -20.402 4.042 14.334 1.00 16.08 C ANISOU 1492 CD1 ILE A 203 2308 2000 1799 -730 403 -217 C ATOM 1493 N ASN A 204 -24.200 2.892 17.177 1.00 10.58 N ANISOU 1493 N ASN A 204 1254 1589 1176 437 196 -178 N ATOM 1494 CA ASN A 204 -25.552 2.860 17.802 1.00 11.36 C ANISOU 1494 CA ASN A 204 1088 1725 1500 107 190 -536 C ATOM 1495 C ASN A 204 -26.634 2.708 16.723 1.00 11.10 C ANISOU 1495 C ASN A 204 1185 1481 1548 159 270 -115 C ATOM 1496 O ASN A 204 -26.668 3.461 15.747 1.00 13.34 O ANISOU 1496 O ASN A 204 1540 1706 1820 399 -6 -17 O ATOM 1497 CB ASN A 204 -25.710 4.204 18.534 1.00 13.08 C ANISOU 1497 CB ASN A 204 1458 1772 1737 128 557 -583 C ATOM 1498 CG ASN A 204 -26.911 4.276 19.448 1.00 17.41 C ANISOU 1498 CG ASN A 204 1962 2355 2296 -17 955 -508 C ATOM 1499 OD1 ASN A 204 -27.589 3.297 19.670 1.00 21.26 O ANISOU 1499 OD1 ASN A 204 2476 2888 2715 -78 1313 -665 O ATOM 1500 ND2 ASN A 204 -26.979 5.377 20.188 1.00 24.90 N ANISOU 1500 ND2 ASN A 204 3782 2537 3140 585 1480 -747 N ATOM 1501 N GLY A 205 -27.434 1.651 16.855 1.00 11.57 N ANISOU 1501 N GLY A 205 1144 1672 1578 -21 201 -268 N ATOM 1502 CA GLY A 205 -28.534 1.327 15.958 1.00 13.79 C ANISOU 1502 CA GLY A 205 1254 2257 1728 25 143 -727 C ATOM 1503 C GLY A 205 -28.118 0.833 14.585 1.00 12.64 C ANISOU 1503 C GLY A 205 1245 2073 1484 276 140 -326 C ATOM 1504 O GLY A 205 -28.952 0.713 13.688 1.00 16.04 O ANISOU 1504 O GLY A 205 1526 2759 1808 253 -17 -676 O ATOM 1505 N GLY A 206 -26.842 0.517 14.397 1.00 11.69 N ANISOU 1505 N GLY A 206 1302 1698 1442 240 320 -156 N ATOM 1506 CA GLY A 206 -26.376 0.213 13.045 1.00 11.46 C ANISOU 1506 CA GLY A 206 1414 1554 1386 99 179 -514 C ATOM 1507 C GLY A 206 -26.892 -1.137 12.561 1.00 10.84 C ANISOU 1507 C GLY A 206 1072 1610 1435 70 257 -146 C ATOM 1508 O GLY A 206 -26.858 -2.112 13.299 1.00 12.40 O ANISOU 1508 O GLY A 206 1529 1605 1575 125 1 -138 O ATOM 1509 N SER A 207 -27.240 -1.217 11.275 1.00 11.48 N ANISOU 1509 N SER A 207 1124 1888 1348 144 38 -387 N ATOM 1510 CA SER A 207 -27.476 -2.510 10.623 1.00 10.76 C ANISOU 1510 CA SER A 207 1040 1725 1323 371 -70 -414 C ATOM 1511 C SER A 207 -26.147 -3.085 10.153 1.00 9.92 C ANISOU 1511 C SER A 207 1117 1416 1235 145 160 -156 C ATOM 1512 O SER A 207 -25.112 -2.432 10.284 1.00 10.39 O ANISOU 1512 O SER A 207 1073 1609 1265 -46 -9 -51 O ATOM 1513 CB SER A 207 -28.397 -2.316 9.415 1.00 13.55 C ANISOU 1513 CB SER A 207 1647 2346 1154 252 -195 -85 C ATOM 1514 OG SER A 207 -27.647 -1.844 8.291 1.00 16.74 O ANISOU 1514 OG SER A 207 1946 2714 1700 194 -170 -8 O ATOM 1515 N HIS A 208 -26.185 -4.261 9.548 1.00 10.42 N ANISOU 1515 N HIS A 208 1103 1599 1255 261 141 -312 N ATOM 1516 CA HIS A 208 -24.953 -4.908 9.085 1.00 10.90 C ANISOU 1516 CA HIS A 208 1075 1470 1594 40 371 -171 C ATOM 1517 C HIS A 208 -24.123 -4.024 8.135 1.00 9.75 C ANISOU 1517 C HIS A 208 987 1319 1396 146 -63 5 C ATOM 1518 O HIS A 208 -22.902 -4.205 8.053 1.00 9.90 O ANISOU 1518 O HIS A 208 873 1289 1599 -3 92 -40 O ATOM 1519 CB HIS A 208 -25.350 -6.210 8.399 1.00 10.15 C ANISOU 1519 CB HIS A 208 958 1169 1729 110 124 -117 C ATOM 1520 CG HIS A 208 -24.200 -7.070 7.966 1.00 9.86 C ANISOU 1520 CG HIS A 208 903 1402 1438 15 126 -82 C ATOM 1521 ND1 HIS A 208 -23.194 -7.493 8.814 1.00 10.15 N ANISOU 1521 ND1 HIS A 208 947 1380 1528 -39 136 -148 N ATOM 1522 CD2 HIS A 208 -23.989 -7.691 6.790 1.00 11.03 C ANISOU 1522 CD2 HIS A 208 856 1802 1531 -206 311 -241 C ATOM 1523 CE1 HIS A 208 -22.406 -8.338 8.162 1.00 11.43 C ANISOU 1523 CE1 HIS A 208 1262 1580 1500 -34 87 -338 C ATOM 1524 NE2 HIS A 208 -22.840 -8.434 6.911 1.00 11.44 N ANISOU 1524 NE2 HIS A 208 954 1870 1524 -37 200 -52 N ATOM 1525 N SER A 209 -24.755 -3.077 7.427 1.00 9.71 N ANISOU 1525 N SER A 209 1047 1336 1305 -103 56 42 N ATOM 1526 CA SER A 209 -24.088 -2.207 6.471 1.00 9.51 C ANISOU 1526 CA SER A 209 1109 1318 1186 -66 -109 123 C ATOM 1527 C SER A 209 -23.675 -0.839 7.062 1.00 9.41 C ANISOU 1527 C SER A 209 781 1498 1295 210 -8 0 C ATOM 1528 O SER A 209 -23.367 0.100 6.323 1.00 10.37 O ANISOU 1528 O SER A 209 1233 1362 1344 108 -16 -45 O ATOM 1529 CB SER A 209 -24.962 -2.046 5.231 1.00 13.47 C ANISOU 1529 CB SER A 209 1236 2349 1534 460 23 566 C ATOM 1530 OG SER A 209 -26.191 -1.472 5.607 1.00 17.42 O ANISOU 1530 OG SER A 209 1723 2632 2264 273 -176 18 O ATOM 1531 N CYS A 210 -23.568 -0.745 8.391 1.00 9.48 N ANISOU 1531 N CYS A 210 992 1350 1259 28 22 -218 N ATOM 1532 CA CYS A 210 -23.397 0.577 9.033 1.00 10.44 C ANISOU 1532 CA CYS A 210 1180 1351 1434 20 311 -171 C ATOM 1533 C CYS A 210 -22.084 1.303 8.751 1.00 9.18 C ANISOU 1533 C CYS A 210 1133 1237 1117 217 235 21 C ATOM 1534 O CYS A 210 -21.983 2.499 9.035 1.00 10.51 O ANISOU 1534 O CYS A 210 1275 1198 1517 204 211 47 O ATOM 1535 CB CYS A 210 -23.655 0.493 10.555 1.00 10.97 C ANISOU 1535 CB CYS A 210 1256 1563 1348 86 308 10 C ATOM 1536 SG CYS A 210 -22.252 -0.078 11.586 1.00 11.01 S ANISOU 1536 SG CYS A 210 1400 1513 1269 -67 107 -113 S ATOM 1537 N ALA A 211 -21.071 0.588 8.251 1.00 7.93 N ANISOU 1537 N ALA A 211 940 1120 951 107 122 9 N ATOM 1538 CA ALA A 211 -19.795 1.225 7.918 1.00 7.66 C ANISOU 1538 CA ALA A 211 923 1078 907 149 112 -62 C ATOM 1539 C ALA A 211 -19.561 1.176 6.402 1.00 8.10 C ANISOU 1539 C ALA A 211 1128 992 956 204 54 -67 C ATOM 1540 O ALA A 211 -18.451 1.441 5.939 1.00 8.89 O ANISOU 1540 O ALA A 211 1007 1171 1197 97 50 5 O ATOM 1541 CB ALA A 211 -18.643 0.549 8.667 1.00 9.73 C ANISOU 1541 CB ALA A 211 912 1377 1409 179 -186 114 C ATOM 1542 N ASN A 212 -20.615 0.913 5.623 1.00 8.08 N ANISOU 1542 N ASN A 212 1069 1039 960 213 -125 56 N ATOM 1543 CA ASN A 212 -20.474 0.821 4.162 1.00 7.75 C ANISOU 1543 CA ASN A 212 985 877 1083 105 -128 -19 C ATOM 1544 C ASN A 212 -20.599 2.159 3.457 1.00 8.32 C ANISOU 1544 C ASN A 212 943 1009 1209 152 -20 24 C ATOM 1545 O ASN A 212 -20.982 3.178 4.058 1.00 9.73 O ANISOU 1545 O ASN A 212 1209 1187 1298 452 -47 -213 O ATOM 1546 CB ASN A 212 -21.506 -0.165 3.593 1.00 8.85 C ANISOU 1546 CB ASN A 212 1291 913 1159 -29 -87 -211 C ATOM 1547 CG ASN A 212 -21.255 -1.598 4.021 1.00 8.34 C ANISOU 1547 CG ASN A 212 974 1094 1099 19 -17 -32 C ATOM 1548 OD1 ASN A 212 -20.388 -1.900 4.881 1.00 9.46 O ANISOU 1548 OD1 ASN A 212 1074 1134 1386 194 -15 -130 O ATOM 1549 ND2 ASN A 212 -22.039 -2.494 3.449 1.00 10.22 N ANISOU 1549 ND2 ASN A 212 1168 1400 1313 -242 -27 -261 N ATOM 1550 N SER A 213 -20.366 2.146 2.152 1.00 8.58 N ANISOU 1550 N SER A 213 915 1113 1232 68 63 153 N ATOM 1551 CA SER A 213 -20.596 3.365 1.392 1.00 8.36 C ANISOU 1551 CA SER A 213 1267 810 1098 360 5 -85 C ATOM 1552 C SER A 213 -22.023 3.842 1.602 1.00 9.92 C ANISOU 1552 C SER A 213 1203 1124 1441 134 70 -123 C ATOM 1553 O SER A 213 -22.951 3.028 1.677 1.00 10.31 O ANISOU 1553 O SER A 213 1132 1341 1443 266 -126 36 O ATOM 1554 CB SER A 213 -20.343 3.114 -0.084 1.00 9.49 C ANISOU 1554 CB SER A 213 1132 1479 991 290 47 22 C ATOM 1555 OG SER A 213 -19.023 2.590 -0.258 1.00 8.93 O ANISOU 1555 OG SER A 213 919 1253 1221 -46 -11 -11 O ATOM 1556 N GLY A 214 -22.200 5.152 1.759 1.00 10.67 N ANISOU 1556 N GLY A 214 1455 1318 1280 648 -77 -75 N ATOM 1557 CA GLY A 214 -23.527 5.670 1.976 1.00 10.90 C ANISOU 1557 CA GLY A 214 1269 1546 1324 491 30 3 C ATOM 1558 C GLY A 214 -23.962 5.678 3.436 1.00 8.89 C ANISOU 1558 C GLY A 214 1126 1206 1044 414 -69 -53 C ATOM 1559 O GLY A 214 -25.089 6.051 3.727 1.00 10.15 O ANISOU 1559 O GLY A 214 1077 1164 1613 287 -81 -65 O ATOM 1560 N ASN A 215 -23.101 5.285 4.376 1.00 9.72 N ANISOU 1560 N ASN A 215 1232 1312 1147 347 -59 61 N ATOM 1561 CA ASN A 215 -23.513 5.324 5.768 1.00 8.45 C ANISOU 1561 CA ASN A 215 1055 1015 1139 120 -82 -36 C ATOM 1562 C ASN A 215 -23.605 6.766 6.281 1.00 9.06 C ANISOU 1562 C ASN A 215 791 1214 1435 156 -127 77 C ATOM 1563 O ASN A 215 -22.989 7.689 5.723 1.00 9.74 O ANISOU 1563 O ASN A 215 1097 1226 1378 113 -20 -4 O ATOM 1564 CB ASN A 215 -22.603 4.445 6.644 1.00 10.38 C ANISOU 1564 CB ASN A 215 1267 1175 1500 274 -204 205 C ATOM 1565 CG ASN A 215 -21.260 5.090 6.973 1.00 9.22 C ANISOU 1565 CG ASN A 215 1154 1184 1163 328 -80 -179 C ATOM 1566 OD1 ASN A 215 -21.177 5.983 7.820 1.00 9.76 O ANISOU 1566 OD1 ASN A 215 1158 1361 1187 374 -114 -208 O ATOM 1567 ND2 ASN A 215 -20.187 4.606 6.332 1.00 10.01 N ANISOU 1567 ND2 ASN A 215 997 1482 1321 427 34 68 N ATOM 1568 N SER A 216 -24.380 6.959 7.345 1.00 9.35 N ANISOU 1568 N SER A 216 1068 1201 1283 286 -22 -54 N ATOM 1569 CA SER A 216 -24.610 8.298 7.882 1.00 10.94 C ANISOU 1569 CA SER A 216 1098 1413 1644 326 9 -213 C ATOM 1570 C SER A 216 -23.696 8.640 9.043 1.00 11.78 C ANISOU 1570 C SER A 216 1401 1442 1632 300 -32 -350 C ATOM 1571 O SER A 216 -23.945 9.623 9.724 1.00 14.58 O ANISOU 1571 O SER A 216 1792 1715 2030 560 -486 -654 O ATOM 1572 CB SER A 216 -26.061 8.439 8.320 1.00 12.54 C ANISOU 1572 CB SER A 216 1221 1876 1666 333 -93 -254 C ATOM 1573 OG SER A 216 -26.873 8.645 7.165 1.00 18.14 O ANISOU 1573 OG SER A 216 1882 2343 2666 671 -485 -196 O ATOM 1574 N ASN A 217 -22.602 7.899 9.199 1.00 9.67 N ANISOU 1574 N ASN A 217 1131 1215 1328 2 -170 -45 N ATOM 1575 CA ASN A 217 -21.614 8.197 10.227 1.00 9.88 C ANISOU 1575 CA ASN A 217 1313 1343 1095 -142 -38 54 C ATOM 1576 C ASN A 217 -20.220 8.327 9.657 1.00 9.22 C ANISOU 1576 C ASN A 217 944 1417 1140 238 -18 110 C ATOM 1577 O ASN A 217 -19.245 7.906 10.268 1.00 9.99 O ANISOU 1577 O ASN A 217 1149 1232 1412 142 -325 136 O ATOM 1578 CB ASN A 217 -21.616 7.150 11.330 1.00 11.51 C ANISOU 1578 CB ASN A 217 1316 1694 1361 -29 123 436 C ATOM 1579 CG ASN A 217 -22.763 7.353 12.268 1.00 12.85 C ANISOU 1579 CG ASN A 217 1927 1577 1377 180 374 -30 C ATOM 1580 OD1 ASN A 217 -22.872 8.404 12.913 1.00 19.68 O ANISOU 1580 OD1 ASN A 217 3745 2071 1660 105 372 -470 O ATOM 1581 ND2 ASN A 217 -23.685 6.400 12.277 1.00 14.35 N ANISOU 1581 ND2 ASN A 217 1612 1456 2384 146 559 -182 N ATOM 1582 N GLN A 218 -20.102 8.910 8.468 1.00 9.38 N ANISOU 1582 N GLN A 218 1073 1253 1239 46 55 113 N ATOM 1583 CA GLN A 218 -18.799 8.958 7.830 1.00 9.60 C ANISOU 1583 CA GLN A 218 1143 1269 1234 -15 148 -33 C ATOM 1584 C