HEADER MEMBRANE PROTEIN/HYDROLASE 24-OCT-10 3PDS TITLE IRREVERSIBLE AGONIST-BETA2 ADRENOCEPTOR COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: FUSION PROTEIN BETA-2 ADRENERGIC RECEPTOR/LYSOZYME; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: BETA-2 ADRENORECEPTOR, BETA-2 ADRENOCEPTOR; COMPND 5 EC: 3.2.1.17; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 10665; SOURCE 5 GENE: ADRB2, ADRB2R, B2AR; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR, SIGNALING, BETA ADRENERGIC AGONIST, FUSION PROTEIN, MEMBRANE KEYWDS 2 PROTEIN-HYDROLASE COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR D.M.ROSENBAUM,C.ZHANG,J.A.LYONS,R.HOLL,D.ARAGAO,D.H.ARLOW, AUTHOR 2 S.G.F.RASMUSSEN,H.-J.CHOI,B.T.DEVREE,R.K.SUNAHARA,P.S.CHAE, AUTHOR 3 S.H.GELLMAN,R.O.DROR,D.E.SHAW,W.I.WEIS,M.CAFFREY,P.GMEINER, AUTHOR 4 B.K.KOBILKA REVDAT 4 29-MAR-23 3PDS 1 AUTHOR JRNL REMARK SEQADV REVDAT 4 2 1 LINK REVDAT 3 26-JUL-17 3PDS 1 SOURCE REMARK REVDAT 2 09-FEB-11 3PDS 1 JRNL AUTHOR REVDAT 1 12-JAN-11 3PDS 0 JRNL AUTH D.M.ROSENBAUM,C.ZHANG,J.A.LYONS,R.HOLL,D.ARAGAO,D.H.ARLOW, JRNL AUTH 2 S.G.F.RASMUSSEN,H.J.CHOI,B.T.DEVREE,R.K.SUNAHARA,P.S.CHAE, JRNL AUTH 3 S.H.GELLMAN,R.O.DROR,D.E.SHAW,W.I.WEIS,M.CAFFREY,P.GMEINER, JRNL AUTH 4 B.K.KOBILKA JRNL TITL STRUCTURE AND FUNCTION OF AN IRREVERSIBLE AGONIST-BETA(2) JRNL TITL 2 ADRENOCEPTOR COMPLEX JRNL REF NATURE V. 469 236 2011 JRNL REFN ISSN 0028-0836 JRNL PMID 21228876 JRNL DOI 10.1038/NATURE09665 REMARK 2 REMARK 2 RESOLUTION. 3.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.8.0 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.21 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 9352 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) : 0.241 REMARK 3 R VALUE (WORKING SET) : 0.238 REMARK 3 FREE R VALUE : 0.283 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.090 REMARK 3 FREE R VALUE TEST SET COUNT : 944 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 5 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.91 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2496 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2375 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2217 REMARK 3 BIN R VALUE (WORKING SET) : 0.2338 REMARK 3 BIN FREE R VALUE : 0.2663 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 11.18 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 279 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3539 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 89 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 81.80 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 7.55370 REMARK 3 B22 (A**2) : 14.06710 REMARK 3 B33 (A**2) : -21.62080 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 COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.879 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.847 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.770 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3708 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 5041 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1240 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 72 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 544 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3672 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 498 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 4176 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 0.89 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.57 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.03 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|29 - A|230 A|263 - A|342 } REMARK 3 ORIGIN FOR THE GROUP (A): 28.5295 7.5758 7.4465 REMARK 3 T TENSOR REMARK 3 T11: -0.2547 T22: 0.0561 REMARK 3 T33: 0.3897 T12: -0.0369 REMARK 3 T13: -0.0143 T23: 0.0208 REMARK 3 L TENSOR REMARK 3 L11: 0.8276 L22: 1.7725 REMARK 3 L33: 0.6525 L12: -0.1286 REMARK 3 L13: 0.1233 L23: -0.0659 REMARK 3 S TENSOR REMARK 3 S11: -0.0385 S12: 0.1642 S13: -0.0835 REMARK 3 S21: 0.0741 S22: 0.1115 S23: 0.5950 REMARK 3 S31: 0.0864 S32: 0.1853 S33: -0.0730 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { A|1002 - A|1161 } REMARK 3 ORIGIN FOR THE GROUP (A): 71.3516 22.6544 15.9417 REMARK 3 T TENSOR REMARK 3 T11: -0.1642 T22: 0.0921 REMARK 3 T33: -0.0431 T12: -0.0046 REMARK 3 T13: -0.0007 T23: 0.0722 REMARK 3 L TENSOR REMARK 3 L11: 1.7561 L22: 4.1022 REMARK 3 L33: 3.4864 L12: -0.5541 REMARK 3 L13: -0.5257 L23: 2.9168 REMARK 3 S TENSOR REMARK 3 S11: -0.1886 S12: -0.0196 S13: -0.0317 REMARK 3 S21: -0.0028 S22: 0.0146 S23: -0.2817 REMARK 3 S31: -0.0386 S32: 0.1317 S33: 0.1740 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3PDS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-OCT-10. REMARK 100 THE DEPOSITION ID IS D_1000062255. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-JUN-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.7 REMARK 200 NUMBER OF CRYSTALS USED : 19 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9385 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500 REMARK 200 RESOLUTION RANGE LOW (A) : 65.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.20200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.69 REMARK 200 COMPLETENESS FOR SHELL (%) : 94.0 REMARK 200 DATA REDUNDANCY IN SHELL : 2.90 REMARK 200 R MERGE FOR SHELL (I) : 0.44300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 2RH1 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 65.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.51 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 26 %(V/V) PEG 400, 200 MM LI2SO4, 4 REMARK 280 %(V/V) DMSO, 3.5 %(V/V) 1,4-BUTANDEDIOL, 100 MM MES PH 6.7, REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X+1/2,Y+1/2,-Z REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 141.22000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.02000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 141.22000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 20.02000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 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 THR A 25 REMARK 465 GLN A 26 REMARK 465 GLN A 27 REMARK 465 ARG A 28 REMARK 465 ARG A 343 REMARK 465 ARG A 344 REMARK 465 SER A 345 REMARK 465 SER A 346 REMARK 465 LEU A 347 REMARK 465 LYS A 348 REMARK 465 HIS A 349 REMARK 465 HIS A 350 REMARK 465 HIS A 351 REMARK 465 HIS A 352 REMARK 465 HIS A 353 REMARK 465 HIS A 354 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ASP A 29 CG OD1 OD2 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 GLN A 65 46.64 -103.93 REMARK 500 HIS A 172 113.07 -23.44 REMARK 500 TRP A 173 -14.82 -148.49 REMARK 500 PHE A 208 -61.50 -148.55 REMARK 500 ILE A1050 -62.63 -95.17 REMARK 500 ASN A1055 -1.17 65.77 REMARK 500 CYS A 341 80.85 59.97 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ERC A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLR A 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1203 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1204 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1205 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1206 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1207 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1208 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2RH1 RELATED DB: PDB REMARK 900 BETA2-ADRENERGIC RECEPTOR WITH INVERSE AGONIST CARAZOLOL BOUND. DBREF 3PDS A 25 230 UNP P07550 ADRB2_HUMAN 25 230 DBREF 3PDS A 1002 263 UNP P00720 LYS_BPT4 2 162 DBREF 3PDS A 264 348 UNP P07550 ADRB2_HUMAN 264 348 SEQADV 3PDS GLN A 27 UNP P07550 GLU 27 CONFLICT SEQADV 3PDS CYS A 93 UNP P07550 HIS 93 ENGINEERED MUTATION SEQADV 3PDS GLU A 187 UNP P07550 ASN 187 ENGINEERED MUTATION SEQADV 3PDS THR A 1054 UNP P00720 CYS 54 ENGINEERED MUTATION SEQADV 3PDS ALA A 1097 UNP P00720 CYS 97 CONFLICT SEQADV 3PDS HIS A 349 UNP P07550 EXPRESSION TAG SEQADV 3PDS HIS A 350 UNP P07550 EXPRESSION TAG SEQADV 3PDS HIS A 351 UNP P07550 EXPRESSION TAG SEQADV 3PDS HIS A 352 UNP P07550 EXPRESSION TAG SEQADV 3PDS HIS A 353 UNP P07550 EXPRESSION TAG SEQADV 3PDS HIS A 354 UNP P07550 EXPRESSION TAG SEQRES 1 A 458 THR GLN GLN ARG ASP GLU VAL TRP VAL VAL GLY MET GLY SEQRES 2 A 458 ILE VAL MET SER LEU ILE VAL LEU ALA ILE VAL PHE GLY SEQRES 3 A 458 ASN VAL LEU VAL ILE THR ALA ILE ALA LYS PHE GLU ARG SEQRES 4 A 458 LEU GLN THR VAL THR ASN TYR PHE ILE THR SER LEU ALA SEQRES 5 A 458 CYS ALA ASP LEU VAL MET GLY LEU ALA VAL VAL PRO PHE SEQRES 6 A 458 GLY ALA ALA CYS ILE LEU MET LYS MET TRP THR PHE GLY SEQRES 7 A 458 ASN PHE TRP CYS GLU PHE TRP THR SER ILE ASP VAL LEU SEQRES 8 A 458 CYS VAL THR ALA SER ILE GLU THR LEU CYS VAL ILE ALA SEQRES 9 A 458 VAL ASP ARG TYR PHE ALA ILE THR SER PRO PHE LYS TYR SEQRES 10 A 458 GLN SER LEU LEU THR LYS ASN LYS ALA ARG VAL ILE ILE SEQRES 11 A 458 LEU MET VAL TRP ILE VAL SER GLY LEU THR SER PHE LEU SEQRES 12 A 458 PRO ILE GLN MET HIS TRP TYR ARG ALA THR HIS GLN GLU SEQRES 13 A 458 ALA ILE ASN CYS TYR ALA GLU GLU THR CYS CYS ASP PHE SEQRES 14 A 458 PHE THR ASN GLN ALA TYR ALA ILE ALA SER SER ILE VAL SEQRES 15 A 458 SER PHE TYR VAL PRO LEU VAL ILE MET VAL PHE VAL TYR SEQRES 16 A 458 SER ARG VAL PHE GLN GLU ALA LYS ARG GLN LEU ASN ILE SEQRES 17 A 458 PHE GLU MET LEU ARG ILE ASP GLU GLY LEU ARG LEU LYS SEQRES 18 A 458 ILE TYR LYS ASP THR GLU GLY TYR TYR THR ILE GLY ILE SEQRES 19 A 458 GLY HIS LEU LEU THR LYS SER PRO SER LEU ASN ALA ALA SEQRES 20 A 458 LYS SER GLU LEU ASP LYS ALA ILE GLY ARG ASN THR ASN SEQRES 21 A 458 GLY VAL ILE THR LYS ASP GLU ALA GLU LYS LEU PHE ASN SEQRES 22 A 458 GLN ASP VAL ASP ALA ALA VAL ARG GLY ILE LEU ARG ASN SEQRES 23 A 458 ALA LYS LEU LYS PRO VAL TYR ASP SER LEU ASP ALA VAL SEQRES 24 A 458 ARG ARG ALA ALA LEU ILE ASN MET VAL PHE GLN MET GLY SEQRES 25 A 458 GLU THR GLY VAL ALA GLY PHE THR ASN SER LEU ARG MET SEQRES 26 A 458 LEU GLN GLN LYS ARG TRP ASP GLU ALA ALA VAL ASN LEU SEQRES 27 A 458 ALA LYS SER ARG TRP TYR ASN GLN THR PRO ASN ARG ALA SEQRES 28 A 458 LYS ARG VAL ILE THR THR PHE ARG THR GLY THR TRP ASP SEQRES 29 A 458 ALA TYR LYS PHE CYS LEU LYS GLU HIS LYS ALA LEU LYS SEQRES 30 A 458 THR LEU GLY ILE ILE MET GLY THR PHE THR LEU CYS TRP SEQRES 31 A 458 LEU PRO PHE PHE ILE VAL ASN ILE VAL HIS VAL ILE GLN SEQRES 32 A 458 ASP ASN LEU ILE ARG LYS GLU VAL TYR ILE LEU LEU ASN SEQRES 33 A 458 TRP ILE GLY TYR VAL ASN SER GLY PHE ASN PRO LEU ILE SEQRES 34 A 458 TYR CYS ARG SER PRO ASP PHE ARG ILE ALA PHE GLN GLU SEQRES 35 A 458 LEU LEU CYS LEU ARG ARG SER SER LEU LYS HIS HIS HIS SEQRES 36 A 458 HIS HIS HIS HET ERC A1201 31 HET CLR A1202 28 HET SO4 A1203 5 HET SO4 A1204 5 HET SO4 A1205 5 HET SO4 A1206 5 HET SO4 A1207 5 HET SO4 A1208 5 HETNAM ERC 8-HYDROXY-5-[(1R)-1-HYDROXY-2-({2-[3-METHOXY-4-(3- HETNAM 2 ERC SULFANYLPROPOXY)PHENYL]ETHYL}AMINO)ETHYL]QUINOLIN- HETNAM 3 ERC 2(1H)-ONE HETNAM CLR CHOLESTEROL HETNAM SO4 SULFATE ION FORMUL 2 ERC C23 H28 N2 O5 S FORMUL 3 CLR C27 H46 O FORMUL 4 SO4 6(O4 S 2-) HELIX 1 1 VAL A 31 PHE A 61 1 31 HELIX 2 2 GLU A 62 GLN A 65 5 4 HELIX 3 3 THR A 66 VAL A 86 1 21 HELIX 4 4 VAL A 86 MET A 96 1 11 HELIX 5 5 GLY A 102 THR A 136 1 35 HELIX 6 6 THR A 146 SER A 165 1 20 HELIX 7 7 SER A 165 MET A 171 1 7 HELIX 8 8 HIS A 178 GLU A 187 1 10 HELIX 9 9 ASN A 196 VAL A 206 1 11 HELIX 10 10 PHE A 208 GLN A 229 1 22 HELIX 11 11 ASN A 1002 GLU A 1011 1 10 HELIX 12 12 SER A 1038 GLY A 1051 1 14 HELIX 13 13 THR A 1059 ASN A 1081 1 23 HELIX 14 14 LYS A 1083 ASP A 1089 1 7 HELIX 15 15 ASP A 1092 GLY A 1107 1 16 HELIX 16 16 GLY A 1107 GLY A 1113 1 7 HELIX 17 17 PHE A 1114 GLN A 1123 1 10 HELIX 18 18 ARG A 1125 LYS A 1135 1 11 HELIX 19 19 SER A 1136 THR A 1142 1 7 HELIX 20 20 THR A 1142 GLY A 1156 1 15 HELIX 21 21 TRP A 1158 LYS A 263 5 5 HELIX 22 22 LEU A 266 ILE A 294 1 29 HELIX 23 23 ILE A 294 GLN A 299 1 6 HELIX 24 24 ARG A 304 ASN A 318 1 15 HELIX 25 25 PHE A 321 TYR A 326 1 6 HELIX 26 26 SER A 329 CYS A 341 1 13 SHEET 1 A 3 ARG A1014 LYS A1019 0 SHEET 2 A 3 TYR A1025 GLY A1028 -1 O THR A1026 N TYR A1018 SHEET 3 A 3 HIS A1031 THR A1034 -1 O LEU A1033 N TYR A1025 SSBOND 1 CYS A 106 CYS A 191 1555 1555 2.03 SSBOND 2 CYS A 184 CYS A 190 1555 1555 2.04 LINK SG CYS A 93 S1 ERC A1201 1555 1555 2.00 SITE 1 AC1 21 GLY A 90 CYS A 93 TRP A 99 TRP A 109 SITE 2 AC1 21 ASP A 113 VAL A 114 CYS A 191 ASP A 192 SITE 3 AC1 21 PHE A 193 ALA A 200 SER A 203 SER A 207 SITE 4 AC1 21 TRP A 286 PHE A 289 PHE A 290 ASN A 293 SITE 5 AC1 21 TYR A 308 ILE A 309 ASN A 312 TRP A 313 SITE 6 AC1 21 TYR A 316 SITE 1 AC2 7 GLN A 65 TYR A 70 THR A 73 CYS A 77 SITE 2 AC2 7 ILE A 154 LEU A 155 TRP A 158 SITE 1 AC3 6 THR A 66 VAL A 67 THR