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*** HYDROLASE 05-OCT-21 7PW1 ***elNémo ID: 2402100940482257236Job options:ID = 2402100940482257236 JOBID = HYDROLASE 05-OCT-21 7PW1 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 05-OCT-21 7PW1 TITLE CRYSTAL STRUCTURE OF ANCESTRAL HALOALKANE DEHALOGENASE ANCLINB-DMBA COMPND MOL_ID: 1; COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE; COMPND 3 CHAIN: A; COMPND 4 EC: 3.8.1.5; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 3 ORGANISM_TAXID: 32630; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008 KEYWDS ANCESTRAL ENZYME, BALBES, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR A.MAZUR,P.GRINKEVICH,T.PRUDNIKOVA REVDAT 3 31-JAN-24 7PW1 1 REMARK REVDAT 2 13-APR-22 7PW1 1 JRNL REVDAT 1 06-APR-22 7PW1 0 JRNL AUTH A.MAZUR,P.GRINKEVICH,R.CHALOUPKOVA,P.HAVLICKOVA,B.KASCAKOVA, JRNL AUTH 2 M.KUTY,J.DAMBORSKY,I.KUTA SMATANOVA,T.PRUDNIKOVA JRNL TITL STRUCTURAL ANALYSIS OF THE ANCESTRAL HALOALKANE DEHALOGENASE JRNL TITL 2 ANCLINB-DMBA. JRNL REF INT J MOL SCI V. 22 2021 JRNL REFN ESSN 1422-0067 JRNL PMID 34769421 JRNL DOI 10.3390/IJMS222111992 REMARK 2 REMARK 2 RESOLUTION. 1.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0189 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.04 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 58297 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) : 0.140 REMARK 3 R VALUE (WORKING SET) : 0.138 REMARK 3 FREE R VALUE : 0.174 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 3064 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54 REMARK 3 REFLECTION IN BIN (WORKING SET) : 4064 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.86 REMARK 3 BIN R VALUE (WORKING SET) : 0.2290 REMARK 3 BIN FREE R VALUE SET COUNT : 215 REMARK 3 BIN FREE R VALUE : 0.2540 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2331 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 9 REMARK 3 SOLVENT ATOMS : 317 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.27 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.10000 REMARK 3 B22 (A**2) : 0.10000 REMARK 3 B33 (A**2) : -0.19000 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): 0.061 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.058 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.041 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.495 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.978 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.966 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2509 ; 0.046 ; 0.019 REMARK 3 BOND LENGTHS OTHERS (A): 2274 ; 0.006 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3418 ; 2.968 ; 1.951 REMARK 3 BOND ANGLES OTHERS (DEGREES): 5268 ; 1.357 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 314 ; 6.784 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 131 ;34.622 ;23.435 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 406 ;12.107 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;17.662 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 350 ; 0.205 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2877 ; 0.016 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 552 ; 0.002 ; 0.020 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): 1220 ; 1.463 ; 1.868 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1219 ; 1.459 ; 1.865 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1537 ; 1.459 ; 2.801 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1538 ; 1.460 ; 2.803 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1289 ; 2.770 ; 2.188 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1289 ; 2.770 ; 2.188 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1879 ; 2.429 ; 3.172 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3006 ; 2.228 ;24.038 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2924 ; 2.126 ;23.260 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): 4783 ; 6.979 ; 3.000 REMARK 3 SPHERICITY; FREE ATOMS (A**2): 207 ;10.499 ; 5.000 REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 4829 ; 4.045 ; 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 : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 7PW1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-OCT-21. REMARK 100 THE DEPOSITION ID IS D_1292118257. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 31-JAN-15 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 : BESSY REMARK 200 BEAMLINE : 14.1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61367 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500 REMARK 200 RESOLUTION RANGE LOW (A) : 63.040 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 10.45 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.6800 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.650 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: 2QVB REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.15 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 0.1 M SODIUM CITRATE PH REMARK 280 5.6, 0.2 M AMMONIUM ACETATE, PH 7.5, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 78.12950 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 34.44850 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.44850 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 117.19425 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.44850 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 34.44850 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 39.06475 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 34.44850 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.44850 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 117.19425 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 34.44850 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.44850 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 39.06475 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 78.12950 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: 690 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 11170 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ALA A 297 REMARK 465 ALA A 298 REMARK 465 GLY A 299 REMARK 465 VAL A 300 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 GLU A 16 CD GLU A 16 OE2 0.153 REMARK 500 ARG A 87 CZ ARG A 87 NH1 -0.139 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 PRO A 40 52.58 -101.69 REMARK 500 THR A 41 -160.44 -107.90 REMARK 500 ASP A 109 -134.84 51.72 REMARK 500 ARG A 156 47.73 -88.69 REMARK 500 ALA A 248 -65.68 -149.35 REMARK 500 ALA A 272 -99.73 -97.49 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 816 DISTANCE = 6.21 ANGSTROMS REMARK 525 HOH A 817 DISTANCE = 6.24 ANGSTROMS REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A 402 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 PHE A 35 O REMARK 620 2 GLN A 36 OE1 92.3 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A 403 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 PHE A 35 O REMARK 620 2 CYS A 62 O 115.8 REMARK 620 N 1 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A 405 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 TYR A 81 O REMARK 620 2 PRO A 204 O 140.6 REMARK 620 N 1 DBREF 7PW1 A 5 300 PDB 7PW1 7PW1 5 300 SEQRES 1 A 296 GLY ALA GLU PRO TYR GLY GLN LYS LYS PHE ILE GLU ILE SEQRES 2 A 296 ALA GLY LYS ARG MET ALA TYR ILE ASP GLU GLY GLU GLY SEQRES 3 A 296 ASP PRO ILE VAL PHE GLN HIS GLY ASN PRO THR SER SER SEQRES 4 A 296 TYR LEU TRP ARG ASN ILE MET PRO HIS LEU GLU GLY LEU SEQRES 5 A 296 GLY ARG LEU ILE ALA CYS ASP LEU ILE GLY MET GLY ASP SEQRES 6 A 296 SER ASP LYS LEU SER PRO SER GLY PRO ASP ARG TYR SER SEQRES 7 A 296 TYR ALA GLU HIS ARG ASP TYR LEU PHE ALA LEU TRP GLU SEQRES 8 A 296 ALA LEU ASP LEU GLY ASP ASN VAL VAL LEU VAL ILE HIS SEQRES 9 A 296 ASP TRP GLY SER ALA LEU GLY PHE ASP TRP ALA ASN GLN SEQRES 10 A 296 HIS ARG ASP ARG VAL GLN GLY ILE ALA TYR MET GLU ALA SEQRES 11 A 296 ILE VAL THR PRO LEU GLU TRP ALA ASP TRP PRO GLU GLU SEQRES 12 A 296 VAL ARG ASP ILE PHE GLN GLY PHE ARG SER PRO ALA GLY SEQRES 13 A 296 GLU GLU MET VAL LEU GLU ASN ASN ILE PHE VAL GLU ARG SEQRES 14 A 296 VAL LEU PRO GLY ALA ILE LEU ARG GLN LEU SER ASP GLU SEQRES 15 A 296 GLU MET ALA GLU TYR ARG ARG PRO PHE LEU ASN ALA GLY SEQRES 16 A 296 GLU ASP ARG ARG PRO THR LEU SER TRP PRO ARG GLN ILE SEQRES 17 A 296 PRO ILE ASP GLY GLU PRO ALA ASP VAL VAL ALA ILE VAL SEQRES 18 A 296 SER ASP TYR ALA SER TRP LEU ALA GLU SER ASP ILE PRO SEQRES 19 A 296 LYS LEU PHE ILE ASN ALA GLU PRO GLY ALA ILE VAL THR SEQRES 20 A 296 GLY ARG MET ARG ASP PHE CYS ARG SER TRP PRO ASN GLN SEQRES 21 A 296 THR GLU ILE THR VAL LYS GLY ALA HIS PHE ILE GLN GLU SEQRES 22 A 296 ASP SER PRO ASP GLU ILE GLY ALA ALA ILE ALA GLU PHE SEQRES 23 A 296 VAL ARG ARG LEU ARG VAL ALA ALA GLY VAL HET CL A 401 1 HET NA A 402 1 HET NA A 403 1 HET NA A 404 1 HET NA A 405 1 HET EDO A 406 8 HETNAM CL CHLORIDE ION HETNAM NA SODIUM ION HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 2 CL CL 1- FORMUL 3 NA 4(NA 1+) FORMUL 7 EDO C2 H6 O2 FORMUL 8 HOH *317(H2 O) HELIX 1 AA1 SER A 42 ARG A 47 5 6 HELIX 2 AA2 ILE A 49 GLU A 54 5 6 HELIX 3 AA3 SER A 82 LEU A 97 1 16 HELIX 4 AA4 ASP A 109 HIS A 122 1 14 HELIX 5 AA5 GLU A 140 TRP A 144 5 5 HELIX 6 AA6 PRO A 145 ARG A 156 1 12 HELIX 7 AA7 ALA A 159 LEU A 165 1 7 HELIX 8 AA8 ASN A 168 ARG A 173 1 6 HELIX 9 AA9 ARG A 173 ALA A 178 1 6 HELIX 10 AB1 SER A 184 ARG A 193 1 10 HELIX 11 AB2 PRO A 194 LEU A 196 5 3 HELIX 12 AB3 GLY A 199 ASP A 201 5 3 HELIX 13 AB4 ARG A 202 TRP A 208 1 7 HELIX 14 AB5 PRO A 209 ILE A 212 5 4 HELIX 15 AB6 PRO A 218 SER A 235 1 18 HELIX 16 AB7 THR A 251 SER A 260 1 10 HELIX 17 AB8 PHE A 274 ASP A 278 5 5 HELIX 18 AB9 SER A 279 VAL A 296 1 18 SHEET 1 AA1 8 LYS A 13 ILE A 17 0 SHEET 2 AA1 8 LYS A 20 GLU A 27 -1 O LYS A 20 N ILE A 17 SHEET 3 AA1 8 ARG A 58 CYS A 62 -1 O LEU A 59 N GLU A 27 SHEET 4 AA1 8 PRO A 32 GLN A 36 1 N PHE A 35 O ILE A 60 SHEET 5 AA1 8 VAL A 103 HIS A 108 1 O VAL A 104 N VAL A 34 SHEET 6 AA1 8 VAL A 126 MET A 132 1 O ALA A 130 N LEU A 105 SHEET 7 AA1 8 LYS A 239 PRO A 246 1 O LEU A 240 N TYR A 131 SHEET 8 AA1 8 GLN A 264 GLY A 271 1 O THR A 265 N PHE A 241 LINK O PHE A 35 NA NA A 402 1555 1555 2.88 LINK O PHE A 35 NA NA A 403 1555 1555 2.79 LINK OE1 GLN A 36 NA NA A 402 1555 1555 2.72 LINK O CYS A 62 NA NA A 403 1555 1555 2.87 LINK O TYR A 81 NA NA A 405 1555 1555 2.99 LINK O HIS A 86 NA NA A 404 1555 1555 3.05 LINK O PRO A 204 NA NA A 405 1555 1555 2.89 CISPEP 1 ASN A 39 PRO A 40 0 -13.40 CISPEP 2 SER A 74 PRO A 75 0 -19.25 CISPEP 3 SER A 74 PRO A 75 0 8.23 CISPEP 4 GLU A 217 PRO A 218 0 -3.24 CISPEP 5 GLU A 245 PRO A 246 0 3.51 CISPEP 6 GLU A 245 PRO A 246 0 0.34 CRYST1 68.897 68.897 156.259 90.00 90.00 90.00 P 43 21 2 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.014514 0.000000 0.000000 0.00000 SCALE2 0.000000 0.014514 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006400 0.00000 ATOM 1 N GLY A 5 11.758 9.966 -30.673 1.00 36.00 N ANISOU 1 N GLY A 5 5154 4182 4342 -244 -204 691 N ATOM 2 CA GLY A 5 11.446 9.060 -29.575 1.00 29.39 C ANISOU 2 CA GLY A 5 4074 3560 3532 -428 113 -205 C ATOM 3 C GLY A 5 10.756 7.776 -29.992 1.00 25.53 C ANISOU 3 C GLY A 5 3571 3068 3059 -78 -250 -64 C ATOM 4 O GLY A 5 10.637 6.880 -29.219 1.00 23.07 O ANISOU 4 O GLY A 5 3139 2792 2832 -44 -124 178 O ATOM 5 N ALA A 6 10.303 7.721 -31.230 1.00 23.29 N ANISOU 5 N ALA A 6 3246 2652 2951 -49 -206 153 N ATOM 6 CA ALA A 6 9.680 6.551 -31.792 1.00 21.41 C ANISOU 6 CA ALA A 6 2835 2637 2661 -29 -328 303 C ATOM 7 C ALA A 6 10.658 5.570 -32.440 1.00 20.34 C ANISOU 7 C ALA A 6 2691 2660 2374 0 -145 150 C ATOM 8 O ALA A 6 10.302 4.464 -32.672 1.00 21.28 O ANISOU 8 O ALA A 6 2883 2519 2684 -152 -161 53 O ATOM 9 CB ALA A 6 8.613 6.960 -32.812 1.00 21.08 C ANISOU 9 CB ALA A 6 2734 2725 2549 10 -209 181 C ATOM 10 N GLU A 7 11.874 5.984 -32.708 1.00 19.70 N ANISOU 10 N GLU A 7 2613 2387 2483 70 -74 110 N ATOM 11 CA GLU A 7 12.827 5.120 -33.359 1.00 20.08 C ANISOU 11 CA GLU A 7 2526 2710 2390 120 0 193 C ATOM 12 C GLU A 7 13.324 3.981 -32.493 1.00 19.24 C ANISOU 12 C GLU A 7 2516 2283 2510 -33 25 76 C ATOM 13 O GLU A 7 13.621 4.158 -31.377 1.00 18.94 O ANISOU 13 O GLU A 7 2566 2256 2374 -110 10 29 O ATOM 14 CB GLU A 7 14.057 5.901 -33.770 1.00 25.70 C ANISOU 14 CB GLU A 7 3429 3153 3184 -305 -110 79 C ATOM 15 CG GLU A 7 13.848 6.910 -34.866 1.00 34.70 C ANISOU 15 CG GLU A 7 4468 4291 4426 149 28 382 C ATOM 16 CD GLU A 7 15.132 7.616 -35.289 1.00 52.46 C ANISOU 16 CD GLU A 7 5999 6996 6938 -887 828 395 C ATOM 17 OE1 GLU A 7 16.242 7.216 -34.934 1.00 51.00 O ANISOU 17 OE1 GLU A 7 6310 6934 6133 -968 258 1670 O ATOM 18 OE2 GLU A 7 15.023 8.602 -36.010 1.00 76.99 O ANISOU 18 OE2 GLU A 7 11641 8371 9239 1254 497 2533 O ATOM 19 N PRO A 8 13.415 2.800 -33.069 1.00 18.68 N ANISOU 19 N PRO A 8 2509 2303 2285 -52 -43 -12 N ATOM 20 CA PRO A 8 14.000 1.716 -32.290 1.00 17.69 C ANISOU 20 CA PRO A 8 2279 2295 2147 4 162 -92 C ATOM 21 C PRO A 8 15.470 2.005 -31.949 1.00 18.26 C ANISOU 21 C PRO A 8 2239 2311 2387 59 -36 -147 C ATOM 22 O PRO A 8 16.155 2.757 -32.606 1.00 20.96 O ANISOU 22 O PRO A 8 2643 2617 2701 -1 61 356 O ATOM 23 CB PRO A 8 13.923 0.522 -33.241 1.00 19.69 C ANISOU 23 CB PRO A 8 2480 2334 2667 -203 -23 -67 C ATOM 24 CG PRO A 8 12.804 0.851 -34.153 1.00 23.55 C ANISOU 24 CG PRO A 8 3335 2707 2903 22 -172 -93 C ATOM 25 CD PRO A 8 12.946 2.331 -34.376 1.00 22.61 C ANISOU 25 CD PRO A 8 3276 2616 2699 -180 -135 87 C ATOM 26 N TYR A 9 15.958 1.339 -30.931 1.00 17.45 N ANISOU 26 N TYR A 9 2337 2171 2122 -201 72 49 N ATOM 27 CA TYR A 9 17.320 1.503 -30.511 1.00 16.57 C ANISOU 27 CA TYR A 9 2099 2032 2163 -81 142 237 C ATOM 28 C TYR A 9 18.206 0.440 -31.116 1.00 21.16 C ANISOU 28 C TYR A 9 2765 2534 2739 -100 180 213 C ATOM 29 O TYR A 9 17.933 -0.696 -31.036 1.00 21.06 O ANISOU 29 O TYR A 9 2718 2516 2766 -64 173 -83 O ATOM 30 CB TYR A 9 17.426 1.426 -28.982 1.00 18.85 C ANISOU 30 CB TYR A 9 2422 2304 2437 -101 38 89 C ATOM 31 CG TYR A 9 18.842 1.561 -28.474 1.00 18.81 C ANISOU 31 CG TYR A 9 2431 2328 2387 -48 -117 82 C ATOM 32 CD1 TYR A 9 19.416 2.778 -28.357 1.00 25.20 C ANISOU 32 CD1 TYR A 9 3037 3009 3527 -251 -154 -50 C ATOM 33 CD2 TYR A 9 19.567 0.483 -28.099 1.00 21.48 C ANISOU 33 CD2 TYR A 9 2530 2655 2974 -167 130 80 C ATOM 34 CE1 TYR A 9 20.686 2.916 -27.895 1.00 24.62 C ANISOU 34 CE1 TYR A 9 3153 3085 3113 -43 -387 4 C ATOM 35 CE2 TYR A 9 20.841 0.615 -27.654 1.00 23.22 C ANISOU 35 CE2 TYR A 9 2995 2909 2917 212 -397 113 C ATOM 36 CZ TYR A 9 21.387 1.844 -27.559 1.00 23.01 C ANISOU 36 CZ TYR A 9 2956 3033 2752 -67 83 32 C ATOM 37 OH TYR A 9 22.641 2.021 -27.124 1.00 27.34 O ANISOU 37 OH TYR A 9 3286 3923 3178 -253 -207 340 O ATOM 38 N GLY A 10 19.288 0.853 -31.731 1.00 25.23 N ANISOU 38 N GLY A 10 2969 3225 3390 -35 418 -205 N ATOM 39 CA GLY A 10 20.215 -0.093 -32.316 1.00 27.03 C ANISOU 39 CA GLY A 10 3264 3262 3740 -127 216 102 C ATOM 40 C GLY A 10 19.707 -0.914 -33.484 1.00 23.71 C ANISOU 40 C GLY A 10 2686 3306 3014 132 398 -36 C ATOM 41 O GLY A 10 18.799 -0.553 -34.134 1.00 27.51 O ANISOU 41 O GLY A 10 3708 3639 3105 151 344 -50 O ATOM 42 N GLN A 11 20.399 -2.021 -33.733 1.00 26.21 N ANISOU 42 N GLN A 11 3451 2982 3524 -201 458 191 N ATOM 43 CA GLN A 11 20.064 -2.944 -34.806 1.00 24.72 C ANISOU 43 CA GLN A 11 3465 2963 2962 -245 158 518 C ATOM 44 C GLN A 11 20.068 -4.347 -34.222 1.00 20.29 C ANISOU 44 C GLN A 11 2582 2395 2731 46 -5 56 C ATOM 45 O GLN A 11 21.060 -4.784 -33.638 1.00 25.79 O ANISOU 45 O GLN A 11 3303 3091 3404 -415 -221 307 O ATOM 46 CB GLN A 11 21.078 -2.838 -35.945 1.00 35.71 C ANISOU 46 CB GLN A 11 4841 4056 4670 136 1069 115 C ATOM 47 CG GLN A 11 20.983 -1.548 -36.743 1.00 47.90 C ANISOU 47 CG GLN A 11 6738 5610 5849 -274 16 634 C ATOM 48 CD GLN A 11 19.668 -1.420 -37.487 1.00 58.67 C ANISOU 48 CD GLN A 11 7592 7404 7295 -275 110 902 C ATOM 49 OE1 GLN A 11 19.131 -2.404 -37.997 1.00 64.52 O ANISOU 49 OE1 GLN A 11 9709 9195 5609 -943 -733 -193 O ATOM 50 NE2 GLN A 11 19.141 -0.203 -37.551 1.00 69.64 N ANISOU 50 NE2 GLN A 11 9889 7098 9470 1389 1103 1460 N ATOM 51 N LYS A 12 18.955 -5.051 -34.381 1.00 18.65 N ANISOU 51 N LYS A 12 2429 2276 2377 79 -20 166 N ATOM 52 CA LYS A 12 18.818 -6.415 -33.825 1.00 17.02 C ANISOU 52 CA LYS A 12 2292 2061 2111 65 -66 8 C ATOM 53 C LYS A 12 19.720 -7.445 -34.465 1.00 18.88 C ANISOU 53 C LYS A 12 2420 2350 2403 79 141 155 C ATOM 54 O LYS A 12 20.076 -7.405 -35.667 1.00 19.07 O ANISOU 54 O LYS A 12 2618 2364 2264 -41 113 -89 O ATOM 55 CB LYS A 12 17.455 -6.884 -33.852 1.00 18.66 C ANISOU 55 CB LYS A 12 2477 2248 2365 26 40 0 C ATOM 56 CG LYS A 12 16.441 -6.057 -33.076 1.00 20.66 C ANISOU 56 CG LYS A 12 2500 2649 2700 -12 -39 -42 C ATOM 57 CD LYS A 12 15.010 -6.651 -32.974 1.00 20.56 C ANISOU 57 CD LYS A 12 2640 2535 2635 79 2 257 C ATOM 58 CE LYS A 12 14.112 -5.676 -32.453 1.00 16.75 C ANISOU 58 CE LYS A 12 2171 2163 2028 26 56 129 C ATOM 59 NZ LYS A 12 12.719 -6.130 -32.362 1.00 16.95 N ANISOU 59 NZ LYS A 12 2325 2026 2088 -31 40 -15 N ATOM 60 N ALYS A 13 20.205 -8.314 -33.628 0.50 15.25 N ANISOU 60 N ALYS A 13 2086 1938 1769 36 229 -47 N ATOM 61 N BLYS A 13 20.153 -8.346 -33.647 0.50 15.92 N ANISOU 61 N BLYS A 13 2181 2030 1835 52 207 -41 N ATOM 62 CA ALYS A 13 20.947 -9.543 -33.893 0.50 14.71 C ANISOU 62 CA ALYS A 13 1962 1856 1768 -57 170 161 C ATOM 63 CA BLYS A 13 20.888 -9.549 -33.954 0.50 16.10 C ANISOU 63 CA BLYS A 13 2166 1986 1965 -82 245 147 C ATOM 64 C ALYS A 13 19.999 -10.723 -33.737 0.50 14.83 C ANISOU 64 C ALYS A 13 1797 1724 2112 37 147 11 C ATOM 65 C BLYS A 13 19.999 -10.732 -33.731 0.50 15.39 C ANISOU 65 C BLYS A 13 1863 1791 2191 62 158 -2 C ATOM 66 O ALYS A 13 18.941 -10.637 -33.089 0.50 15.75 O ANISOU 66 O ALYS A 13 2189 1812 1981 -87 106 -19 O ATOM 67 O BLYS A 13 18.991 -10.657 -33.032 0.50 16.05 O ANISOU 67 O BLYS A 13 2235 1853 2009 -80 112 -42 O ATOM 68 CB ALYS A 13 22.191 -9.665 -33.046 0.50 14.96 C ANISOU 68 CB ALYS A 13 1965 1759 1957 -181 218 -51 C ATOM 69 CB BLYS A 13 22.168 -9.630 -33.187 0.50 16.86 C ANISOU 69 CB BLYS A 13 2228 2033 2144 -185 227 -85 C ATOM 70 CG ALYS A 13 23.166 -8.471 -33.168 0.50 15.68 C ANISOU 70 CG ALYS A 13 2094 1856 2004 -186 77 266 C ATOM 71 CG BLYS A 13 23.187 -8.562 -33.623 0.50 18.89 C ANISOU 71 CG BLYS A 13 2531 2150 2493 -236 113 -21 C ATOM 72 CD ALYS A 13 24.216 -8.596 -32.074 0.50 17.14 C ANISOU 72 CD ALYS A 13 2149 2177 2186 -102 8 -68 C ATOM 73 CD BLYS A 13 24.279 -8.426 -32.571 0.50 20.41 C ANISOU 73 CD BLYS A 13 2558 2647 2549 -148 44 260 C ATOM 74 CE ALYS A 13 25.386 -7.705 -32.234 0.50 17.88 C ANISOU 74 CE ALYS A 13 2158 2348 2288 -209 50 -224 C ATOM 75 CE BLYS A 13 25.306 -7.351 -32.917 0.50 21.52 C ANISOU 75 CE BLYS A 13 2673 2615 2887 -116 -161 115 C ATOM 76 NZ ALYS A 13 24.974 -6.264 -32.464 0.50 18.24 N ANISOU 76 NZ ALYS A 13 2466 2320 2142 106 227 50 N ATOM 77 NZ BLYS A 13 26.161 -7.003 -31.700 0.50 23.85 N ANISOU 77 NZ BLYS A 13 2975 3242 2844 -226 57 -191 N ATOM 78 N PHE A 14 20.395 -11.859 -34.307 1.00 14.79 N ANISOU 78 N PHE A 14 1898 1881 1841 -32 129 -182 N ATOM 79 CA PHE A 14 19.547 -13.028 -34.292 1.00 16.96 C ANISOU 79 CA PHE A 14 2167 2151 2126 -107 268 73 C ATOM 80 C PHE A 14 20.341 -14.294 -33.921 1.00 17.39 C ANISOU 80 C PHE A 14 2124 2177 2305 38 95 34 C ATOM 81 O PHE A 14 21.540 -14.457 -34.343 1.00 18.63 O ANISOU 81 O PHE A 14 2296 2321 2460 50 210 -21 O ATOM 82 CB PHE A 14 18.917 -13.225 -35.666 1.00 17.63 C ANISOU 82 CB PHE A 14 2177 2138 2384 -31 -69 -239 C ATOM 83 CG PHE A 14 18.249 -12.048 -36.206 1.00 18.09 C ANISOU 83 CG PHE A 14 2315 2441 2114 -86 -194 35 C ATOM 84 CD1 PHE A 14 17.083 -11.639 -35.759 1.00 21.10 C ANISOU 84 CD1 PHE A 14 2737 2841 2438 3 -33 -155 C ATOM 85 CD2 PHE A 14 18.786 -11.365 -37.220 1.00 20.97 C ANISOU 85 CD2 PHE A 14 2602 2604 2759 -229 -30 38 C ATOM 86 CE1 PHE A 14 16.400 -10.558 -36.238 1.00 21.75 C ANISOU 86 CE1 PHE A 14 3011 2683 2567 103 143 -134 C ATOM 87 CE2 PHE A 14 18.156 -10.233 -37.730 1.00 20.99 C ANISOU 87 CE2 PHE A 14 2652 2617 2705 -26 -201 26 C ATOM 88 CZ PHE A 14 16.967 -9.842 -37.245 1.00 21.98 C ANISOU 88 CZ PHE A 14 2859 2674 2818 -124 -3 -115 C ATOM 89 N ILE A 15 19.822 -15.145 -33.058 1.00 18.04 N ANISOU 89 N ILE A 15 2186 2193 2473 178 109 81 N ATOM 90 CA ILE A 15 20.421 -16.457 -32.669 1.00 18.53 C ANISOU 90 CA ILE A 15 2239 2265 2535 97 119 144 C ATOM 91 C ILE A 15 19.349 -17.453 -32.759 1.00 17.81 C ANISOU 91 C ILE A 15 2299 2158 2310 -17 201 14 C ATOM 92 O ILE A 15 18.240 -17.193 -32.278 1.00 17.16 O ANISOU 92 O ILE A 15 2126 2061 2333 12 -20 -40 O ATOM 93 CB ILE A 15 20.956 -16.336 -31.246 1.00 21.91 C ANISOU 93 CB ILE A 15 2732 2552 3040 -118 -589 252 C ATOM 94 CG1 ILE A 15 22.332 -15.632 -31.227 1.00 22.83 C ANISOU 94 CG1 ILE A 15 2857 2871 2943 52 464 20 C ATOM 95 CG2 ILE A 15 21.268 -17.820 -30.667 1.00 25.24 C ANISOU 95 CG2 ILE A 15 3066 3043 3479 97 -580 -8 C ATOM 96 CD1 ILE A 15 23.065 -15.505 -29.855 1.00 28.65 C ANISOU 96 CD1 ILE A 15 3460 3758 3666 -265 138 175 C ATOM 97 N AGLU A 16 19.681 -18.650 -33.221 0.50 17.51 N ANISOU 97 N AGLU A 16 2240 2041 2369 -36 326 -119 N ATOM 98 N BGLU A 16 19.621 -18.663 -33.286 0.50 17.48 N ANISOU 98 N BGLU A 16 2238 2038 2363 -38 328 -121 N ATOM 99 CA AGLU A 16 18.724 -19.730 -33.280 0.50 18.92 C ANISOU 99 CA AGLU A 16 2456 2414 2318 -54 44 -18 C ATOM 100 CA BGLU A 16 18.643 -19.722 -33.313 0.50 18.78 C ANISOU 100 CA BGLU A 16 2418 2384 2329 -25 20 2 C ATOM 101 C AGLU A 16 18.790 -20.512 -31.970 0.50 16.18 C ANISOU 101 C AGLU A 16 2114 1813 2220 -294 -54 -121 C ATOM 102 C BGLU A 16 18.771 -20.540 -31.978 0.50 16.16 C ANISOU 102 C BGLU A 16 2117 1809 2213 -290 -47 -118 C ATOM 103 O AGLU A 16 19.825 -20.976 -31.595 0.50 18.13 O ANISOU 103 O AGLU A 16 2376 2121 2388 185 80 43 O ATOM 104 O BGLU A 16 19.852 -20.987 -31.585 0.50 18.01 O ANISOU 104 O BGLU A 16 2362 2107 2372 186 81 38 O ATOM 105 CB AGLU A 16 19.058 -20.685 -34.418 0.50 20.31 C ANISOU 105 CB AGLU A 16 2715 2479 2522 -103 437 -356 C ATOM 106 CB BGLU A 16 18.953 -20.688 -34.503 0.50 21.29 C ANISOU 106 CB BGLU A 16 2890 2626 2572 -79 480 -363 C ATOM 107 CG AGLU A 16 18.944 -20.062 -35.783 0.50 26.17 C ANISOU 107 CG AGLU A 16 3791 3070 3081 301 -50 100 C ATOM 108 CG BGLU A 16 18.783 -19.997 -35.850 0.50 27.52 C ANISOU 108 CG BGLU A 16 3887 3232 3336 583 189 -55 C ATOM 109 CD AGLU A 16 17.533 -20.099 -36.307 0.50 30.30 C ANISOU 109 CD AGLU A 16 3761 4107 3644 68 -507 -735 C ATOM 110 CD BGLU A 16 17.473 -20.288 -36.655 0.50 36.32 C ANISOU 110 CD BGLU A 16 4248 4975 4577 389 -770 272 C ATOM 111 OE1AGLU A 16 16.797 -20.999 -35.902 0.50 32.54 O ANISOU 111 OE1AGLU A 16 4242 4024 4097 -13 880 -438 O ATOM 112 OE1BGLU A 16 17.174 -21.546 -36.697 0.50 39.53 O ANISOU 112 OE1BGLU A 16 5391 4231 5395 -1513 -123 22 O ATOM 113 OE2AGLU A 16 17.159 -19.240 -37.127 0.50 37.43 O ANISOU 113 OE2AGLU A 16 6299 3473 4449 -95 635 121 O ATOM 114 OE2BGLU A 16 16.814 -19.299 -37.404 0.50 30.89 O ANISOU 114 OE2BGLU A 16 4174 3283 4279 -623 915 -89 O ATOM 115 N ILE A 17 17.656 -20.638 -31.310 1.00 15.10 N ANISOU 115 N ILE A 17 2023 1794 1918 23 5 10 N ATOM 116 CA ILE A 17 17.494 -21.377 -30.017 1.00 16.38 C ANISOU 116 CA ILE A 17 2051 2166 2004 105 -82 14 C ATOM 117 C ILE A 17 16.400 -22.329 -30.257 1.00 16.06 C ANISOU 117 C ILE A 17 2069 1980 2052 59 239 -37 C ATOM 118 O ILE A 17 15.262 -22.051 -30.599 1.00 16.61 O ANISOU 118 O ILE A 17 2162 2128 2020 27 -45 -6 O ATOM 119 CB ILE A 17 17.112 -20.374 -28.907 1.00 16.48 C ANISOU 119 CB ILE A 17 2102 2083 2076 62 54 17 C ATOM 120 CG1 ILE A 17 18.123 -19.330 -28.626 1.00 18.13 C ANISOU 120 CG1 ILE A 17 2404 2286 2198 67 -122 -93 C ATOM 121 CG2 ILE A 17 16.733 -21.154 -27.664 1.00 17.86 C ANISOU 121 CG2 ILE A 17 2331 2215 2238 231 -21 128 C ATOM 122 CD1 ILE A 17 19.478 -19.849 -28.168 1.00 23.19 C ANISOU 122 CD1 ILE A 17 2918 2964 2927 146 -148 -303 C ATOM 123 N ALA A 18 16.738 -23.594 -30.032 1.00 18.14 N ANISOU 123 N ALA A 18 2282 2181 2427 13 -67 209 N ATOM 124 CA ALA A 18 15.757 -24.671 -30.144 1.00 20.72 C ANISOU 124 CA ALA A 18 2690 2395 2786 -50 -12 -322 C ATOM 125 C ALA A 18 14.865 -24.593 -31.374 1.00 19.59 C ANISOU 125 C ALA A 18 2569 2196 2679 182 149 239 C ATOM 126 O ALA A 18 13.683 -24.685 -31.307 1.00 22.50 O ANISOU 126 O ALA A 18 2696 2792 3058 -226 -169 388 O ATOM 127 CB ALA A 18 14.944 -24.799 -28.867 1.00 24.23 C ANISOU 127 CB ALA A 18 3215 2772 3217 93 149 340 C ATOM 128 N GLY A 19 15.508 -24.387 -32.486 1.00 18.24 N ANISOU 128 N GLY A 19 2404 2135 2389 23 -120 -111 N ATOM 129 CA GLY A 19 14.917 -24.332 -33.806 1.00 20.13 C ANISOU 129 CA GLY A 19 2617 2400 2629 -239 -76 61 C ATOM 130 C GLY A 19 14.135 -23.119 -34.142 1.00 18.78 C ANISOU 130 C GLY A 19 2435 2360 2340 191 -99 -129 C ATOM 131 O GLY A 19 13.446 -23.061 -35.187 1.00 22.26 O ANISOU 131 O GLY A 19 2966 2760 2732 168 -247 -280 O ATOM 132 N LYS A 20 14.244 -22.024 -33.354 1.00 16.67 N ANISOU 132 N LYS A 20 2208 2107 2016 46 -20 -44 N ATOM 133 CA LYS A 20 13.600 -20.798 -33.559 1.00 17.63 C ANISOU 133 CA LYS A 20 2301 2282 2116 -122 -66 177 C ATOM 134 C LYS A 20 14.535 -19.624 -33.494 1.00 15.90 C ANISOU 134 C LYS A 20 2047 2014 1979 23 -70 12 C ATOM 135 O LYS A 20 15.432 -19.612 -32.668 1.00 17.09 O ANISOU 135 O LYS A 20 2185 2123 2182 -52 -137 67 O ATOM 136 CB LYS A 20 12.471 -20.564 -32.543 1.00 16.54 C ANISOU 136 CB LYS A 20 2221 1946 2115 161 -17 -45 C ATOM 137 CG LYS A 20 11.307 -21.498 -32.601 1.00 19.21 C ANISOU 137 CG LYS A 20 2512 2410 2374 27 157 -199 C ATOM 138 CD LYS A 20 10.456 -21.305 -33.774 1.00 18.82 C ANISOU 138 CD LYS A 20 2322 2193 2633 166 -113 90 C ATOM 139 CE LYS A 20 9.375 -22.366 -34.152 1.00 23.52 C ANISOU 139 CE LYS A 20 3112 2760 3061 113 113 -183 C ATOM 140 NZ LYS A 20 10.080 -23.566 -34.775 1.00 29.39 N ANISOU 140 NZ LYS A 20 3840 3601 3725 451 -230 -136 N ATOM 141 N AARG A 21 14.311 -18.642 -34.340 0.50 15.35 N ANISOU 141 N AARG A 21 2145 1874 1813 -101 -3 -79 N ATOM 142 N BARG A 21 14.285 -18.637 -34.385 0.50 14.54 N ANISOU 142 N BARG A 21 2030 1772 1723 -115 -6 -95 N ATOM 143 CA AARG A 21 15.142 -17.482 -34.278 0.50 15.86 C ANISOU 143 CA AARG A 21 1997 1963 2063 -154 106 -11 C ATOM 144 CA BARG A 21 14.923 -17.313 -34.245 0.50 13.97 C ANISOU 144 CA BARG A 21 1752 1695 1860 -116 159 2 C ATOM 145 C AARG A 21 14.666 -16.540 -33.196 0.50 16.05 C ANISOU 145 C AARG A 21 2079 2050 1967 9 -108 178 C ATOM 146 C BARG A 21 14.499 -16.561 -33.032 0.50 14.64 C ANISOU 146 C BARG A 21 1817 1797 1947 -26 -113 100 C ATOM 147 O AARG A 21 13.510 -16.256 -33.094 0.50 15.07 O ANISOU 147 O AARG A 21 1918 1962 1845 -28 4 -88 O ATOM 148 O BARG A 21 13.316 -16.410 -32.754 0.50 15.42 O ANISOU 148 O BARG A 21 1984 1825 2048 -41 1 50 O ATOM 149 CB AARG A 21 15.180 -16.754 -35.617 0.50 14.31 C ANISOU 149 CB AARG A 21 1855 1723 1856 77 -99 3 C ATOM 150 CB BARG A 21 14.629 -16.394 -35.431 0.50 13.77 C ANISOU 150 CB BARG A 21 1770 1785 1676 -176 -141 -173 C ATOM 151 CG AARG A 21 16.444 -15.919 -35.761 0.50 17.91 C ANISOU 151 CG AARG A 21 2232 2316 2256 -245 84 60 C ATOM 152 CG BARG A 21 15.184 -14.913 -35.259 0.50 15.27 C ANISOU 152 CG BARG A 21 2023 1833 1945 -46 -56 36 C ATOM 153 CD AARG A 21 16.723 -15.501 -37.184 0.50 17.92 C ANISOU 153 CD AARG A 21 2404 2194 2211 177 -217 -30 C ATOM 154 CD BARG A 21 15.109 -14.106 -36.564 0.50 16.14 C ANISOU 154 CD BARG A 21 2091 1985 2054 19 -85 170 C ATOM 155 NE AARG A 21 15.912 -14.391 -37.580 0.50 16.31 N ANISOU 155 NE AARG A 21 2065 2183 1946 -38 26 -134 N ATOM 156 NE BARG A 21 16.201 -14.468 -37.521 0.50 14.98 N ANISOU 156 NE BARG A 21 2029 1915 1747 -125 -25 -7 N ATOM 157 CZ AARG A 21 16.198 -13.646 -38.629 0.50 18.77 C ANISOU 157 CZ AARG A 21 2426 2368 2336 -82 120 -56 C ATOM 158 CZ BARG A 21 16.506 -13.761 -38.617 0.50 13.90 C ANISOU 158 CZ BARG A 21 1836 1667 1775 -57 -169 -24 C ATOM 159 NH1AARG A 21 17.261 -13.910 -39.344 0.50 17.60 N ANISOU 159 NH1AARG A 21 2258 2191 2236 62 144 21 N ATOM 160 NH1BARG A 21 15.735 -12.712 -38.946 0.50 12.08 N ANISOU 160 NH1BARG A 21 1375 1519 1693 91 -55 0 N ATOM 161 NH2AARG A 21 15.422 -12.660 -38.948 0.50 21.92 N ANISOU 161 NH2AARG A 21 3059 2482 2785 -27 -157 52 N ATOM 162 NH2BARG A 21 17.514 -14.064 -39.394 0.50 15.04 N ANISOU 162 NH2BARG A 21 2044 1918 1752 73 -183 89 N ATOM 163 N AMET A 22 15.589 -16.159 -32.337 0.50 15.86 N ANISOU 163 N AMET A 22 2167 1816 2042 -47 -191 -32 N ATOM 164 N BMET A 22 15.538 -16.087 -32.310 0.50 13.09 N ANISOU 164 N BMET A 22 1797 1492 1682 -12 -125 -34 N ATOM 165 CA AMET A 22 15.344 -15.149 -31.324 0.50 16.68 C ANISOU 165 CA AMET A 22 2074 2011 2252 123 75 -55 C ATOM 166 CA BMET A 22 15.322 -15.071 -31.358 0.50 13.08 C ANISOU 166 CA BMET A 22 1655 1622 1690 114 5 -34 C ATOM 167 C AMET A 22 16.100 -13.902 -31.760 0.50 15.86 C ANISOU 167 C AMET A 22 1885 1977 2165 122 123 27 C ATOM 168 C BMET A 22 16.144 -13.873 -31.676 0.50 14.23 C ANISOU 168 C BMET A 22 1716 1783 1907 21 100 83 C ATOM 169 O AMET A 22 17.194 -13.960 -32.292 0.50 15.75 O ANISOU 169 O AMET A 22 2072 1779 2131 4 14 87 O ATOM 170 O BMET A 22 17.305 -13.918 -32.007 0.50 15.15 O ANISOU 170 O BMET A 22 1936 1735 2084 18 55 66 O ATOM 171 CB AMET A 22 15.836 -15.635 -29.959 0.50 19.19 C ANISOU 171 CB AMET A 22 2664 2491 2135 -373 8 -94 C ATOM 172 CB BMET A 22 15.583 -15.552 -29.999 0.50 12.39 C ANISOU 172 CB BMET A 22 1680 1541 1486 -179 -5 -29 C ATOM 173 CG AMET A 22 15.149 -16.894 -29.330 0.50 24.21 C ANISOU 173 CG AMET A 22 2956 2837 3404 -83 -81 69 C ATOM 174 CG BMET A 22 14.809 -16.838 -29.637 0.50 12.88 C ANISOU 174 CG BMET A 22 1571 1719 1604 -112 59 86 C ATOM 175 SD AMET A 22 13.623 -16.576 -28.417 0.50 28.03 S ANISOU 175 SD AMET A 22 3745 3435 3468 -406 188 -264 S ATOM 176 SD BMET A 22 14.994 -17.272 -27.891 0.50 11.08 S ANISOU 176 SD BMET A 22 1400 1397 1412 48 1 2 S ATOM 177 CE AMET A 22 14.330 -15.626 -27.045 0.50 30.39 C ANISOU 177 CE AMET A 22 4226 3877 3444 -459 -394 35 C ATOM 178 CE BMET A 22 14.027 -16.024 -26.990 0.50 12.49 C ANISOU 178 CE BMET A 22 1653 1665 1428 -49 -161 -10 C ATOM 179 N ALA A 23 15.452 -12.745 -31.554 1.00 13.80 N ANISOU 179 N ALA A 23 1779 1675 1789 -27 15 -36 N ATOM 180 CA ALA A 23 15.957 -11.442 -31.913 1.00 13.28 C ANISOU 180 CA ALA A 23 1667 1707 1671 -124 54 30 C ATOM 181 C ALA A 23 16.316 -10.697 -30.642 1.00 13.94 C ANISOU 181 C ALA A 23 1825 1756 1714 -90 95 15 C ATOM 182 O ALA A 23 15.607 -10.786 -29.612 1.00 14.01 O ANISOU 182 O ALA A 23 1812 1703 1807 -7 84 -118 O ATOM 183 CB ALA A 23 14.921 -10.610 -32.673 1.00 16.09 C ANISOU 183 CB ALA A 23 2109 2036 1966 66 80 -78 C ATOM 184 N TYR A 24 17.404 -9.961 -30.690 1.00 13.48 N ANISOU 184 N TYR A 24 1758 1687 1675 -39 11 -177 N ATOM 185 CA TYR A 24 17.840 -9.228 -29.530 1.00 12.92 C ANISOU 185 CA TYR A 24 1626 1722 1558 2 -5 -68 C ATOM 186 C TYR A 24 18.792 -8.080 -29.897 1.00 15.25 C ANISOU 186 C TYR A 24 2062 1760 1971 -102 159 -44 C ATOM 187 O TYR A 24 19.383 -8.092 -30.900 1.00 16.15 O ANISOU 187 O TYR A 24 2210 1887 2038 -196 164 -170 O ATOM 188 CB TYR A 24 18.580 -10.189 -28.564 1.00 13.87 C ANISOU 188 CB TYR A 24 1780 1693 1794 13 -105 -45 C ATOM 189 CG TYR A 24 19.855 -10.768 -29.148 1.00 13.33 C ANISOU 189 CG TYR A 24 1734 1742 1588 -62 35 4 C ATOM 190 CD1 TYR A 24 19.827 -11.844 -29.986 1.00 14.58 C ANISOU 190 CD1 TYR A 24 1913 1816 1810 -1 -27 30 C ATOM 191 CD2 TYR A 24 21.056 -10.230 -28.847 1.00 14.26 C ANISOU 191 CD2 TYR A 24 1823 1737 1857 8 -72 -90 C ATOM 192 CE1 TYR A 24 20.967 -12.340 -30.529 1.00 16.33 C ANISOU 192 CE1 TYR A 24 2100 2004 2098 102 3 162 C ATOM 193 CE2 TYR A 24 22.210 -10.726 -29.361 1.00 15.16 C ANISOU 193 CE2 TYR A 24 1905 1839 2016 -72 19 -79 C ATOM 194 CZ TYR A 24 22.162 -11.791 -30.212 1.00 16.12 C ANISOU 194 CZ TYR A 24 2093 2025 2006 18 -15 46 C ATOM 195 OH TYR A 24 23.318 -12.277 -30.733 1.00 17.53 O ANISOU 195 OH TYR A 24 2235 2120 2303 58 156 11 O ATOM 196 N ILE A 25 18.846 -7.092 -29.021 1.00 13.93 N ANISOU 196 N ILE A 25 1859 1782 1651 -177 120 -74 N ATOM 197 CA ILE A 25 19.847 -6.036 -29.104 1.00 15.20 C ANISOU 197 CA ILE A 25 1900 1997 1878 -74 77 -36 C ATOM 198 C ILE A 25 21.041 -6.406 -28.292 1.00 15.01 C ANISOU 198 C ILE A 25 2065 1715 1920 -25 -19 -179 C ATOM 199 O ILE A 25 20.877 -6.924 -27.129 1.00 15.16 O ANISOU 199 O ILE A 25 2026 1849 1885 20 38 -78 O ATOM 200 CB ILE A 25 19.194 -4.690 -28.651 1.00 16.56 C ANISOU 200 CB ILE A 25 2049 2060 2180 -47 19 50 C ATOM 201 CG1 ILE A 25 17.994 -4.370 -29.394 1.00 16.34 C ANISOU 201 CG1 ILE A 25 2159 2006 2043 -11 82 28 C ATOM 202 CG2 ILE A 25 20.278 -3.609 -28.647 1.00 18.09 C ANISOU 202 CG2 ILE A 25 2378 2143 2349 -92 61 -16 C ATOM 203 CD1 ILE A 25 17.140 -3.230 -28.801 1.00 18.82 C ANISOU 203 CD1 ILE A 25 2575 2322 2254 145 67 84 C ATOM 204 N ASP A 26 22.240 -6.168 -28.773 1.00 15.70 N ANISOU 204 N ASP A 26 2056 1928 1979 41 103 -60 N ATOM 205 CA ASP A 26 23.459 -6.469 -28.022 1.00 16.99 C ANISOU 205 CA ASP A 26 2255 2106 2092 -87 0 -69 C ATOM 206 C ASP A 26 24.503 -5.467 -28.496 1.00 19.22 C ANISOU 206 C ASP A 26 2468 2372 2462 28 190 -96 C ATOM 207 O ASP A 26 25.077 -5.637 -29.498 1.00 20.66 O ANISOU 207 O ASP A 26 2666 2609 2572 -192 210 -117 O ATOM 208 CB ASP A 26 23.900 -7.926 -28.227 1.00 17.77 C ANISOU 208 CB ASP A 26 2268 2288 2195 59 137 -56 C ATOM 209 CG ASP A 26 25.211 -8.293 -27.521 1.00 20.34 C ANISOU 209 CG ASP A 26 2539 2547 2642 34 -18 -51 C ATOM 210 OD1 ASP A 26 25.763 -7.515 -26.785 1.00 18.52 O ANISOU 210 OD1 ASP A 26 2341 2361 2334 -20 -56 -148 O ATOM 211 OD2 ASP A 26 25.676 -9.399 -27.747 1.00 21.04 O ANISOU 211 OD2 ASP A 26 2628 2544 2822 -116 -26 -160 O ATOM 212 N GLU A 27 24.648 -4.390 -27.742 1.00 18.19 N ANISOU 212 N GLU A 27 2383 2271 2255 -466 165 -75 N ATOM 213 CA GLU A 27 25.544 -3.289 -28.111 1.00 19.90 C ANISOU 213 CA GLU A 27 2599 2467 2494 -389 213 -96 C ATOM 214 C GLU A 27 26.506 -2.902 -27.030 1.00 18.98 C ANISOU 214 C GLU A 27 2365 2411 2434 -35 7 18 C ATOM 215 O GLU A 27 26.119 -2.781 -25.929 1.00 21.29 O ANISOU 215 O GLU A 27 2711 2760 2615 -371 90 -23 O ATOM 216 CB GLU A 27 24.739 -2.025 -28.386 1.00 21.96 C ANISOU 216 CB GLU A 27 2784 2615 2945 -301 -313 178 C ATOM 217 CG GLU A 27 23.643 -2.137 -29.407 1.00 31.93 C ANISOU 217 CG GLU A 27 4000 3897 4231 -170 -371 384 C ATOM 218 CD GLU A 27 24.141 -2.177 -30.811 1.00 37.95 C ANISOU 218 CD GLU A 27 4534 5710 4172 -436 13 280 C ATOM 219 OE1 GLU A 27 25.326 -1.901 -31.040 1.00 49.26 O ANISOU 219 OE1 GLU A 27 6217 7443 5054 -2027 -615 753 O ATOM 220 OE2 GLU A 27 23.359 -2.489 -31.689 1.00 36.38 O ANISOU 220 OE2 GLU A 27 4444 5089 4287 -1096 317 210 O ATOM 221 N GLY A 28 27.751 -2.660 -27.379 1.00 21.71 N ANISOU 221 N GLY A 28 2697 2805 2746 -206 163 -104 N ATOM 222 CA GLY A 28 28.703 -2.227 -26.366 1.00 23.27 C ANISOU 222 CA GLY A 28 2872 3209 2761 -460 206 243 C ATOM 223 C GLY A 28 29.521 -3.288 -25.745 1.00 24.46 C ANISOU 223 C GLY A 28 2837 3146 3308 -6 315 -204 C ATOM 224 O GLY A 28 29.304 -4.491 -25.995 1.00 26.73 O ANISOU 224 O GLY A 28 3154 3237 3764 -34 264 -170 O ATOM 225 N GLU A 29 30.484 -2.879 -24.911 1.00 25.95 N ANISOU 225 N GLU A 29 3360 3323 3174 -11 43 -149 N ATOM 226 CA GLU A 29 31.448 -3.741 -24.290 1.00 29.00 C ANISOU 226 CA GLU A 29 3656 3763 3598 -165 7 67 C ATOM 227 C GLU A 29 31.300 -3.743 -22.796 1.00 23.91 C ANISOU 227 C GLU A 29 2651 3010 3421 -156 -40 -9 C ATOM 228 O GLU A 29 30.855 -2.810 -22.191 1.00 28.04 O ANISOU 228 O GLU A 29 3397 3719 3537 -81 0 -159 O ATOM 229 CB GLU A 29 32.939 -3.337 -24.623 1.00 37.44 C ANISOU 229 CB GLU A 29 4172 5194 4859 319 75 180 C ATOM 230 CG GLU A 29 33.300 -3.141 -26.126 1.00 48.54 C ANISOU 230 CG GLU A 29 5881 6906 5654 329 777 666 C ATOM 231 CD GLU A 29 32.936 -4.387 -26.962 1.00 61.46 C ANISOU 231 CD GLU A 29 6996 8189 8166 690 1574 -1049 C ATOM 232 OE1 GLU A 29 33.092 -5.539 -26.452 1.00 75.47 O ANISOU 232 OE1 GLU A 29 9378 9572 9722 2533 2533 1594 O ATOM 233 OE2 GLU A 29 32.419 -4.248 -28.118 1.00 79.54 O ANISOU 233 OE2 GLU A 29 10017 12048 8155 -202 1280 2200 O ATOM 234 N GLY A 30 31.733 -4.818 -22.205 1.00 25.64 N ANISOU 234 N GLY A 30 2949 3464 3329 -147 368 326 N ATOM 235 CA GLY A 30 31.803 -4.807 -20.743 1.00 25.64 C ANISOU 235 CA GLY A 30 2987 3243 3510 -196 -176 -23 C ATOM 236 C GLY A 30 30.809 -5.824 -20.129 1.00 20.24 C ANISOU 236 C GLY A 30 2477 2630 2584 -114 173 4 C ATOM 237 O GLY A 30 30.250 -6.701 -20.832 1.00 22.51 O ANISOU 237 O GLY A 30 2878 2911 2761 32 75 -162 O ATOM 238 N ASP A 31 30.565 -5.698 -18.892 1.00 19.57 N ANISOU 238 N ASP A 31 2366 2501 2568 -134 -146 0 N ATOM 239 CA ASP A 31 29.639 -6.528 -18.149 1.00 18.46 C ANISOU 239 CA ASP A 31 2348 2265 2400 66 151 65 C ATOM 240 C ASP A 31 28.216 -6.124 -18.585 1.00 18.09 C ANISOU 240 C ASP A 31 2240 2199 2431 48 -209 -14 C ATOM 241 O ASP A 31 27.915 -4.962 -18.879 1.00 18.38 O ANISOU 241 O ASP A 31 2352 2257 2371 -106 -38 -57 O ATOM 242 CB ASP A 31 29.813 -6.479 -16.690 1.00 19.59 C ANISOU 242 CB ASP A 31 2354 2359 2727 42 -148 -132 C ATOM 243 CG ASP A 31 31.133 -7.157 -16.246 1.00 24.13 C ANISOU 243 CG ASP A 31 3017 3106 3043 210 -199 151 C ATOM 244 OD1 ASP A 31 31.381 -8.290 -16.788 1.00 26.68 O ANISOU 244 OD1 ASP A 31 3237 3310 3589 286 -223 -207 O ATOM 245 OD2 ASP A 31 31.704 -6.625 -15.377 1.00 26.64 O ANISOU 245 OD2 ASP A 31 3243 3342 3535 -117 -219 -22 O ATOM 246 N PRO A 32 27.275 -7.084 -18.710 1.00 17.28 N ANISOU 246 N PRO A 32 2099 2125 2341 61 -22 9 N ATOM 247 CA PRO A 32 26.016 -6.841 -19.305 1.00 16.41 C ANISOU 247 CA PRO A 32 2033 2041 2158 14 73 91 C ATOM 248 C PRO A 32 25.044 -6.093 -18.366 1.00 15.02 C ANISOU 248 C PRO A 32 1928 1922 1854 -39 27 -92 C ATOM 249 O PRO A 32 25.051 -6.217 -17.155 1.00 15.66 O ANISOU 249 O PRO A 32 1961 1951 2036 9 -17 89 O ATOM 250 CB PRO A 32 25.443 -8.198 -19.581 1.00 19.67 C ANISOU 250 CB PRO A 32 2357 2538 2576 -9 92 -401 C ATOM 251 CG PRO A 32 26.418 -9.099 -19.213 1.00 26.75 C ANISOU 251 CG PRO A 32 3573 2864 3726 -37 -398 102 C ATOM 252 CD PRO A 32 27.502 -8.520 -18.439 1.00 19.75 C ANISOU 252 CD PRO A 32 2434 2412 2657 11 -22 183 C ATOM 253 N ILE A 33 24.198 -5.324 -19.084 1.00 14.99 N ANISOU 253 N ILE A 33 1898 1871 1925 -41 55 45 N ATOM 254 CA ILE A 33 23.028 -4.741 -18.540 1.00 14.31 C ANISOU 254 CA ILE A 33 1803 1776 1858 50 -83 61 C ATOM 255 C ILE A 33 21.862 -5.198 -19.385 1.00 14.04 C ANISOU 255 C ILE A 33 1862 1680 1792 -15 -21 -23 C ATOM 256 O ILE A 33 21.842 -4.914 -20.576 1.00 14.98 O ANISOU 256 O ILE A 33 1917 1857 1916 26 -50 -16 O ATOM 257 CB ILE A 33 23.112 -3.176 -18.497 1.00 14.25 C ANISOU 257 CB ILE A 33 1808 1754 1852 -49 -9 -8 C ATOM 258 CG1 ILE A 33 24.450 -2.705 -17.888 1.00 16.61 C ANISOU 258 CG1 ILE A 33 2130 2070 2110 25 34 168 C ATOM 259 CG2 ILE A 33 21.839 -2.651 -17.836 1.00 15.41 C ANISOU 259 CG2 ILE A 33 2063 1847 1944 -16 45 -105 C ATOM 260 CD1 ILE A 33 24.678 -1.158 -18.104 1.00 16.41 C ANISOU 260 CD1 ILE A 33 2155 1965 2113 -134 -73 22 C ATOM 261 N VAL A 34 21.027 -6.043 -18.756 1.00 13.70 N ANISOU 261 N VAL A 34 1728 1804 1672 -30 -17 30 N ATOM 262 CA VAL A 34 20.074 -6.882 -19.454 1.00 13.54 C ANISOU 262 CA VAL A 34 1761 1679 1703 -72 63 -40 C ATOM 263 C VAL A 34 18.695 -6.345 -19.244 1.00 14.47 C ANISOU 263 C VAL A 34 1892 1691 1913 -30 -9 56 C ATOM 264 O VAL A 34 18.243 -6.400 -18.129 1.00 15.49 O ANISOU 264 O VAL A 34 2040 1904 1940 67 44 -48 O ATOM 265 CB