GLN A 218 -17.810 9.857 8.552 1.00 8.97 C ANISOU 1584 C GLN A 218 1000 1122 1285 62 42 75 C ATOM 1585 O GLN A 218 -16.601 9.611 8.477 1.00 10.02 O ANISOU 1585 O GLN A 218 1099 1243 1462 264 -49 187 O ATOM 1586 CB GLN A 218 -18.934 9.338 6.363 1.00 10.07 C ANISOU 1586 CB GLN A 218 1227 1307 1292 112 -48 232 C ATOM 1587 CG GLN A 218 -19.595 8.241 5.557 1.00 12.01 C ANISOU 1587 CG GLN A 218 1588 1609 1364 -84 -151 -63 C ATOM 1588 CD GLN A 218 -19.906 8.688 4.141 1.00 13.72 C ANISOU 1588 CD GLN A 218 1851 1847 1512 125 16 211 C ATOM 1589 OE1 GLN A 218 -19.053 9.251 3.441 1.00 17.18 O ANISOU 1589 OE1 GLN A 218 2159 2425 1941 -96 -72 529 O ATOM 1590 NE2 GLN A 218 -21.096 8.328 3.661 1.00 15.92 N ANISOU 1590 NE2 GLN A 218 1650 2848 1550 -82 -191 162 N ATOM 1591 N ALA A 219 -18.295 10.862 9.278 1.00 9.57 N ANISOU 1591 N ALA A 219 1174 1210 1249 230 -249 -43 N ATOM 1592 CA ALA A 219 -17.387 11.745 9.996 1.00 9.63 C ANISOU 1592 CA ALA A 219 1079 1040 1538 192 -135 -29 C ATOM 1593 C ALA A 219 -16.640 10.932 11.070 1.00 9.81 C ANISOU 1593 C ALA A 219 1375 1081 1269 143 -15 37 C ATOM 1594 O ALA A 219 -15.406 10.966 11.150 1.00 10.64 O ANISOU 1594 O ALA A 219 1291 1285 1465 100 -31 -26 O ATOM 1595 CB ALA A 219 -18.146 12.907 10.638 1.00 12.15 C ANISOU 1595 CB ALA A 219 1561 1373 1680 493 33 -169 C ATOM 1596 N LEU A 220 -17.385 10.222 11.910 1.00 9.16 N ANISOU 1596 N LEU A 220 1303 1063 1111 201 -86 -16 N ATOM 1597 CA LEU A 220 -16.789 9.453 13.003 1.00 8.79 C ANISOU 1597 CA LEU A 220 1180 1313 844 264 38 -131 C ATOM 1598 C LEU A 220 -16.046 8.225 12.469 1.00 7.67 C ANISOU 1598 C LEU A 220 970 1070 873 92 -14 -73 C ATOM 1599 O LEU A 220 -14.908 7.935 12.891 1.00 8.72 O ANISOU 1599 O LEU A 220 1061 1161 1090 234 -115 -81 O ATOM 1600 CB LEU A 220 -17.904 9.019 13.966 1.00 10.45 C ANISOU 1600 CB LEU A 220 1432 1408 1130 145 201 181 C ATOM 1601 CG LEU A 220 -17.422 8.023 15.025 1.00 14.48 C ANISOU 1601 CG LEU A 220 1966 2041 1493 148 297 386 C ATOM 1602 CD1 LEU A 220 -16.281 8.611 15.864 1.00 15.68 C ANISOU 1602 CD1 LEU A 220 2545 2326 1083 358 -170 50 C ATOM 1603 CD2 LEU A 220 -18.593 7.555 15.885 1.00 19.43 C ANISOU 1603 CD2 LEU A 220 2069 2405 2908 374 1166 432 C ATOM 1604 N ILE A 221 -16.701 7.445 11.614 1.00 7.77 N ANISOU 1604 N ILE A 221 1116 937 898 105 108 -112 N ATOM 1605 CA ILE A 221 -16.091 6.202 11.160 1.00 8.28 C ANISOU 1605 CA ILE A 221 1003 1072 1071 35 29 -188 C ATOM 1606 C ILE A 221 -14.846 6.521 10.348 1.00 7.80 C ANISOU 1606 C ILE A 221 1138 922 901 103 -42 -14 C ATOM 1607 O ILE A 221 -13.810 5.877 10.519 1.00 8.11 O ANISOU 1607 O ILE A 221 1050 963 1069 108 -137 -51 O ATOM 1608 CB ILE A 221 -17.112 5.368 10.352 1.00 8.08 C ANISOU 1608 CB ILE A 221 1033 959 1077 -60 45 -118 C ATOM 1609 CG1 ILE A 221 -18.231 4.846 11.273 1.00 9.43 C ANISOU 1609 CG1 ILE A 221 1042 1377 1164 -250 77 9 C ATOM 1610 CG2 ILE A 221 -16.397 4.176 9.687 1.00 9.23 C ANISOU 1610 CG2 ILE A 221 1177 1187 1140 171 -166 -292 C ATOM 1611 CD1 ILE A 221 -19.391 4.205 10.527 1.00 10.17 C ANISOU 1611 CD1 ILE A 221 1230 1419 1214 -101 -195 -94 C ATOM 1612 N GLY A 222 -14.930 7.529 9.471 1.00 7.94 N ANISOU 1612 N GLY A 222 1258 970 785 -148 37 57 N ATOM 1613 CA GLY A 222 -13.755 7.913 8.675 1.00 8.26 C ANISOU 1613 CA GLY A 222 935 1035 1168 -127 -10 -99 C ATOM 1614 C GLY A 222 -12.649 8.480 9.545 1.00 7.77 C ANISOU 1614 C GLY A 222 1009 916 1025 -4 10 15 C ATOM 1615 O GLY A 222 -11.474 8.204 9.302 1.00 8.09 O ANISOU 1615 O GLY A 222 888 957 1228 91 -41 28 O ATOM 1616 N LYS A 223 -12.985 9.294 10.554 1.00 7.51 N ANISOU 1616 N LYS A 223 1034 930 889 -33 -85 19 N ATOM 1617 CA LYS A 223 -11.947 9.816 11.459 1.00 8.55 C ANISOU 1617 CA LYS A 223 1235 895 1115 211 -252 -131 C ATOM 1618 C LYS A 223 -11.246 8.649 12.133 1.00 7.46 C ANISOU 1618 C LYS A 223 861 933 1040 82 -44 -53 C ATOM 1619 O LYS A 223 -10.016 8.639 12.205 1.00 8.28 O ANISOU 1619 O LYS A 223 1004 1056 1084 110 -29 -43 O ATOM 1620 CB LYS A 223 -12.601 10.681 12.549 1.00 9.87 C ANISOU 1620 CB LYS A 223 1309 1238 1201 334 -227 -338 C ATOM 1621 CG LYS A 223 -11.663 10.970 13.714 1.00 10.06 C ANISOU 1621 CG LYS A 223 1448 1243 1128 175 -207 -438 C ATOM 1622 CD LYS A 223 -12.175 12.109 14.603 1.00 12.14 C ANISOU 1622 CD LYS A 223 1526 1429 1656 377 6 -404 C ATOM 1623 CE LYS A 223 -13.474 11.747 15.283 1.00 13.56 C ANISOU 1623 CE LYS A 223 1811 1532 1806 175 332 -650 C ATOM 1624 NZ LYS A 223 -13.925 12.815 16.217 1.00 15.40 N ANISOU 1624 NZ LYS A 223 1991 1936 1923 467 37 -960 N ATOM 1625 N LYS A 224 -12.000 7.653 12.636 1.00 7.93 N ANISOU 1625 N LYS A 224 1225 935 852 124 -167 67 N ATOM 1626 CA LYS A 224 -11.367 6.579 13.378 1.00 7.70 C ANISOU 1626 CA LYS A 224 1158 818 948 61 5 57 C ATOM 1627 C LYS A 224 -10.537 5.698 12.445 1.00 7.67 C ANISOU 1627 C LYS A 224 932 916 1064 -36 -78 -70 C ATOM 1628 O LYS A 224 -9.442 5.264 12.813 1.00 8.01 O ANISOU 1628 O LYS A 224 972 1054 1018 64 -81 1 O ATOM 1629 CB LYS A 224 -12.431 5.764 14.116 1.00 8.16 C ANISOU 1629 CB LYS A 224 1057 1174 869 58 197 -17 C ATOM 1630 CG LYS A 224 -12.718 6.362 15.482 1.00 7.91 C ANISOU 1630 CG LYS A 224 931 1176 896 228 -89 -151 C ATOM 1631 CD LYS A 224 -11.584 6.069 16.456 1.00 8.88 C ANISOU 1631 CD LYS A 224 1102 1300 971 251 -81 -61 C ATOM 1632 CE LYS A 224 -11.869 6.519 17.889 1.00 7.87 C ANISOU 1632 CE LYS A 224 1103 999 886 135 -102 -80 C ATOM 1633 NZ LYS A 224 -10.662 6.212 18.715 1.00 8.63 N ANISOU 1633 NZ LYS A 224 1144 1137 997 146 -179 -62 N ATOM 1634 N GLY A 225 -11.061 5.374 11.263 1.00 7.41 N ANISOU 1634 N GLY A 225 1008 926 882 45 76 -101 N ATOM 1635 CA GLY A 225 -10.291 4.526 10.353 1.00 7.71 C ANISOU 1635 CA GLY A 225 884 967 1078 -24 10 -58 C ATOM 1636 C GLY A 225 -8.996 5.205 9.942 1.00 6.60 C ANISOU 1636 C GLY A 225 904 897 707 -28 -145 -70 C ATOM 1637 O GLY A 225 -7.924 4.578 9.919 1.00 8.24 O ANISOU 1637 O GLY A 225 981 1074 1076 52 -128 -121 O ATOM 1638 N VAL A 226 -9.081 6.466 9.528 1.00 7.14 N ANISOU 1638 N VAL A 226 979 938 795 -148 -159 60 N ATOM 1639 CA VAL A 226 -7.877 7.206 9.152 1.00 7.46 C ANISOU 1639 CA VAL A 226 1045 848 939 -117 -143 69 C ATOM 1640 C VAL A 226 -6.906 7.321 10.322 1.00 7.47 C ANISOU 1640 C VAL A 226 999 987 849 176 -58 -97 C ATOM 1641 O VAL A 226 -5.710 7.084 10.159 1.00 8.01 O ANISOU 1641 O VAL A 226 993 1004 1045 91 38 44 O ATOM 1642 CB VAL A 226 -8.228 8.601 8.580 1.00 8.65 C ANISOU 1642 CB VAL A 226 1332 986 966 9 -115 174 C ATOM 1643 CG1 VAL A 226 -6.961 9.435 8.408 1.00 9.44 C ANISOU 1643 CG1 VAL A 226 1233 1138 1213 -69 -32 188 C ATOM 1644 CG2 VAL A 226 -8.983 8.451 7.264 1.00 10.25 C ANISOU 1644 CG2 VAL A 226 1363 1339 1191 151 -362 76 C ATOM 1645 N ALA A 227 -7.421 7.652 11.514 1.00 7.14 N ANISOU 1645 N ALA A 227 1071 791 850 -95 -69 -91 N ATOM 1646 CA ALA A 227 -6.536 7.833 12.656 1.00 7.64 C ANISOU 1646 CA ALA A 227 1205 885 812 193 -183 -190 C ATOM 1647 C ALA A 227 -5.810 6.538 12.987 1.00 6.97 C ANISOU 1647 C ALA A 227 889 955 801 -94 -16 -82 C ATOM 1648 O ALA A 227 -4.628 6.550 13.341 1.00 7.52 O ANISOU 1648 O ALA A 227 924 931 1001 81 -57 -53 O ATOM 1649 CB ALA A 227 -7.286 8.378 13.854 1.00 9.32 C ANISOU 1649 CB ALA A 227 1351 1235 955 107 121 -406 C ATOM 1650 N TRP A 228 -6.543 5.424 12.946 1.00 7.09 N ANISOU 1650 N TRP A 228 1042 889 759 -67 -28 -7 N ATOM 1651 CA TRP A 228 -5.957 4.126 13.280 1.00 7.37 C ANISOU 1651 CA TRP A 228 884 852 1063 -2 193 72 C ATOM 1652 C TRP A 228 -4.855 3.790 12.280 1.00 6.70 C ANISOU 1652 C TRP A 228 730 1021 793 -52 -41 44 C ATOM 1653 O TRP A 228 -3.740 3.383 12.642 1.00 7.36 O ANISOU 1653 O TRP A 228 798 948 1048 4 -108 -19 O ATOM 1654 CB TRP A 228 -7.042 3.043 13.279 1.00 7.46 C ANISOU 1654 CB TRP A 228 892 751 1189 -102 -31 198 C ATOM 1655 CG TRP A 228 -6.580 1.773 13.913 1.00 6.89 C ANISOU 1655 CG TRP A 228 808 859 948 39 -27 120 C ATOM 1656 CD1 TRP A 228 -6.137 0.636 13.295 1.00 7.24 C ANISOU 1656 CD1 TRP A 228 807 876 1068 9 -35 43 C ATOM 1657 CD2 TRP A 228 -6.554 1.499 15.324 1.00 7.61 C ANISOU 1657 CD2 TRP A 228 1085 979 826 -14 3 -30 C ATOM 1658 NE1 TRP A 228 -5.814 -0.331 14.254 1.00 6.92 N ANISOU 1658 NE1 TRP A 228 894 856 878 42 -71 81 N ATOM 1659 CE2 TRP A 228 -6.033 0.200 15.501 1.00 7.20 C ANISOU 1659 CE2 TRP A 228 954 952 827 -59 22 89 C ATOM 1660 CE3 TRP A 228 -6.915 2.249 16.465 1.00 7.42 C ANISOU 1660 CE3 TRP A 228 870 1135 814 -103 -23 -15 C ATOM 1661 CZ2 TRP A 228 -5.917 -0.395 16.780 1.00 7.47 C ANISOU 1661 CZ2 TRP A 228 966 1046 825 -23 46 -76 C ATOM 1662 CZ3 TRP A 228 -6.770 1.676 17.725 1.00 8.44 C ANISOU 1662 CZ3 TRP A 228 1110 1132 964 44 115 128 C ATOM 1663 CH2 TRP A 228 -6.278 0.364 17.870 1.00 7.91 C ANISOU 1663 CH2 TRP A 228 988 1009 1005 -44 -57 -197 C ATOM 1664 N MET A 229 -5.165 3.958 10.985 1.00 6.87 N ANISOU 1664 N MET A 229 1046 824 738 -24 -22 -74 N ATOM 1665 CA MET A 229 -4.172 3.672 9.956 1.00 7.30 C ANISOU 1665 CA MET A 229 908 1005 859 -151 -11 -227 C ATOM 1666 C MET A 229 -2.968 4.600 10.025 1.00 6.63 C ANISOU 1666 C MET A 229 840 942 736 -10 -119 -59 C ATOM 1667 O MET A 229 -1.833 4.165 9.883 1.00 8.03 O ANISOU 1667 O MET A 229 972 1124 954 100 -112 -10 O ATOM 1668 CB MET A 229 -4.807 3.692 8.564 1.00 8.71 C ANISOU 1668 CB MET A 229 1201 1349 757 -257 -92 -13 C ATOM 1669 CG MET A 229 -5.861 2.591 8.353 1.00 8.02 C ANISOU 1669 CG MET A 229 1149 789 1106 143 -200 121 C ATOM 1670 SD MET A 229 -4.997 1.001 8.192 1.00 13.22 S ANISOU 1670 SD MET A 229 1439 1369 2213 42 -277 120 S ATOM 1671 CE MET A 229 -6.246 -0.199 8.508 1.00 17.31 C ANISOU 1671 CE MET A 229 1396 1538 3641 -331 -1081 139 C ATOM 1672 N LYS A 230 -3.193 5.873 10.290 1.00 7.91 N ANISOU 1672 N LYS A 230 1083 849 1074 -181 17 -161 N ATOM 1673 CA LYS A 230 -2.059 6.806 10.429 1.00 8.50 C ANISOU 1673 CA LYS A 230 1151 973 1104 -210 -3 29 C ATOM 1674 C LYS A 230 -1.201 6.410 11.625 1.00 8.00 C ANISOU 1674 C LYS A 230 1039 1056 944 -166 30 -200 C ATOM 1675 O LYS A 230 0.042 6.347 11.541 1.00 8.48 O ANISOU 1675 O LYS A 230 923 1150 1146 -192 91 -124 O ATOM 1676 CB LYS A 230 -2.600 8.233 10.630 1.00 9.67 C ANISOU 1676 CB LYS A 230 1438 836 1397 -28 -95 -120 C ATOM 1677 CG