A 68 ARG A 131 SITE 2 AC3 6 TYR A 141 SER A 143 SITE 1 AC4 4 PHE A 264 LYS A 270 LYS A 273 ARG A 328 SITE 1 AC5 3 THR A 146 LYS A 147 ASN A1040 SITE 1 AC6 5 PHE A1114 THR A1115 ASN A1116 SER A1117 SITE 2 AC6 5 ASN A1132 SITE 1 AC7 4 THR A1142 PRO A1143 ASN A1144 ARG A1145 SITE 1 AC8 4 ASP A1092 ALA A1093 ARG A1096 ARG A1119 CRYST1 282.440 40.040 65.210 90.00 90.00 90.00 P 21 21 2 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.003541 0.000000 0.000000 0.00000 SCALE2 0.000000 0.024975 0.000000 0.00000 SCALE3 0.000000 0.000000 0.015335 0.00000 ATOM 1 N ASP A 29 8.698 29.115 -3.435 1.00147.52 N ANISOU 1 N ASP A 29 13630 16457 25963 -878 -2051 1731 N ATOM 2 CA ASP A 29 8.175 29.509 -4.741 1.00149.05 C ANISOU 2 CA ASP A 29 13787 16610 26235 -900 -2340 1808 C ATOM 3 C ASP A 29 7.915 28.303 -5.658 1.00149.63 C ANISOU 3 C ASP A 29 13837 16727 26289 -924 -2542 1781 C ATOM 4 O ASP A 29 8.367 27.194 -5.363 1.00148.76 O ANISOU 4 O ASP A 29 13767 16704 26052 -930 -2458 1701 O ATOM 5 CB ASP A 29 9.110 30.529 -5.412 1.00149.01 C ANISOU 5 CB ASP A 29 13943 16708 25966 -942 -2436 1862 C ATOM 6 N GLU A 30 7.174 28.529 -6.764 1.00147.53 N ANISOU 6 N GLU A 30 13510 16392 26153 -935 -2815 1847 N ATOM 7 CA GLU A 30 6.806 27.513 -7.756 1.00148.49 C ANISOU 7 CA GLU A 30 13609 16532 26278 -958 -3050 1828 C ATOM 8 C GLU A 30 8.011 26.970 -8.535 1.00147.57 C ANISOU 8 C GLU A 30 13697 16623 25750 -1006 -3135 1783 C ATOM 9 O GLU A 30 8.151 25.752 -8.661 1.00147.15 O ANISOU 9 O GLU A 30 13657 16628 25625 -1015 -3151 1707 O ATOM 10 CB GLU A 30 5.740 28.060 -8.724 1.00150.47 C ANISOU 10 CB GLU A 30 13756 16654 26762 -956 -3330 1918 C ATOM 11 CG GLU A 30 4.336 28.105 -8.144 1.00151.96 C ANISOU 11 CG GLU A 30 13698 16629 27410 -908 -3299 1942 C ATOM 12 CD GLU A 30 3.563 26.807 -8.260 1.00152.87 C ANISOU 12 CD GLU A 30 13683 16685 27716 -910 -3391 1892 C ATOM 13 OE1 GLU A 30 3.075 26.503 -9.373 1.00154.07 O ANISOU 13 OE1 GLU A 30 13816 16816 27907 -933 -3688 1916 O ATOM 14 OE2 GLU A 30 3.432 26.099 -7.236 1.00152.54 O ANISOU 14 OE2 GLU A 30 13560 16610 27788 -889 -3169 1830 O ATOM 15 N VAL A 31 8.873 27.870 -9.052 1.00143.75 N ANISOU 15 N VAL A 31 13369 16244 25005 -1036 -3182 1831 N ATOM 16 CA VAL A 31 10.070 27.523 -9.834 1.00143.08 C ANISOU 16 CA VAL A 31 13483 16358 24523 -1082 -3252 1800 C ATOM 17 C VAL A 31 11.271 27.175 -8.921 1.00141.16 C ANISOU 17 C VAL A 31 13340 16253 24041 -1085 -2987 1722 C ATOM 18 O VAL A 31 12.264 26.618 -9.397 1.00140.50 O ANISOU 18 O VAL A 31 13398 16336 23649 -1114 -3005 1675 O ATOM 19 CB VAL A 31 10.429 28.594 -10.912 1.00144.19 C ANISOU 19 CB VAL A 31 13747 16549 24491 -1118 -3438 1895 C ATOM 20 CG1 VAL A 31 11.115 27.953 -12.117 1.00144.30 C ANISOU 20 CG1 VAL A 31 13918 16717 24192 -1158 -3615 1869 C ATOM 21 CG2 VAL A 31 9.199 29.380 -11.364 1.00146.11 C ANISOU 21 CG2 VAL A 31 13867 16613 25035 -1100 -3627 1993 C ATOM 22 N TRP A 32 11.156 27.481 -7.608 1.00136.69 N ANISOU 22 N TRP A 32 12698 15614 23624 -1051 -2745 1706 N ATOM 23 CA TRP A 32 12.168 27.220 -6.576 1.00135.01 C ANISOU 23 CA TRP A 32 12563 15504 23230 -1046 -2489 1635 C ATOM 24 C TRP A 32 12.491 25.722 -6.428 1.00134.10 C ANISOU 24 C TRP A 32 12468 15473 23011 -1041 -2442 1536 C ATOM 25 O TRP A 32 13.644 25.376 -6.159 1.00132.82 O ANISOU 25 O TRP A 32 12427 15459 22580 -1053 -2327 1479 O ATOM 26 CB TRP A 32 11.726 27.833 -5.234 1.00134.77 C ANISOU 26 CB TRP A 32 12437 15345 23424 -1003 -2265 1642 C ATOM 27 CG TRP A 32 12.600 27.497 -4.061 1.00133.21 C ANISOU 27 CG TRP A 32 12306 15226 23082 -989 -2005 1565 C ATOM 28 CD1 TRP A 32 13.801 28.059 -3.743 1.00132.05 C ANISOU 28 CD1 TRP A 32 12296 15199 22678 -1011 -1895 1553 C ATOM 29 CD2 TRP A 32 12.327 26.528 -3.040 1.00132.77 C ANISOU 29 CD2 TRP A 32 12183 15127 23136 -950 -1830 1495 C ATOM 30 NE1 TRP A 32 14.299 27.493 -2.592 1.00130.92 N ANISOU 30 NE1 TRP A 32 12178 15093 22473 -986 -1673 1475 N ATOM 31 CE2 TRP A 32 13.413 26.551 -2.138 1.00131.33 C ANISOU 31 CE2 TRP A 32 12112 15047 22740 -947 -1625 1441 C ATOM 32 CE3 TRP A 32 11.266 25.636 -2.801 1.00133.54 C ANISOU 32 CE3 TRP A 32 12136 15106 23496 -920 -1827 1475 C ATOM 33 CZ2 TRP A 32 13.470 25.719 -1.013 1.00130.64 C ANISOU 33 CZ2 TRP A 32 12009 14948 22681 -911 -1422 1372 C ATOM 34 CZ3 TRP A 32 11.324 24.812 -1.688 1.00132.85 C ANISOU 34 CZ3 TRP A 32 12029 15006 23441 -888 -1614 1409 C ATOM 35 CH2 TRP A 32 12.414 24.859 -0.807 1.00131.42 C ANISOU 35 CH2 TRP A 32 11973 14929 23032 -882 -1415 1359 C ATOM 36 N VAL A 33 11.478 24.846 -6.620 1.00130.94 N ANISOU 36 N VAL A 33 11946 14973 22833 -1024 -2538 1516 N ATOM 37 CA VAL A 33 11.595 23.381 -6.545 1.00130.41 C ANISOU 37 CA VAL A 33 11881 14954 22715 -1018 -2519 1426 C ATOM 38 C VAL A 33 12.555 22.878 -7.642 1.00130.04 C ANISOU 38 C VAL A 33 11996 15084 22329 -1055 -2665 1391 C ATOM 39 O VAL A 33 13.384 22.004 -7.376 1.00128.92 O ANISOU 39 O VAL A 33 11935 15057 21992 -1053 -2565 1311 O ATOM 40 CB VAL A 33 10.207 22.674 -6.607 1.00131.74 C ANISOU 40 CB VAL A 33 11871 14956 23228 -1000 -2615 1425 C ATOM 41 CG1 VAL A 33 10.326 21.181 -6.306 1.00131.21 C ANISOU 41 CG1 VAL A 33 11800 14920 23134 -992 -2552 1332 C ATOM 42 CG2 VAL A 33 9.205 23.327 -5.655 1.00132.46 C ANISOU 42 CG2 VAL A 33 11795 14867 23667 -963 -2482 1474 C ATOM 43 N VAL A 34 12.454 23.462 -8.858 1.00127.67 N ANISOU 43 N VAL A 34 11748 14804 21957 -1085 -2894 1452 N ATOM 44 CA VAL A 34 13.299 23.152 -10.020 1.00127.69 C ANISOU 44 CA VAL A 34 11914 14967 21635 -1120 -3043 1432 C ATOM 45 C VAL A 34 14.746 23.596 -9.727 1.00126.26 C ANISOU 45 C VAL A 34 11878 14954 21141 -1137 -2877 1420 C ATOM 46 O VAL A 34 15.684 22.850 -10.014 1.00125.56 O ANISOU 46 O VAL A 34 11902 15014 20791 -1146 -2856 1352 O ATOM 47 CB VAL A 34 12.743 23.777 -11.336 1.00129.31 C ANISOU 47 CB VAL A 34 12142 15134 21856 -1145 -3325 1515 C ATOM 48 CG1 VAL A 34 13.564 23.348 -12.552 1.00129.47 C ANISOU 48 CG1 VAL A 34 12340 15318 21535 -1177 -3474 1488 C ATOM 49 CG2 VAL A 34 11.270 23.425 -11.541 1.00130.84 C ANISOU 49 CG2 VAL A 34 12170 15148 22395 -1128 -3493 1532 C ATOM 50 N GLY A 35 14.891 24.784 -9.134 1.00122.09 N ANISOU 50 N GLY A 35 11338 14392 20658 -1139 -2761 1481 N ATOM 51 CA GLY A 35 16.173 25.367 -8.749 1.00120.85 C ANISOU 51 CA GLY A 35 11296 14368 20253 -1159 -2603 1479 C ATOM 52 C GLY A 35 16.891 24.581 -7.670 1.00119.41 C ANISOU 52 C GLY A 35 11127 14255 19988 -1135 -2380 1384 C ATOM 53 O GLY A 35 18.112 24.410 -7.738 1.00118.48 O ANISOU 53 O GLY A 35 11126 14298 19593 -1154 -2310 1345 O ATOM 54 N MET A 36 16.130 24.080 -6.674 1.00114.80 N ANISOU 54 N MET A 36 10422 13548 19649 -1093 -2267 1350 N ATOM 55 CA MET A 36 16.642 23.267 -5.566 1.00113.60 C ANISOU 55 CA MET A 36 10275 13436 19452 -1063 -2058 1265 C ATOM 56 C MET A 36 17.029 21.866 -6.059 1.00113.35 C ANISOU 56 C MET A 36 10293 13501 19273 -1060 -2119 1184 C ATOM 57 O MET A 36 17.938 21.249 -5.499 1.00112.25 O ANISOU 57 O MET A 36 10218 13464 18967 -1047 -1981 1115 O ATOM 58 CB MET A 36 15.600 23.168 -4.440 1.00113.86 C ANISOU 58 CB MET A 36 10166 13295 19801 -1020 -1927 1265 C ATOM 59 CG MET A 36 16.205 22.900 -3.081 1.00112.67 C ANISOU 59 CG MET A 36 10043 13172 19595 -990 -1674 1208 C ATOM 60 SD MET A 36 14.961 22.454 -1.851 1.00113.00 S ANISOU 60 SD MET A 36 9929 13018 19988 -936 -1514 1197 S ATOM 61 CE MET A 36 15.968 22.394 -0.393 1.00111.60 C ANISOU 61 CE MET A 36 9844 12909 19650 -908 -1238 1140 C ATOM 62 N GLY A 37 16.331 21.392 -7.096 1.00108.83 N ANISOU 62 N GLY A 37 9693 12890 18767 -1070 -2332 1191 N ATOM 63 CA GLY A 37 16.557 20.098 -7.731 1.00108.88 C ANISOU 63 CA GLY A 37 9748 12970 18652 -1069 -2427 1114 C ATOM 64 C GLY A 37 17.928 19.978 -8.363 1.00108.26 C ANISOU 64 C GLY A 37 9832 13092 18209 -1090 -2435 1079 C ATOM 65 O GLY A 37 18.578 18.939 -8.228 1.00107.53 O ANISOU 65 O GLY A 37 9792 13088 17976 -1072 -2373 993 O ATOM 66 N ILE A 38 18.384 21.058 -9.040 1.00103.47 N ANISOU 66 N ILE A 38 9304 12555 17455 -1126 -2502 1147 N ATOM 67 CA ILE A 38 19.700 21.156 -9.690 1.00103.07 C ANISOU 67 CA ILE A 38 9404 12695 17064 -1152 -2499 1132 C ATOM 68 C ILE A 38 20.799 21.131 -8.613 1.00101.57 C ANISOU 68 C ILE A 38 9244 12598 16750 -1140 -2263 1086 C ATOM 69 O ILE A 38 21.823 20.471 -8.804 1.00100.99 O ANISOU 69 O ILE A 38 9258 12670 16444 -1136 -2218 1021 O ATOM 70 CB ILE A 38 19.790 22.413 -10.621 1.00103.91 C ANISOU 70 CB ILE A 38 9575 12827 17080 -1198 -2623 1234 C ATOM 71 CG1 ILE A 38 18.623 22.493 -11.656 1.00105.56 C ANISOU 71 CG1 ILE A 38 9753 12929 17427 -1207 -2876 1287 C ATOM 72 CG2 ILE A 38 21.169 22.569 -11.291 1.00103.59 C ANISOU 72 CG2 ILE A 38 9686 12983 16691 -1230 -2600 1228 C ATOM 73 CD1 ILE A 38 18.493 21.332 -12.736 1.00106.42 C ANISOU 73 CD1 ILE A 38 9926 13086 17423 -1203 -3056 1222 C ATOM 74 N VAL A 39 20.558 21.822 -7.476 1.00 96.86 N ANISOU 74 N VAL A 39 8575 11912 16316 -1129 -2117 1117 N ATOM 75 CA VAL A 39 21.460 21.891 -6.318 1.00 95.58 C ANISOU 75 CA VAL A 39 8435 11810 16071 -1115 -1900 1078 C ATOM 76 C VAL A 39 21.608 20.487 -5.705 1.00 94.97 C ANISOU 76 C VAL A 39 8345 11751 15988 -1070 -1812 979 C ATOM 77 O VAL A 39 22.735 20.043 -5.477 1.00 94.15 O ANISOU 77 O VAL A 39 8316 11781 15676 -1063 -1722 921 O ATOM 78 CB VAL A 39 20.995 22.955 -5.277 1.00 95.46 C ANISOU 78 CB VAL A 39 8350 11670 16250 -1109 -1782 1131 C ATOM 79 CG1 VAL A 39 21.856 22.929 -4.014 1.00 94.29 C ANISOU 79 CG1 VAL A 39 8230 11571 16025 -1089 -1566 1081 C ATOM 80 CG2 VAL A 39 20.988 24.355 -5.885 1.00 95.73 C ANISOU 80 CG2 VAL A 39 8410 11695 16267 -1154 -1863 1227 C ATOM 81 N MET A 40 20.475 19.785 -5.489 1.00 92.86 N ANISOU 81 N MET A 40 7982 11346 15955 -1041 -1846 964 N ATOM 82 CA MET A 40 20.449 18.429 -4.935 1.00 92.46 C ANISOU 82 CA MET A 40 7911 11285 15935 -1000 -1774 880 C ATOM 83 C MET A 40 21.032 17.379 -5.885 1.00 92.67 C ANISOU 83 C MET A 40 8018 11430 15762 -1000 -1883 811 C ATOM 84 O MET A 40 21.586 16.388 -5.411 1.00 92.23 O ANISOU 84 O MET A 40 7992 11428 15624 -968 -1792 735 O ATOM 85 CB MET A 40 19.043 18.043 -4.454 1.00 92.97 C ANISOU 85 CB MET A 40 7842 11159 16324 -976 -1775 891 C ATOM 86 CG MET A 40 18.703 18.625 -3.101 1.00 92.34 C ANISOU 86 CG MET A 40 7698 10977 16410 -953 -1582 920 C ATOM 87 SD MET A 40 17.166 17.977 -2.409 1.00 93.18 S ANISOU 87 SD MET A 40 7645 10870 16889 -920 -1536 925 S ATOM 88 CE MET A 40 17.188 18.764 -0.819 1.00 92.32 C ANISOU 88 CE MET A 40 7518 10693 16866 -890 -1277 948 C ATOM 89 N SER A 41 20.931 17.608 -7.216 1.00 90.55 N ANISOU 89 N SER A 41 7795 11203 15406 -1033 -2075 838 N ATOM 90 CA SER A 41 21.481 16.717 -8.245 1.00 90.88 C ANISOU 90 CA SER A 41 7931 11360 15239 -1032 -2188 774 C ATOM 91 C SER A 41 23.012 16.760 -8.235 1.00 89.93 C ANISOU 91 C SER A 41 7921 11428 14820 -1034 -2079 738 C ATOM 92 O SER A 41 23.652 15.728 -8.447 1.00 89.57 O ANISOU 92 O SER A 41 7933 11473 14626 -1008 -2067 654 O ATOM 93 CB SER A 41 20.959 17.096 -9.627 1.00 92.19 C ANISOU 93 CB SER A 41 8129 11515 15384 -1067 -2417 822 C ATOM 94 OG SER A 41 19.557 16.910 -9.717 1.00 93.22 O ANISOU 94 OG SER A 41 8151 11473 15796 -1064 -2541 845 O ATOM 95 N LEU A 42 23.589 17.954 -7.977 1.00 86.38 N ANISOU 95 N LEU A 42 7494 11031 14296 -1063 -1999 801 N ATOM 96 CA LEU A 42 25.036 18.174 -7.896 1.00 85.61 C ANISOU 96 CA LEU A 42 7481 11104 13943 -1072 -1889 779 C ATOM 97 C LEU A 42 25.626 17.516 -6.648 1.00 84.41 C ANISOU 97 C LEU A 42 7311 10974 13787 -1029 -1707 710 C ATOM 98 O LEU A 42 26.778 17.085 -6.685 1.00 83.86 O ANISOU 98 O LEU A 42 7306 11046 13511 -1017 -1642 656 O ATOM 99 CB LEU A 42 25.376 19.674 -7.931 1.00 85.77 C ANISOU 99 CB LEU A 42 7520 11150 13919 -1121 -1864 871 C ATOM 100 CG LEU A 42 25.247 20.373 -9.289 1.00 86.97 C ANISOU 100 CG LEU A 42 7731 11334 13979 -1169 -2030 943 C ATOM 101 CD1 LEU A 42 24.967 21.850 -9.113 1.00 87.26 C ANISOU 101 CD1 LEU A 42 7743 11304 14108 -1210 -2025 1049 C ATOM 102 CD2 LEU A 42 26.494 20.173 -10.143 1.00 87.29 C ANISOU 102 CD2 LEU A 42 7886 11565 13715 -1186 -2031 915 C ATOM 103 N ILE A 43 24.831 17.431 -5.553 1.00 82.33 N ANISOU 103 N ILE A 43 6961 10569 13752 -1003 -1626 715 N ATOM 104 CA ILE A 43 25.213 16.790 -4.287 1.00 81.37 C ANISOU 104 CA ILE A 43 6826 10441 13650 -958 -1457 657 C ATOM 105 C ILE A 43 25.371 15.280 -4.531 1.00 81.36 C ANISOU 105 C ILE A 43 6847 10475 13591 -917 -1485 568 C ATOM 106 O ILE A 43 26.381 14.707 -4.121 1.00 80.69 O ANISOU 106 O ILE A 43 6811 10493 13355 -888 -1391 508 O ATOM 107 CB ILE A 43 24.219 17.137 -3.131 1.00 81.36 C ANISOU 107 CB ILE A 43 6735 10269 13909 -941 -1362 694 C ATOM 108 CG1 ILE A 43 24.259 18.650 -2.804 1.00 81.27 C ANISOU 108 