VAL A 34 20.221 -8.375 -19.062 1.00 13.78 C ANISOU 265 CB VAL A 34 1760 1827 1648 -74 -92 209 C ATOM 266 CG1 VAL A 34 19.128 -9.197 -19.743 1.00 16.12 C ANISOU 266 CG1 VAL A 34 2134 1987 2002 -147 0 15 C ATOM 267 CG2 VAL A 34 21.567 -8.846 -19.401 1.00 16.55 C ANISOU 267 CG2 VAL A 34 2224 1983 2080 98 48 144 C ATOM 268 N PHE A 35 18.038 -5.823 -20.270 1.00 12.80 N ANISOU 268 N PHE A 35 1660 1615 1588 56 19 -49 N ATOM 269 CA PHE A 35 16.702 -5.259 -20.175 1.00 13.51 C ANISOU 269 CA PHE A 35 1648 1840 1645 -51 60 167 C ATOM 270 C PHE A 35 15.657 -6.193 -20.644 1.00 14.98 C ANISOU 270 C PHE A 35 1993 1881 1815 -56 32 -46 C ATOM 271 O PHE A 35 15.742 -6.642 -21.812 1.00 15.34 O ANISOU 271 O PHE A 35 1954 1970 1903 -134 40 -44 O ATOM 272 CB PHE A 35 16.626 -3.950 -21.065 1.00 15.32 C ANISOU 272 CB PHE A 35 1988 1862 1970 32 -3 39 C ATOM 273 CG PHE A 35 17.634 -2.859 -20.728 1.00 14.54 C ANISOU 273 CG PHE A 35 1811 1848 1865 80 58 69 C ATOM 274 CD1 PHE A 35 18.963 -2.969 -21.083 1.00 14.07 C ANISOU 274 CD1 PHE A 35 1786 1765 1793 -93 53 52 C ATOM 275 CD2 PHE A 35 17.252 -1.761 -20.019 1.00 15.24 C ANISOU 275 CD2 PHE A 35 1951 1862 1975 -34 -65 -9 C ATOM 276 CE1 PHE A 35 19.855 -1.968 -20.729 1.00 15.42 C ANISOU 276 CE1 PHE A 35 1948 1891 2017 -54 -54 32 C ATOM 277 CE2 PHE A 35 18.127 -0.747 -19.715 1.00 15.85 C ANISOU 277 CE2 PHE A 35 2017 1942 2064 50 -42 25 C ATOM 278 CZ PHE A 35 19.412 -0.868 -20.093 1.00 15.71 C ANISOU 278 CZ PHE A 35 2004 1971 1994 -81 84 52 C ATOM 279 N GLN A 36 14.678 -6.600 -19.825 1.00 13.11 N ANISOU 279 N GLN A 36 1733 1621 1627 4 -37 -115 N ATOM 280 CA GLN A 36 13.693 -7.549 -20.235 1.00 13.48 C ANISOU 280 CA GLN A 36 1707 1762 1652 -54 49 159 C ATOM 281 C GLN A 36 12.300 -7.054 -20.177 1.00 12.48 C ANISOU 281 C GLN A 36 1654 1464 1624 -50 34 84 C ATOM 282 O GLN A 36 11.767 -6.782 -19.068 1.00 13.31 O ANISOU 282 O GLN A 36 1752 1638 1665 47 48 19 O ATOM 283 CB GLN A 36 13.856 -8.858 -19.423 1.00 13.87 C ANISOU 283 CB GLN A 36 1879 1618 1771 58 -67 25 C ATOM 284 CG GLN A 36 13.080 -10.004 -20.078 1.00 14.34 C ANISOU 284 CG GLN A 36 1877 1780 1790 -16 17 -16 C ATOM 285 CD GLN A 36 13.415 -10.199 -21.547 1.00 13.35 C ANISOU 285 CD GLN A 36 1673 1649 1751 -34 -6 23 C ATOM 286 OE1 GLN A 36 14.567 -10.503 -21.807 1.00 14.06 O ANISOU 286 OE1 GLN A 36 1815 1696 1831 60 77 30 O ATOM 287 NE2 GLN A 36 12.458 -10.017 -22.452 1.00 14.02 N ANISOU 287 NE2 GLN A 36 1850 1674 1801 44 -94 -103 N ATOM 288 N HIS A 37 11.647 -6.954 -21.317 1.00 11.79 N ANISOU 288 N HIS A 37 1505 1474 1501 0 78 9 N ATOM 289 CA HIS A 37 10.269 -6.647 -21.489 1.00 12.95 C ANISOU 289 CA HIS A 37 1634 1623 1664 -36 -62 -25 C ATOM 290 C HIS A 37 9.350 -7.778 -21.068 1.00 14.38 C ANISOU 290 C HIS A 37 1889 1785 1788 34 38 -96 C ATOM 291 O HIS A 37 9.770 -8.941 -20.969 1.00 14.61 O ANISOU 291 O HIS A 37 1875 1827 1849 21 2 18 O ATOM 292 CB HIS A 37 9.973 -6.261 -22.970 1.00 13.21 C ANISOU 292 CB HIS A 37 1645 1659 1714 -15 59 -50 C ATOM 293 CG HIS A 37 9.830 -7.459 -23.878 1.00 12.69 C ANISOU 293 CG HIS A 37 1700 1599 1522 -53 89 0 C ATOM 294 ND1 HIS A 37 8.647 -8.102 -24.058 1.00 12.56 N ANISOU 294 ND1 HIS A 37 1616 1631 1525 67 -68 4 N ATOM 295 CD2 HIS A 37 10.770 -8.126 -24.600 1.00 13.37 C ANISOU 295 CD2 HIS A 37 1645 1651 1785 -24 -38 70 C ATOM 296 CE1 HIS A 37 8.830 -9.102 -24.888 1.00 11.84 C ANISOU 296 CE1 HIS A 37 1527 1472 1499 33 -30 69 C ATOM 297 NE2 HIS A 37 10.128 -9.194 -25.205 1.00 12.70 N ANISOU 297 NE2 HIS A 37 1614 1579 1633 -43 17 65 N ATOM 298 N GLY A 38 8.071 -7.439 -21.010 1.00 13.96 N ANISOU 298 N GLY A 38 1764 1769 1770 -94 -62 14 N ATOM 299 CA GLY A 38 6.946 -8.341 -20.799 1.00 14.38 C ANISOU 299 CA GLY A 38 1930 1722 1810 -52 1 -57 C ATOM 300 C GLY A 38 5.856 -8.269 -21.763 1.00 13.91 C ANISOU 300 C GLY A 38 1806 1650 1826 -51 -42 -33 C ATOM 301 O GLY A 38 6.078 -8.025 -22.966 1.00 15.32 O ANISOU 301 O GLY A 38 1878 2004 1938 -61 68 -2 O ATOM 302 N ASN A 39 4.615 -8.424 -21.317 1.00 15.29 N ANISOU 302 N ASN A 39 2000 1838 1971 -22 17 -38 N ATOM 303 CA ASN A 39 3.505 -8.491 -22.176 1.00 13.96 C ANISOU 303 CA ASN A 39 1786 1690 1825 22 18 73 C ATOM 304 C ASN A 39 2.895 -7.080 -22.418 1.00 17.32 C ANISOU 304 C ASN A 39 2250 2173 2157 103 120 77 C ATOM 305 O ASN A 39 2.702 -6.382 -21.388 1.00 21.07 O ANISOU 305 O ASN A 39 3032 2437 2534 135 -158 -21 O ATOM 306 CB ASN A 39 2.437 -9.473 -21.602 1.00 15.46 C ANISOU 306 CB ASN A 39 1897 1970 2004 -47 111 45 C ATOM 307 CG ASN A 39 1.315 -9.810 -22.583 1.00 14.71 C ANISOU 307 CG ASN A 39 1864 1882 1843 46 88 153 C ATOM 308 OD1 ASN A 39 1.604 -10.001 -23.802 1.00 16.67 O ANISOU 308 OD1 ASN A 39 2134 2089 2110 -93 1 -139 O ATOM 309 ND2 ASN A 39 0.074 -10.005 -22.059 1.00 15.53 N ANISOU 309 ND2 ASN A 39 1891 1908 2101 1 41 -11 N ATOM 310 N PRO A 40 2.402 -6.702 -23.608 1.00 15.10 N ANISOU 310 N PRO A 40 1856 1962 1920 27 31 86 N ATOM 311 CA PRO A 40 2.539 -7.305 -24.879 1.00 13.67 C ANISOU 311 CA PRO A 40 1676 1699 1817 -28 -154 -24 C ATOM 312 C PRO A 40 3.605 -6.521 -25.689 1.00 16.59 C ANISOU 312 C PRO A 40 2131 2147 2024 -87 37 3 C ATOM 313 O PRO A 40 3.360 -6.106 -26.813 1.00 16.00 O ANISOU 313 O PRO A 40 2028 1957 2091 -27 -59 9 O ATOM 314 CB PRO A 40 1.146 -7.079 -25.517 1.00 16.78 C ANISOU 314 CB PRO A 40 2057 2158 2160 -80 -116 -77 C ATOM 315 CG PRO A 40 0.852 -5.641 -25.027 1.00 17.03 C ANISOU 315 CG PRO A 40 2040 2162 2269 119 106 139 C ATOM 316 CD PRO A 40 1.472 -5.539 -23.667 1.00 15.66 C ANISOU 316 CD PRO A 40 1980 1885 2082 -46 133 -43 C ATOM 317 N THR A 41 4.805 -6.335 -25.086 1.00 14.36 N ANISOU 317 N THR A 41 1845 1816 1795 6 -94 114 N ATOM 318 CA THR A 41 5.797 -5.438 -25.583 1.00 14.42 C ANISOU 318 CA THR A 41 1743 1876 1857 15 -20 1 C ATOM 319 C THR A 41 6.958 -6.217 -26.181 1.00 15.10 C ANISOU 319 C THR A 41 1860 1927 1948 19 -60 -81 C ATOM 320 O THR A 41 6.754 -7.352 -26.618 1.00 15.36 O ANISOU 320 O THR A 41 1966 1905 1964 35 95 -62 O ATOM 321 CB THR A 41 6.246 -4.444 -24.505 1.00 15.33 C ANISOU 321 CB THR A 41 1924 1913 1985 86 62 -32 C ATOM 322 OG1 THR A 41 6.853 -5.142 -23.427 1.00 16.34 O ANISOU 322 OG1 THR A 41 2115 2070 2024 -10 -30 -69 O ATOM 323 CG2 THR A 41 5.058 -3.595 -24.014 1.00 16.27 C ANISOU 323 CG2 THR A 41 2116 1943 2120 14 22 130 C ATOM 324 N SER A 42 8.112 -5.628 -26.336 1.00 13.74 N ANISOU 324 N SER A 42 1828 1581 1809 19 110 -49 N ATOM 325 CA SER A 42 9.272 -6.196 -26.930 1.00 13.34 C ANISOU 325 CA SER A 42 1721 1719 1627 7 31 115 C ATOM 326 C SER A 42 10.425 -5.403 -26.465 1.00 13.96 C ANISOU 326 C SER A 42 1822 1823 1659 -105 84 54 C ATOM 327 O SER A 42 10.292 -4.435 -25.632 1.00 13.79 O ANISOU 327 O SER A 42 1800 1700 1737 0 90 -5 O ATOM 328 CB SER A 42 9.288 -6.225 -28.498 1.00 14.49 C ANISOU 328 CB SER A 42 1889 1761 1853 -2 -126 -29 C ATOM 329 OG SER A 42 9.342 -4.857 -28.973 1.00 15.22 O ANISOU 329 OG SER A 42 2012 1853 1917 -37 -16 91 O ATOM 330 N SER A 43 11.644 -5.633 -26.999 1.00 12.96 N ANISOU 330 N SER A 43 1654 1658 1609 29 36 -55 N ATOM 331 CA SER A 43 12.804 -4.828 -26.724 1.00 12.60 C ANISOU 331 CA SER A 43 1669 1607 1509 -42 -10 125 C ATOM 332 C SER A 43 12.522 -3.307 -26.983 1.00 13.45 C ANISOU 332 C SER A 43 1652 1734 1721 3 16 14 C ATOM 333 O SER A 43 13.190 -2.506 -26.333 1.00 13.98 O ANISOU 333 O SER A 43 1851 1681 1778 -1 -12 43 O ATOM 334 CB SER A 43 14.006 -5.261 -27.568 1.00 13.11 C ANISOU 334 CB SER A 43 1655 1585 1741 -37 -109 78 C ATOM 335 OG SER A 43 13.677 -5.272 -28.919 1.00 14.41 O ANISOU 335 OG SER A 43 1975 1726 1772 82 130 -47 O ATOM 336 N TYR A 44 11.599 -3.004 -27.854 1.00 13.48 N ANISOU 336 N TYR A 44 1778 1628 1716 -53 -43 65 N ATOM 337 CA TYR A 44 11.253 -1.629 -28.171 1.00 13.42 C ANISOU 337 CA TYR A 44 1749 1650 1699 -12 -54 55 C ATOM 338 C TYR A 44 10.875 -0.769 -26.959 1.00 13.04 C ANISOU 338 C TYR A 44 1694 1598 1660 83 -9 24 C ATOM 339 O TYR A 44 11.064 0.377 -26.941 1.00 14.03 O ANISOU 339 O TYR A 44 1849 1664 1816 -68 13 23 O ATOM 340 CB TYR A 44 10.142 -1.659 -29.221 1.00 16.01 C ANISOU 340 CB TYR A 44 2071 1961 2049 -129 -68 94 C ATOM 341 CG TYR A 44 9.688 -0.368 -29.815 1.00 14.78 C ANISOU 341 CG TYR A 44 1821 1898 1895 25 -150 55 C ATOM 342 CD1 TYR A 44 10.449 0.275 -30.744 1.00 16.58 C ANISOU 342 CD1 TYR A 44 2097 2163 2038 51 -64 82 C ATOM 343 CD2 TYR A 44 8.483 0.156 -29.494 1.00 15.28 C ANISOU 343 CD2 TYR A 44 2083 1819 1903 66 25 101 C ATOM 344 CE1 TYR A 44 10.032 1.454 -31.308 1.00 16.91 C ANISOU 344 CE1 TYR A 44 2241 2044 2139 79 -5 109 C ATOM 345 CE2 TYR A 44 8.057 1.334 -30.058 1.00 16.82 C ANISOU 345 CE2 TYR A 44 2179 2032 2177 213 50 102 C ATOM 346 CZ TYR A 44 8.833 1.970 -30.964 1.00 18.41 C ANISOU 346 CZ TYR A 44 2377 2262 2354 112 106 130 C ATOM 347 OH TYR A 44 8.383 3.138 -31.521 1.00 18.25 O ANISOU 347 OH TYR A 44 2526 2173 2232 250 -39 65 O ATOM 348 N LEU A 45 10.305 -1.404 -25.974 1.00 13.32 N ANISOU 348 N LEU A 45 1795 1583 1683 -37 40 -108 N ATOM 349 CA LEU A 45 9.913 -0.779 -24.761 1.00 13.37 C ANISOU 349 CA LEU A 45 1793 1713 1573 66 -34 55 C ATOM 350 C LEU A 45 11.008 0.018 -24.152 1.00 14.03 C ANISOU 350 C LEU A 45 1816 1687 1826 -66 63 78 C ATOM 351 O LEU A 45 10.765 1.045 -23.463 1.00 14.78 O ANISOU 351 O LEU A 45 1938 1823 1855 20 33 -67 O ATOM 352 CB LEU A 45 9.419 -1.829 -23.771 1.00 14.68 C ANISOU 352 CB LEU A 45 1996 1754 1825 -173 127 -89 C ATOM 353 CG LEU A 45 8.848 -1.277 -22.429 1.00 16.00 C ANISOU 353 CG LEU A 45 2208 2007 1863 -58 17 -85 C ATOM 354 CD1 LEU A 45 7.625 -0.412 -22.618 1.00 17.34 C ANISOU 354 CD1 LEU A 45 2195 2211 2183 -102 74 -202 C ATOM 355 CD2 LEU A 45 8.610 -2.479 -21.499 1.00 18.96 C ANISOU 355 CD2 LEU A 45 2599 2246 2358 -91 148 -57 C ATOM 356 N TRP A 46 12.249 -0.387 -24.323 1.00 13.45 N ANISOU 356 N TRP A 46 1741 1700 1670 1 1 -72 N ATOM 357 CA TRP A 46 13.369 0.172 -23.671 1.00 14.62 C ANISOU 357 CA TRP A 46 1797 1885 1871 87 -33 6 C ATOM 358 C TRP A 46 14.182 1.205 -24.474 1.00 15.56 C ANISOU 358 C TRP A 46 1968 1930 2013 24 -20 -39 C ATOM 359 O TRP A 46 15.255 1.602 -24.071 1.00 14.34 O ANISOU 359 O TRP A 46 1842 1686 1918 43 -12 31 O ATOM 360 CB TRP A 46 14.379 -0.939 -23.199 1.00 14.29 C ANISOU 360 CB TRP A 46 1908 1714 1807 30 64 -38 C ATOM 361 CG TRP A 46 13.750 -2.004 -22.331 1.00 13.27 C ANISOU 361 CG TRP A 46 1706 1660 1674 44 48 -43 C ATOM 362 CD1 TRP A 46 13.400 -3.235 -22.710 1.00 14.01 C ANISOU 362 CD1 TRP A 46 1799 1777 1747 7 -28 -52 C ATOM 363 CD2 TRP A 46 13.373 -1.853 -20.959 1.00 13.96 C ANISOU 363 CD2 TRP A 46 1824 1778 1702 -28 19 61 C ATOM 364 NE1 TRP A 46 12.888 -3.896 -21.631 1.00 14.58 N ANISOU 364 NE1 TRP A 46 1973 1707 1857 -36 29 -27 N ATOM 365 CE2 TRP A 46 12.891 -3.090 -20.522 1.00 13.66 C ANISOU 365 CE2 TRP A 46 1770 1735 1685 -56 -18 -20 C ATOM 366 CE3 TRP A 46 13.504 -0.848 -20.049 1.00 12.97 C ANISOU 366 CE3 TRP A 46 1686 1552 1688 -77 64 70 C ATOM 367 CZ2 TRP A 46 12.484 -3.296 -19.225 1.00 13.37 C ANISOU 367 CZ2 TRP A 46 1728 1636 1715 -60 107 -34 C ATOM 368 CZ3 TRP A 46 13.153 -1.051 -18.766 1.00 14.42 C ANISOU 368 CZ3 TRP A 46 1882 1788 1808 -108 -5 -110 C ATOM 369 CH2 TRP A 46 12.644 -2.310 -18.320 1.00 13.92 C ANISOU 369 CH2 TRP A 46 1908 1686 1693 -51 35 2 C ATOM 370 N ARG A 47 13.640 1.551 -25.632 1.00 15.07 N ANISOU 370 N ARG A 47 1886 1908 1928 -138 24 93 N ATOM 371 CA ARG A 47 14.463 2.311 -26.636 1.00 13.86 C ANISOU 371 CA ARG A 47 1851 1634 1778 46 109 55 C ATOM 372 C ARG A 47 14.877 3.694 -26.146 1.00 15.17 C ANISOU 372 C ARG A 47 1904 1894 1966 -45 106 -101 C ATOM 373 O ARG A 47 15.949 4.110 -26.607 1.00 16.59 O ANISOU 373 O ARG A 47 2103 1934 2265 -138 104 -44 O ATOM 374 CB ARG A 47 13.629 2.471 -27.902 1.00 14.27 C ANISOU 374 CB ARG A 47 1783 1829 1809 -150 -1 24 C ATOM 375 CG ARG A 47 12.430 3.396 -27.813 1.00 15.95 C ANISOU 375 CG ARG A 47 2165 1956 1939 -15 26 121 C ATOM 376 CD ARG A 47 11.413 3.218 -28.897 1.00 16.03 C ANISOU 376 CD ARG A 47 2087 1983 2021 146 19 82 C ATOM 377 NE ARG A 47 10.241 4.041 -28.743 1.00 15.58 N ANISOU 377 NE ARG A 47 2027 1971 1921 191 -15 183 N ATOM 378 CZ ARG A 47 9.322 3.891 -27.807 1.00 15.92 C ANISOU 378 CZ ARG A 47 1914 2049 2084 99 136 92 C ATOM 379 NH1 ARG A 47 9.264 2.796 -27.051 1.00 16.06 N ANISOU 379 NH1 ARG A 47 2074 2017 2011 175 189 -16 N ATOM 380 NH2 ARG A 47 8.382 4.771 -27.657 1.00 18.71 N ANISOU 380 NH2 ARG A 47 2494 2268 2346 206 124 141 N ATOM 381 N ASN A 48 14.092 4.300 -25.243 1.00 14.59 N ANISOU 381 N ASN A 48 1929 1722 1893 -44 40 14 N ATOM 382 CA ASN A 48 14.525 5.660 -24.725 1.00 14.72 C ANISOU 382 CA ASN A 48 1862 1835 1896 -157 136 -21 C ATOM 383 C ASN A 48 15.194 5.613 -23.409 1.00 16.63 C ANISOU 383 C ASN A 48 2191 2040 2085 11 -93 -26 C ATOM 384 O ASN A 48 15.540 6.604 -22.790 1.00 18.01 O ANISOU 384 O ASN A 48 2348 2150 2345 -58 -12 -34 O ATOM 385 CB ASN A 48 13.269 6.553 -24.769 1.00 15.02 C ANISOU 385 CB ASN A 48 1954 1685 2064 -180 -137 -43 C ATOM 386 CG ASN A 48 12.754 6.794 -26.102 1.00 15.43 C ANISOU 386 CG ASN A 48 2019 1722 2122 78 58 32 C ATOM 387 OD1 ASN A 48 13.571 7.047 -27.020 1.00 19.68 O ANISOU 387 OD1 ASN A 48 2634 2374 2468 56 158 136 O ATOM 388 ND2 ASN A 48 11.473 6.724 -26.277 1.00 16.66 N ANISOU 388 ND2 ASN A 48 2183 1786 2361 -36 -16 172 N ATOM 389 N ILE A 49 15.375 4.383 -22.842 1.00 15.36 N ANISOU 389 N ILE A 49 2021 1898 1914 -8 -39 -14 N ATOM 390 CA ILE A 49 16.089 4.105 -21.630 1.00 15.91 C ANISOU 390 CA ILE A 49 2187 1877 1979 -49 -8 -81 C ATOM 391 C ILE A 49 17.474 3.711 -21.870 1.00 15.05 C ANISOU 391 C ILE A 49 1954 1959 1803 4 -80 81 C ATOM 392 O ILE A 49 18.458 4.183 -21.267 1.00 15.56 O ANISOU 392 O ILE A 49 1970 1878 2063 -89 7 -1 O ATOM 393 CB ILE A 49 15.301 3.153 -20.768 1.00 15.12 C ANISOU 393 CB ILE A 49 1938 1919 1885 -46 4 -59 C ATOM 394 CG1 ILE A 49 13.912 3.958 -20.319 1.00 19.68 C ANISOU 394 CG1 ILE A 49 2435 2582 2460 -36 -63 27 C ATOM 395 CG2 ILE A 49 16.071 2.767 -19.538 1.00 15.93 C ANISOU 395 CG2 ILE A 49 2052 1844 2156 -40 8 -17 C ATOM 396 CD1 ILE A 49 12.967 2.970 -19.752 1.00 24.09 C ANISOU 396 CD1 ILE A 49 2967 2957 3230 -51 -112 -114 C ATOM 397 N MET A 50 17.641 2.721 -22.781 1.00 15.84 N ANISOU 397 N MET A 50 1938 2012 2066 -29 17 -76 N ATOM 398 CA MET A 50 18.989 2.179 -23.106 1.00 14.86 C ANISOU 398 CA MET A 50 1863 1843 1939 59 31 32 C ATOM 399 C MET A 50 20.091 3.221 -23.470 1.00 13.88 C ANISOU 399 C MET A 50 1798 1734 1741 49 -23 -36 C ATOM 400 O MET A 50 21.215 3.019 -22.991 1.00 16.90 O ANISOU 400 O MET A 50 2051 2151 2219 -1 -1 -185 O ATOM 401 CB MET A 50 18.914 1.052 -24.192 1.00 15.16 C ANISOU 401 CB MET A 50 1868 1914 1975 27 38 77 C ATOM 402 CG MET A 50 18.210 -0.108 -23.637 1.00 16.62 C ANISOU 402 CG MET A 50 2153 2022 2139 -42 51 -68 C ATOM 403 SD MET A 50 17.864 -1.450 -24.845 1.00 16.50 S ANISOU 403 SD MET A 50 2106 1998 2163 -14 -41 -50 S ATOM 404 CE MET A 50 19.508 -2.119 -25.015 1.00 16.61 C ANISOU 404 CE MET A 50 2170 2024 2117 -10 -35 -241 C ATOM 405 N PRO A 51 19.768 4.320 -24.148 1.00 16.26 N ANISOU 405 N PRO A 51 2020 1963 2194 -179 0 -18 N ATOM 406 CA PRO A 51 20.884 5.286 -24.464 1.00 17.32 C ANISOU 406 CA PRO A 51 1976 2239 2362 -145 144 -29 C ATOM 407 C PRO A 51 21.534 5.883 -23.213 1.00 17.30 C ANISOU 407 C PRO A 51 2242 2196 2134 113 158 -145 C ATOM 408 O PRO A 51 22.718 6.155 -23.252 1.00 19.49 O ANISOU 408 O PRO A 51 2463 2456 2486 -200 3 -157 O ATOM 409 CB PRO A 51 20.171 6.386 -25.153 1.00 18.41 C ANISOU 409 CB PRO A 51 2311 2350 2331 -62 78 101 C ATOM 410 CG PRO A 51 18.952 5.716 -25.872 1.00 22.05 C ANISOU 410 CG PRO A 51 2769 2837 2770 -20 59 226 C ATOM 411 CD PRO A 51 18.557 4.639 -24.802 1.00 17.50 C ANISOU 411 CD PRO A 51 2347 2069 2229 128 -88 96 C ATOM 412 N HIS A 52 20.849 5.906 -22.065 1.00 16.14 N ANISOU 412 N HIS A 52 2113 2017 2000 -170 26 -36 N ATOM 413 CA HIS A 52 21.443 6.413 -20.830 1.00 17.60 C ANISOU 413 CA HIS A 52 2327 2071 2290 -236 -9 135 C ATOM 414 C HIS A 52 22.422 5.496 -20.226 1.00 17.64 C ANISOU 414 C HIS A 52 2180 2227 2293 -66 -134 88 C ATOM 415 O HIS A 52 23.127 5.888 -19.292 1.00 19.12 O ANISOU 415 O HIS A 52 2574 2301 2389 12 -108 -68 O ATOM 416 CB HIS A 52 20.311 6.671 -19.852 1.00 17.73 C ANISOU 416 CB HIS A 52 2269 2142 2324 -55 -30 -197 C ATOM 417 CG HIS A 52 19.351 7.723 -20.229 1.00 18.74 C ANISOU 417 CG HIS A 52 2393 2424 2303 -24 129 -13 C ATOM 418 ND1 HIS A 52 19.748 9.051 -20.074 1.00 19.26 N ANISOU 418 ND1 HIS A 52 2572 2240 2503 92 158 -153 N ATOM 419 CD2 HIS A 52 18.117 7.726 -20.754 1.00 20.39 C ANISOU 419 CD2 HIS A 52 2732 2424 2592 29 -25 -129 C ATOM 420 CE1 HIS A 52 18.734 9.800 -20.498 1.00 20.34 C ANISOU 420 CE1 HIS A 52 2630 2561 2535 38 -130 26 C ATOM 421 NE2 HIS A 52 17.746 9.064 -20.935 1.00 22.25 N ANISOU 421 NE2 HIS A 52 2847 2777 2827 54 110 27 N ATOM 422 N LEU A 53 22.588 4.254 -20.762 1.00 17.00 N ANISOU 422 N LEU A 53 2190 2137 2131 55 -186 -28 N ATOM 423 CA LEU A 53 23.549 3.331 -20.264 1.00 16.49 C ANISOU 423 CA LEU A 53 2113 1982 2167 -143 -26 126 C ATOM 424 C LEU A 53 24.719 3.116 -21.187 1.00 16.82 C ANISOU 424 C LEU A 53 2190 2026 2174 -18 -76 -137 C ATOM 425 O LEU A 53 25.607 2.320 -20.884 1.00 18.44 O ANISOU 425 O LEU A 53 2330 2278 2399 -25 -96 3 O ATOM 426 CB LEU A 53 22.852 1.959 -19.913 1.00 17.06 C ANISOU 426 CB LEU A 53 2202 2034 2246 -101 0 -85 C ATOM 427 CG LEU A 53 22.038 1.928 -18.689 1.00 16.45 C ANISOU 427 CG LEU A 53 2157 2025 2069 -84 -39 138 C ATOM 428 CD1 LEU A 53 22.837 2.374 -17.428 1.00 19.52 C ANISOU 428 CD1 LEU A 53 2390 2598 2426 35 48 24 C ATOM 429 CD2 LEU A 53 20.702 2.628 -18.779 1.00 18.40 C ANISOU 429 CD2 LEU A 53 2334 2330 2325 -108 198 -234 C ATOM 430 N GLU A 54 24.809 3.855 -22.317 1.00 17.65 N ANISOU 430 N GLU A 54 2216 2199 2291 22 12 2 N ATOM 431 CA GLU A 54 25.902 3.783 -23.218 1.00 19.00 C ANISOU 431 CA GLU A 54 2506 2182 2532 -71 38 -80 C ATOM 432 C GLU A 54 27.217 3.981 -22.521 1.00 19.85 C ANISOU 432 C GLU A 54 2520 2536 2486 95 123 -26 C ATOM 433 O GLU A 54 27.432 4.928 -21.708 1.00 20.68 O ANISOU 433 O GLU A 54 2610 2577 2668 -191 66 -3 O ATOM 434 CB GLU A 54 25.706 4.753 -24.327 1.00 21.90 C ANISOU 434 CB GLU A 54 2857 2832 2630 40 13 -65 C ATOM 435 CG GLU A 54 24.764 4.143 -25.368 1.00 27.50 C ANISOU 435 CG GLU A 54 3370 3555 3523 -94 -443 2 C ATOM 436 CD GLU A 54 24.339 5.072 -26.448 1.00 39.18 C ANISOU 436 CD GLU A 54 4703 5213 4971 -406 -439 1291 C ATOM 437 OE1 GLU A 54 24.994 6.092 -26.584 1.00 39.85 O ANISOU 437 OE1 GLU A 54 4936 4752 5451 -446 -680 523 O ATOM 438 OE2 GLU A 54 23.247 4.836 -27.094 1.00 31.21 O ANISOU 438 OE2 GLU A 54 3936 4337 3583 -821 -186 265 O ATOM 439 N GLY A 55 28.137 3.094 -22.784 1.00 18.55 N ANISOU 439 N GLY A 55 2374 2257 2414 104 -8 13 N ATOM 440 CA GLY A 55 29.493 3.121 -22.183 1.00 20.23 C ANISOU 440 CA GLY A 55 2520 2482 2684 -85 -188 -74 C ATOM 441 C GLY A 55 29.585 2.617 -20.785 1.00 20.40 C ANISOU 441 C GLY A 55 2580 2488 2681 85 71 -35 C ATOM 442 O GLY A 55 30.660 2.559 -20.162 1.00 23.75 O ANISOU 442 O GLY A 55 2797 3061 3166 -164 -69 15 O ATOM 443 N LEU A 56 28.447 2.136 -20.170 1.00 17.54 N ANISOU 443 N LEU A 56 2268 2113 2281 -99 97 -98 N ATOM 444 CA LEU A 56 28.494 1.633 -18.877 1.00 17.31 C ANISOU 444 CA LEU A 56 2246 1954 2376 -162 -124 -44 C ATOM 445 C LEU A 56 28.427 0.046 -18.777 1.00 17.50 C ANISOU 445 C LEU A 56 2371 2053 2226 -106 -120 43 C ATOM 446 O LEU A 56 28.558 -0.467 -17.701 1.00 20.49 O ANISOU 446 O LEU A 56 2685 2473 2625 -179 -30 -74 O ATOM 447 CB LEU A 56 27.382 2.193 -18.027 1.00 17.89 C ANISOU 447 CB LEU A 56 2303 2143 2350 -34 93 61 C ATOM 448 CG LEU A 56 27.421 3.742 -17.818 1.00 21.63 C ANISOU 448 CG LEU A 56 2642 2669 2905 -100 187 139 C ATOM 449 CD1 LEU A 56 26.232 4.233 -17.042 1.00 21.26 C ANISOU 449 CD1 LEU A 56 2771 2592 2713 135 -122 -345 C ATOM 450 CD2 LEU A 56 28.733 4.094 -17.165 1.00 25.12 C ANISOU 450 CD2 LEU A 56 3133 2931 3480 9 -99 -547 C ATOM 451 N GLY A 57 28.269 -0.474 -19.979 1.00 17.96 N ANISOU 451 N GLY A 57 2370 2103 2348 -10 -110 -124 N ATOM 452 CA GLY A 57 28.198 -1.986 -20.029 1.00 17.65 C ANISOU 452 CA GLY A 57 2276 2111 2317 13 -179 172 C ATOM 453 C GLY A 57 27.750 -2.378 -21.401 1.00 16.94 C ANISOU 453 C GLY A 57 2075 2139 2221 -70 41 -76 C ATOM 454 O GLY A 57 27.489 -1.594 -22.309 1.00 17.88 O ANISOU 454 O GLY A 57 2273 2188 2334 -61 -64 78 O ATOM 455 N ARG A 58 27.618 -3.685 -21.546 1.00 16.24 N ANISOU 455 N ARG A 58 2089 1978 2101 22 -60 -9 N ATOM 456 CA ARG A 58 27.129 -4.343 -22.738 1.00 16.38 C ANISOU 456 CA ARG A 58 2072 2068 2084 49 -41 102 C ATOM 457 C ARG A 58 25.603 -4.359 -22.602 1.00 15.36 C ANISOU 457 C ARG A 58 1963 1935 1935 -52 9 -25 C ATOM 458 O ARG A 58 25.072 -4.933 -21.717 1.00 17.36 O ANISOU 458 O ARG A 58 2235 2158 2199 -3 75 -3 O ATOM 459 CB ARG A 58 27.737 -5.738 -22.809 1.00 18.94 C ANISOU 459 CB ARG A 58 2422 2374 2400 53 67 -129 C ATOM 460 CG ARG A 58 27.196 -6.623 -23.895 1.00 17.24 C ANISOU 460 CG ARG A 58 2226 2056 2268 -75 -19 -23 C ATOM 461 CD ARG A 58 27.709 -8.043 -23.734 1.00 17.45 C ANISOU 461 CD ARG A 58 2117 2210 2300 140 -65 -16 C ATOM 462 NE ARG A 58 27.128 -8.923 -24.720 1.00 17.53 N ANISOU 462 NE ARG A 58 2295 2074 2290 -9 66 4 N ATOM 463 CZ ARG A 58 27.139 -10.234 -24.614 1.00 17.59 C ANISOU 463 CZ ARG A 58 2198 2292 2190 16 92 31 C ATOM 464 NH1 ARG A 58 27.668 -10.781 -23.572 1.00 19.57 N ANISOU 464 NH1 ARG A 58 2427 2401 2605 90 10 -71 N ATOM 465 NH2 ARG A 58 26.595 -10.974 -25.532 1.00 18.54 N ANISOU 465 NH2 ARG A 58 2313 2233 2496 2 47 -103 N ATOM 466 N LEU A 59 24.948 -3.686 -23.512 1.00 14.70 N ANISOU 466 N LEU A 59 1884 1793 1907 -56 58 -32 N ATOM 467 CA LEU A 59 23.491 -3.450 -23.391 1.00 15.58 C ANISOU 467 CA LEU A 59 1961 1920 2035 -71 12 -19 C ATOM 468 C LEU A 59 22.756 -4.489 -24.227 1.00 17.20 C ANISOU 468 C LEU A 59 2381 2101 2050 -205 140 -46 C ATOM 469 O LEU A 59 22.911 -4.547 -25.404 1.00 17.71 O ANISOU 469 O LEU A 59 2391 2086 2250 -287 41 -51 O ATOM 470 CB LEU A 59 23.175 -2.024 -23.900 1.00 15.60 C ANISOU 470 CB LEU A 59 1883 2088 1954 -56 -29 193 C ATOM 471 CG LEU A 59 24.009 -0.890 -23.276 1.00 16.46 C ANISOU 471 CG LEU A 59 2149 2021 2083 3 101 4 C ATOM 472 CD1 LEU A 59 23.455 0.437 -23.845 1.00 18.34 C ANISOU 472 CD1 LEU A 59 2352 2222 2393 -58 -64 -44 C ATOM 473 CD2 LEU A 59 24.121 -0.911 -21.823 1.00 17.06 C ANISOU 473 CD2 LEU A 59 2218 2030 2231 -66 -23 -74 C ATOM 474 N ILE A 60 21.897 -5.275 -23.522 1.00 14.61 N ANISOU 474 N ILE A 60 1869 1799 1882 -101 52 -99 N ATOM 475 CA ILE A 60 21.211 -6.441 -24.115 1.00 14.33 C ANISOU 475 CA ILE A 60 1905 1770 1768 -10 35 -38 C ATOM 476 C ILE A 60 19.752 -6.271 -23.896 1.00 14.28 C ANISOU 476 C ILE A 60 1845 1740 1841 -102 -59 79 C ATOM 477 O ILE A 60 19.292 -5.933 -22.779 1.00 15.23 O ANISOU 477 O ILE A 60 1970 1903 1912 -85 32 -49 O ATOM 478 CB ILE A 60 21.711 -7.669 -23.486 1.00 15.75 C ANISOU 478 CB ILE A 60 1965 1963 2053 -66 -113 -44 C ATOM 479 CG1 ILE A 60 23.197 -7.910 -23.842 1.00 20.24 C ANISOU 479 CG1 ILE A 60 2447 2462 2779 -102 191 129 C ATOM 480 CG2 ILE A 60 20.850 -8.892 -23.925 1.00 16.82 C ANISOU 480 CG2 ILE A 60 2205 1969 2216 -73 -152 -145 C ATOM 481 CD1 ILE A 60 23.789 -9.039 -23.158 1.00 21.86 C ANISOU 481 CD1 ILE A 60 2710 2847 2747 -168 18 87 C ATOM 482 N ALA A 61 18.942 -6.472 -24.927 1.00 13.19 N ANISOU 482 N ALA A 61 1739 1622 1650 -140 31 25 N ATOM 483 CA ALA A 61 17.481 -6.480 -24.786 1.00 13.18 C ANISOU 483 CA ALA A 61 1738 1636 1632 61 -31 -3 C ATOM 484 C ALA A 61 16.915 -7.485 -25.731 1.00 13.43 C ANISOU 484 C ALA A 61 1819 1627 1654 -8 107 -66 C ATOM 485 O ALA A 61 16.960 -7.322 -26.995 1.00 14.43 O ANISOU 485 O ALA A 61 1906 1789 1784 -58 25 -29 O ATOM 486 CB ALA A 61 16.877 -5.117 -25.037 1.00 14.60 C ANISOU 486 CB ALA A 61 1954 1749 1843 -48 76 -1 C ATOM 487 N CYS A 62 16.378 -8.557 -25.160 1.00 13.16 N ANISOU 487 N CYS A 62 1773 1640 1585 -132 182 -115 N ATOM 488 CA CYS A 62 15.918 -9.690 -25.914 1.00 12.92 C ANISOU 488 CA CYS A 62 1698 1563 1646 10 -28 -88 C ATOM 489 C CYS A 62 14.470 -9.617 -26.174 1.00 12.81 C ANISOU 489 C CYS A 62 1631 1531 1705 -58 24 12 C ATOM 490 O CYS A 62 13.684 -9.248 -25.269 1.00 14.88 O ANISOU 490 O CYS A 62 1882 1922 1848 -91 64 -1 O ATOM 491 CB CYS A 62 16.219 -11.039 -25.233 1.00 12.69 C ANISOU 491 CB CYS A 62 1674 1625 1521 -140 -54 59 C ATOM 492 SG CYS A 62 17.978 -11.298 -24.906 1.00 15.21 S ANISOU 492 SG CYS A 62 1964 1866 1946 46 -10 7 S ATOM 493 N ASP A 63 14.004 -10.099 -27.340 1.00 13.33 N ANISOU 493 N ASP A 63 1707 1657 1699 25 -15 -5 N ATOM 494 CA ASP A 63 12.572 -10.259 -27.616 1.00 12.85 C ANISOU 494 CA ASP A 63 1661 1554 1665 29 -18 61 C ATOM 495 C ASP A 63 12.168 -11.674 -27.250 1.00 12.89 C ANISOU 495 C ASP A 63 1608 1616 1671 -111 34 -85 C ATOM 496 O ASP A 63 12.741 -12.638 -27.739 1.00 13.60 O ANISOU 496 O ASP A 63 1722 1709 1735 65 -17 24 O ATOM 497 CB ASP A 63 12.207 -10.062 -29.129 1.00 12.93 C ANISOU 497 CB ASP A 63 1625 1635 1650 -48 -46 -7 C ATOM 498 CG ASP A 63 12.376 -8.633 -29.615 1.00 14.40 C ANISOU 498 CG ASP A 63 1848 1799 1822 -89 -23 27 C ATOM 499 OD1 ASP A 63 12.479 -7.679 -28.803 1.00 14.27 O ANISOU 499 OD1 ASP A 63 1847 1777 1797 1 15 16 O ATOM 500 OD2 ASP A 63 12.432 -8.485 -30.888 1.00 15.22 O ANISOU 500 OD2 ASP A 63 2014 1875 1891 -57 1 -19 O ATOM 501 N LEU A 64 11.181 -11.807 -26.379 1.00 12.51 N ANISOU 501 N LEU A 64 1656 1465 1631 -58 82 -36 N ATOM 502 CA LEU A 64 10.669 -13.146 -25.956 1.00 13.19 C ANISOU 502 CA LEU A 64 1753 1582 1677 -14 65 55 C ATOM 503 C LEU A 64 10.150 -13.843 -27.180 1.00 13.00 C ANISOU 503 C LEU A 64 1604 1653 1679 16 -7 -40 C ATOM 504 O LEU A 64 9.755 -13.317 -28.179 1.00 13.58 O ANISOU 504 O LEU A 64 1760 1657 1741 -29 13 11 O ATOM 505 CB LEU A 64 9.591 -12.957 -24.923 1.00 13.01 C ANISOU 505 CB LEU A 64 1684 1547 1712 -27 148 66 C ATOM 506 CG LEU A 64 10.007 -12.350 -23.575 1.00 15.12 C ANISOU 506 CG LEU A 64 1854 1875 2016 -45 89 76 C ATOM 507 CD1 LEU A 64 8.750 -12.082 -22.737 1.00 15.75 C ANISOU 507 CD1 LEU A 64 2094 1913 1977 -146 135 -63 C ATOM 508 CD2 LEU A 64 11.038 -13.102 -22.857 1.00 15.88 C ANISOU 508 CD2 LEU A 64 2113 2030 1889 -110 -49 -7 C ATOM 509 N ILE A 65 10.143 -15.191 -27.037 1.00 13.15 N ANISOU 509 N ILE A 65 1690 1642 1664 -53 -82 26 N ATOM 510 CA ILE A 65 9.621 -16.026 -28.155 1.00 14.10 C ANISOU 510 CA ILE A 65 1774 1807 1775 -89 -19 -40 C ATOM 511 C ILE A 65 8.263 -15.651 -28.543 1.00 13.53 C ANISOU 511 C ILE A 65 1810 1556 1774 -83 41 -42 C ATOM 512 O ILE A 65 7.445 -15.372 -27.695 1.00 13.85 O ANISOU 512 O ILE A 65 1790 1681 1789 3 50 29 O ATOM 513 CB ILE A 65 9.825 -17.524 -27.807 1.00 14.04 C ANISOU 513 CB ILE A 65 1733 1789 1811 13 -38 -74 C ATOM 514 CG1 ILE A 65 9.829 -18.403 -29.077 1.00 14.80 C ANISOU 514 CG1 ILE A 65 1907 1775 1939 -37 37 -104 C ATOM 515 CG2 ILE A 65 8.763 -17.963 -26.851 1.00 13.64 C ANISOU 515 CG2 ILE A 65 1728 1667 1788 -39 34 -67 C ATOM 516 CD1 ILE A 65 11.025 -18.307 -29.933 1.00 16.75 C ANISOU 516 CD1 ILE A 65 2300 2009 2054 -33 30 -239 C ATOM 517 N GLY A 66 7.997 -15.619 -29.825 1.00 14.03 N ANISOU 517 N GLY A 66 1797 1739 1793 -27 9 4 N ATOM 518 CA GLY A 66 6.733 -15.183 -30.317 1.00 15.42 C ANISOU 518 CA GLY A 66 2006 1932 1921 -16 -32 -95 C ATOM 519 C GLY A 66 6.358 -13.734 -30.247 1.00 14.22 C ANISOU 519 C GLY A 66 1844 1800 1757 27 -176 -44 C ATOM 520 O GLY A 66 5.218 -13.358 -30.525 1.00 15.18 O ANISOU 520 O GLY A 66 1893 1921 1951 6 75 -98 O ATOM 521 N MET A 67 7.324 -12.926 -29.796 1.00 14.16 N ANISOU 521 N MET A 67 1755 1725 1899 -38 50 58 N ATOM 522 CA MET A 67 7.094 -11.483 -29.555 1.00 12.76 C ANISOU 522 CA MET A 67 1594 1605 1649 6 12 -71 C ATOM 523 C MET A 67 8.160 -10.759 -30.326 1.00 13.35 C ANISOU 523 C MET A 67 1707 1656 1710 34 41 41 C ATOM 524 O MET A 67 9.261 -11.248 -30.664 1.00 13.99 O ANISOU 524 O MET A 67 1806 1797 1713 71 30 11 O ATOM 525 CB MET A 67 7.108 -11.182 -28.045 1.00 13.79 C ANISOU 525 CB MET A 67 1754 1723 1763 11 -48 16 C ATOM 526 CG MET A 67 6.153 -12.111 -27.290 1.00 14.82 C ANISOU 526 CG MET A 67 1903 1912 1816 -69 -17 -33 C ATOM 527 SD MET A 67 5.909 -11.682 -25.558 1.00 14.87 S ANISOU 527 SD MET A 67 1930 1870 1850 0 37 9 S ATOM 528 CE MET A 67 4.867 -10.277 -25.737 1.00 17.12 C ANISOU 528 CE MET A 67 2157 2179 2169 31 85 79 C ATOM 529 N GLY A 68 7.961 -9.427 -30.556 1.00 14.03 N ANISOU 529 N GLY A 68 1761 1742 1827 24 49 11 N ATOM 530 CA GLY A 68 8.966 -8.664 -31.277 1.00 14.28 C ANISOU 530 CA GLY A 68 1828 1823 1772 2 0 21 C ATOM 531 C GLY A 68 9.288 -9.303 -32.553 1.00 15.02 C ANISOU 531 C GLY A 68 1923 1901 1880 -39 27 55 C ATOM 532 O GLY A 68 8.413 -9.672 -33.349 1.00 14.78 O ANISOU 532 O GLY A 68 1865 1866 1883 21 -47 4 O ATOM 533 N ASP A 69 10.587 -9.459 -32.791 1.00 13.28 N ANISOU 533 N ASP A 69 1676 1676 1691 -11 -30 -73 N ATOM 534 CA ASP A 69 11.101 -10.090 -34.031 1.00 15.27 C ANISOU 534 CA ASP A 69 1936 1933 1931 -27 -6 -28 C ATOM 535 C ASP A 69 11.555 -11.488 -33.820 1.00 15.54 C ANISOU 535 C ASP A 69 2054 1960 1889 89 -6 14 C ATOM 536 O ASP A 69 12.221 -12.047 -34.714 1.00 16.00 O ANISOU 536 O ASP A 69 2121 1940 2015 37 124 29 O ATOM 537 CB ASP A 69 12.198 -9.174 -34.681 1.00 14.84 C ANISOU 537 CB ASP A 69 1905 1930 1803 -1 90 -2 C ATOM 538 CG ASP A 69 11.594 -8.008 -35.286 1.00 17.32 C ANISOU 538 CG ASP A 69 2247 2192 2140 -36 -64 49 C ATOM 539 OD1 ASP A 69 10.700 -8.215 -36.191 1.00 19.03 O ANISOU 539 OD1 ASP A 69 2367 2420 2444 95 -61 -81 O ATOM 540 OD2 ASP A 69 11.840 -6.868 -34.824 1.00 16.98 O ANISOU 540 OD2 ASP A 69 2316 2082 2054 -27 -73 19 O ATOM 541 N SER A 70 11.255 -12.083 -32.678 1.00 13.08 N ANISOU 541 N SER A 70 1695 1557 1715 38 56 -20 N ATOM 542 CA SER A 70 11.483 -13.549 -32.505 1.00 12.82 C ANISOU 542 CA SER A 70 1660 1589 1619 -12 71 13 C ATOM 543 C SER A 70 10.442 -14.333 -33.193 1.00 15.45 C ANISOU 543 C SER A 70 2026 1906 1937 58 -34 -29 C ATOM 544 O SER A 70 9.289 -13.935 -33.281 1.00 17.03 O ANISOU 544 O SER A 70 2058 2087 2325 -75 -15 -32 O ATOM 545 CB SER A 70 11.582 -13.783 -30.995 1.00 13.84 C ANISOU 545 CB SER A 70 1729 1749 1779 -1 -65 70 C ATOM 546 OG SER A 70 12.736 -13.223 -30.437 1.00 14.28 O ANISOU 546 OG SER A 70 1835 1764 1824 -71 -1 13 O ATOM 547 N ASP A 71 10.809 -15.548 -33.631 1.00 15.59 N ANISOU 547 N ASP A 71 1990 1913 2020 -29 36 6 N ATOM 548 CA ASP A 71 9.869 -16.385 -34.309 1.00 14.79 C ANISOU 548 CA ASP A 71 1937 1824 1859 77 -157 116 C ATOM 549 C ASP A 71 8.736 -16.849 -33.470 1.00 16.58 C ANISOU 549 C ASP A 71 2125 2024 2149 106 -46 -13 C ATOM 550 O ASP A 71 8.829 -16.944 -32.224 1.00 16.54 O ANISOU 550 O ASP A 71 2211 2039 2034 -156 11 -65 O ATOM 551 CB ASP A 71 10.607 -17.618 -34.866 1.00 15.35 C ANISOU 551 CB ASP A 71 1900 1939 1991 -11 43 -140 C ATOM 552 CG ASP A 71 11.553 -17.357 -36.086 1.00 17.56 C ANISOU 552 CG ASP A 71 2322 2108 2240 92 35 -93 C ATOM 553 OD1 ASP A 71 11.386 -16.321 -36.710 1.00 19.22 O ANISOU 553 OD1 ASP A 71 2576 2489 2236 100 250 75 O ATOM 554 OD2 ASP A 71 12.277 -18.336 -36.431 1.00 19.23 O ANISOU 554 OD2 ASP A 71 2454 2590 2263 188 -64 -106 O ATOM 555 N LYS A 72 7.631 -17.174 -34.107 1.00 16.59 N ANISOU 555 N LYS A 72 2144 2047 2112 -124 -90 -46 N ATOM 556 CA LYS A 72 6.462 -17.765 -33.494 1.00 15.88 C ANISOU 556 CA LYS A 72 1987 2068 1978 110 -16 -88 C ATOM 557 C LYS A 72 6.665 -19.329 -33.269 1.00 16.23 C ANISOU 557 C LYS A 72 1987 2092 2085 -108 -35 -53 C ATOM 558 O LYS A 72 7.284 -20.009 -34.136 1.00 17.70 O ANISOU 558 O LYS A 72 2187 2269 2270 29 -45 -102 O ATOM 559 CB LYS A 72 5.218 -17.605 -34.374 1.00 16.78 C ANISOU 559 CB LYS A 72 2108 2089 2178 -68 -9 -2 C ATOM 560 CG LYS A 72 4.866 -16.150 -34.703 1.00 17.98 C ANISOU 560 CG LYS A 72 2261 2286 2282 -57 -213 -28 C ATOM 561 CD LYS A 72 4.404 -15.313 -33.505 1.00 18.55 C ANISOU 561 CD LYS A 72 2255 2465 2327 127 -122 -30 C ATOM 562 CE LYS A 72 4.181 -13.880 -33.943 1.00 19.67 C ANISOU 562 CE LYS A 72 2379 2592 2503 -5 -54 -1 C ATOM 563 NZ LYS A 72 3.645 -13.083 -32.797 1.00 20.90 N ANISOU 563 NZ LYS A 72 2709 2606 2625 -11 -176 -72 N ATOM 564 N LEU A 73 6.110 -19.788 -32.177 1.00 16.10 N ANISOU 564 N LEU A 73 2181 1892 2043 13 4 -43 N ATOM 565 CA LEU A 73 6.020 -21.256 -32.005 1.00 16.44 C ANISOU 565 CA LEU A 73 2113 1951 2182 -64 -59 135 C ATOM 566 C LEU A 73 5.009 -21.839 -32.971 1.00 22.15 C ANISOU 566 C LEU A 73 2812 2711 2891 160 -75 -132 C ATOM 567 O LEU A 73 4.045 -21.137 -33.363 1.00 21.93 O ANISOU 567 O LEU A 73 2769 2730 2833 -97 -402 -32 O ATOM 568 CB LEU A 73 5.585 -21.477 -30.577 1.00 16.14 C ANISOU 568 CB LEU A 73 2072 1904 2154 -44 32 -76 C ATOM 569 CG LEU A 73 6.582 -21.026 -29.515 1.00 16.63 C ANISOU 569 CG LEU A 73 2150 2041 2127 -64 5 -113 C ATOM 570 CD1 LEU A 73 6.001 -21.240 -28.096 1.00 17.67 C ANISOU 570 CD1 LEU A 73 2315 2129 2269 1 -158 33 C ATOM 571 CD2 LEU A 73 7.910 -21.671 -29.651 1.00 18.48 C ANISOU 571 CD2 LEU A 73 2327 2153 2541 -150 -243 65 C ATOM 572 N ASER A 74 5.216 -23.143 -33.217 0.50 20.96 N ANISOU 572 N ASER A 74 2646 2619 2698 -309 -537 -151 N ATOM 573 N BSER A 74 5.082 -23.133 -33.199 0.50 22.64 N ANISOU 573 N BSER A 74 2958 2766 2877 -350 -527 -168 N ATOM 574 CA ASER A 74 4.209 -23.906 -34.052 0.50 24.83 C ANISOU 574 CA ASER A 74 3189 2944 3301 -682 -347 81 C ATOM 575 CA BSER A 74 4.011 -23.711 -34.152 0.50 25.12 C ANISOU 575 CA BSER A 74 3131 3003 3410 -821 -556 132 C ATOM 576 C ASER A 74 4.109 -25.372 -33.596 0.50 25.37 C ANISOU 576 C ASER A 74 3087 2921 3631 104 -159 -338 C ATOM 577 C BSER A 74 4.069 -25.194 -33.936 0.50 26.29 C ANISOU 577 C BSER A 74 3313 3065 3609 193 250 -307 C ATOM 578 O ASER A 74 5.003 -26.046 -33.092 0.50 20.90 O ANISOU 578 O ASER A 74 2705 2593 2642 -300 -85 -32 O ATOM 579 O BSER A 74 5.157 -25.714 -34.006 0.50 22.52 O ANISOU 579 O BSER A 74 2899 2773 2881 -67 -290 -711 O ATOM 580 CB ASER A 74 4.545 -23.738 -35.490 0.50 25.74 C ANISOU 580 CB ASER A 74 3228 3280 3271 -68 -97 -528 C ATOM 581 CB BSER A 74 4.398 -23.335 -35.562 0.50 29.12 C ANISOU 581 CB BSER A 74 3943 3524 3597 63 -191 -640 C ATOM 582 OG ASER A 74 3.491 -24.240 -36.364 0.50 26.74 O ANISOU 582 OG ASER A 74 3282 3906 2970 -197 -749 -283 O ATOM 583 OG BSER A 74 5.617 -23.945 -35.906 0.50 36.23 O ANISOU 583 OG BSER A 74 3875 5321 4569 -77 296 -815 O ATOM 584 N PRO A 75 2.888 -25.860 -33.642 1.00 26.38 N ANISOU 584 N PRO A 75 3218 3002 3802 -254 -82 -329 N ATOM 585 CA PRO A 75 1.598 -25.290 -33.687 1.00 24.54 C ANISOU 585 CA PRO A 75 3140 2855 3329 -166 -118 -256 C ATOM 586 C PRO A 75 1.259 -24.544 -32.416 1.00 23.33 C ANISOU 586 C PRO A 75 3007 2937 2918 -41 -42 9 C ATOM 587 O PRO A 75 1.370 -25.070 -31.314 1.00 26.18 O ANISOU 587 O PRO A 75 3514 3069 3362 -197 -206 -219 O ATOM 588 CB PRO A 75 0.677 -26.521 -33.759 1.00 27.83 C ANISOU 588 CB PRO A 75 3286 3462 3823 -411 -76 -245 C ATOM 589 CG PRO A 75 1.386 -27.605 -32.969 1.00 29.48 C ANISOU 589 CG PRO A 75 3947 3437 3815 -193 292 -155 C ATOM 590 CD PRO A 75 2.848 -27.385 -33.443 1.00 29.31 C ANISOU 590 CD PRO A 75 3708 3234 4193 55 -294 62 C ATOM 591 N SER A 76 0.852 -23.286 -32.605 1.00 23.38 N ANISOU 591 N SER A 76 2999 2861 3023 -110 -133 -229 N ATOM 592 CA SER A 76 0.390 -22.488 -31.421 1.00 21.96 C ANISOU 592 CA SER A 76 2728 2821 2792 -171 98 -42 C ATOM 593 C SER A 76 -0.949 -22.799 -30.969 1.00 24.16 C ANISOU 593 C SER A 76 2985 3128 3065 51 -6 -37 C ATOM 594 O SER A 76 -1.801 -23.273 -31.817 1.00 24.78 O ANISOU 594 O SER A 76 3103 3112 3200 -169 -313 -192 O ATOM 595 CB SER A 76 0.526 -21.047 -31.806 1.00 20.82 C ANISOU 595 CB SER A 76 2452 2768 2688 131 -59 -1 C ATOM 596 OG SER A 76 0.144 -20.167 -30.819 1.00 21.44 O ANISOU 596 OG SER A 76 2548 2783 2815 -220 -100 -232 O ATOM 597 N GLY A 77 -1.210 -22.710 -29.707 1.00 21.40 N ANISOU 597 N GLY A 77 2613 2784 2733 -229 -113 -118 N ATOM 598 CA GLY A 77 -2.514 -22.917 -29.123 1.00 21.16 C ANISOU 598 CA GLY A 77 2655 2697 2684 -114 -22 -236 C ATOM 599 C GLY A 77 -2.478 -22.722 -27.645 1.00 21.68 C ANISOU 599 C GLY A 77 2796 2761 2680 -47 -20 27 C ATOM 600 O GLY A 77 -1.502 -22.174 -27.123 1.00 20.38 O ANISOU 600 O GLY A 77 2458 2564 2720 -128 -171 -50 O ATOM 601 N PRO A 78 -3.489 -23.072 -26.885 1.00 20.35 N ANISOU 601 N PRO A 78 2447 2602 2681 -105 -98 6 N ATOM 602 CA PRO A 78 -3.589 -22.752 -25.538 1.00 21.98 C ANISOU 602 CA PRO A 78 2588 2882 2879 -146 119 -21 C ATOM 603 C PRO A 78 -2.572 -23.331 -24.574 1.00 21.55 C ANISOU 603 C PRO A 78 2628 2777 2783 -6 185 94 C ATOM 604 O PRO A 78 -2.393 -22.815 -23.464 1.00 25.22 O ANISOU 604 O PRO A 78 3129 3241 3212 -246 6 -249 O ATOM 605 CB PRO A 78 -5.053 -23.209 -25.070 1.00 26.26 C ANISOU 605 CB PRO A 78 2957 3437 3580 -39 184 -4 C ATOM 606 CG PRO A 78 -5.498 -24.072 -26.245 1.00 29.00 C ANISOU 606 CG PRO A 78 3528 3848 3641 -341 74 -265 C ATOM 607 CD PRO A 78 -4.613 -23.950 -27.394 1.00 29.32 C ANISOU 607 CD PRO A 78 3553 3772 3813 -432 -338 -180 C ATOM 608 N ASP A 79 -1.892 -24.374 -25.014 1.00 21.19 N ANISOU 608 N ASP A 79 2635 2574 2842 -244 38 -56 N ATOM 609 CA ASP A 79 -0.880 -25.004 -24.228 1.00 22.27 C ANISOU 609 CA ASP A 79 2703 2782 2974 -148 26 -183 C ATOM 610 C ASP A 79 0.509 -24.428 -24.497 1.00 19.46 C ANISOU 610 C ASP A 79 2413 2489 2490 -243 -69 301 C ATOM 611 O ASP A 79 1.469 -24.848 -23.929 1.00 21.53 O ANISOU 611 O ASP A 79 2681 2529 2971 -134 54 184 O ATOM 612 CB ASP A 79 -0.823 -26.484 -24.499 1.00 30.12 C ANISOU 612 CB ASP A 79 3750 2951 4741 -152 254 -19 C ATOM 613 CG ASP A 79 -0.082 -27.180 -23.451 1.00 56.08 C ANISOU 613 CG ASP A 79 8272 7272 5761 -287 -288 -496 C ATOM 614 OD1 ASP A 79 -0.019 -26.663 -22.337 1.00 35.31 O ANISOU 614 OD1 ASP A 79 4669 3676 5071 -194 112 -108 O ATOM 615 OD2 ASP A 79 0.462 -28.251 -23.705 1.00 78.20 O ANISOU 615 OD2 ASP A 79 9771 8501 11439 2533 6 1828 O ATOM 616 N ARG A 80 0.587 -23.441 -25.365 1.00 18.47 N ANISOU 616 N ARG A 80 2258 2249 2511 -65 -68 90 N ATOM 617 CA ARG A 80 1.874 -22.840 -25.706 1.00 19.14 C ANISOU 617 CA ARG A 80 2368 2358 2544 -22 -113 122 C ATOM 618 C ARG A 80 2.084 -21.465 -25.045 1.00 16.70 C ANISOU 618 C ARG A 80 2134 2147 2064 31 104 -25 C ATOM 619 O ARG A 80 1.177 -20.873 -24.609 1.00 17.64 O ANISOU 619 O ARG A 80 2194 2211 2295 5 -21 23 O ATOM 620 CB ARG A 80 2.007 -22.696 -27.221 1.00 18.62 C ANISOU 620 CB ARG A 80 2403 2290 2382 -210 108 -47 C ATOM 621 CG ARG A 80 1.731 -23.957 -28.016 1.00 19.13 C ANISOU 621 CG ARG A 80 2493 2441 2334 -87 45 -130 C ATOM 622 CD ARG A 80 2.613 -25.089 -27.586 1.00 19.84 C ANISOU 622 CD ARG A 80 2508 2462 2568 -112 66 -134 C ATOM 623 NE ARG A 80 4.036 -24.896 -27.778 1.00 19.78 N ANISOU 623 NE ARG A 80 2531 2333 2649 -126 -40 -175 N ATOM 624 CZ ARG A 80 4.675 -25.109 -28.896 1.00 21.83 C ANISOU 624 CZ ARG A 80 2722 2743 2830 -295 39 113 C ATOM 625 NH1 ARG A 80 4.046 -25.478 -29.982 1.00 23.71 N ANISOU 625 NH1 ARG A 80 3050 2959 2999 -108 -103 -238 N ATOM 626 NH2 ARG A 80 5.959 -24.955 -28.937 1.00 21.39 N ANISOU 626 NH2 ARG A 80 2667 2624 2835 33 -33 -362 N ATOM 627 N TYR A 81 3.333 -21.038 -25.001 1.00 15.79 N ANISOU 627 N TYR A 81 2053 1951 1993 -47 -61 -99 N ATOM 628 CA TYR A 81 3.718 -19.760 -24.450 1.00 15.77 C ANISOU 628 CA TYR A 81 2077 1954 1961 43 63 -28 C ATOM 629 C TYR A 81 3.447 -19.630 -22.949 1.00 16.28 C ANISOU 629 C TYR A 81 2001 2097 2087 66 147 36 C ATOM 630 O TYR A 81 3.211 -18.576 -22.474 1.00 16.39 O ANISOU 630 O TYR A 81 2104 1963 2159 -45 103 -35 O ATOM 631 CB TYR A 81 3.146 -18.601 -25.250 1.00 16.85 C ANISOU 631 CB TYR A 81 2139 2129 2133 82 17 -66 C ATOM 632 