LYS A 230 -3.075 8.853 9.325 1.00 11.73 C ANISOU 1677 CG LYS A 230 1263 1334 1856 161 377 416 C ATOM 1678 CD LYS A 230 -1.847 9.348 8.584 1.00 16.19 C ANISOU 1678 CD LYS A 230 1689 1889 2571 -18 708 707 C ATOM 1679 CE LYS A 230 -2.173 10.572 7.773 1.00 11.92 C ANISOU 1679 CE LYS A 230 1760 1225 1543 -182 148 67 C ATOM 1680 NZ LYS A 230 -1.017 11.063 6.985 1.00 11.19 N ANISOU 1680 NZ LYS A 230 1568 1390 1292 -359 34 -106 N ATOM 1681 N ARG A 231 -1.844 6.158 12.763 1.00 7.97 N ANISOU 1681 N ARG A 231 1066 1077 882 -122 96 -193 N ATOM 1682 CA ARG A 231 -1.071 5.858 13.976 1.00 8.39 C ANISOU 1682 CA ARG A 231 1111 1101 974 48 152 -96 C ATOM 1683 C ARG A 231 -0.205 4.621 13.747 1.00 7.87 C ANISOU 1683 C ARG A 231 931 1031 1029 -67 -9 -389 C ATOM 1684 O ARG A 231 0.973 4.601 14.130 1.00 9.26 O ANISOU 1684 O ARG A 231 978 1294 1246 1 -79 -266 O ATOM 1685 CB ARG A 231 -2.025 5.667 15.176 1.00 8.68 C ANISOU 1685 CB ARG A 231 1137 1248 913 -61 100 -46 C ATOM 1686 CG ARG A 231 -1.319 5.078 16.399 1.00 8.76 C ANISOU 1686 CG ARG A 231 1075 1228 1023 -145 -197 -99 C ATOM 1687 CD ARG A 231 -0.213 6.002 16.915 1.00 9.99 C ANISOU 1687 CD ARG A 231 1267 1300 1226 -153 -260 -202 C ATOM 1688 NE ARG A 231 0.508 5.397 18.021 1.00 10.39 N ANISOU 1688 NE ARG A 231 1403 1275 1268 20 -252 -269 N ATOM 1689 CZ ARG A 231 1.537 4.574 17.911 1.00 12.78 C ANISOU 1689 CZ ARG A 231 1339 2077 1438 204 -167 -79 C ATOM 1690 NH1 ARG A 231 2.038 4.275 16.726 1.00 14.62 N ANISOU 1690 NH1 ARG A 231 1725 2210 1618 329 -167 -433 N ATOM 1691 NH2 ARG A 231 2.093 4.087 19.012 1.00 20.07 N ANISOU 1691 NH2 ARG A 231 2575 3334 1716 1146 -615 -70 N ATOM 1692 N PHE A 232 -0.780 3.563 13.162 1.00 7.63 N ANISOU 1692 N PHE A 232 1035 947 915 -63 118 -306 N ATOM 1693 CA PHE A 232 -0.116 2.274 13.143 1.00 7.39 C ANISOU 1693 CA PHE A 232 767 981 1060 -43 124 -120 C ATOM 1694 C PHE A 232 0.634 1.982 11.847 1.00 7.23 C ANISOU 1694 C PHE A 232 932 945 867 -89 -11 -156 C ATOM 1695 O PHE A 232 1.732 1.421 11.894 1.00 9.95 O ANISOU 1695 O PHE A 232 1131 1544 1104 352 31 -82 O ATOM 1696 CB PHE A 232 -1.078 1.189 13.567 1.00 8.12 C ANISOU 1696 CB PHE A 232 1164 1094 827 -81 142 42 C ATOM 1697 CG PHE A 232 -1.480 1.332 15.014 1.00 7.30 C ANISOU 1697 CG PHE A 232 969 1024 777 19 -16 -96 C ATOM 1698 CD1 PHE A 232 -0.512 1.174 16.016 1.00 8.75 C ANISOU 1698 CD1 PHE A 232 1145 1187 992 14 -197 -179 C ATOM 1699 CD2 PHE A 232 -2.781 1.652 15.376 1.00 7.42 C ANISOU 1699 CD2 PHE A 232 996 892 928 3 158 -94 C ATOM 1700 CE1 PHE A 232 -0.842 1.315 17.358 1.00 9.52 C ANISOU 1700 CE1 PHE A 232 1226 1281 1106 -1 76 -123 C ATOM 1701 CE2 PHE A 232 -3.124 1.849 16.709 1.00 7.96 C ANISOU 1701 CE2 PHE A 232 870 1141 1012 -160 -78 -232 C ATOM 1702 CZ PHE A 232 -2.143 1.677 17.703 1.00 8.90 C ANISOU 1702 CZ PHE A 232 1156 1034 1191 -48 -78 21 C ATOM 1703 N MET A 233 0.098 2.430 10.701 1.00 6.97 N ANISOU 1703 N MET A 233 937 969 741 -60 12 -301 N ATOM 1704 CA MET A 233 0.871 2.235 9.460 1.00 7.71 C ANISOU 1704 CA MET A 233 994 1135 798 -172 54 -145 C ATOM 1705 C MET A 233 2.037 3.181 9.357 1.00 7.58 C ANISOU 1705 C MET A 233 878 930 1071 -72 -1 -73 C ATOM 1706 O MET A 233 3.066 2.821 8.777 1.00 8.67 O ANISOU 1706 O MET A 233 980 1150 1164 -72 153 -206 O ATOM 1707 CB MET A 233 0.006 2.400 8.237 1.00 8.97 C ANISOU 1707 CB MET A 233 910 1542 954 -364 -135 -231 C ATOM 1708 CG MET A 233 -1.097 1.375 8.279 1.00 13.89 C ANISOU 1708 CG MET A 233 1640 2184 1451 -888 335 -1582 C ATOM 1709 SD MET A 233 -1.985 1.117 6.751 1.00 14.95 S ANISOU 1709 SD MET A 233 1981 2022 1678 -553 183 -272 S ATOM 1710 CE MET A 233 -0.721 1.042 5.459 1.00 8.99 C ANISOU 1710 CE MET A 233 1343 1495 575 -248 158 150 C ATOM 1711 N ASP A 234 1.861 4.408 9.859 1.00 7.64 N ANISOU 1711 N ASP A 234 1000 947 956 -151 -57 -206 N ATOM 1712 CA ASP A 234 2.879 5.457 9.713 1.00 8.68 C ANISOU 1712 CA ASP A 234 1041 1223 1032 -178 -168 -118 C ATOM 1713 C ASP A 234 3.635 5.664 11.014 1.00 8.03 C ANISOU 1713 C ASP A 234 1022 1022 1007 -105 64 -140 C ATOM 1714 O ASP A 234 4.475 6.560 11.084 1.00 9.70 O ANISOU 1714 O ASP A 234 1147 1232 1305 -394 21 -229 O ATOM 1715 CB ASP A 234 2.276 6.787 9.251 1.00 8.69 C ANISOU 1715 CB ASP A 234 1193 1093 1014 -91 -108 -53 C ATOM 1716 CG ASP A 234 1.609 6.736 7.889 1.00 8.04 C ANISOU 1716 CG ASP A 234 1038 901 1116 -86 3 -131 C ATOM 1717 OD1 ASP A 234 1.653 5.712 7.184 1.00 8.86 O ANISOU 1717 OD1 ASP A 234 1170 1057 1140 -121 65 -185 O ATOM 1718 OD2 ASP A 234 1.068 7.814 7.531 1.00 10.34 O ANISOU 1718 OD2 ASP A 234 1603 1075 1250 -113 -131 -253 O ATOM 1719 N ASN A 235 3.315 4.894 12.049 1.00 8.08 N ANISOU 1719 N ASN A 235 991 1123 954 0 -46 -142 N ATOM 1720 CA ASN A 235 3.887 5.098 13.404 1.00 8.69 C ANISOU 1720 CA ASN A 235 1043 1241 1015 27 -172 -298 C ATOM 1721 C ASN A 235 3.680 6.547 13.850 1.00 10.30 C ANISOU 1721 C ASN A 235 1349 1160 1403 -96 -337 -212 C ATOM 1722 O ASN A 235 4.517 7.117 14.561 1.00 12.10 O ANISOU 1722 O ASN A 235 1701 1333 1563 -203 -549 -363 O ATOM 1723 CB ASN A 235 5.388 4.767 13.429 1.00 10.25 C ANISOU 1723 CB ASN A 235 1078 1363 1451 146 -308 -286 C ATOM 1724 CG ASN A 235 5.690 3.375 12.943 1.00 11.11 C ANISOU 1724 CG ASN A 235 1389 1440 1391 100 -194 -49 C ATOM 1725 OD1 ASN A 235 4.821 2.507 12.921 1.00 13.58 O ANISOU 1725 OD1 ASN A 235 1628 1526 2003 224 -185 -265 O ATOM 1726 ND2 ASN A 235 6.934 3.157 12.545 1.00 15.40 N ANISOU 1726 ND2 ASN A 235 1474 2041 2336 118 122 -360 N ATOM 1727 N ASP A 236 2.590 7.172 13.406 1.00 9.01 N ANISOU 1727 N ASP A 236 1253 1077 1092 -62 9 -174 N ATOM 1728 CA ASP A 236 2.495 8.616 13.509 1.00 9.96 C ANISOU 1728 CA ASP A 236 1484 1121 1177 25 145 -180 C ATOM 1729 C ASP A 236 1.764 8.994 14.795 1.00 9.22 C ANISOU 1729 C ASP A 236 1164 1107 1231 -91 -80 -102 C ATOM 1730 O ASP A 236 0.519 8.982 14.857 1.00 9.31 O ANISOU 1730 O ASP A 236 1136 1229 1170 -194 -39 -407 O ATOM 1731 CB ASP A 236 1.791 9.167 12.264 1.00 9.86 C ANISOU 1731 CB ASP A 236 1376 1022 1345 -130 -96 -18 C ATOM 1732 CG ASP A 236 1.851 10.690 12.169 1.00 9.35 C ANISOU 1732 CG ASP A 236 1203 1098 1251 -128 -24 -66 C ATOM 1733 OD1 ASP A 236 2.178 11.370 13.185 1.00 9.64 O ANISOU 1733 OD1 ASP A 236 1356 1173 1130 -182 -43 -242 O ATOM 1734 OD2 ASP A 236 1.555 11.220 11.067 1.00 10.92 O ANISOU 1734 OD2 ASP A 236 1559 1297 1292 -231 -133 -61 O ATOM 1735 N THR A 237 2.538 9.319 15.824 1.00 9.47 N ANISOU 1735 N THR A 237 1294 1135 1166 -178 -152 -251 N ATOM 1736 CA THR A 237 1.943 9.568 17.128 1.00 9.57 C ANISOU 1736 CA THR A 237 1363 1179 1093 54 -98 -207 C ATOM 1737 C THR A 237 1.185 10.902 17.196 1.00 8.40 C ANISOU 1737 C THR A 237 1202 936 1052 -127 -94 -207 C ATOM 1738 O THR A 237 0.493 11.156 18.168 1.00 9.66 O ANISOU 1738 O THR A 237 1296 1181 1193 -171 68 -358 O ATOM 1739 CB THR A 237 2.958 9.477 18.277 1.00 11.01 C ANISOU 1739 CB THR A 237 1565 1246 1369 -120 -364 33 C ATOM 1740 OG1 THR A 237 3.966 10.461 18.063 1.00 12.50 O ANISOU 1740 OG1 THR A 237 1703 1488 1556 -278 -427 -206 O ATOM 1741 CG2 THR A 237 3.582 8.063 18.349 1.00 12.78 C ANISOU 1741 CG2 THR A 237 2024 1411 1421 264 -287 -245 C ATOM 1742 N ARG A 238 1.248 11.718 16.140 1.00 8.46 N ANISOU 1742 N ARG A 238 1126 900 1188 -250 -131 -118 N ATOM 1743 CA ARG A 238 0.354 12.868 16.090 1.00 9.51 C ANISOU 1743 CA ARG A 238 1320 1186 1105 -115 -44 68 C ATOM 1744 C ARG A 238 -1.092 12.387 16.152 1.00 9.69 C ANISOU 1744 C ARG A 238 1282 1020 1379 -257 43 -59 C ATOM 1745 O ARG A 238 -1.993 13.170 16.488 1.00 11.11 O ANISOU 1745 O ARG A 238 1476 1321 1424 1 -2 -140 O ATOM 1746 CB ARG A 238 0.557 13.671 14.796 1.00 8.82 C ANISOU 1746 CB ARG A 238 1304 931 1116 -237 -26 42 C ATOM 1747 CG ARG A 238 1.923 14.342 14.691 1.00 9.60 C ANISOU 1747 CG ARG A 238 1294 1151 1199 -346 13 -61 C ATOM 1748 CD ARG A 238 2.015 15.159 13.410 1.00 9.29 C ANISOU 1748 CD ARG A 238 1347 1152 1028 -313 -229 -218 C ATOM 1749 NE ARG A 238 1.946 14.255 12.254 1.00 10.03 N ANISOU 1749 NE ARG A 238 1385 1369 1055 -377 -75 -291 N ATOM 1750 CZ ARG A 238 1.844 14.666 10.992 1.00 9.82 C ANISOU 1750 CZ ARG A 238 1445 1181 1105 -135 -122 2 C ATOM 1751 NH1 ARG A 238 1.719 15.969 10.705 1.00 10.88 N ANISOU 1751 NH1 ARG A 238 1727 1138 1268 -279 7 -4 N ATOM 1752 NH2 ARG A 238 1.849 13.760 10.013 1.00 11.68 N ANISOU 1752 NH2 ARG A 238 1885 1382 1168 -119 -61 -342 N ATOM 1753 N TYR A 239 -1.324 11.136 15.726 1.00 8.98 N ANISOU 1753 N TYR A 239 1153 1179 1079 -202 -7 -236 N ATOM 1754 CA TYR A 239 -2.668 10.570 15.697 1.00 8.58 C ANISOU 1754 CA TYR A 239 1188 1132 940 -191 -11 -280 C ATOM 1755 C TYR A 239 -3.007 9.725 16.917 1.00 8.87 C ANISOU 1755 C TYR A 239 1087 1229 1054 -113 59 -365 C ATOM 1756 O TYR A 239 -4.087 9.133 16.948 1.00 10.65 O ANISOU 1756 O TYR A 239 1236 1587 1221 -430 160 -292 O ATOM 1757 CB TYR A 239 -2.807 9.733 14.418 1.00 9.20 C ANISOU 1757 CB TYR A 239 1439 1197 858 -277 10 -247 C ATOM 1758 CG TYR A 239 -2.881 10.613 13.201 1.00 9.19 C ANISOU 1758 CG TYR A 239 1298 1199 993 -269 -78 -51 C ATOM 1759 CD1 TYR A 239 -1.731 11.100 12.604 1.00 9.45 C ANISOU 1759 CD1 TYR A 239 1477 1220 894 -363 136 -231 C ATOM 1760 CD2 TYR A 239 -4.113 10.958 12.652 1.00 10.12 C ANISOU 1760 CD2 TYR A 239 1397 1174 1274 -72 -232 -98 C ATOM 1761 CE1 TYR A 239 -1.794 11.933 11.488 1.00 9.94 C ANISOU 1761 CE1 TYR A 239 1619 1152 1003 -386 -173 -263 C ATOM 1762 CE2 TYR A 239 -4.201 11.778 11.527 1.00 10.10 C ANISOU 1762 CE2 TYR A 239 1506 992 1336 -305 -91 -129 C ATOM 1763 CZ TYR A 239 -3.043 12.251 10.952 1.00 10.98 C ANISOU 1763 CZ TYR A 239 1731 1212 1226 -175 -113 -84 C ATOM 1764 OH TYR A 239 -3.164 13.085 9.862 1.00 12.64 O ANISOU 1764 OH TYR A 239 2117 1286 1397 -200 -316 58 O ATOM 1765 N SER A 240 -2.146 9.696 17.933 1.00 9.12 N ANISOU 1765 N SER A 240 1420 1114 929 -26 35 -133 N ATOM 1766 CA SER A 240 -2.395 8.788 19.052 1.00 9.32 C ANISOU 1766 CA SER A 240 1375 1195 968 -2 8 -88 C ATOM 1767 C SER A 240 -3.699 9.106 19.789 1.00 9.18 C ANISOU 1767 C SER A 240 1224 1277 984 -231 18 -288 C ATOM 1768 O SER A 240 -4.397 8.191 20.208 1.00 10.65 O ANISOU 1768 O SER A 240 1531 1462 1053 -362 211 -94 O ATOM 1769 CB SER