CG1 ILE A 43 6717 10235 13927 -975 -1315 770 C ATOM 109 CG2 ILE A 43 24.498 16.304 -1.865 1.00 80.63 C ANISOU 109 CG2 ILE A 43 6640 10158 13837 -889 -1199 634 C ATOM 110 CD1 ILE A 43 22.985 19.229 -2.146 1.00 81.74 C ANISOU 110 CD1 ILE A 43 6681 10108 14269 -968 -1279 825 C ATOM 111 N VAL A 44 24.403 14.663 -5.253 1.00 82.11 N ANISOU 111 N VAL A 44 6909 10485 13805 -915 -1626 559 N ATOM 112 CA VAL A 44 24.399 13.242 -5.640 1.00 82.34 C ANISOU 112 CA VAL A 44 6960 10525 13800 -882 -1684 474 C ATOM 113 C VAL A 44 25.653 12.954 -6.488 1.00 82.37 C ANISOU 113 C VAL A 44 7074 10715 13508 -880 -1715 422 C ATOM 114 O VAL A 44 26.338 11.957 -6.248 1.00 81.90 O ANISOU 114 O VAL A 44 7051 10720 13347 -838 -1653 342 O ATOM 115 CB VAL A 44 23.083 12.841 -6.379 1.00 83.43 C ANISOU 115 CB VAL A 44 7041 10531 14128 -893 -1858 482 C ATOM 116 CG1 VAL A 44 23.123 11.392 -6.865 1.00 83.72 C ANISOU 116 CG1 VAL A 44 7113 10580 14117 -863 -1933 389 C ATOM 117 CG2 VAL A 44 21.858 13.066 -5.498 1.00 83.50 C ANISOU 117 CG2 VAL A 44 6926 10354 14447 -890 -1809 532 C ATOM 118 N LEU A 45 25.964 13.859 -7.442 1.00 82.59 N ANISOU 118 N LEU A 45 7152 10825 13403 -925 -1799 471 N ATOM 119 CA LEU A 45 27.129 13.777 -8.323 1.00 82.83 C ANISOU 119 CA LEU A 45 7286 11034 13152 -931 -1819 437 C ATOM 120 C LEU A 45 28.439 13.918 -7.532 1.00 81.84 C ANISOU 120 C LEU A 45 7182 11030 12883 -915 -1644 414 C ATOM 121 O LEU A 45 29.400 13.215 -7.837 1.00 81.86 O ANISOU 121 O LEU A 45 7243 11156 12704 -887 -1615 343 O ATOM 122 CB LEU A 45 27.039 14.848 -9.428 1.00 83.71 C ANISOU 122 CB LEU A 45 7442 11184 13180 -987 -1938 516 C ATOM 123 CG LEU A 45 27.982 14.689 -10.627 1.00 84.61 C ANISOU 123 CG LEU A 45 7672 11465 13011 -997 -1988 487 C ATOM 124 CD1 LEU A 45 27.383 13.773 -11.687 1.00 85.98 C ANISOU 124 CD1 LEU A 45 7897 11616 13156 -979 -2154 430 C ATOM 125 CD2 LEU A 45 28.298 16.036 -11.245 1.00 84.30 C ANISOU 125 CD2 LEU A 45 7674 11483 12873 -1057 -2021 586 C ATOM 126 N ALA A 46 28.465 14.806 -6.513 1.00 80.35 N ANISOU 126 N ALA A 46 6946 10802 12781 -931 -1533 469 N ATOM 127 CA ALA A 46 29.635 15.041 -5.659 1.00 79.45 C ANISOU 127 CA ALA A 46 6846 10787 12555 -921 -1379 451 C ATOM 128 C ALA A 46 29.966 13.834 -4.777 1.00 78.83 C ANISOU 128 C ALA A 46 6760 10705 12486 -855 -1285 367 C ATOM 129 O ALA A 46 31.144 13.572 -4.524 1.00 78.51 O ANISOU 129 O ALA A 46 6754 10788 12289 -833 -1203 322 O ATOM 130 CB ALA A 46 29.421 16.275 -4.797 1.00 78.98 C ANISOU 130 CB ALA A 46 6744 10660 12604 -953 -1303 527 C ATOM 131 N ILE A 47 28.930 13.102 -4.317 1.00 77.72 N ANISOU 131 N ILE A 47 6572 10421 12537 -824 -1297 349 N ATOM 132 CA ILE A 47 29.083 11.914 -3.472 1.00 77.25 C ANISOU 132 CA ILE A 47 6508 10333 12511 -762 -1213 279 C ATOM 133 C ILE A 47 29.610 10.724 -4.294 1.00 77.61 C ANISOU 133 C ILE A 47 6607 10465 12417 -727 -1278 193 C ATOM 134 O ILE A 47 30.604 10.114 -3.898 1.00 77.14 O ANISOU 134 O ILE A 47 6579 10494 12236 -683 -1196 134 O ATOM 135 CB ILE A 47 27.780 11.585 -2.675 1.00 77.31 C ANISOU 135 CB ILE A 47 6444 10150 12780 -746 -1190 299 C ATOM 136 CG1 ILE A 47 27.401 12.735 -1.710 1.00 76.90 C ANISOU 136 CG1 ILE A 47 6349 10019 12850 -768 -1094 373 C ATOM 137 CG2 ILE A 47 27.918 10.267 -1.905 1.00 77.02 C ANISOU 137 CG2 ILE A 47 6413 10080 12771 -684 -1113 230 C ATOM 138 CD1 ILE A 47 25.913 12.802 -1.308 1.00 77.27 C ANISOU 138 CD1 ILE A 47 6311 9874 13174 -771 -1099 418 C ATOM 139 N VAL A 48 28.954 10.412 -5.435 1.00 78.56 N ANISOU 139 N VAL A 48 6739 10556 12554 -742 -1428 183 N ATOM 140 CA VAL A 48 29.316 9.297 -6.323 1.00 79.12 C ANISOU 140 CA VAL A 48 6870 10693 12499 -709 -1505 96 C ATOM 141 C VAL A 48 30.712 9.476 -6.942 1.00 79.05 C ANISOU 141 C VAL A 48 6935 10878 12222 -706 -1474 66 C ATOM 142 O VAL A 48 31.602 8.684 -6.633 1.00 78.65 O ANISOU 142 O VAL A 48 6909 10904 12070 -654 -1397 -4 O ATOM 143 CB VAL A 48 28.216 8.966 -7.374 1.00 80.27 C ANISOU 143 CB VAL A 48 7018 10748 12733 -729 -1686 92 C ATOM 144 CG1 VAL A 48 28.651 7.834 -8.304 1.00 80.90 C ANISOU 144 CG1 VAL A 48 7177 10899 12663 -693 -1765 -7 C ATOM 145 CG2 VAL A 48 26.896 8.612 -6.697 1.00 80.45 C ANISOU 145 CG2 VAL A 48 6952 10577 13039 -726 -1703 112 C ATOM 146 N PHE A 49 30.903 10.519 -7.784 1.00 78.71 N ANISOU 146 N PHE A 49 6923 10910 12073 -761 -1529 125 N ATOM 147 CA PHE A 49 32.166 10.837 -8.469 1.00 78.86 C ANISOU 147 CA PHE A 49 7007 11111 11846 -770 -1496 113 C ATOM 148 C PHE A 49 33.361 10.978 -7.516 1.00 77.93 C ANISOU 148 C PHE A 49 6869 11089 11653 -749 -1335 99 C ATOM 149 O PHE A 49 34.465 10.550 -7.860 1.00 78.03 O ANISOU 149 O PHE A 49 6920 11238 11489 -720 -1288 43 O ATOM 150 CB PHE A 49 32.001 12.084 -9.363 1.00 79.52 C ANISOU 150 CB PHE A 49 7118 11227 11869 -841 -1572 203 C ATOM 151 CG PHE A 49 33.250 12.611 -10.031 1.00 79.81 C ANISOU 151 CG PHE A 49 7214 11442 11668 -864 -1522 213 C ATOM 152 CD1 PHE A 49 33.744 12.019 -11.187 1.00 80.71 C ANISOU 152 CD1 PHE A 49 7414 11663 11590 -845 -1573 156 C ATOM 153 CD2 PHE A 49 33.907 13.729 -9.529 1.00 79.31 C ANISOU 153 CD2 PHE A 49 7122 11435 11577 -907 -1425 281 C ATOM 154 CE1 PHE A 49 34.893 12.515 -11.810 1.00 81.10 C ANISOU 154 CE1 PHE A 49 7513 11876 11425 -867 -1510 171 C ATOM 155 CE2 PHE A 49 35.055 14.224 -10.151 1.00 79.69 C ANISOU 155 CE2 PHE A 49 7214 11644 11421 -934 -1373 297 C ATOM 156 CZ PHE A 49 35.537 13.617 -11.290 1.00 80.60 C ANISOU 156 CZ PHE A 49 7408 11867 11349 -914 -1410 245 C ATOM 157 N GLY A 50 33.121 11.559 -6.341 1.00 74.51 N ANISOU 157 N GLY A 50 6376 10579 11356 -761 -1256 148 N ATOM 158 CA GLY A 50 34.130 11.751 -5.306 1.00 73.68 C ANISOU 158 CA GLY A 50 6251 10541 11203 -743 -1118 139 C ATOM 159 C GLY A 50 34.612 10.448 -4.702 1.00 73.38 C ANISOU 159 C GLY A 50 6217 10517 11147 -665 -1059 49 C ATOM 160 O GLY A 50 35.820 10.196 -4.662 1.00 73.40 O ANISOU 160 O GLY A 50 6234 10649 11005 -637 -994 5 O ATOM 161 N ASN A 51 33.666 9.609 -4.233 1.00 70.57 N ANISOU 161 N ASN A 51 5843 10022 10948 -628 -1079 23 N ATOM 162 CA ASN A 51 33.961 8.310 -3.621 1.00 70.36 C ANISOU 162 CA ASN A 51 5824 9980 10930 -553 -1030 -55 C ATOM 163 C ASN A 51 34.469 7.256 -4.608 1.00 71.06 C ANISOU 163 C ASN A 51 5962 10151 10886 -509 -1086 -143 C ATOM 164 O ASN A 51 35.222 6.373 -4.194 1.00 70.94 O ANISOU 164 O ASN A 51 5960 10183 10811 -445 -1027 -211 O ATOM 165 CB ASN A 51 32.785 7.797 -2.793 1.00 70.14 C ANISOU 165 CB ASN A 51 5761 9771 11118 -534 -1022 -45 C ATOM 166 CG ASN A 51 32.614 8.534 -1.487 1.00 69.46 C ANISOU 166 CG ASN A 51 5641 9618 11133 -545 -917 15 C ATOM 167 OD1 ASN A 51 33.388 8.361 -0.538 1.00 68.92 O ANISOU 167 OD1 ASN A 51 5584 9589 11013 -508 -818 -5 O ATOM 168 ND2 ASN A 51 31.590 9.368 -1.406 1.00 69.57 N ANISOU 168 ND2 ASN A 51 5616 9526 11292 -594 -939 87 N ATOM 169 N VAL A 52 34.076 7.352 -5.905 1.00 72.89 N ANISOU 169 N VAL A 52 6228 10401 11066 -541 -1202 -144 N ATOM 170 CA VAL A 52 34.530 6.446 -6.974 1.00 73.74 C ANISOU 170 CA VAL A 52 6400 10589 11029 -502 -1262 -230 C ATOM 171 C VAL A 52 36.053 6.591 -7.126 1.00 73.74 C ANISOU 171 C VAL A 52 6420 10773 10825 -481 -1171 -260 C ATOM 172 O VAL A 52 36.761 5.584 -7.146 1.00 73.94 O ANISOU 172 O VAL A 52 6468 10854 10771 -413 -1137 -346 O ATOM 173 CB VAL A 52 33.751 6.656 -8.311 1.00 74.73 C ANISOU 173 CB VAL A 52 6570 10691 11133 -546 -1412 -216 C ATOM 174 CG1 VAL A 52 34.562 6.225 -9.535 1.00 75.68 C ANISOU 174 CG1 VAL A 52 6776 10951 11029 -523 -1446 -285 C ATOM 175 CG2 VAL A 52 32.413 5.927 -8.284 1.00 75.09 C ANISOU 175 CG2 VAL A 52 6598 10562 11371 -539 -1516 -234 C ATOM 176 N LEU A 53 36.543 7.850 -7.157 1.00 72.74 N ANISOU 176 N LEU A 53 6277 10729 10632 -540 -1127 -186 N ATOM 177 CA LEU A 53 37.960 8.198 -7.270 1.00 72.83 C ANISOU 177 CA LEU A 53 6289 10910 10474 -536 -1036 -195 C ATOM 178 C LEU A 53 38.807 7.656 -6.116 1.00 72.18 C ANISOU 178 C LEU A 53 6166 10855 10404 -475 -929 -241 C ATOM 179 O LEU A 53 39.951 7.268 -6.347 1.00 72.56 O ANISOU 179 O LEU A 53 6219 11031 10319 -434 -874 -296 O ATOM 180 CB LEU A 53 38.137 9.719 -7.396 1.00 72.69 C ANISOU 180 CB LEU A 53 6252 10940 10426 -622 -1017 -94 C ATOM 181 CG LEU A 53 37.935 10.312 -8.791 1.00 73.68 C ANISOU 181 CG LEU A 53 6434 11121 10440 -676 -1096 -55 C ATOM 182 CD1 LEU A 53 37.549 11.773 -8.708 1.00 73.54 C ANISOU 182 CD1 LEU A 53 6394 11068 10480 -763 -1110 61 C ATOM 183 CD2 LEU A 53 39.184 10.150 -9.647 1.00 74.26 C ANISOU 183 CD2 LEU A 53 6545 11373 10298 -661 -1040 -95 C ATOM 184 N VAL A 54 38.245 7.616 -4.888 1.00 69.56 N ANISOU 184 N VAL A 54 5797 10401 10231 -465 -900 -217 N ATOM 185 CA VAL A 54 38.919 7.112 -3.682 1.00 68.96 C ANISOU 185 CA VAL A 54 5695 10330 10177 -406 -811 -251 C ATOM 186 C VAL A 54 39.120 5.587 -3.780 1.00 69.29 C ANISOU 186 C VAL A 54 5764 10364 10199 -316 -820 -350 C ATOM 187 O VAL A 54 40.238 5.111 -3.574 1.00 69.39 O ANISOU 187 O VAL A 54 5770 10476 10119 -260 -763 -403 O ATOM 188 CB VAL A 54 38.199 7.544 -2.370 1.00 68.16 C ANISOU 188 CB VAL A 54 5565 10094 10238 -422 -773 -193 C ATOM 189 CG1 VAL A 54 38.921 7.018 -1.130 1.00 67.67 C ANISOU 189 CG1 VAL A 54 5493 10039 10179 -359 -689 -226 C ATOM 190 CG2 VAL A 54 38.057 9.062 -2.293 1.00 67.92 C ANISOU 190 CG2 VAL A 54 5511 10069 10226 -507 -764 -102 C ATOM 191 N ILE A 55 38.047 4.841 -4.122 1.00 69.30 N ANISOU 191 N ILE A 55 5792 10245 10294 -302 -898 -375 N ATOM 192 CA ILE A 55 38.057 3.378 -4.277 1.00 69.71 C ANISOU 192 CA ILE A 55 5876 10263 10348 -223 -922 -468 C ATOM 193 C ILE A 55 38.973 2.951 -5.442 1.00 70.58 C ANISOU 193 C ILE A 55 6027 10516 10273 -189 -938 -544 C ATOM 194 O ILE A 55 39.722 1.982 -5.299 1.00 70.81 O ANISOU 194 O ILE A 55 6067 10588 10250 -110 -901 -622 O ATOM 195 CB ILE A 55 36.606 2.802 -4.380 1.00 69.90 C ANISOU 195 CB ILE A 55 5911 10111 10536 -231 -1010 -468 C ATOM 196 CG1 ILE A 55 35.775 3.160 -3.123 1.00 69.14 C ANISOU 196 CG1 ILE A 55 5770 9875 10626 -254 -965 -395 C ATOM 197 CG2 ILE A 55 36.604 1.277 -4.612 1.00 70.40 C ANISOU 197 CG2 ILE A 55 6013 10130 10605 -154 -1045 -568 C ATOM 198 CD1 ILE A 55 34.253 3.243 -3.327 1.00 69.40 C ANISOU 198 CD1 ILE A 55 5784 9748 10836 -301 -1048 -354 C ATOM 199 N THR A 56 38.937 3.698 -6.569 1.00 71.49 N ANISOU 199 N THR A 56 6168 10706 10288 -248 -986 -517 N ATOM 200 CA THR A 56 39.755 3.430 -7.759 1.00 72.47 C ANISOU 200 CA THR A 56 6342 10970 10223 -224 -990 -579 C ATOM 201 C THR A 56 41.251 3.655 -7.489 1.00 72.39 C ANISOU 201 C THR A 56 6294 11118 10093 -196 -873 -593 C ATOM 202 O THR A 56 42.055 2.802 -7.862 1.00 72.99 O ANISOU 202 O THR A 56 6389 11272 10072 -123 -840 -680 O ATOM 203 CB THR A 56 39.230 4.199 -8.988 1.00 73.17 C ANISOU 203 CB THR A 56 6480 11083 10238 -296 -1075 -536 C ATOM 204 OG1 THR A 56 37.812 4.049 -9.069 1.00 73.45 O ANISOU 204 OG1 THR A 56 6530 10959 10419 -324 -1191 -516 O ATOM 205 CG2 THR A 56 39.857 3.723 -10.296 1.00 74.30 C ANISOU 205 CG2 THR A 56 6701 11345 10185 -264 -1091 -611 C ATOM 206 N ALA A 57 41.617 4.778 -6.828 1.00 72.56 N ANISOU 206 N ALA A 57 6257 11179 10134 -251 -812 -510 N ATOM 207 CA ALA A 57 43.008 5.122 -6.498 1.00 72.51 C ANISOU 207 CA ALA A 57 6199 11314 10038 -237 -709 -512 C ATOM 208 C ALA A 57 43.692 4.086 -5.601 1.00 72.27 C ANISOU 208 C ALA A 57 6138 11283 10038 -141 -656 -583 C ATOM 209 O ALA A 57 44.881 3.827 -5.779 1.00 72.81 O ANISOU 209 O ALA A 57 6179 11478 10007 -96 -592 -630 O ATOM 210 CB ALA A 57 43.080 6.499 -5.856 1.00 71.83 C ANISOU 210 CB ALA A 57 6061 11235 9996 -320 -675 -410 C ATOM 211 N ILE A 58 42.943 3.492 -4.653 1.00 72.38 N ANISOU 211 N ILE A 58 6157 11152 10192 -109 -680 -588 N ATOM 212 CA ILE A 58 43.458 2.471 -3.737 1.00 72.20 C ANISOU 212 CA ILE A 58 6119 11106 10208 -16 -641 -646 C ATOM 213 C ILE A 58 43.626 1.125 -4.469 1.00 73.07 C ANISOU 213 C ILE A 58 6274 11224 10265 70 -667 -753 C ATOM 214 O ILE A 58 44.672 0.489 -4.334 1.00 73.45 O ANISOU 214 O ILE A 58 6302 11351 10255 147 -617 -815 O ATOM 215 CB ILE A 58 42.605 2.384 -2.430 1.00 71.35 C ANISOU 215 CB ILE A 58 6009 10839 10262 -16 -645 -602 C ATOM 216 CG1 ILE A 58 42.700 3.706 -1.626 1.00 70.62 C ANISOU 216 CG1 ILE A 58 5876 10756 10200 -88 -604 -511 C ATOM 217 CG2 ILE A 58 43.012 1.183 -1.555 1.00 71.34 C ANISOU 217 CG2 ILE A 58 6013 10795 10299 85 -617 -661 C ATOM 218 CD1 ILE A 58 41.537 3.998 -0.660 1.00 69.96 C ANISOU 218 CD1 ILE A 58 5802 10509 10270 -119 -610 -448 C ATOM 219 N ALA A 59 42.615 0.719 -5.262 1.00 76.01 N ANISOU 219 N ALA A 59 6706 11513 10661 57 -749 -775 N ATOM 220 CA ALA A 59 42.619 -0.538 -6.017 1.00 76.92 C ANISOU 220 CA ALA A 59 6878 11616 10732 131 -790 -881 C ATOM 221 C ALA A 59 43.615 -0.570 -7.186 1.00 77.94 C ANISOU 221 