CG TYR A 81 3.462 -18.510 -26.740 1.00 14.35 C ANISOU 632 CG TYR A 81 1833 1824 1794 106 -16 66 C ATOM 633 CD1 TYR A 81 4.668 -18.036 -27.185 1.00 15.31 C ANISOU 633 CD1 TYR A 81 1947 1881 1987 -12 -31 -6 C ATOM 634 CD2 TYR A 81 2.531 -18.867 -27.688 1.00 15.27 C ANISOU 634 CD2 TYR A 81 1810 1984 2007 -103 95 40 C ATOM 635 CE1 TYR A 81 4.930 -17.933 -28.515 1.00 16.14 C ANISOU 635 CE1 TYR A 81 2039 2070 2021 -42 4 74 C ATOM 636 CE2 TYR A 81 2.788 -18.747 -29.027 1.00 14.81 C ANISOU 636 CE2 TYR A 81 1848 1856 1922 3 -123 -43 C ATOM 637 CZ TYR A 81 3.987 -18.286 -29.433 1.00 14.81 C ANISOU 637 CZ TYR A 81 1929 1826 1870 66 28 41 C ATOM 638 OH TYR A 81 4.225 -18.126 -30.744 1.00 15.95 O ANISOU 638 OH TYR A 81 2096 1930 2033 -36 92 -100 O ATOM 639 N SER A 82 3.538 -20.732 -22.250 1.00 15.49 N ANISOU 639 N SER A 82 1958 1933 1993 -81 -20 66 N ATOM 640 CA SER A 82 3.438 -20.661 -20.830 1.00 15.74 C ANISOU 640 CA SER A 82 2001 1984 1995 25 56 40 C ATOM 641 C SER A 82 4.707 -20.011 -20.275 1.00 16.50 C ANISOU 641 C SER A 82 2176 2015 2075 6 -43 55 C ATOM 642 O SER A 82 5.648 -19.820 -20.968 1.00 16.25 O ANISOU 642 O SER A 82 2051 2044 2078 31 83 19 O ATOM 643 CB SER A 82 3.350 -22.089 -20.259 1.00 18.05 C ANISOU 643 CB SER A 82 2306 2202 2349 -24 219 260 C ATOM 644 OG SER A 82 4.527 -22.799 -20.491 1.00 17.57 O ANISOU 644 OG SER A 82 2255 2085 2335 -30 74 0 O ATOM 645 N TYR A 83 4.674 -19.642 -19.013 1.00 14.89 N ANISOU 645 N TYR A 83 1925 1844 1887 32 56 30 N ATOM 646 CA TYR A 83 5.856 -19.139 -18.379 1.00 15.86 C ANISOU 646 CA TYR A 83 2066 1930 2027 -29 110 91 C ATOM 647 C TYR A 83 7.050 -20.098 -18.569 1.00 15.11 C ANISOU 647 C TYR A 83 1949 1885 1907 -3 85 32 C ATOM 648 O TYR A 83 8.123 -19.686 -18.881 1.00 15.14 O ANISOU 648 O TYR A 83 1884 1861 2006 -22 34 61 O ATOM 649 CB TYR A 83 5.641 -18.877 -16.854 1.00 15.40 C ANISOU 649 CB TYR A 83 2057 1850 1944 87 -11 111 C ATOM 650 CG TYR A 83 6.910 -18.451 -16.171 1.00 14.91 C ANISOU 650 CG TYR A 83 1922 1862 1880 -15 52 0 C ATOM 651 CD1 TYR A 83 7.289 -17.141 -16.122 1.00 16.07 C ANISOU 651 CD1 TYR A 83 2146 1911 2047 -40 -37 170 C ATOM 652 CD2 TYR A 83 7.768 -19.373 -15.632 1.00 16.46 C ANISOU 652 CD2 TYR A 83 2153 2032 2065 87 -40 50 C ATOM 653 CE1 TYR A 83 8.478 -16.773 -15.557 1.00 18.09 C ANISOU 653 CE1 TYR A 83 2340 2216 2318 71 -75 2 C ATOM 654 CE2 TYR A 83 8.955 -19.003 -15.071 1.00 17.34 C ANISOU 654 CE2 TYR A 83 2239 2084 2262 -125 -95 149 C ATOM 655 CZ TYR A 83 9.305 -17.696 -15.039 1.00 16.64 C ANISOU 655 CZ TYR A 83 2197 2032 2091 107 -291 -66 C ATOM 656 OH TYR A 83 10.503 -17.345 -14.519 1.00 18.78 O ANISOU 656 OH TYR A 83 2392 2227 2515 -131 -76 116 O ATOM 657 N ALA A 84 6.831 -21.387 -18.358 1.00 15.54 N ANISOU 657 N ALA A 84 1999 1952 1952 -42 132 44 N ATOM 658 CA ALA A 84 7.929 -22.253 -18.424 1.00 16.98 C ANISOU 658 CA ALA A 84 2186 2092 2172 -21 133 139 C ATOM 659 C ALA A 84 8.509 -22.368 -19.833 1.00 15.34 C ANISOU 659 C ALA A 84 2053 1792 1983 48 39 54 C ATOM 660 O ALA A 84 9.724 -22.468 -20.000 1.00 14.96 O ANISOU 660 O ALA A 84 1892 1803 1987 -17 38 60 O ATOM 661 CB ALA A 84 7.454 -23.704 -18.059 1.00 17.60 C ANISOU 661 CB ALA A 84 2304 2077 2305 122 237 154 C ATOM 662 N GLU A 85 7.657 -22.316 -20.825 1.00 14.87 N ANISOU 662 N GLU A 85 1862 1845 1940 -18 77 22 N ATOM 663 CA GLU A 85 8.125 -22.347 -22.212 1.00 14.70 C ANISOU 663 CA GLU A 85 1941 1755 1887 85 -23 58 C ATOM 664 C GLU A 85 8.940 -21.061 -22.570 1.00 14.72 C ANISOU 664 C GLU A 85 1845 1824 1921 -19 117 3 C ATOM 665 O GLU A 85 10.015 -21.150 -23.137 1.00 14.65 O ANISOU 665 O GLU A 85 1907 1754 1905 -43 44 79 O ATOM 666 CB GLU A 85 7.012 -22.624 -23.180 1.00 16.07 C ANISOU 666 CB GLU A 85 2067 1904 2133 -138 -107 19 C ATOM 667 CG GLU A 85 7.487 -22.857 -24.593 1.00 16.04 C ANISOU 667 CG GLU A 85 2051 1928 2113 -19 -29 5 C ATOM 668 CD GLU A 85 6.509 -23.524 -25.510 1.00 15.27 C ANISOU 668 CD GLU A 85 2027 1872 1901 24 65 185 C ATOM 669 OE1 GLU A 85 5.257 -23.300 -25.351 1.00 16.37 O ANISOU 669 OE1 GLU A 85 2079 1943 2198 -35 -3 -12 O ATOM 670 OE2 GLU A 85 7.018 -24.203 -26.460 1.00 16.29 O ANISOU 670 OE2 GLU A 85 2147 1949 2091 -7 36 6 O ATOM 671 N HIS A 86 8.434 -19.949 -22.128 1.00 15.20 N ANISOU 671 N HIS A 86 1874 1891 2007 -76 40 -5 N ATOM 672 CA HIS A 86 9.214 -18.721 -22.274 1.00 13.92 C ANISOU 672 CA HIS A 86 1814 1677 1795 70 156 65 C ATOM 673 C HIS A 86 10.507 -18.727 -21.617 1.00 14.08 C ANISOU 673 C HIS A 86 1836 1715 1797 25 29 -52 C ATOM 674 O HIS A 86 11.547 -18.291 -22.164 1.00 15.11 O ANISOU 674 O HIS A 86 1950 1837 1953 38 42 35 O ATOM 675 CB HIS A 86 8.410 -17.481 -21.770 1.00 12.77 C ANISOU 675 CB HIS A 86 1669 1545 1636 8 91 -79 C ATOM 676 CG HIS A 86 7.476 -16.911 -22.742 1.00 12.75 C ANISOU 676 CG HIS A 86 1646 1599 1599 54 108 -133 C ATOM 677 ND1 HIS A 86 7.917 -16.165 -23.833 1.00 14.72 N ANISOU 677 ND1 HIS A 86 1939 1765 1886 -36 -11 15 N ATOM 678 CD2 HIS A 86 6.134 -16.904 -22.797 1.00 13.00 C ANISOU 678 CD2 HIS A 86 1611 1583 1744 -87 -83 -8 C ATOM 679 CE1 HIS A 86 6.875 -15.728 -24.478 1.00 14.51 C ANISOU 679 CE1 HIS A 86 1788 1784 1941 46 -4 50 C ATOM 680 NE2 HIS A 86 5.740 -16.184 -23.902 1.00 14.34 N ANISOU 680 NE2 HIS A 86 1883 1798 1766 -70 135 60 N ATOM 681 N AARG A 87 10.529 -19.288 -20.415 0.50 13.53 N ANISOU 681 N AARG A 87 1650 1763 1728 -243 2 17 N ATOM 682 N BARG A 87 10.552 -19.276 -20.363 0.50 14.52 N ANISOU 682 N BARG A 87 1784 1891 1839 -268 12 31 N ATOM 683 CA AARG A 87 11.744 -19.408 -19.635 0.50 12.88 C ANISOU 683 CA AARG A 87 1761 1370 1760 43 -20 83 C ATOM 684 CA BARG A 87 11.738 -19.445 -19.586 0.50 14.61 C ANISOU 684 CA BARG A 87 1977 1532 2039 64 -35 71 C ATOM 685 C AARG A 87 12.742 -20.321 -20.344 0.50 13.14 C ANISOU 685 C AARG A 87 1598 1756 1637 34 63 -22 C ATOM 686 C BARG A 87 12.740 -20.336 -20.316 0.50 14.09 C ANISOU 686 C BARG A 87 1721 1878 1754 5 50 -34 C ATOM 687 O AARG A 87 13.909 -20.053 -20.381 0.50 13.80 O ANISOU 687 O AARG A 87 1743 1714 1784 2 6 54 O ATOM 688 O BARG A 87 13.941 -20.034 -20.423 0.50 14.73 O ANISOU 688 O BARG A 87 1862 1829 1904 2 1 59 O ATOM 689 CB AARG A 87 11.423 -19.959 -18.244 0.50 13.08 C ANISOU 689 CB AARG A 87 1721 1726 1521 -34 3 -340 C ATOM 690 CB BARG A 87 11.365 -20.015 -18.204 0.50 16.56 C ANISOU 690 CB BARG A 87 2215 2198 1878 -47 72 -438 C ATOM 691 CG AARG A 87 12.639 -20.390 -17.452 0.50 13.87 C ANISOU 691 CG AARG A 87 1664 1764 1841 143 -58 -28 C ATOM 692 CG BARG A 87 12.490 -20.172 -17.217 0.50 18.90 C ANISOU 692 CG BARG A 87 2179 2569 2431 272 -77 120 C ATOM 693 CD AARG A 87 12.275 -20.694 -16.022 0.50 14.60 C ANISOU 693 CD AARG A 87 1699 1997 1850 -112 10 245 C ATOM 694 CD BARG A 87 13.220 -21.495 -17.335 0.50 22.37 C ANISOU 694 CD BARG A 87 3071 2610 2818 40 -261 -146 C ATOM 695 NE AARG A 87 11.521 -21.939 -15.886 0.50 16.51 N ANISOU 695 NE AARG A 87 2413 1847 2013 0 -161 14 N ATOM 696 NE BARG A 87 12.466 -22.657 -17.845 0.50 22.94 N ANISOU 696 NE BARG A 87 2964 3052 2700 186 -75 302 N ATOM 697 CZ AARG A 87 11.075 -22.393 -14.731 0.50 15.80 C ANISOU 697 CZ AARG A 87 1987 1980 2033 -160 69 25 C ATOM 698 CZ BARG A 87 11.782 -23.439 -17.114 0.50 21.61 C ANISOU 698 CZ BARG A 87 2344 2733 3133 -165 102 141 C ATOM 699 NH1AARG A 87 11.317 -21.713 -13.619 0.50 14.23 N ANISOU 699 NH1AARG A 87 2067 1645 1693 -84 111 37 N ATOM 700 NH1BARG A 87 11.210 -24.351 -17.615 0.50 15.62 N ANISOU 700 NH1BARG A 87 2267 2112 1554 98 168 -185 N ATOM 701 NH2AARG A 87 10.401 -23.522 -14.683 0.50 19.64 N ANISOU 701 NH2AARG A 87 2598 2299 2562 -61 -88 -138 N ATOM 702 NH2BARG A 87 11.596 -23.211 -15.744 0.50 27.58 N ANISOU 702 NH2BARG A 87 3755 3655 3067 -72 -100 -306 N ATOM 703 N ASP A 88 12.246 -21.397 -20.929 1.00 15.27 N ANISOU 703 N ASP A 88 1867 1853 2081 -5 38 12 N ATOM 704 CA ASP A 88 13.138 -22.285 -21.647 1.00 15.98 C ANISOU 704 CA ASP A 88 2059 1955 2054 -35 89 -125 C ATOM 705 C ASP A 88 13.863 -21.524 -22.757 1.00 15.06 C ANISOU 705 C ASP A 88 1985 1842 1894 90 -9 -121 C ATOM 706 O ASP A 88 15.051 -21.583 -22.843 1.00 14.86 O ANISOU 706 O ASP A 88 1880 1831 1934 -28 1 -76 O ATOM 707 CB ASP A 88 12.390 -23.445 -22.278 1.00 16.42 C ANISOU 707 CB ASP A 88 2047 1993 2196 -30 -43 -88 C ATOM 708 CG ASP A 88 11.868 -24.440 -21.256 1.00 18.34 C ANISOU 708 CG ASP A 88 2356 2427 2183 59 80 25 C ATOM 709 OD1 ASP A 88 12.416 -24.551 -20.194 1.00 18.00 O ANISOU 709 OD1 ASP A 88 2350 2092 2395 10 -126 -25 O ATOM 710 OD2 ASP A 88 10.896 -25.066 -21.568 1.00 20.87 O ANISOU 710 OD2 ASP A 88 2777 2447 2706 -165 -87 16 O ATOM 711 N TYR A 89 13.104 -20.818 -23.588 1.00 14.05 N ANISOU 711 N TYR A 89 1820 1691 1824 -31 0 -80 N ATOM 712 CA TYR A 89 13.737 -20.064 -24.653 1.00 15.22 C ANISOU 712 CA TYR A 89 2009 1922 1849 -43 26 -92 C ATOM 713 C TYR A 89 14.631 -18.929 -24.176 1.00 14.05 C ANISOU 713 C TYR A 89 1784 1757 1795 -118 47 -99 C ATOM 714 O TYR A 89 15.713 -18.801 -24.646 1.00 13.88 O ANISOU 714 O TYR A 89 1791 1634 1846 10 37 -94 O ATOM 715 CB TYR A 89 12.710 -19.526 -25.684 1.00 13.76 C ANISOU 715 CB TYR A 89 1731 1704 1790 0 54 40 C ATOM 716 CG TYR A 89 12.201 -20.608 -26.599 1.00 14.61 C ANISOU 716 CG TYR A 89 1794 1888 1866 70 43 -25 C ATOM 717 CD1 TYR A 89 11.107 -21.341 -26.268 1.00 14.99 C ANISOU 717 CD1 TYR A 89 1999 1786 1909 83 -23 -35 C ATOM 718 CD2 TYR A 89 12.854 -20.922 -27.754 1.00 16.60 C ANISOU 718 CD2 TYR A 89 2148 2105 2055 -47 -24 43 C ATOM 719 CE1 TYR A 89 10.663 -22.360 -27.052 1.00 16.90 C ANISOU 719 CE1 TYR A 89 2011 2188 2221 -224 -18 -98 C ATOM 720 CE2 TYR A 89 12.401 -21.932 -28.546 1.00 17.67 C ANISOU 720 CE2 TYR A 89 2338 2184 2191 34 92 -206 C ATOM 721 CZ TYR A 89 11.301 -22.633 -28.183 1.00 18.81 C ANISOU 721 CZ TYR A 89 2393 2348 2407 -24 -13 -247 C ATOM 722 OH TYR A 89 10.881 -23.671 -28.960 1.00 23.36 O ANISOU 722 OH TYR A 89 2938 2925 3010 227 -341 -464 O ATOM 723 N LEU A 90 14.148 -18.144 -23.221 1.00 13.77 N ANISOU 723 N LEU A 90 1643 1808 1780 10 -69 -4 N ATOM 724 CA LEU A 90 14.956 -16.989 -22.776 1.00 14.36 C ANISOU 724 CA LEU A 90 1874 1796 1786 -27 -10 46 C ATOM 725 C LEU A 90 16.190 -17.386 -22.023 1.00 13.05 C ANISOU 725 C LEU A 90 1668 1632 1657 65 104 -44 C ATOM 726 O LEU A 90 17.287 -16.838 -22.271 1.00 14.15 O ANISOU 726 O LEU A 90 1808 1723 1844 -26 1 -27 O ATOM 727 CB LEU A 90 14.121 -16.045 -21.940 1.00 15.03 C ANISOU 727 CB LEU A 90 1917 1843 1949 -35 -51 48 C ATOM 728 CG LEU A 90 14.849 -14.740 -21.547 1.00 15.09 C ANISOU 728 CG LEU A 90 1869 1907 1957 -35 -8 44 C ATOM 729 CD1 LEU A 90 15.147 -13.900 -22.732 1.00 15.83 C ANISOU 729 CD1 LEU A 90 2063 1969 1981 88 49 -28 C ATOM 730 CD2 LEU A 90 13.979 -14.086 -20.537 1.00 16.43 C ANISOU 730 CD2 LEU A 90 2091 2006 2146 -134 -49 -165 C ATOM 731 N PHE A 91 16.082 -18.382 -21.148 1.00 12.88 N ANISOU 731 N PHE A 91 1593 1606 1695 16 11 4 N ATOM 732 CA PHE A 91 17.242 -18.787 -20.388 1.00 13.48 C ANISOU 732 CA PHE A 91 1778 1649 1693 -44 -116 -44 C ATOM 733 C PHE A 91 18.291 -19.414 -21.326 1.00 12.43 C ANISOU 733 C PHE A 91 1560 1484 1678 -59 -5 5 C ATOM 734 O PHE A 91 19.448 -19.276 -21.106 1.00 14.02 O ANISOU 734 O PHE A 91 1752 1681 1893 1 -43 -116 O ATOM 735 CB PHE A 91 16.889 -19.730 -19.232 1.00 14.45 C ANISOU 735 CB PHE A 91 1879 1846 1766 -80 -30 -9 C ATOM 736 CG PHE A 91 16.197 -19.084 -18.045 1.00 14.35 C ANISOU 736 CG PHE A 91 1810 1816 1827 -33 -15 108 C ATOM 737 CD1 PHE A 91 15.623 -17.833 -18.109 1.00 15.90 C ANISOU 737 CD1 PHE A 91 2003 2032 2004 42 136 -114 C ATOM 738 CD2 PHE A 91 16.132 -19.774 -16.858 1.00 15.69 C ANISOU 738 CD2 PHE A 91 1971 2030 1960 -69 -46 -12 C ATOM 739 CE1 PHE A 91 14.981 -17.303 -17.014 1.00 16.36 C ANISOU 739 CE1 PHE A 91 2161 2024 2030 164 -20 -40 C ATOM 740 CE2 PHE A 91 15.520 -19.234 -15.762 1.00 15.98 C ANISOU 740 CE2 PHE A 91 2149 2045 1878 -8 -4 15 C ATOM 741 CZ PHE A 91 14.930 -18.011 -15.849 1.00 15.74 C ANISOU 741 CZ PHE A 91 2087 1980 1912 -34 174 -107 C ATOM 742 N ALA A 92 17.857 -20.126 -22.358 1.00 13.14 N ANISOU 742 N ALA A 92 1671 1673 1647 -16 110 57 N ATOM 743 CA ALA A 92 18.775 -20.663 -23.324 1.00 14.43 C ANISOU 743 CA ALA A 92 1840 1734 1907 -53 109 -55 C ATOM 744 C ALA A 92 19.478 -19.542 -24.052 1.00 12.71 C ANISOU 744 C ALA A 92 1670 1557 1602 1 117 -28 C ATOM 745 O ALA A 92 20.719 -19.664 -24.246 1.00 13.42 O ANISOU 745 O ALA A 92 1665 1627 1805 -13 -16 -15 O ATOM 746 CB ALA A 92 18.080 -21.650 -24.280 1.00 16.31 C ANISOU 746 CB ALA A 92 2099 2027 2069 -20 -30 -21 C ATOM 747 N LEU A 93 18.756 -18.514 -24.463 1.00 13.80 N ANISOU 747 N LEU A 93 1691 1712 1839 -11 74 -28 N ATOM 748 CA LEU A 93 19.352 -17.363 -25.134 1.00 15.50 C ANISOU 748 CA LEU A 93 2047 1924 1915 65 -7 -32 C ATOM 749 C LEU A 93 20.365 -16.706 -24.218 1.00 13.86 C ANISOU 749 C LEU A 93 1816 1632 1816 -8 -7 29 C ATOM 750 O LEU A 93 21.507 -16.431 -24.653 1.00 13.82 O ANISOU 750 O LEU A 93 1773 1618 1858 60 113 -34 O ATOM 751 CB LEU A 93 18.284 -16.397 -25.594 1.00 14.80 C ANISOU 751 CB LEU A 93 1889 1891 1841 -7 13 -83 C ATOM 752 CG LEU A 93 18.810 -15.114 -26.226 1.00 14.97 C ANISOU 752 CG LEU A 93 1941 1879 1867 -30 -40 -51 C ATOM 753 CD1 LEU A 93 19.613 -15.413 -27.443 1.00 16.59 C ANISOU 753 CD1 LEU A 93 2204 1846 2253 -58 133 91 C ATOM 754 CD2 LEU A 93 17.606 -14.355 -26.601 1.00 17.14 C ANISOU 754 CD2 LEU A 93 2239 2074 2199 -15 -1 -20 C ATOM 755 N TRP A 94 20.019 -16.463 -22.942 1.00 13.98 N ANISOU 755 N TRP A 94 1808 1683 1818 -17 44 85 N ATOM 756 CA TRP A 94 20.925 -15.839 -22.042 1.00 14.26 C ANISOU 756 CA TRP A 94 1922 1681 1814 50 -27 103 C ATOM 757 C TRP A 94 22.193 -16.606 -21.857 1.00 14.60 C ANISOU 757 C TRP A 94 1819 1825 1900 -8 -14 -71 C ATOM 758 O TRP A 94 23.320 -16.116 -21.707 1.00 16.48 O ANISOU 758 O TRP A 94 2077 2000 2182 2 30 -135 O ATOM 759 CB TRP A 94 20.261 -15.539 -20.767 1.00 15.42 C ANISOU 759 CB TRP A 94 2028 1882 1948 -31 -94 -107 C ATOM 760 CG TRP A 94 19.321 -14.359 -20.790 1.00 14.23 C ANISOU 760 CG TRP A 94 1835 1739 1832 74 -91 7 C ATOM 761 CD1 TRP A 94 19.091 -13.587 -21.886 1.00 15.64 C ANISOU 761 CD1 TRP A 94 2006 2018 1919 81 107 90 C ATOM 762 CD2 TRP A 94 18.548 -13.829 -19.742 1.00 13.98 C ANISOU 762 CD2 TRP A 94 1874 1705 1733 44 6 111 C ATOM 763 NE1 TRP A 94 18.208 -12.529 -21.547 1.00 15.60 N ANISOU 763 NE1 TRP A 94 2093 1876 1956 144 86 67 N ATOM 764 CE2 TRP A 94 17.824 -12.671 -20.239 1.00 14.14 C ANISOU 764 CE2 TRP A 94 1907 1681 1783 50 13 -111 C ATOM 765 CE3 TRP A 94 18.336 -14.210 -18.436 1.00 18.74 C ANISOU 765 CE3 TRP A 94 2557 2414 2148 220 32 90 C ATOM 766 CZ2 TRP A 94 16.922 -11.963 -19.486 1.00 14.87 C ANISOU 766 CZ2 TRP A 94 1885 1816 1945 38 72 134 C ATOM 767 CZ3 TRP A 94 17.418 -13.497 -17.659 1.00 20.66 C ANISOU 767 CZ3 TRP A 94 2756 2685 2407 417 77 174 C ATOM 768 CH2 TRP A 94 16.741 -12.343 -18.197 1.00 18.66 C ANISOU 768 CH2 TRP A 94 2549 2289 2250 309 138 -113 C ATOM 769 N GLU A 95 22.069 -17.947 -21.880 1.00 13.89 N ANISOU 769 N GLU A 95 1776 1633 1866 -46 -89 44 N ATOM 770 CA GLU A 95 23.265 -18.802 -21.788 1.00 15.53 C ANISOU 770 CA GLU A 95 1976 1966 1956 -63 -29 12 C ATOM 771 C GLU A 95 24.149 -18.660 -23.032 1.00 15.73 C ANISOU 771 C GLU A 95 2013 1790 2171 70 100 19 C ATOM 772 O GLU A 95 25.336 -18.525 -22.942 1.00 17.15 O ANISOU 772 O GLU A 95 2141 2042 2332 57 -168 -69 O ATOM 773 CB GLU A 95 22.864 -20.268 -21.579 1.00 15.13 C ANISOU 773 CB GLU A 95 1942 1815 1990 -38 -44 38 C ATOM 774 CG GLU A 95 23.985 -21.285 -21.381 1.00 16.19 C ANISOU 774 CG GLU A 95 2043 1928 2177 -2 -62 -77 C ATOM 775 CD GLU A 95 23.424 -22.697 -21.204 1.00 15.71 C ANISOU 775 CD GLU A 95 2136 1927 1904 -76 -64 88 C ATOM 776 OE1 GLU A 95 23.149 -23.326 -22.202 1.00 15.56 O ANISOU 776 OE1 GLU A 95 2055 1826 2031 6 35 -26 O ATOM 777 OE2 GLU A 95 23.260 -23.062 -20.070 1.00 16.10 O ANISOU 777 OE2 GLU A 95 2123 1949 2044 -13 60 -39 O ATOM 778 N ALA A 96 23.501 -18.690 -24.182 1.00 14.32 N ANISOU 778 N ALA A 96 1866 1725 1848 61 118 -24 N ATOM 779 CA ALA A 96 24.170 -18.558 -25.441 1.00 14.87 C ANISOU 779 CA ALA A 96 1892 1807 1949 95 56 87 C ATOM 780 C ALA A 96 24.915 -17.249 -25.588 1.00 14.67 C ANISOU 780 C ALA A 96 1951 1770 1852 14 55 55 C ATOM 781 O ALA A 96 25.949 -17.197 -26.262 1.00 18.47 O ANISOU 781 O ALA A 96 2304 2202 2513 28 202 -35 O ATOM 782 CB ALA A 96 23.210 -18.748 -26.588 1.00 16.51 C ANISOU 782 CB ALA A 96 2232 1957 2084 -63 170 -44 C ATOM 783 N LEU A 97 24.377 -16.197 -24.956 1.00 14.52 N ANISOU 783 N LEU A 97 1770 1797 1947 -31 66 -148 N ATOM 784 CA LEU A 97 24.981 -14.839 -25.021 1.00 15.49 C ANISOU 784 CA LEU A 97 1843 1917 2125 32 64 181 C ATOM 785 C LEU A 97 26.203 -14.653 -24.125 1.00 17.80 C ANISOU 785 C LEU A 97 2368 2280 2116 -28 68 -49 C ATOM 786 O LEU A 97 26.856 -13.619 -24.271 1.00 19.41 O ANISOU 786 O LEU A 97 2439 2390 2546 -146 -5 4 O ATOM 787 CB LEU A 97 23.922 -13.816 -24.662 1.00 15.79 C ANISOU 787 CB LEU A 97 2137 1747 2116 -66 -3 -120 C ATOM 788 CG LEU A 97 22.846 -13.576 -25.683 1.00 17.62 C ANISOU 788 CG LEU A 97 2341 2069 2283 -56 50 -117 C ATOM 789 CD1 LEU A 97 21.821 -12.637 -25.214 1.00 19.97 C ANISOU 789 CD1 LEU A 97 2583 2310 2692 18 -17 68 C ATOM 790 CD2 LEU A 97 23.413 -13.105 -27.006 1.00 21.74 C ANISOU 790 CD2 LEU A 97 2671 2896 2693 26 -140 73 C ATOM 791 N ASP A 98 26.590 -15.629 -23.323 1.00 16.61 N ANISOU 791 N ASP A 98 2068 1975 2265 -43 -43 -93 N ATOM 792 CA ASP A 98 27.801 -15.595 -22.505 1.00 18.60 C ANISOU 792 CA ASP A 98 2528 2181 2359 -59 25 6 C ATOM 793 C ASP A 98 27.890 -14.323 -21.703 1.00 18.50 C ANISOU 793 C ASP A 98 2467 2369 2191 -185 65 -91 C ATOM 794 O ASP A 98 28.738 -13.508 -21.892 1.00 20.28 O ANISOU 794 O ASP A 98 2577 2496 2630 -20 -35 -40 O ATOM 795 CB ASP A 98 29.025 -15.758 -23.383 1.00 20.97 C ANISOU 795 CB ASP A 98 2593 2480 2893 15 70 -224 C ATOM 796 CG ASP A 98 30.293 -16.027 -22.577 1.00 26.62 C ANISOU 796 CG ASP A 98 3328 3442 3341 -115 -210 -159 C ATOM 797 OD1 ASP A 98 30.235 -16.294 -21.402 1.00 29.01 O ANISOU 797 OD1 ASP A 98 3587 3660 3772 263 10 -54 O ATOM 798 OD2 ASP A 98 31.360 -15.983 -23.171 1.00 36.41 O ANISOU 798 OD2 ASP A 98 3993 5256 4582 -152 346 -228 O ATOM 799 N LEU A 99 26.982 -14.235 -20.783 1.00 17.92 N ANISOU 799 N LEU A 99 2296 2137 2373 -12 -76 -227 N ATOM 800 CA LEU A 99 26.817 -12.994 -19.968 1.00 16.32 C ANISOU 800 CA LEU A 99 2215 1870 2116 45 0 -76 C ATOM 801 C LEU A 99 27.883 -12.801 -18.930 1.00 19.96 C ANISOU 801 C LEU A 99 2521 2425 2636 252 -271 -64 C ATOM 802 O LEU A 99 28.018 -11.678 -18.367 1.00 21.33 O ANISOU 802 O LEU A 99 2677 2607 2821 16 -283 -126 O ATOM 803 CB LEU A 99 25.439 -12.974 -19.397 1.00 15.59 C ANISOU 803 CB LEU A 99 2112 1720 2092 72 -12 10 C ATOM 804 CG LEU A 99 24.275 -12.984 -20.304 1.00 16.86 C ANISOU 804 CG LEU A 99 2277 1969 2157 -16 60 -69 C ATOM 805 CD1 LEU A 99 23.037 -13.059 -19.568 1.00 18.92 C ANISOU 805 CD1 LEU A 99 2348 2299 2541 178 -43 -21 C ATOM 806 CD2 LEU A 99 24.209 -11.788 -21.268 1.00 19.95 C ANISOU 806 CD2 LEU A 99 2562 2468 2549 -2 32 115 C ATOM 807 N GLY A 100 28.469 -13.875 -18.418 1.00 18.82 N ANISOU 807 N GLY A 100 2460 2372 2319 72 -151 0 N ATOM 808 CA GLY A 100 29.370 -13.733 -17.257 1.00 18.59 C ANISOU 808 CA GLY A 100 2333 2185 2544 -6 -51 -116 C ATOM 809 C GLY A 100 28.689 -13.577 -15.991 1.00 17.70 C ANISOU 809 C GLY A 100 2202 2165 2354 81 21 41 C ATOM 810 O GLY A 100 27.537 -13.944 -15.809 1.00 16.82 O ANISOU 810 O GLY A 100 2161 1987 2242 36 -81 -84 O ATOM 811 N ASP A 101 29.444 -13.153 -14.993 1.00 19.72 N ANISOU 811 N ASP A 101 2456 2457 2578 168 -77 -151 N ATOM 812 CA ASP A 101 28.967 -13.189 -13.615 1.00 20.83 C ANISOU 812 CA ASP A 101 2599 2646 2667 316 -107 34 C ATOM 813 C ASP A 101 28.730 -11.893 -12.845 1.00 20.81 C ANISOU 813 C ASP A 101 2733 2484 2690 -44 -260 13 C ATOM 814 O ASP A 101 28.644 -11.893 -11.661 1.00 22.84 O ANISOU 814 O ASP A 101 3120 2659 2896 291 64 22 O ATOM 815 CB ASP A 101 29.917 -14.033 -12.758 1.00 23.82 C ANISOU 815 CB ASP A 101 3137 2886 3025 125 -160 28 C ATOM 816 CG ASP A 101 30.110 -15.446 -13.263 1.00 29.82 C ANISOU 816 CG ASP A 101 3900 3601 3827 253 -283 -568 C ATOM 817 OD1 ASP A 101 29.336 -15.968 -14.021 1.00 27.87 O ANISOU 817 OD1 ASP A 101 3373 3404 3813 143 -114 171 O ATOM 818 OD2 ASP A 101 31.107 -16.021 -12.851 1.00 35.84 O ANISOU 818 OD2 ASP A 101 4443 4141 5032 944 -808 -312 O ATOM 819 N ASN A 102 28.640 -10.820 -13.575 1.00 18.88 N ANISOU 819 N ASN A 102 2453 2315 2407 33 -365 189 N ATOM 820 CA ASN A 102 28.390 -9.463 -13.076 1.00 19.72 C ANISOU 820 CA ASN A 102 2491 2651 2350 -41 12 -240 C ATOM 821 C ASN A 102 27.278 -8.819 -13.827 1.00 17.34 C ANISOU 821 C ASN A 102 2114 2059 2413 51 11 102 C ATOM 822 O ASN A 102 27.295 -7.603 -14.252 1.00 18.95 O ANISOU 822 O ASN A 102 2477 2268 2454 -102 -87 0 O ATOM 823 CB ASN A 102 29.594 -8.542 -13.149 1.00 20.75 C ANISOU 823 CB ASN A 102 2595 2484 2805 -34 -78 46 C ATOM 824 CG ASN A 102 30.712 -8.989 -12.144 1.00 29.03 C ANISOU 824 CG ASN A 102 3584 4040 3404 -314 54 -48 C ATOM 825 OD1 ASN A 102 30.445 -9.096 -10.965 1.00 28.27 O ANISOU 825 OD1 ASN A 102 3633 3697 3411 -338 -559 135 O ATOM 826 ND2 ASN A 102 31.893 -9.186 -12.654 1.00 37.88 N ANISOU 826 ND2 ASN A 102 4106 5127 5159 705 -454 -604 N ATOM 827 N VAL A 103 26.138 -9.474 -13.874 1.00 15.91 N ANISOU 827 N VAL A 103 2003 1868 2173 94 -72 -37 N ATOM 828 CA VAL A 103 25.002 -9.061 -14.700 1.00 16.88 C ANISOU 828 CA VAL A 103 2309 2068 2035 27 -28 -91 C ATOM 829 C VAL A 103 24.131 -8.088 -13.899 1.00 15.01 C ANISOU 829 C VAL A 103 1863 1869 1972 77 89 83 C ATOM 830 O VAL A 103 23.763 -8.324 -12.730 1.00 16.39 O ANISOU 830 O VAL A 103 2194 2045 1988 103 -77 -26 O ATOM 831 CB VAL A 103 24.125 -10.282 -15.063 1.00 18.14 C ANISOU 831 CB VAL A 103 2156 2313 2423 -2 0 82 C ATOM 832 CG1 VAL A 103 22.931 -9.820 -15.817 1.00 19.94 C ANISOU 832 CG1 VAL A 103 2569 2418 2588 69 -119 -39 C ATOM 833 CG2 VAL A 103 24.969 -11.321 -15.838 1.00 18.94 C ANISOU 833 CG2 VAL A 103 2540 2370 2285 -7 -43 -61 C ATOM 834 N VAL A 104 23.760 -6.933 -14.538 1.00 15.14 N ANISOU 834 N VAL A 104 1995 1899 1858 9 50 16 N ATOM 835 CA VAL A 104 22.702 -6.118 -14.010 1.00 14.14 C ANISOU 835 CA VAL A 104 1749 1855 1767 55 -21 127 C ATOM 836 C VAL A 104 21.458 -6.376 -14.770 1.00 13.81 C ANISOU 836 C VAL A 104 1778 1723 1745 -76 -19 -40 C ATOM 837 O VAL A 104 21.480 -6.324 -16.033 1.00 15.44 O ANISOU 837 O VAL A 104 1959 2021 1886 17 69 55 O ATOM 838 CB VAL A 104 23.051 -4.622 -14.063 1.00 14.06 C ANISOU 838 CB VAL A 104 1738 1832 1769 -13 -119 18 C ATOM 839 CG1 VAL A 104 21.900 -3.760 -13.692 1.00 16.49 C ANISOU 839 CG1 VAL A 104 2214 1914 2136 0 -29 14 C ATOM 840 CG2 VAL A 104 24.271 -4.303 -13.159 1.00 16.21 C ANISOU 840 CG2 VAL A 104 2016 2025 2117 44 -71 -154 C ATOM 841 N LEU A 105 20.380 -6.713 -14.135 1.00 13.56 N ANISOU 841 N LEU A 105 1755 1706 1689 51 -25 -48 N ATOM 842 CA LEU A 105 19.073 -6.912 -14.653 1.00 13.49 C ANISOU 842 CA LEU A 105 1664 1673 1786 97 -94 28 C ATOM 843 C LEU A 105 18.188 -5.693 -14.523 1.00 14.87 C ANISOU 843 C LEU A 105 1948 1787 1914 52 -59 -102 C ATOM 844 O LEU A 105 18.198 -5.053 -13.467 1.00 16.41 O ANISOU 844 O LEU A 105 2184 2082 1968 146 -39 -43 O ATOM 845 CB LEU A 105 18.359 -8.048 -14.010 1.00 15.77 C ANISOU 845 CB LEU A 105 2038 2001 1950 -84 -28 -17 C ATOM 846 CG LEU A 105 19.007 -9.412 -14.224 1.00 16.62 C ANISOU 846 CG LEU A 105 2000 2225 2090 37 -16 75 C ATOM 847 CD1 LEU A 105 18.505 -10.543 -13.300 1.00 16.70 C ANISOU 847 CD1 LEU A 105 2229 1978 2138 70 22 -59 C ATOM 848 CD2 LEU A 105 18.844 -9.919 -15.572 1.00 20.41 C ANISOU 848 CD2 LEU A 105 2875 2336 2543 56 -15 55 C ATOM 849 N VAL A 106 17.518 -5.346 -15.625 1.00 13.55 N ANISOU 849 N VAL A 106 1785 1616 1746 77 -23 -146 N ATOM 850 CA VAL A 106 16.567 -4.223 -15.680 1.00 13.87 C ANISOU 850 CA VAL A 106 1773 1762 1732 110 -16 62 C ATOM 851 C VAL A 106 15.271 -4.739 -16.156 1.00 12.72 C ANISOU 851 C VAL A 106 1667 1494 1670 16 14 93 C ATOM 852 O VAL A 106 15.181 -5.175 -17.376 1.00 13.65 O ANISOU 852 O VAL A 106 1804 1696 1686 -1 -14 -10 O ATOM 853 CB VAL A 106 17.071 -3.030 -16.542 1.00 13.04 C ANISOU 853 CB VAL A 106 1654 1618 1679 9 98 14 C ATOM 854 CG1 VAL A 106 16.024 -1.973 -16.522 1.00 14.95 C ANISOU 854 CG1 VAL A 106 1899 1883 1896 31 98 43 C ATOM 855 CG2 VAL A 106 18.460 -2.600 -16.131 1.00 14.66 C ANISOU 855 CG2 VAL A 106 1965 1713 1890 40 -28 58 C ATOM 856 N ILE A 107 14.228 -4.860 -15.342 1.00 13.74 N ANISOU 856 N ILE A 107 1785 1718 1716 35 37 -54 N ATOM 857 CA ILE A 107 13.128 -5.731 -15.571 1.00 12.48 C ANISOU 857 CA ILE A 107 1672 1581 1488 -16 100 77 C ATOM 858 C ILE A 107 11.790 -5.183 -15.379 1.00 13.11 C ANISOU 858 C ILE A 107 1713 1642 1623 12 5 105 C ATOM 859 O ILE A 107 11.596 -4.316 -14.420 1.00 14.45 O ANISOU 859 O ILE A 107 1932 1683 1876 1 43 -139 O ATOM 860 CB ILE A 107 13.308 -7.163 -14.870 1.00 13.60 C ANISOU 860 CB ILE A 107 1701 1680 1785 -13 -21 71 C ATOM 861 CG1 ILE A 107 13.359 -6.946 -13.371 1.00 14.71 C ANISOU 861 CG1 ILE A 107 1902 1796 1891 -43 -19 52 C ATOM 862 CG2 ILE A 107 14.558 -7.806 -15.380 1.00 14.80 C ANISOU 862 CG2 ILE A 107 1910 1762 1951 120 15 12 C ATOM 863 CD1 ILE A 107 13.778 -8.225 -12.573 1.00 16.78 C ANISOU 863 CD1 ILE A 107 2159 2005 2209 -9 -33 52 C ATOM 864 N HIS A 108 10.789 -5.616 -16.106 1.00 14.44 N ANISOU 864 N HIS A 108 1827 1784 1875 85 8 -182 N ATOM 865 CA HIS A 108 9.431 -5.117 -16.012 1.00 15.91 C ANISOU 865 CA HIS A 108 1977 2109 1956 109 21 -105 C ATOM 866 C HIS A 108 8.365 -6.211 -16.261 1.00 17.88 C ANISOU 866 C HIS A 108 2201 2270 2322 -83 74 23 C ATOM 867 O HIS A 108 8.602 -7.036 -17.064 1.00 16.64 O ANISOU 867 O HIS A 108 2129 2015 2179 61 100 -24 O ATOM 868 CB HIS A 108 9.276 -4.093 -17.153 1.00 16.67 C ANISOU 868 CB HIS A 108 2103 2035 2194 -16 39 -21 C ATOM 869 CG HIS A 108 7.918 -3.460 -17.259 1.00 14.81 C ANISOU 869 CG HIS A 108 1886 1879 1861 -5 12 83 C ATOM 870 ND1 HIS A 108 7.154 -3.537 -18.389 1.00 16.65 N ANISOU 870 ND1 HIS A 108 2181 2028 2114 69 0 5 N ATOM 871 CD2 HIS A 108 7.206 -2.733 -16.379 1.00 16.91 C ANISOU 871 CD2 HIS A 108 2169 2067 2188 29 -48 -64 C ATOM 872 CE1 HIS A 108 6.025 -2.895 -18.202 1.00 17.83 C ANISOU 872 CE1 HIS A 108 2259 2258 2256 120 17 57 C ATOM 873 NE2 HIS A 108 6.028 -2.405 -16.984 1.00 15.55 N ANISOU 873 NE2 HIS A 108 2004 1919 1984 7 -130 -29 N ATOM 874 N ASP A 109 7.206 -6.184 -15.615 1.00 18.56 N ANISOU 874 N ASP A 109 2381 2349 2321 19 251 -92 N ATOM 875 CA ASP A 109 6.110 -7.128 -15.993 1.00 18.51 C ANISOU 875 CA ASP A 109 2499 2239 2294 16 68 78 C ATOM 876 C ASP A 109 6.548 -8.592 -16.045 1.00 17.62 C ANISOU 876 C ASP A 109 2252 2208 2233 226 -61 -160 C ATOM 877 O ASP A 109 7.193 -9.024 -15.142 1.00 19.28 O ANISOU 877 O ASP A 109 2584 2447 2292 111 -16 -193 O ATOM 878 CB ASP A 109 5.581 -6.652 -17.355 1.00 18.75 C ANISOU 878 CB ASP A 109 2214 2378 2529 33 -135 -36 C ATOM 879 CG ASP A 109 4.294 -7.303 -17.790 1.00 25.90 C ANISOU 879 CG ASP A 109 3310 3240 3291 -642 -166 -619 C ATOM 880 OD1 ASP A 109 3.275 -6.788 -17.411 1.00 39.37 O ANISOU 880 OD1 ASP A 109 3955 4734 6267 -80 -227 -1947 O ATOM 881 OD2 ASP A 109 4.293 -8.234 -18.529 1.00 17.99 O ANISOU 881 OD2 ASP A 109 2304 2245 2286 154 61 87 O ATOM 882 N TRP A 110 6.181 -9.360 -17.070 1.00 15.54 N ANISOU 882 N TRP A 110 1946 1933 2025 79 -2 6 N ATOM 883 CA TRP A 110 6.725 -10.728 -17.080 1.00 13.59 C ANISOU 883 CA TRP A 110 1809 1661 1694 -45 74 72 C ATOM 884 C TRP A 110 8.181 -10.792 -17.204 1.00 14.64 C ANISOU 884 C TRP A 110 1898 1841 1821 -10 -67 44 C ATOM 885 O TRP A 110 8.817 -11.809 -16.872 1.00 15.27 O ANISOU 885 O TRP A 110 1980 1858 1962 95 48 64 O ATOM 886 CB TRP A 110 5.996 -11.504 -18.236 1.00 12.78 C ANISOU 886 CB TRP A 110 1656 1534 1666 -69 6 49 C ATOM 887 CG TRP A 110 4.639 -11.910 -17.814 1.00 13.71 C ANISOU 887 CG TRP A 110 1731 1731 1745 85 14 11 C ATOM 888 CD1 TRP A 110 3.475 -11.410 -18.210 1.00 16.06 C ANISOU 888 CD1 TRP A 110 2049 2120 1931 -27 39 -68 C ATOM 889 CD2 TRP A 110 4.365 -12.870 -16.783 1.00 13.92 C ANISOU 889 CD2 TRP A 110 1729 1771 1787 -28 -14 2 C ATOM 890 NE1 TRP A 110 2.432 -12.011 -17.537 1.00 17.22 N ANISOU 890 NE1 TRP A 110 2108 2163 2270 -111 77 1 N ATOM 891 CE2 TRP A 110 2.986 -12.918 -16.651 1.00 15.10 C ANISOU 891 CE2 TRP A 110 1937 1874 1923 -38 8 29 C ATOM 892 CE3 TRP A 110 5.175 -13.698 -16.026 1.00 15.03 C ANISOU 892 CE3 TRP A 110 1932 1888 1889 22 109 51 C ATOM 893 CZ2 TRP A 110 2.410 -13.822 -15.786 1.00 16.47 C ANISOU 893 CZ2 TRP A 110 1973 2148 2136 -92 104 138 C ATOM 894 CZ3 TRP A 110 4.571 -14.619 -15.186 1.00 15.92 C ANISOU 894 CZ3 TRP A 110 2034 1973 2040 23 0 142 C ATOM 895 CH2 TRP A 110 3.205 -14.576 -15.015 1.00 17.30 C ANISOU 895 CH2 TRP A 110 2093 2155 2323 -93 68 235 C ATOM 896 N GLY A 111 8.859 -9.757 -17.727 1.00 13.17 N ANISOU 896 N GLY A 111 1693 1646 1666 -103 36 -1 N ATOM 897 CA GLY A 111 10.297 -9.699 -17.681 1.00 14.58 C ANISOU 897 CA GLY A 111 1841 1870 1826 122 -15 69 C ATOM 898 C GLY A 111 10.871 -9.755 -16.272 1.00 13.39 C ANISOU 898 C GLY A 111 1639 1690 1755 -199 -15 31 C ATOM 899 O GLY A 111 11.983 -10.207 -16.066 1.00 13.90 O ANISOU 899 O GLY A 111 1809 1703 1768 92 14 16 O ATOM 900 N SER A 112 10.129 -9.223 -15.326 1.00 13.81 N ANISOU 900 N SER A 112 1803 1697 1745 88 -57 68 N ATOM 901 CA SER A 112 10.574 -9.254 -13.897 1.00 13.90 C ANISOU 901 CA SER A 112 1854 1675 1749 -12 70 -63 C ATOM 902 C SER A 112 10.377 -10.700 -13.335 1.00 12.93 C ANISOU 902 C SER A 112 1678 1614 1617 19 9 40 C ATOM 903 O SER A 112 11.285 -11.080 -12.649 1.00 14.93 O ANISOU 903 O SER A 112 1934 1829 1910 61 -70 -44 O ATOM 904 CB SER A 112 9.799 -8.281 -13.027 1.00 14.21 C ANISOU 904 CB SER A 112 1918 1672 1809 95 -33 -104 C ATOM 905 OG SER A 112 8.448 -8.524 -12.908 1.00 15.10 O ANISOU 905 OG SER A 112 1927 1843 1967 112 88 -65 O ATOM 906 N ALA A 113 9.310 -11.374 -13.737 1.00 13.84 N ANISOU 906 N ALA A 113 1799 1663 1795 76 -18 106 N ATOM 907 CA ALA A 113 9.196 -12.820 -13.223 1.00 15.39 C ANISOU 907 CA ALA A 113 1918 1942 1986 -47 48 88 C ATOM 908 C ALA A 113 10.340 -13.601 -13.745 1.00 14.91 C ANISOU 908 C ALA A 113 1882 1952 1829 62 -51 -125 C ATOM 909 O ALA A 113 11.073 -14.282 -13.063 1.00 15.17 O ANISOU 909 O ALA A 113 2097 1832 1833 83 42 21 O ATOM 910 CB ALA A 113 7.926 -13.380 -13.547 1.00 15.98 C ANISOU 910 CB ALA A 113 2029 1909 2130 -104 14 -13 C ATOM 911 N LEU A 114 10.637 -13.488 -15.058 1.00 14.18 N ANISOU 911 N LEU A 114 1873 1719 1792 -23 59 60 N ATOM 912 CA LEU A 114 11.710 -14.187 -15.612 1.00 13.85 C ANISOU 912 CA LEU A 114 1860 1615 1786 81 121 181 C ATOM 913 C LEU A 114 13.034 -13.817 -15.082 1.00 15.04 C ANISOU 913 C LEU A 114 1954 1898 1862 96 14 -33 C ATOM 914 O LEU A 114 13.927 -14.628 -14.812 1.00 15.29 O ANISOU 914 O LEU A 114 1998 1895 1915 72 -35 79 O ATOM 915 CB LEU A 114 11.659 -14.009 -17.182 1.00 14.75 C ANISOU 915 CB LEU A 114 1907 1915 1781 128 11 -56 C ATOM 916 CG LEU A 114 10.552 -14.650 -17.901 1.00 15.16 C ANISOU 916 CG LEU A 114 2047 1850 1859 -14 -31 93 C ATOM 917 CD1 LEU A 114 10.267 -13.940 -19.255 1.00 16.43 C ANISOU 917 CD1 LEU A 114 2180 2122 1941 86 -21 21 C ATOM 918 CD2 LEU A 114 10.859 -16.162 -18.148 1.00 16.80 C ANISOU 918 CD2 LEU A 114 2129 2034 2220 150 -47 -113 C ATOM 919 N GLY A 115 13.323 -12.515 -14.921 1.00 13.79 N ANISOU 919 N GLY A 115 1790 1775 1674 -7 -16 6 N ATOM 920 CA GLY A 115 14.564 -12.072 -14.423 1.00 14.83 C ANISOU 920 CA GLY A 115 1907 1807 1918 -52 -23 34 C ATOM 921 C GLY A 115 14.804 -12.361 -12.906 1.00 13.77 C ANISOU 921 C GLY A 115 1693 1757 1781 -138 -21 22 C ATOM 922 O GLY A 115 15.915 -12.750 -12.550 1.00 14.37 O ANISOU 922 O GLY A 115 1891 1718 1850 28 8 -25 O ATOM 923 N PHE A 116 13.787 -12.190 -12.098 1.00 13.32 N ANISOU 923 N PHE A 116 1805 1608 1646 84 -24 -18 N ATOM 924 CA PHE A 116 13.908 -12.505 -10.696 1.00 14.48 C ANISOU 924 CA PHE A 116 1948 1716 1837 180 87 22 C ATOM 925 C PHE A 116 14.141 -14.018 -10.568 1.00 13.76 C ANISOU 925 C PHE A 116 1850 1612 1766 -29 -102 -14 C ATOM 926 O PHE A 116 14.877 -14.402 -9.757 1.00 15.62 O ANISOU 926 O PHE A 116 2067 1878 1988 142 -123 -49 O ATOM 927 CB PHE A 116 12.629 -12.167 -9.939 1.00 14.94 C ANISOU 927 CB PHE A 116 1999 1842 1834 161 147 58 C ATOM 928 CG PHE A 116 12.426 -10.700 -9.614 1.00 14.61 C ANISOU 928 CG PHE A 116 1945 1875 1729 -15 -79 79 C ATOM 929 CD1 PHE A 116 13.441 -9.902 -9.196 1.00 14.20 C ANISOU 929 CD1 PHE A 116 1892 1685 1815 49 117 26 C ATOM 930 CD2 PHE A 116 11.164 -10.185 -9.671 1.00 15.04 C ANISOU 930 CD2 PHE A 116 1975 1883 1854 -50 69 -138 C ATOM 931 CE1 PHE A 116 13.197 -8.599 -8.878 1.00 16.32 C ANISOU 931 CE1 PHE A 116 2229 1992 1978 52 70 49 C ATOM 932 CE2 PHE A 116 10.923 -8.874 -9.345 1.00 15.64 C ANISOU 932 CE2 PHE A 116 2070 2029 1841 103 145 114 C ATOM 933 CZ PHE A 116 11.938 -8.106 -8.938 1.00 14.79 C ANISOU 933 CZ PHE A 116 1987 1819 1814 24 68 46 C ATOM 934 N ASP A 117 13.442 -14.825 -11.361 1.00 14.28 N ANISOU 934 N ASP A 117 1912 1706 1807 102 -101 63 N ATOM 935 CA ASP A 117 13.644 -16.319 -11.318 1.00 13.80 C ANISOU 935 CA ASP A 117 1866 1601 1775 81 57 156 C ATOM 936 C ASP A 117 15.037 -16.621 -11.742 1.00 15.19 C ANISOU 936 C ASP A 117 1889 2037 1845 19 -10 -47 C ATOM 937 O ASP A 117 15.813 -17.389 -11.043 1.00 16.49 O ANISOU 937 O ASP A 117 2204 1937 2124 85 -29 -2 O ATOM 938 CB ASP A 117 12.642 -16.922 -12.168 1.00 15.57 C ANISOU 938 CB ASP A 117 2064 1857 1995 14 17 132 C ATOM 939 CG ASP A 117 12.623 -18.481 -12.225 1.00 19.53 C ANISOU 939 CG ASP A 117 2761 2180 2476 -202 -202 -27 C ATOM 940 OD1 ASP A 117 12.985 -19.061 -11.122 1.00 18.89 O ANISOU 940 OD1 ASP A 117 2533 2301 2343 112 -153 -33 O ATOM 941 OD2 ASP A 117 12.079 -19.021 -13.207 1.00 19.00 O ANISOU 941 OD2 ASP A 117 2603 2291 2324 60 -98 139 O ATOM 942 N TRP A 118 15.550 -16.061 -12.843 1.00 13.35 N ANISOU 942 N TRP A 118 1770 1525 1776 94 68 132 N ATOM 943 CA TRP A 118 16.926 -16.254 -13.248 1.00 13.91 C ANISOU 943 CA TRP A 118 1827 1651 1806 -6 -62 144 C ATOM 944 C TRP A 118 17.913 -15.910 -12.185 1.00 16.71 C ANISOU 944 C TRP A 118 2126 2137 2086 62 -41 -124 C ATOM 945 O TRP A 118 18.849 -16.623 -11.906 1.00 15.65 O ANISOU 945 O TRP A 118 2068 1866 2012 17 -85 21 O ATOM 946 CB TRP A 118 17.226 -15.544 -14.535 1.00 15.66 C ANISOU 946 CB TRP A 118 2008 1973 1968 46 78 97 C ATOM 947 CG TRP A 118 18.525 -15.962 -15.231 1.00 14.87 C ANISOU 947 CG TRP A 118 1878 1857 1913 197 25 24 C ATOM 948 CD1 TRP A 118 18.608 -17.029 -16.125 1.00 14.99 C ANISOU 948 CD1 TRP A 118 1898 1955 1843 -58 -131 0 C ATOM 949 CD2 TRP A 118 19.820 -15.435 -15.104 1.00 15.19 C ANISOU 949 CD2 TRP A 118 2037 1813 1919 0 -86 7 C ATOM 950 NE1 TRP A 118 19.897 -17.152 -16.564 1.00 15.24 N ANISOU 950 NE1 TRP A 118 1942 1915 1931 63 -3 -37 N ATOM 951 CE2 TRP A 118 20.673 -16.158 -15.989 1.00 15.17 C ANISOU 951 CE2 TRP A 118 1860 1902 2001 8 -24 83 C ATOM 952 CE3 TRP A 118 20.370 -14.381 -14.394 1.00 16.84 C ANISOU 952 CE3 TRP A 118 2188 2025 2183 85 -4 -42 C ATOM 953 CZ2 TRP A 118 22.023 -15.891 -16.150 1.00 16.85 C ANISOU 953 CZ2 TRP A 118 2198 2121 2082 105 43 -4 C ATOM 954 CZ3 TRP A 118 21.689 -14.118 -14.528 1.00 17.35 C ANISOU 954 CZ3 TRP A 118 2242 2155 2194 -118 -147 -85 C ATOM 955 CH2 TRP A 118 22.529 -14.813 -15.415 1.00 17.32 C ANISOU 955 CH2 TRP A 118 2086 2185 2309 -97 -140 111 C ATOM 956 N ALA A 119 17.777 -14.743 -11.524 1.00 14.15 N ANISOU 956 N ALA A 119 1867 1689 1819 129 -188 62 N ATOM 957 CA ALA A 119 18.628 -14.343 -10.540 1.00 15.17 C ANISOU 957 CA ALA A 119 1970 1817 1977 -41 -96 -37 C ATOM 958 C ALA A 119 18.523 -15.308 -9.350 1.00 15.78 C ANISOU 958 C ALA A 119 1951 2012 2032 -11 48 -65 C ATOM 959 O ALA A 119 19.634 -15.602 -8.816 1.00 16.28 O ANISOU 959 O ALA A 119 2099 1947 2137 63 -218 92 O ATOM 960 CB ALA A 119 18.309 -12.880 -10.095 1.00 16.17 C ANISOU 960 CB ALA A 119 2091 1992 2059 170 14 -25 C ATOM 961 N ASN A 120 17.356 -15.750 -8.968 1.00 15.48 N ANISOU 961 N ASN A 120 2089 1932 1860 -84 -124 159 N ATOM 962 CA ASN A 120 17.230 -16.691 -7.874 1.00 15.52 C ANISOU 962 CA ASN A 120 2138 1905 1853 -18 -155 159 C ATOM 963 C ASN A 120 18.003 -17.972 -8.184 1.00 17.85 C ANISOU 963 C ASN A 120 2369 2245 2166 79 83 -47 C ATOM 964 O ASN A 120 18.537 -18.568 -7.304 1.00 20.25 O ANISOU 964 O ASN A 120 2684 2513 2495 153 -133 91 O ATOM 965 CB ASN A 120 15.758 -16.984 -7.624 1.00 16.66 C ANISOU 965 CB ASN A 120 2306 2017 2006 -28 96 106 C ATOM 966 CG ASN A 120 15.519 -17.728 -6.330 1.00 17.06 C ANISOU 966 CG ASN A 120 2241 2060 2179 31 -134 14 C ATOM 967 OD1 ASN A 120 16.313 -17.695 -5.456 1.00 19.73 O ANISOU 967 OD1 ASN A 120 2724 2309 2463 46 -110 128 O ATOM 968 ND2 ASN A 120 14.422 -18.385 -6.259 1.00 18.58 N ANISOU 968 ND2 ASN A 120 2441 2205 2411 33 175 320 N ATOM 969 N GLN A 121 18.032 -18.369 -9.439 1.00 15.14 N ANISOU 969 N GLN A 121 2054 1758 1938 139 -65 69 N ATOM 970 CA GLN A 121 18.789 -19.586 -9.849 1.00 16.91 C ANISOU 970 CA GLN A 121 2315 1998 2111 150 50 25 C ATOM 971 C GLN A 121 20.209 -19.381 -10.062 1.00 20.17 C ANISOU 971 C GLN A 121 2446 2563 2652 -41 -161 -119 C ATOM 972 O GLN A 121 20.996 -20.305 -10.331 1.00 23.88 O ANISOU 972 O GLN A 121 3152 2689 3229 184 -13 87 O ATOM 973 CB GLN A 121 18.078 -20.160 -11.094 1.00 19.28 C ANISOU 973 CB GLN A 121 2590 2257 2477 226 -77 60 C ATOM 974 CG GLN A 121 16.670 -20.610 -10.791 1.00 20.77 C ANISOU 974 CG GLN A 121 2726 2379 2783 349 -142 -125 C ATOM 975 CD GLN A 121 16.019 -21.356 -11.955 1.00 26.91 C ANISOU 975 CD GLN A 121 3323 3446 3456 -303 -300 -160 C ATOM 976 OE1 GLN A 121 16.695 -22.227 -12.533 1.00 32.00 O ANISOU 976 OE1 GLN A 121 3775 3829 4552 201 104 -687 O ATOM 977 NE2 GLN A 121 14.814 -21.033 -12.366 1.00 24.91 N ANISOU 977 NE2 GLN A 121 3178 2977 3309 307 -104 167 N ATOM 978 N HIS A 122 20.726 -18.121 -10.214 1.00 16.07 N ANISOU 978 N HIS A 122 2083 1896 2125 104 -43 76 N ATOM 979 CA HIS A 122 22.061 -17.755 -10.503 1.00 16.32 C ANISOU 979 CA HIS A 122 2124 1955 2121 215 -61 26 C ATOM 980 C HIS A 122 22.477 -16.615 -9.582 1.00 17.68 C ANISOU 980 C HIS A 122 2178 2267 2272 35 10 -15 C ATOM 981 O HIS A 122 22.966 -15.536 -10.032 1.00 19.01 O ANISOU 981 O HIS A 122 2564 2306 2350 -3 -144 110 O ATOM 982 CB HIS A 122 22.230 -17.351 -11.968 1.00 16.89 C ANISOU 982 CB HIS A 122 2100 2068 2248 155 -34 -24 C ATOM 983 CG HIS A 122 21.772 -18.374 -12.936 1.00 18.19 C ANISOU 983 CG HIS A 122 2292 2180 2438 116 39 -117 C ATOM 984 ND1 HIS A 122 20.488 -18.473 -13.422 1.00 19.99 N ANISOU 984 ND1 HIS A 122 2803 2288 2503 -82 -176 -298 N ATOM 985 CD2 HIS A 122 22.499 -19.402 -13.487 1.00 22.23 C ANISOU 985 CD2 HIS A 122 2613 2723 3110 91 132 -232 C ATOM 986 CE1 HIS A 122 20.435 -19.576 -14.208 1.00 21.42 C ANISOU 986 CE1 HIS A 122 2788 2747 2600 -7 -90 -120 C ATOM 987 NE2 HIS A 122 21.609 -20.055 -14.323 1.00 20.44 N ANISOU 987 NE2 HIS A 122 2720 2476 2568 108 9 -235 N ATOM 988 N ARG A 123 22.329 -16.809 -8.290 1.00 18.56 N ANISOU 988 N ARG A 123 2548 2204 2300 18 -167 -62 N ATOM 989 CA ARG A 123 22.595 -15.750 -7.325 1.00 18.04 C ANISOU 989 CA ARG A 123 2382 2159 2312 99 -80 -11 C ATOM 990 C ARG A 123 23.990 -15.173 -7.348 1.00 19.24 C ANISOU 990 C ARG A 123 2596 2441 2272 66 -49 68 C ATOM 991 O ARG A 123 24.169 -14.034 -7.044 1.00 25.55 O ANISOU 991 O ARG A 123 3354 2908 3446 -92 -318 -278 O ATOM 992 CB ARG A 123 22.218 -16.191 -5.907 1.00 21.14 C ANISOU 992 CB ARG A 123 2803 2699 2529 9 -3 -103 C ATOM 993 CG