A 240 -1.234 8.807 20.054 1.00 10.46 C ANISOU 1769 CB SER A 240 1250 1407 1315 -139 -181 -466 C ATOM 1770 OG SER A 240 -0.133 8.123 19.483 1.00 10.66 O ANISOU 1770 OG SER A 240 1368 1366 1317 -113 106 -233 O ATOM 1771 N THR A 241 -4.003 10.381 20.034 1.00 10.99 N ANISOU 1771 N THR A 241 1255 1697 1221 -130 131 -526 N ATOM 1772 CA THR A 241 -5.245 10.687 20.725 1.00 11.08 C ANISOU 1772 CA THR A 241 1303 1647 1259 148 39 -492 C ATOM 1773 C THR A 241 -6.440 10.282 19.889 1.00 9.46 C ANISOU 1773 C THR A 241 1038 1387 1166 17 166 -22 C ATOM 1774 O THR A 241 -7.348 9.632 20.380 1.00 10.53 O ANISOU 1774 O THR A 241 1411 1518 1071 -90 -51 -36 O ATOM 1775 CB THR A 241 -5.362 12.167 21.101 1.00 13.06 C ANISOU 1775 CB THR A 241 1408 1798 1754 119 94 -868 C ATOM 1776 OG1 THR A 241 -4.253 12.511 21.935 1.00 17.07 O ANISOU 1776 OG1 THR A 241 1909 2677 1898 -432 24 -916 O ATOM 1777 CG2 THR A 241 -6.649 12.398 21.901 1.00 18.73 C ANISOU 1777 CG2 THR A 241 1987 2815 2314 224 740 -1049 C ATOM 1778 N PHE A 242 -6.449 10.659 18.607 1.00 9.13 N ANISOU 1778 N PHE A 242 1328 1100 1041 1 63 -182 N ATOM 1779 CA PHE A 242 -7.577 10.289 17.772 1.00 9.50 C ANISOU 1779 CA PHE A 242 1260 1207 1139 -105 -157 -118 C ATOM 1780 C PHE A 242 -7.725 8.777 17.642 1.00 8.50 C ANISOU 1780 C PHE A 242 1096 1163 969 40 87 -120 C ATOM 1781 O PHE A 242 -8.844 8.258 17.636 1.00 9.55 O ANISOU 1781 O PHE A 242 1202 1198 1228 -178 108 -32 O ATOM 1782 CB PHE A 242 -7.472 10.925 16.373 1.00 10.06 C ANISOU 1782 CB PHE A 242 1569 1012 1240 4 79 -61 C ATOM 1783 CG PHE A 242 -7.473 12.429 16.405 1.00 10.29 C ANISOU 1783 CG PHE A 242 1453 1113 1340 -57 -277 -176 C ATOM 1784 CD1 PHE A 242 -8.601 13.116 16.848 1.00 12.77 C ANISOU 1784 CD1 PHE A 242 1865 1296 1691 161 78 -178 C ATOM 1785 CD2 PHE A 242 -6.334 13.152 16.067 1.00 11.19 C ANISOU 1785 CD2 PHE A 242 1486 1172 1593 -124 -168 -94 C ATOM 1786 CE1 PHE A 242 -8.642 14.505 16.834 1.00 14.30 C ANISOU 1786 CE1 PHE A 242 2044 1313 2077 248 22 -94 C ATOM 1787 CE2 PHE A 242 -6.330 14.542 16.139 1.00 14.65 C ANISOU 1787 CE2 PHE A 242 2116 1182 2267 10 102 -43 C ATOM 1788 CZ PHE A 242 -7.485 15.207 16.513 1.00 15.67 C ANISOU 1788 CZ PHE A 242 2312 1479 2162 35 87 -287 C ATOM 1789 N ALA A 243 -6.618 8.052 17.545 1.00 8.26 N ANISOU 1789 N ALA A 243 1144 1034 960 -20 46 -167 N ATOM 1790 CA ALA A 243 -6.678 6.610 17.408 1.00 8.14 C ANISOU 1790 CA ALA A 243 1054 931 1107 6 168 40 C ATOM 1791 C ALA A 243 -7.163 5.937 18.688 1.00 8.51 C ANISOU 1791 C ALA A 243 999 1193 1040 60 -96 -16 C ATOM 1792 O ALA A 243 -7.976 5.016 18.629 1.00 9.48 O ANISOU 1792 O ALA A 243 1229 1167 1203 -96 34 47 O ATOM 1793 CB ALA A 243 -5.305 6.057 17.015 1.00 9.51 C ANISOU 1793 CB ALA A 243 984 1404 1224 62 211 -78 C ATOM 1794 N CYS A 244 -6.694 6.419 19.846 1.00 9.10 N ANISOU 1794 N CYS A 244 1310 1139 1008 -104 -73 13 N ATOM 1795 CA CYS A 244 -6.930 5.707 21.101 1.00 10.20 C ANISOU 1795 CA CYS A 244 1202 1474 1197 113 -31 202 C ATOM 1796 C CYS A 244 -8.128 6.177 21.902 1.00 9.90 C ANISOU 1796 C CYS A 244 1393 1333 1033 -63 17 -150 C ATOM 1797 O CYS A 244 -8.601 5.428 22.773 1.00 12.28 O ANISOU 1797 O CYS A 244 2016 1515 1135 -151 292 24 O ATOM 1798 CB CYS A 244 -5.687 5.734 21.975 1.00 12.97 C ANISOU 1798 CB CYS A 244 1571 1893 1461 -61 -157 -159 C ATOM 1799 SG CYS A 244 -4.250 4.945 21.218 1.00 15.17 S ANISOU 1799 SG CYS A 244 1596 2209 1956 121 -98 420 S ATOM 1800 N GLU A 245 -8.625 7.386 21.647 1.00 9.92 N ANISOU 1800 N GLU A 245 1382 1330 1057 -59 182 -217 N ATOM 1801 CA GLU A 245 -9.629 7.972 22.533 1.00 11.19 C ANISOU 1801 CA GLU A 245 1317 1426 1507 -135 367 -186 C ATOM 1802 C GLU A 245 -10.974 7.273 22.403 1.00 10.32 C ANISOU 1802 C GLU A 245 1306 1584 1031 -206 186 -116 C ATOM 1803 O GLU A 245 -11.406 6.857 21.323 1.00 10.68 O ANISOU 1803 O GLU A 245 1353 1647 1057 -230 193 -235 O ATOM 1804 CB GLU A 245 -9.812 9.468 22.237 1.00 12.08 C ANISOU 1804 CB GLU A 245 2155 1344 1089 -15 306 -208 C ATOM 1805 CG GLU A 245 -10.439 9.775 20.867 1.00 13.18 C ANISOU 1805 CG GLU A 245 1745 1662 1598 82 -60 88 C ATOM 1806 CD GLU A 245 -10.544 11.264 20.563 1.00 16.16 C ANISOU 1806 CD GLU A 245 2206 1990 1942 129 278 -204 C ATOM 1807 OE1 GLU A 245 -10.323 12.107 21.470 1.00 19.90 O ANISOU 1807 OE1 GLU A 245 3243 1934 2382 -20 88 -314 O ATOM 1808 OE2 GLU A 245 -10.800 11.600 19.387 1.00 17.60 O ANISOU 1808 OE2 GLU A 245 2838 1753 2095 168 73 -103 O ATOM 1809 N ASN A 246 -11.734 7.295 23.492 1.00 10.96 N ANISOU 1809 N ASN A 246 1329 1678 1156 -155 440 -166 N ATOM 1810 CA ASN A 246 -13.173 7.041 23.410 1.00 10.74 C ANISOU 1810 CA ASN A 246 1352 1680 1048 -71 481 102 C ATOM 1811 C ASN A 246 -13.782 8.334 22.858 1.00 11.27 C ANISOU 1811 C ASN A 246 1472 1588 1222 -114 341 -203 C ATOM 1812 O ASN A 246 -13.621 9.384 23.479 1.00 15.12 O ANISOU 1812 O ASN A 246 2255 1677 1810 -22 471 -539 O ATOM 1813 CB ASN A 246 -13.672 6.732 24.834 1.00 10.67 C ANISOU 1813 CB ASN A 246 1321 1853 879 -318 284 -113 C ATOM 1814 CG ASN A 246 -15.127 6.320 24.890 1.00 9.92 C ANISOU 1814 CG ASN A 246 1362 1257 1148 33 298 -118 C ATOM 1815 OD1 ASN A 246 -15.605 5.771 25.911 1.00 14.22 O ANISOU 1815 OD1 ASN A 246 2181 1903 1316 -287 607 -72 O ATOM 1816 ND2 ASN A 246 -15.859 6.678 23.878 1.00 9.20 N ANISOU 1816 ND2 ASN A 246 1159 1299 1035 53 510 -24 N ATOM 1817 N PRO A 247 -14.521 8.268 21.727 1.00 11.46 N ANISOU 1817 N PRO A 247 1965 1256 1133 269 274 9 N ATOM 1818 CA PRO A 247 -15.088 9.511 21.188 1.00 14.35 C ANISOU 1818 CA PRO A 247 2293 1672 1486 171 602 -83 C ATOM 1819 C PRO A 247 -16.146 10.106 22.103 1.00 12.26 C ANISOU 1819 C PRO A 247 1527 1536 1592 202 465 217 C ATOM 1820 O PRO A 247 -16.561 11.245 21.885 1.00 15.00 O ANISOU 1820 O PRO A 247 2193 1720 1786 459 347 185 O ATOM 1821 CB PRO A 247 -15.704 9.093 19.847 1.00 18.39 C ANISOU 1821 CB PRO A 247 3361 2427 1197 1252 40 -111 C ATOM 1822 CG PRO A 247 -15.594 7.630 19.755 1.00 18.44 C ANISOU 1822 CG PRO A 247 2231 2368 2407 481 -705 215 C ATOM 1823 CD PRO A 247 -14.743 7.099 20.852 1.00 11.61 C ANISOU 1823 CD PRO A 247 1580 1663 1167 0 117 -247 C ATOM 1824 N ASN A 248 -16.675 9.293 23.016 1.00 12.19 N ANISOU 1824 N ASN A 248 1733 1673 1225 199 363 -24 N ATOM 1825 CA ASN A 248 -17.741 9.704 23.954 1.00 12.68 C ANISOU 1825 CA ASN A 248 1914 1640 1260 310 390 -215 C ATOM 1826 C ASN A 248 -18.902 10.306 23.127 1.00 13.75 C ANISOU 1826 C ASN A 248 1967 1871 1387 221 426 -147 C ATOM 1827 O ASN A 248 -19.350 11.434 23.351 1.00 15.03 O ANISOU 1827 O ASN A 248 2228 1825 1654 292 189 -127 O ATOM 1828 CB ASN A 248 -17.213 10.697 25.020 1.00 14.12 C ANISOU 1828 CB ASN A 248 1911 2358 1094 279 37 -321 C ATOM 1829 CG ASN A 248 -16.123 10.105 25.948 1.00 15.83 C ANISOU 1829 CG ASN A 248 2251 2070 1692 150 -105 -425 C ATOM 1830 OD1 ASN A 248 -16.094 8.897 26.254 1.00 22.32 O ANISOU 1830 OD1 ASN A 248 3116 2563 2799 476 -91 -225 O ATOM 1831 ND2 ASN A 248 -15.190 10.948 26.367 1.00 19.13 N ANISOU 1831 ND2 ASN A 248 2204 2696 2367 -565 367 46 N ATOM 1832 N SER A 249 -19.368 9.540 22.153 1.00 13.69 N ANISOU 1832 N SER A 249 1905 2002 1295 120 195 144 N ATOM 1833 CA SER A 249 -20.316 10.026 21.159 1.00 13.19 C ANISOU 1833 CA SER A 249 1668 1803 1538 225 49 38 C ATOM 1834 C SER A 249 -21.653 9.294 21.332 1.00 11.95 C ANISOU 1834 C SER A 249 1611 1413 1515 204 88 -98 C ATOM 1835 O SER A 249 -21.686 8.074 21.506 1.00 12.71 O ANISOU 1835 O SER A 249 1701 1623 1505 100 321 -74 O ATOM 1836 CB SER A 249 -19.771 9.706 19.766 1.00 13.37 C ANISOU 1836 CB SER A 249 1879 1959 1240 -12 -114 -244 C ATOM 1837 OG SER A 249 -20.768 9.898 18.773 1.00 15.83 O ANISOU 1837 OG SER A 249 1815 2464 1735 -262 29 -39 O ATOM 1838 N THR A 250 -22.760 10.017 21.156 1.00 13.68 N ANISOU 1838 N THR A 250 1561 1914 1722 354 187 -233 N ATOM 1839 CA THR A 250 -24.069 9.386 21.151 1.00 15.10 C ANISOU 1839 CA THR A 250 1504 1929 2302 500 264 -24 C ATOM 1840 C THR A 250 -24.270 8.479 19.938 1.00 15.04 C ANISOU 1840 C THR A 250 1798 2057 1859 54 92 231 C ATOM 1841 O THR A 250 -25.171 7.648 19.934 1.00 18.18 O ANISOU 1841 O THR A 250 1671 2499 2735 -96 321 185 O ATOM 1842 CB THR A 250 -25.203 10.414 21.238 1.00 19.13 C ANISOU 1842 CB THR A 250 2342 2087 2838 850 792 157 C ATOM 1843 OG1 THR A 250 -25.200 11.228 20.068 1.00 22.88 O ANISOU 1843 OG1 THR A 250 2631 2689 3373 659 141 463 O ATOM 1844 CG2 THR A 250 -25.039 11.294 22.456 1.00 22.43 C ANISOU 1844 CG2 THR A 250 2634 2599 3287 745 1248 -494 C ATOM 1845 N ARG A 251 -23.360 8.529 18.965 1.00 13.15 N ANISOU 1845 N ARG A 251 1579 1741 1675 279 150 -101 N ATOM 1846 CA ARG A 251 -23.407 7.615 17.801 1.00 12.17 C ANISOU 1846 CA ARG A 251 1377 1521 1725 154 -67 159 C ATOM 1847 C ARG A 251 -22.775 6.240 18.111 1.00 12.24 C ANISOU 1847 C ARG A 251 1270 1678 1702 349 104 -141 C ATOM 1848 O ARG A 251 -22.816 5.361 17.267 1.00 11.58 O ANISOU 1848 O ARG A 251 1561 1536 1299 -112 21 10 O ATOM 1849 CB ARG A 251 -22.680 8.227 16.597 1.00 14.84 C ANISOU 1849 CB ARG A 251 2172 1794 1670 332 145 324 C ATOM 1850 CG ARG A 251 -23.255 9.553 16.139 1.00 16.83 C ANISOU 1850 CG ARG A 251 2450 1780 2161 453 -48 92 C ATOM 1851 CD ARG A 251 -22.274 10.340 15.283 1.00 25.23 C ANISOU 1851 CD ARG A 251 4169 2130 3285 86 248 971 C ATOM 1852 NE ARG A 251 -22.798 11.660 14.946 1.00 32.87 N ANISOU 1852 NE ARG A 251 5656 3027 3804 990 -653 1226 N ATOM 1853 CZ ARG A 251 -23.630 11.899 13.938 1.00 55.23 C ANISOU 1853 CZ ARG A 251 9656 4222 7107 3332 -3632 889 C ATOM 1854 NH1 ARG A 251 -24.016 10.909 13.139 1.00 44.67 N ANISOU 1854 NH1 ARG A 251 6835 6324 3813 1104 -625 1131 N ATOM 1855 NH2 ARG A 251 -24.052 13.136 13.709 1.00 43.28 N ANISOU 1855 NH2 ARG A 251 8278 3338 4828 2785 -244 -33 N ATOM 1856 N VAL A 252 -22.180 6.080 19.302 1.00 11.18 N ANISOU 1856 N VAL A 252 1521 1340 1387 243 146 10 N ATOM 1857 CA VAL A 252 -21.438 4.880 19.632 1.00 11.46 C ANISOU 1857 CA VAL A 252 1325 1411 1619 228 358 185 C ATOM 1858 C VAL A 252 -22.121 4.180 20.798 1.00 10.82 C ANISOU 1858 C VAL A 252 1715 1284 1112 33 54 -85 C ATOM 1859 O VAL A 252 -22.220 4.733 21.916 1.00 12.65 O ANISOU 1859 O VAL A 252 2101 1539 1166 -176 