C ALA A 59 7029 11909 10675 157 -758 -941 C ATOM 222 O ALA A 59 44.291 -1.585 -7.368 1.00 78.60 O ANISOU 222 O ALA A 59 7127 12031 10707 249 -731 -1036 O ATOM 223 CB ALA A 59 41.216 -0.863 -6.508 1.00 77.19 C ANISOU 223 CB ALA A 59 6968 11507 10854 99 -900 -883 C ATOM 224 N LYS A 60 43.702 0.524 -7.975 1.00 81.35 N ANISOU 224 N LYS A 60 7466 12434 11009 78 -756 -886 N ATOM 225 CA LYS A 60 44.591 0.619 -9.138 1.00 82.41 C ANISOU 225 CA LYS A 60 7627 12726 10958 90 -713 -929 C ATOM 226 C LYS A 60 46.063 0.774 -8.743 1.00 82.52 C ANISOU 226 C LYS A 60 7561 12883 10909 129 -592 -940 C ATOM 227 O LYS A 60 46.891 -0.029 -9.176 1.00 83.45 O ANISOU 227 O LYS A 60 7687 13080 10940 213 -543 -1030 O ATOM 228 CB LYS A 60 44.146 1.749 -10.084 1.00 82.50 C ANISOU 228 CB LYS A 60 7677 12779 10890 -11 -753 -855 C ATOM 229 CG LYS A 60 44.440 1.482 -11.557 1.00 83.88 C ANISOU 229 CG LYS A 60 7941 13050 10880 7 -761 -917 C ATOM 230 CD LYS A 60 43.806 2.532 -12.475 1.00 83.96 C ANISOU 230 CD LYS A 60 8008 13073 10820 -92 -825 -836 C ATOM 231 CE LYS A 60 42.374 2.213 -12.850 1.00 84.86 C ANISOU 231 CE LYS A 60 8197 13036 11009 -114 -978 -842 C ATOM 232 NZ LYS A 60 41.762 3.295 -13.666 1.00 84.84 N ANISOU 232 NZ LYS A 60 8245 13040 10950 -209 -1050 -754 N ATOM 233 N PHE A 61 46.386 1.799 -7.929 1.00 83.61 N ANISOU 233 N PHE A 61 7620 13050 11097 71 -546 -850 N ATOM 234 CA PHE A 61 47.752 2.071 -7.478 1.00 83.67 C ANISOU 234 CA PHE A 61 7538 13186 11067 94 -444 -850 C ATOM 235 C PHE A 61 48.156 1.161 -6.324 1.00 83.34 C ANISOU 235 C PHE A 61 7453 13094 11118 187 -427 -899 C ATOM 236 O PHE A 61 47.429 1.056 -5.334 1.00 82.39 O ANISOU 236 O PHE A 61 7338 12843 11124 183 -470 -868 O ATOM 237 CB PHE A 61 47.922 3.547 -7.077 1.00 82.97 C ANISOU 237 CB PHE A 61 7388 13139 10997 -10 -415 -737 C ATOM 238 CG PHE A 61 47.835 4.538 -8.213 1.00 83.51 C ANISOU 238 CG PHE A 61 7486 13286 10957 -99 -410 -680 C ATOM 239 CD1 PHE A 61 46.617 5.100 -8.575 1.00 83.64 C ANISOU 239 CD1 PHE A 61 7566 13211 11002 -174 -494 -619 C ATOM 240 CD2 PHE A 61 48.976 4.936 -8.899 1.00 83.97 C ANISOU 240 CD2 PHE A 61 7505 13508 10892 -110 -319 -680 C ATOM 241 CE1 PHE A 61 46.538 6.025 -9.621 1.00 84.22 C ANISOU 241 CE1 PHE A 61 7676 13353 10971 -255 -497 -558 C ATOM 242 CE2 PHE A 61 48.897 5.862 -9.943 1.00 84.54 C ANISOU 242 CE2 PHE A 61 7614 13650 10857 -194 -308 -618 C ATOM 243 CZ PHE A 61 47.679 6.400 -10.297 1.00 84.67 C ANISOU 243 CZ PHE A 61 7706 13572 10893 -266 -402 -556 C ATOM 244 N GLU A 62 49.327 0.512 -6.452 1.00 86.15 N ANISOU 244 N GLU A 62 7767 13553 11413 273 -361 -973 N ATOM 245 CA GLU A 62 49.891 -0.374 -5.428 1.00 86.06 C ANISOU 245 CA GLU A 62 7712 13510 11477 372 -345 -1022 C ATOM 246 C GLU A 62 50.431 0.457 -4.258 1.00 85.30 C ANISOU 246 C GLU A 62 7528 13437 11445 334 -317 -948 C ATOM 247 O GLU A 62 50.474 -0.029 -3.128 1.00 84.72 O ANISOU 247 O GLU A 62 7440 13288 11462 386 -334 -952 O ATOM 248 CB GLU A 62 51.008 -1.252 -6.021 1.00 87.36 C ANISOU 248 CB GLU A 62 7851 13783 11558 476 -282 -1124 C ATOM 249 CG GLU A 62 50.519 -2.303 -7.006 1.00 88.27 C ANISOU 249 CG GLU A 62 8065 13856 11617 537 -316 -1219 C ATOM 250 CD GLU A 62 51.609 -3.136 -7.654 1.00 89.63 C ANISOU 250 CD GLU A 62 8220 14134 11701 644 -243 -1325 C ATOM 251 OE1 GLU A 62 52.432 -2.565 -8.406 1.00 90.40 O ANISOU 251 OE1 GLU A 62 8276 14382 11690 624 -160 -1322 O ATOM 252 OE2 GLU A 62 51.620 -4.369 -7.434 1.00 90.01 O ANISOU 252 OE2 GLU A 62 8298 14110 11792 750 -266 -1411 O ATOM 253 N ARG A 63 50.820 1.717 -4.547 1.00 85.39 N ANISOU 253 N ARG A 63 7490 13548 11407 240 -279 -878 N ATOM 254 CA ARG A 63 51.367 2.730 -3.639 1.00 84.89 C ANISOU 254 CA ARG A 63 7345 13521 11389 182 -255 -805 C ATOM 255 C ARG A 63 50.473 3.003 -2.415 1.00 83.66 C ANISOU 255 C ARG A 63 7219 13218 11350 150 -312 -747 C ATOM 256 O ARG A 63 50.999 3.214 -1.320 1.00 83.30 O ANISOU 256 O ARG A 63 7123 13170 11357 160 -306 -726 O ATOM 257 CB ARG A 63 51.611 4.029 -4.431 1.00 85.26 C ANISOU 257 CB ARG A 63 7363 13671 11361 72 -217 -736 C ATOM 258 CG ARG A 63 52.510 5.057 -3.758 1.00 85.23 C ANISOU 258 CG ARG A 63 7257 13743 11384 14 -178 -676 C ATOM 259 CD ARG A 63 52.903 6.137 -4.747 1.00 85.59 C ANISOU 259 CD ARG A 63 7273 13904 11343 -81 -124 -621 C ATOM 260 NE ARG A 63 53.500 7.303 -4.093 1.00 85.90 N ANISOU 260 NE ARG A 63 7227 13984 11426 -163 -105 -548 N ATOM 261 CZ ARG A 63 52.876 8.462 -3.906 1.00 85.43 C ANISOU 261 CZ ARG A 63 7190 13871 11399 -271 -135 -458 C ATOM 262 NH1 ARG A 63 51.625 8.627 -4.321 1.00 84.61 N ANISOU 262 NH1 ARG A 63 7183 13671 11294 -309 -187 -426 N ATOM 263 NH2 ARG A 63 53.498 9.467 -3.305 1.00 85.88 N ANISOU 263 NH2 ARG A 63 7169 13964 11498 -341 -120 -402 N ATOM 264 N LEU A 64 49.137 3.004 -2.604 1.00 78.75 N ANISOU 264 N LEU A 64 6679 12474 10768 114 -366 -721 N ATOM 265 CA LEU A 64 48.164 3.268 -1.538 1.00 77.72 C ANISOU 265 CA LEU A 64 6580 12197 10752 82 -406 -665 C ATOM 266 C LEU A 64 47.393 2.014 -1.078 1.00 77.44 C ANISOU 266 C LEU A 64 6607 12021 10796 161 -444 -710 C ATOM 267 O LEU A 64 46.199 2.099 -0.782 1.00 76.78 O ANISOU 267 O LEU A 64 6571 11804 10798 126 -481 -670 O ATOM 268 CB LEU A 64 47.200 4.401 -1.953 1.00 77.37 C ANISOU 268 CB LEU A 64 6563 12110 10724 -31 -433 -583 C ATOM 269 CG LEU A 64 47.768 5.821 -1.960 1.00 77.29 C ANISOU 269 CG LEU A 64 6497 12191 10679 -124 -400 -511 C ATOM 270 CD1 LEU A 64 47.039 6.688 -2.960 1.00 77.36 C ANISOU 270 CD1 LEU A 64 6538 12198 10657 -217 -426 -453 C ATOM 271 CD2 LEU A 64 47.710 6.451 -0.574 1.00 76.50 C ANISOU 271 CD2 LEU A 64 6377 12023 10666 -150 -397 -458 C ATOM 272 N GLN A 65 48.083 0.860 -0.989 1.00 74.93 N ANISOU 272 N GLN A 65 6283 11728 10460 268 -432 -791 N ATOM 273 CA GLN A 65 47.476 -0.402 -0.551 1.00 74.83 C ANISOU 273 CA GLN A 65 6328 11582 10522 348 -465 -837 C ATOM 274 C GLN A 65 47.862 -0.770 0.896 1.00 74.47 C ANISOU 274 C GLN A 65 6271 11484 10541 408 -453 -826 C ATOM 275 O GLN A 65 48.216 -1.919 1.179 1.00 74.94 O ANISOU 275 O GLN A 65 6343 11518 10613 509 -457 -887 O ATOM 276 CB GLN A 65 47.764 -1.542 -1.549 1.00 75.74 C ANISOU 276 CB GLN A 65 6468 11731 10579 429 -473 -938 C ATOM 277 CG GLN A 65 46.945 -1.454 -2.831 1.00 76.06 C ANISOU 277 CG GLN A 65 6561 11762 10577 379 -512 -951 C ATOM 278 CD GLN A 65 46.859 -2.777 -3.546 1.00 76.97 C ANISOU 278 CD GLN A 65 6732 11844 10669 464 -540 -1054 C ATOM 279 OE1 GLN A 65 45.940 -3.572 -3.323 1.00 76.95 O ANISOU 279 OE1 GLN A 65 6784 11695 10758 487 -594 -1073 O ATOM 280 NE2 GLN A 65 47.805 -3.037 -4.435 1.00 77.92 N ANISOU 280 NE2 GLN A 65 6839 12096 10672 512 -501 -1125 N ATOM 281 N THR A 66 47.770 0.217 1.811 1.00 70.19 N ANISOU 281 N THR A 66 5715 10919 10035 346 -443 -748 N ATOM 282 CA THR A 66 48.086 0.051 3.236 1.00 69.85 C ANISOU 282 CA THR A 66 5678 10824 10038 390 -437 -727 C ATOM 283 C THR A 66 46.873 -0.441 4.032 1.00 69.35 C ANISOU 283 C THR A 66 5695 10578 10076 400 -450 -696 C ATOM 284 O THR A 66 45.738 -0.277 3.581 1.00 69.10 O ANISOU 284 O THR A 66 5696 10464 10095 345 -462 -671 O ATOM 285 CB THR A 66 48.670 1.344 3.837 1.00 69.56 C ANISOU 285 CB THR A 66 5592 10858 9979 322 -421 -668 C ATOM 286 OG1 THR A 66 47.770 2.429 3.616 1.00 68.94 O ANISOU 286 OG1 THR A 66 5530 10740 9925 214 -420 -601 O ATOM 287 CG2 THR A 66 50.050 1.679 3.295 1.00 70.21 C ANISOU 287 CG2 THR A 66 5582 11115 9980 327 -402 -699 C ATOM 288 N VAL A 67 47.126 -1.027 5.225 1.00 67.05 N ANISOU 288 N VAL A 67 5435 10224 9818 470 -446 -694 N ATOM 289 CA VAL A 67 46.132 -1.571 6.167 1.00 66.73 C ANISOU 289 CA VAL A 67 5474 10011 9869 491 -441 -659 C ATOM 290 C VAL A 67 45.027 -0.542 6.475 1.00 66.02 C ANISOU 290 C VAL A 67 5408 9838 9838 392 -420 -580 C ATOM 291 O VAL A 67 43.846 -0.888 6.421 1.00 65.86 O ANISOU 291 O VAL A 67 5428 9688 9907 375 -418 -560 O ATOM 292 CB VAL A 67 46.803 -2.130 7.457 1.00 66.91 C ANISOU 292 CB VAL A 67 5530 10006 9887 576 -438 -658 C ATOM 293 CG1 VAL A 67 45.783 -2.787 8.387 1.00 66.72 C ANISOU 293 CG1 VAL A 67 5598 9801 9951 602 -419 -619 C ATOM 294 CG2 VAL A 67 47.924 -3.112 7.121 1.00 67.68 C ANISOU 294 CG2 VAL A 67 5592 10185 9939 679 -461 -736 C ATOM 295 N THR A 68 45.415 0.719 6.761 1.00 63.25 N ANISOU 295 N THR A 68 5026 9559 9447 325 -408 -536 N ATOM 296 CA THR A 68 44.487 1.819 7.045 1.00 62.69 C ANISOU 296 CA THR A 68 4972 9419 9429 233 -386 -464 C ATOM 297 C THR A 68 43.679 2.222 5.811 1.00 62.62 C ANISOU 297 C THR A 68 4936 9409 9447 161 -405 -454 C ATOM 298 O THR A 68 42.497 2.539 5.945 1.00 62.27 O ANISOU 298 O THR A 68 4918 9248 9494 114 -395 -407 O ATOM 299 CB THR A 68 45.201 3.011 7.696 1.00 62.52 C ANISOU 299 CB THR A 68 4929 9470 9356 187 -375 -428 C ATOM 300 OG1 THR A 68 46.399 3.311 6.975 1.00 62.93 O ANISOU 300 OG1 THR A 68 4904 9686 9320 182 -396 -464 O ATOM 301 CG2 THR A 68 45.513 2.772 9.164 1.00 62.46 C ANISOU 301 CG2 THR A 68 4982 9403 9347 242 -360 -414 C ATOM 302 N ASN A 69 44.307 2.179 4.613 1.00 62.40 N ANISOU 302 N ASN A 69 4860 9507 9342 157 -432 -500 N ATOM 303 CA ASN A 69 43.662 2.504 3.336 1.00 62.51 C ANISOU 303 CA ASN A 69 4861 9534 9356 96 -462 -496 C ATOM 304 C ASN A 69 42.586 1.488 2.940 1.00 62.73 C ANISOU 304 C ASN A 69 4930 9438 9466 123 -494 -522 C ATOM 305 O ASN A 69 41.668 1.841 2.198 1.00 62.78 O ANISOU 305 O ASN A 69 4938 9400 9516 63 -528 -499 O ATOM 306 CB ASN A 69 44.691 2.686 2.217 1.00 63.01 C ANISOU 306 CB ASN A 69 4875 9766 9299 91 -470 -538 C ATOM 307 CG ASN A 69 45.306 4.067 2.148 1.00 62.81 C ANISOU 307 CG ASN A 69 4800 9847 9218 12 -450 -489 C ATOM 308 OD1 ASN A 69 44.643 5.093 2.348 1.00 62.39 O ANISOU 308 OD1 ASN A 69 4752 9743 9210 -68 -450 -420 O ATOM 309 ND2 ASN A 69 46.583 4.125 1.804 1.00 63.23 N ANISOU 309 ND2 ASN A 69 4799 10048 9178 32 -431 -524 N ATOM 310 N TYR A 70 42.691 0.237 3.448 1.00 62.62 N ANISOU 310 N TYR A 70 4948 9363 9482 213 -490 -568 N ATOM 311 CA TYR A 70 41.717 -0.839 3.229 1.00 62.89 C ANISOU 311 CA TYR A 70 5022 9264 9610 245 -520 -595 C ATOM 312 C TYR A 70 40.410 -0.477 3.944 1.00 62.42 C ANISOU 312 C TYR A 70 4983 9046 9688 194 -500 -519 C ATOM 313 O TYR A 70 39.329 -0.755 3.421 1.00 62.55 O ANISOU 313 O TYR A 70 5005 8963 9798 165 -537 -515 O ATOM 314 CB TYR A 70 42.268 -2.186 3.740 1.00 63.33 C ANISOU 314 CB TYR A 70 5108 9291 9663 354 -512 -653 C ATOM 315 CG TYR A 70 43.025 -3.010 2.715 1.00 64.05 C ANISOU 315 CG TYR A 70 5190 9476 9670 416 -546 -747 C ATOM 316 CD1 TYR A 70 44.056 -2.450 1.962 1.00 64.29 C ANISOU 316 CD1 TYR A 70 5173 9678 9576 404 -542 -775 C ATOM 317 CD2 TYR A 70 42.770 -4.369 2.558 1.00 64.59 C ANISOU 317 CD2 TYR A 70 5298 9459 9784 492 -571 -809 C ATOM 318 CE1 TYR A 70 44.774 -3.210 1.038 1.00 65.08 C ANISOU 318 CE1 TYR A 70 5267 9865 9595 467 -556 -865 C ATOM 319 CE2 TYR A 70 43.489 -5.142 1.645 1.00 65.35 C ANISOU 319 CE2 TYR A 70 5392 9637 9801 557 -596 -903 C ATOM 320 CZ TYR A 70 44.487 -4.556 0.884 1.00 65.61 C ANISOU 320 CZ TYR A 70 5379 9844 9705 547 -584 -932 C ATOM 321 OH TYR A 70 45.195 -5.307 -0.024 1.00 66.47 O ANISOU 321 OH TYR A 70 5489 10034 9733 615 -594 -1027 O ATOM 322 N PHE A 71 40.519 0.176 5.124 1.00 58.02 N ANISOU 322 N PHE A 71 4435 8466 9143 182 -443 -462 N ATOM 323 CA PHE A 71 39.378 0.659 5.903 1.00 57.63 C ANISOU 323 CA PHE A 71 4405 8276 9215 137 -402 -387 C ATOM 324 C PHE A 71 38.815 1.929 5.263 1.00 57.37 C ANISOU 324 C PHE A 71 4332 8263 9203 39 -420 -340 C ATOM 325 O PHE A 71 37.609 2.161 5.340 1.00 57.27 O ANISOU 325 O PHE A 71 4316 8127 9317 -4 -413 -294 O ATOM 326 CB PHE A 71 39.768 0.922 7.367 1.00 57.37 C ANISOU 326 CB PHE A 71 4413 8219 9166 164 -334 -350 C ATOM 327 CG PHE A 71 40.264 -0.279 8.139 1.00 57.69 C ANISOU 327 CG PHE A 71 4505 8225 9190 262 -317 -382 C ATOM 328 CD1 PHE A 71 39.421 -1.351 8.410 1.00 58.01 C ANISOU 328 CD1 PHE A 71 4584 8119 9338 299 -302 -380 C ATOM 329 CD2 PHE A 71 41.556 -0.313 8.646 1.00 57.73 C ANISOU 329 CD2 PHE A 71 4518 8333 9084 314 -318 -407 C ATOM 330 CE1 PHE A 71 39.878 -2.457 9.132 1.00 58.36 C ANISOU 330 CE1 PHE A 71 4683 8123 9368 390 -288 -403 C ATOM 331 CE2 PHE A 71 42.012 -1.417 9.373 1.00 58.11 C ANISOU 331 CE2 PHE A 71 4616 8343 9120 409 -311 -431 C ATOM 332 CZ PHE A 71 41.169 -2.480 9.613 1.00 58.41 C ANISOU 332 CZ PHE A 71 4702 8235 9256 447 -294 -427 C ATOM 333 N ILE A 72 39.689 2.740 4.618 1.00 56.76 N ANISOU 333 N ILE A 72 4220 8337 9009 4 -443 -349 N ATOM 334 CA ILE A 72 39.318 3.968 3.900 1.00 56.63 C ANISOU 334 CA ILE A 72 4169 8355 8993 -87 -467 -303 C ATOM 335 C ILE A 72 38.429 3.593 2.700 1.00 57.03 C ANISOU 335 C ILE A 72 4211 8362 9096 -111 -539 -319 C ATOM 336 O ILE A 72 37.448 4.290 2.433 1.00 56.96 O ANISOU 336 O ILE A 72 4186 