ARG A 123 20.757 -16.535 -5.695 1.00 20.19 C ANISOU 993 CG ARG A 123 2668 2615 2386 248 193 53 C ATOM 994 CD ARG A 123 20.506 -17.192 -4.351 1.00 20.51 C ANISOU 994 CD ARG A 123 2787 2630 2374 126 -32 -20 C ATOM 995 NE ARG A 123 19.165 -17.681 -4.207 1.00 19.99 N ANISOU 995 NE ARG A 123 2684 2543 2366 153 -43 150 N ATOM 996 CZ ARG A 123 18.685 -18.155 -3.086 1.00 22.14 C ANISOU 996 CZ ARG A 123 2743 2905 2764 42 50 16 C ATOM 997 NH1 ARG A 123 19.456 -18.163 -2.046 1.00 26.47 N ANISOU 997 NH1 ARG A 123 3339 3503 3212 296 -182 249 N ATOM 998 NH2 ARG A 123 17.450 -18.571 -2.996 1.00 21.38 N ANISOU 998 NH2 ARG A 123 3004 2647 2470 26 3 230 N ATOM 999 N ASP A 124 24.947 -15.963 -7.746 1.00 17.61 N ANISOU 999 N ASP A 124 2270 2225 2195 -8 -149 82 N ATOM 1000 CA ASP A 124 26.298 -15.519 -7.798 1.00 21.27 C ANISOU 1000 CA ASP A 124 2800 2662 2620 -1 -3 43 C ATOM 1001 C ASP A 124 26.690 -14.775 -9.075 1.00 20.11 C ANISOU 1001 C ASP A 124 2537 2670 2431 -113 -101 20 C ATOM 1002 O ASP A 124 27.783 -14.356 -9.223 1.00 24.97 O ANISOU 1002 O ASP A 124 3058 3388 3040 -94 -284 421 O ATOM 1003 CB ASP A 124 27.185 -16.740 -7.660 1.00 24.46 C ANISOU 1003 CB ASP A 124 3087 3044 3159 299 -200 246 C ATOM 1004 CG ASP A 124 26.954 -17.765 -8.776 1.00 33.86 C ANISOU 1004 CG ASP A 124 4107 4269 4487 -10 -575 -450 C ATOM 1005 OD1 ASP A 124 25.829 -18.065 -9.171 1.00 25.37 O ANISOU 1005 OD1 ASP A 124 3335 3007 3296 311 -90 -82 O ATOM 1006 OD2 ASP A 124 27.955 -18.275 -9.248 1.00 44.57 O ANISOU 1006 OD2 ASP A 124 4978 5947 6007 656 91 -1368 O ATOM 1007 N ARG A 125 25.766 -14.629 -9.996 1.00 16.42 N ANISOU 1007 N ARG A 125 2064 1999 2176 46 -50 0 N ATOM 1008 CA ARG A 125 26.065 -13.982 -11.257 1.00 16.82 C ANISOU 1008 CA ARG A 125 2211 2044 2133 44 -12 -74 C ATOM 1009 C ARG A 125 25.379 -12.619 -11.435 1.00 18.71 C ANISOU 1009 C ARG A 125 2440 2302 2365 77 197 17 C ATOM 1010 O ARG A 125 25.556 -12.006 -12.432 1.00 18.39 O ANISOU 1010 O ARG A 125 2481 2238 2267 151 41 1 O ATOM 1011 CB ARG A 125 25.663 -14.892 -12.421 1.00 18.85 C ANISOU 1011 CB ARG A 125 2442 2415 2304 173 -122 -45 C ATOM 1012 CG ARG A 125 26.419 -16.204 -12.458 1.00 18.15 C ANISOU 1012 CG ARG A 125 2345 2246 2304 75 -35 -35 C ATOM 1013 CD ARG A 125 26.092 -17.081 -13.662 1.00 17.75 C ANISOU 1013 CD ARG A 125 2363 2139 2242 16 -38 -69 C ATOM 1014 NE ARG A 125 26.246 -16.383 -14.902 1.00 17.60 N ANISOU 1014 NE ARG A 125 2198 2219 2267 -20 -150 39 N ATOM 1015 CZ ARG A 125 25.724 -16.748 -16.055 1.00 17.38 C ANISOU 1015 CZ ARG A 125 2326 2106 2173 5 -22 20 C ATOM 1016 NH1 ARG A 125 25.024 -17.856 -16.172 1.00 18.62 N ANISOU 1016 NH1 ARG A 125 2425 2320 2329 -177 -69 -158 N ATOM 1017 NH2 ARG A 125 25.889 -15.983 -17.079 1.00 18.33 N ANISOU 1017 NH2 ARG A 125 2335 2284 2343 -89 22 -28 N ATOM 1018 N VAL A 126 24.641 -12.174 -10.420 1.00 17.75 N ANISOU 1018 N VAL A 126 2374 2188 2179 134 -46 -49 N ATOM 1019 CA VAL A 126 23.848 -10.944 -10.551 1.00 17.26 C ANISOU 1019 CA VAL A 126 2271 2175 2112 53 -103 -17 C ATOM 1020 C VAL A 126 24.492 -9.887 -9.679 1.00 17.95 C ANISOU 1020 C VAL A 126 2489 2102 2230 43 -24 -19 C ATOM 1021 O VAL A 126 24.531 -10.044 -8.469 1.00 19.47 O ANISOU 1021 O VAL A 126 2794 2190 2412 1 52 -16 O ATOM 1022 CB VAL A 126 22.436 -11.211 -10.253 1.00 17.13 C ANISOU 1022 CB VAL A 126 2204 2155 2148 109 -86 -121 C ATOM 1023 CG1 VAL A 126 21.624 -9.928 -10.307 1.00 21.34 C ANISOU 1023 CG1 VAL A 126 2666 2443 2996 81 61 98 C ATOM 1024 CG2 VAL A 126 21.824 -12.162 -11.332 1.00 20.58 C ANISOU 1024 CG2 VAL A 126 2543 2505 2769 -70 -102 -150 C ATOM 1025 N GLN A 127 24.898 -8.790 -10.277 1.00 16.46 N ANISOU 1025 N GLN A 127 2153 2041 2058 -4 -43 -95 N ATOM 1026 CA GLN A 127 25.472 -7.626 -9.607 1.00 16.14 C ANISOU 1026 CA GLN A 127 1987 2023 2122 145 -228 -93 C ATOM 1027 C GLN A 127 24.452 -6.749 -9.053 1.00 16.95 C ANISOU 1027 C GLN A 127 2128 2241 2068 19 -7 10 C ATOM 1028 O GLN A 127 24.670 -6.082 -8.022 1.00 17.30 O ANISOU 1028 O GLN A 127 2258 2071 2242 86 -106 -100 O ATOM 1029 CB GLN A 127 26.371 -6.947 -10.601 1.00 18.02 C ANISOU 1029 CB GLN A 127 2330 2114 2400 118 -196 -11 C ATOM 1030 CG GLN A 127 27.220 -5.750 -10.090 1.00 16.74 C ANISOU 1030 CG GLN A 127 2091 2045 2223 68 -190 -20 C ATOM 1031 CD GLN A 127 28.019 -5.219 -11.152 1.00 20.03 C ANISOU 1031 CD GLN A 127 2659 2418 2532 -177 -43 -129 C ATOM 1032 OE1 GLN A 127 27.569 -4.832 -12.243 1.00 20.90 O ANISOU 1032 OE1 GLN A 127 2571 2577 2793 -83 -192 123 O ATOM 1033 NE2 GLN A 127 29.368 -5.323 -11.010 1.00 24.51 N ANISOU 1033 NE2 GLN A 127 2796 3016 3499 69 -246 -96 N ATOM 1034 N GLY A 128 23.273 -6.626 -9.688 1.00 15.94 N ANISOU 1034 N GLY A 128 2052 1927 2075 63 -129 -119 N ATOM 1035 CA GLY A 128 22.218 -5.747 -9.146 1.00 16.23 C ANISOU 1035 CA GLY A 128 2058 1990 2117 -37 -31 7 C ATOM 1036 C GLY A 128 20.963 -5.915 -10.010 1.00 13.30 C ANISOU 1036 C GLY A 128 1773 1583 1696 83 -103 22 C ATOM 1037 O GLY A 128 21.043 -6.416 -11.141 1.00 14.74 O ANISOU 1037 O GLY A 128 1936 1776 1885 145 5 -20 O ATOM 1038 N ILE A 129 19.843 -5.569 -9.443 1.00 13.43 N ANISOU 1038 N ILE A 129 1712 1671 1720 -70 -34 -68 N ATOM 1039 CA ILE A 129 18.504 -5.673 -10.024 1.00 13.58 C ANISOU 1039 CA ILE A 129 1712 1778 1667 126 -34 -60 C ATOM 1040 C ILE A 129 17.788 -4.350 -9.954 1.00 14.76 C ANISOU 1040 C ILE A 129 1957 1817 1831 40 29 0 C ATOM 1041 O ILE A 129 17.528 -3.886 -8.853 1.00 15.60 O ANISOU 1041 O ILE A 129 2069 1899 1959 -7 25 8 O ATOM 1042 CB ILE A 129 17.677 -6.749 -9.457 1.00 15.13 C ANISOU 1042 CB ILE A 129 1961 1922 1863 67 26 -49 C ATOM 1043 CG1 ILE A 129 18.410 -8.090 -9.478 1.00 17.59 C ANISOU 1043 CG1 ILE A 129 2319 2214 2147 110 48 -5 C ATOM 1044 CG2 ILE A 129 16.372 -6.849 -10.192 1.00 17.54 C ANISOU 1044 CG2 ILE A 129 2155 2184 2324 5 56 -47 C ATOM 1045 CD1 ILE A 129 17.717 -9.238 -8.822 1.00 20.36 C ANISOU 1045 CD1 ILE A 129 2643 2381 2711 54 124 72 C ATOM 1046 N ALA A 130 17.406 -3.768 -11.137 1.00 14.08 N ANISOU 1046 N ALA A 130 1788 1801 1761 138 21 -81 N ATOM 1047 CA ALA A 130 16.502 -2.645 -11.203 1.00 13.53 C ANISOU 1047 CA ALA A 130 1738 1679 1724 76 -118 76 C ATOM 1048 C ALA A 130 15.189 -3.118 -11.673 1.00 14.10 C ANISOU 1048 C ALA A 130 1836 1678 1842 30 72 107 C ATOM 1049 O ALA A 130 15.115 -3.811 -12.750 1.00 15.24 O ANISOU 1049 O ALA A 130 1991 1912 1885 34 -64 -80 O ATOM 1050 CB ALA A 130 17.070 -1.609 -12.156 1.00 14.68 C ANISOU 1050 CB ALA A 130 1843 1780 1954 -40 -105 -165 C ATOM 1051 N TYR A 131 14.116 -2.856 -10.967 1.00 13.19 N ANISOU 1051 N TYR A 131 1708 1694 1608 -17 51 8 N ATOM 1052 CA TYR A 131 12.816 -3.361 -11.352 1.00 13.25 C ANISOU 1052 CA TYR A 131 1728 1689 1615 -5 39 -45 C ATOM 1053 C TYR A 131 11.733 -2.299 -11.214 1.00 14.82 C ANISOU 1053 C TYR A 131 1920 1899 1810 -77 4 36 C ATOM 1054 O TYR A 131 11.888 -1.391 -10.504 1.00 14.55 O ANISOU 1054 O TYR A 131 1941 1789 1798 42 -9 -24 O ATOM 1055 CB TYR A 131 12.466 -4.627 -10.515 1.00 15.39 C ANISOU 1055 CB TYR A 131 1942 1924 1981 31 14 -46 C ATOM 1056 CG TYR A 131 12.266 -4.360 -9.030 1.00 13.55 C ANISOU 1056 CG TYR A 131 1798 1607 1740 10 0 130 C ATOM 1057 CD1 TYR A 131 13.310 -4.326 -8.175 1.00 14.27 C ANISOU 1057 CD1 TYR A 131 1785 1810 1825 14 99 -86 C ATOM 1058 CD2 TYR A 131 11.027 -4.125 -8.537 1.00 14.98 C ANISOU 1058 CD2 TYR A 131 2006 1854 1830 82 -3 51 C ATOM 1059 CE1 TYR A 131 13.131 -4.053 -6.844 1.00 15.00 C ANISOU 1059 CE1 TYR A 131 1964 1879 1856 58 1 35 C ATOM 1060 CE2 TYR A 131 10.824 -3.853 -7.215 1.00 15.61 C ANISOU 1060 CE2 TYR A 131 2032 1920 1976 -62 172 -94 C ATOM 1061 CZ TYR A 131 11.884 -3.823 -6.373 1.00 14.76 C ANISOU 1061 CZ TYR A 131 1952 1813 1840 19 -63 118 C ATOM 1062 OH TYR A 131 11.681 -3.568 -5.053 1.00 16.88 O ANISOU 1062 OH TYR A 131 2250 2058 2104 59 118 -87 O ATOM 1063 N MET A 132 10.642 -2.506 -11.917 1.00 14.16 N ANISOU 1063 N MET A 132 1758 1821 1800 43 62 -61 N ATOM 1064 CA MET A 132 9.519 -1.613 -11.963 1.00 14.25 C ANISOU 1064 CA MET A 132 1854 1759 1798 98 -90 -14 C ATOM 1065 C MET A 132 8.297 -2.302 -12.379 1.00 15.05 C ANISOU 1065 C MET A 132 1916 1909 1892 -94 86 109 C ATOM 1066 O MET A 132 8.353 -3.148 -13.322 1.00 15.30 O ANISOU 1066 O MET A 132 1941 1874 1999 26 37 -96 O ATOM 1067 CB MET A 132 9.912 -0.487 -12.928 1.00 16.12 C ANISOU 1067 CB MET A 132 2138 1901 2086 102 -29 1 C ATOM 1068 CG MET A 132 10.052 -0.842 -14.383 1.00 17.06 C ANISOU 1068 CG MET A 132 2241 2013 2228 -4 121 142 C ATOM 1069 SD MET A 132 11.338 0.141 -15.219 1.00 17.84 S ANISOU 1069 SD MET A 132 2326 2216 2234 -36 83 31 S ATOM 1070 CE MET A 132 12.779 -0.574 -14.625 1.00 18.42 C ANISOU 1070 CE MET A 132 2276 2379 2343 -399 133 -465 C ATOM 1071 N GLU A 133 7.165 -1.982 -11.808 1.00 14.48 N ANISOU 1071 N GLU A 133 1906 1703 1892 10 14 -118 N ATOM 1072 CA GLU A 133 5.901 -2.531 -12.227 1.00 14.61 C ANISOU 1072 CA GLU A 133 1767 1865 1917 139 143 -52 C ATOM 1073 C GLU A 133 6.050 -4.013 -12.535 1.00 15.67 C ANISOU 1073 C GLU A 133 2027 1979 1946 89 25 -141 C ATOM 1074 O GLU A 133 5.709 -4.491 -13.555 1.00 15.69 O ANISOU 1074 O GLU A 133 1943 2033 1985 39 -53 45 O ATOM 1075 CB GLU A 133 5.325 -1.707 -13.371 1.00 16.00 C ANISOU 1075 CB GLU A 133 2056 2031 1989 24 48 -112 C ATOM 1076 CG GLU A 133 4.561 -0.475 -12.877 1.00 16.94 C ANISOU 1076 CG GLU A 133 2117 2128 2190 62 -59 22 C ATOM 1077 CD GLU A 133 3.279 -0.847 -12.142 1.00 16.00 C ANISOU 1077 CD GLU A 133 2018 2068 1990 65 -114 -21 C ATOM 1078 OE1 GLU A 133 2.499 -1.580 -12.698 1.00 15.68 O ANISOU 1078 OE1 GLU A 133 1986 1971 2001 15 81 -25 O ATOM 1079 OE2 GLU A 133 3.084 -0.394 -11.022 1.00 16.63 O ANISOU 1079 OE2 GLU A 133 2152 2111 2054 66 135 -52 O ATOM 1080 N ALA A 134 6.502 -4.684 -11.504 1.00 15.05 N ANISOU 1080 N ALA A 134 2032 1775 1910 176 179 -70 N ATOM 1081 CA ALA A 134 6.885 -6.078 -11.531 1.00 14.82 C ANISOU 1081 CA ALA A 134 1937 1786 1905 46 102 -84 C ATOM 1082 C ALA A 134 5.999 -7.002 -10.751 1.00 16.04 C ANISOU 1082 C ALA A 134 2143 1851 2100 -28 197 88 C ATOM 1083 O ALA A 134 5.196 -6.572 -10.020 1.00 18.12 O ANISOU 1083 O ALA A 134 2392 2175 2318 163 41 36 O ATOM 1084 CB ALA A 134 8.277 -6.149 -10.944 1.00 16.89 C ANISOU 1084 CB ALA A 134 2278 2062 2076 156 -35 -156 C ATOM 1085 N ILE A 135 6.189 -8.295 -10.986 1.00 15.59 N ANISOU 1085 N ILE A 135 2207 1817 1899 20 145 -96 N ATOM 1086 CA ILE A 135 5.552 -9.343 -10.207 1.00 17.14 C ANISOU 1086 CA ILE A 135 2235 2174 2103 -77 166 -58 C ATOM 1087 C ILE A 135 6.460 -9.692 -9.131 1.00 17.30 C ANISOU 1087 C ILE A 135 2138 2224 2212 -108 98 10 C ATOM 1088 O ILE A 135 7.492 -10.280 -9.285 1.00 18.45 O ANISOU 1088 O ILE A 135 2432 2294 2284 97 -15 104 O ATOM 1089 CB ILE A 135 5.247 -10.561 -11.132 1.00 17.01 C ANISOU 1089 CB ILE A 135 2206 2026 2229 -56 -12 58 C ATOM 1090 CG1 ILE A 135 4.307 -10.120 -12.202 1.00 19.92 C ANISOU 1090 CG1 ILE A 135 2681 2454 2432 -233 -143 -157 C ATOM 1091 CG2 ILE A 135 4.593 -11.725 -10.238 1.00 19.30 C ANISOU 1091 CG2 ILE A 135 2471 2305 2557 -27 217 160 C ATOM 1092 CD1 ILE A 135 4.093 -11.244 -13.287 1.00 24.43 C ANISOU 1092 CD1 ILE A 135 3329 2895 3058 353 -190 -269 C ATOM 1093 N VAL A 136 6.117 -9.208 -7.918 1.00 17.93 N ANISOU 1093 N VAL A 136 2408 2215 2187 230 85 7 N ATOM 1094 CA VAL A 136 6.987 -9.272 -6.739 1.00 16.84 C ANISOU 1094 CA VAL A 136 2072 2089 2236 -66 39 -25 C ATOM 1095 C VAL A 136 6.557 -10.334 -5.679 1.00 19.49 C ANISOU 1095 C VAL A 136 2427 2456 2520 -54 -185 14 C ATOM 1096 O VAL A 136 7.387 -10.617 -4.856 1.00 22.64 O ANISOU 1096 O VAL A 136 3097 2728 2775 -174 -6 252 O ATOM 1097 CB VAL A 136 7.134 -7.917 -6.042 1.00 18.64 C ANISOU 1097 CB VAL A 136 2383 2341 2356 -8 103 -107 C ATOM 1098 CG1 VAL A 136 7.815 -6.885 -7.014 1.00 20.44 C ANISOU 1098 CG1 VAL A 136 2757 2572 2435 -67 58 -32 C ATOM 1099 CG2 VAL A 136 5.852 -7.352 -5.472 1.00 18.88 C ANISOU 1099 CG2 VAL A 136 2526 2414 2233 -2 93 45 C ATOM 1100 N THR A 137 5.381 -10.790 -5.818 1.00 17.91 N ANISOU 1100 N THR A 137 2384 2231 2189 -60 190 192 N ATOM 1101 CA THR A 137 4.778 -11.807 -4.815 1.00 19.81 C ANISOU 1101 CA THR A 137 2702 2417 2408 -108 236 323 C ATOM 1102 C THR A 137 3.486 -12.226 -5.410 1.00 22.84 C ANISOU 1102 C THR A 137 3038 2866 2771 -124 61 -117 C ATOM 1103 O THR A 137 2.860 -11.562 -6.243 1.00 20.92 O ANISOU 1103 O THR A 137 2742 2661 2544 81 39 70 O ATOM 1104 CB THR A 137 4.525 -11.016 -3.524 1.00 23.19 C ANISOU 1104 CB THR A 137 3009 2840 2959 -455 -21 123 C ATOM 1105 OG1 THR A 137 4.349 -11.945 -2.478 1.00 27.60 O ANISOU 1105 OG1 THR A 137 3734 3626 3127 -198 166 252 O ATOM 1106 CG2 THR A 137 3.385 -10.113 -3.586 1.00 27.09 C ANISOU 1106 CG2 THR A 137 3671 3531 3090 -106 340 -218 C ATOM 1107 N PRO A 138 2.942 -13.414 -5.045 1.00 19.97 N ANISOU 1107 N PRO A 138 2702 2501 2384 -87 9 202 N ATOM 1108 CA PRO A 138 1.696 -13.839 -5.588 1.00 19.73 C ANISOU 1108 CA PRO A 138 2628 2493 2376 0 92 185 C ATOM 1109 C PRO A 138 0.532 -12.935 -5.280 1.00 21.89 C ANISOU 1109 C PRO A 138 2781 2657 2877 -318 125 32 C ATOM 1110 O PRO A 138 0.542 -12.258 -4.197 1.00 24.95 O ANISOU 1110 O PRO A 138 3250 3315 2915 -225 250 -199 O ATOM 1111 CB PRO A 138 1.519 -15.305 -4.968 1.00 23.31 C ANISOU 1111 CB PRO A 138 3118 2823 2914 -236 79 219 C ATOM 1112 CG PRO A 138 2.945 -15.681 -4.819 1.00 24.70 C ANISOU 1112 CG PRO A 138 3421 2866 3095 2 -123 335 C ATOM 1113 CD PRO A 138 3.675 -14.480 -4.226 1.00 23.20 C ANISOU 1113 CD PRO A 138 3077 2929 2807 144 86 253 C ATOM 1114 N LEU A 139 -0.418 -12.792 -6.173 1.00 22.46 N ANISOU 1114 N LEU A 139 2915 2839 2780 48 152 74 N ATOM 1115 CA LEU A 139 -1.455 -11.843 -6.110 1.00 24.49 C ANISOU 1115 CA LEU A 139 3012 3208 3085 12 -52 -207 C ATOM 1116 C LEU A 139 -2.784 -12.428 -5.684 1.00 22.34 C ANISOU 1116 C LEU A 139 3041 2718 2726 -210 269 -131 C ATOM 1117 O LEU A 139 -3.029 -13.662 -5.798 1.00 23.09 O ANISOU 1117 O LEU A 139 2995 2910 2866 -82 398 71 O ATOM 1118 CB LEU A 139 -1.626 -11.101 -7.433 1.00 23.41 C ANISOU 1118 CB LEU A 139 2986 2870 3038 -20 -83 87 C ATOM 1119 CG LEU A 139 -0.438 -10.290 -7.891 1.00 26.33 C ANISOU 1119 CG LEU A 139 3333 3211 3460 -58 185 -95 C ATOM 1120 CD1 LEU A 139 -0.568 -9.903 -9.320 1.00 46.61 C ANISOU 1120 CD1 LEU A 139 6464 6105 5140 -879 -341 708 C ATOM 1121 CD2 LEU A 139 -0.198 -9.080 -7.070 1.00 39.30 C ANISOU 1121 CD2 LEU A 139 4892 4822 5216 -339 259 -852 C ATOM 1122 N GLU A 140 -3.697 -11.506 -5.309 1.00 26.87 N ANISOU 1122 N GLU A 140 3274 3475 3460 -61 278 119 N ATOM 1123 CA GLU A 140 -5.147 -11.838 -5.294 1.00 27.77 C ANISOU 1123 CA GLU A 140 3551 3733 3265 99 212 -339 C ATOM 1124 C GLU A 140 -5.792 -10.814 -6.075 1.00 28.00 C ANISOU 1124 C GLU A 140 3741 3853 3042 13 612 -233 C ATOM 1125 O GLU A 140 -5.265 -9.744 -6.335 1.00 29.08 O ANISOU 1125 O GLU A 140 3685 3768 3593 -248 153 -450 O ATOM 1126 CB GLU A 140 -5.671 -11.688 -3.795 1.00 31.87 C ANISOU 1126 CB GLU A 140 4008 4397 3703 -196 834 23 C ATOM 1127 CG GLU A 140 -4.885 -12.580 -2.788 1.00 36.26 C ANISOU 1127 CG GLU A 140 4347 5103 4326 -34 782 62 C ATOM 1128 CD GLU A 140 -5.291 -13.983 -2.627 1.00 55.70 C ANISOU 1128 CD GLU A 140 7064 6424 7674 -175 1008 372 C ATOM 1129 OE1 GLU A 140 -6.251 -14.433 -3.276 1.00 68.58 O ANISOU 1129 OE1 GLU A 140 8056 9814 8187 -271 230 -1469 O ATOM 1130 OE2 GLU A 140 -4.667 -14.649 -1.789 1.00 63.94 O ANISOU 1130 OE2 GLU A 140 7192 9381 7720 779 -803 1279 O ATOM 1131 N TRP A 141 -7.075 -11.063 -6.438 1.00 27.61 N ANISOU 1131 N TRP A 141 3443 3954 3091 -59 8 -98 N ATOM 1132 CA TRP A 141 -7.829 -10.106 -7.264 1.00 28.04 C ANISOU 1132 CA TRP A 141 3580 3449 3624 -69 255 -359 C ATOM 1133 C TRP A 141 -7.975 -8.696 -6.701 1.00 28.32 C ANISOU 1133 C TRP A 141 3476 3438 3845 260 -10 17 C ATOM 1134 O TRP A 141 -7.935 -7.737 -7.427 1.00 32.19 O ANISOU 1134 O TRP A 141 4032 4339 3859 55 118 -129 O ATOM 1135 CB TRP A 141 -9.174 -10.747 -7.668 1.00 32.67 C ANISOU 1135 CB TRP A 141 3818 4431 4161 -8 379 -313 C ATOM 1136 CG TRP A 141 -9.073 -11.750 -8.750 1.00 32.97 C ANISOU 1136 CG TRP A 141 4146 4262 4119 -407 442 -103 C ATOM 1137 CD1 TRP A 141 -9.336 -13.090 -8.699 1.00 30.31 C ANISOU 1137 CD1 TRP A 141 3863 3860 3792 -66 732 -132 C ATOM 1138 CD2 TRP A 141 -8.642 -11.466 -10.080 1.00 30.81 C ANISOU 1138 CD2 TRP A 141 3975 3819 3910 268 654 -88 C ATOM 1139 NE1 TRP A 141 -9.131 -13.655 -9.929 1.00 33.16 N ANISOU 1139 NE1 TRP A 141 4233 4260 4106 -191 213 -96 N ATOM 1140 CE2 TRP A 141 -8.709 -12.661 -10.777 1.00 28.73 C ANISOU 1140 CE2 TRP A 141 3696 3714 3506 -135 182 -131 C ATOM 1141 CE3 TRP A 141 -8.290 -10.299 -10.735 1.00 30.23 C ANISOU 1141 CE3 TRP A 141 3695 4045 3744 237 83 -51 C ATOM 1142 CZ2 TRP A 141 -8.368 -12.745 -12.172 1.00 28.23 C ANISOU 1142 CZ2 TRP A 141 3841 3613 3271 -102 320 20 C ATOM 1143 CZ3 TRP A 141 -7.915 -10.381 -12.086 1.00 30.85 C ANISOU 1143 CZ3 TRP A 141 3624 3963 4132 313 112 187 C ATOM 1144 CH2 TRP A 141 -7.937 -11.579 -12.768 1.00 27.66 C ANISOU 1144 CH2 TRP A 141 3583 3468 3460 -142 -100 -34 C ATOM 1145 N ALA A 142 -7.983 -8.592 -5.385 1.00 35.03 N ANISOU 1145 N ALA A 142 4597 4660 4050 263 350 -191 N ATOM 1146 CA ALA A 142 -7.956 -7.261 -4.704 1.00 40.34 C ANISOU 1146 CA ALA A 142 5169 5094 5062 -77 -507 439 C ATOM 1147 C ALA A 142 -6.712 -6.421 -5.033 1.00 40.36 C ANISOU 1147 C ALA A 142 5215 5130 4988 130 -780 582 C ATOM 1148 O ALA A 142 -6.727 -5.202 -5.109 1.00 37.39 O ANISOU 1148 O ALA A 142 5057 4574 4575 798 -274 -829 O ATOM 1149 CB ALA A 142 -8.085 -7.519 -3.201 1.00 44.78 C ANISOU 1149 CB ALA A 142 6082 5835 5098 513 1254 -1349 C ATOM 1150 N ASP A 143 -5.571 -7.064 -5.322 1.00 34.05 N ANISOU 1150 N ASP A 143 4345 4111 4481 107 401 -208 N ATOM 1151 CA ASP A 143 -4.386 -6.348 -5.673 1.00 29.66 C ANISOU 1151 CA ASP A 143 3928 3604 3735 272 -386 -423 C ATOM 1152 C ASP A 143 -4.429 -5.770 -7.095 1.00 32.88 C ANISOU 1152 C ASP A 143 4231 4193 4066 -213 -326 112 C ATOM 1153 O ASP A 143 -3.625 -4.893 -7.489 1.00 36.49 O ANISOU 1153 O ASP A 143 4677 4736 4448 -295 -494 53 O ATOM 1154 CB ASP A 143 -3.255 -7.326 -5.574 1.00 28.25 C ANISOU 1154 CB ASP A 143 3637 3592 3502 45 102 -593 C ATOM 1155 CG ASP A 143 -3.089 -7.889 -4.190 1.00 31.39 C ANISOU 1155 CG ASP A 143 4014 3831 4080 196 -307 360 C ATOM 1156 OD1 ASP A 143 -3.026 -7.037 -3.225 1.00 32.59 O ANISOU 1156 OD1 ASP A 143 4575 4070 3737 350 -167 -422 O ATOM 1157 OD2 ASP A 143 -2.902 -9.087 -3.978 1.00 30.33 O ANISOU 1157 OD2 ASP A 143 3697 3869 3956 -273 148 -483 O ATOM 1158 N TRP A 144 -5.290 -6.320 -7.937 1.00 32.47 N ANISOU 1158 N TRP A 144 4174 4059 4104 53 -231 -187 N ATOM 1159 CA TRP A 144 -5.357 -5.894 -9.323 1.00 32.66 C ANISOU 1159 CA TRP A 144 4057 4033 4317 -145 59 48 C ATOM 1160 C TRP A 144 -6.155 -4.582 -9.470 1.00 33.20 C ANISOU 1160 C TRP A 144 4313 4206 4096 -186 -104 164 C ATOM 1161 O TRP A 144 -7.172 -4.433 -8.850 1.00 33.34 O ANISOU 1161 O TRP A 144 4054 4623 3990 99 10 -13 O ATOM 1162 CB TRP A 144 -5.928 -7.056 -10.185 1.00 31.52 C ANISOU 1162 CB TRP A 144 4206 4111 3656 -280 -68 -335 C ATOM 1163 CG TRP A 144 -5.415 -7.092 -11.556 1.00 29.23 C ANISOU 1163 CG TRP A 144 3859 3165 4080 9 -245 -98 C ATOM 1164 CD1 TRP A 144 -6.055 -6.682 -12.661 1.00 38.26 C ANISOU 1164 CD1 TRP A 144 5160 4620 4755 -663 148 -234 C ATOM 1165 CD2 TRP A 144 -4.131 -7.505 -11.974 1.00 31.67 C ANISOU 1165 CD2 TRP A 144 4327 4224 3479 -535 274 24 C ATOM 1166 NE1 TRP A 144 -5.264 -6.819 -13.747 1.00 35.88 N ANISOU 1166 NE1 TRP A 144 5084 4235 4314 -312 -206 -152 N ATOM 1167 CE2 TRP A 144 -4.060 -7.306 -13.354 1.00 31.86 C ANISOU 1167 CE2 TRP A 144 4370 3413 4319 220 -94 -165 C ATOM 1168 CE3 TRP A 144 -3.031 -8.041 -11.321 1.00 31.21 C ANISOU 1168 CE3 TRP A 144 3784 3819 4255 90 414 404 C ATOM 1169 CZ2 TRP A 144 -2.950 -7.632 -14.079 1.00 26.98 C ANISOU 1169 CZ2 TRP A 144 3657 3189 3402 -636 164 244 C ATOM 1170 CZ3 TRP A 144 -1.932 -8.324 -12.028 1.00 34.28 C ANISOU 1170 CZ3 TRP A 144 5349 3415 4258 100 505 166 C ATOM 1171 CH2 TRP A 144 -1.895 -8.133 -13.405 1.00 32.56 C ANISOU 1171 CH2 TRP A 144 4650 3698 4023 -155 -24 -53 C ATOM 1172 N PRO A 145 -5.676 -3.634 -10.296 1.00 32.84 N ANISOU 1172 N PRO A 145 3868 4443 4165 -124 -42 -301 N ATOM 1173 CA PRO A 145 -6.425 -2.373 -10.463 1.00 31.32 C ANISOU 1173 CA PRO A 145 4053 3970 3877 -292 -34 -180 C ATOM 1174 C PRO A 145 -7.887 -2.633 -10.862 1.00 31.78 C ANISOU 1174 C PRO A 145 3747 4309 4018 51 -173 -174 C ATOM 1175 O PRO A 145 -8.188 -3.376 -11.827 1.00 29.72 O ANISOU 1175 O PRO A 145 3685 3835 3771 95 168 -239 O ATOM 1176 CB PRO A 145 -5.648 -1.583 -11.503 1.00 36.17 C ANISOU 1176 CB PRO A 145 4485 4647 4609 -258 391 -699 C ATOM 1177 CG PRO A 145 -4.358 -2.260 -11.555 1.00 31.53 C ANISOU 1177 CG PRO A 145 3878 4208 3893 -309 -618 165 C ATOM 1178 CD PRO A 145 -4.382 -3.644 -11.078 1.00 31.57 C ANISOU 1178 CD PRO A 145 3950 4259 3786 -290 27 -327 C ATOM 1179 N GLU A 146 -8.826 -2.099 -10.087 1.00 31.74 N ANISOU 1179 N GLU A 146 4078 3915 4067 -7 136 -628 N ATOM 1180 CA GLU A 146 -10.250 -2.385 -10.318 1.00 35.23 C ANISOU 1180 CA GLU A 146 4193 4647 4544 298 62 -110 C ATOM 1181 C GLU A 146 -10.767 -2.214 -11.814 1.00 32.63 C ANISOU 1181 C GLU A 146 4021 4027 4349 218 393 -483 C ATOM 1182 O GLU A 146 -11.610 -2.968 -12.354 1.00 35.17 O ANISOU 1182 O GLU A 146 4079 4453 4830 228 394 -245 O ATOM 1183 CB GLU A 146 -11.003 -1.497 -9.271 1.00 47.54 C ANISOU 1183 CB GLU A 146 6162 6262 5638 1204 533 -745 C ATOM 1184 CG GLU A 146 -12.424 -1.923 -9.043 1.00 60.43 C ANISOU 1184 CG GLU A 146 6906 8037 8016 -891 532 147 C ATOM 1185 CD GLU A 146 -13.371 -1.419 -10.128 1.00 73.04 C ANISOU 1185 CD GLU A 146 9546 9052 9153 1194 347 225 C ATOM 1186 OE1 GLU A 146 -12.986 -0.460 -10.912 1.00 60.71 O ANISOU 1186 OE1 GLU A 146 7452 7174 8439 981 1750 -768 O ATOM 1187 OE2 GLU A 146 -14.486 -2.036 -10.228 1.00 78.36 O ANISOU 1187 OE2 GLU A 146 8138 10693 10940 -670 1490 -1702 O ATOM 1188 N GLU A 147 -10.246 -1.176 -12.436 1.00 31.79 N ANISOU 1188 N GLU A 147 4048 3843 4187 530 292 -235 N ATOM 1189 CA GLU A 147 -10.651 -0.784 -13.755 1.00 36.13 C ANISOU 1189 CA GLU A 147 4521 4609 4597 616 95 -903 C ATOM 1190 C GLU A 147 -10.282 -1.762 -14.828 1.00 30.51 C ANISOU 1190 C GLU A 147 3910 3956 3726 164 58 -245 C ATOM 1191 O GLU A 147 -10.792 -1.667 -15.907 1.00 34.52 O ANISOU 1191 O GLU A 147 3978 4412 4724 707 47 75 O ATOM 1192 CB GLU A 147 -10.154 0.599 -14.103 1.00 45.44 C ANISOU 1192 CB GLU A 147 6136 5207 5923 -206 -77 650 C ATOM 1193 CG GLU A 147 -8.653 0.702 -14.183 1.00 53.54 C ANISOU 1193 CG GLU A 147 6694 6472 7177 276 215 66 C ATOM 1194 CD GLU A 147 -7.995 1.262 -12.925 1.00 62.51 C ANISOU 1194 CD GLU A 147 8659 7711 7380 -994 -632 301 C ATOM 1195 OE1 GLU A 147 -8.438 1.011 -11.782 1.00 48.28 O ANISOU 1195 OE1 GLU A 147 6174 5464 6705 -545 -436 -846 O ATOM 1196 OE2 GLU A 147 -6.999 1.966 -13.104 1.00 60.00 O ANISOU 1196 OE2 GLU A 147 6052 8472 8272 -1283 1093 -31 O ATOM 1197 N VAL A 148 -9.351 -2.657 -14.548 1.00 30.77 N ANISOU 1197 N VAL A 148 3888 3989 3813 144 -3 -384 N ATOM 1198 CA VAL A 148 -9.084 -3.708 -15.553 1.00 26.25 C ANISOU 1198 CA VAL A 148 3053 3261 3658 275 -43 -162 C ATOM 1199 C VAL A 148 -9.316 -5.059 -15.012 1.00 27.99 C ANISOU 1199 C VAL A 148 3281 3722 3630 -218 40 375 C ATOM 1200 O VAL A 148 -8.944 -6.058 -15.651 1.00 27.05 O ANISOU 1200 O VAL A 148 3289 3490 3496 43 248 -303 O ATOM 1201 CB VAL A 148 -7.601 -3.649 -16.128 1.00 25.28 C ANISOU 1201 CB VAL A 148 3196 3091 3315 -13 289 -41 C ATOM 1202 CG1 VAL A 148 -7.469 -2.376 -16.960 1.00 31.65 C ANISOU 1202 CG1 VAL A 148 3919 4007 4096 -67 148 234 C ATOM 1203 CG2 VAL A 148 -6.604 -3.731 -14.970 1.00 28.51 C ANISOU 1203 CG2 VAL A 148 3485 3597 3751 51 67 -28 C ATOM 1204 N ARG A 149 -9.997 -5.214 -13.858 1.00 26.05 N ANISOU 1204 N ARG A 149 3210 3464 3222 170 232 -209 N ATOM 1205 CA ARG A 149 -10.189 -6.509 -13.374 1.00 24.76 C ANISOU 1205 CA ARG A 149 3006 3275 3127 109 190 -195 C ATOM 1206 C ARG A 149 -11.094 -7.382 -14.268 1.00 25.81 C ANISOU 1206 C ARG A 149 3205 3387 3213 16 272 23 C ATOM 1207 O ARG A 149 -10.880 -8.617 -14.427 1.00 25.11 O ANISOU 1207 O ARG A 149 2959 3267 3313 101 457 -81 O ATOM 1208 CB ARG A 149 -10.776 -6.352 -11.945 1.00 31.55 C ANISOU 1208 CB ARG A 149 4265 4113 3607 699 537 -258 C ATOM 1209 CG ARG A 149 -10.863 -7.502 -11.080 1.00 38.64 C ANISOU 1209 CG ARG A 149 5381 4268 5029 133 642 -238 C ATOM 1210 CD ARG A 149 -11.280 -6.986 -9.654 1.00 49.26 C ANISOU 1210 CD ARG A 149 6876 6740 5097 97 193 -180 C ATOM 1211 NE ARG A 149 -10.184 -6.205 -8.929 1.00 47.05 N ANISOU 1211 NE ARG A 149 5912 6155 5807 -326 1325 -380 N ATOM 1212 CZ ARG A 149 -10.375 -5.328 -7.933 1.00 50.23 C ANISOU 1212 CZ ARG A 149 6430 6130 6523 -834 -290 220 C ATOM 1213 NH1 ARG A 149 -11.605 -5.029 -7.540 1.00 49.35 N ANISOU 1213 NH1 ARG A 149 6289 6150 6312 764 1270 -256 N ATOM 1214 NH2 ARG A 149 -9.354 -4.732 -7.329 1.00 47.85 N ANISOU 1214 NH2 ARG A 149 6118 6486 5576 -419 665 301 N ATOM 1215 N ASP A 150 -12.155 -6.769 -14.784 1.00 28.06 N ANISOU 1215 N ASP A 150 3404 3627 3630 140 175 -193 N ATOM 1216 CA ASP A 150 -13.124 -7.473 -15.619 1.00 27.25 C ANISOU 1216 CA ASP A 150 3358 3542 3452 79 113 -45 C ATOM 1217 C ASP A 150 -12.494 -8.008 -16.895 1.00 26.35 C ANISOU 1217 C ASP A 150 3276 3231 3501 -33 142 -115 C ATOM 1218 O ASP A 150 -12.864 -9.074 -17.389 1.00 26.94 O ANISOU 1218 O ASP A 150 3050 3608 3578 104 322 -308 O ATOM 1219 CB ASP A 150 -14.301 -6.557 -15.961 1.00 31.53 C ANISOU 1219 CB ASP A 150 3549 4073 4357 381 35 50 C ATOM 1220 CG ASP A 150 -15.293 -6.433 -14.821 1.00 41.06 C ANISOU 1220 CG ASP A 150 5225 5682 4690 356 72 485 C ATOM 1221 OD1 ASP A 150 -15.076 -7.073 -13.771 1.00 37.87 O ANISOU 1221 OD1 ASP A 150 4551 5062 4773 326 580 -428 O ATOM 1222 OD2 ASP A 150 -16.289 -5.695 -14.975 1.00 57.45 O ANISOU 1222 OD2 ASP A 150 7158 7219 7448 1592 1477 13 O ATOM 1223 N ILE A 151 -11.538 -7.256 -17.422 1.00 26.28 N ANISOU 1223 N ILE A 151 3052 3527 3406 162 149 -77 N ATOM 1224 CA ILE A 151 -10.852 -7.625 -18.631 1.00 23.59 C ANISOU 1224 CA ILE A 151 2809 3110 3043 43 -204 -386 C ATOM 1225 C ILE A 151 -9.914 -8.777 -18.337 1.00 22.39 C ANISOU 1225 C ILE A 151 2843 2811 2851 138 -34 -36 C ATOM 1226 O ILE A 151 -9.859 -9.712 -19.075 1.00 22.71 O ANISOU 1226 O ILE A 151 2474 3022 3132 -66 87 -200 O ATOM 1227 CB ILE A 151 -10.093 -6.431 -19.197 1.00 27.72 C ANISOU 1227 CB ILE A 151 3841 3181 3507 340 526 588 C ATOM 1228 CG1 ILE A 151 -11.067 -5.485 -19.861 1.00 33.86 C ANISOU 1228 CG1 ILE A 151 3741 4675 4449 251 130 440 C ATOM 1229 CG2 ILE A 151 -9.080 -6.865 -20.214 1.00 30.68 C ANISOU 1229 CG2 ILE A 151 3903 3720 4031 56 15 35 C ATOM 1230 CD1 ILE A 151 -10.515 -4.102 -20.068 1.00 45.22 C ANISOU 1230 CD1 ILE A 151 5710 5366 6105 -225 -396 212 C ATOM 1231 N PHE A 152 -9.173 -8.667 -17.251 1.00 21.71 N ANISOU 1231 N PHE A 152 2577 2762 2907 6 107 -163 N ATOM 1232 CA PHE A 152 -8.317 -9.777 -16.901 1.00 23.53 C ANISOU 1232 CA PHE A 152 2884 3028 3026 -43 38 68 C ATOM 1233 C PHE A 152 -8.921 -11.059 -16.504 1.00 25.16 C ANISOU 1233 C PHE A 152 3106 3016 3434 28 182 83 C ATOM 1234 O PHE A 152 -8.500 -12.196 -16.827 1.00 22.69 O ANISOU 1234 O PHE A 152 2731 3019 2869 -76 277 -152 O ATOM 1235 CB PHE A 152 -7.183 -9.396 -15.919 1.00 23.98 C ANISOU 1235 CB PHE A 152 2936 3132 3041 -156 -130 -5 C ATOM 1236 CG PHE A 152 -6.065 -8.601 -16.584 1.00 19.72 C ANISOU 1236 CG PHE A 152 2427 2456 2608 13 -13 -85 C ATOM 1237 CD1 PHE A 152 -6.186 -7.282 -16.939 1.00 21.35 C ANISOU 1237 CD1 PHE A 152 2519 2638 2954 -58 56 99 C ATOM 1238 CD2 PHE A 152 -4.876 -9.234 -16.890 1.00 19.35 C ANISOU 1238 CD2 PHE A 152 2341 2267 2741 -141 114 -138 C ATOM 1239 CE1 PHE A 152 -5.184 -6.545 -17.562 1.00 20.98 C ANISOU 1239 CE1 PHE A 152 2653 2591 2725 191 164 -75 C ATOM 1240 CE2 PHE A 152 -3.869 -8.491 -17.520 1.00 20.10 C ANISOU 1240 CE2 PHE A 152 2487 2538 2611 -65 107 -60 C ATOM 1241 CZ PHE A 152 -3.996 -7.162 -17.756 1.00 18.68 C ANISOU 1241 CZ PHE A 152 2185 2438 2473 6 -52 155 C ATOM 1242 N GLN A 153 -10.107 -10.902 -15.819 1.00 23.89 N ANISOU 1242 N GLN A 153 2835 3038 3203 -100 493 71 N ATOM 1243 CA GLN A 153 -10.839 -12.193 -15.537 1.00 25.38 C ANISOU 1243 CA GLN A 153 3051 3153 3438 38 346 -184 C ATOM 1244 C GLN A 153 -11.407 -12.724 -16.842 1.00 22.56 C ANISOU 1244 C GLN A 153 2336 3061 3175 -41 492 127 C ATOM 1245 O GLN A 153 -11.460 -13.943 -16.995 1.00 25.41 O ANISOU 1245 O GLN A 153 2824 3266 3563 13 379 -197 O ATOM 1246 CB GLN A 153 -12.004 -11.774 -14.534 1.00 26.97 C ANISOU 1246 CB GLN A 153 3249 3652 3346 -102 457 100 C ATOM 1247 CG GLN A 153 -11.413 -11.603 -13.183 1.00 29.74 C ANISOU 1247 CG GLN A 153 3543 3841 3913 -158 73 -117 C ATOM 1248 CD GLN A 153 -12.384 -11.176 -12.124 1.00 47.86 C ANISOU 1248 CD GLN A 153 5698 6904 5580 1347 857 267 C ATOM 1249 OE1 GLN A 153 -13.398 -10.525 -12.429 1.00 38.86 O ANISOU 1249 OE1 GLN A 153 4581 5328 4853 247 56 -204 O ATOM 1250 NE2 GLN A 153 -12.063 -11.523 -10.872 1.00 47.72 N ANISOU 1250 NE2 GLN A 153 5775 7452 4905 961 491 64 N ATOM 1251 N GLY A 154 -11.739 -11.889 -17.823 1.00 21.73 N ANISOU 1251 N GLY A 154 2377 3027 2852 -2 178 -47 N ATOM 1252 CA GLY A 154 -12.135 -12.296 -19.153 1.00 23.23 C ANISOU 1252 CA GLY A 154 2700 2966 3158 83 345 -84 C ATOM 1253 C GLY A 154 -11.036 -13.136 -19.905 1.00 22.60 C ANISOU 1253 C GLY A 154 2668 3039 2880 73 217 -353 C ATOM 1254 O GLY A 154 -11.278 -14.148 -20.530 1.00 22.26 O ANISOU 1254 O GLY A 154 2571 2844 3039 -57 319 -54 O ATOM 1255 N PHE A 155 -9.827 -12.612 -19.828 1.00 24.40 N ANISOU 1255 N PHE A 155 2939 3126 3203 -91 169 -179 N ATOM 1256 CA PHE A 155 -8.706 -13.275 -20.426 1.00 21.54 C ANISOU 1256 CA PHE A 155 2638 2688 2856 -6 25 -242 C ATOM 1257 C PHE A 155 -8.578 -14.669 -19.827 1.00 21.40 C ANISOU 1257 C PHE A 155 2360 3023 2748 -155 -45 -174 C ATOM 1258 O PHE A 155 -8.312 -15.581 -20.520 1.00 20.99 O ANISOU 1258 O PHE A 155 2548 2545 2883 -133 89 -165 O ATOM 1259 CB PHE A 155 -7.381 -12.544 -20.176 1.00 19.83 C ANISOU 1259 CB PHE A 155 2238 2752 2543 -64 149 -191 C ATOM 1260 CG PHE A 155 -7.236 -11.209 -20.852 1.00 20.76 C ANISOU 1260 CG PHE A 155 2389 2762 2735 89 110 -196 C ATOM 1261 CD1 PHE A 155 -7.748 -10.954 -22.071 1.00 20.24 C ANISOU 1261 CD1 PHE A 155 2459 2619 2611 -165 -84 178 C ATOM 1262 CD2 PHE A 155 -6.527 -10.222 -20.247 1.00 20.90 C ANISOU 1262 CD2 PHE A 155 2372 2731 2835 101 144 -166 C ATOM 1263 CE1 PHE A 155 -7.580 -9.736 -22.667 1.00 21.87 C ANISOU 1263 CE1 PHE A 155 2674 2709 2925 36 -219 -88 C ATOM 1264 CE2 PHE A 155 -6.342 -9.007 -20.832 1.00 21.32 C ANISOU 1264 CE2 PHE A 155 2561 2797 2740 -17 -22 85 C ATOM 1265 CZ PHE A 155 -6.870 -8.756 -22.042 1.00 21.63 C ANISOU 1265 CZ PHE A 155 2691 2777 2750 -85 131 -47 C ATOM 1266 N ARG A 156 -8.758 -14.771 -18.523 1.00 21.27 N ANISOU 1266 N ARG A 156 2475 2832 2772 -158 10 146 N ATOM 1267 CA ARG A 156 -8.641 -16.004 -17.814 1.00 21.13 C ANISOU 1267 CA ARG A 156 2423 2738 2865 -171 -130 122 C ATOM 1268 C ARG A 156 -9.973 -16.755 -17.775 1.00 26.80 C ANISOU 1268 C ARG A 156 3187 3729 3267 -531 134 -57 C ATOM 1269 O ARG A 156 -10.370 -17.222 -16.764 1.00 29.41 O ANISOU 1269 O ARG A 156 3716 3631 3825 -194 79 263 O ATOM 1270 CB ARG A 156 -8.174 -15.712 -16.397 1.00 21.53 C ANISOU 1270 CB ARG A 156 2650 2797 2732 -162 311 7 C ATOM 1271 CG ARG A 156 -6.760 -15.175 -16.346 1.00 21.04 C ANISOU 1271 CG ARG A 156 2547 2772 2673 -290 76 -68 C ATOM 1272 CD ARG A 156 -6.393 -14.586 -15.015 1.00 22.02 C ANISOU 1272 CD ARG A 156 2610 2905 2849 -62 178 95 C ATOM 1273 NE ARG A 156 -6.201 -15.553 -13.954 1.00 20.42 N ANISOU 1273 NE ARG A 156 2503 2651 2604 -100 164 126 N ATOM 1274 CZ ARG A 156 -5.048 -16.036 -13.569 1.00 20.77 C ANISOU 1274 CZ ARG A 156 2591 2655 2645 -105 -9 105 C ATOM 1275 NH1 ARG A 156 -3.948 -15.688 -14.181 1.00 20.36 N ANISOU 1275 NH1 ARG A 156 2473 2605 2655 -184 341 36 N ATOM 1276 NH2 ARG A 156 -4.973 -16.854 -12.553 1.00 22.62 N ANISOU 1276 NH2 ARG A 156 2843 2786 2963 -163 88 301 N ATOM 1277 N SER A 157 -10.601 -16.859 -18.916 1.00 24.63 N ANISOU 1277 N SER A 157 2873 3290 3194 -285 145 160 N ATOM 1278 CA SER A 157 -11.938 -17.530 -19.108 1.00 25.52 C ANISOU 1278 CA SER A 157 3147 3090 3460 -324 -172 -12 C ATOM 1279 C SER A 157 -11.940 -17.958 -20.481 1.00 27.73 C ANISOU 1279 C SER A 157 3526 3774 3235 -374 -36 -25 C ATOM 1280 O SER A 157 -11.126 -17.516 -21.335 1.00 24.20 O ANISOU 1280 O SER A 157 2937 3039 3215 -337 271 -95 O ATOM 1281 CB SER A 157 -13.010 -16.549 -18.889 1.00 24.00 C ANISOU 1281 CB SER A 157 2706 3283 3127 -237 93 17 C ATOM 1282 OG SER A 157 -13.324 -15.684 -19.985 1.00 24.14 O ANISOU 1282 OG SER A 157 2865 3169 3137 -219 -1 -6 O ATOM 1283 N PRO A 158 -12.925 -18.786 -20.925 1.00 26.96 N ANISOU 1283 N PRO A 158 3331 3462 3450 -602 314 -89 N ATOM 1284 CA PRO A 158 -13.020 -19.109 -22.333 1.00 25.01 C ANISOU 1284 CA PRO A 158 2754 3361 3387 -506 130 -68 C ATOM 1285 C PRO A 158 -13.281 -18.043 -23.290 1.00 22.85 C ANISOU 1285 C PRO A 158 2448 3074 3158 -504 155 -222 C ATOM 1286 O PRO A 158 -13.044 -18.243 -24.509 1.00 26.50 O ANISOU 1286 O PRO A 158 3179 3536 3354 -341 -88 -145 O ATOM 1287 CB PRO A 158 -14.207 -20.204 -22.381 1.00 31.82 C ANISOU 1287 CB PRO A 158 3790 3910 4388 -598 209 38 C ATOM 1288 CG PRO A 158 -14.223 -20.706 -20.973 1.00 32.79 C ANISOU 1288 CG PRO A 158 4160 4208 4089 -742 -300 -72 C ATOM 1289 CD PRO A 158 -13.913 -19.503 -20.017 1.00 31.69 C ANISOU 1289 CD PRO A 158 4096 3812 4131 -625 381 117 C ATOM 1290 N ALA A 159 -13.678 -16.854 -22.831 1.00 23.83 N ANISOU 1290 N ALA A 159 2628 3174 3251 -143 39 50 N ATOM 1291 CA ALA A 159 -13.869 -15.728 -23.624 1.00 24.86 C ANISOU 1291 CA ALA A 159 2778 3242 3423 -382 50 -59 C ATOM 1292 C ALA A 159 -12.480 -15.102 -24.154 1.00 23.33 C ANISOU 1292 C ALA A 159 2778 2925 3161 -47 27 412 C ATOM 1293 O ALA A 159 -12.481 -14.316 -25.016 1.00 24.48 O ANISOU 1293 O ALA A 159 2770 3252 3279 -155 140 117 O ATOM 1294 CB ALA A 159 -14.560 -14.657 -22.807 1.00 27.96 C ANISOU 1294 CB ALA A 159 3199 3727 3697 205 229 38 C ATOM 1295 N GLY A 160 -11.398 -15.511 -23.542 1.00 22.76 N ANISOU 1295 N GLY A 160 2646 2882 3119 -271 24 63 N ATOM 1296 CA GLY A 160 -10.094 -14.971 -23.866 1.00 23.63 C ANISOU 1296 CA GLY A 160 2655 3155 3166 -202 217 -162 C ATOM 1297 C GLY A 160 -9.661 -15.063 -25.303 1.00 22.60 C ANISOU 1297 C GLY A 160 2916 2835 2835 7 -77 199 C ATOM 1298 O GLY A 160 -9.085 -14.141 -25.817 1.00 20.88 O ANISOU 1298 O GLY A 160 2379 2695 2858 -64 -152 12 O ATOM 1299 N GLU A 161 -9.921 -16.192 -25.940 1.00 18.98 N ANISOU 1299 N GLU A 161 2258 2463 2489 -108 24 -95 N ATOM 1300 CA GLU A 161 -9.551 -16.365 -27.320 1.00 20.09 C ANISOU 1300 CA GLU A 161 2464 2472 2697 -353 -31 -55 C ATOM 1301 C GLU A 161 -10.228 -15.314 -28.186 1.00 22.17 C ANISOU 1301 C GLU A 161 2709 2898 2815 54 -175 -13 C ATOM 1302 O GLU A 161 -9.595 -14.709 -28.987 1.00 22.91 O ANISOU 1302 O GLU A 161 2713 2961 3030 -114 -107 129 O ATOM 1303 CB GLU A 161 -9.820 -17.782 -27.809 1.00 20.81 C ANISOU 1303 CB GLU A 161 2636 2556 2713 -60 -84 -80 C ATOM 1304 CG GLU A 161 -8.718 -18.764 -27.491 1.00 21.63 C ANISOU 1304 CG GLU A 161 2661 2761 2796 -11 134 -91 C ATOM 1305 CD GLU A 161 -8.734 -19.263 -26.076 1.00 19.75 C ANISOU 1305 CD GLU A 161 2579 2314 2611 -191 -170 -282 C ATOM 1306 OE1 GLU A 161 -9.636 -18.904 -25.331 1.00 26.00 O ANISOU 1306 OE1 GLU A 161 3081 3506 3290 -179 10 -119 O ATOM 1307 OE2 GLU A 161 -7.851 -20.017 -25.735 1.00 22.36 O ANISOU 1307 OE2 GLU A 161 2681 2852 2961 -169 -42 -23 O ATOM 1308 N GLU A 162 -11.503 -15.083 -28.023 0.90 20.03 N ANISOU 1308 N GLU A 162 2273 2636 2701 -125 105 82 N ATOM 1309 CA GLU A 162 -12.127 -14.053 -28.817 0.90 20.74 C ANISOU 1309 CA GLU A 162 2419 2730 2731 0 125 167 C ATOM 1310 C GLU A 162 -11.577 -12.665 -28.517 0.90 21.12 C ANISOU 1310 C GLU A 162 2412 2912 2701 107 -318 51 C ATOM 1311 O GLU A 162 -11.365 -11.883 -29.394 0.90 23.51 O ANISOU 1311 O GLU A 162 2636 3162 3133 -253 -266 -46 O ATOM 1312 CB GLU A 162 -13.633 -14.081 -28.604 0.90 25.18 C ANISOU 1312 CB GLU A 162 2716 3248 3602 -201 166 59 C ATOM 1313 CG GLU A 162 -14.406 -13.108 -29.477 0.90 28.71 C ANISOU 1313 CG GLU A 162 2988 4004 3916 30 -32 599 C ATOM 1314 CD GLU A 162 -15.928 -13.200 -29.291 0.90 47.19 C ANISOU 1314 CD GLU A 162 5399 6383 6146 121 -128 -752 C ATOM 1315 OE1 GLU A 162 -16.645 -12.279 -29.704 0.90 43.66 O ANISOU 1315 OE1 GLU A 162 5757 5285 5547 -769 -1434 -361 O ATOM 1316 OE2 GLU A 162 -16.414 -14.200 -28.748 0.90 62.29 O ANISOU 1316 OE2 GLU A 162 7627 8000 8040 1237 -1327 1979 O ATOM 1317 N MET A 163 -11.372 -12.380 -27.252 1.00 22.37 N ANISOU 1317 N MET A 163 2645 2964 2888 115 188 23 N ATOM 1318 CA MET A 163 -10.867 -11.128 -26.814 1.00 20.05 C ANISOU 1318 CA MET A 163 2373 2609 2636 133 215 -90 C ATOM 1319 C MET A 163 -9.466 -10.785 -27.410 1.00 21.41 C ANISOU 1319 C MET A 163 2490 2727 2915 -27 -92 200 C ATOM 1320 O MET A 163 -9.210 -9.655 -27.854 1.00 21.05 O ANISOU 1320 O MET A 163 2405 2695 2898 -57 -128 112 O ATOM 1321 CB MET A 163 -10.751 -11.055 -25.365 1.00 22.03 C ANISOU 1321 CB MET A 163 2716 2809 2843 137 138 41 C ATOM 1322 CG MET A 163 -12.124 -11.037 -24.525 1.00 21.92 C ANISOU 1322 CG MET A 163 2518 2742 3066 -186 79 -11 C ATOM 1323 SD MET A 163 -11.854 -11.230 -22.796 1.00 26.31 S ANISOU 1323 SD MET A 163 3090 3432 3475 -114 121 -30 S ATOM 1324 CE MET A 163 -11.303 -9.673 -22.198 1.00 25.89 C ANISOU 1324 CE MET A 163 3186 3478 3174 112 187 -403 C ATOM 1325 N VAL A 164 -8.622 -11.791 -27.445 1.00 21.42 N ANISOU 1325 N VAL A 164 2648 2700 2787 -122 145 -182 N ATOM 1326 CA VAL A 164 -7.277 -11.583 -27.908 1.00 18.85 C ANISOU 1326 CA VAL A 164 2333 2284 2545 -127 -5 -18 C ATOM 1327 C VAL A 164 -6.977 -12.059 -29.299 1.00 20.10 C ANISOU 1327 C VAL A 164 2338 2584 2713 86 -152 164 C ATOM 1328 O VAL A 164 -6.527 -11.309 -30.105 1.00 21.42 O ANISOU 1328 O VAL A 164 2539 2836 2762 17 -179 63 O ATOM 1329 CB VAL A 164 -6.281 -12.195 -26.926 1.00 18.19 C ANISOU 1329 CB VAL A 164 2156 2399 2356 -21 62 27 C ATOM 1330 CG1 VAL A 164 -4.857 -12.112 -27.477 1.00 21.64 C ANISOU 1330 CG1 VAL A 164 2461 2790 2968 -123 5 170 C ATOM 1331 CG2 VAL A 164 -6.385 -11.462 -25.617 1.00 21.54 C ANISOU 1331 CG2 VAL A 164 2525 2825 2834 -249 -90 -180 C ATOM 1332 N LEU A 165 -7.258 -13.307 -29.580 1.00 19.13 N ANISOU 1332 N LEU A 165 2279 2442 2546 -24 -205 -36 N ATOM 1333 CA LEU A 165 -6.940 -13.782 -30.875 1.00 19.78 C ANISOU 1333 CA LEU A 165 2317 2646 2549 -39 -29 43 C ATOM 1334 C LEU A 165 -7.709 -13.063 -31.976 1.00 20.59 C ANISOU 1334 C LEU A 165 2539 2789 2494 80 -68 33 C ATOM 1335 O LEU A 165 -7.226 -12.743 -33.061 1.00 21.83 O ANISOU 1335 O LEU A 165 2557 2883 2851 -153 -269 44 O ATOM 1336 CB LEU A 165 -7.073 -15.295 -31.058 1.00 21.92 C ANISOU 1336 CB LEU A 165 2563 2811 2954 -75 216 25 C ATOM 1337 CG LEU A 165 -6.408 -16.105 -29.970 1.00 25.28 C ANISOU 1337 CG LEU A 165 3071 3027 3504 -334 7 165 C ATOM 1338 CD1 LEU A 165 -6.464 -17.620 -30.457 1.00 28.45 C ANISOU 1338 CD1 LEU A 165 3774 3350 3684 184 -260 -387 C ATOM 1339 CD2 LEU A 165 -4.964 -15.754 -29.749 1.00 24.07 C ANISOU 1339 CD2 LEU A 165 2974 2905 3264 220 -204 47 C ATOM 1340 N GLU A 166 -9.011 -12.824 -31.697 1.00 21.87 N ANISOU 1340 N GLU A 166 2635 2951 2722 -33 12 129 N ATOM 1341 CA AGLU A 166 -9.749 -12.094 -32.729 0.50 21.99 C ANISOU 1341 CA AGLU A 166 2457 3043 2854 -170 -155 276 C ATOM 1342 CA BGLU A 166 -9.809 -12.080 -32.673 0.50 