248 -201 O ATOM 1860 CB VAL A 252 -19.996 5.246 20.017 1.00 10.24 C ANISOU 1860 CB VAL A 252 1345 1347 1196 114 323 62 C ATOM 1861 CG1 VAL A 252 -19.239 4.021 20.519 1.00 12.57 C ANISOU 1861 CG1 VAL A 252 1869 1441 1466 67 27 164 C ATOM 1862 CG2 VAL A 252 -19.300 5.861 18.809 1.00 12.32 C ANISOU 1862 CG2 VAL A 252 1492 1774 1412 89 427 243 C ATOM 1863 N SER A 253 -22.593 2.963 20.568 1.00 9.56 N ANISOU 1863 N SER A 253 1038 1362 1232 87 265 84 N ATOM 1864 CA SER A 253 -23.275 2.229 21.621 1.00 9.45 C ANISOU 1864 CA SER A 253 1142 1202 1245 41 307 135 C ATOM 1865 C SER A 253 -22.323 1.371 22.445 1.00 10.40 C ANISOU 1865 C SER A 253 1173 1455 1321 72 251 -64 C ATOM 1866 O SER A 253 -22.687 0.926 23.528 1.00 13.55 O ANISOU 1866 O SER A 253 1685 2163 1299 121 259 310 O ATOM 1867 CB SER A 253 -24.399 1.369 21.035 1.00 12.27 C ANISOU 1867 CB SER A 253 1188 1856 1615 3 341 -277 C ATOM 1868 OG SER A 253 -23.937 0.683 19.879 1.00 12.01 O ANISOU 1868 OG SER A 253 1445 1665 1450 50 62 -98 O ATOM 1869 N ASP A 254 -21.098 1.138 21.971 1.00 10.56 N ANISOU 1869 N ASP A 254 1225 1457 1328 243 90 -86 N ATOM 1870 CA ASP A 254 -20.131 0.340 22.747 1.00 10.74 C ANISOU 1870 CA ASP A 254 1284 1294 1502 167 30 16 C ATOM 1871 C ASP A 254 -18.744 0.744 22.280 1.00 9.83 C ANISOU 1871 C ASP A 254 1262 1411 1062 -100 12 -23 C ATOM 1872 O ASP A 254 -18.488 0.760 21.075 1.00 11.54 O ANISOU 1872 O ASP A 254 1407 2018 957 -109 14 29 O ATOM 1873 CB ASP A 254 -20.374 -1.163 22.512 1.00 12.21 C ANISOU 1873 CB ASP A 254 1823 1349 1468 75 -167 133 C ATOM 1874 CG ASP A 254 -19.697 -2.056 23.538 1.00 13.77 C ANISOU 1874 CG ASP A 254 1983 1693 1555 -80 -131 64 C ATOM 1875 OD1 ASP A 254 -18.647 -1.702 24.055 1.00 16.56 O ANISOU 1875 OD1 ASP A 254 2144 1687 2458 29 -679 481 O ATOM 1876 OD2 ASP A 254 -20.145 -3.200 23.717 1.00 18.28 O ANISOU 1876 OD2 ASP A 254 2857 1893 2193 -347 -216 551 O ATOM 1877 N PHE A 255 -17.886 1.144 23.204 1.00 9.56 N ANISOU 1877 N PHE A 255 982 1342 1308 -36 33 -118 N ATOM 1878 CA PHE A 255 -16.499 1.459 22.889 1.00 10.20 C ANISOU 1878 CA PHE A 255 1002 1432 1441 0 45 -96 C ATOM 1879 C PHE A 255 -15.616 0.656 23.834 1.00 9.03 C ANISOU 1879 C PHE A 255 1184 1414 831 150 73 -235 C ATOM 1880 O PHE A 255 -15.830 0.703 25.065 1.00 11.81 O ANISOU 1880 O PHE A 255 1673 2013 800 303 70 -88 O ATOM 1881 CB PHE A 255 -16.219 2.951 23.105 1.00 10.54 C ANISOU 1881 CB PHE A 255 1338 1531 1134 49 359 -98 C ATOM 1882 CG PHE A 255 -14.766 3.307 22.893 1.00 10.56 C ANISOU 1882 CG PHE A 255 1262 1518 1228 199 202 -84 C ATOM 1883 CD1 PHE A 255 -14.290 3.521 21.609 1.00 11.65 C ANISOU 1883 CD1 PHE A 255 1601 1217 1608 82 665 -99 C ATOM 1884 CD2 PHE A 255 -13.862 3.339 23.963 1.00 11.78 C ANISOU 1884 CD2 PHE A 255 1468 1415 1591 -112 43 -155 C ATOM 1885 CE1 PHE A 255 -12.953 3.768 21.387 1.00 11.71 C ANISOU 1885 CE1 PHE A 255 1553 1097 1796 134 431 -145 C ATOM 1886 CE2 PHE A 255 -12.506 3.543 23.731 1.00 12.84 C ANISOU 1886 CE2 PHE A 255 1725 1370 1783 -89 -133 -81 C ATOM 1887 CZ PHE A 255 -12.052 3.773 22.443 1.00 12.64 C ANISOU 1887 CZ PHE A 255 1714 1202 1884 330 191 -74 C ATOM 1888 N ARG A 256 -14.560 0.040 23.308 1.00 9.37 N ANISOU 1888 N ARG A 256 1060 1324 1173 21 37 -55 N ATOM 1889 CA ARG A 256 -13.548 -0.614 24.166 1.00 9.51 C ANISOU 1889 CA ARG A 256 1317 1147 1149 161 132 188 C ATOM 1890 C ARG A 256 -12.197 -0.414 23.519 1.00 9.34 C ANISOU 1890 C ARG A 256 1195 1415 936 -91 33 -113 C ATOM 1891 O ARG A 256 -12.108 -0.349 22.291 1.00 9.16 O ANISOU 1891 O ARG A 256 1284 1336 858 179 -3 -139 O ATOM 1892 CB ARG A 256 -13.812 -2.131 24.314 1.00 11.55 C ANISOU 1892 CB ARG A 256 1381 1445 1560 -120 -169 269 C ATOM 1893 CG ARG A 256 -15.246 -2.439 24.701 1.00 13.81 C ANISOU 1893 CG ARG A 256 1878 1534 1834 -359 59 183 C ATOM 1894 CD ARG A 256 -15.568 -3.924 24.685 1.00 17.34 C ANISOU 1894 CD ARG A 256 2179 1553 2855 -433 42 312 C ATOM 1895 NE ARG A 256 -17.011 -4.079 24.787 1.00 15.96 N ANISOU 1895 NE ARG A 256 2213 1656 2194 -387 -37 376 N ATOM 1896 CZ ARG A 256 -17.659 -4.865 25.646 1.00 16.27 C ANISOU 1896 CZ ARG A 256 2157 2088 1937 -219 -161 455 C ATOM 1897 NH1 ARG A 256 -17.018 -5.813 26.342 1.00 16.52 N ANISOU 1897 NH1 ARG A 256 2389 1913 1973 -2 -150 416 N ATOM 1898 NH2 ARG A 256 -18.985 -4.857 25.618 1.00 16.93 N ANISOU 1898 NH2 ARG A 256 2253 2107 2071 -377 107 21 N ATOM 1899 N THR A 257 -11.128 -0.347 24.304 1.00 9.09 N ANISOU 1899 N THR A 257 1093 1346 1014 158 91 -54 N ATOM 1900 CA THR A 257 -9.803 -0.327 23.684 1.00 8.76 C ANISOU 1900 CA THR A 257 1071 1351 903 140 -21 79 C ATOM 1901 C THR A 257 -8.810 -0.898 24.677 1.00 9.93 C ANISOU 1901 C THR A 257 1160 1465 1144 164 -68 113 C ATOM 1902 O THR A 257 -9.024 -0.800 25.895 1.00 12.35 O ANISOU 1902 O THR A 257 1601 2054 1035 111 47 10 O ATOM 1903 CB THR A 257 -9.453 1.105 23.196 1.00 10.14 C ANISOU 1903 CB THR A 257 1386 1300 1166 -236 263 -170 C ATOM 1904 OG1 THR A 257 -8.398 1.059 22.226 1.00 10.37 O ANISOU 1904 OG1 THR A 257 1363 1473 1102 50 101 137 O ATOM 1905 CG2 THR A 257 -9.028 2.036 24.337 1.00 12.02 C ANISOU 1905 CG2 THR A 257 1747 1427 1392 63 -220 -356 C ATOM 1906 N ALA A 258 -7.702 -1.428 24.169 1.00 9.45 N ANISOU 1906 N ALA A 258 1157 1236 1199 208 -147 44 N ATOM 1907 CA ALA A 258 -6.646 -1.973 25.027 1.00 9.15 C ANISOU 1907 CA ALA A 258 1127 1378 970 48 -137 97 C ATOM 1908 C ALA A 258 -5.310 -1.758 24.359 1.00 9.02 C ANISOU 1908 C ALA A 258 1165 1170 1090 -8 -21 -93 C ATOM 1909 O ALA A 258 -5.186 -1.842 23.128 1.00 9.55 O ANISOU 1909 O ALA A 258 1320 1297 1011 168 -97 -22 O ATOM 1910 CB ALA A 258 -6.865 -3.446 25.316 1.00 12.40 C ANISOU 1910 CB ALA A 258 1848 1326 1537 -112 -362 184 C ATOM 1911 N ASN A 259 -4.292 -1.531 25.177 1.00 11.21 N ANISOU 1911 N ASN A 259 1206 1572 1481 -107 -413 -18 N ATOM 1912 CA ASN A 259 -2.908 -1.483 24.709 1.00 9.98 C ANISOU 1912 CA ASN A 259 1406 1434 952 -202 -75 34 C ATOM 1913 C ASN A 259 -2.701 -0.398 23.657 1.00 10.76 C ANISOU 1913 C ASN A 259 1379 1525 1184 -79 -316 160 C ATOM 1914 O ASN A 259 -1.864 -0.534 22.782 1.00 13.70 O ANISOU 1914 O ASN A 259 1974 1805 1424 -111 96 187 O ATOM 1915 CB ASN A 259 -2.440 -2.823 24.165 1.00 11.75 C ANISOU 1915 CB ASN A 259 1518 1561 1384 19 -195 108 C ATOM 1916 CG ASN A 259 -2.585 -3.921 25.172 1.00 13.69 C ANISOU 1916 CG ASN A 259 2474 1642 1082 35 -635 356 C ATOM 1917 OD1 ASN A 259 -2.328 -3.721 26.373 1.00 17.70 O ANISOU 1917 OD1 ASN A 259 3363 2091 1270 430 -922 292 O ATOM 1918 ND2 ASN A 259 -3.066 -5.068 24.718 1.00 17.65 N ANISOU 1918 ND2 ASN A 259 3304 1913 1490 -247 -124 30 N ATOM 1919 N CYS A 260 -3.460 0.689 23.758 1.00 11.49 N ANISOU 1919 N CYS A 260 1471 1441 1452 -72 -376 274 N ATOM 1920 CA CYS A 260 -3.371 1.711 22.720 1.00 13.67 C ANISOU 1920 CA CYS A 260 1959 1427 1808 -111 -661 406 C ATOM 1921 C CYS A 260 -2.543 2.902 23.213 1.00 20.34 C ANISOU 1921 C CYS A 260 3217 2029 2482 -539 -439 412 C ATOM 1922 O CYS A 260 -2.731 3.343 24.315 1.00 27.31 O ANISOU 1922 O CYS A 260 5475 2714 2187 -1166 -56 -557 O ATOM 1923 CB CYS A 260 -4.789 2.115 22.336 1.00 14.45 C ANISOU 1923 CB CYS A 260 2216 1468 1805 330 -539 270 C ATOM 1924 SG CYS A 260 -4.913 3.027 20.784 1.00 16.34 S ANISOU 1924 SG CYS A 260 2113 2405 1688 407 -268 50 S ATOM 1925 N SER A 261 -1.602 3.366 22.398 1.00 19.61 N ANISOU 1925 N SER A 261 2261 2339 2849 34 -349 65 N ATOM 1926 CA SER A 261 -0.686 4.481 22.737 1.00 23.62 C ANISOU 1926 CA SER A 261 3104 3806 2064 -123 -541 519 C ATOM 1927 C SER A 261 -0.415 5.293 21.479 1.00 25.57 C ANISOU 1927 C SER A 261 2630 5187 1897 600 95 578 C ATOM 1928 O SER A 261 -0.764 4.846 20.384 1.00 23.98 O ANISOU 1928 O SER A 261 3752 2900 2459 -513 1015 123 O ATOM 1929 CB SER A 261 0.655 3.901 23.205 1.00 28.92 C ANISOU 1929 CB SER A 261 2633 4337 4017 -119 310 -269 C ATOM 1930 OG SER A 261 1.310 3.286 22.087 1.00 27.00 O ANISOU 1930 OG SER A 261 2851 3660 3748 355 -237 579 O ATOM 1931 OXT SER A 261 0.202 6.365 21.530 1.00 32.69 O ANISOU 1931 OXT SER A 261 4590 3749 4079 78 -505 266 O TER 1932 SER A 261 HETATM 1933 C13 856 A 301 -22.941 -9.084 3.322 1.00 31.85 C ANISOU 1933 C13 856 A 301 5490 3646 2964 1197 -1128 78 C HETATM 1934 C15 856 A 301 -23.084 -13.371 5.525 1.00 21.51 C ANISOU 1934 C15 856 A 301 2729 3515 1928 -444 -65 169 C HETATM 1935 C01 856 A 301 -23.730 -16.712 10.658 1.00 32.65 C ANISOU 1935 C01 856 A 301 7033 2229 3142 797 2463 1526 C HETATM 1936 O02 856 A 301 -23.020 -15.874 9.777 1.00 24.94 O ANISOU 1936 O02 856 A 301 3697 2727 3052 -872 365 278 O HETATM 1937 C03 856 A 301 -23.583 -15.736 8.503 1.00 23.76 C ANISOU 1937 C03 856 A 301 3252 2866 2909 -24 328 704 C HETATM 1938 O04 856 A 301 -24.627 -16.244 8.239 1.00 28.17 O ANISOU 1938 O04 856 A 301 3133 3541 4026 -303 348 89 O HETATM 1939 C05 856 A 301 -22.976 -14.689 7.580 1.00 19.50 C ANISOU 1939 C05 856 A 301 2367 2152 2890 19 853 -1 C HETATM 1940 C06 856 A 301 -21.843 -14.025 7.996 1.00 21.56 C ANISOU 1940 C06 856 A 301 2001 3229 2960 635 51 483 C HETATM 1941 C07 856 A 301 -21.292 -13.087 7.123 1.00 23.08 C ANISOU 1941 C07 856 A 301 2779 3770 2219 187 278 454 C HETATM 1942 C08 856 A 301 -21.893 -12.766 5.909 1.00 18.87 C ANISOU 1942 C08 856 A 301 1514 3426 2228 -208 384 587 C HETATM 1943 C09 856 A 301 -21.362 -11.546 5.132 1.00 16.54 C ANISOU 1943 C09 856 A 301 1575 2256 2452 -113 544 -236 C HETATM 1944 O10 856 A 301 -20.289 -11.556 4.626 1.00 9.55 O ANISOU 1944 O10 856 A 301 975 1481 1170 -20 79 -364 O HETATM 1945 O11 856 A 301 -22.224 -10.446 4.966 1.00 19.65 O ANISOU 1945 O11 856 A 301 1820 3073 2573 -66 515 -4 O HETATM 1946 C12 856 A 301 -21.906 -9.224 4.413 1.00 21.85 C ANISOU 1946 C12 856 A 301 2934 3509 1857 615 19 -258 C HETATM 1947 O14 856 A 301 -22.207 -8.686 2.224 1.00 31.75 O ANISOU 1947 O14 856 A 301 4954 2628 4482 288 528 -1426 O HETATM 1948 C16 856 A 301 -23.612 -14.348 6.371 1.00 25.13 C ANISOU 1948 C16 856 A 301 3588 2682 3278 -526 196 259 C HETATM 1949 S SO4 A 302 8.283 0.110 10.702 1.00 25.64 S ANISOU 1949 S SO4 A 302 3075 3203 3462 -221 92 -129 S HETATM 1950 O1 SO4 A 302 9.551 0.855 10.484 1.00 36.17 O ANISOU 1950 O1 SO4 A 302 2850 3878 7015 -572 -481 -276 O HETATM 1951 O2 SO4 A 302 7.350 0.330 9.563 1.00 22.32 O ANISOU 1951 O2 SO4 A 302 2794 3071 2615 62 -48 36 O HETATM 1952 O3 SO4 A 302 8.618 -1.342 10.758 1.00 35.08 O ANISOU 1952 O3 SO4 A 302 5144 2209 5973 173 -155 -101 O HETATM 1953 O4 SO4 A 302 7.671 0.515 11.982 1.00 30.00 O ANISOU 1953 O4 SO4 A 302 3823 4423 3151 888 18 -988 O HETATM 1954 S SO4 A 303 -22.560 13.427 19.581 1.00 51.24 S ANISOU 1954 S SO4 A 303 7424 5181 6862 -2087 -1994 2302 S HETATM 1955 O1 SO4 A 303 -21.847 12.804 18.436 1.00 76.61 O ANISOU 1955 O1 SO4 A 303 12670 5739 10698 -2788 1463 668 O HETATM 1956 O2 SO4 A 303 -24.031 13.307 19.402 1.00 46.10 O ANISOU 1956 O2 SO4 A 303 6053 5583 5880 -1474 -59 2660 O HETATM 1957 O3 SO4 A 303 -22.180 12.723 20.826 1.00 29.19 O ANISOU 1957 O3 SO4 A 303 4192 2169 4729 736 136 819 O HETATM 1958 O4 SO4 A 303 -22.195 14.861 19.652 1.00 51.42 O ANISOU 1958 O4 SO4 A 303 6027 3525 9984 -271 44 3266 O HETATM 1959 C1 GOL A 304 -1.773 -14.847 3.429 1.00 18.56 C ANISOU 1959 C1 GOL A 304 2175 2163 2715 -304 -246 -531 C HETATM 1960 O1 GOL A 304 -1.179 -15.390 4.224 1.00 12.61 O ANISOU 1960 O1 GOL A 304 1505 1557 1727 -203 142 -471 O HETATM 1961 C2 GOL A 304 -2.470 -16.078 3.119 1.00 32.37 C ANISOU 1961 C2 GOL A 304 3221 4615 4462 1903 367 -771 C HETATM 1962 O2 GOL A 304 -2.156 -16.064 1.691 1.00103.72 O ANISOU 1962 O2 GOL A 304 22287 9437 7685 -2038 1286 -8055 O HETATM 1963 C3 GOL A 304 -3.841 -15.619 3.523 1.00 33.24 C ANISOU 1963 C3 GOL A 304 5582 3558 3487 1514 -310 -869 C HETATM 1964 O3 GOL A 304 -3.963 -15.269 4.894 1.00 15.01 O ANISOU 1964 O3 GOL A 304 1614 2212 1876 588 146 92 O HETATM 1965 O HOH A 401 -23.039 14.613 22.009 1.00 44.28 O ANISOU 1965 O HOH A 401 2451 4246 10125 175 -1020 834 O HETATM 1966 O HOH A 402 -1.093 14.277 8.956 1.00 14.68 O ANISOU 1966 O HOH A 402 2004 1763 1811 -358 -100 147 O HETATM 1967 O HOH A 403 -11.275 -13.911 -11.121 1.00 32.61 O ANISOU 1967 O HOH A 403 4444 3309 4634 -373 60 -153 O HETATM 1968 O HOH A 404 3.510 15.030 3.173 1.00 16.27 O ANISOU 1968 O HOH A 404 2209 2210 1763 -811 448 67 O HETATM 1969 O HOH A 405 -8.887 22.004 11.390 1.00 46.44 O ANISOU 1969 O HOH A 405 6623 2856 8166 -588 -3038 1020 O HETATM 1970 O HOH A 406 -5.943 16.179 8.267 1.00 33.28 O ANISOU 1970 O HOH A 406 3944 4457 4244 962 197 -477 O HETATM 1971 O HOH A 407 -10.578 -18.860 10.389 1.00 51.37 O ANISOU 1971 O HOH A 407 6236 6366 6912 1570 2817 2411 O HETATM 1972 O HOH A 408 -30.896 -5.379 11.924 1.00 38.08 O ANISOU 1972 O HOH A 408 2902 6581 4984 499 -1025 -1412 O HETATM 1973 O HOH A 409 -19.163 16.622 3.694 1.00 28.41 O ANISOU 1973 O HOH A 409 3369 3640 3785 1154 -1049 -858 O HETATM 1974 O HOH A 410 -21.966 -4.496 22.356 1.00 25.98 O ANISOU 1974 O HOH A 410 4277 2757 2835 -1402 -752 300 O HETATM 1975 O HOH A 411 -16.803 -12.225 24.174 1.00 35.19 O ANISOU 1975 O HOH A 411 4593 5739 3038 -1012 855 -652 O HETATM 1976 O HOH A 412 -17.739 17.053 11.774 1.00 40.18 O ANISOU 1976 O HOH A 412 6768 4997 3499 3661 221 192 O HETATM 1977 O HOH A 413 3.133 17.260 -0.771 1.00 26.37 O ANISOU 1977 O HOH A 413 2787 2783 4447 -611 626 -759 O HETATM 1978 O HOH A 414 -13.052 11.287 0.355 1.00 30.62 O ANISOU 1978 O HOH A 414 5342 3115 3174 1097 -726 -1398 O HETATM 1979 O HOH A 415 -18.158 -1.696 26.646 1.00 23.28 O ANISOU 1979 O HOH A 415 3921 2819 2103 -365 -279 -323 O HETATM 1980 O HOH A 416 -27.903 1.430 22.245 1.00 27.74 O ANISOU 1980 O HOH A 416 3398 3693 3448 -124 555 -1438 O HETATM 1981 O HOH A 417 -16.649 -9.035 26.974 1.00 38.05 O ANISOU 1981 O HOH A 417 4686 3944 5827 54 2548 -286 O HETATM 1982 O HOH A 418 -16.873 -20.053 6.080 1.00 24.25 O ANISOU 1982 O HOH A 418 3040 3624 2550 597 -41 -119 O HETATM 1983 O HOH A 419 9.415 7.630 -4.749 1.00 27.01 O ANISOU 1983 O HOH A 419 3162 3729 3370 -1951 -589 956 O HETATM 1984 O HOH A 420 -10.642 10.850 8.025 1.00 14.94 O ANISOU 1984 O HOH A 420 1916 1784 1975 184 -94 -109 O HETATM 1985 O HOH A 421 -13.630 -18.399 -6.156 1.00 22.05 O ANISOU 1985 O HOH A 421 3002 2342 3033 -319 942 -579 O HETATM 1986 O HOH A 422 -12.533 0.109 -11.345 1.00 24.07 O ANISOU 1986 O HOH A 422 3277 3892 1975 -603 -306 -174 O HETATM 1987 O HOH A 423 -17.479 -3.840 -8.852 1.00 19.08 O ANISOU 1987 O HOH A 423 2268 2291 2689 579 233 143 O HETATM 1988 O HOH A 424 -11.899 13.637 18.086 1.00 17.85 O ANISOU 1988 O HOH A 424 2592 2189 2002 190 -218 -373 O HETATM 1989 O HOH A 425 -14.016 1.186 -5.711 1.00 18.61 O ANISOU 1989 O HOH A 425 1714 1761 3594 34 514 147 O HETATM 1990 O HOH A 426 -12.449 -19.187 7.835 1.00 39.21 O ANISOU 1990 O HOH A 426 5696 3063 6138 -452 1888 1216 O HETATM 1991 O HOH A 427 -22.847 -6.863 23.848 1.00 40.15 O ANISOU 1991 O HOH A 427 2868 4516 7870 -951 1742 -2141 O HETATM 1992 O HOH A 428 -8.879 15.404 -1.324 1.00 40.06 O ANISOU 1992 O HOH A 428 2401 6512 6307 1328 1150 4150 O HETATM 1993 O HOH A 429 -21.385 -14.724 -7.830 1.00 14.43 O ANISOU 1993 O HOH A 429 1638 2164 1679 99 -387 -455 O HETATM 1994 O HOH A 430 -6.921 -1.598 -16.246 1.00 35.14 O ANISOU 1994 O HOH A 430 7141 3815 2392 2215 -1153 70 O HETATM 1995 O HOH A 431 1.072 5.960 4.589 1.00 9.41 O ANISOU 1995 O HOH A 431 1148 1318 1107 -65 9 -213 O HETATM 1996 O HOH A 432 -3.146 -7.477 26.376 1.00 24.77 O ANISOU 1996 O HOH A 432 4540 2491 2377 -48 -297 -7 O HETATM 1997 O HOH A 433 -24.953 -8.907 -4.990 1.00 25.60 O ANISOU 1997 O HOH A 433 2736 4112 2876 -1107 -857 1224 O HETATM 1998 O HOH A 434 2.524 -7.849 14.607 1.00 20.67 O ANISOU 1998 O HOH A 434 3545 2410 1897 -493 851 -373 O HETATM 1999 O HOH A 435 -17.405 11.335 3.806 1.00 58.76 O ANISOU 1999 O HOH A 435 7013 11251 4060 -4182 -1544 -621 O HETATM 2000 O HOH A 436 -6.082 -17.466 16.628 1.00 32.10 O ANISOU 2000 O HOH A 436 3055 3873 5265 -107 -731 -1460 O HETATM 2001 O HOH A 437 -6.940 7.341 -13.998 1.00 38.44 O ANISOU 2001 O HOH A 437 5530 5101 3975 -1409 -653 -1600 O HETATM 2002 O HOH A 438 0.252 -14.018 13.937 1.00 21.83 O ANISOU 2002 O HOH A 438 2696 2558 3039 424 -510 -553 O HETATM 2003 O HOH A 439 -24.846 -2.463 22.503 1.00 28.45 O ANISOU 2003 O HOH A 439 4017 4095 2698 -851 923 346 O HETATM 2004 O HOH A 440 -3.947 12.583 18.249 1.00 16.66 O ANISOU 2004 O HOH A 440 2282 2126 1921 145 455 -51 O HETATM 2005 O HOH A 441 -30.068 1.294 19.590 1.00 36.99 O ANISOU 2005 O HOH A 441 3350 5689 5013 1271 1220 231 O HETATM 2006 O HOH A 442 0.168 9.146 5.364 1.00 10.53 O ANISOU 2006 O HOH A 442 1518 1232 1249 -345 -47 -209 O HETATM 2007 O HOH A 443 -10.993 13.714 6.480 1.00 14.68 O ANISOU 2007 O HOH A 443 1699 1875 2002 511 -94 -207 O HETATM 2008 O HOH A 444 -9.612 12.468 24.055 1.00 30.13 O ANISOU 2008 O HOH A 444 5015 3542 2889 469 588 -805 O HETATM 2009 O HOH A 445 -17.059 -10.714 -7.319 1.00 15.91 O ANISOU 2009 O HOH A 445 1168 2096 2781 -150 -22 -266 O HETATM 2010 O HOH A 446 4.421 7.893 -9.727 1.00 27.43 O ANISOU 2010 O HOH A 446 3341 3429 3651 56 1108 1089 O HETATM 2011 O HOH A 447 -4.378 14.030 7.585 1.00 17.50 O ANISOU 2011 O HOH A 447 2367 2186 2093 -263 47 -108 O HETATM 2012 O HOH A 448 1.362 10.347 8.483 1.00 10.05 O ANISOU 2012 O HOH A 448 1469 1285 1061 -377 -46 33 O HETATM 2013 O HOH A 449 7.911 5.530 3.454 1.00 13.21 O ANISOU 2013 O HOH A 449 1520 2119 1379 -619 239 -240 O HETATM 2014 O HOH A 450 -9.720 14.731 21.034 1.00 37.96 O ANISOU 2014 O HOH A 450 6146 2255 6021 78 -1092 -814 O HETATM 2015 O HOH A 451 -6.698 -13.444 -11.582 1.00 38.79 O ANISOU 2015 O HOH A 451 5919 4774 4043 -682 881 -1961 O HETATM 2016 O HOH A 452 -13.213 -2.347 7.002 1.00 7.57 O ANISOU 2016 O HOH A 452 837 1052 984 45 37 -92 O HETATM 2017 O HOH A 453 -29.263 -12.852 13.769 1.00 42.55 O ANISOU 2017 O HOH A 453 5959 7104 3101 -3772 -554 -1014 O HETATM 2018 O HOH A 454 -3.653 -11.548 20.151 1.00 14.42 O ANISOU 2018 O HOH A 454 2476 1792 1210 -264 -139 33 O HETATM 2019 O HOH A 455 -23.580 4.238 10.427 1.00 14.60 O ANISOU 2019 O HOH A 455 2088 1879 1578 369 416 40 O HETATM 2020 O HOH A 456 7.614 -2.463 -5.430 1.00 26.04 O ANISOU 2020 O HOH A 456 3768 3357 2768 13 461 -237 O HETATM 2021 O HOH A 457 -9.306 17.267 5.891 1.00 19.75 O ANISOU 2021 O HOH A 457 2834 2287 2381 -237 -38 -226 O HETATM 2022 O HOH A 458 -15.556 16.531 17.083 1.00 40.18 O ANISOU 2022 O HOH A 458 4675 6448 4141 737 1336 -879 O HETATM 2023 O HOH A 459 10.583 0.036 2.360 1.00 33.56 O ANISOU 2023 O HOH A 459 2425 3581 6743 554 904 196 O HETATM 2024 O HOH A 460 9.865 1.296 5.535 1.00 23.96 O ANISOU 2024 O HOH A 460 3429 2983 2691 838 -1257 -1016 O HETATM 2025 O HOH A 461 -20.507 -19.653 -0.534 1.00 11.10 O ANISOU 2025 O HOH A 461 1543 1197 1476 70 -94 -193 O HETATM 2026 O HOH A 462 4.187 6.174 -14.278 1.00 38.77 O ANISOU 2026 O HOH A 462 5363 3334 6031 -166 1676 580 O HETATM 2027 O HOH A 463 4.887 11.707 13.534 1.00 22.56 O ANISOU 2027 O HOH A 463 1925 4293 2355 -663 98 -385 O HETATM 2028 O HOH A 464 -0.574 -11.456 13.711 1.00 11.01 O ANISOU 2028 O HOH A 464 1248 1744 1190 16 13 -71 O HETATM 2029 O HOH A 465 -14.370 -6.630 26.563 1.00 26.54 O ANISOU 2029 O HOH A 465 3760 3300 3023 304 69 200 O HETATM 2030 O HOH A 466 -10.765 -7.633 25.705 1.00 29.15 O ANISOU 2030 O HOH A 466 3235 5533 2308 701 905 136 O HETATM 2031 O HOH A 467 -10.724 -3.879 26.031 1.00 23.23 O ANISOU 2031 O HOH A 467 2547 3192 3087 -557 -1222 -372 O HETATM 2032 O HOH A 468 -19.830 -11.046 -10.679 1.00 40.11 O ANISOU 2032 O HOH A 468 3082 6492 5664 -1055 1361 -1623 O HETATM 2033 O HOH A 469 1.939 -1.342 13.537 1.00 16.31 O ANISOU 2033 O HOH A 469 1719 2908 1570 -220 -327 -105 O HETATM 2034 O HOH A 470 8.372 -1.193 -15.398 1.00 41.30 O ANISOU 2034 O HOH A 470 6206 3760 5723 2323 3646 995 O HETATM 2035 O HOH A 471 3.296 -3.987 6.656 1.00 9.99 O ANISOU 2035 O HOH A 471 1277 1263 1253 313 -31 158 O HETATM 2036 O HOH A 472 -11.229 9.900 17.248 1.00 15.51 O ANISOU 2036 O HOH A 472 1761 1741 2388 140 -244 38 O HETATM 2037 O HOH A 473 6.922 6.900 15.913 1.00 31.60 O ANISOU 2037 O HOH A 473 2642 4696 4667 928 -1525 -2189 O HETATM 2038 O HOH A 474 -9.961 -4.840 -12.211 1.00 12.04 O ANISOU 2038 O HOH A 474 1880 1754 941 -311 109 140 O HETATM 2039 O HOH A 475 -4.458 18.441 -2.402 1.00 15.88 O