8282 9174 -176 -561 -266 O ATOM 337 CB ILE A 72 40.576 4.823 3.520 1.00 56.65 C ANISOU 337 CB ILE A 72 4138 8531 8855 -116 -467 -308 C ATOM 338 CG1 ILE A 72 41.293 5.417 4.772 1.00 56.28 C ANISOU 338 CG1 ILE A 72 4097 8507 8779 -110 -412 -283 C ATOM 339 CG2 ILE A 72 40.293 5.904 2.457 1.00 56.78 C ANISOU 339 CG2 ILE A 72 4125 8599 8850 -205 -506 -269 C ATOM 340 CD1 ILE A 72 40.482 6.433 5.697 1.00 55.85 C ANISOU 340 CD1 ILE A 72 4062 8343 8815 -165 -371 -208 C ATOM 341 N THR A 73 38.745 2.459 2.027 1.00 57.88 N ANISOU 341 N THR A 73 4333 8501 9158 -54 -579 -394 N ATOM 342 CA THR A 73 37.973 1.919 0.901 1.00 58.41 C ANISOU 342 CA THR A 73 4407 8522 9264 -65 -660 -426 C ATOM 343 C THR A 73 36.588 1.497 1.401 1.00 58.37 C ANISOU 343 C THR A 73 4405 8327 9446 -73 -666 -393 C ATOM 344 O THR A 73 35.595 1.799 0.742 1.00 58.57 O ANISOU 344 O THR A 73 4413 8286 9555 -128 -728 -367 O ATOM 345 CB THR A 73 38.707 0.748 0.221 1.00 59.04 C ANISOU 345 CB THR A 73 4511 8671 9250 9 -691 -523 C ATOM 346 OG1 THR A 73 40.109 1.010 0.177 1.00 59.06 O ANISOU 346 OG1 THR A 73 4499 8837 9104 35 -651 -549 O ATOM 347 CG2 THR A 73 38.190 0.475 -1.187 1.00 59.73 C ANISOU 347 CG2 THR A 73 4615 8761 9319 -14 -785 -563 C ATOM 348 N SER A 74 36.529 0.834 2.581 1.00 59.35 N ANISOU 348 N SER A 74 4550 8362 9638 -20 -601 -389 N ATOM 349 CA SER A 74 35.296 0.387 3.239 1.00 59.39 C ANISOU 349 CA SER A 74 4557 8182 9826 -23 -578 -352 C ATOM 350 C SER A 74 34.445 1.588 3.659 1.00 59.04 C ANISOU 350 C SER A 74 4481 8071 9881 -96 -542 -264 C ATOM 351 O SER A 74 33.216 1.517 3.603 1.00 59.28 O ANISOU 351 O SER A 74 4484 7965 10075 -128 -558 -230 O ATOM 352 CB SER A 74 35.624 -0.468 4.458 1.00 59.27 C ANISOU 352 CB SER A 74 4584 8109 9827 51 -500 -358 C ATOM 353 OG SER A 74 34.451 -0.943 5.099 1.00 59.34 O ANISOU 353 OG SER A 74 4597 7937 10013 48 -463 -317 O ATOM 354 N LEU A 75 35.108 2.685 4.072 1.00 60.27 N ANISOU 354 N LEU A 75 4635 8318 9947 -120 -496 -230 N ATOM 355 CA LEU A 75 34.469 3.935 4.474 1.00 59.95 C ANISOU 355 CA LEU A 75 4570 8228 9981 -185 -459 -153 C ATOM 356 C LEU A 75 33.909 4.647 3.239 1.00 60.20 C ANISOU 356 C LEU A 75 4558 8277 10038 -256 -549 -133 C ATOM 357 O LEU A 75 32.786 5.150 3.289 1.00 60.32 O ANISOU 357 O LEU A 75 4540 8179 10200 -300 -552 -78 O ATOM 358 CB LEU A 75 35.478 4.831 5.215 1.00 59.49 C ANISOU 358 CB LEU A 75 4530 8269 9805 -188 -399 -134 C ATOM 359 CG LEU A 75 34.901 5.921 6.120 1.00 59.16 C ANISOU 359 CG LEU A 75 4489 8147 9842 -229 -327 -63 C ATOM 360 CD1 LEU A 75 34.318 5.331 7.394 1.00 59.26 C ANISOU 360 CD1 LEU A 75 4542 8019 9955 -184 -235 -43 C ATOM 361 CD2 LEU A 75 35.964 6.930 6.484 1.00 58.84 C ANISOU 361 CD2 LEU A 75 4461 8224 9671 -248 -303 -55 C ATOM 362 N ALA A 76 34.678 4.654 2.127 1.00 62.64 N ANISOU 362 N ALA A 76 4869 8725 10206 -262 -621 -177 N ATOM 363 CA ALA A 76 34.282 5.257 0.851 1.00 63.01 C ANISOU 363 CA ALA A 76 4894 8806 10241 -323 -716 -162 C ATOM 364 C ALA A 76 33.176 4.445 0.172 1.00 63.63 C ANISOU 364 C ALA A 76 4964 8771 10442 -324 -804 -183 C ATOM 365 O ALA A 76 32.348 5.026 -0.531 1.00 63.99 O ANISOU 365 O ALA A 76 4983 8773 10558 -380 -879 -145 O ATOM 366 CB ALA A 76 35.484 5.383 -0.070 1.00 63.18 C ANISOU 366 CB ALA A 76 4933 9008 10065 -322 -748 -205 C ATOM 367 N CYS A 77 33.157 3.108 0.391 1.00 67.32 N ANISOU 367 N CYS A 77 5453 9184 10942 -261 -801 -242 N ATOM 368 CA CYS A 77 32.139 2.199 -0.145 1.00 68.01 C ANISOU 368 CA CYS A 77 5532 9149 11159 -258 -884 -270 C ATOM 369 C CYS A 77 30.790 2.485 0.507 1.00 68.04 C ANISOU 369 C CYS A 77 5484 8979 11390 -294 -859 -198 C ATOM 370 O CYS A 77 29.790 2.586 -0.201 1.00 68.58 O ANISOU 370 O CYS A 77 5515 8968 11574 -338 -954 -181 O ATOM 371 CB CYS A 77 32.547 0.738 0.032 1.00 68.29 C ANISOU 371 CB CYS A 77 5606 9167 11173 -180 -876 -349 C ATOM 372 SG CYS A 77 33.598 0.093 -1.295 1.00 68.94 S ANISOU 372 SG CYS A 77 5740 9404 11050 -141 -960 -454 S ATOM 373 N ALA A 78 30.775 2.659 1.852 1.00 68.28 N ANISOU 373 N ALA A 78 5512 8952 11480 -276 -732 -154 N ATOM 374 CA ALA A 78 29.584 2.982 2.648 1.00 68.32 C ANISOU 374 CA ALA A 78 5470 8795 11694 -303 -671 -83 C ATOM 375 C ALA A 78 29.009 4.340 2.233 1.00 68.30 C ANISOU 375 C ALA A 78 5417 8789 11745 -374 -707 -18 C ATOM 376 O ALA A 78 27.790 4.521 2.251 1.00 68.72 O ANISOU 376 O ALA A 78 5410 8706 11995 -407 -722 28 O ATOM 377 CB ALA A 78 29.930 2.991 4.128 1.00 67.83 C ANISOU 377 CB ALA A 78 5441 8704 11627 -263 -520 -55 C ATOM 378 N ASP A 79 29.891 5.278 1.838 1.00 67.62 N ANISOU 378 N ASP A 79 5353 8849 11491 -396 -722 -14 N ATOM 379 CA ASP A 79 29.519 6.607 1.361 1.00 67.63 C ANISOU 379 CA ASP A 79 5319 8864 11514 -463 -763 47 C ATOM 380 C ASP A 79 29.016 6.540 -0.085 1.00 68.33 C ANISOU 380 C ASP A 79 5389 8958 11615 -499 -921 35 C ATOM 381 O ASP A 79 28.161 7.340 -0.460 1.00 68.62 O ANISOU 381 O ASP A 79 5379 8931 11763 -550 -977 92 O ATOM 382 CB ASP A 79 30.704 7.582 1.480 1.00 67.04 C ANISOU 382 CB ASP A 79 5277 8940 11255 -476 -720 57 C ATOM 383 CG ASP A 79 31.150 7.892 2.900 1.00 66.44 C ANISOU 383 CG ASP A 79 5224 8854 11166 -451 -582 76 C ATOM 384 OD1 ASP A 79 30.277 7.973 3.797 1.00 66.45 O ANISOU 384 OD1 ASP A 79 5207 8717 11325 -447 -507 117 O ATOM 385 OD2 ASP A 79 32.364 8.105 3.106 1.00 66.06 O ANISOU 385 OD2 ASP A 79 5213 8935 10951 -436 -550 52 O ATOM 386 N LEU A 80 29.536 5.585 -0.889 1.00 67.00 N ANISOU 386 N LEU A 80 5262 8863 11332 -469 -995 -42 N ATOM 387 CA LEU A 80 29.145 5.390 -2.290 1.00 67.81 C ANISOU 387 CA LEU A 80 5371 8977 11417 -496 -1152 -68 C ATOM 388 C LEU A 80 27.719 4.841 -2.426 1.00 68.51 C ANISOU 388 C LEU A 80 5404 8888 11739 -509 -1231 -58 C ATOM 389 O LEU A 80 26.971 5.313 -3.285 1.00 69.11 O ANISOU 389 O LEU A 80 5453 8925 11881 -557 -1353 -29 O ATOM 390 CB LEU A 80 30.160 4.492 -3.029 1.00 68.09 C ANISOU 390 CB LEU A 80 5476 9139 11256 -451 -1193 -162 C ATOM 391 CG LEU A 80 29.940 4.270 -4.534 1.00 69.09 C ANISOU 391 CG LEU A 80 5637 9298 11316 -471 -1352 -202 C ATOM 392 CD1 LEU A 80 30.171 5.546 -5.331 1.00 69.33 C ANISOU 392 CD1 LEU A 80 5681 9425 11236 -530 -1404 -148 C ATOM 393 CD2 LEU A 80 30.821 3.156 -5.053 1.00 69.42 C ANISOU 393 CD2 LEU A 80 5748 9431 11198 -411 -1368 -306 C ATOM 394 N VAL A 81 27.345 3.857 -1.575 1.00 68.32 N ANISOU 394 N VAL A 81 5362 8752 11844 -470 -1163 -79 N ATOM 395 CA VAL A 81 26.010 3.236 -1.561 1.00 69.02 C ANISOU 395 CA VAL A 81 5387 8659 12178 -482 -1218 -69 C ATOM 396 C VAL A 81 24.943 4.280 -1.156 1.00 68.99 C ANISOU 396 C VAL A 81 5295 8544 12374 -532 -1192 27 C ATOM 397 O VAL A 81 23.804 4.198 -1.622 1.00 69.76 O ANISOU 397 O VAL A 81 5324 8519 12663 -565 -1292 48 O ATOM 398 CB VAL A 81 25.948 1.922 -0.721 1.00 69.05 C ANISOU 398 CB VAL A 81 5399 8573 12264 -429 -1137 -109 C ATOM 399 CG1 VAL A 81 24.617 1.201 -0.909 1.00 69.90 C ANISOU 399 CG1 VAL A 81 5437 8497 12624 -449 -1213 -106 C ATOM 400 CG2 VAL A 81 27.093 0.980 -1.081 1.00 69.15 C ANISOU 400 CG2 VAL A 81 5498 8701 12075 -373 -1157 -203 C ATOM 401 N MET A 82 25.338 5.288 -0.342 1.00 69.64 N ANISOU 401 N MET A 82 5380 8670 12411 -536 -1067 82 N ATOM 402 CA MET A 82 24.479 6.398 0.078 1.00 69.62 C ANISOU 402 CA MET A 82 5304 8576 12573 -576 -1027 169 C ATOM 403 C MET A 82 24.062 7.221 -1.145 1.00 70.19 C ANISOU 403 C MET A 82 5349 8669 12650 -630 -1187 199 C ATOM 404 O MET A 82 22.871 7.368 -1.400 1.00 70.94 O ANISOU 404 O MET A 82 5362 8633 12959 -660 -1259 238 O ATOM 405 CB MET A 82 25.200 7.302 1.096 1.00 68.73 C ANISOU 405 CB MET A 82 5225 8527 12363 -566 -874 205 C ATOM 406 CG MET A 82 25.072 6.843 2.526 1.00 68.42 C ANISOU 406 CG MET A 82 5188 8398 12411 -524 -706 215 C ATOM 407 SD MET A 82 23.467 7.203 3.286 1.00 69.13 S ANISOU 407 SD MET A 82 5172 8272 12822 -543 -626 294 S ATOM 408 CE MET A 82 23.660 8.944 3.658 1.00 68.81 C ANISOU 408 CE MET A 82 5134 8274 12738 -573 -562 358 C ATOM 409 N GLY A 83 25.046 7.688 -1.916 1.00 70.89 N ANISOU 409 N GLY A 83 5507 8920 12508 -642 -1244 179 N ATOM 410 CA GLY A 83 24.835 8.494 -3.115 1.00 71.46 C ANISOU 410 CA GLY A 83 5580 9034 12538 -692 -1392 210 C ATOM 411 C GLY A 83 24.207 7.788 -4.301 1.00 72.50 C ANISOU 411 C GLY A 83 5711 9125 12711 -704 -1578 172 C ATOM 412 O GLY A 83 23.876 8.444 -5.291 1.00 73.15 O ANISOU 412 O GLY A 83 5795 9222 12776 -745 -1715 205 O ATOM 413 N LEU A 84 24.040 6.453 -4.222 1.00 73.19 N ANISOU 413 N LEU A 84 5802 9157 12850 -668 -1591 103 N ATOM 414 CA LEU A 84 23.446 5.650 -5.293 1.00 74.30 C ANISOU 414 CA LEU A 84 5948 9247 13036 -677 -1773 52 C ATOM 415 C LEU A 84 22.083 5.062 -4.929 1.00 75.03 C ANISOU 415 C LEU A 84 5935 9137 13435 -686 -1807 68 C ATOM 416 O LEU A 84 21.205 4.997 -5.792 1.00 76.08 O ANISOU 416 O LEU A 84 6031 9192 13683 -719 -1980 72 O ATOM 417 CB LEU A 84 24.401 4.529 -5.740 1.00 74.35 C ANISOU 417 CB LEU A 84 6052 9356 12842 -631 -1791 -53 C ATOM 418 CG LEU A 84 25.608 4.939 -6.586 1.00 74.19 C ANISOU 418 CG LEU A 84 6135 9532 12521 -628 -1816 -84 C ATOM 419 CD1 LEU A 84 26.693 3.890 -6.513 1.00 74.27 C ANISOU 419 CD1 LEU A 84 6221 9637 12361 -566 -1756 -180 C ATOM 420 CD2 LEU A 84 25.219 5.177 -8.041 1.00 75.17 C ANISOU 420 CD2 LEU A 84 6300 9676 12585 -666 -2015 -88 C ATOM 421 N ALA A 85 21.908 4.623 -3.667 1.00 76.75 N ANISOU 421 N ALA A 85 6107 9269 13785 -657 -1646 79 N ATOM 422 CA ALA A 85 20.671 3.994 -3.199 1.00 77.49 C ANISOU 422 CA ALA A 85 6097 9167 14178 -665 -1644 97 C ATOM 423 C ALA A 85 19.870 4.784 -2.151 1.00 77.36 C ANISOU 423 C ALA A 85 5976 9035 14382 -680 -1511 191 C ATOM 424 O ALA A 85 18.687 4.493 -1.966 1.00 78.26 O ANISOU 424 O ALA A 85 5982 8982 14771 -698 -1534 221 O ATOM 425 CB ALA A 85 20.962 2.589 -2.690 1.00 77.44 C ANISOU 425 CB ALA A 85 6124 9126 14173 -619 -1576 29 C ATOM 426 N VAL A 86 20.497 5.765 -1.467 1.00 76.89 N ANISOU 426 N VAL A 86 5947 9056 14212 -671 -1372 234 N ATOM 427 CA VAL A 86 19.828 6.550 -0.418 1.00 76.81 C ANISOU 427 CA VAL A 86 5856 8941 14387 -677 -1228 315 C ATOM 428 C VAL A 86 19.546 8.004 -0.843 1.00 76.92 C ANISOU 428 C VAL A 86 5834 8972 14420 -717 -1285 383 C ATOM 429 O VAL A 86 18.386 8.418 -0.841 1.00 77.74 O ANISOU 429 O VAL A 86 5826 8940 14772 -742 -1319 440 O ATOM 430 CB VAL A 86 20.560 6.455 0.954 1.00 75.85 C ANISOU 430 CB VAL A 86 5791 8852 14176 -632 -1005 316 C ATOM 431 CG1 VAL A 86 19.800 7.204 2.043 1.00 76.05 C ANISOU 431 CG1 VAL A 86 5743 8756 14397 -634 -849 393 C ATOM 432 CG2 VAL A 86 20.784 5.004 1.369 1.00 75.79 C ANISOU 432 CG2 VAL A 86 5821 8816 14160 -590 -955 256 C ATOM 433 N VAL A 87 20.606 8.770 -1.176 1.00 80.10 N ANISOU 433 N VAL A 87 6326 9536 14573 -722 -1292 380 N ATOM 434 CA VAL A 87 20.551 10.185 -1.577 1.00 80.13 C ANISOU 434 CA VAL A 87 6318 9574 14554 -759 -1339 445 C ATOM 435 C VAL A 87 19.648 10.482 -2.814 1.00 81.26 C ANISOU 435 C VAL A 87 6404 9660 14811 -802 -1555 474 C ATOM 436 O VAL A 87 18.841 11.410 -2.707 1.00 81.68 O ANISOU 436 O VAL A 87 6375 9621 15039 -824 -1564 547 O ATOM 437 CB VAL A 87 21.952 10.875 -1.636 1.00 79.16 C ANISOU 437 CB VAL A 87 6303 9635 14139 -760 -1291 435 C ATOM 438 CG1 VAL A 87 21.826 12.390 -1.791 1.00 79.12 C ANISOU 438 CG1 VAL A 87 6280 9636 14146 -798 -1304 513 C ATOM 439 CG2 VAL A 87 22.787 10.552 -0.397 1.00 78.21 C ANISOU 439 CG2 VAL A 87 6234 9559 13923 -716 -1098 406 C ATOM 440 N PRO A 88 19.713 9.743 -3.962 1.00 85.47 N ANISOU 440 N PRO A 88 6978 10236 15261 -811 -1732 419 N ATOM 441 CA PRO A 88 18.823 10.079 -5.095 1.00 86.69 C ANISOU 441 CA PRO A 88 7085 10329 15524 -850 -1948 451 C ATOM 442 C PRO A 88 17.338 9.854 -4.807 1.00 87.70 C ANISOU 442 C PRO A 88 7063 10252 16007 -860 -1984 488 C ATOM 443 O PRO A 88 16.510 10.659 -5.235 1.00 88.55 O ANISOU 443 O PRO A 88 7095 10283 16267 -890 -2090 553 O ATOM 444 CB PRO A 88 19.318 9.179 -6.235 1.00 87.13 C ANISOU 444 CB PRO A 88 7237 10476 15393 -848 -2105 368 C ATOM 445 CG PRO A 88 20.630 8.656 -5.796 1.00 86.05 C ANISOU 445 CG PRO A 88 7201 10477 15017 -810 -1967 304 C ATOM 446 CD PRO A 88 20.587 8.604 -4.307 1.00 85.25 C ANISOU 446 CD PRO A 88 7046 10310 15036 -782 -1752 325 C ATOM 447 N PHE A 89 17.008 8.772 -4.074 1.00 91.55 N ANISOU 447 N PHE A 89 7503 10648 16634 -835 -1893 450 N ATOM 448 CA PHE A 89 15.634 8.434 -3.693 1.00 92.55 C ANISOU 448 CA PHE A 89 7478 10575 17112 -844 -1899 483 C ATOM 449 C PHE A 89 15.127 9.333 -2.561 1.00 92.24 C ANISOU 449 C PHE A 89 7347 10446 17254 -837 -1713 563 C ATOM 450 O PHE A 89 13.923 9.572 -2.461 1.00 93.21 O ANISOU 450 O PHE A 89 7329 10413 17674 -853 -1742 617 O ATOM 451 CB PHE A 89 15.514 6.947 -3.323 1.00 92.78 C ANISOU 451 CB PHE A 89 7498 10538 17216 -824 -1860 417 C ATOM 452 CG PHE A 89 15.785 6.001 -4.470 1.00 93.34 C ANISOU 452 CG PHE A 89 7643 10661 17160 -831 -2060 333 C ATOM 453 CD1 PHE A 89 14.780 5.665 -5.369 1.00 94.79 C ANISOU 453 CD1 PHE A 89 7752 10737 17527 -865 -2278 327 C ATOM 454 CD2 PHE A 89 17.045 5.443 -4.651 1.00 92.50 C ANISOU 454 CD2 PHE A 89 7682 10709 16755 -800 -2032 257 C ATOM 455 CE1 PHE A 89 15.031 4.791 -6.431 1.00 95.42 C ANISOU 455 CE1 PHE A 89 7915 10861 17479 -870 -2467 241 C ATOM 456 CE2 PHE A 89 17.296 4.568 -5.712 1.00 93.11 C ANISOU 456 CE2 PHE A 89 7836 10831 16711 -801 -2208 172 C ATOM 457 CZ PHE A 89 16.287 4.248 -6.595 1.00 94.56 C ANISOU 457 CZ PHE A 89 7958 10905 17066 -836 -2425 163 C ATOM 458 N GLY A 90 16.054 9.827 -1.738 1.00 94.10 N ANISOU 458 N GLY A 90 7664 10778 17312 -812 -1529 569 N ATOM 459 CA GLY A 90 15.768 10.730 -0.629 1.00 93.75 C ANISOU 459 CA GLY A 90 7567 10668 17385 -799 -1341 633 C ATOM 460 C GLY A 90 15.441 12.135 -1.096 1.00 94.07 C ANISOU 460 C GLY A 90 7570 10703 17469 -826 -1419 702 C ATOM 461 O GLY A 90 14.549 12.780 -0.537 1.00 94.54 O ANISOU 461 O GLY A 90 7521 10633 17766 -824 -1344 764 O ATOM 462 N ALA A 91 16.165 12.615 -2.132 1.00 97.36 N ANISOU 462 N ALA A 91 8079 11258 17656 -850 -1566 694 N ATOM 463 CA ALA A 91 15.986 13.937 -2.739 1.00 97.72 C ANISOU 463 CA ALA A 91 8112 11314 17703 -880 -1666 761 C ATOM 464 C ALA A 91 14.655 14.037 -3.487 1.00 99.21 C ANISOU 464 C ALA A 91 8174 11361 18161 -904 -1852 805 C ATOM 465 O ALA A 91 14.026 15.096 -3.470 1.00 99.70 O ANISOU 465 O ALA A 91 8161 11345 18375 -914 -1869 878 O ATOM 466 CB ALA A 91 17.141 14.244 -3.679 1.00 97.29 C ANISOU 466 CB ALA A 91 8198 11444 17324 -900 -1770 739 C ATOM 467 N ALA A 92 14.224 12.927 -4.123 1.00103.08 N ANISOU 467 N ALA A 92 8637 11811 18717 -911 -1994 757 N ATOM 468 CA ALA A 92 12.963 12.827 -4.864 1.00104.65 C ANISOU 468 CA ALA A 92 8712 11872 19178 -935 -2194 787 C ATOM 469 C ALA A 92 11.754 12.866 -3.921 1.00105.30 C ANISOU 469 C ALA A 92 8615 11761 19633 -922 -2076 834 C ATOM 470 O ALA A 92 10.672 13.285 -4.330 1.00106.57 O ANISOU 470 O ALA A 92 8648 11796 20048 -939 -2204 888 O ATOM 471 CB ALA A 92 12.944 11.552 -5.691 1.00105.28 C ANISOU 471 CB ALA A 92 8826 11965 19210 -945 -2362 710 C ATOM 472 N CYS A 93 11.944 12.451 -2.655 1.00107.58 N ANISOU 472 N CYS A 93 8897 12024 19954 -891 -1828 818 N ATOM 473 CA CYS A 93 10.893 12.450 -1.637 1.00108.19 C ANISOU 473 CA CYS A 93 8819 11925 20363 -874 -1670 862 C ATOM 474 C CYS A 93 10.505 13.860 -1.176 1.00108.32 C ANISOU 474 C CYS A 93 8773 11886 20497 -864 -1580 941 C ATOM 475 O CYS A 93 9.463 14.018 -0.540 1.00109.33 O ANISOU 475 O CYS A 93 8751 11854 20936 -852 -1484 987 O ATOM 476 CB CYS A 93 11.350 11.635 -0.433 1.00107.25 C ANISOU 476 CB CYS A 93 8746 11813 20191 -840 -1426 823 C ATOM 477 SG CYS A 93 9.944 11.123 0.498 1.00108.32 S ANISOU 477 SG CYS A 93 8689 11722 20747 -829 -1283 863 S ATOM 478 N ILE A 94 11.344 14.871 -1.478 1.00108.00 N ANISOU 478 N ILE A 94 8846 11972 20217 -870 -1602 957 N ATOM 479 CA ILE A 94 11.112 16.277 -1.129 1.00108.12 C ANISOU 479 CA ILE A 94 8825 11945 20310 -862 -1533 1027 C ATOM 480 C ILE A 94 10.562 17.027 -2.355 1.00109.17 C ANISOU 480 C ILE A 94 8908 12051 20521 -893 -1788 1081 C ATOM 481 O ILE A 94 9.708 17.903 -2.199 1.00109.93 O ANISOU 481 O ILE A 94 8890 12026 20852 -886 -1784 1148 O ATOM 482 CB ILE A 94 12.384 16.961 -0.543 1.00106.70 C ANISOU 482 CB ILE A 94 8800 11906 19836 -849 -1377 1015 C ATOM 483 CG1 ILE A 94 13.155 16.025 0.416 1.00105.54 C ANISOU 483 CG1 ILE A 94 8740 11824 19536 -822 -1186 949 C ATOM 484 CG2 ILE A 94 12.036 18.288 0.152 1.00106.89 C ANISOU 484 CG2 ILE A 94 8777 11850 19987 -832 -1247 1078 C ATOM 485 CD1 ILE A 94 14.653 16.104 0.285 1.00104.32 C ANISOU 485 CD1 ILE A 94 8760 11866 19012 -827 -1174 905 C ATOM 486 N LEU A 95 11.050 16.670 -3.566 1.00110.11 N ANISOU 486 N LEU A 95 9118 12279 20440 -924 -2008 1050 N ATOM 487 CA LEU A 95 10.649 17.259 -4.852 1.00111.20 C ANISOU 487 CA LEU A 95 9243 12410 20598 -956 -2275 1096 C ATOM 488 C LEU A 95 9.158 17.063 -5.156 1.00112.96 C ANISOU 488 C LEU A 95 9276 12445 21198 -960 -2416 1133 C ATOM 489 O LEU A 95 8.523 17.972 -5.694 1.00114.02 O ANISOU 489 O LEU A 95 9345 12512 21465 -970 -2559 1203 O ATOM 490 CB LEU A 95 11.503 16.693 -6.003 1.00111.01 C ANISOU 490 CB LEU A 95 9371 12542 20266 -982 -2456 1041 C ATOM 491 CG LEU A 95 12.956 17.167 -6.088 1.00109.70 C ANISOU 491 CG LEU A 95 9386 12570 19725 -988 -2385 1025 C ATOM 492 CD1 LEU A 95 13.831 16.117 -6.739 1.00109.63 C ANISOU 492 CD1 LEU A 95 9508 12702 19445 -995 -2459 940 C ATOM 493 CD2 LEU A 95 13.069 18.485 -6.845 1.00109.96 C ANISOU 493 CD2 LEU A 95 9464 12638 19679 -1013 -2509 1102 C ATOM 494 N MET A 96 8.609 15.882 -4.810 1.00114.34 N ANISOU 494 N MET A 96 9360 12532 21552 -954 -2379 1089 N ATOM 495 CA MET A 96 7.198 15.536 -5.014 1.00116.05 C ANISOU 495 CA MET A 96 9380 12563 22151 -962 -2499 1117 C ATOM 496 C MET A 96 6.410 15.550 -3.694 1.00116.29 C ANISOU 496 C MET A 96 9249 12441 22495 -931 -2250 1147 C ATOM 497 O MET A 96 5.180 15.442 -3.719 1.00117.82 O ANISOU 497 O MET A 96 9253 12467 23047 -935 -2313 1183 O ATOM 498 CB MET A 96 7.063 14.159 -5.694 1.00116.73 C ANISOU 498 CB MET A 96 9472 12647 22233 -987 -2671 1046 C ATOM 499 CG MET A 96 7.477 14.147 -7.148 1.00116.99 C ANISOU 499 CG MET A 96 9631 12787 22032 -1017 -2959 1023 C ATOM 500 SD MET A 96 9.241 13.820 -7.357 1.00115.61 S ANISOU 500 SD MET A 96 9714 12853 21359 -1014 -2895 939 S ATOM 501 CE MET A 96 9.331 13.709 -9.125 1.00115.84 C ANISOU 501 CE MET A 96 9853 12957 21204 -1049 -3252 922 C ATOM 502 N LYS A 97 7.124 15.667 -2.545 1.00115.52 N ANISOU 502 N LYS A 97 9230 12401 22261 -900 -1967 1131 N ATOM 503 CA LYS A 97 6.591 15.666 -1.171 1.00115.59 C ANISOU 503 CA LYS A 97 9134 12290 22496 -865 -1687 1153 C ATOM 504 C LYS A 97 5.903 14.340 -0.777 1.00116.32 C ANISOU 504 C LYS A 97 9114 12270 22812 -868 -1633 1123 C ATOM 505 O LYS A 97 5.225 14.272 0.252 1.00116.77 O ANISOU 505 O LYS A 97 9053 12199 23116 -843 -1421 1151 O ATOM 506 CB LYS A 97 5.715 16.905 -0.877 1.00116.53 C ANISOU 506 CB LYS A 97 9115 12280 22881 -844 -1639 1235 C ATOM 507 CG LYS A 97 6.512 18.190 -0.693 1.00115.62 C ANISOU 507 CG LYS A 97 9124 12261 22546 -829 -1567 1260 C ATOM 508 CD LYS A 97 5.605 19.374 -0.397 1.00116.62 C ANISOU 508 CD LYS A 97 9112 12246 22953 -804 -1521 1337 C ATOM 509 CE LYS A 97 6.386 20.653 -0.228 1.00116.06 C ANISOU 509 CE LYS A 97 9167 12259 22672 -793 -1460 1361 C ATOM 510 NZ LYS A 97 5.494 21.810 0.043 1.00117.11 N ANISOU 510 NZ LYS A 97 9167 12245 23084 -763 -1421 1433 N ATOM 511 N MET A 98 6.120 13.281 -1.585 1.00118.03 N ANISOU 511 N MET A 98 9379 12537 22931 -899 -1817 1065 N ATOM 512 CA MET A 98 5.564 11.938 -1.391 1.00118.77 C ANISOU 512 CA MET A 98 9385 12533 23209 -911 -1808 1029 C ATOM 513 C MET A 98 6.465 10.842 -1.994 1.00118.14 C ANISOU 513 C MET A 98 9460 12580 22848 -928 -1926 941 C ATOM 514 O MET A 98 7.376 11.147 -2.767 1.00117.52 O ANISOU 514 O MET A 98 9534 12656 22462 -936 -2058 912 O ATOM 515 CB MET A 98 4.115 11.847 -1.926 1.00120.84 C ANISOU 515 CB MET A 98 9423 12611 23880 -937 -1983 1072 C ATOM 516 CG MET A 98 3.989 12.021 -3.432 1.00121.80 C ANISOU 516 CG MET A 98 9559 12766 23953 -973 -2340 1065 C ATOM 517 SD MET A 98 2.289 11.813 -4.006 1.00122.21 S ANISOU 517 SD MET A 98 9336 12593 24505 -1002 -2551 1116 S ATOM 518 CE MET A 98 2.561 11.696 -5.756 1.00124.24 C ANISOU 518 CE MET A 98 9699 12932 24575 -1046 -2964 1064 C ATOM 519 N TRP A 99 6.197 9.572 -1.637 1.00117.92 N ANISOU 519 N TRP A 99 9390 12480 22933 -933 -1869 901 N ATOM 520 CA TRP A 99 6.941 8.404 -2.107 1.00117.48 C ANISOU 520 CA TRP A 99 9465 12516 22656 -944 -1962 813 C ATOM 521 C TRP A 99 6.307 7.826 -3.376 1.00118.96 C ANISOU 521 C TRP A 99 9591 12644 22964 -988 -2279 782 C ATOM 522 O TRP A 99 5.105 7.555 -3.395 1.00120.51 O ANISOU 522 O TRP A 99 9600 12667 23522 -1011 -2343 814 O ATOM 523 CB TRP A 99 7.008 7.343 -0.997 1.00117.19 C ANISOU 523 CB TRP A 99 9424 12423 22679 -925 -1730 789 C ATOM 524 CG TRP A 99 8.062 6.301 -1.213 1.00116.29 C ANISOU 524 CG TRP A 99 9479 12430 22275 -918 -1756 700 C ATOM 525 CD1 TRP A 99 7.869 5.008 -1.602 1.00117.02 C ANISOU 525 CD1 TRP A 99 9563 12468 22432 -938 -1866 641 C ATOM 526 CD2 TRP A 99 9.475 6.465 -1.046 1.00114.59 C ANISOU 526 CD2 TRP A 99 9463 12405 21671 -886 -1670 659 C ATOM 527 NE1 TRP A 99 9.076 4.353 -1.683 1.00115.86 N ANISOU 527 NE1 TRP A 99 9599 12465 21957 -915 -1848 564 N ATOM 528 CE2 TRP A 99 10.080 5.225 -1.351 1.00114.36 C ANISOU 528 CE2 TRP A 99 9534 12429 21488 -883 -1729 575 C ATOM 529 CE3 TRP A 99 10.295 7.544 -0.672 1.00113.29 C ANISOU 529 CE3 TRP A 99 9397 12367 21281 -860 -1552 684 C ATOM 530 CZ2 TRP A 99 11.464 5.032 -1.286 1.00112.90 C ANISOU 530 CZ2 TRP A 99 9536 12421 20940 -851 -1670 517 C ATOM 531 CZ3 TRP A 99 11.667 7.351 -0.610 1.00111.86 C ANISOU 531 CZ3 TRP A 99 9398 12360 20743 -835 -1499 627 C ATOM 532 CH2 TRP A 99 12.238 6.110 -0.920 1.00111.70 C ANISOU 532 CH2 TRP A 99 9467 12392 20582 -829 -1557 546 C ATOM 533 N THR A 100 7.113 7.661 -4.440 1.00119.66 N ANISOU 533 N THR A 100 9838 12875 22752 -998 -2477 720 N ATOM 534 CA THR A 100 6.659 7.127 -5.732 1.00121.06 C ANISOU 534 CA THR A 100 10001 13018 22979 -1036 -2796 678 C ATOM 535 C THR A 100 7.488 5.903 -6.169 1.00120.69 C ANISOU 535 C THR A 100 10109 13063 22685 -1036 -2863 570 C ATOM 536 O THR A 100 7.837 5.774 -7.347 1.00121.20 O ANISOU 536 O THR A 100 10281 13209 22561 -1051 -3100 518 O ATOM 537 CB THR A 100 6.594 8.243 -6.800 1.00121.46 C ANISOU 537 CB THR A 100 10082 13126 22941 -1051 -3020 717 C ATOM 538 OG1 THR A 100 7.831 8.959 -6.821 1.00119.88 O ANISOU 538 OG1 THR A 100 10063 13116 22370 -1028 -2933 714 O ATOM 539 CG2 THR A 100 5.426 9.202 -6.588 1.00122.44 C ANISOU 539 CG2 THR A 100 10009 13103 23409 -1058 -3034 816 C ATOM 540 N PHE A 101 7.796 5.002 -5.214 1.00121.56 N ANISOU 540 N PHE A 101 10234 13155 22798 -1014 -2650 538 N ATOM 541 CA PHE A 101 8.593 3.798 -5.471 1.00121.17 C ANISOU 541 CA PHE A 101 10325 13180 22533 -1005 -2681 436 C ATOM 542 C PHE A 101 7.986 2.510 -4.891 1.00121.93 C ANISOU 542 C PHE A 101 10326 13121 22880 -1014 -2612 410 C ATOM 543 O PHE A 101 8.358 1.416 -5.321 1.00122.14 O ANISOU 543 O PHE A 101 10441 13167 22800 -1015 -2701 323 O ATOM 544 CB PHE A 101 10.054 3.992 -5.013 1.00119.23 C ANISOU 544 CB PHE A 101 10265 13128 21909 -959 -2500 408 C ATOM 545 CG PHE A 101 10.734 5.217 -5.584 1.00118.46 C ANISOU 545 CG PHE A 101 10266 13185 21558 -955 -2557 434 C ATOM 546 CD1 PHE A 101 10.825 6.390 -4.844 1.00117.58 C ANISOU 546 CD1 PHE A 101 10125 13097 21453 -940 -2383 513 C ATOM 547 CD2 PHE A 101 11.261 5.205 -6.871 1.00118.78 C ANISOU 547 CD2 PHE A 101 10432 13341 21358 -967 -2782 380 C ATOM 548 CE1 PHE A 101 11.440 7.527 -5.377 1.00116.97 C ANISOU 548 CE1 PHE A 101 10137 13153 21154 -942 -2438 542 C ATOM 549 CE2 PHE A 101 11.874 6.344 -7.404 1.00118.19 C ANISOU 549 CE2 PHE A 101 10448 13403 21055 -967 -2828 414 C ATOM 550 CZ PHE A 101 11.960 7.497 -6.653 1.00117.28 C ANISOU 550 CZ PHE A 101 10296 13305 20960 -957 -2658 496 C ATOM 551 N GLY A 102 7.059 2.656 -3.943 1.00123.52 N ANISOU 551 N GLY A 102 10352 13168 23412 -1021 -2452 487 N ATOM 552 CA GLY A 102 6.372 1.538 -3.300 1.00124.41 C ANISOU 552 CA GLY A 102 10353 13115 23802 -1036 -2361 483 C ATOM 553 C GLY A 102 6.806 1.265 -1.874 1.00123.29 C ANISOU 553 C GLY A 102 10246 12976 23623 -996 -2027 508 C ATOM 554 O GLY A 102 7.851 1.754 -1.435 1.00121.66 O ANISOU 554 O GLY A 102 10183 12921 23121 -953 -1883 505 O ATOM 555 N ASN A 103 6.000 0.466 -1.144 1.00124.71 N ANISOU 555 N ASN A 103 10295 12982 24107 -1012 -1906 536 N ATOM 556 CA ASN A 103 6.253 0.085 0.250 1.00123.98 C ANISOU 556 CA ASN A 103 10228 12861 24017 -977 -1587 568 C ATOM 557 C ASN A 103 7.437 -0.874 0.414 1.00122.95 C ANISOU 557 C ASN A 103 10294 12841 23581 -943 -1537 490 C ATOM 558 O ASN A 103 8.063 -0.881 1.477 1.00122.04 O ANISOU 558 O ASN A 103 10266 12775 23328 -899 -1289 510 O ATOM 559 CB ASN A 103 4.992 -0.488 0.903 1.00125.51 C ANISOU 559 CB ASN A 103 10221 12830 24637 -1009 -1477 628 C ATOM 560 CG ASN A 103 3.917 0.538 1.170 1.00126.10 C ANISOU 560 CG ASN A 103 10102 12798 25012 -1021 -1415 722 C ATOM 561 OD1 ASN A 103 2.895 0.594 0.480 1.00127.77 O ANISOU 561 OD1 ASN A 103 10140 12887 25520 -1068 -1600 740 O ATOM 562 ND2 ASN A 103 4.110 1.360 2.195 1.00124.86 N ANISOU 562 ND2 ASN A 103 9970 12679 24792 -978 -1154 782 N ATOM 563 N PHE A 104 7.741 -1.680 -0.630 1.00123.11 N ANISOU 563 N PHE A 104 10386 12895 23495 -960 -1774 398 N ATOM 564 CA PHE A 104 8.857 -2.633 -0.639 1.00122.21 C