22.16 C ANISOU 1342 CA BGLU A 166 2518 3020 2878 -158 -186 277 C ATOM 1343 C GLU A 166 -9.738 -10.583 -32.583 1.00 20.84 C ANISOU 1343 C GLU A 166 2115 3001 2802 128 -174 37 C ATOM 1344 O GLU A 166 -9.536 -9.901 -33.613 1.00 25.51 O ANISOU 1344 O GLU A 166 3006 3442 3241 -182 -296 290 O ATOM 1345 CB AGLU A 166 -11.170 -12.710 -32.904 0.50 26.65 C ANISOU 1345 CB AGLU A 166 2843 3546 3733 -512 -276 74 C ATOM 1346 CB BGLU A 166 -11.286 -12.575 -32.555 0.50 25.66 C ANISOU 1346 CB BGLU A 166 2732 3465 3552 -478 -251 -5 C ATOM 1347 CG AGLU A 166 -11.172 -14.087 -33.629 0.50 32.44 C ANISOU 1347 CG AGLU A 166 3425 4145 4754 -16 359 -154 C ATOM 1348 CG BGLU A 166 -11.397 -14.104 -32.695 0.50 28.50 C ANISOU 1348 CG BGLU A 166 4006 3534 3286 28 74 -18 C ATOM 1349 CD AGLU A 166 -10.641 -14.043 -35.043 0.50 32.80 C ANISOU 1349 CD AGLU A 166 4109 4285 4067 -77 -590 -69 C ATOM 1350 CD BGLU A 166 -12.847 -14.592 -33.012 0.50 39.95 C ANISOU 1350 CD BGLU A 166 4424 4684 6068 -358 -578 -109 C ATOM 1351 OE1AGLU A 166 -11.108 -13.185 -35.831 0.50 38.14 O ANISOU 1351 OE1AGLU A 166 4603 5265 4623 122 -928 -377 O ATOM 1352 OE1BGLU A 166 -13.717 -13.826 -33.568 0.50 40.29 O ANISOU 1352 OE1BGLU A 166 4078 5569 5661 433 -667 -306 O ATOM 1353 OE2AGLU A 166 -9.625 -14.748 -35.350 0.50 37.82 O ANISOU 1353 OE2AGLU A 166 5357 4005 5004 108 821 -930 O ATOM 1354 OE2BGLU A 166 -13.080 -15.795 -32.758 0.50 40.34 O ANISOU 1354 OE2BGLU A 166 3719 4827 6779 -1143 524 1127 O ATOM 1355 N ASN A 167 -9.883 -10.015 -31.389 1.00 21.46 N ANISOU 1355 N ASN A 167 2495 2766 2890 -117 -239 123 N ATOM 1356 CA ASN A 167 -10.039 -8.641 -31.122 1.00 22.28 C ANISOU 1356 CA ASN A 167 2684 2932 2847 -81 -173 -164 C ATOM 1357 C ASN A 167 -8.745 -7.919 -30.628 1.00 23.33 C ANISOU 1357 C ASN A 167 2873 2850 3142 188 -364 -195 C ATOM 1358 O ASN A 167 -8.717 -6.715 -30.602 1.00 24.24 O ANISOU 1358 O ASN A 167 2935 2955 3319 -56 -250 9 O ATOM 1359 CB ASN A 167 -11.193 -8.393 -30.203 1.00 24.02 C ANISOU 1359 CB ASN A 167 2895 3296 2933 -111 -420 75 C ATOM 1360 CG ASN A 167 -12.576 -8.680 -30.900 1.00 28.12 C ANISOU 1360 CG ASN A 167 3108 4017 3558 -53 -189 491 C ATOM 1361 OD1 ASN A 167 -12.636 -8.426 -32.066 1.00 30.00 O ANISOU 1361 OD1 ASN A 167 3239 4299 3858 -182 -481 3 O ATOM 1362 ND2 ASN A 167 -13.460 -9.368 -30.230 1.00 32.92 N ANISOU 1362 ND2 ASN A 167 3551 4435 4522 -78 -393 420 N ATOM 1363 N ASN A 168 -7.668 -8.709 -30.466 1.00 21.02 N ANISOU 1363 N ASN A 168 2436 2763 2785 -80 -242 4 N ATOM 1364 CA ASN A 168 -6.318 -8.037 -30.073 1.00 20.76 C ANISOU 1364 CA ASN A 168 2540 2652 2695 -305 -73 -8 C ATOM 1365 C ASN A 168 -6.462 -7.119 -28.942 1.00 20.26 C ANISOU 1365 C ASN A 168 2556 2556 2585 83 -120 98 C ATOM 1366 O ASN A 168 -5.709 -6.076 -28.901 1.00 19.90 O ANISOU 1366 O ASN A 168 2445 2484 2631 -124 -144 138 O ATOM 1367 CB ASN A 168 -5.695 -7.450 -31.297 1.00 19.38 C ANISOU 1367 CB ASN A 168 2382 2624 2355 -67 -226 -114 C ATOM 1368 CG ASN A 168 -4.193 -7.555 -31.343 1.00 20.64 C ANISOU 1368 CG ASN A 168 2531 2711 2597 -51 -80 106 C ATOM 1369 OD1 ASN A 168 -3.586 -8.276 -30.552 1.00 20.41 O ANISOU 1369 OD1 ASN A 168 2537 2564 2652 -118 -117 46 O ATOM 1370 ND2 ASN A 168 -3.588 -6.758 -32.241 1.00 22.37 N ANISOU 1370 ND2 ASN A 168 2794 2860 2845 -167 -88 128 N ATOM 1371 N ILE A 169 -7.275 -7.374 -27.905 1.00 19.70 N ANISOU 1371 N ILE A 169 2380 2464 2641 -43 -129 0 N ATOM 1372 CA ILE A 169 -7.548 -6.411 -26.890 1.00 21.92 C ANISOU 1372 CA ILE A 169 2782 2918 2625 -105 -131 52 C ATOM 1373 C ILE A 169 -6.353 -6.011 -26.015 1.00 19.61 C ANISOU 1373 C ILE A 169 2378 2425 2647 149 -196 -95 C ATOM 1374 O ILE A 169 -6.291 -4.891 -25.470 1.00 20.70 O ANISOU 1374 O ILE A 169 2476 2613 2775 7 -145 -63 O ATOM 1375 CB ILE A 169 -8.785 -6.910 -26.047 1.00 24.73 C ANISOU 1375 CB ILE A 169 2660 3456 3280 -52 -16 -291 C ATOM 1376 CG1 ILE A 169 -10.032 -6.524 -26.957 1.00 29.56 C ANISOU 1376 CG1 ILE A 169 3680 3919 3632 106 -346 -42 C ATOM 1377 CG2 ILE A 169 -8.867 -6.362 -24.656 1.00 30.92 C ANISOU 1377 CG2 ILE A 169 3491 4188 4068 -350 -3 36 C ATOM 1378 CD1 ILE A 169 -11.298 -7.145 -26.341 1.00 39.92 C ANISOU 1378 CD1 ILE A 169 4912 4941 5313 -244 263 -201 C ATOM 1379 N PHE A 170 -5.391 -6.944 -25.844 1.00 18.82 N ANISOU 1379 N PHE A 170 2340 2329 2482 27 -148 -177 N ATOM 1380 CA PHE A 170 -4.227 -6.572 -24.963 1.00 17.99 C ANISOU 1380 CA PHE A 170 2215 2247 2373 81 24 13 C ATOM 1381 C PHE A 170 -3.490 -5.486 -25.645 1.00 17.71 C ANISOU 1381 C PHE A 170 2223 2254 2251 75 14 -17 C ATOM 1382 O PHE A 170 -3.120 -4.464 -25.004 1.00 18.62 O ANISOU 1382 O PHE A 170 2338 2343 2392 16 -40 -18 O ATOM 1383 CB PHE A 170 -3.402 -7.840 -24.689 1.00 18.92 C ANISOU 1383 CB PHE A 170 2366 2404 2418 14 -43 131 C ATOM 1384 CG PHE A 170 -2.804 -7.809 -23.278 1.00 17.03 C ANISOU 1384 CG PHE A 170 2227 2091 2150 13 -60 -110 C ATOM 1385 CD1 PHE A 170 -1.966 -6.796 -22.852 1.00 18.97 C ANISOU 1385 CD1 PHE A 170 2320 2462 2426 -197 66 69 C ATOM 1386 CD2 PHE A 170 -3.154 -8.763 -22.346 1.00 17.39 C ANISOU 1386 CD2 PHE A 170 2171 2259 2176 39 78 -2 C ATOM 1387 CE1 PHE A 170 -1.451 -6.804 -21.566 1.00 18.08 C ANISOU 1387 CE1 PHE A 170 2186 2356 2327 3 80 80 C ATOM 1388 CE2 PHE A 170 -2.710 -8.746 -21.074 1.00 18.05 C ANISOU 1388 CE2 PHE A 170 2195 2317 2343 -32 -146 -13 C ATOM 1389 CZ PHE A 170 -1.833 -7.784 -20.654 1.00 17.73 C ANISOU 1389 CZ PHE A 170 2245 2162 2329 66 -8 97 C ATOM 1390 N VAL A 171 -3.129 -5.663 -26.965 1.00 16.75 N ANISOU 1390 N VAL A 171 2111 2138 2112 -112 -147 -29 N ATOM 1391 CA VAL A 171 -2.423 -4.603 -27.729 1.00 17.69 C ANISOU 1391 CA VAL A 171 2154 2355 2212 -71 -78 42 C ATOM 1392 C VAL A 171 -3.213 -3.352 -27.847 1.00 18.23 C ANISOU 1392 C VAL A 171 2314 2297 2313 -156 -186 -43 C ATOM 1393 O VAL A 171 -2.709 -2.250 -27.693 1.00 19.86 O ANISOU 1393 O VAL A 171 2559 2526 2461 -11 -41 85 O ATOM 1394 CB VAL A 171 -1.996 -5.182 -29.041 1.00 18.36 C ANISOU 1394 CB VAL A 171 2303 2332 2338 36 -8 -56 C ATOM 1395 CG1 VAL A 171 -1.459 -4.105 -29.980 1.00 21.59 C ANISOU 1395 CG1 VAL A 171 2583 2798 2821 37 117 86 C ATOM 1396 CG2 VAL A 171 -0.999 -6.332 -28.890 1.00 19.22 C ANISOU 1396 CG2 VAL A 171 2363 2507 2433 55 85 19 C ATOM 1397 N GLU A 172 -4.554 -3.488 -28.221 1.00 18.91 N ANISOU 1397 N GLU A 172 2188 2346 2648 14 -21 103 N ATOM 1398 CA GLU A 172 -5.293 -2.337 -28.666 1.00 21.16 C ANISOU 1398 CA GLU A 172 2803 2539 2696 12 -465 -48 C ATOM 1399 C GLU A 172 -5.905 -1.554 -27.540 1.00 21.60 C ANISOU 1399 C GLU A 172 2540 2817 2850 75 -3 107 C ATOM 1400 O GLU A 172 -6.228 -0.332 -27.743 1.00 25.12 O ANISOU 1400 O GLU A 172 3155 2903 3486 24 -308 134 O ATOM 1401 CB GLU A 172 -6.412 -2.760 -29.672 1.00 21.83 C ANISOU 1401 CB GLU A 172 2508 2886 2899 118 -236 -49 C ATOM 1402 CG GLU A 172 -5.854 -3.265 -30.941 1.00 23.55 C ANISOU 1402 CG GLU A 172 2801 3333 2814 -97 -136 116 C ATOM 1403 CD GLU A 172 -5.078 -2.371 -31.953 1.00 24.66 C ANISOU 1403 CD GLU A 172 3269 3079 3021 108 -383 200 C ATOM 1404 OE1 GLU A 172 -4.939 -1.191 -31.764 1.00 30.29 O ANISOU 1404 OE1 GLU A 172 4384 3458 3667 -282 -880 174 O ATOM 1405 OE2 GLU A 172 -4.807 -2.916 -33.028 1.00 28.24 O ANISOU 1405 OE2 GLU A 172 3537 3547 3644 134 147 277 O ATOM 1406 N ARG A 173 -6.169 -2.136 -26.415 1.00 21.99 N ANISOU 1406 N ARG A 173 2716 2900 2736 171 -111 -65 N ATOM 1407 CA ARG A 173 -6.832 -1.563 -25.288 1.00 20.52 C ANISOU 1407 CA ARG A 173 2615 2541 2638 18 -48 -23 C ATOM 1408 C ARG A 173 -5.929 -1.505 -24.052 1.00 20.92 C ANISOU 1408 C ARG A 173 2571 2641 2734 46 -86 117 C ATOM 1409 O ARG A 173 -5.726 -0.443 -23.442 1.00 21.07 O ANISOU 1409 O ARG A 173 2491 2616 2898 127 -132 -186 O ATOM 1410 CB ARG A 173 -8.163 -2.198 -25.035 1.00 23.64 C ANISOU 1410 CB ARG A 173 2763 2898 3320 -28 -69 -294 C ATOM 1411 CG ARG A 173 -8.831 -1.606 -23.785 1.00 38.84 C ANISOU 1411 CG ARG A 173 4909 4986 4863 54 320 -417 C ATOM 1412 CD ARG A 173 -10.347 -2.010 -23.418 1.00 50.63 C ANISOU 1412 CD ARG A 173 5881 5759 7597 -821 138 342 C ATOM 1413 NE ARG A 173 -11.128 -2.321 -24.645 1.00 51.91 N ANISOU 1413 NE ARG A 173 6054 6328 7341 -179 -1237 166 N ATOM 1414 CZ ARG A 173 -12.092 -3.292 -24.725 1.00 70.03 C ANISOU 1414 CZ ARG A 173 8342 9175 9089 -723 -984 1383 C ATOM 1415 NH1 ARG A 173 -12.423 -4.063 -23.648 1.00 52.56 N ANISOU 1415 NH1 ARG A 173 5316 7589 7063 -1187 -315 148 N ATOM 1416 NH2 ARG A 173 -12.732 -3.531 -25.905 1.00 69.58 N ANISOU 1416 NH2 ARG A 173 8941 9268 8225 778 -579 -449 N ATOM 1417 N VAL A 174 -5.443 -2.656 -23.573 1.00 19.55 N ANISOU 1417 N VAL A 174 2381 2443 2604 60 58 50 N ATOM 1418 CA VAL A 174 -4.757 -2.655 -22.334 1.00 17.49 C ANISOU 1418 CA VAL A 174 2136 2210 2299 54 128 -125 C ATOM 1419 C VAL A 174 -3.437 -1.841 -22.379 1.00 18.08 C ANISOU 1419 C VAL A 174 2183 2407 2280 -95 49 -67 C ATOM 1420 O VAL A 174 -3.124 -1.120 -21.438 1.00 18.45 O ANISOU 1420 O VAL A 174 2275 2371 2363 19 56 -95 O ATOM 1421 CB VAL A 174 -4.480 -4.131 -21.844 1.00 20.09 C ANISOU 1421 CB VAL A 174 2438 2581 2613 -67 68 262 C ATOM 1422 CG1 VAL A 174 -3.653 -4.176 -20.579 1.00 18.14 C ANISOU 1422 CG1 VAL A 174 2350 2210 2332 -140 206 104 C ATOM 1423 CG2 VAL A 174 -5.784 -4.862 -21.713 1.00 22.23 C ANISOU 1423 CG2 VAL A 174 2759 2693 2994 -118 21 75 C ATOM 1424 N LEU A 175 -2.647 -2.013 -23.438 1.00 17.66 N ANISOU 1424 N LEU A 175 2269 2209 2230 -36 -30 -100 N ATOM 1425 CA LEU A 175 -1.375 -1.341 -23.553 1.00 17.28 C ANISOU 1425 CA LEU A 175 2183 2128 2253 4 69 4 C ATOM 1426 C LEU A 175 -1.588 0.182 -23.511 1.00 16.93 C ANISOU 1426 C LEU A 175 2168 2100 2161 -25 -108 49 C ATOM 1427 O LEU A 175 -1.048 0.833 -22.638 1.00 17.38 O ANISOU 1427 O LEU A 175 2215 2138 2250 122 -92 13 O ATOM 1428 CB LEU A 175 -0.638 -1.861 -24.766 1.00 17.70 C ANISOU 1428 CB LEU A 175 2251 2199 2275 37 -35 73 C ATOM 1429 CG LEU A 175 0.571 -1.125 -25.319 1.00 16.88 C ANISOU 1429 CG LEU A 175 2128 2166 2118 0 -72 -17 C ATOM 1430 CD1 LEU A 175 1.631 -1.149 -24.280 1.00 17.51 C ANISOU 1430 CD1 LEU A 175 2100 2239 2312 64 23 -52 C ATOM 1431 CD2 LEU A 175 1.053 -1.589 -26.657 1.00 20.12 C ANISOU 1431 CD2 LEU A 175 2418 2608 2617 -16 75 -100 C ATOM 1432 N PRO A 176 -2.356 0.753 -24.459 1.00 18.04 N ANISOU 1432 N PRO A 176 2274 2176 2404 -22 -86 -22 N ATOM 1433 CA PRO A 176 -2.471 2.254 -24.362 1.00 20.11 C ANISOU 1433 CA PRO A 176 2545 2440 2654 89 -93 -103 C ATOM 1434 C PRO A 176 -3.243 2.668 -23.168 1.00 18.08 C ANISOU 1434 C PRO A 176 2314 2301 2255 0 -189 150 C ATOM 1435 O PRO A 176 -2.996 3.829 -22.649 1.00 19.61 O ANISOU 1435 O PRO A 176 2546 2365 2538 174 -98 38 O ATOM 1436 CB PRO A 176 -3.269 2.588 -25.665 1.00 23.29 C ANISOU 1436 CB PRO A 176 3066 2877 2903 245 -15 120 C ATOM 1437 CG PRO A 176 -3.801 1.353 -26.192 1.00 23.78 C ANISOU 1437 CG PRO A 176 3013 2818 3202 116 -369 161 C ATOM 1438 CD PRO A 176 -2.995 0.163 -25.634 1.00 18.74 C ANISOU 1438 CD PRO A 176 2373 2470 2275 161 -1 13 C ATOM 1439 N GLY A 177 -4.080 1.856 -22.594 1.00 18.55 N ANISOU 1439 N GLY A 177 2307 2394 2346 161 -78 -37 N ATOM 1440 CA GLY A 177 -4.805 2.203 -21.370 1.00 19.39 C ANISOU 1440 CA GLY A 177 2383 2376 2608 -53 -28 -178 C ATOM 1441 C GLY A 177 -3.958 2.396 -20.200 1.00 20.18 C ANISOU 1441 C GLY A 177 2618 2630 2416 126 -93 43 C ATOM 1442 O GLY A 177 -4.316 3.068 -19.232 1.00 22.39 O ANISOU 1442 O GLY A 177 2683 2858 2964 234 55 -266 O ATOM 1443 N ALA A 178 -2.734 1.831 -20.189 1.00 17.56 N ANISOU 1443 N ALA A 178 2167 2230 2272 50 77 -127 N ATOM 1444 CA ALA A 178 -1.826 1.873 -19.041 1.00 17.92 C ANISOU 1444 CA ALA A 178 2327 2201 2281 75 97 27 C ATOM 1445 C ALA A 178 -0.565 2.669 -19.331 1.00 16.84 C ANISOU 1445 C ALA A 178 2128 2106 2165 64 -63 -124 C ATOM 1446 O ALA A 178 0.506 2.483 -18.715 1.00 17.39 O ANISOU 1446 O ALA A 178 2208 2186 2212 66 -17 -74 O ATOM 1447 CB ALA A 178 -1.539 0.435 -18.580 1.00 19.77 C ANISOU 1447 CB ALA A 178 2426 2433 2652 45 -112 41 C ATOM 1448 N ILE A 179 -0.673 3.576 -20.309 1.00 17.80 N ANISOU 1448 N ILE A 179 2152 2339 2271 -20 29 14 N ATOM 1449 CA ILE A 179 0.292 4.591 -20.674 1.00 17.46 C ANISOU 1449 CA ILE A 179 2217 2054 2364 194 -338 89 C ATOM 1450 C ILE A 179 -0.423 5.980 -20.507 1.00 19.69 C ANISOU 1450 C ILE A 179 2365 2361 2752 123 5 -230 C ATOM 1451 O ILE A 179 -1.560 6.090 -20.937 1.00 18.98 O ANISOU 1451 O ILE A 179 2410 2309 2490 68 -165 -81 O ATOM 1452 CB ILE A 179 0.791 4.444 -22.069 1.00 17.85 C ANISOU 1452 CB ILE A 179 2050 2198 2533 126 46 -5 C ATOM 1453 CG1 ILE A 179 1.590 3.128 -22.258 1.00 18.44 C ANISOU 1453 CG1 ILE A 179 2266 2201 2539 39 -151 102 C ATOM 1454 CG2 ILE A 179 1.678 5.688 -22.485 1.00 20.04 C ANISOU 1454 CG2 ILE A 179 2483 2465 2665 175 56 76 C ATOM 1455 CD1 ILE A 179 1.808 2.753 -23.705 1.00 19.00 C ANISOU 1455 CD1 ILE A 179 2287 2315 2615 130 75 23 C ATOM 1456 N LEU A 180 0.204 6.841 -19.762 1.00 17.10 N ANISOU 1456 N LEU A 180 2107 2086 2303 259 -13 -37 N ATOM 1457 CA LEU A 180 -0.464 8.183 -19.477 1.00 19.01 C ANISOU 1457 CA LEU A 180 2273 2321 2627 284 162 -42 C ATOM 1458 C LEU A 180 -0.478 9.056 -20.680 1.00 21.49 C ANISOU 1458 C LEU A 180 2664 2734 2764 90 28 -16 C ATOM 1459 O LEU A 180 -1.589 9.634 -21.015 1.00 21.30 O ANISOU 1459 O LEU A 180 2543 2594 2956 325 -54 48 O ATOM 1460 CB LEU A 180 0.178 8.873 -18.343 1.00 17.44 C ANISOU 1460 CB LEU A 180 2192 2155 2277 198 223 8 C ATOM 1461 CG LEU A 180 0.234 8.173 -17.015 1.00 20.81 C ANISOU 1461 CG LEU A 180 2558 2695 2654 126 -124 13 C ATOM 1462 CD1 LEU A 180 1.019 9.005 -16.076 1.00 21.14 C ANISOU 1462 CD1 LEU A 180 2838 2584 2608 114 74 -143 C ATOM 1463 CD2 LEU A 180 -1.114 7.699 -16.492 1.00 23.93 C ANISOU 1463 CD2 LEU A 180 3116 3043 2932 55 141 13 C ATOM 1464 N ARG A 181 0.569 9.082 -21.467 1.00 19.30 N ANISOU 1464 N ARG A 181 2531 2341 2460 60 55 192 N ATOM 1465 CA ARG A 181 0.538 9.840 -22.700 1.00 20.07 C ANISOU 1465 CA ARG A 181 2536 2509 2579 279 -60 96 C ATOM 1466 C ARG A 181 -0.129 9.035 -23.825 1.00 21.60 C ANISOU 1466 C ARG A 181 2602 2788 2814 102 58 58 C ATOM 1467 O ARG A 181 -0.449 7.901 -23.663 1.00 20.86 O ANISOU 1467 O ARG A 181 2594 2540 2791 63 -268 42 O ATOM 1468 CB ARG A 181 1.955 10.221 -23.128 1.00 19.77 C ANISOU 1468 CB ARG A 181 2576 2498 2437 136 -53 186 C ATOM 1469 CG ARG A 181 2.775 9.074 -23.712 1.00 20.13 C ANISOU 1469 CG ARG A 181 2652 2427 2568 188 28 67 C ATOM 1470 CD ARG A 181 4.131 9.542 -24.160 1.00 19.88 C ANISOU 1470 CD ARG A 181 2665 2397 2491 175 29 -146 C ATOM 1471 NE ARG A 181 5.003 8.484 -24.639 1.00 19.98 N ANISOU 1471 NE ARG A 181 2636 2434 2519 177 109 43 N ATOM 1472 CZ ARG A 181 5.244 8.199 -25.901 1.00 20.37 C ANISOU 1472 CZ ARG A 181 2601 2624 2515 165 -105 -58 C ATOM 1473 NH1 ARG A 181 4.651 8.855 -26.856 1.00 19.93 N ANISOU 1473 NH1 ARG A 181 2636 2478 2455 190 -3 163 N ATOM 1474 NH2 ARG A 181 6.079 7.230 -26.196 1.00 18.98 N ANISOU 1474 NH2 ARG A 181 2497 2335 2377 250 10 0 N ATOM 1475 N GLN A 182 -0.382 9.701 -24.935 1.00 21.30 N ANISOU 1475 N GLN A 182 2714 2698 2678 311 45 -14 N ATOM 1476 CA GLN A 182 -0.865 9.049 -26.140 1.00 23.06 C ANISOU 1476 CA GLN A 182 2911 2895 2953 104 -6 104 C ATOM 1477 C GLN A 182 0.313 8.664 -27.028 1.00 22.41 C ANISOU 1477 C GLN A 182 2674 2874 2967 -89 19 -137 C ATOM 1478 O GLN A 182 1.107 9.473 -27.443 1.00 24.09 O ANISOU 1478 O GLN A 182 3183 2750 3220 162 85 66 O ATOM 1479 CB GLN A 182 -1.714 10.081 -26.955 1.00 27.15 C ANISOU 1479 CB GLN A 182 3564 3382 3368 371 -209 229 C ATOM 1480 CG GLN A 182 -2.378 9.421 -28.172 1.00 32.42 C ANISOU 1480 CG GLN A 182 4102 4421 3793 245 33 5 C ATOM 1481 CD GLN A 182 -3.414 8.421 -27.931 1.00 39.72 C ANISOU 1481 CD GLN A 182 5498 4809 4784 -65 -889 206 C ATOM 1482 OE1 GLN A 182 -4.312 8.623 -27.108 1.00 52.87 O ANISOU 1482 OE1 GLN A 182 5244 7393 7449 366 1094 58 O ATOM 1483 NE2 GLN A 182 -3.273 7.279 -28.609 1.00 52.30 N ANISOU 1483 NE2 GLN A 182 7616 6439 5817 194 -1384 -669 N ATOM 1484 N LEU A 183 0.434 7.329 -27.366 1.00 20.89 N ANISOU 1484 N LEU A 183 2692 2609 2636 144 -50 -55 N ATOM 1485 CA LEU A 183 1.440 6.978 -28.297 1.00 19.92 C ANISOU 1485 CA LEU A 183 2531 2513 2524 -80 -159 -41 C ATOM 1486 C LEU A 183 1.144 7.526 -29.676 1.00 19.86 C ANISOU 1486 C LEU A 183 2584 2383 2578 13 102 -102 C ATOM 1487 O LEU A 183 -0.027 7.612 -30.089 1.00 22.93 O ANISOU 1487 O LEU A 183 2901 2837 2973 249 -187 -74 O ATOM 1488 CB LEU A 183 1.490 5.397 -28.361 1.00 19.71 C ANISOU 1488 CB LEU A 183 2606 2464 2420 84 -60 44 C ATOM 1489 CG LEU A 183 1.935 4.638 -27.099 1.00 20.72 C ANISOU 1489 CG LEU A 183 2733 2609 2531 -34 -117 66 C ATOM 1490 CD1 LEU A 183 1.943 3.163 -27.435 1.00 20.54 C ANISOU 1490 CD1 LEU A 183 2658 2471 2672 132 -112 110 C ATOM 1491 CD2 LEU A 183 3.366 5.067 -26.694 1.00 22.01 C ANISOU 1491 CD2 LEU A 183 2725 2886 2750 -82 41 269 C ATOM 1492 N SER A 184 2.172 7.750 -30.416 1.00 19.63 N ANISOU 1492 N SER A 184 2503 2413 2540 219 -96 80 N ATOM 1493 CA SER A 184 2.067 8.120 -31.831 1.00 22.12 C ANISOU 1493 CA SER A 184 2765 2844 2794 527 -169 51 C ATOM 1494 C SER A 184 1.601 6.984 -32.662 1.00 24.23 C ANISOU 1494 C SER A 184 3277 2905 3023 3 -268 -180 C ATOM 1495 O SER A 184 1.648 5.787 -32.279 1.00 21.56 O ANISOU 1495 O SER A 184 2867 2687 2637 242 -111 208 O ATOM 1496 CB SER A 184 3.366 8.724 -32.307 1.00 24.05 C ANISOU 1496 CB SER A 184 3199 2895 3043 283 74 213 C ATOM 1497 OG SER A 184 4.342 7.643 -32.540 1.00 23.32 O ANISOU 1497 OG SER A 184 3043 2819 2997 324 210 115 O ATOM 1498 N ASP A 185 1.119 7.270 -33.853 1.00 22.57 N ANISOU 1498 N ASP A 185 3226 2622 2727 450 -233 327 N ATOM 1499 CA ASP A 185 0.670 6.207 -34.711 1.00 25.09 C ANISOU 1499 CA ASP A 185 3233 3289 3010 313 -506 434 C ATOM 1500 C ASP A 185 1.817 5.266 -35.023 1.00 21.23 C ANISOU 1500 C ASP A 185 2891 2866 2309 159 -330 116 C ATOM 1501 O ASP A 185 1.638 4.099 -35.103 1.00 25.52 O ANISOU 1501 O ASP A 185 3456 3322 2916 84 -301 43 O ATOM 1502 CB ASP A 185 0.070 6.725 -36.040 1.00 30.27 C ANISOU 1502 CB ASP A 185 4288 3981 3229 465 -455 191 C ATOM 1503 CG ASP A 185 -1.238 7.455 -35.862 1.00 41.42 C ANISOU 1503 CG ASP A 185 4852 5926 4960 788 259 595 C ATOM 1504 OD1 ASP A 185 -1.886 7.334 -34.844 1.00 36.87 O ANISOU 1504 OD1 ASP A 185 4344 4920 4745 1006 -18 228 O ATOM 1505 OD2 ASP A 185 -1.615 8.167 -36.784 1.00 42.08 O ANISOU 1505 OD2 ASP A 185 5310 5512 5167 1175 -511 446 O ATOM 1506 N GLU A 186 2.988 5.825 -35.182 1.00 22.80 N ANISOU 1506 N GLU A 186 3139 2850 2671 340 -12 421 N ATOM 1507 CA GLU A 186 4.164 5.050 -35.488 1.00 25.77 C ANISOU 1507 CA GLU A 186 3449 3451 2890 373 -226 154 C ATOM 1508 C GLU A 186 4.535 4.123 -34.343 1.00 23.74 C ANISOU 1508 C GLU A 186 3389 2835 2795 114 -30 6 C ATOM 1509 O GLU A 186 4.910 3.002 -34.541 1.00 20.45 O ANISOU 1509 O GLU A 186 2751 2533 2484 180 58 92 O ATOM 1510 CB GLU A 186 5.324 5.965 -35.822 1.00 30.50 C ANISOU 1510 CB GLU A 186 4080 3601 3904 52 418 307 C ATOM 1511 CG GLU A 186 5.147 6.719 -37.131 1.00 36.61 C ANISOU 1511 CG GLU A 186 4894 4902 4112 703 199 530 C ATOM 1512 CD GLU A 186 4.129 7.878 -37.091 1.00 53.07 C ANISOU 1512 CD GLU A 186 7956 5985 6223 1655 606 108 C ATOM 1513 OE1 GLU A 186 3.776 8.385 -36.027 1.00 37.01 O ANISOU 1513 OE1 GLU A 186 5627 4080 4355 328 8 460 O ATOM 1514 OE2 GLU A 186 3.663 8.267 -38.184 1.00 59.52 O ANISOU 1514 OE2 GLU A 186 8717 6874 7022 1383 881 1181 O ATOM 1515 N GLU A 187 4.470 4.661 -33.152 1.00 21.92 N ANISOU 1515 N GLU A 187 2963 2647 2716 157 -39 265 N ATOM 1516 CA GLU A 187 4.744 3.758 -31.927 1.00 19.73 C ANISOU 1516 CA GLU A 187 2627 2519 2349 266 -112 81 C ATOM 1517 C GLU A 187 3.807 2.691 -31.888 1.00 17.90 C ANISOU 1517 C GLU A 187 2286 2277 2235 145 193 -54 C ATOM 1518 O GLU A 187 4.135 1.459 -31.597 1.00 18.56 O ANISOU 1518 O GLU A 187 2490 2351 2210 194 80 59 O ATOM 1519 CB GLU A 187 4.783 4.651 -30.691 1.00 20.44 C ANISOU 1519 CB GLU A 187 2704 2551 2512 157 -49 -1 C ATOM 1520 CG GLU A 187 5.970 5.498 -30.599 1.00 20.56 C ANISOU 1520 CG GLU A 187 2600 2637 2575 166 13 52 C ATOM 1521 CD GLU A 187 5.971 6.668 -29.557 1.00 20.50 C ANISOU 1521 CD GLU A 187 2558 2511 2717 -104 43 69 C ATOM 1522 OE1 GLU A 187 4.881 7.221 -29.319 1.00 21.69 O ANISOU 1522 OE1 GLU A 187 2798 2602 2841 278 -18 67 O ATOM 1523 OE2 GLU A 187 6.971 6.956 -28.943 1.00 20.93 O ANISOU 1523 OE2 GLU A 187 2765 2496 2689 51 -115 114 O ATOM 1524 N MET A 188 2.546 3.045 -32.114 1.00 19.14 N ANISOU 1524 N MET A 188 2479 2526 2266 113 -251 -158 N ATOM 1525 CA MET A 188 1.463 2.067 -32.088 1.00 19.88 C ANISOU 1525 CA MET A 188 2511 2664 2376 236 76 310 C ATOM 1526 C MET A 188 1.725 0.934 -33.070 1.00 18.12 C ANISOU 1526 C MET A 188 2201 2354 2328 -83 -71 -3 C ATOM 1527 O MET A 188 1.617 -0.243 -32.728 1.00 20.75 O ANISOU 1527 O MET A 188 2562 2693 2628 96 -171 164 O ATOM 1528 CB MET A 188 0.126 2.740 -32.405 1.00 24.72 C ANISOU 1528 CB MET A 188 3139 3340 2912 730 -190 15 C ATOM 1529 CG MET A 188 -1.047 2.198 -31.604 1.00 32.41 C ANISOU 1529 CG MET A 188 3923 4122 4269 315 -625 1120 C ATOM 1530 SD MET A 188 -0.531 1.367 -30.089 1.00 25.40 S ANISOU 1530 SD MET A 188 3114 3380 3153 -46 169 230 S ATOM 1531 CE MET A 188 -1.860 0.184 -29.882 1.00 28.39 C ANISOU 1531 CE MET A 188 3622 3767 3396 -275 -526 -239 C ATOM 1532 N ALA A 189 2.071 1.308 -34.295 1.00 18.11 N ANISOU 1532 N ALA A 189 2278 2326 2276 56 -189 29 N ATOM 1533 CA ALA A 189 2.355 0.360 -35.344 1.00 18.71 C ANISOU 1533 CA ALA A 189 2401 2423 2283 85 -49 188 C ATOM 1534 C ALA A 189 3.428 -0.592 -35.085 1.00 17.28 C ANISOU 1534 C ALA A 189 2205 2281 2079 44 201 -24 C ATOM 1535 O ALA A 189 3.350 -1.772 -35.438 1.00 18.48 O ANISOU 1535 O ALA A 189 2365 2363 2289 -53 -120 56 O ATOM 1536 CB ALA A 189 2.620 1.106 -36.646 1.00 21.55 C ANISOU 1536 CB ALA A 189 2722 2934 2532 183 -57 374 C ATOM 1537 N GLU A 190 4.452 -0.095 -34.339 1.00 17.91 N ANISOU 1537 N GLU A 190 2283 2218 2301 -53 -99 40 N ATOM 1538 CA GLU A 190 5.555 -0.964 -33.904 1.00 17.58 C ANISOU 1538 CA GLU A 190 2240 2230 2209 -27 78 -25 C ATOM 1539 C GLU A 190 5.048 -1.947 -32.912 1.00 16.54 C ANISOU 1539 C GLU A 190 2112 2060 2109 0 0 46 C ATOM 1540 O GLU A 190 5.340 -3.173 -33.030 1.00 17.95 O ANISOU 1540 O GLU A 190 2334 2272 2212 68 -8 -78 O ATOM 1541 CB GLU A 190 6.731 -0.197 -33.361 1.00 16.21 C ANISOU 1541 CB GLU A 190 2083 2150 1924 -30 -8 38 C ATOM 1542 CG GLU A 190 7.795 -1.039 -32.786 1.00 17.87 C ANISOU 1542 CG GLU A 190 2269 2211 2309 21 0 -127 C ATOM 1543 CD GLU A 190 8.632 -1.822 -33.773 1.00 21.74 C ANISOU 1543 CD GLU A 190 2690 2930 2640 204 22 -59 C ATOM 1544 OE1 GLU A 190 8.446 -1.643 -34.983 1.00 20.61 O ANISOU 1544 OE1 GLU A 190 2757 2596 2477 220 72 64 O ATOM 1545 OE2 GLU A 190 9.364 -2.768 -33.340 1.00 20.50 O ANISOU 1545 OE2 GLU A 190 2639 2582 2567 50 31 46 O ATOM 1546 N TYR A 191 4.275 -1.515 -31.934 1.00 17.23 N ANISOU 1546 N TYR A 191 2148 2173 2223 -102 -27 21 N ATOM 1547 CA TYR A 191 3.751 -2.471 -30.978 1.00 17.54 C ANISOU 1547 CA TYR A 191 2192 2289 2184 73 8 71 C ATOM 1548 C TYR A 191 2.770 -3.492 -31.582 1.00 16.87 C ANISOU 1548 C TYR A 191 2249 2146 2015 -113 23 44 C ATOM 1549 O TYR A 191 2.710 -4.585 -31.148 1.00 18.03 O ANISOU 1549 O TYR A 191 2347 2245 2258 -12 -140 -4 O ATOM 1550 CB TYR A 191 3.129 -1.755 -29.796 1.00 16.94 C ANISOU 1550 CB TYR A 191 2243 2141 2052 -72 32 -58 C ATOM 1551 CG TYR A 191 4.107 -1.254 -28.769 1.00 15.95 C ANISOU 1551 CG TYR A 191 1902 2078 2078 9 1 94 C ATOM 1552 CD1 TYR A 191 4.931 -2.116 -28.108 1.00 17.61 C ANISOU 1552 CD1 TYR A 191 2242 2149 2298 84 -98 93 C ATOM 1553 CD2 TYR A 191 4.143 0.060 -28.416 1.00 16.04 C ANISOU 1553 CD2 TYR A 191 1877 2084 2130 23 87 -21 C ATOM 1554 CE1 TYR A 191 5.785 -1.673 -27.164 1.00 19.13 C ANISOU 1554 CE1 TYR A 191 2583 2330 2353 0 -214 99 C ATOM 1555 CE2 TYR A 191 4.998 0.508 -27.465 1.00 17.13 C ANISOU 1555 CE2 TYR A 191 2211 2144 2152 24 -19 6 C ATOM 1556 CZ TYR A 191 5.816 -0.372 -26.834 1.00 18.35 C ANISOU 1556 CZ TYR A 191 2395 2254 2320 24 -20 62 C ATOM 1557 OH TYR A 191 6.670 0.041 -25.890 1.00 17.67 O ANISOU 1557 OH TYR A 191 2272 2181 2259 -31 -206 92 O ATOM 1558 N ARG A 192 2.039 -3.100 -32.610 1.00 17.92 N ANISOU 1558 N ARG A 192 2194 2273 2339 51 -45 97 N ATOM 1559 CA ARG A 192 1.121 -3.982 -33.261 1.00 18.91 C ANISOU 1559 CA ARG A 192 2454 2346 2384 55 -76 60 C ATOM 1560 C ARG A 192 1.731 -4.955 -34.194 1.00 18.85 C ANISOU 1560 C ARG A 192 2385 2441 2335 33 -127 35 C ATOM 1561 O ARG A 192 1.198 -6.055 -34.387 1.00 19.37 O ANISOU 1561 O ARG A 192 2357 2523 2478 -27 -155 37 O ATOM 1562 CB ARG A 192 0.127 -3.141 -34.126 1.00 20.16 C ANISOU 1562 CB ARG A 192 2490 2581 2587 91 74 -39 C ATOM 1563 CG ARG A 192 -1.038 -3.882 -34.590 1.00 28.40 C ANISOU 1563 CG ARG A 192 3588 3469 3731 261 -155 -65 C ATOM 1564 CD ARG A 192 -1.938 -2.955 -35.440 1.00 31.45 C ANISOU 1564 CD ARG A 192 4072 4045 3832 288 -182 -106 C ATOM 1565 NE ARG A 192 -2.633 -2.055 -34.503 1.00 28.33 N ANISOU 1565 NE ARG A 192 3784 3680 3300 280 -265 109 N ATOM 1566 CZ ARG A 192 -2.345 -0.817 -34.416 1.00 25.51 C ANISOU 1566 CZ ARG A 192 3497 2963 3233 -250 -369 -164 C ATOM 1567 NH1 ARG A 192 -1.515 -0.223 -35.303 1.00 28.55 N ANISOU 1567 NH1 ARG A 192 3470 3765 3610 5 58 -258 N ATOM 1568 NH2 ARG A 192 -3.041 -0.059 -33.654 1.00 23.93 N ANISOU 1568 NH2 ARG A 192 2642 3670 2778 -195 174 -230 N ATOM 1569 N ARG A 193 2.859 -4.585 -34.740 1.00 18.29 N ANISOU 1569 N ARG A 193 2305 2416 2226 -83 -173 -127 N ATOM 1570 CA ARG A 193 3.539 -5.341 -35.772 1.00 19.11 C ANISOU 1570 CA ARG A 193 2265 2491 2505 139 -131 97 C ATOM 1571 C ARG A 193 3.634 -6.884 -35.636 1.00 18.56 C ANISOU 1571 C ARG A 193 2422 2309 2320 -100 -48 -26 C ATOM 1572 O ARG A 193 3.318 -7.592 -36.540 1.00 20.19 O ANISOU 1572 O ARG A 193 2583 2588 2498 91 -72 10 O ATOM 1573 CB ARG A 193 4.876 -4.645 -36.055 1.00 23.88 C ANISOU 1573 CB ARG A 193 3153 2898 3022 -153 217 191 C ATOM 1574 CG ARG A 193 5.647 -5.181 -37.177 1.00 26.36 C ANISOU 1574 CG ARG A 193 3528 3201 3286 34 111 324 C ATOM 1575 CD ARG A 193 6.823 -4.272 -37.465 1.00 21.72 C ANISOU 1575 CD ARG A 193 2722 2702 2829 -182 132 -174 C ATOM 1576 NE ARG A 193 7.842 -4.162 -36.435 1.00 19.79 N ANISOU 1576 NE ARG A 193 2631 2461 2428 86 109 90 N ATOM 1577 CZ ARG A 193 8.799 -5.059 -36.219 1.00 18.37 C ANISOU 1577 CZ ARG A 193 2163 2440 2374 106 27 -136 C ATOM 1578 NH1 ARG A 193 8.848 -6.149 -36.940 1.00 19.24 N ANISOU 1578 NH1 ARG A 193 2293 2346 2668 0 -12 -4 N ATOM 1579 NH2 ARG A 193 9.692 -4.879 -35.288 1.00 19.41 N ANISOU 1579 NH2 ARG A 193 2639 2357 2378 319 50 -245 N ATOM 1580 N PRO A 194 4.046 -7.365 -34.469 1.00 16.53 N ANISOU 1580 N PRO A 194 2130 2088 2062 69 -44 5 N ATOM 1581 CA PRO A 194 4.124 -8.799 -34.280 1.00 18.06 C ANISOU 1581 CA PRO A 194 2371 2223 2266 55 10 -43 C ATOM 1582 C PRO A 194 2.847 -9.514 -34.190 1.00 20.53 C ANISOU 1582 C PRO A 194 2543 2529 2727 -25 65 81 C ATOM 1583 O PRO A 194 2.784 -10.778 -34.181 1.00 20.28 O ANISOU 1583 O PRO A 194 2622 2512 2570 80 82 26 O ATOM 1584 CB PRO A 194 4.941 -8.971 -32.975 1.00 20.40 C ANISOU 1584 CB PRO A 194 2369 2756 2626 -23 -26 80 C ATOM 1585 CG PRO A 194 5.507 -7.645 -32.745 1.00 21.17 C ANISOU 1585 CG PRO A 194 2851 2585 2608 298 -213 8 C ATOM 1586 CD PRO A 194 4.534 -6.619 -33.315 1.00 18.63 C ANISOU 1586 CD PRO A 194 2343 2434 2301 30 32 -6 C ATOM 1587 N PHE A 195 1.746 -8.728 -34.073 1.00 20.01 N ANISOU 1587 N PHE A 195 2392 2573 2634 -5 147 183 N ATOM 1588 CA PHE A 195 0.382 -9.267 -33.764 1.00 18.83 C ANISOU 1588 CA PHE A 195 2444 2286 2422 -228 66 48 C ATOM 1589 C PHE A 195 -0.642 -8.808 -34.730 1.00 21.21 C ANISOU 1589 C PHE A 195 2679 2655 2723 21 62 -37 C ATOM 1590 O PHE A 195 -1.834 -8.798 -34.463 1.00 20.86 O ANISOU 1590 O PHE A 195 2684 2601 2641 -70 -3 -8 O ATOM 1591 CB PHE A 195 0.024 -8.755 -32.366 1.00 19.12 C ANISOU 1591 CB PHE A 195 2515 2352 2396 -95 -32 -18 C ATOM 1592 CG PHE A 195 1.037 -9.209 -31.340 1.00 18.93 C ANISOU 1592 CG PHE A 195 2348 2455 2387 109 41 64 C ATOM 1593 CD1 PHE A 195 1.393 -10.577 -31.128 1.00 17.97 C ANISOU 1593 CD1 PHE A 195 2256 2275 2297 -135 170 -195 C ATOM 1594 CD2 PHE A 195 1.653 -8.323 -30.486 1.00 18.63 C ANISOU 1594 CD2 PHE A 195 2274 2356 2446 -201 123 -37 C ATOM 1595 CE1 PHE A 195 2.366 -10.876 -30.223 1.00 18.73 C ANISOU 1595 CE1 PHE A 195 2389 2207 2520 59 245 89 C ATOM 1596 CE2 PHE A 195 2.590 -8.680 -29.592 1.00 19.08 C ANISOU 1596 CE2 PHE A 195 2495 2287 2466 -148 207 18 C ATOM 1597 CZ PHE A 195 2.949 -9.987 -29.397 1.00 17.69 C ANISOU 1597 CZ PHE A 195 2039 2495 2187 257 225 128 C ATOM 1598 N LEU A 196 -0.200 -8.373 -35.936 1.00 21.17 N ANISOU 1598 N LEU A 196 2717 2705 2621 -95 53 28 N ATOM 1599 CA LEU A 196 -1.151 -7.882 -36.903 1.00 21.38 C ANISOU 1599 CA LEU A 196 2811 2569 2742 54 167 43 C ATOM 1600 C LEU A 196 -2.188 -8.833 -37.369 1.00 22.02 C ANISOU 1600 C LEU A 196 2716 2909 2742 10 143 98 C ATOM 1601 O LEU A 196 -3.299 -8.418 -37.633 1.00 25.04 O ANISOU 1601 O LEU A 196 3104 3191 3218 88 -68 379 O ATOM 1602 CB LEU A 196 -0.363 -7.511 -38.198 1.00 26.34 C ANISOU 1602 CB LEU A 196 3399 3211 3398 26 488 -135 C ATOM 1603 CG LEU A 196 0.268 -6.201 -38.253 1.00 32.16 C ANISOU 1603 CG LEU A 196 4170 3952 4098 15 -210 190 C ATOM 1604 CD1 LEU A 196 0.704 -6.022 -39.720 1.00 31.13 C ANISOU 1604 CD1 LEU A 196 4102 3739 3986 480 1138 37 C ATOM 1605 CD2 LEU A 196 -0.687 -5.079 -37.996 1.00 28.51 C ANISOU 1605 CD2 LEU A 196 3469 3553 3811 -18 685 -498 C ATOM 1606 N ASN A 197 -1.886 -10.118 -37.482 1.00 22.30 N ANISOU 1606 N ASN A 197 2691 2900 2878 -129 60 127 N ATOM 1607 CA ASN A 197 -2.813 -11.135 -37.970 1.00 23.69 C ANISOU 1607 CA ASN A 197 3170 3032 2799 -207 -102 -145 C ATOM 1608 C ASN A 197 -3.639 -11.689 -36.910 1.00 23.71 C ANISOU 1608 C ASN A 197 2958 3050 2998 -133 188 -69 C ATOM 1609 O ASN A 197 -3.146 -12.267 -35.928 1.00 22.70 O ANISOU 1609 O ASN A 197 2816 3015 2793 147 -230 34 O ATOM 1610 CB ASN A 197 -2.037 -12.294 -38.636 1.00 25.01 C ANISOU 1610 CB ASN A 197 3293 3335 2871 -127 88 -9 C ATOM 1611 CG ASN A 197 -1.214 -11.764 -39.844 1.00 28.36 C ANISOU 1611 CG ASN A 197 3489 3562 3726 -220 -184 -45 C ATOM 1612 OD1 ASN A 197 -1.788 -11.026 -40.632 1.00 30.55 O ANISOU 1612 OD1 ASN A 197 4203 3720 3682 -315 -19 91 O ATOM 1613 ND2 ASN A 197 0.016 -12.104 -39.920 1.00 28.87 N ANISOU 1613 ND2 ASN A 197 3617 3837 3514 -233 274 -110 N ATOM 1614 N ALA A 198 -4.962 -11.699 -37.070 1.00 23.40 N ANISOU 1614 N ALA A 198 2872 3190 2826 71 -139 140 N ATOM 1615 CA ALA A 198 -5.804 -12.398 -36.128 1.00 23.75 C ANISOU 1615 CA ALA A 198 2919 3183 2922 159 -258 150 C ATOM 1616 C ALA A 198 -5.471 -13.851 -36.111 1.00 24.05 C ANISOU 1616 C ALA A 198 2950 3073 3112 -194 -130 59 C ATOM 1617 O ALA A 198 -5.089 -14.406 -37.129 1.00 27.37 O ANISOU 1617 O ALA A 198 3608 3535 3255 8 -115 -140 O ATOM 1618 CB ALA A 198 -7.326 -12.135 -36.540 1.00 26.39 C ANISOU 1618 CB ALA A 198 3036 3599 3390 -109 -22 86 C ATOM 1619 N GLY A 199 -5.659 -14.504 -34.994 1.00 20.51 N ANISOU 1619 N GLY A 199 2519 2709 2562 -27 -148 -164 N ATOM 1620 CA GLY A 199 -5.344 -15.886 -34.818 1.00 20.74 C ANISOU 1620 CA GLY A 199 2495 2723 2662 -178 -178 32 C ATOM 1621 C GLY A 199 -4.094 -16.081 -33.901 1.00 21.23 C ANISOU 1621 C GLY A 199 2761 2684 2619 78 -116 82 C ATOM 1622 O GLY A 199 -3.892 -15.260 -33.036 1.00 19.72 O ANISOU 1622 O GLY A 199 2333 2553 2607 -73 -90 -100 O ATOM 1623 N GLU A 200 -3.482 -17.199 -34.036 1.00 21.60 N ANISOU 1623 N GLU A 200 2577 2908 2720 -64 -216 -229 N ATOM 1624 CA GLU A 200 -2.460 -17.674 -33.187 1.00 19.85 C ANISOU 1624 CA GLU A 200 2657 2431 2453 21 -83 14 C ATOM 1625 C GLU A 200 -1.245 -16.726 -33.125 1.00 20.00 C ANISOU 1625 C GLU A 200 2474 2595 2530 -39 -89 154 C ATOM 1626 O GLU A 200 -0.521 -16.858 -32.033 1.00 17.88 O ANISOU 1626 O GLU A 200 2282 2356 2152 -101 -106 -15 O ATOM 1627 CB GLU A 200 -2.046 -19.058 -33.522 1.00 20.83 C ANISOU 1627 CB GLU A 200 2639 2751 2524 41 17 -47 C ATOM 1628 CG GLU A 200 -3.132 -20.094 -33.155 1.00 21.42 C ANISOU 1628 CG GLU A 200 2635 2772 2729 -154 -80 -199 C ATOM 1629 CD GLU A 200 -3.476 -20.259 -31.734 1.00 22.87 C ANISOU 1629 CD GLU A 200 2791 3037 2860 70 72 65 C ATOM 1630 OE1 GLU A 200 -2.609 -19.992 -30.848 1.00 20.24 O ANISOU 1630 OE1 GLU A 200 2539 2609 2543 -248 -125 2 O ATOM 1631 OE2 GLU A 200 -4.639 -20.717 -31.364 1.00 22.82 O ANISOU 1631 OE2 GLU A 200 2789 2998 2882 -323 0 -244 O ATOM 1632 N ASP A 201 -0.998 -15.860 -34.026 1.00 19.27 N ANISOU 1632 N ASP A 201 2323 2549 2449 -185 -131 -47 N ATOM 1633 CA ASP A 201 0.108 -14.950 -33.856 1.00 18.55 C ANISOU 1633 CA ASP A 201 2336 2321 2388 -52 -55 -76 C ATOM 1634 C ASP A 201 -0.071 -14.131 -32.603 1.00 18.63 C ANISOU 1634 C ASP A 201 2399 2353 2323 18 -15 -32 C ATOM 1635 O ASP A 201 0.944 -13.679 -31.987 1.00 16.54 O ANISOU 1635 O ASP A 201 2029 2103 2150 -95 -98 -52 O ATOM 1636 CB ASP A 201 0.299 -14.017 -34.995 1.00 18.54 C ANISOU 1636 CB ASP A 201 2383 2298 2362 -100 -151 -29 C ATOM 1637 CG ASP A 201 0.891 -14.607 -36.219 1.00 21.13 C ANISOU 1637 CG ASP A 201 2545 2756 2725 -85 -61 -78 C ATOM 1638 OD1 ASP A 201 1.308 -15.818 -36.219 1.00 22.53 O ANISOU 1638 OD1 ASP A 201 2967 2770 2823 -82 -168 -43 O ATOM 1639 OD2 ASP A 201 0.966 -13.847 -37.231 1.00 25.25 O ANISOU 1639 OD2 ASP A 201 3419 3125 3049 -197 -126 -21 O ATOM 1640 N ARG A 202 -1.239 -13.954 -32.157 1.00 16.86 N ANISOU 1640 N ARG A 202 2171 2098 2133 -11 -11 -52 N ATOM 1641 CA ARG A 202 -1.562 -13.131 -30.939 1.00 17.79 C ANISOU 1641 CA ARG A 202 2135 2347 2276 -22 -170 -160 C ATOM 1642 C ARG A 202 -1.531 -13.919 -29.680 1.00 16.89 C ANISOU 1642 C ARG A 202 2010 2173 2234 99 -7 -20 C ATOM 1643 O ARG A 202 -1.640 -13.393 -28.577 1.00 16.16 O ANISOU 1643 O ARG A 202 1994 2059 2085 20 -70 18 O ATOM 1644 CB ARG A 202 -2.968 -12.451 -31.126 1.00 18.26 C ANISOU 1644 CB ARG A 202 2178 2287 2473 -8 -41 -9 C ATOM 1645 CG ARG A 202 -2.921 -11.415 -32.229 1.00 20.26 C ANISOU 1645 CG ARG A 202 2430 2601 2667 -65 -165 -92 C ATOM 1646 CD ARG A 202 -4.348 -11.010 -32.616 1.00 20.81 C ANISOU 1646 CD ARG A 202 2505 2651 2750 32 -165 263 C ATOM 1647 NE ARG A 202 -4.251 -10.052 -33.661 1.00 22.26 N ANISOU 1647 NE ARG A 202 2795 2882 2779 -69 -81 186 N ATOM 1648 CZ ARG A 202 -5.355 -9.488 -34.185 1.00 21.99 C ANISOU 1648 CZ ARG A 202 2647 3001 2706 -96 -46 150 C ATOM 1649 NH1 ARG A 202 -6.523 -9.943 -33.825 1.00 23.19 N ANISOU 1649 NH1 ARG A 202 2841 3130 2840 -209 -84 83 N ATOM 1650 NH2 ARG A 202 -5.213 -8.590 -35.126 1.00 22.37 N ANISOU 1650 NH2 ARG A 202 2647 2884 2968 103 -157 198 N ATOM 1651 N ARG A 203 -1.394 -15.267 -29.742 1.00 16.64 N ANISOU 1651 N ARG A 203 2100 2122 2100 -121 -104 -68 N ATOM 1652 CA ARG A 203 -1.401 -16.105 -28.601 1.00 15.10 C ANISOU 1652 CA ARG A 203 1819 1939 1977 13 19 -62 C ATOM 1653 C ARG A 203 -0.546 -15.694 -27.390 1.00 17.13 C ANISOU 1653 C ARG A 203 2104 2240 2164 -104 -57 43 C ATOM 1654 O ARG A 203 -0.977 -15.829 -26.256 1.00 17.30 O ANISOU 1654 O ARG A 203 2166 2191 2213 -137 -58 -108 O ATOM 1655 CB ARG A 203 -1.156 -17.583 -29.002 1.00 18.40 C ANISOU 1655 CB ARG A 203 2267 2274 2447 -93 -67 -206 C ATOM 1656 CG ARG A 203 -1.198 -18.587 -27.928 1.00 16.95 C ANISOU 1656 CG ARG A 203 2097 2171 2172 56 -32 -103 C ATOM 1657 CD ARG A 203 -2.498 -18.871 -27.216 1.00 16.79 C ANISOU 1657 CD ARG A 203 2157 2040 2181 -62 -102 -101 C ATOM 1658 NE ARG A 203 -3.393 -19.497 -28.211 1.00 19.75 N ANISOU 1658 NE ARG A 203 2414 2638 2449 -65 -75 24 N ATOM 1659 CZ ARG A 203 -4.657 -19.897 -27.833 1.00 22.09 C ANISOU 1659 CZ ARG A 203 2723 2984 2684 -180 62 -37 C ATOM 1660 NH1 ARG A 203 -5.077 -19.722 -26.649 1.00 19.66 N ANISOU 1660 NH1 ARG A 203 2437 2477 2556 -173 -19 -88 N ATOM 1661 NH2 ARG A 203 -5.453 -20.454 -28.734 1.00 23.42 N ANISOU 1661 NH2 ARG A 203 2920 2929 3047 -217 -18 -143 N ATOM 1662 N PRO A 204 0.708 -15.196 -27.611 1.00 16.26 N ANISOU 1662 N PRO A 204 2013 2101 2064 -47 7 -46 N ATOM 1663 CA PRO A 204 1.489 -14.889 -26.374 1.00 17.20 C ANISOU 1663 CA PRO A 204 2222 2203 2110 -43 105 0 C ATOM 1664 C PRO A 204 0.806 -13.896 -25.523 1.00 15.81 C ANISOU 1664 C PRO A 204 2105 1895 2003 -92 -27 74 C ATOM 1665 O PRO A 204 0.982 -13.852 -24.301 1.00 15.45 O ANISOU 1665 O PRO A 204 1987 1856 2025 -113 -70 54 O ATOM 1666 CB PRO A 204 2.848 -14.397 -26.969 1.00 16.79 C ANISOU 1666 CB PRO A 204 1945 2085 2345 -73 -28 -198 C ATOM 1667 CG PRO A 204 2.879 -14.803 -28.322 1.00 19.68 C ANISOU 1667 CG PRO A 204 2365 2589 2524 -71 -68 159 C ATOM 1668 CD PRO A 204 1.466 -15.087 -28.832 1.00 17.50 C ANISOU 1668 CD PRO A 204 2202 2285 2161 -48 -90 -18 C ATOM 1669 N THR A 205 0.012 -12.979 -26.173 1.00 15.78 N ANISOU 1669 N THR A 205 1927 2002 2065 25 -179 -45 N ATOM 1670 CA THR A 205 -0.616 -11.960 -25.416 1.00 15.07 C ANISOU 1670 CA THR A 205 1881 1916 1929 -108 -43 -33 C ATOM 1671 C THR A 205 -1.828 -12.353 -24.570 1.00 17.52 C ANISOU 1671 C THR A 205 2185 2231 2239 9 22 -7 C ATOM 1672 O THR A 205 -2.223 -11.682 -23.667 1.00 17.52 O ANISOU 1672 O THR A 205 2163 2191 2299 -44 22 -26 O ATOM 1673 CB THR A 205 -0.924 -10.663 -26.202 1.00 15.55 C ANISOU 1673 CB THR A 205 1997 1995 1916 55 28 -39 C ATOM 1674 OG1 THR A 205 -2.062 -10.867 -27.077 1.00 17.29 O ANISOU 1674 OG1 THR A 205 2154 2165 2249 63 -97 80 O ATOM 1675 CG2 THR A 205 0.242 -10.206 -27.022 1.00 17.43 C ANISOU 1675 CG2 THR A 205 2157 2244 2221 -48 -44 -10 C ATOM 1676 N LEU A 206 -2.310 -13.603 -24.872 1.00 17.43 N ANISOU 1676 N LEU A 206 2232 2068 2322 -90 90 -169 N ATOM 1677 CA LEU A 206 -3.368 -14.258 -24.075 1.00 17.83 C ANISOU 1677 CA LEU A 206 2261 2262 2251 -54 -7 -55 C ATOM 1678 C LEU A 206 -2.798 -15.270 -23.127 1.00 17.42 C ANISOU 1678 C LEU A 206 2205 2169 2243 -77 -59 -63 C ATOM 1679 O LEU A 206 -3.261 -15.437 -21.998 1.00 17.21 O ANISOU 1679 O LEU A 206 2088 2163 2285 -103 -11 -10 O ATOM 1680 CB LEU A 206 -4.319 -15.008 -25.102 1.00 17.07 C ANISOU 1680 CB LEU A 206 2108 2156 2222 0 1 -14 C ATOM 1681 CG LEU A 206 -5.370 -15.829 -24.383 1.00 19.04 C ANISOU 1681 CG LEU A 206 2367 2408 2457 -170 -149 113 C ATOM 1682 CD1 LEU A 206 -6.252 -14.999 -23.475 1.00 18.62 C ANISOU 1682 CD1 LEU A 206 2176 2396 2501 -212 -201 -54 C ATOM 1683 CD2 LEU A 206 -6.272 -16.468 -25.483 1.00 19.69 C ANISOU 1683 CD2 LEU A 206 2444 2596 2438 -69 100 -51 C ATOM 1684 N SER A 207 -1.753 -16.068 -23.553 1.00 16.70 N ANISOU 1684 N SER A 207 1974 2160 2211 -117 37 23 N ATOM 1685 CA SER A 207 -1.126 -16.956 -22.620 1.00 15.43 C ANISOU 1685 CA SER A 207 2008 1870 1983 -152 220 49 C ATOM 1686 C SER A 207 -0.573 -16.288 -21.368 1.00 15.16 C ANISOU 1686 C SER A 207 1857 1902 1999 114 -92 110 C ATOM 1687 O SER A 207 -0.588 -16.790 -20.263 1.00 17.24 O ANISOU 1687 O SER A 207 2183 2191 2174 70 187 -2 O ATOM 1688 CB SER A 207 -0.123 -17.896 -23.242 1.00 17.36 C ANISOU 1688 CB SER A 207 2105 2216 2272 83 0 -15 C ATOM 1689 OG SER A 207 -0.707 -18.730 -24.264 1.00 18.26 O ANISOU 1689 OG SER A 207 2304 2282 2352 -36 -4 10 O ATOM 1690 N TRP A 208 0.008 -15.093 -21.574 1.00 15.49 N ANISOU 1690 N TRP A 208 1899 1952 2032 -7 19 -49 N ATOM 1691 CA TRP A 208 0.591 -14.392 -20.473 1.00 14.53 C ANISOU 1691 CA TRP A 208 1874 1828 1816 -78 0 183 C ATOM 1692 C TRP A 208 -0.409 -14.071 -19.363 1.00 15.52 C ANISOU 1692 C TRP A 208 2023 1895 1977 131 -89 -30 C ATOM 1693 O TRP A 208 -0.072 -14.363 -18.222 1.00 15.73 O ANISOU 1693 O TRP A 208 2005 1969 2002 -60 39 -4 O ATOM 1694 CB TRP A 208 1.383 -13.123 -20.946 1.00 14.97 C ANISOU 1694 CB TRP A 208 1893 1826 1967 -152 -44 14 C ATOM 1695 CG TRP A 208 2.819 -13.343 -21.322 1.00 12.93 C ANISOU 1695 CG TRP A 208 1675 1562 1672 24 9 -48 C ATOM 1696 CD1 TRP A 208 3.462 -12.841 -22.423 1.00 14.41 C ANISOU 1696 CD1 TRP A 208 1854 1753 1866 80 -92 -20 C ATOM 1697 CD2 TRP A 208 3.801 -14.018 -20.595 1.00 13.69 C ANISOU 1697 CD2 TRP A 208 1735 1700 1765 -58 -41 -64 C ATOM 1698 NE1 TRP A 208 4.780 -13.128 -22.389 1.00 14.90 N ANISOU 1698 NE1 TRP A 208 1908 1877 1875 -73 121 11 N ATOM 1699 CE2 TRP A 208 5.038 -13.932 -21.313 1.00 13.33 C ANISOU 1699 CE2 TRP A 208 1661 1683 1720 -17 27 8 C ATOM 1700 CE3 TRP A 208 3.838 -14.759 -19.410 1.00 15.29 C ANISOU 1700 CE3 TRP A 208 1970 1882 1958 -86 -3 0 C ATOM 1701 CZ2 TRP A 208 6.220 -14.446 -20.816 1.00 12.88 C ANISOU 1701 CZ2 TRP A 208 1706 1490 1695 -55 -8 87 C ATOM 1702 CZ3 TRP A 208 4.999 -15.296 -18.980 1.00 15.14 C ANISOU 1702 CZ3 TRP A 208 1921 1864 1964 -102 75 117 C ATOM 1703 CH2 TRP A 208 6.187 -15.154 -19.676 1.00 14.60 C ANISOU 1703 CH2 TRP A 208 1852 1888 1805 151 -24 -22 C ATOM 1704 N PRO A 209 -1.575 -13.470 -19.662 1.00 16.50 N ANISOU 1704 N PRO A 209 2007 2170 2088 18 103 71 N ATOM 1705 CA PRO A 209 -2.429 -13.139 -18.456 1.00 15.93 C ANISOU 1705 CA PRO A 209 2082 1952 2017 -93 31 -37 C ATOM 1706 C PRO A 209 -2.928 -14.414 -17.773 1.00 16.76 C ANISOU 1706 C PRO A 209 2100 2197 2069 -82 18 -126 C ATOM 1707 O PRO A 209 -3.283 -14.328 -16.582 1.00 18.23 O ANISOU 1707 O PRO A 209 2264 2315 2347 -155 153 66 O ATOM 1708 CB PRO A 209 -3.500 -12.240 -19.128 1.00 16.45 C ANISOU 1708 CB PRO A 209 2061 2027 2162 -91 173 55 C ATOM 1709 CG PRO A 209 -3.473 -12.509 -20.568 1.00 16.77 C ANISOU 1709 CG PRO A 209 2019 2095 2255 68 55 107 C ATOM 1710 CD PRO A 209 -1.978 -12.729 -20.838 1.00 15.79 C ANISOU 1710 CD PRO A 209 1912 1943 2143 -123 -42 -24 C ATOM 1711 N ARG A 210 -2.955 -15.505 -18.490 1.00 16.66 N ANISOU 1711 N ARG A 210 2055 2081 2193 -20 163 60 N ATOM 1712 CA ARG A 210 -3.333 -16.769 -17.922 1.00 17.90 C ANISOU 1712 CA ARG A 210 2251 2301 2248 -74 79 121 C ATOM 1713 C ARG A 210 -2.241 -17.367 -17.033 1.00 20.53 C ANISOU 1713 C ARG A 210 2571 2515 2711 50 -32 -113 C ATOM 1714 O ARG A 210 -2.504 -18.308 -16.368 1.00 21.37 O ANISOU 1714 O ARG A 210 2839 2628 2650 -159 146 202 O ATOM 1715 CB ARG A 210 -3.805 -17.741 -19.002 1.00 20.02 C ANISOU 1715 CB ARG A 210 2538 2540 2527 -85 166 -22 C ATOM 1716 CG ARG A 210 -5.141 -17.345 -19.625 1.00 19.19 C ANISOU 1716 CG ARG A 210 2423 2268 2600 -178 124 -28 C ATOM 1717 CD ARG A 210 -5.447 -18.082 -20.916 1.00 19.16 C ANISOU 1717 CD ARG A 210 2473 2348 2456 -116 -34 47 C ATOM 1718 NE ARG A 210 -6.808 -17.866 -21.376 1.00 21.01 N ANISOU 1718 NE ARG A 210 2616 2648 2719 -136 0 59 N ATOM 1719 CZ ARG A 210 -7.348 -18.440 -22.433 1.00 23.41 C ANISOU 1719 CZ ARG A 210 2960 2924 3011 -46 81 29 C ATOM 1720 NH1 ARG A 210 -6.653 -19.247 -23.179 1.00 21.74 N ANISOU 1720 NH1 ARG A 210 2675 2771 2815 -180 -141 -39 N ATOM 1721 NH2 ARG A 210 -8.586 -18.177 -22.754 1.00 22.31 N ANISOU 1721 NH2 ARG A 210 2538 2941 2998 -43 -34 -30 N ATOM 1722 N GLN A 211 -1.077 -16.771 -17.031 1.00 17.72 N ANISOU 1722 N GLN A 211 2249 2222 2259 7 151 32 N ATOM 1723 CA GLN A 211 -0.031 -17.239 -16.179 1.00 17.15 C ANISOU 1723 CA GLN A 211 2183 2164 2166 -30 291 -51 C ATOM 1724 C GLN A 211 0.115 -16.392 -14.905 1.00 16.56 C ANISOU 1724 C GLN A 211 2062 2036 2190 -287 -43 127 C ATOM 1725 O GLN A 211 0.808 -16.791 -14.035 1.00 18.42 O ANISOU 1725 O GLN A 211 2311 2339 2347 -225 175 234 O ATOM 1726 CB GLN A 211 1.273 -17.285 -16.960 1.00 20.41 C ANISOU 1726 CB GLN A 211 2437 2549 2769 29 188 34 C ATOM 1727 CG GLN A 211 1.263 -18.337 -18.061 1.00 20.93 C ANISOU 1727 CG GLN A 211 2624 2900 2428 196 52 168 C ATOM 1728 CD GLN A 211 1.488 -19.730 -17.527 1.00 19.56 C ANISOU 1728 CD GLN A 211 2401 2477 2553 -137 146 -185 C ATOM 1729 OE1 GLN A 211 2.552 -20.105 -17.268 1.00 20.46 O ANISOU 1729 OE1 GLN A 211 2612 2524 2638 -137 104 146 O ATOM 1730 NE2 GLN A 211 0.414 -20.464 -17.317 1.00 27.37 N ANISOU 1730 NE2 GLN A 211 3250 3336 3813 -563 61 -128 N ATOM 1731 N ILE A 212 -0.585 -15.257 -14.812 1.00 17.31 N ANISOU 1731 N ILE A 212 2080 2339 2156 -1 155 39 N ATOM 1732 CA ILE A 212 -0.358 -14.383 -13.656 1.00 17.51 C ANISOU 1732 CA ILE A 212 2185 2143 2324 -172 63 57 C ATOM 1733 C ILE A 212 -0.720 -15.167 -12.393 1.00 19.29 C ANISOU 1733 C ILE A 212 2420 2459 2447 0 74 -33 C ATOM 1734 O ILE A 212 -1.794 -15.772 -12.362 1.00 19.63 O ANISOU 1734 O ILE A 212 2453 2498 2506 -138 -12 -42 O ATOM 1735 CB ILE A 212 -1.224 -13.136 -13.764 1.00 19.05 C ANISOU 1735 CB ILE A 212 2441 2437 2360 -123 44 17 C ATOM 1736 CG1 ILE A 212 -0.856 -12.292 -15.009 1.00 18.21 C ANISOU 1736 CG1 ILE A 212 2320 2290 2307 -72 51 -16 C ATOM 1737 CG2 ILE A 212 -0.955 -12.200 -12.603 1.00 19.94 C ANISOU 1737 CG2 ILE A 212 2629 2453 2491 -133 406 15 C ATOM 1738 CD1 ILE A 212 -1.975 -11.342 -15.353 1.00 20.75 C ANISOU 1738 CD1 ILE A 212 2693 2625 2562 100 132 -88 C ATOM 1739 N PRO A 213 0.067 -15.101 -11.366 1.00 18.07 N ANISOU 1739 N PRO A 213 2284 2421 2161 -37 75 122 N ATOM 1740 CA PRO A 213 -0.218 -15.929 -10.094 1.00 20.06 C ANISOU 1740 CA PRO A 213 2678 2407 2535 -100 84 254 C ATOM 1741 C PRO A 213 -1.281 -15.209 -9.291 1.00 21.02 C ANISOU 1741 C PRO A 213 2626 2658 2700 -44 253 -19 C ATOM 1742 O PRO A 213 -0.958 -14.183 -8.645 1.00 21.40 O ANISOU 1742 O PRO A 213 2672 2807 2651 -159 301 -67 O ATOM 1743 CB PRO A 213 1.113 -15.993 -9.408 1.00 21.42 C ANISOU 1743 CB PRO A 213 2723 2753 2662 -51 120 317 C ATOM 1744 CG PRO A 213 1.893 -14.714 -9.863 1.00 19.62 C ANISOU 1744 CG PRO A 213 2515 2304 2636 -206 -28 -36 C ATOM 1745 CD PRO A 213 1.470 -14.585 -11.285 1.00 19.73 C ANISOU 1745 CD PRO A 213 2429 2474 2590 -214 72 -97 C ATOM 1746 N ILE A 214 -2.575 -15.576 -9.483 1.00 20.82 N ANISOU 1746 N ILE A 214 2743 2605 2561 63 44 -32 N ATOM 1747 CA ILE A 214 -3.639 -14.854 -8.780 1.00 24.17 C ANISOU 1747 CA ILE A 214 3019 3132 3031 -111 242 84 C ATOM 1748 C ILE A 214 -4.497 -15.922 -8.118 1.00 26.73 C ANISOU 1748 C ILE A 214 3318 3518 3317 -494 387 -119 C ATOM 1749 O ILE A 214 -4.950 -16.846 -8.742 1.00 26.37 O ANISOU 1749 O ILE A 214 3281 3464 3270 -215 498 -228 O ATOM 1750 CB ILE A 214 -4.531 -14.108 -9.731 1.00 28.57 C ANISOU 1750 CB ILE A 214 3541 3378 3933 175 309 275 C ATOM 1751 CG1 ILE A 214 -3.765 -13.141 -10.688 1.00 26.39 C ANISOU 1751 CG1 ILE A 214 3287 3397 3341 73 270 75 C ATOM 1752 CG2 ILE A 214 -5.547 -13.285 -8.921 1.00 32.36 C ANISOU 1752 CG2 ILE A 214 4448 4081 3765 380 540 101 C ATOM 1753 CD1 ILE A 214 -4.628 -12.490 -11.649 1.00 27.61 C ANISOU 1753 CD1 ILE A 214 3440 3543 3505 -37 488 -181 C ATOM 1754 N ASP A 215 -4.753 -15.712 -6.846 1.00 27.78 N ANISOU 1754 N ASP A 215 3621 3461 3473 -609 335 -120 N ATOM 1755 CA ASP A 215 -5.569 -16.619 -6.074 1.00 28.81 C ANISOU 1755 CA ASP A 215 3843 3761 3340 -274 114 361 C ATOM 1756 C ASP A 215 -5.068 -18.034 -6.111 1.00 30.31 C ANISOU 1756 C ASP A 215 3956 4018 3539 -54 89 -469 C ATOM 1757 O ASP A 215 -5.830 -18.917 -6.140 1.00 29.98 O ANISOU 1757 O ASP A 215 3673 3999 3719 -734 557 123 O ATOM 1758 CB ASP A 215 -7.005 -16.596 -6.547 1.00 36.18 C ANISOU 1758 CB ASP A 215 4706 4859 4180 -742 98 228 C ATOM 1759 CG ASP A 215 -7.794 -15.444 -6.015 1.00 50.85 C ANISOU 1759 CG ASP A 215 6580 6515 6224 530 127 45 C ATOM 1760 OD1 ASP A 215 -7.254 -14.488 -5.429 1.00 46.74 O ANISOU 1760 OD1 ASP A 215 5377 6000 6381 -938 33 -228 O ATOM 1761 OD2 ASP A 215 -9.005 -15.495 -6.178 1.00 51.25 O ANISOU 1761 OD2 ASP A 215 5754 7682 6036 -1261 -117 72 O ATOM 1762 N GLY A 216 -3.766 -18.224 -6.125 1.00 25.96 N ANISOU 1762 N GLY A 216 3340 3463 3060 -191 253 166 N ATOM 1763 CA GLY A 216 -3.178 -19.484 -6.100 1.00 27.61 C ANISOU 1763 CA GLY A 216 3630 3494 3364 -298 298 52 C ATOM 1764 C GLY A 216 -3.065 -20.278 -7.431 1.00 25.67 C ANISOU 1764 C GLY A 216 3053 3416 3285 -81 207 -51 C ATOM 1765 O GLY A 216 -2.529 -21.378 -7.486 1.00 28.48 O ANISOU 1765 O GLY A 216 3730 3431 3659 -380 424 509 O ATOM 1766 N GLU A 217 -3.434 -19.640 -8.518 1.00 24.40 N ANISOU 1766 N GLU A 217 3096 2987 3187 -336 64 118 N ATOM 1767 CA GLU A 217 -3.370 -20.266 -9.815 1.00 25.58 C ANISOU 1767 CA GLU A 217 3379 3204 3137 -237 289 342 C ATOM 1768 C GLU A 217 -2.760 -19.361 -10.878 1.00 22.40 C ANISOU 1768 C GLU A 217 2798 2863 2848 22 232 326 C ATOM 1769 O GLU A 217 -3.001 -18.219 -10.877 1.00 24.65 O ANISOU 1769 O GLU A 217 3256 3081 3029 -72 277 8 O ATOM 1770 CB GLU A 217 -4.756 -20.721 -10.264 1.00 29.95 C ANISOU 1770 CB GLU A 217 3663 3949 3768 -295 -29 37 C ATOM 1771 CG GLU A 217 -5.362 -21.845 -9.428 1.00 38.24 C ANISOU 1771 CG GLU A 217 4745 4827 4957 -895 519 298 C ATOM 1772 CD GLU A 217 -4.602 -23.177 -9.464 1.00 52.34 C ANISOU 1772 CD GLU A 217 6525 6136 7223 21 -47 -155 C ATOM 1773 OE1 GLU A 217 -3.903 -23.535 -10.432 1.00 43.33 O ANISOU 1773 OE1 GLU A 217 5951 4804 5706 -1179 305 278 O ATOM 1774 OE2 GLU A 217 -4.710 -23.889 -8.459 1.00 74.61 O ANISOU 1774 OE2 GLU A 217 10218 9663 8467 -2533 2058 1777 O ATOM 1775 N PRO A 218 -1.962 -19.926 -11.776 1.00 22.05 N ANISOU 1775 N PRO A 218 2993 2675 2709 -14 51 49 N ATOM 1776 CA PRO A 218 -1.525 -21.333 -11.848 1.00 24.50 C ANISOU 1776 CA PRO A 218 3246 2901 3160 -11 364 37 C ATOM 1777 C PRO A 218 -0.532 -21.631 -10.802 1.00 23.37 C ANISOU 1777 C PRO A 218 3006 2907 2964 64 -275 171 C ATOM 1778 O PRO A 218 0.371 -20.896 -10.462 1.00 22.57 O ANISOU 1778 O PRO A 218 2973 2738 2864 -184 163 201 O ATOM 1779 CB PRO A 218 -0.912 -21.548 -13.197 1.00 25.25 C ANISOU 1779 CB PRO A 218 3482 2912 3200 19 -41 271 C ATOM 1780 CG PRO A 218 -0.560 -20.096 -13.641 1.00 24.37 C ANISOU 1780 CG PRO A 218 3235 2873 3149 -305 441 156 C ATOM 1781 CD PRO A 218 -1.494 -19.176 -12.963 1.00 21.73 C ANISOU 1781 CD PRO A 218 2864 2596 2797 -92 25 136 C ATOM 1782 N ALA A 219 -0.673 -22.815 -10.210 1.00 24.41 N ANISOU 1782 N ALA A 219 3169 2784 3321 -507 85 238 N ATOM 1783 CA ALA A 219 0.175 -23.200 -9.110 1.00 23.51 C ANISOU 1783 CA ALA A 219 3219 2544 3170 -335 46 353 C ATOM 1784 C ALA A 219 1.674 -23.224 -9.358 1.00 21.68 C ANISOU 1784 C ALA A 219 3102 2323 2812 -252 -68 441 C ATOM 1785 O ALA A 219 2.408 -22.907 -8.515 1.00 25.48 O ANISOU 1785 O ALA A 219 3560 3027 3091 -403 -138 437 O ATOM 1786 CB ALA A 219 -0.279 -24.548 -8.536 1.00 28.22 C ANISOU 1786 CB ALA A 219 4040 3224 3458 -637 -120 379 C ATOM 1787 N ASP A 220 2.102 -23.615 -10.532 1.00 23.85 N ANISOU 1787 N ASP A 220 3158 2677 3226 -76 179 134 N ATOM 1788 CA ASP A 220 3.457 -23.714 -10.835 1.00 24.36 C ANISOU 1788 CA ASP A 220 3196 2830 3228 -8 -251 290 C ATOM 1789 C ASP A 220 4.093 -22.256 -10.757 1.00 23.05 C ANISOU 1789 C ASP A 220 2930 2844 2985 -157 -1 180 C ATOM 1790 O ASP A 220 5.166 -22.084 -10.154 1.00 23.22 O ANISOU 1790 O ASP A 220 3138 2820 2864 -210 7 230 O ATOM 1791 CB ASP A 220 3.741 -24.427 -12.121 1.00 30.66 C ANISOU 1791 CB ASP A 220 4255 3491 3903 -12 22 292 C ATOM 1792 CG ASP A 220 3.347 -23.666 -13.406 1.00 32.97 C ANISOU 1792 CG ASP A 220 4237 4158 4130 174 -144 495 C ATOM 1793 OD1 ASP A 220 2.191 -23.159 -13.446 1.00 31.12 O ANISOU 1793 OD1 ASP A 220 3981 3914 3927 -151 183 74 O ATOM 1794 OD2 ASP A 220 4.257 -23.550 -14.307 1.00 35.25 O ANISOU 1794 OD2 ASP A 220 4725 4139 4530 525 -68 -9 O ATOM 1795 N VAL A 221 3.402 -21.328 -11.360 1.00 22.42 N ANISOU 1795 N VAL A 221 2841 2845 2830 -76 -55 -87 N ATOM 1796 CA VAL A 221 3.924 -19.922 -11.356 1.00 20.86 C ANISOU 1796 CA VAL A 221 2612 2669 2644 -75 140 38 C ATOM 1797 C VAL A 221 3.866 -19.319 -9.968 1.00 19.77 C ANISOU 1797 C VAL A 221 2378 2643 2487 56 43 -19 C ATOM 1798 O VAL A 221 4.785 -18.662 -9.503 1.00 19.38 O ANISOU 1798 O VAL A 221 2596 2432 2335 -162 -14 163 O ATOM 1799 CB VAL A 221 3.257 -19.066 -12.373 1.00 20.31 C ANISOU 1799 CB VAL A 221 2616 2496 2605 -53 113 59 C ATOM 1800 CG1 VAL A 221 3.806 -17.668 -12.376 1.00 21.15 C ANISOU 1800 CG1 VAL A 221 2583 2614 2837 72 -50 106 C ATOM 1801 CG2 VAL A 221 3.382 -19.665 -13.789 1.00 21.89 C ANISOU 1801 CG2 VAL A 221 2797 2685 2835 -93 -4 73 C ATOM 1802 N VAL A 222 2.803 -19.594 -9.203 1.00 20.04 N ANISOU 1802 N VAL A 222 2664 2343 2606 -213 92 139 N ATOM 1803 CA VAL A 222 2.763 -19.148 -7.831 1.00 21.88 C ANISOU 1803 CA VAL A 222 2704 2716 2892 -56 104 27 C ATOM 1804 C VAL A 222 3.979 -19.587 -7.059 1.00 20.34 C ANISOU 1804 C VAL A 222 2814 2564 2348 -218 70 219 C ATOM 1805 O VAL A 222 4.570 -18.869 -6.287 1.00 20.78 O ANISOU 1805 O VAL A 222 2833 2527 2534 -243 94 272 O ATOM 1806 CB VAL A 222 1.413 -19.627 -7.211 1.00 21.97 C ANISOU 1806 CB VAL A 222 2865 2652 2831 -316 206 -17 C ATOM 1807 CG1 VAL A 222 1.365 -19.386 -5.637 1.00 25.64 C ANISOU 1807 CG1 VAL A 222 3513 3061 3167 -518 287 414 C ATOM 1808 CG2 VAL A 222 0.241 -19.032 -7.826 1.00 22.89 C ANISOU 1808 CG2 VAL A 222 3009 2908 2779 -287 408 202 C ATOM 1809 N ALA A 223 4.348 -20.865 -7.237 1.00 22.05 N ANISOU 1809 N ALA A 223 2886 2775 2716 31 39 158 N ATOM 1810 CA ALA A 223 5.471 -21.378 -6.507 1.00 22.00 C ANISOU 1810 CA ALA A 223 2683 2732 2943 -104 58 257 C ATOM 1811 C ALA A 223 6.792 -20.717 -6.876 1.00 20.30 C ANISOU 1811 C ALA A 223 2649 2484 2578 -167 -73 63 C ATOM 1812 O ALA A 223 7.576 -20.465 -6.027 1.00 20.40 O ANISOU 1812 O ALA A 223 2732 2436 2582 -71 -86 191 O ATOM 1813 CB ALA A 223 5.541 -22.909 -6.722 1.00 25.68 C ANISOU 1813 CB ALA A 223 3607 3049 3101 67 -107 88 C ATOM 1814 N ILE A 224 6.982 -20.519 -8.235 1.00 20.25 N ANISOU 1814 N ILE A 224 2643 2493 2558 -127 -46 154 N ATOM 1815 CA ILE A 224 8.176 -19.871 -8.743 1.00 19.31 C ANISOU 1815 CA ILE A 224 2455 2367 2513 122 120 -90 C ATOM 1816 C ILE A 224 8.313 -18.432 -8.082 1.00 16.68 C ANISOU 1816 C ILE A 224 2172 2107 2058 -132 63 85 C ATOM 1817 O ILE A 224 9.362 -18.054 -7.621 1.00 18.38 O ANISOU 1817 O ILE A 224 2421 2306 2255 30 -73 186 O ATOM 1818 CB ILE A 224 8.127 -19.757 -10.215 1.00 19.00 C ANISOU 1818 CB ILE A 224 2390 2393 2433 31 6 -29 C ATOM 1819 CG1 ILE A 224 8.381 -21.145 -10.784 1.00 20.87 C ANISOU 1819 CG1 ILE A 224 2771 2614 2542 -66 160 161 C ATOM 1820 CG2 ILE A 224 9.237 -18.806 -10.788 1.00 21.25 C ANISOU 1820 CG2 ILE A 224 2836 2594 2643 -41 40 105 C ATOM 1821 CD1 ILE A 224 7.877 -21.298 -12.268 1.00 25.71 C ANISOU 1821 CD1 ILE A 224 3518 3266 2983 32 -219 -115 C ATOM 1822 N VAL A 225 7.209 -17.721 -8.101 1.00 17.20 N ANISOU 1822 N VAL A 225 2244 2175 2114 -23 -31 70 N ATOM 1823 CA VAL A 225 7.153 -16.348 -7.607 1.00 18.44 C ANISOU 1823 CA VAL A 225 2518 2322 2166 -85 118 -13 C ATOM 1824 C VAL A 225 7.367 -16.308 -6.064 1.00 19.39 C ANISOU 1824 C VAL A 225 2545 2495 2328 -185 -20 47 C ATOM 1825 O VAL A 225 8.102 -15.533 -5.576 1.00 20.86 O ANISOU 1825 O VAL A 225 2758 2708 2457 -114 -17 126 O ATOM 1826 CB VAL A 225 5.891 -15.623 -8.027 1.00 18.58 C ANISOU 1826 CB VAL A 225 2405 2286 2367 -84 102 53 C ATOM 1827 CG1 VAL A 225 5.761 -14.316 -7.414 1.00 20.39 C ANISOU 1827 CG1 VAL A 225 2634 2602 2508 -207 190 -3 C ATOM 1828 CG2 VAL A 225 5.868 -15.449 -9.578 1.00 19.99 C ANISOU 1828 CG2 VAL A 225 2580 2386 2628 -63 -105 82 C ATOM 1829 N SER A 226 6.668 -17.205 -5.354 1.00 19.36 N ANISOU 1829 N SER A 226 2594 2336 2425 -231 -70 22 N ATOM 1830 CA ASER A 226 6.905 -17.300 -3.925 0.50 19.73 C ANISOU 1830 CA ASER A 226 2740 2331 2422 -187 251 144 C ATOM 1831 CA BSER A 226 6.872 -17.254 -3.940 0.50 20.43 C ANISOU 1831 CA BSER A 226 2846 2425 2488 -174 245 153 C ATOM 1832 C SER A 226 8.322 -17.541 -3.581 1.00 19.43 C ANISOU 1832 C SER A 226 2716 2403 2261 -66 97 451 C ATOM 1833 O SER A 226 8.873 -17.043 -2.601 1.00 21.50 O ANISOU 1833 O SER A 226 2993 2446 2726 -261 13 117 O ATOM 1834 CB ASER A 226 6.038 -18.395 -3.313 0.50 20.41 C ANISOU 1834 CB ASER A 226 2655 2672 2426 -253 182 442 C ATOM 1835 CB BSER A 226 5.862 -18.218 -3.320 0.50 21.93 C ANISOU 1835 CB BSER A 226 2605 2858 2869 -166 270 445 C ATOM 1836 OG ASER A 226 4.730 -17.981 -3.305 0.50 24.93 O ANISOU 1836 OG ASER A 226 3051 3325 3095 333 381 865 O ATOM 1837 OG BSER A 226 6.225 -18.488 -2.022 0.50 31.28 O ANISOU 1837 OG BSER A 226 3947 4204 3733 157 -198 -327 O ATOM 1838 N ASP A 227 8.970 -18.391 -4.354 1.00 18.70 N ANISOU 1838 N ASP A 227 2571 2287 2247 -17 35 335 N ATOM 1839 CA ASP A 227 10.366 -18.745 -4.136 1.00 19.98 C ANISOU 1839 CA ASP A 227 2632 2488 2469 -142 20 104 C ATOM 1840 C ASP A 227 11.276 -17.538 -4.284 1.00 20.76 C ANISOU 1840 C ASP A 227 2619 2641 2626 -258 -138 366 C ATOM 1841 O ASP A 227 12.058 -17.246 -3.448 1.00 20.84 O ANISOU 1841 O ASP A 227 2907 2445 2563 -15 -82 204 O ATOM 1842 CB ASP A 227 10.721 -19.883 -5.090 1.00 20.57 C ANISOU 1842 CB ASP A 227 2721 2534 2559 -170 -26 107 C ATOM 1843 CG ASP A 227 12.116 -20.400 -4.958 1.00 25.45 C ANISOU 1843 CG ASP A 227 3265 3015 3388 -96 -10 138 C ATOM 1844 OD1 ASP A 227 12.891 -19.958 -4.159 1.00 32.47 O ANISOU 1844 OD1 ASP A 227 4537 4087 3714 81 -162 205 O ATOM 1845 OD2 ASP A 227 12.436 -21.275 -5.732 1.00 31.52 O ANISOU 1845 OD2 ASP A 227 4248 3927 3798 236 50 -180 O ATOM 1846 N TYR A 228 11.140 -16.824 -5.384 1.00 18.43 N ANISOU 1846 N TYR A 228 2420 2367 2215 -115 -128 233 N ATOM 1847 CA TYR A 228 11.986 -15.665 -5.543 1.00 18.49 C ANISOU 1847 CA TYR A 228 2571 2337 2115 -48 -149 173 C ATOM 1848 C TYR A 228 11.628 -14.529 -4.601 1.00 17.18 C ANISOU 1848 C TYR A 228 2200 2269 2058 -59 -87 277 C ATOM 1849 O TYR A 228 12.471 -13.851 -4.192 1.00 18.39 O ANISOU 1849 O TYR A 228 2500 2308 2179 -129 -135 76 O ATOM 1850 CB TYR A 228 12.195 -15.223 -7.014 1.00 17.56 C ANISOU 1850 CB TYR A 228 2484 2134 2051 54 38 27 C ATOM 1851 CG TYR A 228 11.057 -14.581 -7.798 1.00 16.48 C ANISOU 1851 CG TYR A 228 2130 2024 2107 55 34 -18 C ATOM 1852 CD1 TYR A 228 10.488 -13.391 -7.410 1.00 17.13 C ANISOU 1852 CD1 TYR A 228 2231 2131 2145 2 57 14 C ATOM 1853 CD2 TYR A 228 10.624 -15.133 -8.961 1.00 18.26 C ANISOU 1853 CD2 TYR A 228 2284 2298 2354 -105 34 161 C ATOM 1854 CE1 TYR A 228 9.510 -12.785 -8.156 1.00 16.50 C ANISOU 1854 CE1 TYR A 228 2139 2069 2059 49 -123 -33 C ATOM 1855 CE2 TYR A 228 9.640 -14.541 -9.712 1.00 17.86 C ANISOU 1855 CE2 TYR A 228 2397 2227 2162 46 54 25 C ATOM 1856 CZ TYR A 228 9.089 -13.351 -9.307 1.00 15.61 C ANISOU 1856 CZ TYR A 228 2087 1930 1913 19 8 20 C ATOM 1857 OH TYR A 228 8.143 -12.759 -10.068 1.00 15.27 O ANISOU 1857 OH TYR A 228 1937 1855 2010 -72 68 81 O ATOM 1858 N ALA A 229 10.366 -14.412 -4.258 1.00 18.15 N ANISOU 1858 N ALA A 229 2496 2229 2170 111 40 43 N ATOM 1859 CA ALA A 229 9.903 -13.305 -3.327 1.00 19.16 C ANISOU 1859 CA ALA A 229 2662 2320 2298 7 52 80 C ATOM 1860 C ALA A 229 10.567 -13.504 -1.960 1.00 19.83 C ANISOU 1860 C ALA A 229 2645 2382 2507 -148 -64 77 C ATOM 1861 O ALA A 229 11.095 -12.604 -1.372 1.00 21.15 O ANISOU 1861 O ALA A 229 2890 2699 2446 33 15 81 O ATOM 1862 CB ALA A 229 8.454 -13.285 -3.260 1.00 19.73 C ANISOU 1862 CB ALA A 229 2775 2393 2328 7 6 149 C ATOM 1863 N ASER A 230 10.610 -14.781 -1.540 0.50 20.71 N ANISOU 1863 N ASER A 230 3064 2473 2332 178 -319 402 N ATOM 1864 N BSER A 230 10.634 -14.770 -1.524 0.50 21.05 N ANISOU 1864 N BSER A 230 3123 2499 2377 189 -351 428 N ATOM 1865 CA ASER A 230 11.202 -15.074 -0.199 0.50 22.05 C ANISOU 1865 CA ASER A 230 3144 2674 2559 -221 -348 -152 C ATOM 1866 CA BSER A 230 11.184 -14.972 -0.142 0.50 21.40 C ANISOU 1866 CA BSER A 230 3095 2575 2461 -192 -330 -189 C ATOM 1867 C ASER A 230 12.654 -14.846 -0.190 0.50 18.41 C ANISOU 1867 C ASER A 230 2562 2043 2390 221 142 121 C ATOM 1868 C BSER A 230 12.680 -14.908 -0.161 0.50 18.74 C ANISOU 1868 C BSER A 230 2617 2035 2465 190 204 89 C ATOM 1869 O ASER A 230 13.231 -14.289 0.772 0.50 22.32 O ANISOU 1869 O ASER A 230 3039 2803 2635 -15 -97 159 O ATOM 1870 O BSER A 230 13.329 -14.555 0.824 0.50 23.46 O ANISOU 1870 O BSER A 230 3125 3048 2739 110 -159 129 O ATOM 1871 CB ASER A 230 10.888 -16.597 0.044 0.50 21.37 C ANISOU 1871 CB ASER A 230 2998 2597 2525 116 228 318 C ATOM 1872 CB BSER A 230 10.674 -16.371 0.358 0.50 23.59 C ANISOU 1872 CB BSER A 230 3019 2910 3031 -318 297 544 C ATOM 1873 OG ASER A 230 9.558 -16.718 0.401 0.50 26.59 O ANISOU 1873 OG ASER A 230 3226 3535 3338 -238 -354 632 O ATOM 1874 OG BSER A 230 11.254 -17.458 -0.330 0.50 26.26 O ANISOU 1874 OG BSER A 230 3867 3071 3037 -246 -146 114 O ATOM 1875 N TRP A 231 13.285 -15.097 -1.323 1.00 17.95 N ANISOU 1875 N TRP A 231 2465 2221 2132 77 -124 65 N ATOM 1876 CA TRP A 231 14.716 -14.923 -1.448 1.00 18.46 C ANISOU 1876 CA TRP A 231 2527 2252 2233 36 65 154 C ATOM 1877 C TRP A 231 15.016 -13.401 -1.489 1.00 19.25 C ANISOU 1877 C TRP A 231 2364 2367 2581 -152 -51 125 C ATOM 1878 O TRP A 231 15.847 -12.934 -0.790 1.00 19.56 O ANISOU 1878 O TRP A 231 2668 2434 2329 134 -117 182 O ATOM 1879 CB TRP A 231 15.281 -15.567 -2.736 1.00 19.94 C ANISOU 1879 CB TRP A 231 2832 2195 2550 302 1 133 C ATOM 1880 CG TRP A 231 16.634 -15.063 -3.106 1.00 19.71 C ANISOU 1880 CG TRP A 231 2667 2341 2478 122 -39 5 C ATOM 1881 CD1 TRP A 231 17.731 -15.113 -2.366 1.00 20.76 C ANISOU 1881 CD1 TRP A 231 2635 2533 2718 110 -57 -17 C ATOM 1882 CD2 TRP A 231 17.000 -14.365 -4.301 1.00 20.52 C ANISOU 1882 CD2 TRP A 231 2723 2487 2584 180 113 40 C ATOM 1883 NE1 TRP A 231 18.774 -14.512 -2.995 1.00 22.40 N ANISOU 1883 NE1 TRP A 231 3020 2714 2773 196 -13 -17 N ATOM 1884 CE2 TRP A 231 18.345 -14.051 -4.199 1.00 20.39 C ANISOU 1884 CE2 TRP A 231 2816 2474 2456 72 63 -177 C ATOM 1885 CE3 TRP A 231 16.321 -14.005 -5.452 1.00 22.10 C ANISOU 1885 CE3 TRP A 231 2893 2661 2843 106 74 -355 C ATOM 1886 CZ2 TRP A 231 19.016 -13.391 -5.195 1.00 22.52 C ANISOU 1886 CZ2 TRP A 231 2982 2627 2948 64 -60 -35 C ATOM 1887 CZ3 TRP A 231 16.993 -13.357 -6.424 1.00 20.15 C ANISOU 1887 CZ3 TRP A 231 2795 2514 2346 30 44 11 C ATOM 1888 CH2 TRP A 231 18.310 -13.064 -6.300 1.00 21.42 C ANISOU 1888 CH2 TRP A 231 2796 2708 2634 19 81 -1 C ATOM 1889 N LEU A 232 14.300 -12.663 -2.333 1.00 18.73 N ANISOU 1889 N LEU A 232 2546 2320 2249 -59 11 -35 N ATOM 1890 CA LEU A 232 14.587 -11.225 -2.493 1.00 18.66 C ANISOU 1890 CA LEU A 232 2448 2366 2276 -184 68 -76 C ATOM 1891 C LEU A 232 14.390 -10.481 -1.088 1.00 19.26 C ANISOU 1891 C LEU A 232 2447 2493 2377 -147 -26 -47 C ATOM 1892 O LEU A 232 15.132 -9.497 -0.830 1.00 19.60 O ANISOU 1892 O LEU A 232 2755 2451 2241 -31 10 114 O ATOM 1893 CB LEU A 232 13.709 -10.662 -3.515 1.00 18.78 C ANISOU 1893 CB LEU A 232 2610 2152 2371 -16 162 14 C ATOM 1894 CG LEU A 232 14.180 -11.023 -4.961 1.00 19.28 C ANISOU 1894 CG LEU A 232 2481 2379 2465 161 8 -73 C ATOM 1895 CD1 LEU A 232 12.999 -10.906 -5.896 1.00 19.50 C ANISOU 1895 CD1 LEU A 232 2661 2325 2422 -149 -14 33 C ATOM 1896 CD2 LEU A 232 15.337 -10.214 -5.429 1.00 21.86 C ANISOU 1896 CD2 LEU A 232 3003 2679 2622 -233 1 18 C ATOM 1897 N ALA A 233 13.370 -10.909 -0.325 1.00 19.18 N ANISOU 1897 N ALA A 233 2706 2267 2313 42 13 -111 N ATOM 1898 CA ALA A 233 13.093 -10.219 0.963 1.00 19.74 C ANISOU 1898 CA ALA A 233 2758 2384 2355 73 15 46 C ATOM 1899 C ALA A 233 14.266 -10.352 1.940 1.00 22.62 C ANISOU 1899 C ALA A 233 2893 2647 3053 -246 21 -10 C ATOM 1900 O ALA A 233 14.272 -9.514 2.905 1.00 23.13 O ANISOU 1900 O ALA A 233 3173 2988 2627 -102 97 -45 O ATOM 1901 CB ALA A 233 11.864 -10.766 1.523 1.00 21.71 C ANISOU 1901 CB ALA A 233 2829 2930 2488 57 125 -203 C ATOM 1902 N GLU A 234 15.159 -11.292 1.729 1.00 21.92 N ANISOU 1902 N GLU A 234 2913 2844 2570 -36 -139 107 N ATOM 1903 CA GLU A 234 16.341 -11.465 2.596 1.00 23.55 C ANISOU 1903 CA GLU A 234 2972 2917 3057 129 -201 123 C ATOM 1904 C GLU A 234 17.613 -11.262 1.992 1.00 28.02 C ANISOU 1904 C GLU A 234 3495 3719 3432 -72 77 140 C ATOM 1905 O GLU A 234 18.643 -11.369 2.614 1.00 30.70 O ANISOU 1905 O GLU A 234 3962 4040 3663 -109 -517 370 O ATOM 1906 CB GLU A 234 16.286 -12.902 3.275 1.00 27.88 C ANISOU 1906 CB GLU A 234 3743 3526 3321 255 -510 728 C ATOM 1907 CG GLU A 234 15.025 -13.152 3.980 1.00 41.23 C ANISOU 1907 CG GLU A 234 4553 5453 5657 -243 74 1085 C ATOM 1908 CD GLU A 234 14.797 -12.441 5.268 1.00 62.13 C ANISOU 1908 CD GLU A 234 8073 8356 7178 -158 -179 -1856 C ATOM 1909 OE1 GLU A 234 15.752 -12.331 6.098 1.00 81.21 O ANISOU 1909 OE1 GLU A 234 8359 12185 10312 2533 -693 173 O ATOM 1910 OE2 GLU A 234 13.600 -12.080 5.526 1.00 77.96 O ANISOU 1910 OE2 GLU A 234 9412 10473 9735 1241 -427 -113 O ATOM 1911 N SER A 235 17.649 -11.043 0.661 1.00 21.33 N ANISOU 1911 N SER A 235 2880 2680 2542 -84 -134 269 N ATOM 1912 CA SER A 235 18.861 -10.976 -0.049 1.00 20.75 C ANISOU 1912 CA SER A 235 2592 2550 2741 296 -147 222 C ATOM 1913 C SER A 235 19.601 -9.622 0.008 1.00 20.84 C ANISOU 1913 C SER A 235 2680 2722 2516 103 49 -108 C ATOM 1914 O SER A 235 18.966 -8.572 -0.175 1.00 21.61 O ANISOU 1914 O SER A 235 2990 2690 2529 92 -271 -17 O ATOM 1915 CB SER A 235 18.623 -11.195 -1.544 1.00 22.38 C ANISOU 1915 CB SER A 235 2864 2690 2947 -157 181 -265 C ATOM 1916 OG SER A 235 19.815 -11.007 -2.326 1.00 24.98 O ANISOU 1916 OG SER A 235 3176 3048 3266 -265 171 -128 O ATOM 1917 N ASP A 236 20.904 -9.684 0.071 1.00 23.27 N ANISOU 1917 N ASP A 236 3052 2940 2849 -219 -247 373 N ATOM 1918 CA ASP A 236 21.678 -8.477 0.069 1.00 21.94 C ANISOU 1918 CA ASP A 236 2857 2671 2806 -137 -138 199 C ATOM 1919 C ASP A 236 22.105 -8.013 -1.317 1.00 19.53 C ANISOU 1919 C ASP A 236 2431 2625 2362 20 -176 -46 C ATOM 1920 O ASP A 236 22.888 -7.137 -1.431 1.00 21.94 O ANISOU 1920 O ASP A 236 2925 2739 2671 -99 -165 167 O ATOM 1921 CB ASP A 236 22.841 -8.539 1.031 1.00 28.23 C ANISOU 1921 CB ASP A 236 3510 3931 3284 173 -429 282 C ATOM 1922 CG ASP A 236 22.392 -8.355 2.486 1.00 45.67 C ANISOU 1922 CG ASP A 236 5595 6480 5275 127 24 -406 C ATOM 1923 OD1 ASP A 236 21.592 -7.467 2.789 1.00 49.03 O ANISOU 1923 OD1 ASP A 236 6213 6819 5595 567 -924 -1096 O ATOM 1924 OD2 ASP A 236 22.837 -9.129 3.327 1.00 58.97 O ANISOU 1924 OD2 ASP A 236 7584 7188 7633 215 -350 505 O ATOM 1925 N ILE A 237 21.580 -8.637 -2.357 1.00 19.32 N ANISOU 1925 N ILE A 237 2655 2214 2470 7 -182 47 N ATOM 1926 CA ILE A 237 21.878 -8.146 -3.627 1.00 18.42 C ANISOU 1926 CA ILE A 237 2333 2281 2384 26 -24 -54 C ATOM 1927 C ILE A 237 21.408 -6.673 -3.832 1.00 17.71 C ANISOU 1927 C ILE A 237 2258 2191 2279 -9 43 -43 C ATOM 1928 O ILE A 237 20.292 -6.380 -3.421 1.00 18.73 O ANISOU 1928 O ILE A 237 2416 2272 2426 -20 -29 30 O ATOM 1929 CB ILE A 237 21.149 -9.068 -4.709 1.00 22.14 C ANISOU 1929 CB ILE A 237 2796 2733 2881 13 -182 -129 C ATOM 1930 CG1 ILE A 237 21.554 -8.696 -6.062 1.00 24.57 C ANISOU 1930 CG1 ILE A 237 3158 3056 3120 -100 64 -13 C ATOM 1931 CG2 ILE A 237 19.570 -9.006 -4.572 1.00 27.67 C ANISOU 1931 CG2 ILE A 237 3574 3470 3467 182 98 49 C ATOM 1932 CD1 ILE A 237 21.395 -10.013 -6.878 1.00 38.27 C ANISOU 1932 CD1 ILE A 237 4789 5148 4603 37 492 -791 C ATOM 1933 N PRO A 238 22.197 -5.845 -4.430 1.00 16.33 N ANISOU 1933 N PRO A 238 2155 2074 1974 14 -111 -92 N ATOM 1934 CA PRO A 238 21.808 -4.413 -4.618 1.00 17.10 C ANISOU 1934 CA PRO A 238 2271 2147 2079 138 -108 -17 C ATOM 1935 C PRO A 238 20.508 -4.345 -5.492 1.00 17.92 C ANISOU 1935 C PRO A 238 2293 2244 2271 116 -208 -124 C ATOM 1936 O PRO A 238 20.442 -5.033 -6.555 1.00 17.08 O ANISOU 1936 O PRO A 238 2239 2162 2089 150 -17 -30 O ATOM 1937 CB PRO A 238 22.956 -3.794 -5.278 1.00 18.45 C ANISOU 1937 CB PRO A 238 2323 2283 2403 -47 -219 -83 C ATOM 1938 CG PRO A 238 24.102 -4.622 -4.821 1.00 21.94 C ANISOU 1938 CG PRO A 238 2828 2765 2741 40 -80 65 C ATOM 1939 CD PRO A 238 23.550 -6.010 -4.809 1.00 18.46 C ANISOU 1939 CD PRO A 238 2316 2374 2323 91 -57 61 C ATOM 1940 N LYS A 239 19.565 -3.468 -5.101 1.00 15.56 N ANISOU 1940 N LYS A 239 1973 1992 1945 -22 -53 17 N ATOM 1941 CA LYS A 239 18.354 -3.326 -5.816 1.00 14.27 C ANISOU 1941 CA LYS A 239 1862 1786 1771 78 31 -86 C ATOM 1942 C LYS A 239 18.078 -1.874 -6.095 1.00 16.06 C ANISOU 1942 C LYS A 239 2208 1897 1995 2 -281 37 C ATOM 1943 O LYS A 239 18.356 -1.018 -5.240 1.00 16.06 O ANISOU 1943 O LYS A 239 2259 1922 1920 -1 -64 -39 O ATOM 1944 CB LYS A 239 17.189 -3.953 -5.098 1.00 14.18 C ANISOU 1944 CB LYS A 239 1815 1738 1834 25 -58 -109 C ATOM 1945 CG LYS A 239 17.420 -5.431 -4.709 1.00 15.08 C ANISOU 1945 CG LYS A 239 1984 1830 1912 18 -71 -25 C ATOM 1946 CD LYS A 239 16.400 -5.987 -3.840 1.00 17.59 C ANISOU 1946 CD LYS A 239 2310 2163 2209 149 109 -18 C ATOM 1947 CE LYS A 239 16.753 -7.265 -3.082 1.00 18.86 C ANISOU 1947 CE LYS A 239 2376 2226 2563 -3 81 54 C ATOM 1948 NZ LYS A 239 17.931 -7.063 -2.223 1.00 18.35 N ANISOU 1948 NZ LYS A 239 2555 2068 2347 181 -72 5 N ATOM 1949 N LEU A 240 17.423 -1.584 -7.195 1.00 14.08 N ANISOU 1949 N LEU A 240 1895 1747 1706 104 -29 -66 N ATOM 1950 CA LEU A 240 16.825 -0.276 -7.514 1.00 14.85 C ANISOU 1950 CA LEU A 240 2008 1804 1830 36 -25 -30 C ATOM 1951 C LEU A 240 15.356 -0.517 -7.780 1.00 14.62 C ANISOU 1951 C LEU A 240 1883 1861 1808 49 -37 18 C ATOM 1952 O LEU A 240 14.965 -1.217 -8.751 1.00 14.48 O ANISOU 1952 O LEU A 240 1881 1774 1847 29 -10 -63 O ATOM 1953 CB LEU A 240 17.488 0.287 -8.673 1.00 14.84 C ANISOU 1953 CB LEU A 240 1871 1808 1960 29 32 -79 C ATOM 1954 CG LEU A 240 16.897 1.602 -9.266 1.00 15.83 C ANISOU 1954 CG LEU A 240 2079 1948 1984 86 -37 -38 C ATOM 1955 CD1 LEU A 240 16.855 2.741 -8.245 1.00 17.34 C ANISOU 1955 CD1 LEU A 240 2301 2151 2137 -17 39 -37 C ATOM 1956 CD2 LEU A 240 17.568 2.107 -10.519 1.00 16.39 C ANISOU 1956 CD2 LEU A 240 2181 1953 2092 34 -72 -39 C ATOM 1957 N PHE A 241 14.490 0.043 -6.959 1.00 13.61 N ANISOU 1957 N PHE A 241 1735 1749 1686 -35 -88 -55 N ATOM 1958 CA PHE A 241 13.057 -0.034 -7.148 1.00 14.30 C ANISOU 1958 CA PHE A 241 1841 1745 1845 86 89 -48 C ATOM 1959 C PHE A 241 12.556 1.265 -7.789 1.00 16.15 C ANISOU 1959 C PHE A 241 2074 1977 2083 12 -110 73 C ATOM 1960 O PHE A 241 12.692 2.290 -7.204 1.00 16.70 O ANISOU 1960 O PHE A 241 2208 2103 2032 41 -56 -87 O ATOM 1961 CB PHE A 241 12.358 -0.244 -5.777 1.00 16.22 C ANISOU 1961 CB PHE A 241 2215 1847 2099 -50 -37 54 C ATOM 1962 CG PHE A 241 10.855 -0.097 -5.795 1.00 15.56 C ANISOU 1962 CG PHE A 241 2059 1851 2003 48 39 55 C ATOM 1963 CD1 PHE A 241 10.120 -0.511 -6.844 1.00 14.88 C ANISOU 1963 CD1 PHE A 241 1925 1755 1972 62 -25 4 C ATOM 1964 CD2 PHE A 241 10.209 0.448 -4.728 1.00 15.83 C ANISOU 1964 CD2 PHE A 241 2065 1996 1953 -2 -38 -126 C ATOM 1965 CE1 PHE A 241 8.765 -0.388 -6.857 1.00 14.84 C ANISOU 1965 CE1 PHE A 241 2017 1722 1899 -102 81 114 C ATOM 1966 CE2 PHE A 241 8.859 0.575 -4.733 1.00 15.80 C ANISOU 1966 CE2 PHE A 241 2059 1927 2016 -7 108 -79 C ATOM 1967 CZ PHE A 241 8.135 0.167 -5.801 1.00 17.61 C ANISOU 1967 CZ PHE A 241 2214 2255 2222 -9 20 99 C ATOM 1968 N ILE A 242 11.999 1.199 -8.996 1.00 14.71 N ANISOU 1968 N ILE A 242 2030 1731 1828 81 -44 -74 N ATOM 1969 CA ILE A 242 11.435 2.372 -9.653 1.00 15.00 C ANISOU 1969 CA ILE A 242 2021 1812 1866 28 -130 -122 C ATOM 1970 C ILE A 242 9.945 2.268 -9.403 1.00 15.37 C ANISOU 1970 C ILE A 242 1987 1909 1941 -20 110 -10 C ATOM 1971 O ILE A 242 9.207 1.489 -10.027 1.00 17.36 O ANISOU 1971 O ILE A 242 2206 2232 2156 -50 35 -122 O ATOM 1972 CB ILE A 242 11.775 2.484 -11.155 1.00 16.08 C ANISOU 1972 CB ILE A 242 2116 1923 2070 5 77 26 C ATOM 1973 CG1 ILE A 242 13.316 2.622 -11.244 1.00 18.81 C ANISOU 1973 CG1 ILE A 242 2432 2348 2367 200 26 22 C ATOM 1974 CG2 ILE A 242 11.046 3.703 -11.676 1.00 17.38 C ANISOU 1974 CG2 ILE A 242 2206 2225 2173 -188 -79 32 C ATOM 1975 CD1 ILE A 242 13.878 2.657 -12.606 1.00 24.87 C ANISOU 1975 CD1 ILE A 242 3168 3032 3247 125 38 51 C ATOM 1976 N ASN A 243 9.428 3.025 -8.420 1.00 14.34 N ANISOU 1976 N ASN A 243 1883 1745 1820 36 -36 53 N ATOM 1977 CA ASN A 243 8.040 3.153 -8.152 1.00 14.98 C ANISOU 1977 CA ASN A 243 1981 1763 1946 -21 29 -22 C ATOM 1978 C ASN A 243 7.326 4.050 -9.072 1.00 16.28 C ANISOU 1978 C ASN A 243 2164 2137 1883 -54 41 -72 C ATOM 1979 O ASN A 243 7.998 5.031 -9.616 1.00 17.46 O ANISOU 1979 O ASN A 243 2204 2129 2301 -47 27 -41 O ATOM 1980 CB ASN A 243 7.873 3.729 -6.690 1.00 16.09 C ANISOU 1980 CB ASN A 243 2254 1868 1989 72 18 52 C ATOM 1981 CG ASN A 243 6.492 3.789 -6.236 1.00 18.57 C ANISOU 1981 CG ASN A 243 2309 2321 2423 -81 36 -213 C ATOM 1982 OD1 ASN A 243 5.662 2.911 -6.407 1.00 18.31 O ANISOU 1982 OD1 ASN A 243 2379 2300 2276 19 244 27 O ATOM 1983 ND2 ASN A 243 6.084 5.092 -5.804 1.00 20.20 N ANISOU 1983 ND2 ASN A 243 2711 2398 2563 126 199 -199 N ATOM 1984 N ALA A 244 6.034 3.842 -9.350 1.00 17.54 N ANISOU 1984 N ALA A 244 2246 2300 2116 171 124 -8 N ATOM 1985 CA ALA A 244 5.289 4.683 -10.237 1.00 17.94 C ANISOU 1985 CA ALA A 244 2296 2243 2276 187 137 108 C ATOM 1986 C ALA A 244 4.052 5.264 -9.577 1.00 18.72 C ANISOU 1986 C ALA A 244 2458 2264 2389 110 258 27 C ATOM 1987 O ALA A 244 3.510 4.661 -8.660 1.00 18.79 O ANISOU 1987 O ALA A 244 2393 2293 2452 172 219 34 O ATOM 1988 CB ALA A 244 4.867 3.922 -11.500 1.00 19.93 C ANISOU 1988 CB ALA A 244 2404 2513 2652 -97 25 -2 C ATOM 1989 N AGLU A 245 3.688 6.472 -9.981 0.50 16.68 N ANISOU 1989 N AGLU A 245 2111 2150 2074 275 446 353 N ATOM 1990 N BGLU A 245 3.737 6.542 -9.948 0.50 17.00 N ANISOU 1990 N BGLU A 245 2196 2158 2104 269 445 301 N ATOM 1991 CA AGLU A 245 2.522 7.159 -9.470 0.50 18.08 C ANISOU 1991 CA AGLU A 245 2283 2206 2378 107 51 -21 C ATOM 1992 CA BGLU A 245 2.481 7.121 -9.473 0.50 18.85 C ANISOU 1992 CA BGLU A 245 2287 2317 2557 72 89 -62 C ATOM 1993 C AGLU A 245 1.615 7.491 -10.644 0.50 16.78 C ANISOU 1993 C AGLU A 245 2202 1864 2308 149 240 -394 C ATOM 1994 C BGLU A 245 1.629 7.438 -10.627 0.50 16.56 C ANISOU 1994 C BGLU A 245 2198 1827 2266 141 251 -368 C ATOM 1995 O AGLU A 245 2.018 8.225 -11.518 0.50 18.18 O ANISOU 1995 O AGLU A 245 2440 2306 2160 238 347 28 O ATOM 1996 O BGLU A 245 2.104 8.300 -11.509 0.50 18.26 O ANISOU 1996 O BGLU A 245 2476 2292 2169 203 371 30 O ATOM 1997 CB AGLU A 245 2.969 8.448 -8.773 0.50 19.27 C ANISOU 1997 CB AGLU A 245 2574 2204 2542 34 47 -152 C ATOM 1998 CB BGLU A 245 2.828 8.363 -8.595 0.50 21.19 C ANISOU 1998 CB BGLU A 245 2830 2483 2738 204 75 -307 C ATOM 1999 CG AGLU A 245 1.873 9.239 -8.085 0.50 22.28 C ANISOU 1999 CG AGLU A 245 2565 2884 3016 220 85 -155 C ATOM 2000 CG BGLU A 245 3.364 7.972 -7.261 0.50 24.04 C ANISOU 2000 CG BGLU A 245 3217 2883 3033 152 -7 -241 C ATOM 2001 CD AGLU A 245 0.959 8.385 -7.214 0.50 24.93 C ANISOU 2001 CD AGLU A 245 3188 3163 3119 270 -69 145 C ATOM 2002 CD BGLU A 245 2.442 7.090 -6.380 0.50 22.88 C ANISOU 2002 CD BGLU A 245 2749 3179 2766 -10 -309 -71 C ATOM 2003 OE1AGLU A 245 1.444 7.464 -6.505 0.50 26.27 O ANISOU 2003 OE1AGLU A 245 3291 3646 3041 -156 32 -162 O ATOM 2004 OE1BGLU A 245 1.165 7.192 -6.496 0.50 23.09 O ANISOU 2004 OE1BGLU A 245 3192 2682 2898 -109 648 -498 O ATOM 2005 OE2AGLU A 245 -0.256 8.621 -7.266 0.50 25.79 O ANISOU 2005 OE2AGLU A 245 3363 3501 2935 -195 289 25 O ATOM 2006 OE2BGLU A 245 3.120 6.316 -5.605 0.50 22.08 O ANISOU 2006 OE2BGLU A 245 3065 2487 2836 251 189 294 O ATOM 2007 N PRO A 246 0.403 6.927 -10.682 1.00 18.98 N ANISOU 2007 N PRO A 246 2460 2346 2403 159 117 -62 N ATOM 2008 CA PRO A 246 -0.221 6.063 -9.693 1.00 20.40 C ANISOU 2008 CA PRO A 246 2533 2422 2796 49 37 -82 C ATOM 2009 C PRO A 246 0.185 4.610 -9.734 1.00 20.81 C ANISOU 2009 C PRO A 246 2787 2462 2657 423 35 -142 C ATOM 2010 O PRO A 246 0.051 3.901 -8.731 1.00 22.07 O ANISOU 2010 O PRO A 246 3070 2559 2757 32 583 -295 O ATOM 2011 CB PRO A 246 -1.678 6.130 -10.092 1.00 21.62 C ANISOU 2011 CB PRO A 246 2531 2571 3112 -95 54 -170 C ATOM 2012 CG PRO A 246 -1.699 6.284 -11.494 1.00 24.90 C ANISOU 2012 CG PRO A 246 2939 3004 3518 -3 -67 24 C ATOM 2013 CD PRO A 246 -0.469 7.164 -11.859 1.00 24.17 C ANISOU 2013 CD PRO A 246 2907 3037 3237 72 217 -227 C ATOM 2014 N GLY A 247 1.002 4.185 -10.777 1.00 18.74 N ANISOU 2014 N GLY A 247 2478 2334 2306 -113 272 109 N ATOM 2015 CA GLY A 247 1.375 2.808 -10.776 1.00 18.78 C ANISOU 2015 CA GLY A 247 2414 2389 2332 32 168 93 C ATOM 2016 C GLY A 247 0.219 1.966 -11.154 1.00 18.80 C ANISOU 2016 C GLY A 247 2346 2398 2395 15 95 -26 C ATOM 2017 O GLY A 247 -0.898 2.457 -11.443 1.00 20.70 O ANISOU 2017 O GLY A 247 2504 2510 2851 71 -28 -89 O ATOM 2018 N ALA A 248 0.352 0.625 -11.138 1.00 16.62 N ANISOU 2018 N ALA A 248 2075 2135 2104 69 68 71 N ATOM 2019 CA ALA A 248 -0.674 -0.281 -11.513 1.00 18.34 C ANISOU 2019 CA ALA A 248 2251 2349 2368 122 130 -19 C ATOM 2020 C ALA A 248 -0.606 -1.558 -10.788 1.00 22.60 C ANISOU 2020 C ALA A 248 3069 2659 2858 169 268 -73 C ATOM 2021 O ALA A 248 -1.511 -1.837 -9.977 1.00 25.30 O ANISOU 2021 O ALA A 248 3225 3014 3372 21 528 124 O ATOM 2022 CB ALA A 248 -0.749 -0.471 -13.013 1.00 20.88 C ANISOU 2022 CB ALA A 248 2615 2644 2672 54 -200 36 C ATOM 2023 N ILE A 249 0.426 -2.365 -10.979 1.00 16.96 N ANISOU 2023 N ILE A 249 2085 2182 2177 19 192 182 N ATOM 2024 CA ILE A 249 0.537 -3.667 -10.289 1.00 18.66 C ANISOU 2024 CA ILE A 249 2404 2284 2400 -33 150 -33 C ATOM 2025 C ILE A 249 1.427 -3.587 -9.115 1.00 19.18 C ANISOU 2025 C ILE A 249 2500 2398 2390 96 -5 -51 C ATOM 2026 O ILE A 249 1.355 -4.516 -8.275 1.00 22.04 O ANISOU 2026 O ILE A 249 2957 2710 2707 -92 109 101 O ATOM 2027 CB ILE A 249 0.818 -4.798 -11.217 1.00 19.61 C ANISOU 2027 CB ILE A 249 2518 2351 2582 36 -11 -80 C ATOM 2028 CG1 ILE A 249 2.242 -4.809 -11.692 1.00 18.97 C ANISOU 2028 CG1 ILE A 249 2535 2238 2433 -67 208 -150 C ATOM 2029 CG2 ILE A 249 -0.248 -4.829 -12.274 1.00 23.82 C ANISOU 2029 CG2 ILE A 249 3041 2805 3204 -81 -225 169 C ATOM 2030 CD1 ILE A 249 2.666 -6.167 -12.455 1.00 22.22 C ANISOU 2030 CD1 ILE A 249 2865 2600 2977 62 -107 -168 C ATOM 2031 N VAL A 250 2.283 -2.573 -8.956 1.00 17.50 N ANISOU 2031 N VAL A 250 2285 2311 2051 52 118 24 N ATOM 2032 CA VAL A 250 3.063 -2.393 -7.724 1.00 16.72 C ANISOU 2032 CA VAL A 250 2150 1980 2222 110 4 -81 C ATOM 2033 C VAL A 250 2.443 -1.186 -6.938 1.00 17.76 C ANISOU 2033 C VAL A 250 2363 2215 2168 -16 155 -133 C ATOM 2034 O VAL A 250 2.859 -0.084 -7.111 1.00 18.72 O ANISOU 2034 O VAL A 250 2520 2338 2252 -86 302 -93 O ATOM 2035 CB VAL A 250 4.505 -2.229 -7.944 1.00 17.88 C ANISOU 2035 CB VAL A 250 2303 2200 2289 63 113 -92 C ATOM 2036 CG1 VAL A 250 5.272 -2.113 -6.675 1.00 19.28 C ANISOU 2036 CG1 VAL A 250 2480 2471 2372 272 114 -33 C ATOM 2037 CG2 VAL A 250 5.014 -3.526 -8.594 1.00 19.07 C ANISOU 2037 CG2 VAL A 250 2506 2317 2422 100 100 -108 C ATOM 2038 N THR A 251 1.384 -1.502 -6.235 1.00 17.32 N ANISOU 2038 N THR A 251 2230 2175 2173 15 135 -167 N ATOM 2039 CA THR A 251 0.661 -0.491 -5.406 1.00 18.32 C ANISOU 2039 CA THR A 251 2431 2232 2296 263 76 -134 C ATOM 2040 C THR A 251 0.319 -1.284 -4.114 1.00 19.07 C ANISOU 2040 C THR A 251 2511 2396 2336 198 122 23 C ATOM 2041 O THR A 251 0.554 -2.483 -3.919 1.00 18.62 O ANISOU 2041 O THR A 251 2433 2278 2363 36 179 -38 O ATOM 2042 CB THR A 251 -0.675 -0.055 -6.038 1.00 19.79 C ANISOU 2042 CB THR A 251 2542 2533 2441 69 213 -187 C ATOM 2043 OG1 THR A 251 -1.561 -1.156 -6.142 1.00 24.75 O ANISOU 2043 OG1 THR A 251 3123 3129 3150 -97 74 -119 O ATOM 2044 CG2 THR A 251 -0.387 0.567 -7.472 1.00 21.90 C ANISOU 2044 CG2 THR A 251 2958 2650 2712 368 68 -61 C ATOM 2045 N GLY A 252 -0.268 -0.540 -3.143 1.00 20.13 N ANISOU 2045 N GLY A 252 2670 2438 2537 194 180 58 N ATOM 2046 CA GLY A 252 -0.831 -1.218 -1.936 1.00 21.22 C ANISOU 2046 CA GLY A 252 2734 2799 2527 195 255 -58 C ATOM 2047 C GLY A 252 0.086 -2.071 -1.202 1.00 16.40 C ANISOU 2047 C GLY A 252 2204 2140 1884 3 192 -256 C