ANISOU 2039 O HOH A 475 2159 1576 2299 -16 378 394 O HETATM 2040 O HOH A 476 -11.723 -8.133 -13.865 1.00 18.31 O ANISOU 2040 O HOH A 476 3322 2156 1478 155 33 151 O HETATM 2041 O HOH A 477 3.552 7.367 4.981 1.00 11.13 O ANISOU 2041 O HOH A 477 1392 1318 1517 -222 87 -218 O HETATM 2042 O HOH A 478 -15.460 -18.824 8.223 1.00 26.58 O ANISOU 2042 O HOH A 478 4056 2967 3076 8 -267 -512 O HETATM 2043 O HOH A 479 -1.007 0.589 -13.257 1.00 19.88 O ANISOU 2043 O HOH A 479 2212 2943 2399 -585 202 -53 O HETATM 2044 O HOH A 480 -9.127 5.364 25.508 1.00 27.73 O ANISOU 2044 O HOH A 480 5339 3134 2063 -216 659 169 O HETATM 2045 O HOH A 481 8.144 12.609 7.220 1.00 32.80 O ANISOU 2045 O HOH A 481 3430 5589 3444 -864 3 371 O HETATM 2046 O HOH A 482 1.829 10.988 -3.805 1.00 16.47 O ANISOU 2046 O HOH A 482 1754 2442 2061 -211 -127 -779 O HETATM 2047 O HOH A 483 -16.858 -9.061 -5.102 1.00 13.17 O ANISOU 2047 O HOH A 483 1023 2267 1712 -59 297 -194 O HETATM 2048 O HOH A 484 -19.450 -17.114 18.571 1.00 46.55 O ANISOU 2048 O HOH A 484 6908 4221 6556 1288 376 2073 O HETATM 2049 O HOH A 485 -18.375 6.721 22.660 1.00 13.10 O ANISOU 2049 O HOH A 485 2036 1711 1229 36 273 -31 O HETATM 2050 O HOH A 486 -22.083 -4.165 -3.307 1.00 11.18 O ANISOU 2050 O HOH A 486 1510 1299 1437 379 82 -483 O HETATM 2051 O HOH A 487 -9.785 -11.539 26.773 1.00 42.17 O ANISOU 2051 O HOH A 487 6193 7485 2344 -1544 473 429 O HETATM 2052 O HOH A 488 -4.927 -7.093 23.153 1.00 12.17 O ANISOU 2052 O HOH A 488 1712 1409 1503 0 -275 245 O HETATM 2053 O HOH A 489 -15.352 8.881 0.622 1.00 19.09 O ANISOU 2053 O HOH A 489 2572 1528 3154 650 -133 335 O HETATM 2054 O HOH A 490 -1.918 -10.473 -12.999 1.00 38.69 O ANISOU 2054 O HOH A 490 3303 2569 8829 1077 -2099 -312 O HETATM 2055 O HOH A 491 -20.698 -2.253 7.647 1.00 10.14 O ANISOU 2055 O HOH A 491 1193 1067 1590 66 -6 -237 O HETATM 2056 O HOH A 492 -17.690 -10.716 -2.587 1.00 8.75 O ANISOU 2056 O HOH A 492 1035 1082 1205 -71 83 -79 O HETATM 2057 O HOH A 493 3.215 8.672 -2.531 1.00 19.41 O ANISOU 2057 O HOH A 493 2216 3158 1999 358 -441 -916 O HETATM 2058 O HOH A 494 -11.233 4.482 -11.423 1.00 35.18 O ANISOU 2058 O HOH A 494 4493 3789 5081 -933 -2210 -88 O HETATM 2059 O HOH A 495 -8.557 -1.859 28.456 1.00 34.90 O ANISOU 2059 O HOH A 495 5880 4743 2636 499 655 808 O HETATM 2060 O HOH A 496 -10.075 7.487 -12.793 1.00 45.11 O ANISOU 2060 O HOH A 496 7769 5758 3612 -460 957 128 O HETATM 2061 O HOH A 497 -13.549 -14.755 22.419 1.00 36.71 O ANISOU 2061 O HOH A 497 3413 4905 5627 792 673 1803 O HETATM 2062 O HOH A 498 6.102 -4.580 9.983 1.00 25.46 O ANISOU 2062 O HOH A 498 2707 3727 3239 -570 -725 -627 O HETATM 2063 O HOH A 499 3.383 15.300 -6.747 1.00 18.67 O ANISOU 2063 O HOH A 499 1606 3096 2390 -424 284 799 O HETATM 2064 O HOH A 500 -18.560 -19.676 -5.725 1.00 19.13 O ANISOU 2064 O HOH A 500 2584 2028 2655 -704 -446 640 O HETATM 2065 O HOH A 501 -20.066 -8.584 13.601 1.00 13.27 O ANISOU 2065 O HOH A 501 1500 1949 1593 -278 -106 -251 O HETATM 2066 O HOH A 502 9.980 4.023 0.512 1.00 29.93 O ANISOU 2066 O HOH A 502 3171 4860 3338 1682 234 108 O HETATM 2067 O HOH A 503 8.688 2.946 -3.630 1.00 28.05 O ANISOU 2067 O HOH A 503 3513 3418 3726 -724 555 -103 O HETATM 2068 O HOH A 504 -22.978 0.596 0.220 1.00 19.85 O ANISOU 2068 O HOH A 504 2530 2453 2558 104 61 -31 O HETATM 2069 O HOH A 505 -16.138 -7.176 -10.803 1.00 40.57 O ANISOU 2069 O HOH A 505 3335 7409 4670 384 -819 -1608 O HETATM 2070 O HOH A 506 -0.066 0.993 21.141 1.00 28.16 O ANISOU 2070 O HOH A 506 3509 3998 3192 -701 464 -678 O HETATM 2071 O HOH A 507 -1.348 10.833 -11.479 1.00 32.70 O ANISOU 2071 O HOH A 507 4873 4362 3188 234 508 2161 O HETATM 2072 O HOH A 508 -13.502 0.461 -14.839 1.00 16.29 O ANISOU 2072 O HOH A 508 1571 3664 955 445 -271 31 O HETATM 2073 O HOH A 509 -16.618 -19.722 -3.776 1.00 20.04 O ANISOU 2073 O HOH A 509 2823 2034 2757 -635 -84 -250 O HETATM 2074 O HOH A 510 8.770 -4.608 1.364 1.00 18.11 O ANISOU 2074 O HOH A 510 2655 2345 1878 1094 313 -104 O HETATM 2075 O HOH A 511 -15.022 18.663 9.255 1.00 28.38 O ANISOU 2075 O HOH A 511 2707 3629 4446 829 -707 -1690 O HETATM 2076 O HOH A 512 8.623 0.262 -1.329 1.00 21.91 O ANISOU 2076 O HOH A 512 2310 2859 3154 -539 1243 -211 O HETATM 2077 O HOH A 513 -5.773 -15.687 -4.734 1.00 36.25 O ANISOU 2077 O HOH A 513 3493 5193 5086 719 -691 1425 O HETATM 2078 O HOH A 514 -21.354 -5.871 13.352 1.00 9.84 O ANISOU 2078 O HOH A 514 1192 1359 1185 -155 252 -106 O HETATM 2079 O HOH A 515 9.799 -2.184 -2.448 1.00 29.73 O ANISOU 2079 O HOH A 515 3749 3173 4371 393 1591 265 O HETATM 2080 O HOH A 516 -17.058 12.488 6.603 1.00 14.85 O ANISOU 2080 O HOH A 516 1753 1871 2015 70 -114 211 O HETATM 2081 O HOH A 517 -16.268 12.013 17.682 1.00 27.75 O ANISOU 2081 O HOH A 517 4895 2272 3374 632 1317 112 O HETATM 2082 O HOH A 518 -25.884 -7.418 16.736 1.00 14.08 O ANISOU 2082 O HOH A 518 1425 1959 1964 -1 313 -212 O HETATM 2083 O HOH A 519 4.522 -4.995 4.258 1.00 19.46 O ANISOU 2083 O HOH A 519 2302 2446 2646 1 184 -343 O HETATM 2084 O HOH A 520 8.591 5.711 12.364 1.00 23.22 O ANISOU 2084 O HOH A 520 2348 2891 3583 -594 -336 -370 O HETATM 2085 O HOH A 521 -5.399 20.500 0.674 1.00 39.46 O ANISOU 2085 O HOH A 521 6843 3316 4833 -116 886 586 O HETATM 2086 O HOH A 522 5.628 9.966 15.749 1.00 11.98 O ANISOU 2086 O HOH A 522 1177 1749 1625 -384 185 -576 O HETATM 2087 O HOH A 523 -3.571 15.323 22.137 1.00 36.40 O ANISOU 2087 O HOH A 523 4139 3227 6462 -1065 -1915 112 O HETATM 2088 O HOH A 524 -24.887 -5.054 19.938 1.00 28.69 O ANISOU 2088 O HOH A 524 3297 3614 3989 -437 825 -814 O HETATM 2089 O HOH A 525 -15.424 10.490 2.911 1.00 22.31 O ANISOU 2089 O HOH A 525 3850 2435 2191 662 -453 -182 O HETATM 2090 O HOH A 526 4.182 15.744 7.839 1.00 34.69 O ANISOU 2090 O HOH A 526 4210 4007 4961 895 -1293 -1045 O HETATM 2091 O HOH A 527 -23.889 -1.712 1.343 1.00 23.58 O ANISOU 2091 O HOH A 527 2310 3524 3123 147 -1319 451 O HETATM 2092 O HOH A 528 2.958 1.063 14.630 1.00 29.37 O ANISOU 2092 O HOH A 528 2637 4416 4104 -18 -247 1771 O HETATM 2093 O HOH A 529 -25.240 5.921 15.118 1.00 27.46 O ANISOU 2093 O HOH A 529 4254 3206 2970 -24 91 -330 O HETATM 2094 O HOH A 530 -2.216 -14.711 -1.656 1.00 31.97 O ANISOU 2094 O HOH A 530 3820 3235 5091 1377 -729 425 O HETATM 2095 O HOH A 531 -10.896 -18.041 -5.664 1.00 28.44 O ANISOU 2095 O HOH A 531 3774 3298 3731 -774 -361 700 O HETATM 2096 O HOH A 532 -10.417 -10.212 3.386 1.00 19.82 O ANISOU 2096 O HOH A 532 2437 2758 2333 91 -120 43 O HETATM 2097 O HOH A 533 -9.164 14.583 -4.752 1.00 22.67 O ANISOU 2097 O HOH A 533 2276 2849 3487 742 -42 90 O HETATM 2098 O HOH A 534 -18.690 -17.399 14.647 1.00 50.97 O ANISOU 2098 O HOH A 534 6566 8900 3898 -5205 -179 1778 O HETATM 2099 O HOH A 535 -27.354 4.021 12.955 1.00 38.37 O ANISOU 2099 O HOH A 535 5112 3883 5583 339 -396 -1095 O HETATM 2100 O HOH A 536 -10.551 3.492 -13.892 1.00 34.20 O ANISOU 2100 O HOH A 536 5479 3779 3735 -1128 -2029 1298 O HETATM 2101 O HOH A 537 -25.622 -9.302 19.097 1.00 18.82 O ANISOU 2101 O HOH A 537 1844 3113 2192 -201 216 57 O HETATM 2102 O HOH A 538 -19.191 -2.411 -7.323 1.00 14.46 O ANISOU 2102 O HOH A 538 2099 1738 1655 137 -267 53 O HETATM 2103 O HOH A 539 -28.452 -3.461 5.969 1.00 49.38 O ANISOU 2103 O HOH A 539 6171 7217 5372 -3288 1768 -1042 O HETATM 2104 O HOH A 540 3.894 -11.554 15.847 1.00 38.56 O ANISOU 2104 O HOH A 540 5484 6614 2553 2413 851 847 O HETATM 2105 O HOH A 541 10.805 10.445 4.410 1.00 51.48 O ANISOU 2105 O HOH A 541 4315 7363 7879 -765 2155 1769 O HETATM 2106 O HOH A 542 7.963 7.851 -9.321 1.00 33.61 O ANISOU 2106 O HOH A 542 3969 2914 5887 -963 262 496 O HETATM 2107 O HOH A 543 -14.171 -19.781 -0.670 1.00 12.77 O ANISOU 2107 O HOH A 543 1348 1395 2106 -150 43 -187 O HETATM 2108 O HOH A 544 -20.324 7.042 0.475 1.00 20.66 O ANISOU 2108 O HOH A 544 1551 3151 3145 -230 404 330 O HETATM 2109 O HOH A 545 -12.871 -19.616 -3.003 1.00 31.49 O ANISOU 2109 O HOH A 545 4613 4178 3171 -1174 674 -482 O HETATM 2110 O HOH A 546 -12.522 -2.626 -10.792 1.00 15.74 O ANISOU 2110 O HOH A 546 1979 2489 1512 -220 63 442 O HETATM 2111 O HOH A 547 0.721 -0.233 -15.495 1.00 29.22 O ANISOU 2111 O HOH A 547 3567 4139 3395 -1111 -51 -1005 O HETATM 2112 O HOH A 548 -8.898 9.490 -11.275 1.00 26.33 O ANISOU 2112 O HOH A 548 4249 2786 2969 -311 -1645 782 O HETATM 2113 O HOH A 549 -7.525 -19.493 -0.313 1.00 39.33 O ANISOU 2113 O HOH A 549 3108 2667 9166 -76 348 199 O HETATM 2114 O HOH A 550 -6.436 -17.609 13.448 1.00 41.79 O ANISOU 2114 O HOH A 550 6727 4060 5090 -1116 -1662 69 O HETATM 2115 O HOH A 551 -19.317 10.313 26.103 1.00 34.62 O ANISOU 2115 O HOH A 551 7377 4097 1680 1815 259 -101 O HETATM 2116 O HOH A 552 0.889 21.194 10.244 1.00 27.09 O ANISOU 2116 O HOH A 552 4609 2997 2686 -735 -299 -134 O HETATM 2117 O HOH A 553 -13.111 -19.587 5.314 1.00 14.18 O ANISOU 2117 O HOH A 553 1429 1533 2423 -382 371 236 O HETATM 2118 O HOH A 554 -31.935 0.634 17.962 1.00 49.08 O ANISOU 2118 O HOH A 554 6075 7426 5144 -169 1132 -1820 O HETATM 2119 O HOH A 555 -8.002 -14.719 -10.200 1.00 31.40 O ANISOU 2119 O HOH A 555 3753 4350 3825 -139 361 -1774 O HETATM 2120 O HOH A 556 -25.847 4.639 8.545 1.00 20.93 O ANISOU 2120 O HOH A 556 2002 3477 2471 125 328 775 O HETATM 2121 O HOH A 557 -11.155 20.489 15.084 1.00 21.71 O ANISOU 2121 O HOH A 557 2688 2294 3266 492 -428 -1140 O HETATM 2122 O HOH A 558 -0.200 -4.436 18.283 1.00 18.86 O ANISOU 2122 O HOH A 558 2383 2489 2291 1025 813 1086 O HETATM 2123 O HOH A 559 -5.477 1.446 25.849 1.00 22.99 O ANISOU 2123 O HOH A 559 2580 2734 3418 9 476 -275 O HETATM 2124 O HOH A 560 8.745 13.072 13.958 1.00 27.56 O ANISOU 2124 O HOH A 560 2496 4212 3762 -291 245 -840 O HETATM 2125 O HOH A 561 -25.380 -15.907 15.653 1.00 19.01 O ANISOU 2125 O HOH A 561 2385 2302 2536 -281 -120 661 O HETATM 2126 O HOH A 562 -5.978 -17.966 3.743 1.00 37.48 O ANISOU 2126 O HOH A 562 2642 4722 6876 246 404 -886 O HETATM 2127 O HOH A 563 -10.050 -11.676 -12.718 1.00 26.43 O ANISOU 2127 O HOH A 563 5235 2719 2088 482 590 -438 O HETATM 2128 O HOH A 564 -25.150 2.363 5.360 1.00 36.24 O ANISOU 2128 O HOH A 564 