ANISOU 564 CA PHE A 104 10454 12882 23098 -925 -1758 313 C ATOM 565 C PHE A 104 10.200 -1.900 -0.601 1.00120.40 C ANISOU 565 C PHE A 104 10403 12876 22468 -873 -1692 291 C ATOM 566 O PHE A 104 11.046 -2.226 0.234 1.00119.29 O ANISOU 566 O PHE A 104 10372 12803 22150 -826 -1501 283 O ATOM 567 CB PHE A 104 8.766 -3.588 -1.852 1.00123.24 C ANISOU 567 CB PHE A 104 10612 12985 23228 -956 -2042 215 C ATOM 568 CG PHE A 104 10.057 -4.275 -2.247 1.00122.18 C ANISOU 568 CG PHE A 104 10686 13001 22736 -913 -2090 112 C ATOM 569 CD1 PHE A 104 10.554 -5.340 -1.504 1.00121.53 C ANISOU 569 CD1 PHE A 104 10679 12897 22600 -879 -1940 82 C ATOM 570 CD2 PHE A 104 10.768 -3.863 -3.369 1.00121.93 C ANISOU 570 CD2 PHE A 104 10774 13130 22424 -904 -2281 46 C ATOM 571 CE1 PHE A 104 11.748 -5.970 -1.867 1.00120.62 C ANISOU 571 CE1 PHE A 104 10746 12918 22166 -833 -1982 -15 C ATOM 572 CE2 PHE A 104 11.962 -4.495 -3.731 1.00121.05 C ANISOU 572 CE2 PHE A 104 10846 13157 21991 -860 -2311 -50 C ATOM 573 CZ PHE A 104 12.442 -5.545 -2.979 1.00120.41 C ANISOU 573 CZ PHE A 104 10828 13051 21871 -823 -2164 -83 C ATOM 574 N TRP A 105 10.391 -0.917 -1.507 1.00119.90 N ANISOU 574 N TRP A 105 10365 12921 22270 -884 -1854 286 N ATOM 575 CA TRP A 105 11.616 -0.123 -1.577 1.00118.35 C ANISOU 575 CA TRP A 105 10321 12933 21714 -845 -1808 271 C ATOM 576 C TRP A 105 11.728 0.853 -0.402 1.00117.37 C ANISOU 576 C TRP A 105 10177 12828 21590 -820 -1554 356 C ATOM 577 O TRP A 105 12.842 1.121 0.034 1.00116.02 O ANISOU 577 O TRP A 105 10140 12801 21142 -778 -1431 341 O ATOM 578 CB TRP A 105 11.761 0.582 -2.940 1.00118.61 C ANISOU 578 CB TRP A 105 10394 13067 21606 -868 -2059 244 C ATOM 579 CG TRP A 105 13.038 1.360 -3.104 1.00117.16 C ANISOU 579 CG TRP A 105 10364 13095 21056 -836 -2019 229 C ATOM 580 CD1 TRP A 105 13.165 2.716 -3.165 1.00116.73 C ANISOU 580 CD1 TRP A 105 10306 13116 20930 -841 -2003 290 C ATOM 581 CD2 TRP A 105 14.370 0.828 -3.184 1.00115.98 C ANISOU 581 CD2 TRP A 105 10385 13103 20580 -793 -1981 152 C ATOM 582 NE1 TRP A 105 14.490 3.064 -3.287 1.00115.38 N ANISOU 582 NE1 TRP A 105 10291 13139 20410 -810 -1958 257 N ATOM 583 CE2 TRP A 105 15.252 1.925 -3.304 1.00114.92 C ANISOU 583 CE2 TRP A 105 10337 13137 20191 -779 -1944 172 C ATOM 584 CE3 TRP A 105 14.905 -0.471 -3.172 1.00115.80 C ANISOU 584 CE3 TRP A 105 10446 13090 20462 -765 -1977 68 C ATOM 585 CZ2 TRP A 105 16.639 1.764 -3.414 1.00113.74 C ANISOU 585 CZ2 TRP A 105 10344 13166 19706 -740 -1900 112 C ATOM 586 CZ3 TRP A 105 16.279 -0.630 -3.278 1.00114.61 C ANISOU 586 CZ3 TRP A 105 10454 13117 19976 -719 -1934 6 C ATOM 587 CH2 TRP A 105 17.130 0.478 -3.399 1.00113.60 C ANISOU 587 CH2 TRP A 105 10399 13157 19607 -708 -1895 28 C ATOM 588 N CYS A 106 10.583 1.339 0.138 1.00116.15 N ANISOU 588 N CYS A 106 9857 12522 21753 -842 -1471 440 N ATOM 589 CA CYS A 106 10.519 2.253 1.289 1.00115.53 C ANISOU 589 CA CYS A 106 9749 12433 21713 -817 -1223 520 C ATOM 590 C CYS A 106 11.193 1.641 2.528 1.00114.73 C ANISOU 590 C CYS A 106 9747 12351 21494 -770 -971 516 C ATOM 591 O CYS A 106 11.932 2.337 3.224 1.00113.57 O ANISOU 591 O CYS A 106 9692 12305 21154 -734 -813 535 O ATOM 592 CB CYS A 106 9.076 2.667 1.574 1.00116.87 C ANISOU 592 CB CYS A 106 9711 12416 22278 -847 -1188 602 C ATOM 593 SG CYS A 106 8.857 3.683 3.063 1.00116.46 S ANISOU 593 SG CYS A 106 9619 12321 22309 -811 -860 695 S ATOM 594 N GLU A 107 10.960 0.337 2.773 1.00110.87 N ANISOU 594 N GLU A 107 9245 11764 21117 -773 -947 490 N ATOM 595 CA GLU A 107 11.554 -0.411 3.882 1.00110.40 C ANISOU 595 CA GLU A 107 9284 11707 20956 -729 -731 486 C ATOM 596 C GLU A 107 13.024 -0.731 3.598 1.00109.05 C ANISOU 596 C GLU A 107 9305 11724 20405 -688 -779 405 C ATOM 597 O GLU A 107 13.842 -0.710 4.520 1.00108.08 O ANISOU 597 O GLU A 107 9294 11674 20098 -640 -598 411 O ATOM 598 CB GLU A 107 10.773 -1.707 4.142 1.00111.76 C ANISOU 598 CB GLU A 107 9373 11700 21390 -750 -707 489 C ATOM 599 CG GLU A 107 9.485 -1.504 4.922 1.00112.81 C ANISOU 599 CG GLU A 107 9332 11644 21886 -775 -548 584 C ATOM 600 CD GLU A 107 8.578 -2.717 5.013 1.00114.30 C ANISOU 600 CD GLU A 107 9409 11642 22377 -811 -552 594 C ATOM 601 OE1 GLU A 107 7.347 -2.542 4.868 1.00115.75 O ANISOU 601 OE1 GLU A 107 9402 11673 22905 -857 -579 646 O ATOM 602 OE2 GLU A 107 9.091 -3.840 5.230 1.00114.06 O ANISOU 602 OE2 GLU A 107 9477 11609 22251 -794 -529 551 O ATOM 603 N PHE A 108 13.352 -1.028 2.321 1.00103.54 N ANISOU 603 N PHE A 108 8646 11101 19593 -705 -1022 328 N ATOM 604 CA PHE A 108 14.702 -1.363 1.862 1.00102.53 C ANISOU 604 CA PHE A 108 8686 11150 19121 -667 -1089 244 C ATOM 605 C PHE A 108 15.633 -0.144 1.861 1.00101.19 C ANISOU 605 C PHE A 108 8602 11161 18684 -646 -1050 254 C ATOM 606 O PHE A 108 16.764 -0.252 2.330 1.00100.14 O ANISOU 606 O PHE A 108 8595 11150 18303 -599 -950 226 O ATOM 607 CB PHE A 108 14.652 -2.031 0.477 1.00103.30 C ANISOU 607 CB PHE A 108 8795 11258 19196 -693 -1355 159 C ATOM 608 CG PHE A 108 15.700 -3.096 0.253 1.00102.79 C ANISOU 608 CG PHE A 108 8873 11281 18901 -650 -1387 64 C ATOM 609 CD1 PHE A 108 15.495 -4.400 0.690 1.00103.30 C ANISOU 609 CD1 PHE A 108 8938 11227 19084 -638 -1340 39 C ATOM 610 CD2 PHE A 108 16.879 -2.802 -0.419 1.00101.90 C ANISOU 610 CD2 PHE A 108 8891 11364 18463 -621 -1463 1 C ATOM 611 CE1 PHE A 108 16.464 -5.386 0.478 1.00102.89 C ANISOU 611 CE1 PHE A 108 9017 11250 18827 -592 -1371 -51 C ATOM 612 CE2 PHE A 108 17.848 -3.788 -0.630 1.00101.52 C ANISOU 612 CE2 PHE A 108 8966 11394 18213 -575 -1486 -89 C ATOM 613 CZ PHE A 108 17.633 -5.073 -0.182 1.00102.02 C ANISOU 613 CZ PHE A 108 9030 11336 18397 -558 -1444 -116 C ATOM 614 N TRP A 109 15.146 1.013 1.355 1.00 95.53 N ANISOU 614 N TRP A 109 7813 10454 18030 -681 -1132 297 N ATOM 615 CA TRP A 109 15.857 2.298 1.285 1.00 94.50 C ANISOU 615 CA TRP A 109 7744 10472 17690 -673 -1109 319 C ATOM 616 C TRP A 109 16.221 2.804 2.687 1.00 93.65 C ANISOU 616 C TRP A 109 7672 10376 17535 -637 -852 370 C ATOM 617 O TRP A 109 17.303 3.365 2.872 1.00 92.53 O ANISOU 617 O TRP A 109 7638 10385 17134 -612 -799 356 O ATOM 618 CB TRP A 109 15.006 3.325 0.510 1.00 95.23 C ANISOU 618 CB TRP A 109 7731 10524 17928 -721 -1251 367 C ATOM 619 CG TRP A 109 15.402 4.764 0.657 1.00 94.47 C ANISOU 619 CG TRP A 109 7661 10523 17711 -720 -1196 416 C ATOM 620 CD1 TRP A 109 16.376 5.421 -0.033 1.00 93.89 C ANISOU 620 CD1 TRP A 109 7691 10621 17362 -721 -1282 391 C ATOM 621 CD2 TRP A 109 14.761 5.746 1.481 1.00 94.46 C ANISOU 621 CD2 TRP A 109 7574 10438 17879 -723 -1051 499 C ATOM 622 NE1 TRP A 109 16.409 6.745 0.339 1.00 93.43 N ANISOU 622 NE1 TRP A 109 7619 10590 17290 -727 -1201 455 N ATOM 623 CE2 TRP A 109 15.426 6.973 1.266 1.00 93.78 C ANISOU 623 CE2 TRP A 109 7551 10479 17602 -725 -1062 518 C ATOM 624 CE3 TRP A 109 13.692 5.707 2.393 1.00 95.04 C ANISOU 624 CE3 TRP A 109 7524 10338 18249 -722 -904 559 C ATOM 625 CZ2 TRP A 109 15.066 8.148 1.935 1.00 93.62 C ANISOU 625 CZ2 TRP A 109 7480 10415 17676 -724 -938 590 C ATOM 626 CZ3 TRP A 109 13.336 6.872 3.055 1.00 94.90 C ANISOU 626 CZ3 TRP A 109 7456 10281 18320 -716 -772 629 C ATOM 627 CH2 TRP A 109 14.014 8.076 2.819 1.00 94.21 C ANISOU 627 CH2 TRP A 109 7439 10319 18038 -717 -795 641 C ATOM 628 N THR A 110 15.325 2.580 3.669 1.00 90.03 N ANISOU 628 N THR A 110 7125 9756 17326 -635 -694 427 N ATOM 629 CA THR A 110 15.516 2.951 5.073 1.00 89.51 C ANISOU 629 CA THR A 110 7097 9674 17239 -598 -440 476 C ATOM 630 C THR A 110 16.567 2.027 5.714 1.00 88.73 C ANISOU 630 C THR A 110 7139 9647 16928 -548 -342 430 C ATOM 631 O THR A 110 17.387 2.496 6.506 1.00 87.83 O ANISOU 631 O THR A 110 7125 9623 16624 -511 -207 437 O ATOM 632 CB THR A 110 14.165 2.944 5.814 1.00 90.69 C ANISOU 632 CB THR A 110 7104 9622 17732 -613 -306 551 C ATOM 633 OG1 THR A 110 13.226 3.739 5.088 1.00 91.29 O ANISOU 633 OG1 THR A 110 7043 9635 18009 -657 -428 588 O ATOM 634 CG2 THR A 110 14.270 3.475 7.234 1.00 90.41 C ANISOU 634 CG2 THR A 110 7113 9564 17674 -575 -39 605 C ATOM 635 N SER A 111 16.546 0.725 5.351 1.00 86.21 N ANISOU 635 N SER A 111 6828 9285 16642 -546 -422 380 N ATOM 636 CA SER A 111 17.480 -0.291 5.846 1.00 85.63 C ANISOU 636 CA SER A 111 6880 9264 16391 -495 -354 333 C ATOM 637 C SER A 111 18.922 -0.006 5.418 1.00 84.46 C ANISOU 637 C SER A 111 6862 9327 15902 -464 -422 269 C ATOM 638 O SER A 111 19.833 -0.198 6.223 1.00 83.69 O ANISOU 638 O SER A 111 6873 9300 15625 -414 -302 259 O ATOM 639 CB SER A 111 17.055 -1.684 5.393 1.00 86.55 C ANISOU 639 CB SER A 111 6965 9277 16643 -505 -450 291 C ATOM 640 OG SER A 111 15.794 -2.038 5.934 1.00 87.73 O ANISOU 640 OG SER A 111 6995 9227 17112 -532 -359 355 O ATOM 641 N ILE A 112 19.123 0.466 4.165 1.00 81.10 N ANISOU 641 N ILE A 112 6427 8998 15390 -494 -613 231 N ATOM 642 CA ILE A 112 20.440 0.823 3.616 1.00 80.16 C ANISOU 642 CA ILE A 112 6416 9080 14962 -473 -683 175 C ATOM 643 C ILE A 112 20.949 2.101 4.304 1.00 79.22 C ANISOU 643 C ILE A 112 6331 9047 14722 -466 -560 223 C ATOM 644 O ILE A 112 22.126 2.169 4.668 1.00 78.38 O ANISOU 644 O ILE A 112 6327 9071 14382 -428 -502 195 O ATOM 645 CB ILE A 112 20.418 0.960 2.060 1.00 80.60 C ANISOU 645 CB ILE A 112 6456 9202 14967 -511 -915 127 C ATOM 646 CG1 ILE A 112 19.901 -0.323 1.373 1.00 81.66 C ANISOU 646 CG1 ILE A 112 6564 9241 15222 -518 -1050 70 C ATOM 647 CG2 ILE A 112 21.803 1.337 1.512 1.00 79.77 C ANISOU 647 CG2 ILE A 112 6461 9306 14542 -489 -964 75 C ATOM 648 CD1 ILE A 112 19.272 -0.096 -0.015 1.00 82.54 C ANISOU 648 CD1 ILE A 112 6620 9339 15403 -570 -1277 51 C ATOM 649 N ASP A 113 20.051 3.097 4.491 1.00 79.56 N ANISOU 649 N ASP A 113 6284 9009 14936 -502 -523 295 N ATOM 650 CA ASP A 113 20.333 4.388 5.128 1.00 78.88 C ANISOU 650 CA ASP A 113 6219 8975 14777 -501 -411 344 C ATOM 651 C ASP A 113 20.961 4.235 6.513 1.00 78.36 C ANISOU 651 C ASP A 113 6244 8922 14607 -450 -210 352 C ATOM 652 O ASP A 113 21.950 4.907 6.799 1.00 77.51 O ANISOU 652 O ASP A 113 6219 8942 14289 -434 -171 342 O ATOM 653 CB ASP A 113 19.061 5.259 5.193 1.00 79.53 C ANISOU 653 CB ASP A 113 6176 8926 15116 -540 -391 418 C ATOM 654 CG ASP A 113 19.269 6.684 5.688 1.00 79.03 C ANISOU 654 CG ASP A 113 6130 8907 14991 -543 -300 465 C ATOM 655 OD1 ASP A 113 18.337 7.235 6.310 1.00 79.60 O ANISOU 655 OD1 ASP A 113 6125 8853 15266 -549 -192 526 O ATOM 656 OD2 ASP A 113 20.356 7.253 5.436 1.00 78.14 O ANISOU 656 OD2 ASP A 113 6104 8951 14635 -541 -337 438 O ATOM 657 N VAL A 114 20.411 3.335 7.353 1.00 76.24 N ANISOU 657 N VAL A 114 5963 8521 14483 -426 -91 371 N ATOM 658 CA VAL A 114 20.924 3.063 8.701 1.00 75.96 C ANISOU 658 CA VAL A 114 6026 8481 14355 -373 98 384 C ATOM 659 C VAL A 114 22.220 2.234 8.610 1.00 75.37 C ANISOU 659 C VAL A 114 6067 8535 14036 -329 52 314 C ATOM 660 O VAL A 114 23.168 2.519 9.343 1.00 74.78 O ANISOU 660 O VAL A 114 6093 8551 13769 -291 136 307 O ATOM 661 CB VAL A 114 19.852 2.436 9.643 1.00 76.93 C ANISOU 661 CB VAL A 114 6101 8412 14717 -364 256 440 C ATOM 662 CG1 VAL A 114 20.371 2.308 11.076 1.00 76.72 C ANISOU 662 CG1 VAL A 114 6193 8382 14575 -309 457 462 C ATOM 663 CG2 VAL A 114 18.562 3.254 9.629 1.00 77.55 C ANISOU 663 CG2 VAL A 114 6045 8365 15055 -406 293 505 C ATOM 664 N LEU A 115 22.270 1.250 7.678 1.00 71.83 N ANISOU 664 N LEU A 115 5602 8095 13596 -332 -91 258 N ATOM 665 CA LEU A 115 23.426 0.375 7.426 1.00 71.41 C ANISOU 665 CA LEU A 115 5643 8154 13335 -287 -150 184 C ATOM 666 C LEU A 115 24.690 1.171 7.087 1.00 70.45 C ANISOU 666 C LEU A 115 5588 8230 12950 -278 -199 148 C ATOM 667 O LEU A 115 25.751 0.883 7.641 1.00 69.89 O ANISOU 667 O LEU A 115 5610 8247 12698 -227 -145 120 O ATOM 668 CB LEU A 115 23.106 -0.641 6.305 1.00 72.03 C ANISOU 668 CB LEU A 115 5681 8197 13490 -302 -313 127 C ATOM 669 CG LEU A 115 24.202 -1.643 5.914 1.00 71.71 C ANISOU 669 CG LEU A 115 5730 8258 13259 -252 -385 40 C ATOM 670 CD1 LEU A 115 24.140 -2.892 6.771 1.00 71.96 C ANISOU 670 CD1 LEU A 115 5805 8184 13353 -204 -290 40 C ATOM 671 CD2 LEU A 115 24.088 -2.025 4.453 1.00 72.25 C ANISOU 671 CD2 LEU A 115 5767 8355 13329 -278 -582 -26 C ATOM 672 N CYS A 116 24.566 2.172 6.193 1.00 66.57 N ANISOU 672 N CYS A 116 5046 7801 12446 -328 -300 154 N ATOM 673 CA CYS A 116 25.667 3.031 5.756 1.00 65.83 C ANISOU 673 CA CYS A 116 5000 7887 12125 -333 -350 130 C ATOM 674 C CYS A 116 26.226 3.908 6.879 1.00 65.15 C ANISOU 674 C CYS A 116 4967 7845 11942 -317 -211 167 C ATOM 675 O CYS A 116 27.427 4.176 6.889 1.00 64.57 O ANISOU 675 O CYS A 116 4958 7918 11657 -299 -219 135 O ATOM 676 CB CYS A 116 25.260 3.861 4.545 1.00 66.07 C ANISOU 676 CB CYS A 116 4966 7950 12187 -393 -490 140 C ATOM 