ATOM 2048 O GLY A 252 1.270 -1.701 -1.040 1.00 19.08 O ANISOU 2048 O GLY A 252 2365 2678 2204 14 187 -274 O ATOM 2049 N ARG A 253 -0.441 -3.194 -0.804 1.00 21.71 N ANISOU 2049 N ARG A 253 2706 2860 2681 54 268 -27 N ATOM 2050 CA AARG A 253 0.359 -4.151 -0.087 0.50 22.38 C ANISOU 2050 CA AARG A 253 2705 2920 2878 224 373 -17 C ATOM 2051 CA BARG A 253 0.437 -4.122 -0.063 0.50 22.06 C ANISOU 2051 CA BARG A 253 2678 2872 2832 211 357 -55 C ATOM 2052 C ARG A 253 1.678 -4.801 -0.828 1.00 20.12 C ANISOU 2052 C ARG A 253 2633 2630 2379 299 32 -61 C ATOM 2053 O ARG A 253 2.760 -5.065 -0.304 1.00 18.97 O ANISOU 2053 O ARG A 253 2463 2410 2334 48 107 -182 O ATOM 2054 CB AARG A 253 -0.486 -5.263 0.529 0.50 28.30 C ANISOU 2054 CB AARG A 253 3214 3692 3845 -111 433 161 C ATOM 2055 CB BARG A 253 -0.389 -5.189 0.630 0.50 27.50 C ANISOU 2055 CB BARG A 253 3145 3587 3717 -93 308 143 C ATOM 2056 CG AARG A 253 -1.057 -6.214 -0.481 0.50 26.97 C ANISOU 2056 CG AARG A 253 3441 3395 3410 -564 492 -285 C ATOM 2057 CG BARG A 253 -1.068 -6.076 -0.302 0.50 23.51 C ANISOU 2057 CG BARG A 253 3134 2811 2986 -138 243 -278 C ATOM 2058 CD AARG A 253 -1.259 -7.635 0.031 0.50 29.87 C ANISOU 2058 CD AARG A 253 3975 3652 3719 468 145 348 C ATOM 2059 CD BARG A 253 -2.095 -7.057 0.386 0.50 25.78 C ANISOU 2059 CD BARG A 253 3057 3617 3121 -351 118 67 C ATOM 2060 NE AARG A 253 -1.513 -8.531 -1.096 0.50 29.45 N ANISOU 2060 NE AARG A 253 3770 3766 3654 -188 214 -110 N ATOM 2061 NE BARG A 253 -2.689 -7.969 -0.605 0.50 25.65 N ANISOU 2061 NE BARG A 253 3432 3279 3035 247 78 -192 N ATOM 2062 CZ AARG A 253 -0.735 -9.549 -1.472 0.50 25.57 C ANISOU 2062 CZ AARG A 253 3453 3129 3132 36 -81 155 C ATOM 2063 CZ BARG A 253 -3.574 -8.910 -0.292 0.50 33.37 C ANISOU 2063 CZ BARG A 253 4888 3784 4004 -790 702 -419 C ATOM 2064 NH1AARG A 253 0.373 -9.841 -0.804 0.50 26.31 N ANISOU 2064 NH1AARG A 253 3498 3274 3223 256 274 108 N ATOM 2065 NH1BARG A 253 -3.881 -9.146 1.000 0.50 31.63 N ANISOU 2065 NH1BARG A 253 4226 4072 3717 -58 21 191 N ATOM 2066 NH2AARG A 253 -1.073 -10.278 -2.529 0.50 20.57 N ANISOU 2066 NH2AARG A 253 2761 2539 2515 170 -62 -28 N ATOM 2067 NH2BARG A 253 -4.099 -9.685 -1.216 0.50 31.64 N ANISOU 2067 NH2BARG A 253 3959 4620 3443 -638 -265 -103 N ATOM 2068 N MET A 254 1.538 -4.770 -2.163 1.00 21.76 N ANISOU 2068 N MET A 254 2666 2949 2654 5 68 -85 N ATOM 2069 CA MET A 254 2.603 -5.284 -2.978 1.00 21.36 C ANISOU 2069 CA MET A 254 2600 2819 2695 139 -28 -155 C ATOM 2070 C MET A 254 3.747 -4.294 -2.934 1.00 17.83 C ANISOU 2070 C MET A 254 2336 2349 2088 53 -50 -214 C ATOM 2071 O MET A 254 4.857 -4.659 -2.858 1.00 18.57 O ANISOU 2071 O MET A 254 2379 2518 2158 142 93 -214 O ATOM 2072 CB MET A 254 2.133 -5.493 -4.413 1.00 22.08 C ANISOU 2072 CB MET A 254 2868 2964 2556 104 270 -136 C ATOM 2073 CG MET A 254 0.805 -6.217 -4.518 1.00 31.03 C ANISOU 2073 CG MET A 254 3445 4493 3852 -161 226 -460 C ATOM 2074 SD MET A 254 1.374 -7.868 -4.465 1.00 37.39 S ANISOU 2074 SD MET A 254 4814 4541 4850 -100 22 -84 S ATOM 2075 CE MET A 254 1.287 -8.151 -2.703 1.00 39.65 C ANISOU 2075 CE MET A 254 4976 6005 4081 -165 -332 -460 C ATOM 2076 N ARG A 255 3.417 -3.029 -3.004 1.00 17.89 N ANISOU 2076 N ARG A 255 2370 2354 2072 21 6 8 N ATOM 2077 CA ARG A 255 4.416 -2.009 -2.904 1.00 16.89 C ANISOU 2077 CA ARG A 255 2018 2306 2090 55 211 -153 C ATOM 2078 C ARG A 255 5.010 -1.984 -1.503 1.00 16.90 C ANISOU 2078 C ARG A 255 2177 2056 2185 24 40 36 C ATOM 2079 O ARG A 255 6.179 -1.817 -1.328 1.00 17.02 O ANISOU 2079 O ARG A 255 2204 2203 2058 57 134 -27 O ATOM 2080 CB ARG A 255 3.815 -0.666 -3.260 1.00 20.38 C ANISOU 2080 CB ARG A 255 2778 2672 2290 -59 3 45 C ATOM 2081 CG ARG A 255 4.818 0.449 -3.186 1.00 22.72 C ANISOU 2081 CG ARG A 255 2977 2918 2735 -10 270 -8 C ATOM 2082 CD ARG A 255 4.469 1.589 -4.111 1.00 27.13 C ANISOU 2082 CD ARG A 255 3169 3479 3660 -60 -238 133 C ATOM 2083 NE ARG A 255 3.123 2.025 -3.908 1.00 23.33 N ANISOU 2083 NE ARG A 255 2809 2781 3271 148 66 -210 N ATOM 2084 CZ ARG A 255 2.412 2.693 -4.788 1.00 20.32 C ANISOU 2084 CZ ARG A 255 2823 2365 2533 -33 -118 -77 C ATOM 2085 NH1 ARG A 255 2.915 3.073 -5.925 1.00 24.12 N ANISOU 2085 NH1 ARG A 255 3139 2814 3209 270 538 -276 N ATOM 2086 NH2 ARG A 255 1.179 2.989 -4.508 1.00 22.36 N ANISOU 2086 NH2 ARG A 255 2769 2849 2876 -6 217 32 N ATOM 2087 N ASP A 256 4.204 -2.160 -0.479 1.00 18.28 N ANISOU 2087 N ASP A 256 2333 2302 2312 36 144 38 N ATOM 2088 CA ASP A 256 4.808 -2.238 0.847 1.00 19.75 C ANISOU 2088 CA ASP A 256 2488 2569 2446 42 -93 -12 C ATOM 2089 C ASP A 256 5.855 -3.388 0.938 1.00 18.41 C ANISOU 2089 C ASP A 256 2419 2407 2168 -85 175 31 C ATOM 2090 O ASP A 256 6.861 -3.248 1.567 1.00 20.32 O ANISOU 2090 O ASP A 256 2518 2797 2403 -27 219 -59 O ATOM 2091 CB ASP A 256 3.750 -2.498 1.927 1.00 20.17 C ANISOU 2091 CB ASP A 256 2568 2576 2520 98 26 -38 C ATOM 2092 CG ASP A 256 2.883 -1.289 2.246 1.00 23.23 C ANISOU 2092 CG ASP A 256 2891 2844 3088 -171 223 -86 C ATOM 2093 OD1 ASP A 256 3.216 -0.178 1.873 1.00 22.59 O ANISOU 2093 OD1 ASP A 256 3252 2659 2671 116 476 -79 O ATOM 2094 OD2 ASP A 256 1.887 -1.510 2.892 1.00 22.26 O ANISOU 2094 OD2 ASP A 256 2840 2880 2736 167 294 -158 O ATOM 2095 N PHE A 257 5.536 -4.532 0.340 1.00 18.34 N ANISOU 2095 N PHE A 257 2374 2395 2197 62 137 -10 N ATOM 2096 CA PHE A 257 6.380 -5.704 0.347 1.00 17.96 C ANISOU 2096 CA PHE A 257 2291 2355 2178 23 2 23 C ATOM 2097 C PHE A 257 7.721 -5.386 -0.357 1.00 19.25 C ANISOU 2097 C PHE A 257 2347 2529 2438 11 272 -231 C ATOM 2098 O PHE A 257 8.821 -5.573 0.271 1.00 18.76 O ANISOU 2098 O PHE A 257 2457 2495 2175 118 84 -51 O ATOM 2099 CB PHE A 257 5.664 -6.845 -0.205 1.00 18.51 C ANISOU 2099 CB PHE A 257 2434 2301 2298 44 118 199 C ATOM 2100 CG PHE A 257 6.492 -8.091 -0.269 1.00 20.20 C ANISOU 2100 CG PHE A 257 2625 2510 2540 221 115 -122 C ATOM 2101 CD1 PHE A 257 7.087 -8.624 0.842 1.00 23.56 C ANISOU 2101 CD1 PHE A 257 3193 2969 2788 556 364 -165 C ATOM 2102 CD2 PHE A 257 6.805 -8.684 -1.542 1.00 20.15 C ANISOU 2102 CD2 PHE A 257 2800 2502 2353 -13 -18 -22 C ATOM 2103 CE1 PHE A 257 7.857 -9.794 0.772 1.00 23.76 C ANISOU 2103 CE1 PHE A 257 3373 2862 2793 317 118 278 C ATOM 2104 CE2 PHE A 257 7.549 -9.833 -1.537 1.00 20.96 C ANISOU 2104 CE2 PHE A 257 2678 2761 2522 202 199 -108 C ATOM 2105 CZ PHE A 257 8.146 -10.346 -0.483 1.00 21.51 C ANISOU 2105 CZ PHE A 257 2872 2610 2689 70 -48 -23 C ATOM 2106 N CYS A 258 7.690 -4.938 -1.583 1.00 17.68 N ANISOU 2106 N CYS A 258 2449 2173 2092 40 -67 34 N ATOM 2107 CA CYS A 258 8.949 -4.724 -2.206 1.00 24.14 C ANISOU 2107 CA CYS A 258 2491 2655 4025 -169 22 -17 C ATOM 2108 C CYS A 258 9.737 -3.598 -1.591 1.00 17.50 C ANISOU 2108 C CYS A 258 2184 2271 2191 238 7 243 C ATOM 2109 O CYS A 258 10.911 -3.620 -1.623 1.00 17.97 O ANISOU 2109 O CYS A 258 2341 2286 2197 -48 47 32 O ATOM 2110 CB CYS A 258 8.865 -4.722 -3.705 1.00 10.87 C ANISOU 2110 CB CYS A 258 1371 1486 1272 -140 504 -196 C ATOM 2111 SG CYS A 258 8.011 -3.320 -4.394 1.00 30.80 S ANISOU 2111 SG CYS A 258 4071 3836 3793 543 269 384 S ATOM 2112 N ARG A 259 9.069 -2.658 -0.965 1.00 18.74 N ANISOU 2112 N ARG A 259 2434 2436 2248 -192 78 -50 N ATOM 2113 CA ARG A 259 9.806 -1.625 -0.280 1.00 23.72 C ANISOU 2113 CA ARG A 259 3030 2921 3061 16 100 -292 C ATOM 2114 C ARG A 259 10.553 -2.169 0.942 1.00 23.29 C ANISOU 2114 C ARG A 259 2865 2815 3167 228 411 -246 C ATOM 2115 O ARG A 259 11.458 -1.571 1.349 1.00 32.01 O ANISOU 2115 O ARG A 259 3744 4021 4396 27 -432 -1128 O ATOM 2116 CB ARG A 259 8.891 -0.491 0.168 1.00 21.79 C ANISOU 2116 CB ARG A 259 2759 2675 2843 90 -82 -86 C ATOM 2117 CG ARG A 259 8.453 0.410 -0.927 1.00 21.34 C ANISOU 2117 CG ARG A 259 2691 2592 2825 -269 -12 -90 C ATOM 2118 CD ARG A 259 7.661 1.579 -0.389 1.00 25.65 C ANISOU 2118 CD ARG A 259 3289 3303 3152 472 636 422 C ATOM 2119 NE ARG A 259 7.670 2.643 -1.345 1.00 23.65 N ANISOU 2119 NE ARG A 259 2985 2970 3029 163 322 120 N ATOM 2120 CZ ARG A 259 6.640 3.405 -1.630 1.00 30.77 C ANISOU 2120 CZ ARG A 259 4099 4050 3539 -64 -18 61 C ATOM 2121 NH1 ARG A 259 5.487 3.249 -1.018 1.00 30.72 N ANISOU 2121 NH1 ARG A 259 3836 3695 4140 192 172 -314 N ATOM 2122 NH2 ARG A 259 6.775 4.334 -2.524 1.00 28.22 N ANISOU 2122 NH2 ARG A 259 3910 3304 3507 181 35 -25 N ATOM 2123 N SER A 260 10.159 -3.303 1.484 1.00 21.75 N ANISOU 2123 N SER A 260 2783 2948 2530 194 153 -32 N ATOM 2124 CA SER A 260 10.821 -3.923 2.642 1.00 26.29 C ANISOU 2124 CA SER A 260 3436 3350 3201 93 -387 -63 C ATOM 2125 C SER A 260 12.092 -4.611 2.240 1.00 29.40 C ANISOU 2125 C SER A 260 3539 4309 3320 574 348 371 C ATOM 2126 O SER A 260 12.852 -5.172 3.032 1.00 26.77 O ANISOU 2126 O SER A 260 3355 3972 2845 30 -97 -20 O ATOM 2127 CB SER A 260 9.814 -4.914 3.212 1.00 23.76 C ANISOU 2127 CB SER A 260 3221 3158 2647 90 173 -22 C ATOM 2128 OG SER A 260 9.672 -6.134 2.631 1.00 29.06 O ANISOU 2128 OG SER A 260 3732 3928 3380 -260 231 335 O ATOM 2129 N TRP A 261 12.343 -4.769 0.937 1.00 22.99 N ANISOU 2129 N TRP A 261 3041 3153 2539 78 0 -178 N ATOM 2130 CA TRP A 261 13.541 -5.496 0.505 1.00 20.69 C ANISOU 2130 CA TRP A 261 2704 2711 2444 50 -395 122 C ATOM 2131 C TRP A 261 14.861 -4.824 0.878 1.00 19.69 C ANISOU 2131 C TRP A 261 2562 2613 2306 -34 222 -34 C ATOM 2132 O TRP A 261 14.966 -3.649 0.870 1.00 21.92 O ANISOU 2132 O TRP A 261 2989 2757 2583 -29 22 46 O ATOM 2133 CB TRP A 261 13.495 -5.849 -0.990 1.00 19.08 C ANISOU 2133 CB TRP A 261 2558 2394 2295 145 232 -51 C ATOM 2134 CG TRP A 261 12.368 -6.738 -1.404 1.00 18.91 C ANISOU 2134 CG TRP A 261 2275 2499 2408 196 184 -47 C ATOM 2135 CD1 TRP A 261 11.499 -7.380 -0.615 1.00 18.00 C ANISOU 2135 CD1 TRP A 261 2266 2296 2275 -11 -101 244 C ATOM 2136 CD2 TRP A 261 11.999 -7.063 -2.741 1.00 18.35 C ANISOU 2136 CD2 TRP A 261 2235 2430 2308 10 43 -53 C ATOM 2137 NE1 TRP A 261 10.623 -8.091 -1.352 1.00 20.18 N ANISOU 2137 NE1 TRP A 261 2758 2510 2398 -19 254 55 N ATOM 2138 CE2 TRP A 261 10.915 -7.921 -2.673 1.00 19.01 C ANISOU 2138 CE2 TRP A 261 2487 2357 2378 57 -20 104 C ATOM 2139 CE3 TRP A 261 12.487 -6.711 -3.988 1.00 17.37 C ANISOU 2139 CE3 TRP A 261 2310 2111 2177 -86 15 150 C ATOM 2140 CZ2 TRP A 261 10.305 -8.417 -3.788 1.00 20.08 C ANISOU 2140 CZ2 TRP A 261 2750 2319 2560 61 239 112 C ATOM 2141 CZ3 TRP A 261 11.897 -7.234 -5.086 1.00 17.94 C ANISOU 2141 CZ3 TRP A 261 2283 2310 2221 64 39 114 C ATOM 2142 CH2 TRP A 261 10.823 -8.065 -4.984 1.00 18.60 C ANISOU 2142 CH2 TRP A 261 2524 2307 2234 -194 -38 -319 C ATOM 2143 N PRO A 262 15.869 -5.607 1.195 1.00 18.41 N ANISOU 2143 N PRO A 262 2481 2329 2184 73 16 47 N ATOM 2144 CA PRO A 262 17.117 -5.070 1.640 1.00 20.24 C ANISOU 2144 CA PRO A 262 2587 2568 2532 101 105 -81 C ATOM 2145 C PRO A 262 18.039 -4.474 0.574 1.00 22.01 C ANISOU 2145 C PRO A 262 2785 2825 2751 -110 -30 186 C ATOM 2146 O PRO A 262 17.849 -4.805 -0.635 1.00 19.17 O ANISOU 2146 O PRO A 262 2606 2298 2376 24 -121 -39 O ATOM 2147 CB PRO A 262 17.934 -6.263 2.222 1.00 22.56 C ANISOU 2147 CB PRO A 262 2932 3076 2562 -54 -6 192 C ATOM 2148 CG PRO A 262 17.019 -7.353 2.383 1.00 24.21 C ANISOU 2148 CG PRO A 262 3104 2843 3252 2 -404 -74 C ATOM 2149 CD PRO A 262 15.898 -7.085 1.352 1.00 21.27 C ANISOU 2149 CD PRO A 262 2847 2655 2580 -154 -137 178 C ATOM 2150 N ASN A 263 18.907 -3.585 0.972 1.00 20.04 N ANISOU 2150 N ASN A 263 2694 2478 2441 -38 -91 196 N ATOM 2151 CA ASN A 263 19.954 -3.064 0.141 1.00 18.26 C ANISOU 2151 CA ASN A 263 2207 2594 2134 25 -105 3 C ATOM 2152 C ASN A 263 19.335 -2.405 -1.183 1.00 17.44 C ANISOU 2152 C ASN A 263 2225 2230 2171 99 -97 102 C ATOM 2153 O ASN A 263 19.860 -2.627 -2.269 1.00 18.67 O ANISOU 2153 O ASN A 263 2474 2264 2356 56 -5 -5 O ATOM 2154 CB ASN A 263 21.036 -4.072 -0.248 1.00 17.68 C ANISOU 2154 CB ASN A 263 2387 2125 2203 117 -178 39 C ATOM 2155 CG ASN A 263 22.310 -3.488 -0.686 1.00 19.55 C ANISOU 2155 CG ASN A 263 2499 2476 2451 87 -326 209 C ATOM 2156 OD1 ASN A 263 22.552 -2.218 -0.553 1.00 22.60 O ANISOU 2156 OD1 ASN A 263 2941 2694 2952 -11 -183 -184 O ATOM 2157 ND2 ASN A 263 23.247 -4.289 -1.273 1.00 21.90 N ANISOU 2157 ND2 ASN A 263 2821 2822 2676 34 -113 -123 N ATOM 2158 N GLN A 264 18.294 -1.649 -0.976 1.00 17.31 N ANISOU 2158 N GLN A 264 2319 2181 2073 76 -97 -111 N ATOM 2159 CA GLN A 264 17.560 -1.107 -2.059 1.00 17.41 C ANISOU 2159 CA GLN A 264 2333 2141 2140 93 5 -107 C ATOM 2160 C GLN A 264 17.403 0.388 -2.029 1.00 18.87 C ANISOU 2160 C GLN A 264 2589 2236 2342 92 129 74 C ATOM 2161 O GLN A 264 17.201 0.955 -0.996 1.00 20.02 O ANISOU 2161 O GLN A 264 2946 2322 2338 53 -46 -52 O ATOM 2162 CB GLN A 264 16.167 -1.695 -2.017 1.00 18.81 C ANISOU 2162 CB GLN A 264 2466 2348 2331 92 -152 -140 C ATOM 2163 CG GLN A 264 15.240 -1.304 -3.145 1.00 18.91 C ANISOU 2163 CG GLN A 264 2623 2309 2252 236 2 -140 C ATOM 2164 CD GLN A 264 13.990 -2.141 -3.127 1.00 18.03 C ANISOU 2164 CD GLN A 264 2246 2260 2345 34 -30 -47 C ATOM 2165 OE1 GLN A 264 13.933 -3.169 -3.706 1.00 17.21 O ANISOU 2165 OE1 GLN A 264 2256 2180 2102 91 41 -7 O ATOM 2166 NE2 GLN A 264 12.999 -1.677 -2.433 1.00 19.20 N ANISOU 2166 NE2 GLN A 264 2498 2460 2335 102 182 35 N ATOM 2167 N THR A 265 17.599 1.004 -3.170 1.00 17.49 N ANISOU 2167 N THR A 265 2239 2204 2202 -6 -174 -23 N ATOM 2168 CA THR A 265 17.202 2.440 -3.286 1.00 20.30 C ANISOU 2168 CA THR A 265 2629 2553 2530 80 -266 -159 C ATOM 2169 C THR A 265 15.972 2.537 -4.177 1.00 17.38 C ANISOU 2169 C THR A 265 2268 2249 2086 155 -276 12 C ATOM 2170 O THR A 265 15.645 1.606 -4.937 1.00 16.57 O ANISOU 2170 O THR A 265 2289 1915 2089 75 -178 30 O ATOM 2171 CB THR A 265 18.175 3.344 -3.759 1.00 29.10 C ANISOU 2171 CB THR A 265 3429 3758 3867 -240 -289 144 C ATOM 2172 OG1 THR A 265 18.626 2.880 -5.004 1.00 27.61 O ANISOU 2172 OG1 THR A 265 3316 3877 3297 -204 49 -42 O ATOM 2173 CG2 THR A 265 19.480 3.340 -2.779 1.00 28.31 C ANISOU 2173 CG2 THR A 265 3531 3424 3800 -35 -466 284 C ATOM 2174 N GLU A 266 15.265 3.636 -4.040 1.00 18.75 N ANISOU 2174 N GLU A 266 2587 2265 2271 70 -218 -193 N ATOM 2175 CA GLU A 266 14.028 3.835 -4.710 1.00 18.86 C ANISOU 2175 CA GLU A 266 2447 2247 2472 100 133 -130 C ATOM 2176 C GLU A 266 13.893 5.221 -5.279 1.00 18.06 C ANISOU 2176 C GLU A 266 2330 2200 2330 69 -49 69 C ATOM 2177 O GLU A 266 14.404 6.146 -4.764 1.00 18.76 O ANISOU 2177 O GLU A 266 2427 2324 2376 -86 -81 -127 O ATOM 2178 CB GLU A 266 12.896 3.641 -3.679 1.00 21.03 C ANISOU 2178 CB GLU A 266 2725 2527 2736 -146 -43 157 C ATOM 2179 CG GLU A 266 11.501 3.837 -4.162 1.00 23.66 C ANISOU 2179 CG GLU A 266 3037 2835 3117 -80 159 -50 C ATOM 2180 CD GLU A 266 10.465 3.793 -3.066 1.00 27.21 C ANISOU 2180 CD GLU A 266 3772 3526 3038 206 132 203 C ATOM 2181 OE1 GLU A 266 10.598 2.996 -2.141 1.00 22.86 O ANISOU 2181 OE1 GLU A 266 3175 2731 2778 91 280 -166 O ATOM 2182 OE2 GLU A 266 9.509 4.529 -3.230 1.00 28.32 O ANISOU 2182 OE2 GLU A 266 3557 3723 3481 465 762 173 O ATOM 2183 N ILE A 267 13.236 5.292 -6.402 1.00 16.58 N ANISOU 2183 N ILE A 267 2268 1985 2045 39 -10 -229 N ATOM 2184 CA ILE A 267 12.823 6.573 -6.993 1.00 16.04 C ANISOU 2184 CA ILE A 267 2181 1967 1947 -17 -39 -31 C ATOM 2185 C ILE A 267 11.326 6.455 -7.288 1.00 17.38 C ANISOU 2185 C ILE A 267 2203 2209 2190 27 8 -30 C ATOM 2186 O ILE A 267 10.817 5.331 -7.482 1.00 17.50 O ANISOU 2186 O ILE A 267 2302 2066 2278 18 -44 -81 O ATOM 2187 CB ILE A 267 13.599 7.076 -8.185 1.00 17.85 C ANISOU 2187 CB ILE A 267 2300 2148 2333 -8 6 -104 C ATOM 2188 CG1 ILE A 267 13.368 6.255 -9.452 1.00 19.25 C ANISOU 2188 CG1 ILE A 267 2611 2287 2416 -67 -25 -103 C ATOM 2189 CG2 ILE A 267 15.047 7.297 -7.880 1.00 18.50 C ANISOU 2189 CG2 ILE A 267 2361 2282 2386 126 43 19 C ATOM 2190 CD1 ILE A 267 13.602 6.992 -10.771 1.00 20.43 C ANISOU 2190 CD1 ILE A 267 2555 2680 2524 -65 14 -301 C ATOM 2191 N THR A 268 10.550 7.519 -7.508 1.00 15.92 N ANISOU 2191 N THR A 268 2078 1917 2053 -10 -6 -53 N ATOM 2192 CA THR A 268 9.222 7.547 -7.952 1.00 16.11 C ANISOU 2192 CA THR A 268 2106 2029 1984 46 103 65 C ATOM 2193 C THR A 268 9.181 8.338 -9.274 1.00 17.47 C ANISOU 2193 C THR A 268 2332 2123 2182 -15 -49 117 C ATOM 2194 O THR A 268 9.797 9.484 -9.281 1.00 20.56 O ANISOU 2194 O THR A 268 2790 2525 2494 -168 2 -38 O ATOM 2195 CB THR A 268 8.208 8.151 -6.947 1.00 17.65 C ANISOU 2195 CB THR A 268 2348 2229 2130 49 -34 -85 C ATOM 2196 OG1 THR A 268 8.202 7.246 -5.812 1.00 20.97 O ANISOU 2196 OG1 THR A 268 2755 2605 2605 -128 278 76 O ATOM 2197 CG2 THR A 268 6.858 8.289 -7.528 1.00 18.47 C ANISOU 2197 CG2 THR A 268 2421 2208 2390 -24 177 -33 C ATOM 2198 N VAL A 269 8.474 7.829 -10.247 1.00 15.98 N ANISOU 2198 N VAL A 269 2141 1944 1985 27 53 118 N ATOM 2199 CA VAL A 269 8.236 8.543 -11.489 1.00 15.61 C ANISOU 2199 CA VAL A 269 2126 1869 1933 73 66 -32 C ATOM 2200 C VAL A 269 6.760 8.482 -11.773 1.00 16.82 C ANISOU 2200 C VAL A 269 2179 2201 2011 -40 70 -74 C ATOM 2201 O VAL A 269 6.007 7.620 -11.268 1.00 18.26 O ANISOU 2201 O VAL A 269 2391 2215 2332 65 -7 -6 O ATOM 2202 CB VAL A 269 9.025 7.915 -12.678 1.00 15.84 C ANISOU 2202 CB VAL A 269 2105 1979 1934 -191 225 80 C ATOM 2203 CG1 VAL A 269 10.501 7.934 -12.339 1.00 17.43 C ANISOU 2203 CG1 VAL A 269 2299 2086 2236 168 108 -92 C ATOM 2204 CG2 VAL A 269 8.553 6.514 -13.052 1.00 18.07 C ANISOU 2204 CG2 VAL A 269 2463 2188 2214 54 -55 -24 C ATOM 2205 N LYS A 270 6.251 9.367 -12.675 1.00 15.31 N ANISOU 2205 N LYS A 270 1964 1839 2011 93 -56 -56 N ATOM 2206 CA LYS A 270 4.918 9.298 -13.168 1.00 15.61 C ANISOU 2206 CA LYS A 270 1974 1871 2085 12 133 -101 C ATOM 2207 C LYS A 270 4.718 8.071 -14.076 1.00 17.65 C ANISOU 2207 C LYS A 270 2232 2223 2248 -134 46 -79 C ATOM 2208 O LYS A 270 5.583 7.880 -14.963 1.00 17.80 O ANISOU 2208 O LYS A 270 2277 2195 2289 157 172 -32 O ATOM 2209 CB LYS A 270 4.468 10.599 -13.873 1.00 18.23 C ANISOU 2209 CB LYS A 270 2324 2351 2249 -213 75 129 C ATOM 2210 CG LYS A 270 4.431 11.766 -12.857 1.00 22.13 C ANISOU 2210 CG LYS A 270 2727 2742 2938 -57 130 -72 C ATOM 2211 CD LYS A 270 4.097 13.065 -13.541 1.00 27.91 C ANISOU 2211 CD LYS A 270 3574 3277 3753 -86 -72 66 C ATOM 2212 CE LYS A 270 4.510 14.227 -12.525 1.00 37.95 C ANISOU 2212 CE LYS A 270 4964 4629 4825 130 -113 -475 C ATOM 2213 NZ LYS A 270 4.374 15.530 -13.294 1.00 49.51 N ANISOU 2213 NZ LYS A 270 6740 5532 6540 -290 -26 248 N ATOM 2214 N GLY A 271 3.590 7.411 -14.024 1.00 16.84 N ANISOU 2214 N GLY A 271 2181 2028 2190 105 123 -27 N ATOM 2215 CA GLY A 271 3.301 6.285 -14.867 1.00 16.59 C ANISOU 2215 CA GLY A 271 2033 2110 2159 131 -30 -14 C ATOM 2216 C GLY A 271 2.258 5.441 -14.351 1.00 16.20 C ANISOU 2216 C GLY A 271 2124 1916 2115 174 -72 83 C ATOM 2217 O GLY A 271 1.971 5.479 -13.126 1.00 17.20 O ANISOU 2217 O GLY A 271 2303 2039 2190 67 116 -45 O ATOM 2218 N ALA A 272 1.633 4.639 -15.202 1.00 16.18 N ANISOU 2218 N ALA A 272 2038 2089 2019 3 132 -40 N ATOM 2219 CA ALA A 272 0.728 3.620 -14.839 1.00 17.56 C ANISOU 2219 CA ALA A 272 2396 2107 2167 83 -61 -140 C ATOM 2220 C ALA A 272 1.456 2.222 -14.797 1.00 16.64 C ANISOU 2220 C ALA A 272 2145 2109 2066 281 -69 -163 C ATOM 2221 O ALA A 272 2.130 1.922 -13.824 1.00 17.74 O ANISOU 2221 O ALA A 272 2285 2133 2321 91 25 -127 O ATOM 2222 CB ALA A 272 -0.533 3.681 -15.687 1.00 19.25 C ANISOU 2222 CB ALA A 272 2459 2253 2599 164 -120 -202 C ATOM 2223 N HIS A 273 1.276 1.466 -15.868 1.00 16.21 N ANISOU 2223 N HIS A 273 2050 2044 2063 173 -135 -45 N ATOM 2224 CA HIS A 273 2.044 0.200 -15.931 1.00 15.93 C ANISOU 2224 CA HIS A 273 2068 1942 2041 87 28 14 C ATOM 2225 C HIS A 273 3.233 0.266 -16.837 1.00 13.81 C ANISOU 2225 C HIS A 273 1712 1776 1758 -1 -65 -47 C ATOM 2226 O HIS A 273 4.348 -0.109 -16.465 1.00 15.06 O ANISOU 2226 O HIS A 273 1925 1831 1966 102 -11 12 O ATOM 2227 CB HIS A 273 1.160 -0.908 -16.394 1.00 16.24 C ANISOU 2227 CB HIS A 273 2024 2020 2126 159 -3 -18 C ATOM 2228 CG HIS A 273 1.855 -2.224 -16.354 1.00 15.70 C ANISOU 2228 CG HIS A 273 2015 1999 1949 203 -45 -59 C ATOM 2229 ND1 HIS A 273 2.353 -2.777 -15.206 1.00 15.91 N ANISOU 2229 ND1 HIS A 273 2020 1959 2067 104 127 -32 N ATOM 2230 CD2 HIS A 273 2.108 -3.094 -17.364 1.00 19.47 C ANISOU 2230 CD2 HIS A 273 2525 2418 2452 30 -220 -185 C ATOM 2231 CE1 HIS A 273 2.964 -3.943 -15.495 1.00 17.02 C ANISOU 2231 CE1 HIS A 273 2315 1954 2196 166 75 54 C ATOM 2232 NE2 HIS A 273 2.831 -4.146 -16.798 1.00 19.27 N ANISOU 2232 NE2 HIS A 273 2556 2305 2459 138 -82 -126 N ATOM 2233 N PHE A 274 3.068 0.742 -18.076 1.00 14.62 N ANISOU 2233 N PHE A 274 1839 1840 1876 19 86 106 N ATOM 2234 CA PHE A 274 4.126 0.779 -19.105 1.00 14.50 C ANISOU 2234 CA PHE A 274 1882 1700 1928 93 105 -69 C ATOM 2235 C PHE A 274 4.929 2.095 -18.926 1.00 16.03 C ANISOU 2235 C PHE A 274 2062 2039 1989 -65 7 -94 C ATOM 2236 O PHE A 274 4.973 2.970 -19.830 1.00 16.54 O ANISOU 2236 O PHE A 274 2171 2008 2104 4 18 38 O ATOM 2237 CB PHE A 274 3.599 0.616 -20.508 1.00 16.06 C ANISOU 2237 CB PHE A 274 2096 1915 2089 16 -2 86 C ATOM 2238 CG PHE A 274 2.827 -0.706 -20.694 1.00 15.15 C ANISOU 2238 CG PHE A 274 1973 1952 1829 -126 21 -17 C ATOM 2239 CD1 PHE A 274 3.518 -1.834 -20.945 1.00 17.73 C ANISOU 2239 CD1 PHE A 274 2188 2248 2299 26 105 207 C ATOM 2240 CD2 PHE A 274 1.514 -0.768 -20.489 1.00 15.81 C ANISOU 2240 CD2 PHE A 274 2050 1979 1978 47 57 -108 C ATOM 2241 CE1 PHE A 274 2.867 -3.031 -21.017 1.00 17.78 C ANISOU 2241 CE1 PHE A 274 2311 2223 2219 92 31 -207 C ATOM 2242 CE2 PHE A 274 0.808 -1.940 -20.612 1.00 17.13 C ANISOU 2242 CE2 PHE A 274 2162 2215 2129 -41 194 96 C ATOM 2243 CZ PHE A 274 1.487 -3.108 -20.874 1.00 16.73 C ANISOU 2243 CZ PHE A 274 2179 2082 2094 -77 42 -73 C ATOM 2244 N ILE A 275 5.580 2.233 -17.781 1.00 13.75 N ANISOU 2244 N ILE A 275 1791 1668 1762 15 -11 7 N ATOM 2245 CA ILE A 275 6.044 3.563 -17.317 1.00 14.30 C ANISOU 2245 CA ILE A 275 1781 1751 1899 -39 45 9 C ATOM 2246 C ILE A 275 7.212 4.021 -18.138 1.00 15.61 C ANISOU 2246 C ILE A 275 1989 1962 1978 -124 20 -98 C ATOM 2247 O ILE A 275 7.548 5.222 -18.108 1.00 15.75 O ANISOU 2247 O ILE A 275 2034 1867 2082 61 -38 76 O ATOM 2248 CB ILE A 275 6.400 3.455 -15.847 1.00 14.31 C ANISOU 2248 CB ILE A 275 1796 1787 1853 71 87 -203 C ATOM 2249 CG1 ILE A 275 7.638 2.625 -15.524 1.00 15.46 C ANISOU 2249 CG1 ILE A 275 1979 1910 1984 76 -85 -25 C ATOM 2250 CG2 ILE A 275 5.181 2.984 -15.031 1.00 16.11 C ANISOU 2250 CG2 ILE A 275 2130 1958 2030 -45 -7 26 C ATOM 2251 CD1 ILE A 275 8.049 2.724 -14.076 1.00 17.73 C ANISOU 2251 CD1 ILE A 275 2289 2109 2337 123 -52 84 C ATOM 2252 N GLN A 276 7.909 3.118 -18.872 1.00 15.11 N ANISOU 2252 N GLN A 276 1916 1884 1939 87 174 -2 N ATOM 2253 CA GLN A 276 8.959 3.515 -19.748 1.00 15.25 C ANISOU 2253 CA GLN A 276 1971 1797 2024 -84 16 -68 C ATOM 2254 C GLN A 276 8.490 4.500 -20.819 1.00 15.60 C ANISOU 2254 C GLN A 276 1989 1983 1955 79 62 -7 C ATOM 2255 O GLN A 276 9.330 5.263 -21.332 1.00 16.22 O ANISOU 2255 O GLN A 276 2038 1996 2127 66 46 -53 O ATOM 2256 CB GLN A 276 9.553 2.258 -20.469 1.00 15.65 C ANISOU 2256 CB GLN A 276 2056 1977 1910 126 55 -49 C ATOM 2257 CG GLN A 276 10.014 1.151 -19.552 1.00 16.11 C ANISOU 2257 CG GLN A 276 2218 1955 1946 69 38 -133 C ATOM 2258 CD GLN A 276 8.983 0.271 -19.017 1.00 15.44 C ANISOU 2258 CD GLN A 276 1872 1929 2066 -93 -175 -64 C ATOM 2259 OE1 GLN A 276 7.770 0.374 -19.179 1.00 15.37 O ANISOU 2259 OE1 GLN A 276 1969 1777 2094 113 4 -76 O ATOM 2260 NE2 GLN A 276 9.488 -0.815 -18.404 1.00 20.91 N ANISOU 2260 NE2 GLN A 276 2659 2453 2831 10 -258 280 N ATOM 2261 N GLU A 277 7.173 4.429 -21.162 1.00 14.44 N ANISOU 2261 N GLU A 277 1891 1805 1790 -69 21 109 N ATOM 2262 CA GLU A 277 6.625 5.354 -22.170 1.00 15.47 C ANISOU 2262 CA GLU A 277 1934 1936 2008 163 48 56 C ATOM 2263 C GLU A 277 6.324 6.698 -21.547 1.00 20.98 C ANISOU 2263 C GLU A 277 2984 2485 2500 1 35 -146 C ATOM 2264 O GLU A 277 6.251 7.707 -22.336 1.00 22.43 O ANISOU 2264 O GLU A 277 3212 2749 2560 320 82 101 O ATOM 2265 CB GLU A 277 5.445 4.779 -22.827 1.00 16.33 C ANISOU 2265 CB GLU A 277 2229 2016 1959 118 -60 -26 C ATOM 2266 CG GLU A 277 5.732 3.442 -23.543 1.00 17.52 C ANISOU 2266 CG GLU A 277 2418 2079 2157 128 112 -6 C ATOM 2267 CD GLU A 277 6.680 3.701 -24.777 1.00 19.57 C ANISOU 2267 CD GLU A 277 2393 2433 2609 -89 84 8 C ATOM 2268 OE1 GLU A 277 7.094 4.812 -25.054 1.00 17.19 O ANISOU 2268 OE1 GLU A 277 2223 2153 2153 78 46 31 O ATOM 2269 OE2 GLU A 277 6.965 2.677 -25.431 1.00 18.15 O ANISOU 2269 OE2 GLU A 277 2348 2353 2194 122 -15 -41 O ATOM 2270 N ASP A 278 6.307 6.827 -20.246 1.00 14.74 N ANISOU 2270 N ASP A 278 1955 1708 1934 71 50 7 N ATOM 2271 CA ASP A 278 5.984 8.097 -19.631 1.00 15.22 C ANISOU 2271 CA ASP A 278 2058 1769 1953 158 45 51 C ATOM 2272 C ASP A 278 7.153 8.837 -18.983 1.00 15.80 C ANISOU 2272 C ASP A 278 1999 1994 2010 25 30 48 C ATOM 2273 O ASP A 278 7.199 10.027 -19.066 1.00 18.55 O ANISOU 2273 O ASP A 278 2391 2094 2563 19 10 19 O ATOM 2274 CB ASP A 278 4.837 7.905 -18.632 1.00 15.71 C ANISOU 2274 CB ASP A 278 1996 1855 2115 59 65 -28 C ATOM 2275 CG ASP A 278 3.502 7.590 -19.312 1.00 19.03 C ANISOU 2275 CG ASP A 278 2395 2419 2416 9 24 -7 C ATOM 2276 OD1 ASP A 278 3.124 8.324 -20.197 1.00 19.50 O ANISOU 2276 OD1 ASP A 278 2490 2425 2494 7 -64 24 O ATOM 2277 OD2 ASP A 278 2.874 6.615 -18.940 1.00 18.68 O ANISOU 2277 OD2 ASP A 278 2312 2288 2498 15 -11 14 O ATOM 2278 N SER A 279 8.103 8.131 -18.390 1.00 14.31 N ANISOU 2278 N SER A 279 1859 1778 1797 50 35 -71 N ATOM 2279 CA SER A 279 9.200 8.710 -17.653 1.00 14.62 C ANISOU 2279 CA SER A 279 1875 1769 1910 71 56 75 C ATOM 2280 C SER A 279 10.528 8.088 -18.013 1.00 12.83 C ANISOU 2280 C SER A 279 1661 1538 1675 -118 8 -51 C ATOM 2281 O SER A 279 11.331 7.769 -17.172 1.00 14.61 O ANISOU 2281 O SER A 279 1929 1769 1852 33 10 40 O ATOM 2282 CB SER A 279 8.920 8.601 -16.172 1.00 15.40 C ANISOU 2282 CB SER A 279 1978 1943 1927 94 -73 -39 C ATOM 2283 OG SER A 279 7.724 9.292 -15.826 1.00 16.96 O ANISOU 2283 OG SER A 279 2153 2076 2213 -20 105 -2 O ATOM 2284 N PRO A 280 10.883 8.052 -19.319 1.00 14.14 N ANISOU 2284 N PRO A 280 1803 1755 1814 -41 21 30 N ATOM 2285 CA PRO A 280 12.161 7.453 -19.652 1.00 14.99 C ANISOU 2285 CA PRO A 280 1913 1847 1935 25 36 71 C ATOM 2286 C PRO A 280 13.386 8.086 -19.141 1.00 15.02 C ANISOU 2286 C PRO A 280 1952 1878 1875 36 22 38 C ATOM 2287 O PRO A 280 14.346 7.419 -18.871 1.00 15.29 O ANISOU 2287 O PRO A 280 1949 1953 1905 3 2 -1 O ATOM 2288 CB PRO A 280 12.098 7.407 -21.228 1.00 15.61 C ANISOU 2288 CB PRO A 280 1995 1959 1975 47 62 80 C ATOM 2289 CG PRO A 280 11.213 8.570 -21.555 1.00 15.85 C ANISOU 2289 CG PRO A 280 2158 1944 1919 23 90 -46 C ATOM 2290 CD PRO A 280 10.103 8.568 -20.499 1.00 14.88 C ANISOU 2290 CD PRO A 280 1851 1887 1915 -130 -45 -43 C ATOM 2291 N ASP A 281 13.404 9.447 -19.084 1.00 13.68 N ANISOU 2291 N ASP A 281 1761 1687 1747 16 -65 45 N ATOM 2292 CA ASP A 281 14.647 10.038 -18.714 1.00 15.39 C ANISOU 2292 CA ASP A 281 2009 1849 1990 -9 -26 70 C ATOM 2293 C ASP A 281 14.962 9.903 -17.220 1.00 13.60 C ANISOU 2293 C ASP A 281 1756 1585 1823 -51 -14 -58 C ATOM 2294 O ASP A 281 16.151 9.729 -16.853 1.00 14.57 O ANISOU 2294 O ASP A 281 1847 1775 1912 -38 24 33 O ATOM 2295 CB ASP A 281 14.676 11.530 -19.155 1.00 15.84 C ANISOU 2295 CB ASP A 281 2129 1875 2012 36 -18 103 C ATOM 2296 CG ASP A 281 14.843 11.649 -20.682 1.00 23.41 C ANISOU 2296 CG ASP A 281 3115 2933 2844 -13 104 26 C ATOM 2297 OD1 ASP A 281 15.322 10.673 -21.319 1.00 24.47 O ANISOU 2297 OD1 ASP A 281 3404 3012 2880 12 185 77 O ATOM 2298 OD2 ASP A 281 14.477 12.684 -21.180 1.00 22.59 O ANISOU 2298 OD2 ASP A 281 3123 2703 2758 -43 -227 112 O ATOM 2299 N GLU A 282 13.925 9.947 -16.357 1.00 13.07 N ANISOU 2299 N GLU A 282 1748 1586 1630 -7 -21 -47 N ATOM 2300 CA GLU A 282 14.123 9.711 -14.944 1.00 14.76 C ANISOU 2300 CA GLU A 282 2011 1709 1886 -27 8 72 C ATOM 2301 C GLU A 282 14.555 8.227 -14.730 1.00 15.41 C ANISOU 2301 C GLU A 282 2020 1807 2027 4 -43 -2 C ATOM 2302 O GLU A 282 15.390 8.000 -13.886 1.00 16.01 O ANISOU 2302 O GLU A 282 2058 1945 2079 -23 -3 -22 O ATOM 2303 CB GLU A 282 12.899 10.056 -14.164 1.00 15.85 C ANISOU 2303 CB GLU A 282 2042 1851 2127 134 69 85 C ATOM 2304 CG GLU A 282 12.649 11.577 -14.055 1.00 15.35 C ANISOU 2304 CG GLU A 282 2005 1854 1974 -115 79 18 C ATOM 2305 CD GLU A 282 11.179 11.919 -13.760 1.00 17.94 C ANISOU 2305 CD GLU A 282 2331 2107 2379 69 -95 19 C ATOM 2306 OE1 GLU A 282 10.342 11.851 -14.670 1.00 19.00 O ANISOU 2306 OE1 GLU A 282 2552 2234 2431 61 -74 -5 O ATOM 2307 OE2 GLU A 282 10.948 12.138 -12.555 1.00 18.29 O ANISOU 2307 OE2 GLU A 282 2518 2165 2263 -8 165 5 O ATOM 2308 N ILE A 283 13.890 7.358 -15.470 1.00 13.70 N ANISOU 2308 N ILE A 283 1721 1737 1744 83 -88 5 N ATOM 2309 CA ILE A 283 14.216 5.897 -15.309 1.00 13.76 C ANISOU 2309 CA ILE A 283 1795 1677 1753 -8 -17 116 C ATOM 2310 C ILE A 283 15.632 5.680 -15.720 1.00 14.64 C ANISOU 2310 C ILE A 283 1880 1852 1828 22 -62 13 C ATOM 2311 O ILE A 283 16.428 5.067 -15.018 1.00 15.35 O ANISOU 2311 O ILE A 283 1974 1846 2010 -13 -10 20 O ATOM 2312 CB ILE A 283 13.205 5.111 -16.058 1.00 13.92 C ANISOU 2312 CB ILE A 283 1833 1639 1814 35 60 -40 C ATOM 2313 CG1 ILE A 283 11.835 5.157 -15.447 1.00 15.06 C ANISOU 2313 CG1 ILE A 283 1999 1846 1876 1 25 26 C ATOM 2314 CG2 ILE A 283 13.732 3.627 -16.206 1.00 16.11 C ANISOU 2314 CG2 ILE A 283 2137 1870 2114 78 -9 -130 C ATOM 2315 CD1 ILE A 283 10.749 4.565 -16.299 1.00 17.91 C ANISOU 2315 CD1 ILE A 283 2175 2292 2338 -83 -37 -8 C ATOM 2316 N GLY A 284 15.995 6.195 -16.913 1.00 13.26 N ANISOU 2316 N GLY A 284 1666 1650 1721 58 1 27 N ATOM 2317 CA GLY A 284 17.332 6.053 -17.397 1.00 14.89 C ANISOU 2317 CA GLY A 284 1895 1796 1966 -15 152 0 C ATOM 2318 C GLY A 284 18.382 6.611 -16.508 1.00 15.05 C ANISOU 2318 C GLY A 284 1988 1930 1801 62 40 -55 C ATOM 2319 O GLY A 284 19.439 6.037 -16.234 1.00 15.57 O ANISOU 2319 O GLY A 284 1972 1931 2009 -14 -39 -4 O ATOM 2320 N ALA A 285 18.167 7.831 -15.954 1.00 14.12 N ANISOU 2320 N ALA A 285 1832 1683 1849 34 -57 51 N ATOM 2321 CA ALA A 285 19.139 8.348 -15.082 1.00 13.83 C ANISOU 2321 CA ALA A 285 1775 1722 1756 7 38 -39 C ATOM 2322 C ALA A 285 19.343 7.573 -13.779 1.00 13.27 C ANISOU 2322 C ALA A 285 1743 1492 1808 -28 -112 -96 C ATOM 2323 O ALA A 285 20.464 7.498 -13.288 1.00 15.66 O ANISOU 2323 O ALA A 285 2042 1781 2124 19 -106 -19 O ATOM 2324 CB ALA A 285 18.700 9.815 -14.671 1.00 16.10 C ANISOU 2324 CB ALA A 285 2078 1856 2180 -62 -106 64 C ATOM 2325 N ALA A 286 18.249 7.079 -13.278 1.00 14.39 N ANISOU 2325 N ALA A 286 1853 1783 1829 59 81 55 N ATOM 2326 CA ALA A 286 18.324 6.271 -12.009 1.00 15.34 C ANISOU 2326 CA ALA A 286 2016 1858 1953 63 -61 4 C ATOM 2327 C ALA A 286 19.104 4.947 -12.303 1.00 14.57 C ANISOU 2327 C ALA A 286 1963 1706 1865 -63 -126 -143 C ATOM 2328 O ALA A 286 19.884 4.553 -11.410 1.00 16.29 O ANISOU 2328 O ALA A 286 2197 1809 2183 44 -103 -9 O ATOM 2329 CB ALA A 286 16.938 5.960 -11.505 1.00 17.29 C ANISOU 2329 CB ALA A 286 2338 2003 2227 242 150 122 C ATOM 2330 N ILE A 287 18.854 4.340 -13.417 1.00 15.16 N ANISOU 2330 N ILE A 287 1993 1884 1882 114 10 66 N ATOM 2331 CA ILE A 287 19.574 3.069 -13.663 1.00 14.45 C ANISOU 2331 CA ILE A 287 1935 1747 1808 81 -17 67 C ATOM 2332 C ILE A 287 21.000 3.377 -13.896 1.00 15.76 C ANISOU 2332 C ILE A 287 2020 1968 2000 24 -11 -129 C ATOM 2333 O ILE A 287 21.920 2.677 -13.448 1.00 16.18 O ANISOU 2333 O ILE A 287 2156 1956 2035 -19 -174 -46 O ATOM 2334 CB ILE A 287 18.938 2.378 -14.851 1.00 15.96 C ANISOU 2334 CB ILE A 287 2112 1861 2088 35 -103 -103 C ATOM 2335 CG1 ILE A 287 17.500 1.988 -14.622 1.00 15.75 C ANISOU 2335 CG1 ILE A 287 2001 1993 1991 154 7 41 C ATOM 2336 CG2 ILE A 287 19.743 1.047 -15.205 1.00 16.47 C ANISOU 2336 CG2 ILE A 287 2092 1929 2236 122 11 -65 C ATOM 2337 CD1 ILE A 287 16.666 1.609 -15.834 1.00 18.95 C ANISOU 2337 CD1 ILE A 287 2450 2300 2450 -66 25 -146 C ATOM 2338 N ALA A 288 21.331 4.484 -14.632 1.00 14.17 N ANISOU 2338 N ALA A 288 1758 1723 1902 40 0 13 N ATOM 2339 CA ALA A 288 22.719 4.847 -14.852 1.00 15.12 C ANISOU 2339 CA ALA A 288 1961 1792 1991 34 53 -1 C ATOM 2340 C ALA A 288 23.437 5.142 -13.527 1.00 15.53 C ANISOU 2340 C ALA A 288 1978 1912 2008 -1 24 46 C ATOM 2341 O ALA A 288 24.578 4.719 -13.381 1.00 15.64 O ANISOU 2341 O ALA A 288 1984 1898 2059 -43 -3 33 O ATOM 2342 CB ALA A 288 22.860 6.082 -15.799 1.00 16.41 C ANISOU 2342 CB ALA A 288 1966 2090 2178 -79 -54 120 C ATOM 2343 N GLU A 289 22.812 5.814 -12.600 1.00 15.66 N ANISOU 2343 N GLU A 289 2105 1843 2000 35 -111 2 N ATOM 2344 CA GLU A 289 23.447 6.108 -11.343 1.00 16.90 C ANISOU 2344 CA GLU A 289 2253 2060 2108 107 -60 180 C ATOM 2345 C GLU A 289 23.712 4.806 -10.596 1.00 15.83 C ANISOU 2345 C GLU A 289 2014 1893 2106 32 14 60 C ATOM 2346 O GLU A 289 24.718 4.639 -10.025 1.00 17.16 O ANISOU 2346 O GLU A 289 2297 2012 2211 -70 -120 27 O ATOM 2347 CB GLU A 289 22.553 7.029 -10.494 1.00 19.58 C ANISOU 2347 CB GLU A 289 2722 2255 2462 -63 -216 -2 C ATOM 2348 CG GLU A 289 23.086 7.418 -9.114 1.00 21.43 C ANISOU 2348 CG GLU A 289 3046 2387 2709 114 -183 -73 C ATOM 2349 CD GLU A 289 22.940 6.373 -8.000 1.00 27.18 C ANISOU 2349 CD GLU A 289 3440 3466 3422 -122 125 265 C ATOM 2350 OE1 GLU A 289 22.031 5.573 -8.052 1.00 26.10 O ANISOU 2350 OE1 GLU A 289 3503 3309 3103 -106 154 -51 O ATOM 2351 OE2 GLU A 289 23.760 6.377 -7.074 1.00 30.42 O ANISOU 2351 OE2 GLU A 289 4134 3771 3652 -184 -174 -134 O ATOM 2352 N PHE A 290 22.753 3.910 -10.655 1.00 16.09 N ANISOU 2352 N PHE A 290 2118 1931 2063 90 -115 38 N ATOM 2353 CA PHE A 290 22.878 2.552 -9.932 1.00 15.43 C ANISOU 2353 CA PHE A 290 2045 1984 1831 -16 35 50 C ATOM 2354 C PHE A 290 24.028 1.790 -10.522 1.00 15.84 C ANISOU 2354 C PHE A 290 2016 1997 2004 -13 -106 -75 C ATOM 2355 O PHE A 290 24.888 1.291 -9.787 1.00 15.65 O ANISOU 2355 O PHE A 290 2019 1847 2079 -2 -125 -112 O ATOM 2356 CB PHE A 290 21.562 1.918 -10.115 1.00 14.83 C ANISOU 2356 CB PHE A 290 1904 1810 1918 9 -132 3 C ATOM 2357 CG PHE A 290 21.389 0.468 -9.574 1.00 16.38 C ANISOU 2357 CG PHE A 290 2254 2000 1968 -175 -51 106 C ATOM 2358 CD1 PHE A 290 21.556 0.227 -8.239 1.00 16.61 C ANISOU 2358 CD1 PHE A 290 2207 2037 2067 -25 -83 -43 C ATOM 2359 CD2 PHE A 290 21.008 -0.541 -10.390 1.00 16.15 C ANISOU 2359 CD2 PHE A 290 2130 2049 1955 -156 -44 114 C ATOM 2360 CE1 PHE A 290 21.287 -1.002 -7.712 1.00 16.91 C ANISOU 2360 CE1 PHE A 290 2282 2041 2100 -79 -144 121 C ATOM 2361 CE2 PHE A 290 20.784 -1.792 -9.881 1.00 15.62 C ANISOU 2361 CE2 PHE A 290 2216 1789 1928 118 -212 -116 C ATOM 2362 CZ PHE A 290 20.886 -2.018 -8.563 1.00 17.05 C ANISOU 2362 CZ PHE A 290 2377 1987 2112 127 56 44 C ATOM 2363 N VAL A 291 24.097 1.702 -11.877 1.00 15.71 N ANISOU 2363 N VAL A 291 2057 1932 1978 27 -40 -2 N ATOM 2364 CA VAL A 291 25.170 0.921 -12.503 1.00 15.76 C ANISOU 2364 CA VAL A 291 2011 1956 2020 65 -38 -34 C ATOM 2365 C VAL A 291 26.517 1.544 -12.237 1.00 18.44 C ANISOU 2365 C VAL A 291 2281 2279 2443 117 -2 -180 C ATOM 2366 O VAL A 291 27.500 0.927 -11.902 1.00 19.43 O ANISOU 2366 O VAL A 291 2541 2376 2462 31 -209 16 O ATOM 2367 CB VAL A 291 24.881 0.777 -13.975 1.00 17.58 C ANISOU 2367 CB VAL A 291 2250 2227 2203 6 125 92 C ATOM 2368 CG1 VAL A 291 26.132 0.203 -14.718 1.00 19.77 C ANISOU 2368 CG1 VAL A 291 2556 2508 2448 207 9 9 C ATOM 2369 CG2 VAL A 291 23.659 -0.047 -14.193 1.00 19.26 C ANISOU 2369 CG2 VAL A 291 2562 2414 2339 46 -168 43 C ATOM 2370 N ARG A 292 26.596 2.859 -12.334 1.00 17.00 N ANISOU 2370 N ARG A 292 2082 2095 2281 -94 -76 129 N ATOM 2371 CA ARG A 292 27.866 3.532 -12.053 1.00 17.31 C ANISOU 2371 CA ARG A 292 2158 2088 2328 -106 -116 -15 C ATOM 2372 C ARG A 292 28.347 3.263 -10.655 1.00 18.36 C ANISOU 2372 C ARG A 292 2379 2160 2434 -176 93 -38 C ATOM 2373 O ARG A 292 29.488 3.065 -10.448 1.00 21.29 O ANISOU 2373 O ARG A 292 2591 2736 2761 -55 -184 66 O ATOM 2374 CB ARG A 292 27.775 5.040 -12.220 1.00 18.50 C ANISOU 2374 CB ARG A 292 2396 2170 2463 32 -189 -24 C ATOM 2375 CG ARG A 292 27.726 5.540 -13.636 1.00 23.15 C ANISOU 2375 CG ARG A 292 3133 2644 3019 -133 -16 -170 C ATOM 2376 CD ARG A 292 27.719 7.068 -13.668 1.00 26.14 C ANISOU 2376 CD ARG A 292 3833 2806 3291 389 -203 -38 C ATOM 2377 NE ARG A 292 27.264 7.538 -14.941 1.00 24.88 N ANISOU 2377 NE ARG A 292 3586 2596 3270 -1 81 -474 N ATOM 2378 CZ ARG A 292 28.051 7.832 -15.928 1.00 21.30 C ANISOU 2378 CZ ARG A 292 2857 2381 2855 -27 99 -331 C ATOM 2379 NH1 ARG A 292 29.356 7.687 -15.782 1.00 27.05 N ANISOU 2379 NH1 ARG A 292 3329 3134 3811 -307 -361 -320 N ATOM 2380 NH2 ARG A 292 27.535 8.211 -17.074 1.00 25.00 N ANISOU 2380 NH2 ARG A 292 3170 2879 3447 -64 -100 43 N ATOM 2381 N ARG A 293 27.436 3.292 -9.723 1.00 17.65 N ANISOU 2381 N ARG A 293 2227 2233 2243 93 -124 -139 N ATOM 2382 CA ARG A 293 27.715 3.029 -8.333 1.00 19.21 C ANISOU 2382 CA ARG A 293 2616 2290 2391 21 -298 27 C ATOM 2383 C ARG A 293 28.238 1.595 -8.158 1.00 23.86 C ANISOU 2383 C ARG A 293 3094 2622 3349 49 -359 2 C ATOM 2384 O ARG A 293 29.218 1.374 -7.506 1.00 24.03 O ANISOU 2384 O ARG A 293 3083 2877 3170 -106 -390 96 O ATOM 2385 CB ARG A 293 26.447 3.294 -7.515 1.00 21.92 C ANISOU 2385 CB ARG A 293 3013 2665 2647 -157 -222 9 C ATOM 2386 CG ARG A 293 26.544 3.005 -6.039 1.00 30.28 C ANISOU 2386 CG ARG A 293 4113 3802 3590 88 -173 166 C ATOM 2387 CD ARG A 293 25.383 3.510 -5.203 1.00 31.00 C ANISOU 2387 CD ARG A 293 4131 4079 3567 456 191 6 C ATOM 2388 NE ARG A 293 24.068 3.739 -5.819 1.00 30.38 N ANISOU 2388 NE ARG A 293 3843 3839 3861 -166 342 -384 N ATOM 2389 CZ ARG A 293 22.995 2.979 -5.636 1.00 32.26 C ANISOU 2389 CZ ARG A 293 4202 3960 4094 137 -300 -382 C ATOM 2390 NH1 ARG A 293 23.072 1.868 -4.936 1.00 31.34 N ANISOU 2390 NH1 ARG A 293 4210 4164 3533 -425 212 -9 N ATOM 2391 NH2 ARG A 293 21.860 3.315 -6.196 1.00 30.38 N ANISOU 2391 NH2 ARG A 293 3831 3729 3982 -43 68 -400 N ATOM 2392 N LEU A 294 27.563 0.636 -8.767 1.00 20.38 N ANISOU 2392 N LEU A 294 2636 2479 2627 48 -362 -62 N ATOM 2393 CA LEU A 294 28.009 -0.758 -8.691 1.00 18.87 C ANISOU 2393 CA LEU A 294 2293 2406 2467 133 -321 159 C ATOM 2394 C LEU A 294 29.252 -1.050 -9.389 1.00 20.08 C ANISOU 2394 C LEU A 294 2629 2509 2491 -133 -128 77 C ATOM 2395 O LEU A 294 29.996 -1.932 -8.819 1.00 24.82 O ANISOU 2395 O LEU A 294 2978 3037 3415 96 -176 198 O ATOM 2396 CB LEU A 294 26.918 -1.686 -9.250 1.00 19.83 C ANISOU 2396 CB LEU A 294 2619 2258 2656 42 -79 -56 C ATOM 2397 CG LEU A 294 25.564 -1.648 -8.544 1.00 21.62 C ANISOU 2397 CG LEU A 294 2768 2692 2755 91 -259 -17 C ATOM 2398 CD1 LEU A 294 24.571 -2.474 -9.253 1.00 26.84 C ANISOU 2398 CD1 LEU A 294 3297 3013 3887 86 -120 -101 C ATOM 2399 CD2 LEU A 294 25.651 -1.933 -7.097 1.00 29.80 C ANISOU 2399 CD2 LEU A 294 3737 3874 3708 -162 418 372 C ATOM 2400 N ARG A 295 29.602 -0.337 -10.417 1.00 17.69 N ANISOU 2400 N ARG A 295 2216 2221 2284 2 -90 -190 N ATOM 2401 CA ARG A 295 30.773 -0.665 -11.156 1.00 19.77 C ANISOU 2401 CA ARG A 295 2481 2407 2620 -189 228 -30 C ATOM 2402 C ARG A 295 31.971 0.210 -10.970 1.00 29.98 C ANISOU 2402 C ARG A 295 3567 3981 3841 -631 -142 -649 C ATOM 2403 O ARG A 295 32.936 0.033 -11.639 1.00 44.11 O ANISOU 2403 O ARG A 295 5302 6218 5237 -875 43 -1143 O ATOM 2404 CB ARG A 295 30.405 -0.741 -12.635 1.00 20.60 C ANISOU 2404 CB ARG A 295 2664 2424 2736 -16 -122 -4 C ATOM 2405 CG ARG A 295 29.333 -1.777 -12.855 1.00 18.84 C ANISOU 2405 CG ARG A 295 2350 2363 2444 157 -55 -55 C ATOM 2406 CD ARG A 295 28.937 -2.054 -14.288 1.00 18.09 C ANISOU 2406 CD ARG A 295 2358 2310 2204 -177 -62 47 C ATOM 2407 NE ARG A 295 28.153 -3.268 -14.351 1.00 17.27 N ANISOU 2407 NE ARG A 295 2203 2212 2144 -107 -1 -76 N ATOM 2408 CZ ARG A 295 27.671 -3.801 -15.456 1.00 17.04 C ANISOU 2408 CZ ARG A 295 2113 2225 2135 28 78 69 C ATOM 2409 NH1 ARG A 295 27.835 -3.214 -16.609 1.00 16.65 N ANISOU 2409 NH1 ARG A 295 2117 2035 2173 28 -60 -14 N ATOM 2410 NH2 ARG A 295 27.036 -4.935 -15.393 1.00 17.04 N ANISOU 2410 NH2 ARG A 295 2132 2134 2206 -22 -19 -158 N ATOM 2411 N VAL A 296 31.960 1.066 -10.000 1.00 25.97 N ANISOU 2411 N VAL A 296 3190 3249 3428 -118 -81 -107 N ATOM 2412 CA VAL A 296 33.156 2.035 -9.868 1.00 37.75 C ANISOU 2412 CA VAL A 296 4716 4627 5000 -552 -417 -340 C ATOM 2413 C VAL A 296 34.584 1.417 -9.669 1.00 42.63 C ANISOU 2413 C VAL A 296 5314 5138 5746 443 -685 -406 C ATOM 2414 O VAL A 296 34.581 0.646 -8.733 1.00 45.55 O ANISOU 2414 O VAL A 296 5762 5810 5733 1176 -1011 184 O ATOM 2415 CB VAL A 296 32.839 2.909 -8.684 1.00 38.06 C ANISOU 2415 CB VAL A 296 4816 4811 4831 -357 -611 16 C ATOM 2416 CG1 VAL A 296 31.725 3.825 -9.072 1.00 58.89 C ANISOU 2416 CG1 VAL A 296 7195 7030 8148 -394 -759 -511 C ATOM 2417 CG2 VAL A 296 32.587 2.073 -7.372 1.00 54.80 C ANISOU 2417 CG2 VAL A 296 7032 7606 6183 -517 366 361 C TER 2418 VAL A 296 HETATM 2419 CL CL A 401 -0.155 -10.373 -18.728 1.00 18.13 CL ANISOU 2419 CL CL A 401 2250 2308 2329 22 50 31 CL HETATM 2420 NA NA A 402 16.881 -9.219 -22.412 1.00 21.47 NA ANISOU 2420 NA NA A 402 2749 2779 2629 -3 9 -69 NA HETATM 2421 NA NA A 403 13.680 -6.862 -23.673 1.00 20.63 NA ANISOU 2421 NA NA A 403 2670 2602 2564 -9 17 -24 NA HETATM 2422 NA NA A 404 10.770 -16.318 -24.355 1.00 21.75 NA ANISOU 2422 NA NA A 404 2769 2670 2826 -58 69 69 NA HETATM 2423 NA NA A 405 2.979 -15.833 -23.636 1.00 22.58 NA ANISOU 2423 NA NA A 405 2866 2742 2970 -3 -54 -60 NA HETATM 2424 C1 AEDO A 406 -2.171 -3.228 -17.250 0.50 15.97 C ANISOU 2424 C1 AEDO A 406 1913 1975 2177 -151 -139 85 C HETATM 2425 C1 BEDO A 406 -1.832 -4.210 -15.507 0.50 14.79 C ANISOU 2425 C1 BEDO A 406 1804 1845 1970 -237 14 -215 C HETATM 2426 O1 AEDO A 406 -2.979 -2.507 -16.312 0.50 25.75 O ANISOU 2426 O1 AEDO A 406 3161 2994 3626 191 -86 121 O HETATM 2427 O1 BEDO A 406 -1.555 -4.118 -17.097 0.50 20.39 O ANISOU 2427 O1 BEDO A 406 2651 2400 2696 429 296 -508 O HETATM 2428 C2 AEDO A 406 -1.482 -4.388 -16.540 0.50 18.77 C ANISOU 2428 C2 AEDO A 406 2764 2462 1906 11 253 345 C HETATM 2429 C2 BEDO A 406 -2.728 -3.132 -15.114 0.50 17.31 C ANISOU 2429 C2 BEDO A 406 2068 2324 2183 -305 106 -38 C HETATM 2430 O2 AEDO A 406 -0.774 -5.181 -17.499 0.50 19.57 O ANISOU 2430 O2 AEDO A 406 2177 2307 2950 -29 -174 -134 O HETATM 2431 O2 BEDO A 406 -3.304 -2.348 -16.314 0.50 28.57 O ANISOU 2431 O2 BEDO A 406 3345 3068 4441 378 -255 424 O HETATM 2432 O HOH A 501 -2.428 -25.085 -11.028 0.50 32.43 O ANISOU 2432 O HOH A 501 3862 4262 4198 -671 470 600 O HETATM 2433 O HOH A 502 7.303 -16.365 -0.382 1.00 44.57 O ANISOU 2433 O HOH A 502 6231 5853 4848 -276 358 -281 O HETATM 2434 O HOH A 503 -5.246 -5.152 -33.960 1.00 28.13 O ANISOU 2434 O HOH A 503 3418 3661 3606 167 -225 461 O HETATM 2435 O HOH A 504 -2.047 5.954 -30.347 1.00 34.08 O ANISOU 2435 O HOH A 504 4409 4063 4476 55 -217 316 O HETATM 2436 O HOH A 505 11.603 -23.368 -11.751 1.00 42.68 O ANISOU 2436 O HOH A 505 6584 4269 5362 1194 -1263 698 O HETATM 2437 O HOH A 506 32.833 -9.874 -15.467 1.00 39.69 O ANISOU 2437 O HOH A 506 4638 4776 5666 640 -209 616 O HETATM 2438 O HOH A 507 4.100 -5.396 -19.353 1.00 32.95 O ANISOU 2438 O HOH A 507 4315 4323 3882 159 44 -284 O HETATM 2439 O HOH A 508 -13.069 -3.929 -14.191 1.00 34.62 O ANISOU 2439 O HOH A 508 3695 4497 4962 611 -66 -345 O HETATM 2440 O HOH A 509 15.744 0.842 1.077 1.00 36.83 O ANISOU 2440 O HOH A 509 5214 4343 4435 383 -46 -165 O HETATM 2441 O HOH A 510 -3.277 -1.641 -8.161 1.00 38.27 O ANISOU 2441 O HOH A 510 4592 5562 4387 -248 122 -16 O HETATM 2442 O HOH A 511 29.650 -17.404 -16.104 1.00 43.09 O ANISOU 2442 O HOH A 511 5140 5071 6158 730 -617 -461 O HETATM 2443 O HOH A 512 15.080 -21.217 -3.736 1.00 39.32 O ANISOU 2443 O HOH A 512 5335 4681 4923 142 -89 206 O HETATM 2444 O HOH A 513 7.648 -25.233 -35.027 1.00 40.07 O ANISOU 2444 O HOH A 513 4937 5374 4911 -1111 -278 -1012 O HETATM 2445 O HOH A 514 7.408 9.450 -29.371 1.00 32.15 O ANISOU 2445 O HOH A 514 4243 3755 4214 46 92 309 O HETATM 2446 O HOH A 515 -14.945 -10.483 -16.851 1.00 33.43 O ANISOU 2446 O HOH A 515 3521 4620 4559 -65 79 -346 O HETATM 2447 O HOH A 516 19.554 5.523 -8.746 1.00 26.90 O ANISOU 2447 O HOH A 516 3591 3748 2881 -327 62 -407 O HETATM 2448 O HOH A 517 -5.863 0.849 -30.000 1.00 32.91 O ANISOU 2448 O HOH A 517 3995 4034 4474 225 -141 626 O HETATM 2449 O HOH A 518 9.937 -26.096 -16.193 1.00 27.54 O ANISOU 2449 O HOH A 518 3463 3278 3720 138 -180 137 O HETATM 2450 O HOH A 519 6.969 -4.361 -29.896 1.00 24.64 O ANISOU 2450 O HOH A 519 2906 3119 3334 -82 107 372 O HETATM 2451 O HOH A 520 10.077 7.131 -4.019 1.00 28.67 O ANISOU 2451 O HOH A 520 4171 3354 3366 146 -299 160 O HETATM 2452 O HOH A 521 14.268 -1.294 1.716 1.00 44.03 O ANISOU 2452 O HOH A 521 5873 5053 5801 108 -610 -1003 O HETATM 2453 O HOH A 522 2.574 -20.373 -35.365 1.00 36.16 O ANISOU 2453 O HOH A 522 4583 4446 4709 -411 -1352 643 O HETATM 2454 O HOH A 523 10.090 -10.297 -37.626 1.00 37.87 O ANISOU 2454 O HOH A 523 4800 5391 4195 -568 -1055 -1946 O HETATM 2455 O HOH A 524 6.614 -24.658 -14.375 1.00 43.94 O ANISOU 2455 O HOH A 524 5674 6115 4905 481 764 418 O HETATM 2456 O HOH A 525 -0.824 4.193 -6.293 1.00 33.21 O ANISOU 2456 O HOH A 525 4530 4181 3908 1364 141 -284 O HETATM 2457 O HOH A 526 -3.898 -21.077 -22.228 1.00 29.75 O ANISOU 2457 O HOH A 526 4085 3579 3637 214 400 173 O HETATM 2458 O HOH A 527 11.715 -20.691 -37.424 1.00 39.77 O ANISOU 2458 O HOH A 527 6153 4186 4772 -160 -977 -940 O HETATM 2459 O HOH A 528 5.948 8.926 -34.161 1.00 43.14 O ANISOU 2459 O HOH A 528 5379 4814 6198 448 360 270 O HETATM 2460 O HOH A 529 28.456 -9.368 -9.283 1.00 38.17 O ANISOU 2460 O HOH A 529 4512 5579 4412 766 -59 184 O HETATM 2461 O HOH A 530 25.898 -12.064 -7.096 1.00 32.79 O ANISOU 2461 O HOH A 530 4542 3693 4222 -48 -88 77 O HETATM 2462 O HOH A 531 26.826 -19.063 -27.882 1.00 41.20 O ANISOU 2462 O HOH A 531 5239 4806 5609 -219 1290 -829 O HETATM 2463 O HOH A 532 -4.814 -5.548 -2.015 1.00 38.61 O ANISOU 2463 O HOH A 532 4624 5329 4715 -74 -143 -89 O HETATM 2464 O HOH A 533 -4.643 -19.739 -15.843 1.00 36.79 O ANISOU 2464 O HOH A 533 4282 4829 4866 -983 463 272 O HETATM 2465 O HOH A 534 7.683 -21.925 -3.843 1.00 30.54 O ANISOU 2465 O HOH A 534 4441 3582 3578 -197 129 549 O HETATM 2466 O HOH A 535 2.073 -17.908 -32.248 1.00 22.85 O ANISOU 2466 O HOH A 535 2769 3058 2853 10 -99 43 O HETATM 2467 O HOH A 536 28.019 -6.084 -27.656 1.00 28.07 O ANISOU 2467 O HOH A 536 3312 3702 3650 -279 393 -313 O HETATM 2468 O HOH A 537 29.451 -3.942 -7.198 1.00 36.71 O ANISOU 2468 O HOH A 537 4900 4410 4636 36 160 747 O HETATM 2469 O HOH A 538 -2.209 5.900 -24.089 1.00 26.78 O ANISOU 2469 O HOH A 538 3343 3366 3464 -32 -343 384 O HETATM 2470 O HOH A 539 -2.203 -23.917 -34.349 1.00 41.51 O ANISOU 2470 O HOH A 539 5472 5153 5146 -467 -241 -627 O HETATM 2471 O HOH A 540 21.913 6.646 -28.491 1.00 44.06 O ANISOU 2471 O HOH A 540 6333 5491 4915 -590 178 1004 O HETATM 2472 O HOH A 541 21.737 -8.573 -37.368 1.00 32.02 O ANISOU 2472 O HOH A 541 4171 4105 3889 106 344 267 O HETATM 2473 O HOH A 542 25.067 -19.521 -11.250 1.00 28.52 O ANISOU 2473 O HOH A 542 3515 3530 3790 334 -244 85 O HETATM 2474 O HOH A 543 3.474 10.947 -19.992 1.00 23.75 O ANISOU 2474 O HOH A 543 2994 2851 3178 288 -283 93 O HETATM 2475 O HOH A 544 11.955 -2.684 -32.770 1.00 22.42 O ANISOU 2475 O HOH A 544 2884 2812 2820 89 -243 14 O HETATM 2476 O HOH A 545 9.358 -14.825 -37.545 1.00 28.59 O ANISOU 2476 O HOH A 545 3852 3651 3357 200 -32 135 O HETATM 2477 O HOH A 546 2.916 -6.667 -8.319 1.00 36.10 O ANISOU 2477 O HOH A 546 4434 4207 5075 401 1220 1201 O HETATM 2478 O HOH A 547 16.774 5.447 -28.752 1.00 29.12 O ANISOU 2478 O HOH A 547 3827 3881 3354 -202 206 739 O HETATM 2479 O HOH A 548 20.920 -22.854 -11.098 1.00 36.98 O ANISOU 2479 O HOH A 548 4684 3963 5402 718 -619 -135 O HETATM 2480 O HOH A 549 0.897 10.636 -11.941 1.00 32.51 O ANISOU 2480 O HOH A 549 3977 3503 4871 952 614 485 O HETATM 2481 O HOH A 550 22.491 -5.135 -31.415 1.00 20.96 O ANISOU 2481 O HOH A 550 2710 2789 2464 -172 243 101 O HETATM 2482 O HOH A 551 17.317 4.990 -31.724 1.00 44.76 O ANISOU 2482 O HOH A 551 5948 4606 6450 -265 -58 82 O HETATM 2483 O HOH A 552 5.239 1.563 1.833 1.00 35.37 O ANISOU 2483 O HOH A 552 4716 3736 4984 15 1085 -206 O HETATM 2484 O HOH A 553 7.433 -4.755 -32.510 1.00 28.89 O ANISOU 2484 O HOH A 553 3422 3843 3709 141 -188 193 O HETATM 2485 O HOH A 554 1.502 -18.110 -34.854 1.00 28.31 O ANISOU 2485 O HOH A 554 3547 3608 3600 -112 -187 78 O HETATM 2486 O HOH A 555 30.579 0.463 -16.216 1.00 32.86 O ANISOU 2486 O HOH A 555 4242 4110 4131 -517 -691 36 O HETATM 2487 O HOH A 556 -6.786 -20.592 -32.959 1.00 30.97 O ANISOU 2487 O HOH A 556 3742 4125 3901 -301 -417 -164 O HETATM 2488 O HOH A 557 22.235 9.484 -13.587 1.00 23.24 O ANISOU 2488 O HOH A 557 3197 2669 2962 -200 59 32 O HETATM 2489 O HOH A 558 17.361 2.016 -34.880 1.00 40.48 O ANISOU 2489 O HOH A 558 5777 5108 4496 -1397 426 -428 O HETATM 2490 O HOH A 559 1.241 -3.918 3.872 1.00 33.93 O ANISOU 2490 O HOH A 559 4705 4062 4123 -123 956 63 O HETATM 2491 O HOH A 560 7.585 -1.471 3.438 1.00 32.36 O ANISOU 2491 O HOH A 560 3942 4701 3650 -301 314 -848 O HETATM 2492 O HOH A 561 -8.380 -22.217 -24.297 1.00 36.63 O ANISOU 2492 O HOH A 561 4378 4221 5318 -226 -107 577 O HETATM 2493 O HOH A 562 -3.047 -3.688 -1.266 1.00 46.50 O ANISOU 2493 O HOH A 562 4829 5481 7358 -1051 -225 391 O HETATM 2494 O HOH A 563 6.396 2.440 -36.717 1.00 33.05 O ANISOU 2494 O HOH A 563 4366 4205 3986 414 519 -145 O HETATM 2495 O HOH A 564 14.636 -21.928 -7.148 1.00 45.73 O ANISOU 2495 O HOH A 564 5195 5128 7051 576 -294 -970 O HETATM 2496 O HOH A 565 -11.781 -15.549 -14.852 1.00 40.87 O ANISOU 2496 O HOH A 565 5514 5139 4874 459 1680 196 O HETATM 2497 O HOH A 566 28.354 -9.468 -28.066 1.00 37.49 O ANISOU 2497 O HOH A 566 4307 5174 4763 -337 255 -517 O HETATM 2498 O HOH A 567 -12.175 -20.530 -25.646 1.00 36.13 O ANISOU 2498 O HOH A 567 4614 4331 4782 -540 -74 69 O HETATM 2499 O HOH A 568 18.913 -6.297 -37.838 1.00 31.23 O ANISOU 2499 O HOH A 568 4411 4096 3356 -84 -308 338 O HETATM 2500 O HOH A 569 25.629 -11.264 -29.764 1.00 20.38 O ANISOU 2500 O HOH A 569 2600 2507 2635 -65 41 -272 O HETATM 2501 O HOH A 570 6.722 -24.260 -9.750 1.00 33.57 O ANISOU 2501 O HOH A 570 4690 3382 4683 242 -671 362 O HETATM 2502 O HOH A 571 -1.394 5.490 -26.586 1.00 29.68 O ANISOU 2502 O HOH A 571 3736 3612 3925 -373 247 -121 O HETATM 2503 O HOH A 572 12.292 -21.518 -10.217 1.00 27.62 O ANISOU 2503 O HOH A 572 3836 3087 3569 -35 336 322 O HETATM 2504 O HOH A 573 1.755 -12.566 -1.794 1.00 29.74 O ANISOU 2504 O HOH A 573 4028 3903 3366 -81 61 334 O HETATM 2505 O HOH A 574 10.352 -4.936 -31.486 1.00 26.99 O ANISOU 2505 O HOH A 574 3814 3684 2756 252 427 226 O HETATM 2506 O HOH A 575 27.348 -15.488 -27.835 1.00 32.60 O ANISOU 2506 O HOH A 575 4002 3596 4787 10 1025 618 O HETATM 2507 O HOH A 576 20.210 -23.645 -32.003 1.00 23.39 O ANISOU 2507 O HOH A 576 3034 2765 3088 130 65 -16 O HETATM 2508 O HOH A 577 -2.986 2.598 -13.174 1.00 38.72 O ANISOU 2508 O HOH A 577 4453 5185 5072 205 35 -307 O HETATM 2509 O HOH A 578 34.417 -6.760 -15.262 1.00 40.53 O ANISOU 2509 O HOH A 578 4335 5174 5888 -99 -571 -491 O HETATM 2510 O HOH A 579 0.914 -11.140 -36.980 1.00 27.96 O ANISOU 2510 O HOH A 579 3613 3553 3454 281 45 30 O HETATM 2511 O HOH A 580 6.963 -0.037 -9.845 1.00 16.89 O ANISOU 2511 O HOH A 580 2324 1983 2108 -64 183 -110 O HETATM 2512 O HOH A 581 26.802 -6.408 -6.365 1.00 28.43 O ANISOU 2512 O HOH A 581 3367 4077 3357 229 -583 -121 O HETATM 2513 O HOH A 582 13.217 -18.884 -1.560 1.00 30.59 O ANISOU 2513 O HOH A 582 4146 3676 3799 -47 -262 834 O HETATM 2514 O HOH A 583 -1.073 -22.353 -5.402 1.00 35.94 O ANISOU 2514 O HOH A 583 4995 4341 4319 -535 40 675 O HETATM 2515 O HOH A 584 2.936 -19.802 -2.362 1.00 48.84 O ANISOU 2515 O HOH A 584 6547 6843 5165 -37 501 -93 O HETATM 2516 O HOH A 585 -9.173 -10.544 -3.899 1.00 38.49 O ANISOU 2516 O HOH A 585 4818 5134 4672 26 1049 34 O HETATM 2517 O HOH A 586 12.025 -14.294 3.218 1.00 32.29 O ANISOU 2517 O HOH A 586 4560 4441 3266 -113 150 223 O HETATM 2518 O HOH A 587 4.446 -5.597 -29.303 1.00 16.65 O ANISOU 2518 O HOH A 587 2258 2000 2069 -34 -13 49 O HETATM 2519 O HOH A 588 0.816 -23.108 -15.802 1.00 33.75 O ANISOU 2519 O HOH A 588 4351 4205 4264 337 542 -58 O HETATM 2520 O HOH A 589 14.108 6.339 -29.807 1.00 25.53 O ANISOU 2520 O HOH A 589 3481 3017 3201 -257 221 247 O HETATM 2521 O HOH A 590 -0.725 2.929 -35.815 1.00 39.66 O ANISOU 2521 O HOH A 590 4617 4892 5561 438 -336 -27 O HETATM 2522 O HOH A 591 13.847 15.266 -20.540 1.00 16.82 O ANISOU 2522 O HOH A 591 2290 2081 2017 -152 -53 178 O HETATM 2523 O HOH A 592 8.159 -19.063 0.563 1.00 46.39 O ANISOU 2523 O HOH A 592 6130 5080 6415 -929 -1005 872 O HETATM 2524 O HOH A 593 11.787 3.564 -23.794 1.00 15.21 O ANISOU 2524 O HOH A 593 1994 1771 2013 109 121 14 O HETATM 2525 O HOH A 594 -15.633 -14.338 -19.377 1.00 37.51 O ANISOU 2525 O HOH A 594 4264 5178 4809 125 278 -3 O HETATM 2526 O HOH A 595 2.679 4.145 -17.760 1.00 17.23 O ANISOU 2526 O HOH A 595 2190 2151 2202 105 74 68 O HETATM 2527 O HOH A 596 23.947 -13.335 -33.188 1.00 25.05 O ANISOU 2527 O HOH A 596 3060 3288 3168 12 290 -313 O HETATM 2528 O HOH A 597 6.173 -5.136 -20.765 1.00 18.45 O ANISOU 2528 O HOH A 597 2569 2270 2170 224 77 16 O HETATM 2529 O HOH A 598 25.069 7.785 -18.847 1.00 24.42 O ANISOU 2529 O HOH A 598 2827 3054 3395 -174 190 -400 O HETATM 2530 O HOH A 599 28.814 -16.646 -19.069 1.00 22.64 O ANISOU 2530 O HOH A 599 2917 2662 3022 263 -180 -86 O HETATM 2531 O HOH A 600 3.817 -23.657 -23.028 1.00 17.71 O ANISOU 2531 O HOH A 600 2291 2195 2243 -126 51 16 O HETATM 2532 O HOH A 601 9.043 -25.532 -27.778 1.00 23.91 O ANISOU 2532 O HOH A 601 3031 2801 3250 -59 55 302 O HETATM 2533 O HOH A 602 -3.745 -8.587 -27.813 1.00 17.86 O ANISOU 2533 O HOH A 602 2221 2180 2385 33 -138 23 O HETATM 2534 O HOH A 603 -1.140 10.138 -9.398 1.00 42.96 O ANISOU 2534 O HOH A 603 5828 4902 5590 488 446 -863 O HETATM 2535 O HOH A 604 25.447 -16.440 -19.972 1.00 16.87 O ANISOU 2535 O HOH A 604 2231 2032 2146 -43 -19 -137 O HETATM 2536 O HOH A 605 21.399 -13.263 -2.560 1.00 27.65 O ANISOU 2536 O HOH A 605 3508 3467 3531 -172 -252 173 O HETATM 2537 O HOH A 606 31.653 -3.393 -17.814 1.00 39.35 O ANISOU 2537 O HOH A 606 5571 4784 4595 -2090 -131 -386 O HETATM 2538 O HOH A 607 -13.827 -9.692 -27.506 1.00 45.73 O ANISOU 2538 O HOH A 607 5361 6166 5847 633 -353 316 O HETATM 2539 O HOH A 608 5.934 -8.025 -29.176 1.00 15.32 O ANISOU 2539 O HOH A 608 1987 1920 1911 31 -113 80 O HETATM 2540 O HOH A 609 15.342 -0.866 -26.931 1.00 15.78 O ANISOU 2540 O HOH A 609 2054 1893 2049 -86 198 5 O HETATM 2541 O HOH A 610 22.474 -21.120 -30.695 1.00 25.86 O ANISOU 2541 O HOH A 610 3172 2962 3691 264 24 296 O HETATM 2542 O HOH A 611 9.699 -24.389 -31.364 1.00 27.55 O ANISOU 2542 O HOH A 611 3430 3704 3331 -122 -121 -97 O HETATM 2543 O HOH A 612 11.567 -25.252 -33.145 1.00 27.16 O ANISOU 2543 O HOH A 612 3714 3164 3441 -46 -179 94 O HETATM 2544 O HOH A 613 -13.416 -16.992 -26.961 1.00 25.91 O ANISOU 2544 O HOH A 613 2832 3390 3620 -440 -94 141 O HETATM 2545 O HOH A 614 27.735 0.577 -24.025 1.00 22.44 O ANISOU 2545 O HOH A 614 3018 2599 2908 -134 235 -138 O HETATM 2546 O HOH A 615 10.881 -21.896 -7.949 1.00 31.37 O ANISOU 2546 O HOH A 615 4314 3873 3730 42 -144 275 O HETATM 2547 O HOH A 616 17.663 -14.302 0.819 1.00 33.75 O ANISOU 2547 O HOH A 616 4587 3843 4392 50 -278 634 O HETATM 2548 O HOH A 617 -16.043 -16.009 -26.662 1.00 36.75 O ANISOU 2548 O HOH A 617 3625 5225 5112 -197 176 744 O HETATM 2549 O HOH A 618 19.231 -23.320 -12.926 1.00 32.95 O ANISOU 2549 O HOH A 618 4273 3839 4407 370 -360 464 O HETATM 2550 O HOH A 619 4.358 -22.289 -16.793 1.00 19.91 O ANISOU 2550 O HOH A 619 2433 2452 2681 -51 149 157 O HETATM 2551 O HOH A 620 16.501 -22.999 -20.921 1.00 17.75 O ANISOU 2551 O HOH A 620 2175 2268 2301 83 -42 49 O HETATM 2552 O HOH A 621 4.503 1.103 -9.138 1.00 17.46 O ANISOU 2552 O HOH A 621 2317 2029 2287 58 138 -13 O HETATM 2553 O HOH A 622 20.748 -0.036 -4.182 1.00 27.47 O ANISOU 2553 O HOH A 622 3526 3362 3546 -150 142 -360 O HETATM 2554 O HOH A 623 14.318 -0.457 -29.547 1.00 16.38 O ANISOU 2554 O HOH A 623 2196 2008 2019 -7 52 133 O HETATM 2555 O HOH A 624 7.110 -12.177 -33.252 1.00 18.96 O ANISOU 2555 O HOH A 624 2313 2373 2516 -25 -137 21 O HETATM 2556 O HOH A 625 16.079 9.804 -11.858 1.00 23.03 O ANISOU 2556 O HOH A 625 2975 2856 2918 -331 30 -353 O HETATM 2557 O HOH A 626 30.464 -12.556 -23.887 1.00 39.04 O ANISOU 2557 O HOH A 626 4823 4449 5559 -307 448 8 O HETATM 2558 O HOH A 627 -7.248 1.850 -23.993 1.00 32.83 O ANISOU 2558 O HOH A 627 3754 4267 4451 25 -544 -124 O HETATM 2559 O HOH A 628 29.189 -10.211 -16.280 1.00 22.36 O ANISOU 2559 O HOH A 628 2978 2548 2969 -100 -300 77 O HETATM 2560 O HOH A 629 17.155 -3.871 -36.183 1.00 34.53 O ANISOU 2560 O HOH A 629 4663 4419 4036 890 -513 59 O HETATM 2561 O HOH A 630 2.015 -2.656 -37.747 1.00 22.49 O ANISOU 2561 O HOH A 630 2960 2895 2688 124 -281 70 O HETATM 2562 O HOH A 631 6.101 11.701 -21.038 1.00 28.30 O ANISOU 2562 O HOH A 631 3647 3378 3726 -130 148 39 O HETATM 2563 O HOH A 632 7.685 11.631 -13.779 1.00 26.00 O ANISOU 2563 O HOH A 632 3139 2974 3764 74 330 82 O HETATM 2564 O HOH A 633 -7.029 -17.547 -10.502 1.00 28.92 O ANISOU 2564 O HOH A 633 3318 4053 3615 -292 197 364 O HETATM 2565 O HOH A 634 2.717 -5.913 2.378 1.00 31.45 O ANISOU 2565 O HOH A 634 3873 4109 3966 -149 419 301 O HETATM 2566 O HOH A 635 31.229 -4.791 -13.295 1.00 29.10 O ANISOU 2566 O HOH A 635 3371 3596 4090 -8 -90 -178 O HETATM 2567 O HOH A 636 13.244 -5.115 -36.526 1.00 34.88 O ANISOU 2567 O HOH A 636 4917 4079 4256 -583 853 472 O HETATM 2568 O HOH A 637 -3.475 10.020 -18.950 1.00 39.45 O ANISOU 2568 O HOH A 637 4580 5395 5014 909 166 -217 O HETATM 2569 O HOH A 638 26.399 6.853 -9.516 1.00 25.13 O ANISOU 2569 O HOH A 638 3317 2808 3422 -49 -348 -92 O HETATM 2570 O HOH A 639 1.776 -23.061 -5.762 1.00 29.63 O ANISOU 2570 O HOH A 639 4151 3505 3602 -575 30 710 O HETATM 2571 O HOH A 640 12.300 -18.448 -8.446 1.00 20.31 O ANISOU 2571 O HOH A 640 2808 2381 2525 181 -114 122 O HETATM 2572 O HOH A 641 -0.752 -26.182 -29.805 1.00 35.13 O ANISOU 2572 O HOH A 641 4366 4375 4605 -563 192 -383 O HETATM 2573 O HOH A 642 -4.526 -11.452 -41.222 1.00 34.28 O ANISOU 2573 O HOH A 642 4270 4924 3827 248 -25 -90 O HETATM 2574 O HOH A 643 -2.291 -15.314 -36.489 1.00 24.93 O ANISOU 2574 O HOH A 643 3019 3393 3057 -46 -250 293 O HETATM 2575 O HOH A 644 31.534 3.242 -12.403 1.00 34.50 O ANISOU 2575 O HOH A 644 4175 4531 4403 -153 -23 13 O HETATM 2576 O HOH A 645 -4.997 -0.753 -19.340 1.00 24.13 O ANISOU 2576 O HOH A 645 3053 2953 3159 -158 419 -291 O HETATM 2577 O HOH A 646 0.612 -22.158 -35.198 1.00 32.34 O ANISOU 2577 O HOH A 646 4647 3963 3675 288 -70 6 O HETATM 2578 O HOH A 647 1.840 -10.591 -41.482 1.00 29.92 O ANISOU 2578 O HOH A 647 3594 4053 3721 237 108 726 O HETATM 2579 O HOH A 648 3.309 -9.043 -7.530 1.00 24.56 O ANISOU 2579 O HOH A 648 3041 3138 3150 21 359 486 O HETATM 2580 O HOH A 649 12.564 1.136 -1.273 1.00 28.74 O ANISOU 2580 O HOH A 649 3743 3673 3503 94 278 59 O HETATM 2581 O HOH A 650 16.070 -2.510 -32.203 1.00 19.08 O ANISOU 2581 O HOH A 650 2585 2255 2406 -88 167 -38 O HETATM 2582 O HOH A 651 9.713 5.510 -24.151 1.00 17.56 O ANISOU 2582 O HOH A 651 2299 2128 2244 14 118 104 O HETATM 2583 O HOH A 652 16.096 8.374 -26.881 1.00 31.29 O ANISOU 2583 O HOH A 652 4008 3602 4276 -190 334 538 O HETATM 2584 O HOH A 653 32.183 -12.474 -15.435 1.00 29.91 O ANISOU 2584 O HOH A 653 3311 3734 4320 257 -254 182 O HETATM 2585 O HOH A 654 0.577 10.015 -34.434 1.00 32.90 O ANISOU 2585 O HOH A 654 4598 3782 4120 750 -253 284 O HETATM 2586 O HOH A 655 19.325 -2.974 3.733 1.00 30.63 O ANISOU 2586 O HOH A 655 4065 4367 3206 -217 -366 -412 O HETATM 2587 O HOH A 656 23.427 -21.701 -10.908 1.00 43.34 O ANISOU 2587 O HOH A 656 5799 5592 5073 724 99 770 O HETATM 2588 O HOH A 657 21.394 0.180 -1.605 1.00 36.00 O ANISOU 2588 O HOH A 657 4773 3991 4911 -67 -103 168 O HETATM 2589 O HOH A 658 -8.695 -16.410 -12.834 1.00 30.91 O ANISOU 2589 O HOH A 658 3431 4137 4176 -537 397 147 O HETATM 2590 O HOH A 659 25.403 0.757 -3.685 1.00 45.72 O ANISOU 2590 O HOH A 659 6123 5901 5347 -671 -38 -65 O HETATM 2591 O HOH A 660 29.701 5.916 -20.255 1.00 37.88 O ANISOU 2591 O HOH A 660 4810 4475 5107 -287 139 188 O HETATM 2592 O HOH A 661 15.768 12.786 -23.741 1.00 26.04 O ANISOU 2592 O HOH A 661 3593 3263 3037 -214 -144 309 O HETATM 2593 O HOH A 662 23.479 -18.984 -18.318 1.00 17.68 O ANISOU 2593 O HOH A 662 2242 2292 2184 -24 -67 -107 O HETATM 2594 O HOH A 663 18.150 -24.609 -33.603 1.00 21.98 O ANISOU 2594 O HOH A 663 2761 2602 2988 10 13 99 O HETATM 2595 O HOH A 664 1.808 1.112 -1.337 1.00 28.47 O ANISOU 2595 O HOH A 664 3661 3683 3470 136 183 -202 O HETATM 2596 O HOH A 665 32.423 1.493 -18.147 1.00 43.38 O ANISOU 2596 O HOH A 665 5325 5757 5399 -209 -10 117 O HETATM 2597 O HOH A 666 -3.566 -19.083 -24.137 1.00 19.65 O ANISOU 2597 O HOH A 666 2392 2584 2488 -86 -8 -183 O HETATM 2598 O HOH A 667 7.173 -24.715 -31.737 1.00 22.57 O ANISOU 2598 O HOH A 667 2916 2573 3085 213 -86 -109 O HETATM 2599 O HOH A 668 0.980 -7.344 -19.072 1.00 30.48 O ANISOU 2599 O HOH A 668 3703 3813 4062 -113 -28 2 O HETATM 2600 O HOH A 669 -1.671 -16.211 -5.907 1.00 27.95 O ANISOU 2600 O HOH A 669 3553 3570 3496 -615 153 122 O HETATM 2601 O HOH A 670 24.736 8.921 -15.167 1.00 24.82 O ANISOU 2601 O HOH A 670 3199 2958 3272 -262 -203 43 O HETATM 2602 O HOH A 671 25.777 -7.096 -1.538 1.00 36.46 O ANISOU 2602 O HOH A 671 4557 4828 4467 36 -485 486 O HETATM 2603 O HOH A 672 20.250 3.579 -31.875 1.00 36.54 O ANISOU 2603 O HOH A 672 4754 4262 4866 -832 670 475 O HETATM 2604 O HOH A 673 -7.858 -22.077 -28.683 1.00 27.89 O ANISOU 2604 O HOH A 673 3159 3437 3999 -449 -295 -165 O HETATM 2605 O HOH A 674 7.696 -16.967 -37.006 1.00 23.21 O ANISOU 2605 O HOH A 674 3010 3192 2614 -168 -126 -102 O HETATM 2606 O HOH A 675 -6.319 -1.445 -35.033 1.00 34.39 O ANISOU 2606 O HOH A 675 4346 4514 4206 7 -274 565 O HETATM 2607 O HOH A 676 29.782 8.333 -18.927 1.00 33.86 O ANISOU 2607 O HOH A 676 4358 4326 4181 105 129 -67 O HETATM 2608 O HOH A 677 17.343 -20.794 -5.849 1.00 33.62 O ANISOU 2608 O HOH A 677 4538 3871 4363 546 208 573 O HETATM 2609 O HOH A 678 23.631 -5.319 -34.905 1.00 38.79 O ANISOU 2609 O HOH A 678 5131 4672 4933 -500 75 -132 O HETATM 2610 O HOH A 679 -7.951 -8.249 -36.076 1.00 39.14 O ANISOU 2610 O HOH A 679 4567 5044 5258 110 -1083 734 O HETATM 2611 O HOH A 680 28.093 -18.950 -23.800 1.00 41.29 O ANISOU 2611 O HOH A 680 4856 5560 5272 1064 367 840 O HETATM 2612 O HOH A 681 28.278 -2.456 -30.244 1.00 42.90 O ANISOU 2612 O HOH A 681 5544 6280 4476 -1225 526 30 O HETATM 2613 O HOH A 682 4.404 -16.112 -1.085 1.00 42.40 O ANISOU 2613 O HOH A 682 5677 5405 5027 204 5 366 O HETATM 2614 O HOH A 683 22.154 -17.217 -1.450 1.00 38.65 O ANISOU 2614 O HOH A 683 4702 5360 4620 -392 -8 259 O HETATM 2615 O HOH A 684 22.359 -12.207 0.372 1.00 36.62 O ANISOU 2615 O HOH A 684 4670 4085 5159 651 -267 839 O HETATM 2616 O HOH A 685 12.949 -11.532 -37.503 1.00 29.87 O ANISOU 2616 O HOH A 685 3738 3773 3838 308 201 302 O HETATM 2617 O HOH A 686 15.923 5.203 -1.648 1.00 26.69 O ANISOU 2617 O HOH A 686 3842 3217 3079 109 -200 -559 O HETATM 2618 O HOH A 687 0.055 -21.522 -21.975 1.00 28.34 O ANISOU 2618 O HOH A 687 3442 3749 3574 -215 492 492 O HETATM 2619 O HOH A 688 22.326 -18.956 -34.463 1.00 26.18 O ANISOU 2619 O HOH A 688 3157 3359 3430 156 596 -288 O HETATM 2620 O HOH A 689 17.255 8.351 -24.417 1.00 29.56 O ANISOU 2620 O HOH A 689 3869 3686 3675 -83 235 84 O HETATM 2621 O HOH A 690 8.745 1.064 -36.096 1.00 32.48 O ANISOU 2621 O HOH A 690 4023 4087 4231 479 248 -119 O HETATM 2622 O HOH A 691 6.711 11.898 -16.742 1.00 22.46 O ANISOU 2622 O HOH A 691 3042 2656 2836 140 199 -170 O HETATM 2623 O HOH A 692 30.396 3.532 -5.885 1.00 35.11 O ANISOU 2623 O HOH A 692 4909 3961 4470 316 -1009 -11 O HETATM 2624 O HOH A 693 7.167 -9.287 -35.990 1.00 28.26 O ANISOU 2624 O HOH A 693 3470 4001 3267 -140 -105 157 O HETATM 2625 O HOH A 694 -4.838 -23.620 -31.829 1.00 41.64 O ANISOU 2625 O HOH A 694 5081 5492 5247 -173 -994 -564 O HETATM 2626 O HOH A 695 13.653 -2.882 -30.644 1.00 16.40 O ANISOU 2626 O HOH A 695 2220 1938 2072 -37 71 -24 O HETATM 2627 O HOH A 696 -6.272 -9.943 -39.042 1.00 42.59 O ANISOU 2627 O HOH A 696 4911 6574 4696 665 -13 827 O HETATM 2628 O HOH A 697 12.753 8.280 -3.565 1.00 36.93 O ANISOU 2628 O HOH A 697 4868 4729 4433 -280 504 -1053 O HETATM 2629 O HOH A 698 3.210 11.478 -26.908 1.00 34.30 O ANISOU 2629 O HOH A 698 4927 3506 4599 644 -21 322 O HETATM 2630 O HOH A 699 18.466 5.559 -6.252 1.00 36.49 O ANISOU 2630 O HOH A 699 4744 4970 4148 154 15 -473 O HETATM 2631 O HOH A 700 -1.232 -19.682 -20.386 1.00 27.10 O ANISOU 2631 O HOH A 700 3469 3338 3488 -135 433 311 O HETATM 2632 O HOH A 701 22.466 -11.542 -36.408 1.00 23.37 O ANISOU 2632 O HOH A 701 2817 3069 2992 -219 400 -244 O HETATM 2633 O HOH A 702 0.051 12.633 -25.077 1.00 28.51 O ANISOU 2633 O HOH A 702 3934 3145 3753 176 -123 285 O HETATM 2634 O HOH A 703 11.794 9.943 -6.330 1.00 22.47 O ANISOU 2634 O HOH A 703 2967 2560 3010 -203 136 -311 O HETATM 2635 O HOH A 704 31.193 -12.817 -20.373 1.00 47.27 O ANISOU 2635 O HOH A 704 5588 7157 5214 -1695 -107 -102 O HETATM 2636 O HOH A 705 0.385 -25.285 -12.290 1.00 37.51 O ANISOU 2636 O HOH A 705 4969 4611 4672 123 -702 304 O HETATM 2637 O HOH A 706 2.117 15.383 -15.227 1.00 42.82 O ANISOU 2637 O HOH A 706 5140 5379 5751 -78 703 689 O HETATM 2638 O HOH A 707 16.944 -1.118 1.625 1.00 30.14 O ANISOU 2638 O HOH A 707 4269 4062 3120 717 214 238 O HETATM 2639 O HOH A 708 25.613 -20.368 -14.682 1.00 28.55 O ANISOU 2639 O HOH A 708 4081 3141 3625 258 -477 33 O HETATM 2640 O HOH A 709 4.033 5.481 -2.768 1.00 36.76 O ANISOU 2640 O HOH A 709 4128 4380 5457 613 336 -287 O HETATM 2641 O HOH A 710 -4.253 -18.840 -36.405 1.00 28.61 O ANISOU 2641 O HOH A 710 3814 3757 3299 -302 -655 -278 O HETATM 2642 O HOH A 711 30.792 -12.204 -9.606 1.00 47.96 O ANISOU 2642 O HOH A 711 5940 6848 5433 1073 -889 -800 O HETATM 2643 O HOH A 712 5.833 -27.881 -30.881 1.00 33.35 O ANISOU 2643 O HOH A 712 4176 3981 4511 305 -417 -651 O HETATM 2644 O HOH A 713 30.595 0.104 -24.685 1.00 35.10 O ANISOU 2644 O HOH A 713 4045 4529 4761 -305 -543 -147 O HETATM 2645 O HOH A 714 -4.539 5.971 -21.212 1.00 45.04 O ANISOU 2645 O HOH A 714 5897 5394 5822 935 648 481 O HETATM 2646 O HOH A 715 28.411 -5.804 -30.106 1.00 50.46 O ANISOU 2646 O HOH A 715 6403 6489 6277 -1048 288 374 O HETATM 2647 O HOH A 716 -12.103 -4.341 -16.933 1.00 34.51 O ANISOU 2647 O HOH A 716 4016 4634 4463 150 481 -257 O HETATM 2648 O HOH A 717 29.491 -9.569 -21.403 1.00 34.39 O ANISOU 2648 O HOH A 717 4919 3973 4171 420 -1074 -25 O HETATM 2649 O HOH A 718 11.613 -7.217 -38.895 1.00 35.19 O ANISOU 2649 O HOH A 718 4612 4625 4131 670 -57 467 O HETATM 2650 O HOH A 719 19.766 1.200 0.606 1.00 36.76 O ANISOU 2650 O HOH A 719 4839 4526 4600 -161 -441 -432 O HETATM 2651 O HOH A 720 -0.406 -1.177 -37.967 1.00 22.73 O ANISOU 2651 O HOH A 720 2828 3079 2728 34 56 -63 O HETATM 2652 O HOH A 721 7.833 10.162 -23.184 1.00 39.11 O ANISOU 2652 O HOH A 721 4698 4436 5724 -420 -643 406 O HETATM 2653 O HOH A 722 7.716 -7.141 -39.606 0.50 26.30 O ANISOU 2653 O HOH A 722 3626 3097 3271 69 -200 -365 O HETATM 2654 O HOH A 723 21.715 -19.635 -7.281 1.00 35.59 O ANISOU 2654 O HOH A 723 5265 4000 4255 -63 -262 -159 O HETATM 2655 O HOH A 724 23.272 -12.917 -4.323 1.00 43.75 O ANISOU 2655 O HOH A 724 6122 4910 5590 -995 664 -1426 O HETATM 2656 O HOH A 725 8.075 -19.537 -37.071 1.00 41.21 O ANISOU 2656 O HOH A 725 4544 4924 6188 38 -42 -738 O HETATM 2657 O HOH A 726 26.075 -3.259 -1.980 1.00 42.71 O ANISOU 2657 O HOH A 726 5077 5484 5664 252 -194 -746 O HETATM 2658 O HOH A 727 12.254 12.155 -23.270 1.00 27.06 O ANISOU 2658 O HOH A 727 3397 3452 3433 105 133 235 O HETATM 2659 O HOH A 728 -4.573 -5.553 -37.218 1.00 33.57 O ANISOU 2659 O HOH A 728 4152 4446 4157 -334 371 586 O HETATM 2660 O HOH A 729 7.276 11.402 -9.518 1.00 36.58 O ANISOU 2660 O HOH A 729 5173 4043 4679 609 931 608 O HETATM 2661 O HOH A 730 -5.026 0.799 -17.051 1.00 40.06 O ANISOU 2661 O HOH A 730 5060 5309 4851 -201 436 -479 O HETATM 2662 O HOH A 731 19.909 -24.017 -29.374 1.00 24.17 O ANISOU 2662 O HOH A 731 3395 2757 3028 -93 127 -8 O HETATM 2663 O HOH A 732 3.863 -24.701 -17.902 1.00 28.63 O ANISOU 2663 O HOH A 732 3507 3319 4050 -412 175 556 O HETATM 2664 O HOH A 733 20.882 6.629 -5.156 1.00 36.16 O ANISOU 2664 O HOH A 733 4563 4112 5063 -112 -224 -255 O HETATM 2665 O HOH A 734 0.096 -23.918 -20.502 1.00 39.74 O ANISOU 2665 O HOH A 734 5436 4563 5098 -1104 115 -65 O HETATM 2666 O HOH A 735 8.793 -20.494 -1.445 1.00 44.18 O ANISOU 2666 O HOH A 735 5696 5533 5555 -633 -209 1303 O HETATM 2667 O HOH A 736 29.050 -12.912 -26.648 1.00 39.84 O ANISOU 2667 O HOH A 736 4919 4965 5251 330 312 -424 O HETATM 2668 O HOH A 737 20.471 9.488 -23.314 1.00 38.42 O ANISOU 2668 O HOH A 737 5237 4413 4946 -306 541 215 O HETATM 2669 O HOH A 738 -10.144 -20.393 -19.923 1.00 48.07 O ANISOU 2669 O HOH A 738 6204 6069 5989 1180 -181 1036 O HETATM 2670 O HOH A 739 -8.461 1.093 -22.229 1.00 48.18 O ANISOU 2670 O HOH A 739 5965 5636 6702 -121 -896 -257 O HETATM 2671 O HOH A 740 26.403 0.571 -26.261 1.00 34.66 O ANISOU 2671 O HOH A 740 4754 4159 4253 323 -389 -473 O HETATM 2672 O HOH A 741 7.787 -13.840 0.503 1.00 38.88 O ANISOU 2672 O HOH A 741 5245 4769 4756 618 10 440 O HETATM 2673 O HOH A 742 27.329 -10.180 -31.657 1.00 35.91 O ANISOU 2673 O HOH A 742 4307 4715 4622 -312 151 301 O HETATM 2674 O HOH A 743 -10.224 -17.223 -31.630 1.00 44.25 O ANISOU 2674 O HOH A 743 5440 5942 5431 -470 -95 -92 O HETATM 2675 O HOH A 744 -6.623 -22.316 -21.734 1.00 43.46 O ANISOU 2675 O HOH A 744 5586 4986 5940 -96 881 652 O HETATM 2676 O HOH A 745 26.999 -13.094 -28.155 1.00 35.13 O ANISOU 2676 O HOH A 745 4331 4223 4791 50 -233 558 O HETATM 2677 O HOH A 746 8.175 -27.240 -32.669 1.00 34.09 O ANISOU 2677 O HOH A 746 4386 4143 4421 -284 32 180 O HETATM 2678 O HOH A 747 0.967 -8.858 -15.967 1.00 37.48 O ANISOU 2678 O HOH A 747 4636 4703 4901 -558 181 -913 O HETATM 2679 O HOH A 748 15.883 -2.227 -34.829 1.00 29.89 O ANISOU 2679 O HOH A 748 4360 3676 3318 26 414 -6 O HETATM 2680 O HOH A 749 -4.716 -20.907 -13.577 1.00 48.63 O ANISOU 2680 O HOH A 749 5984 6607 5886 -606 -47 535 O HETATM 2681 O HOH A 750 28.219 -19.967 -21.708 1.00 38.60 O ANISOU 2681 O HOH A 750 5241 4531 4892 213 717 -62 O HETATM 2682 O HOH A 751 16.728 -24.773 -37.945 1.00 42.45 O ANISOU 2682 O HOH A 751 6014 4923 5191 217 -859 -347 O HETATM 2683 O HOH A 752 -2.368 3.912 -28.796 1.00 36.17 O ANISOU 2683 O HOH A 752 5129 4159 4452 -398 -179 -212 O HETATM 2684 O HOH A 753 20.368 -16.718 -36.759 1.00 38.95 O ANISOU 2684 O HOH A 753 5093 4953 4750 536 508 229 O HETATM 2685 O HOH A 754 23.036 2.368 -1.453 1.00 51.90 O ANISOU 2685 O HOH A 754 7289 6278 6152 263 -920 133 O HETATM 2686 O HOH A 755 9.161 9.023 -24.940 1.00 43.25 O ANISOU 2686 O HOH A 755 5630 5145 5658 -395 -1284 -810 O HETATM 2687 O HOH A 756 13.427 -24.476 -12.830 1.00 52.09 O ANISOU 2687 O HOH A 756 6040 6143 7609 789 -568 -847 O HETATM 2688 O HOH A 757 1.471 -28.079 -29.364 1.00 51.29 O ANISOU 2688 O HOH A 757 6893 5891 6703 126 -1005 -542 O HETATM 2689 O HOH A 758 -6.254 4.371 -24.079 1.00 44.34 O ANISOU 2689 O HOH A 758 5012 5454 6379 -97 -680 504 O HETATM 2690 O HOH A 759 18.101 11.256 -23.780 1.00 36.02 O ANISOU 2690 O HOH A 759 5267 4184 4234 382 331 67 O HETATM 2691 O HOH A 760 13.634 -8.979 -38.214 1.00 24.37 O ANISOU 2691 O HOH A 760 3165 3006 3086 190 -14 43 O HETATM 2692 O HOH A 761 26.952 -18.661 -19.676 1.00 26.77 O ANISOU 2692 O HOH A 761 3424 2892 3856 62 -110 -136 O HETATM 2693 O HOH A 762 31.187 -9.930 -24.125 1.00 40.29 O ANISOU 2693 O HOH A 762 4654 4901 5750 -418 597 -829 O HETATM 2694 O HOH A 763 5.194 -6.357 3.518 1.00 39.11 O ANISOU 2694 O HOH A 763 5120 5610 4127 76 235 169 O HETATM 2695 O HOH A 764 -6.062 -6.298 0.131 0.50 32.85 O ANISOU 2695 O HOH A 764 4243 4402 3835 314 917 -886 O HETATM 2696 O HOH A 765 3.010 -3.222 5.966 1.00 47.07 O ANISOU 2696 O HOH A 765 5896 5983 6004 1056 -284 -296 O HETATM 2697 O HOH A 766 -7.780 -0.945 -20.360 1.00 40.14 O ANISOU 2697 O HOH A 766 4279 5603 5369 169 503 191 O HETATM 2698 O HOH A 767 14.922 -6.890 -36.954 1.00 41.42 O ANISOU 2698 O HOH A 767 5566 5684 4486 529 -759 -978 O HETATM 2699 O HOH A 768 1.276 12.567 -20.276 1.00 31.67 O ANISOU 2699 O HOH A 768 4142 3615 4276 258 -364 -225 O HETATM 2700 O HOH A 769 -7.182 -19.131 -17.482 1.00 39.51 O ANISOU 2700 O HOH A 769 4946 4834 5229 -367 878 987 O HETATM 2701 O HOH A 770 -15.206 -13.218 -17.088 1.00 50.94 O ANISOU 2701 O HOH A 770 6227 6458 6668 -840 -830 139 O HETATM 2702 O HOH A 771 17.529 -27.174 -34.164 1.00 22.62 O ANISOU 2702 O HOH A 771 2944 2720 2930 -118 -192 281 O HETATM 2703 O HOH A 772 5.772 -26.311 -16.525 1.00 36.60 O ANISOU 2703 O HOH A 772 4469 4367 5069 648 755 534 O HETATM 2704 O HOH A 773 3.378 -22.029 -3.673 1.00 35.80 O ANISOU 2704 O HOH A 773 4816 4533 4252 -121 198 35 O HETATM 2705 O HOH A 774 9.005 -23.817 -7.867 1.00 39.52 O ANISOU 2705 O HOH A 774 5313 4576 5123 -610 394 1164 O HETATM 2706 O HOH A 775 -2.921 -1.813 -38.571 1.00 40.49 O ANISOU 2706 O HOH A 775 4609 5749 5024 165 448 -493 O HETATM 2707 O HOH A 776 20.201 -14.390 0.704 1.00 42.24 O ANISOU 2707 O HOH A 776 5370 4727 5950 541 -1199 196 O HETATM 2708 O HOH A 777 -1.147 -17.204 -3.417 1.00 38.34 O ANISOU 2708 O HOH A 777 4956 4872 4738 -560 516 645 O HETATM 2709 O HOH A 778 13.707 5.720 -38.319 0.50 26.02 O ANISOU 2709 O HOH A 778 3464 3556 2864 -230 -419 -402 O HETATM 2710 O HOH A 779 12.414 10.101 -24.518 1.00 37.88 O ANISOU 2710 O HOH A 779 5392 4508 4489 113 573 147 O HETATM 2711 O HOH A 780 3.835 11.371 -17.317 1.00 29.08 O ANISOU 2711 O HOH A 780 3729 3538 3780 0 -207 101 O HETATM 2712 O HOH A 781 10.418 12.782 -21.121 1.00 22.31 O ANISOU 2712 O HOH A 781 3104 2560 2812 -227 -103 44 O HETATM 2713 O HOH A 782 2.742 -12.946 -42.842 1.00 29.95 O ANISOU 2713 O HOH A 782 3641 3881 3855 82 -87 352 O HETATM 2714 O HOH A 783 -13.401 -18.580 -29.048 1.00 35.82 O ANISOU 2714 O HOH A 783 4443 4715 4450 -146 -456 -297 O HETATM 2715 O HOH A 784 32.224 4.772 -16.200 1.00 40.53 O ANISOU 2715 O HOH A 784 4866 5021 5513 -58 -569 221 O HETATM 2716 O HOH A 785 26.801 -10.039 -34.494 1.00 46.51 O ANISOU 2716 O HOH A 785 5968 5811 5893 -55 836 -871 O HETATM 2717 O HOH A 786 8.801 -24.307 -4.937 1.00 51.47 O ANISOU 2717 O HOH A 786 7094 5953 6508 -882 923 1152 O HETATM 2718 O HOH A 787 29.894 -16.622 -27.535 1.00 45.69 O ANISOU 2718 O HOH A 787 5127 6125 6108 -878 1097 584 O HETATM 2719 O HOH A 788 8.086 -27.127 -17.863 1.00 26.77 O ANISOU 2719 O HOH A 788 3628 2870 3672 145 94 294 O HETATM 2720 O HOH A 789 -7.178 -19.012 -34.815 1.00 54.08 O ANISOU 2720 O HOH A 789 6783 6649 7113 -1869 -505 303 O HETATM 2721 O HOH A 790 -0.888 3.416 -38.403 1.00 48.78 O ANISOU 2721 O HOH A 790 6722 5858 5953 861 173 -276 O HETATM 2722 O HOH A 791 21.868 -13.424 -38.417 1.00 30.44 O ANISOU 2722 O HOH A 791 4005 3916 3644 -32 -137 -605 O HETATM 2723 O HOH A 792 -8.984 -20.520 -31.037 1.00 42.18 O ANISOU 2723 O HOH A 792 5085 5470 5470 -524 -961 -924 O HETATM 2724 O HOH A 793 30.654 2.694 -14.519 1.00 34.63 O ANISOU 2724 O HOH A 793 4481 4342 4332 -509 224 -306 O HETATM 2725 O HOH A 794 -7.018 -24.243 -29.929 1.00 41.36 O ANISOU 2725 O HOH A 794 5142 4872 5701 -362 -725 -257 O HETATM 2726 O HOH A 795 5.140 -16.004 -38.132 1.00 38.15 O ANISOU 2726 O HOH A 795 4381 5520 4592 549 -799 238 O HETATM 2727 O HOH A 796 28.716 -8.247 -7.122 1.00 38.92 O ANISOU 2727 O HOH A 796 4673 4448 5665 1109 42 190 O HETATM 2728 O HOH A 797 7.830 13.734 -21.371 1.00 31.62 O ANISOU 2728 O HOH A 797 4071 3769 4171 -184 -24 -89 O HETATM 2729 O HOH A 798 5.292 -26.249 -8.380 1.00 42.93 O ANISOU 2729 O HOH A 798 5807 4973 5530 -233 -77 321 O HETATM 2730 O HOH A 799 24.929 -11.808 -35.360 1.00 36.83 O ANISOU 2730 O HOH A 799 4258 5022 4711 -194 0 -499 O HETATM 2731 O HOH A 800 25.617 -15.618 -32.934 1.00 38.21 O ANISOU 2731 O HOH A 800 4828 4757 4931 192 346 166 O HETATM 2732 O HOH A 801 26.559 -20.997 -12.536 1.00 42.25 O ANISOU 2732 O HOH A 801 5876 5337 4840 885 -679 -700 O HETATM 2733 O HOH A 802 -2.553 11.882 -17.239 1.00 47.92 O ANISOU 2733 O HOH A 802 6051 6031 6123 714 65 -885 O HETATM 2734 O HOH A 803 4.791 11.714 -9.004 1.00 45.89 O ANISOU 2734 O HOH A 803 4904 6879 5651 -633 -408 -166 O HETATM 2735 O HOH A 804 33.021 5.518 -12.078 1.00 48.02 O ANISOU 2735 O HOH A 804 6838 5112 6293 326 385 -165 O HETATM 2736 O HOH A 805 22.630 -23.368 -28.797 1.00 23.75 O ANISOU 2736 O HOH A 805 3298 2902 2822 270 -159 -133 O HETATM 2737 O HOH A 806 5.441 -23.042 -2.851 1.00 41.11 O ANISOU 2737 O HOH A 806 5391 5112 5117 -503 477 973 O HETATM 2738 O HOH A 807 1.835 12.734 -16.105 1.00 39.54 O ANISOU 2738 O HOH A 807 4973 5019 5028 845 226 -443 O HETATM 2739 O HOH A 808 24.441 -19.543 -30.130 1.00 39.73 O ANISOU 2739 O HOH A 808 5127 4999 4968 -65 -455 -163 O HETATM 2740 O HOH A 809 22.934 -21.393 -35.449 1.00 37.17 O ANISOU 2740 O HOH A 809 4818 4538 4764 182 863 -229 O HETATM 2741 O HOH A 810 -0.254 13.019 -17.864 1.00 43.41 O ANISOU 2741 O HOH A 810 5719 4804 5968 491 -626 -346 O HETATM 2742 O HOH A 811 26.702 -16.069 -30.942 1.00 48.75 O ANISOU 2742 O HOH A 811 6871 6079 5570 549 659 -45 O HETATM 2743 O HOH A 812 0.537 12.328 -13.900 1.00 37.04 O ANISOU 2743 O HOH A 812 4829 4407 4837 960 -18 -102 O HETATM 2744 O HOH A 813 16.050 -27.185 -36.531 1.00 30.96 O ANISOU 2744 O HOH A 813 4423 3369 3971 60 -788 2 O HETATM 2745 O HOH A 814 5.902 -9.349 4.273 1.00 50.20 O ANISOU 2745 O HOH A 814 6221 7521 5329 -622 1555 1095 O HETATM 2746 O HOH A 815 26.111 -13.511 -36.958 1.00 44.08 O ANISOU 2746 O HOH A 815 5898 6209 4640 -389 601 -291 O HETATM 2747 O HOH A 816 2.954 -2.966 8.837 1.00 37.77 O ANISOU 2747 O HOH A 816 4292 4648 5408 -14 -231 -769 O HETATM 2748 O HOH A 817 2.764 14.706 -19.899 1.00 45.19 O ANISOU 2748 O HOH A 817 5945 5502 5723 -626 685 -213 O CONECT 271 2420 2421 CONECT 286 2420 CONECT 490 2421 CONECT 630 2423 CONECT 674 2422 CONECT 1665 2423 CONECT 2420 271 286 CONECT 2421 271 490 CONECT 2422 674 CONECT 2423 630 1665 CONECT 2424 2426 2428 CONECT 2425 2427 2429 CONECT 2426 2424 CONECT 2427 2425 CONECT 2428 2424 2430 CONECT 2429 2425 2431 CONECT 2430 2428 CONECT 2431 2429 MASTER 349 0 6 18 8 0 0 6 2657 1 18 23 END If you find results from this site helpful for your research, please cite one of our papers:
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