4679 3089 5999 -236 -854 694 O HETATM 2129 O HOH A 565 -15.402 18.844 15.186 1.00 36.97 O ANISOU 2129 O HOH A 565 6172 3282 4592 1029 452 -1524 O HETATM 2130 O HOH A 566 -21.138 11.962 9.383 1.00 22.76 O ANISOU 2130 O HOH A 566 2137 2787 3723 383 -503 -302 O HETATM 2131 O HOH A 567 -14.329 -20.217 17.541 1.00 45.86 O ANISOU 2131 O HOH A 567 9652 4311 3461 -3657 -258 753 O HETATM 2132 O HOH A 568 9.910 1.560 -7.486 1.00 36.93 O ANISOU 2132 O HOH A 568 3980 4887 5162 -814 94 -490 O HETATM 2133 O HOH A 569 -2.541 13.540 6.038 1.00 19.32 O ANISOU 2133 O HOH A 569 5017 1089 1232 -645 -797 -16 O HETATM 2134 O HOH A 570 -30.314 -2.420 20.446 1.00 51.56 O ANISOU 2134 O HOH A 570 6524 7531 5532 -2109 3218 -2303 O HETATM 2135 O HOH A 571 -10.541 8.411 26.081 1.00 23.96 O ANISOU 2135 O HOH A 571 2337 4020 2744 -140 257 -560 O HETATM 2136 O HOH A 572 9.694 8.933 0.406 1.00 20.18 O ANISOU 2136 O HOH A 572 1951 2494 3220 -582 -402 226 O HETATM 2137 O HOH A 573 9.799 11.799 1.249 1.00 42.85 O ANISOU 2137 O HOH A 573 4033 4180 8066 144 -1659 -98 O HETATM 2138 O HOH A 574 -5.402 -19.510 7.093 1.00 33.54 O ANISOU 2138 O HOH A 574 3459 2013 7272 -450 146 38 O HETATM 2139 O HOH A 575 0.789 -6.025 -12.000 1.00 16.63 O ANISOU 2139 O HOH A 575 1838 2445 2036 -166 114 96 O HETATM 2140 O HOH A 576 -25.647 2.389 3.020 1.00 41.01 O ANISOU 2140 O HOH A 576 3012 5606 6964 402 279 -1355 O HETATM 2141 O HOH A 577 -27.845 5.948 6.021 1.00 47.09 O ANISOU 2141 O HOH A 577 7118 7536 3235 185 -1073 1660 O HETATM 2142 O HOH A 578 -13.370 5.232 27.975 1.00 17.82 O ANISOU 2142 O HOH A 578 3026 2845 897 -1108 202 90 O HETATM 2143 O HOH A 579 -11.350 19.156 3.069 1.00 49.79 O ANISOU 2143 O HOH A 579 5618 3984 9314 112 -1884 1478 O HETATM 2144 O HOH A 580 -8.664 -18.199 -3.358 1.00 53.70 O ANISOU 2144 O HOH A 580 8083 7614 4704 3708 -654 -2185 O HETATM 2145 O HOH A 581 -20.439 10.592 12.297 1.00 15.74 O ANISOU 2145 O HOH A 581 1471 2391 2119 271 -138 -497 O HETATM 2146 O HOH A 582 -21.118 -6.871 26.639 1.00 30.15 O ANISOU 2146 O HOH A 582 3902 4011 3541 -757 564 -926 O HETATM 2147 O HOH A 583 -5.296 20.201 9.361 1.00 44.93 O ANISOU 2147 O HOH A 583 3848 7327 5894 -1370 -1064 -1356 O HETATM 2148 O HOH A 584 -15.197 5.841 -4.774 1.00 41.43 O ANISOU 2148 O HOH A 584 2790 3415 9534 -525 -601 1380 O HETATM 2149 O HOH A 585 -10.772 8.985 -7.988 1.00 41.85 O ANISOU 2149 O HOH A 585 4748 3944 7206 702 1755 1278 O HETATM 2150 O HOH A 586 -2.516 -5.019 -14.265 1.00 23.06 O ANISOU 2150 O HOH A 586 2270 4095 2395 164 -372 1026 O HETATM 2151 O HOH A 587 -28.738 -6.208 9.722 1.00 6.85 O ANISOU 2151 O HOH A 587 229 1138 1235 -233 249 -78 O HETATM 2152 O HOH A 588 -4.842 -1.170 28.266 1.00 31.44 O ANISOU 2152 O HOH A 588 4084 5448 2414 634 -1481 508 O HETATM 2153 O HOH A 589 -9.989 -17.878 13.569 1.00 42.41 O ANISOU 2153 O HOH A 589 8372 3503 4238 -1051 824 358 O HETATM 2154 O HOH A 590 11.612 4.529 -15.076 1.00 42.10 O ANISOU 2154 O HOH A 590 4820 8006 3168 -1387 273 -247 O HETATM 2155 O HOH A 591 0.625 11.523 -9.617 1.00 33.70 O ANISOU 2155 O HOH A 591 4283 2813 5706 1068 1753 229 O HETATM 2156 O HOH A 592 -19.292 5.987 -2.203 1.00 34.53 O ANISOU 2156 O HOH A 592 5994 4205 2920 554 446 522 O HETATM 2157 O HOH A 593 -14.229 17.771 2.646 1.00 21.37 O ANISOU 2157 O HOH A 593 2733 2419 2968 1123 581 543 O HETATM 2158 O HOH A 594 -22.033 -3.025 -7.594 1.00 37.76 O ANISOU 2158 O HOH A 594 4260 3719 6364 -390 -2174 -545 O HETATM 2159 O HOH A 595 6.439 -12.012 9.125 1.00 11.41 O ANISOU 2159 O HOH A 595 961 2005 1369 -191 82 -290 O HETATM 2160 O HOH A 596 -8.897 18.998 17.500 1.00 28.16 O ANISOU 2160 O HOH A 596 4510 3817 2371 -88 150 -644 O HETATM 2161 O HOH A 597 10.026 7.077 4.103 1.00 36.03 O ANISOU 2161 O HOH A 597 3585 5121 4981 -1650 325 -1851 O HETATM 2162 O HOH A 598 6.020 -0.815 -17.601 1.00 40.19 O ANISOU 2162 O HOH A 598 4774 6623 3873 1259 1324 2278 O HETATM 2163 O HOH A 599 4.080 13.484 -4.379 1.00 25.49 O ANISOU 2163 O HOH A 599 2613 3753 3316 380 7 913 O HETATM 2164 O HOH A 600 -21.490 -0.115 26.369 1.00 36.64 O ANISOU 2164 O HOH A 600 5476 5250 3194 73 1310 -336 O HETATM 2165 O HOH A 601 -18.373 16.078 7.907 1.00 44.58 O ANISOU 2165 O HOH A 601 5505 6624 4810 -1747 -1874 550 O HETATM 2166 O HOH A 602 -1.703 1.487 26.830 1.00 50.04 O ANISOU 2166 O HOH A 602 7261 6579 5172 -3215 -1771 1663 O HETATM 2167 O HOH A 603 0.898 6.605 -15.369 1.00 50.68 O ANISOU 2167 O HOH A 603 4791 9539 4925 920 885 2681 O HETATM 2168 O HOH A 604 6.329 14.094 4.067 1.00 35.18 O ANISOU 2168 O HOH A 604 4529 4207 4629 -730 641 72 O HETATM 2169 O HOH A 605 5.081 10.320 -7.936 1.00 40.98 O ANISOU 2169 O HOH A 605 4581 4557 6429 -2106 743 -470 O HETATM 2170 O HOH A 606 -0.152 -8.407 26.547 1.00 27.80 O ANISOU 2170 O HOH A 606 3750 2285 4526 -271 423 -96 O HETATM 2171 O HOH A 607 -8.195 -13.290 25.791 1.00 51.21 O ANISOU 2171 O HOH A 607 4793 12192 2471 3376 -660 162 O HETATM 2172 O HOH A 608 -19.662 12.605 14.276 1.00 37.27 O ANISOU 2172 O HOH A 608 6565 3951 3644 564 1060 -1160 O HETATM 2173 O HOH A 609 -27.180 1.371 9.094 1.00 23.55 O ANISOU 2173 O HOH A 609 2002 2148 4797 -795 1468 -1011 O HETATM 2174 O HOH A 610 -3.170 -1.810 -13.735 1.00 28.02 O ANISOU 2174 O HOH A 610 1709 5486 3448 -1503 163 1318 O HETATM 2175 O HOH A 611 -13.976 13.060 20.691 1.00 44.47 O ANISOU 2175 O HOH A 611 7740 3754 5402 -1144 806 787 O HETATM 2176 O HOH A 612 -3.684 15.910 -9.597 1.00 40.50 O ANISOU 2176 O HOH A 612 3462 5437 6489 -796 1041 1774 O HETATM 2177 O HOH A 613 -6.819 18.145 5.710 1.00 35.46 O ANISOU 2177 O HOH A 613 4131 4635 4705 -850 1596 -2170 O HETATM 2178 O HOH A 614 -29.036 6.102 22.813 1.00 41.53 O ANISOU 2178 O HOH A 614 3482 7908 4387 -309 33 -868 O HETATM 2179 O HOH A 615 -10.472 -14.356 25.637 1.00 34.41 O ANISOU 2179 O HOH A 615 6435 3342 3295 -1025 -161 1208 O HETATM 2180 O HOH A 616 -22.591 -4.280 25.966 1.00 33.63 O ANISOU 2180 O HOH A 616 3795 5826 3156 -210 465 354 O HETATM 2181 O HOH A 617 -24.923 -12.445 3.961 1.00 56.20 O ANISOU 2181 O HOH A 617 3753 12452 5147 -1939 2199 -4685 O HETATM 2182 O HOH A 618 0.608 -4.714 22.992 1.00 42.60 O ANISOU 2182 O HOH A 618 4207 4479 7501 1145 -511 -843 O HETATM 2183 O HOH A 619 -14.971 -9.651 -10.983 1.00 39.56 O ANISOU 2183 O HOH A 619 5638 4629 4762 114 -1027 132 O HETATM 2184 O HOH A 620 -19.898 13.122 7.039 1.00 36.06 O ANISOU 2184 O HOH A 620 4707 3617 5377 977 -797 -24 O HETATM 2185 O HOH A 621 -4.389 15.137 19.483 1.00 35.38 O ANISOU 2185 O HOH A 621 6785 2956 3701 1530 1324 56 O HETATM 2186 O HOH A 622 -15.625 0.746 -7.764 1.00 28.34 O ANISOU 2186 O HOH A 622 3917 2862 3989 -23 -471 396 O HETATM 2187 O HOH A 623 -22.004 -2.514 26.767 1.00 40.07 O ANISOU 2187 O HOH A 623 4833 7687 2705 -1503 -127 -930 O HETATM 2188 O HOH A 624 -9.767 22.891 13.502 1.00 41.63 O ANISOU 2188 O HOH A 624 4613 3251 7953 96 -1260 -1909 O HETATM 2189 O HOH A 625 -5.816 -7.287 25.855 1.00 39.42 O ANISOU 2189 O HOH A 625 4665 5256 5055 1631 -500 1716 O HETATM 2190 O HOH A 626 -18.628 0.577 -7.643 1.00 26.00 O ANISOU 2190 O HOH A 626 3307 3572 2997 -1115 512 -299 O HETATM 2191 O HOH A 627 -11.002 12.705 -1.868 1.00 35.39 O ANISOU 2191 O HOH A 627 5004 4175 4264 769 -553 291 O HETATM 2192 O HOH A 628 -20.546 -10.089 -12.819 1.00 53.98 O ANISOU 2192 O HOH A 628 7831 6834 5845 -4278 -1424 550 O HETATM 2193 O HOH A 629 -1.753 1.767 -15.461 1.00 36.68 O ANISOU 2193 O HOH A 629 4879 5150 3905 -1250 122 -1317 O HETATM 2194 O HOH A 630 -25.832 -10.016 3.405 1.00 54.53 O ANISOU 2194 O HOH A 630 7383 6747 6589 538 1402 743 O HETATM 2195 O HOH A 631 -16.883 7.016 -3.028 1.00 35.31 O ANISOU 2195 O HOH A 631 3349 6091 3977 1130 -43 1992 O HETATM 2196 O HOH A 632 5.947 14.183 13.171 1.00 37.78 O ANISOU 2196 O HOH A 632 2744 4374 7235 -382 -1258 -855 O HETATM 2197 O HOH A 633 -27.594 11.323 11.151 1.00 54.07 O ANISOU 2197 O HOH A 633 8082 9183 3278 3112 -458 1776 O HETATM 2198 O HOH A 634 -26.112 3.250 11.142 1.00 37.05 O ANISOU 2198 O HOH A 634 3809 3707 6558 -365 -470 -325 O HETATM 2199 O HOH A 635 -5.709 -17.953 11.072 1.00 55.75 O ANISOU 2199 O HOH A 635 10092 4369 6721 -2051 -1768 2195 O HETATM 2200 O HOH A 636 -26.274 -5.864 4.742 1.00 21.54 O ANISOU 2200 O HOH A 636 1468 3774 2940 -226 -335 646 O HETATM 2201 O HOH A 637 9.656 7.343 14.677 1.00 37.95 O ANISOU 2201 O HOH A 637 4908 5159 4351 159 1224 280 O HETATM 2202 O HOH A 638 -8.091 9.819 25.160 1.00 40.72 O ANISOU 2202 O HOH A 638 5950 5659 3859 291 -1996 -213 O HETATM 2203 O HOH A 639 -11.236 2.921 27.268 1.00 76.81 O ANISOU 2203 O HOH A 639 5748 18123 5311 -1598 2926 -1663 O HETATM 2204 O HOH A 640 -15.569 -14.547 24.036 1.00 41.03 O ANISOU 2204 O HOH A 640 6876 5328 3386 -423 490 878 O HETATM 2205 O HOH A 641 2.123 -2.989 17.908 1.00 42.69 O ANISOU 2205 O HOH A 641 4199 6251 5767 -2474 -1520 2147 O HETATM 2206 O HOH A 642 -13.746 -3.701 -12.924 1.00 38.05 O ANISOU 2206 O HOH A 642 5939 4616 3902 217 -241 -2231 O HETATM 2207 O HOH A 643 1.528 -0.777 19.407 1.00 46.47 O ANISOU 2207 O HOH A 643 4127 6278 7251 231 -1355 1997 O HETATM 2208 O HOH A 644 -12.351 9.627 -6.077 1.00 58.73 O ANISOU 2208 O HOH A 644 8736 7041 6537 474 -495 3616 O CONECT 1262 1536 CONECT 1536 1262 CONECT 1799 1924 CONECT 1924 1799 CONECT 1933 1946 1947 CONECT 1934 1942 1948 CONECT 1935 1936 CONECT 1936 1935 1937 CONECT 1937 1936 1938 1939 CONECT 1938 1937 CONECT 1939 1937 1940 1948 CONECT 1940 1939 1941 CONECT 1941 1940 1942 CONECT 1942 1934 1941 1943 CONECT 1943 1942 1944 1945 CONECT 1944 1943 CONECT 1945 1943 1946 CONECT 1946 1933 1945 CONECT 1947 1933 CONECT 1948 1934 1939 CONECT 1949 1950 1951 1952 1953 CONECT 1950 1949 CONECT 1951 1949 CONECT 1952 1949 CONECT 1953 1949 CONECT 1954 1955 1956 1957 1958 CONECT 1955 1954 CONECT 1956 1954 CONECT 1957 1954 CONECT 1958 1954 CONECT 1959 1960 1961 CONECT 1960 1959 CONECT 1961 1959 1962 1963 CONECT 1962 1961 CONECT 1963 1961 1964 CONECT 1964 1963 MASTER 313 0 4 10 9 0 8 6 2187 1 36 21 END If you find results from this site helpful for your research, please cite one of our papers:
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