677 SG CYS A 116 24.975 2.891 3.042 1.00 66.81 S ANISOU 677 SG CYS A 116 5035 8044 12306 -408 -689 73 S ATOM 678 N VAL A 117 25.365 4.341 7.823 1.00 63.68 N ANISOU 678 N VAL A 117 4755 7530 11911 -323 -83 232 N ATOM 679 CA VAL A 117 25.756 5.163 8.976 1.00 63.24 C ANISOU 679 CA VAL A 117 4760 7491 11777 -306 56 265 C ATOM 680 C VAL A 117 26.434 4.272 10.028 1.00 63.12 C ANISOU 680 C VAL A 117 4845 7479 11658 -240 159 246 C ATOM 681 O VAL A 117 27.500 4.635 10.531 1.00 62.59 O ANISOU 681 O VAL A 117 4860 7520 11401 -215 190 228 O ATOM 682 CB VAL A 117 24.565 5.975 9.564 1.00 63.64 C ANISOU 682 CB VAL A 117 4750 7400 12030 -333 161 338 C ATOM 683 CG1 VAL A 117 25.007 6.853 10.734 1.00 63.25 C ANISOU 683 CG1 VAL A 117 4780 7369 11883 -313 300 362 C ATOM 684 CG2 VAL A 117 23.899 6.826 8.491 1.00 63.87 C ANISOU 684 CG2 VAL A 117 4677 7421 12169 -394 43 360 C ATOM 685 N THR A 118 25.817 3.106 10.340 1.00 64.22 N ANISOU 685 N THR A 118 4978 7497 11925 -215 202 251 N ATOM 686 CA THR A 118 26.305 2.113 11.307 1.00 64.27 C ANISOU 686 CA THR A 118 5080 7481 11859 -150 295 242 C ATOM 687 C THR A 118 27.702 1.604 10.923 1.00 63.75 C ANISOU 687 C THR A 118 5081 7572 11569 -110 202 170 C ATOM 688 O THR A 118 28.567 1.504 11.794 1.00 63.42 O ANISOU 688 O THR A 118 5135 7583 11379 -61 267 163 O ATOM 689 CB THR A 118 25.282 0.969 11.475 1.00 65.14 C ANISOU 689 CB THR A 118 5151 7422 12176 -143 339 265 C ATOM 690 OG1 THR A 118 23.980 1.519 11.680 1.00 65.72 O ANISOU 690 OG1 THR A 118 5137 7358 12475 -185 414 330 O ATOM 691 CG2 THR A 118 25.626 0.027 12.627 1.00 65.35 C ANISOU 691 CG2 THR A 118 5284 7397 12149 -78 459 276 C ATOM 692 N ALA A 119 27.920 1.308 9.624 1.00 63.75 N ANISOU 692 N ALA A 119 5032 7646 11544 -129 51 116 N ATOM 693 CA ALA A 119 29.203 0.829 9.105 1.00 63.41 C ANISOU 693 CA ALA A 119 5038 7753 11302 -91 -37 44 C ATOM 694 C ALA A 119 30.281 1.913 9.153 1.00 62.71 C ANISOU 694 C ALA A 119 4980 7824 11023 -98 -45 35 C ATOM 695 O ALA A 119 31.407 1.612 9.542 1.00 62.44 O ANISOU 695 O ALA A 119 5012 7885 10828 -48 -36 0 O ATOM 696 CB ALA A 119 29.042 0.307 7.685 1.00 63.70 C ANISOU 696 CB ALA A 119 5019 7816 11368 -113 -187 -10 C ATOM 697 N SER A 120 29.931 3.170 8.788 1.00 63.26 N ANISOU 697 N SER A 120 5000 7915 11121 -160 -63 68 N ATOM 698 CA SER A 120 30.846 4.316 8.775 1.00 62.70 C ANISOU 698 CA SER A 120 4948 7982 10893 -181 -73 67 C ATOM 699 C SER A 120 31.390 4.677 10.160 1.00 62.45 C ANISOU 699 C SER A 120 4997 7953 10778 -147 43 88 C ATOM 700 O SER A 120 32.599 4.870 10.293 1.00 62.11 O ANISOU 700 O SER A 120 4996 8040 10562 -126 23 55 O ATOM 701 CB SER A 120 30.196 5.529 8.118 1.00 62.70 C ANISOU 701 CB SER A 120 4879 7974 10970 -254 -114 108 C ATOM 702 OG SER A 120 29.915 5.287 6.750 1.00 62.95 O ANISOU 702 OG SER A 120 4853 8032 11033 -285 -244 83 O ATOM 703 N ILE A 121 30.511 4.753 11.186 1.00 63.57 N ANISOU 703 N ILE A 121 5160 7952 11042 -139 164 140 N ATOM 704 CA ILE A 121 30.906 5.061 12.568 1.00 63.50 C ANISOU 704 CA ILE A 121 5247 7928 10953 -103 280 160 C ATOM 705 C ILE A 121 31.786 3.942 13.163 1.00 63.59 C ANISOU 705 C ILE A 121 5343 7973 10845 -28 290 125 C ATOM 706 O ILE A 121 32.752 4.242 13.866 1.00 63.42 O ANISOU 706 O ILE A 121 5397 8029 10670 1 307 111 O ATOM 707 CB ILE A 121 29.701 5.483 13.474 1.00 63.86 C ANISOU 707 CB ILE A 121 5299 7810 11155 -113 419 226 C ATOM 708 CG1 ILE A 121 30.156 6.088 14.823 1.00 63.78 C ANISOU 708 CG1 ILE A 121 5401 7799 11034 -84 530 242 C ATOM 709 CG2 ILE A 121 28.690 4.354 13.683 1.00 64.53 C ANISOU 709 CG2 ILE A 121 5364 7743 11411 -91 481 252 C ATOM 710 CD1 ILE A 121 30.194 7.588 14.881 1.00 63.81 C ANISOU 710 CD1 ILE A 121 5395 7820 11030 -131 549 262 C ATOM 711 N GLU A 122 31.473 2.668 12.836 1.00 65.00 N ANISOU 711 N GLU A 122 5507 8094 11096 2 267 108 N ATOM 712 CA GLU A 122 32.220 1.492 13.288 1.00 65.20 C ANISOU 712 CA GLU A 122 5606 8136 11031 77 267 76 C ATOM 713 C GLU A 122 33.596 1.413 12.627 1.00 64.81 C ANISOU 713 C GLU A 122 5554 8264 10807 98 155 8 C ATOM 714 O GLU A 122 34.566 1.077 13.306 1.00 64.79 O ANISOU 714 O GLU A 122 5625 8318 10675 156 164 -12 O ATOM 715 CB GLU A 122 31.421 0.203 13.053 1.00 65.76 C ANISOU 715 CB GLU A 122 5654 8082 11249 95 269 77 C ATOM 716 CG GLU A 122 30.423 -0.101 14.158 1.00 66.36 C ANISOU 716 CG GLU A 122 5772 7983 11458 108 415 146 C ATOM 717 CD GLU A 122 29.493 -1.278 13.921 1.00 67.04 C ANISOU 717 CD GLU A 122 5820 7927 11725 111 424 158 C ATOM 718 OE1 GLU A 122 29.939 -2.293 13.338 1.00 67.11 O ANISOU 718 OE1 GLU A 122 5826 7966 11707 141 333 105 O ATOM 719 OE2 GLU A 122 28.324 -1.199 14.361 1.00 67.59 O ANISOU 719 OE2 GLU A 122 5862 7850 11969 85 528 219 O ATOM 720 N THR A 123 33.682 1.740 11.315 1.00 62.04 N ANISOU 720 N THR A 123 5120 7999 10454 52 51 -25 N ATOM 721 CA THR A 123 34.935 1.748 10.548 1.00 61.78 C ANISOU 721 CA THR A 123 5071 8138 10264 65 -45 -88 C ATOM 722 C THR A 123 35.871 2.839 11.087 1.00 61.39 C ANISOU 722 C THR A 123 5048 8197 10080 53 -28 -80 C ATOM 723 O THR A 123 37.058 2.571 11.285 1.00 61.36 O ANISOU 723 O THR A 123 5073 8298 9943 100 -55 -120 O ATOM 724 CB THR A 123 34.657 1.851 9.035 1.00 61.83 C ANISOU 724 CB THR A 123 4996 8194 10302 16 -146 -117 C ATOM 725 OG1 THR A 123 33.761 0.806 8.652 1.00 62.31 O ANISOU 725 OG1 THR A 123 5039 8138 10498 28 -167 -126 O ATOM 726 CG2 THR A 123 35.922 1.753 8.194 1.00 61.72 C ANISOU 726 CG2 THR A 123 4968 8354 10129 35 -229 -183 C ATOM 727 N LEU A 124 35.324 4.044 11.370 1.00 60.64 N ANISOU 727 N LEU A 124 4943 8067 10031 -6 16 -30 N ATOM 728 CA LEU A 124 36.065 5.176 11.940 1.00 60.36 C ANISOU 728 CA LEU A 124 4936 8110 9888 -27 33 -19 C ATOM 729 C LEU A 124 36.539 4.859 13.361 1.00 60.52 C ANISOU 729 C LEU A 124 5060 8098 9837 36 102 -15 C ATOM 730 O LEU A 124 37.599 5.334 13.770 1.00 60.41 O ANISOU 730 O LEU A 124 5077 8182 9694 45 80 -34 O ATOM 731 CB LEU A 124 35.212 6.455 11.938 1.00 60.24 C ANISOU 731 CB LEU A 124 4892 8035 9961 -100 70 33 C ATOM 732 CG LEU A 124 35.083 7.194 10.606 1.00 60.05 C ANISOU 732 CG LEU A 124 4779 8081 9956 -171 -14 34 C ATOM 733 CD1 LEU A 124 33.850 8.070 10.589 1.00 60.14 C ANISOU 733 CD1 LEU A 124 4756 7980 10114 -228 24 92 C ATOM 734 CD2 LEU A 124 36.320 8.019 10.300 1.00 59.80 C ANISOU 734 CD2 LEU A 124 4738 8208 9775 -199 -67 13 C ATOM 735 N CYS A 125 35.753 4.047 14.099 1.00 61.45 N ANISOU 735 N CYS A 125 5233 8075 10040 78 182 13 N ATOM 736 CA CYS A 125 36.063 3.591 15.454 1.00 61.78 C ANISOU 736 CA CYS A 125 5391 8066 10017 144 253 25 C ATOM 737 C CYS A 125 37.223 2.588 15.409 1.00 61.92 C ANISOU 737 C CYS A 125 5432 8174 9921 214 181 -26 C ATOM 738 O CYS A 125 38.095 2.631 16.277 1.00 62.05 O ANISOU 738 O CYS A 125 5526 8234 9816 258 180 -35 O ATOM 739 CB CYS A 125 34.826 2.989 16.115 1.00 62.22 C ANISOU 739 CB CYS A 125 5489 7942 10210 162 366 77 C ATOM 740 SG CYS A 125 35.058 2.527 17.850 1.00 62.81 S ANISOU 740 SG CYS A 125 5730 7936 10199 239 473 108 S ATOM 741 N VAL A 126 37.233 1.701 14.385 1.00 60.36 N ANISOU 741 N VAL A 126 5169 8001 9764 227 116 -64 N ATOM 742 CA VAL A 126 38.270 0.689 14.149 1.00 60.57 C ANISOU 742 CA VAL A 126 5201 8109 9703 297 46 -120 C ATOM 743 C VAL A 126 39.610 1.374 13.822 1.00 60.33 C ANISOU 743 C VAL A 126 5134 8256 9533 290 -30 -162 C ATOM 744 O VAL A 126 40.634 0.997 14.396 1.00 60.58 O ANISOU 744 O VAL A 126 5208 8346 9463 353 -56 -187 O ATOM 745 CB VAL A 126 37.826 -0.358 13.084 1.00 60.75 C ANISOU 745 CB VAL A 126 5166 8101 9815 308 -1 -154 C ATOM 746 CG1 VAL A 126 39.012 -1.110 12.481 1.00 60.91 C ANISOU 746 CG1 VAL A 126 5163 8243 9736 366 -87 -227 C ATOM 747 CG2 VAL A 126 36.817 -1.341 13.672 1.00 61.23 C ANISOU 747 CG2 VAL A 126 5279 7986 10000 339 70 -117 C ATOM 748 N ILE A 127 39.584 2.402 12.940 1.00 59.21 N ANISOU 748 N ILE A 127 4912 8193 9392 212 -63 -165 N ATOM 749 CA ILE A 127 40.753 3.201 12.538 1.00 59.04 C ANISOU 749 CA ILE A 127 4842 8334 9257 186 -124 -195 C ATOM 750 C ILE A 127 41.401 3.850 13.776 1.00 59.11 C ANISOU 750 C ILE A 127 4919 8359 9181 198 -102 -178 C ATOM 751 O ILE A 127 42.624 3.793 13.918 1.00 59.30 O ANISOU 751 O ILE A 127 4934 8493 9104 231 -155 -214 O ATOM 752 CB ILE A 127 40.389 4.226 11.414 1.00 58.70 C ANISOU 752 CB ILE A 127 4714 8344 9245 93 -151 -184 C ATOM 753 CG1 ILE A 127 40.050 3.498 10.094 1.00 58.82 C ANISOU 753 CG1 ILE A 127 4669 8374 9305 92 -200 -217 C ATOM 754 CG2 ILE A 127 41.508 5.264 11.186 1.00 58.58 C ANISOU 754 CG2 ILE A 127 4656 8478 9124 52 -192 -197 C ATOM 755 CD1 ILE A 127 39.107 4.255 9.139 1.00 58.65 C ANISOU 755 CD1 ILE A 127 4593 8327 9364 8 -216 -187 C ATOM 756 N ALA A 128 40.569 4.406 14.687 1.00 58.46 N ANISOU 756 N ALA A 128 4907 8160 9145 175 -25 -126 N ATOM 757 CA ALA A 128 40.997 5.038 15.940 1.00 58.63 C ANISOU 757 CA ALA A 128 5018 8171 9088 185 1 -110 C ATOM 758 C ALA A 128 41.759 4.063 16.843 1.00 59.13 C ANISOU 758 C ALA A 128 5165 8234 9067 280 -15 -129 C ATOM 759 O ALA A 128 42.776 4.445 17.423 1.00 59.36 O ANISOU 759 O ALA A 128 5224 8339 8991 296 -63 -148 O ATOM 760 CB ALA A 128 39.795 5.613 16.675 1.00 58.61 C ANISOU 760 CB ALA A 128 5082 8024 9163 156 104 -54 C ATOM 761 N VAL A 129 41.285 2.802 16.930 1.00 58.67 N ANISOU 761 N VAL A 129 5141 8090 9061 342 14 -124 N ATOM 762 CA VAL A 129 41.912 1.733 17.717 1.00 59.23 C ANISOU 762 CA VAL A 129 5294 8145 9066 438 -3 -136 C ATOM 763 C VAL A 129 43.195 1.265 17.003 1.00 59.33 C ANISOU 763 C VAL A 129 5226 8304 9013 477 -110 -199 C ATOM 764 O VAL A 129 44.228 1.099 17.657 1.00 59.78 O ANISOU 764 O VAL A 129 5323 8417 8974 533 -162 -218 O ATOM 765 CB VAL A 129 40.923 0.568 18.025 1.00 59.57 C ANISOU 765 CB VAL A 129 5398 8035 9201 485 71 -103 C ATOM 766 CG1 VAL A 129 41.603 -0.564 18.796 1.00 60.25 C ANISOU 766 CG1 VAL A 129 5574 8101 9217 588 47 -110 C ATOM 767 CG2 VAL A 129 39.703 1.068 18.794 1.00 59.52 C ANISOU 767 CG2 VAL A 129 5466 7885 9263 449 193 -37 C ATOM 768 N ASP A 130 43.129 1.091 15.661 1.00 61.61 N ANISOU 768 N ASP A 130 5402 8655 9352 448 -143 -233 N ATOM 769 CA ASP A 130 44.250 0.667 14.813 1.00 61.78 C ANISOU 769 CA ASP A 130 5335 8816 9322 481 -226 -297 C ATOM 770 C ASP A 130 45.421 1.651 14.871 1.00 61.81 C ANISOU 770 C ASP A 130 5291 8962 9232 452 -281 -316 C ATOM 771 O ASP A 130 46.570 1.213 14.940 1.00 62.27 O ANISOU 771 O ASP A 130 5322 9110 9228 512 -342 -356 O ATOM 772 CB ASP A 130 43.792 0.459 13.359 1.00 61.50 C ANISOU 772 CB ASP A 130 5207 8809 9351 443 -239 -324 C ATOM 773 CG ASP A 130 44.837 -0.195 12.476 1.00 61.81 C ANISOU 773 CG ASP A 130 5170 8974 9341 492 -305 -394 C ATOM 774 OD1 ASP A 130 44.898 -1.442 12.455 1.00 62.23 O ANISOU 774 OD1 ASP A 130 5247 8985 9413 572 -316 -424 O ATOM 775 OD2 ASP A 130 45.595 0.542 11.809 1.00 61.70 O ANISOU 775 OD2 ASP A 130 5074 9097 9272 451 -339 -418 O ATOM 776 N ARG A 131 45.128 2.971 14.855 1.00 61.46 N ANISOU 776 N ARG A 131 5231 8931 9190 361 -261 -286 N ATOM 777 CA ARG A 131 46.145 4.024 14.926 1.00 61.53 C ANISOU 777 CA ARG A 131 5193 9059 9126 318 -311 -298 C ATOM 778 C ARG A 131 46.807 4.092 16.302 1.00 62.02 C ANISOU 778 C ARG A 131 5345 9106 9113 365 -337 -294 C ATOM 779 O ARG A 131 47.990 4.419 16.379 1.00 62.42 O ANISOU 779 O ARG A 131 5347 9268 9102 369 -408 -323 O ATOM 780 CB ARG A 131 45.584 5.398 14.506 1.00 61.03 C ANISOU 780 CB ARG A 131 5094 8999 9095 207 -284 -265 C ATOM 781 CG ARG A 131 45.292 5.554 13.007 1.00 60.69 C ANISOU 781 CG ARG A 131 4946 9016 9097 152 -290 -273 C ATOM 782 CD ARG A 131 46.532 5.777 12.151 1.00 60.93 C ANISOU 782 CD ARG A 131 4869 9216 9065 138 -348 -314 C ATOM 783 NE ARG A 131 47.142 4.513 11.735 1.00 61.33 N ANISOU 783 NE ARG A 131 4889 9319 9095 224 -376 -367 N ATOM 784 CZ ARG A 131 48.212 4.411 10.952 1.00 61.70 C ANISOU 784 CZ ARG A 131 4841 9508 9095 235 -413 -411 C ATOM 785 NH1 ARG A 131 48.806 5.502 10.481 1.00 61.77 N ANISOU 785 NH1 ARG A 131 4774 9623 9073 159 -426 -403 N ATOM 786 NH2 ARG A 131 48.693 3.219 10.628 1.00 62.12 N ANISOU 786 NH2 ARG A 131 4874 9592 9136 323 -431 -462 N ATOM 787 N TYR A 132 46.055 3.763 17.377 1.00 63.49 N ANISOU 787 N TYR A 132 5664 9153 9306 402 -282 -257 N ATOM 788 CA TYR A 132 46.562 3.742 18.752 1.00 64.08 C ANISOU 788 CA TYR A 132 5856 9195 9297 454 -305 -249 C ATOM 789 C TYR A 132 47.530 2.575 18.958 1.00 64.70 C ANISOU 789 C TYR A 132 5935 9319 9329 557 -377 -283 C ATOM 790 O TYR A 132 48.560 2.749 19.611 1.00 65.25 O ANISOU 790 O TYR A 132 6021 9450 9321 587 -456 -302 O ATOM 791 CB TYR A 132 45.409 3.697 19.776 1.00 64.15 C ANISOU 791 CB TYR A 132 6013 9038 9322 465 -206 -195 C ATOM 792 CG TYR A 132 45.865 3.560 21.215 1.00 64.90 C ANISOU 792 CG TYR A 132 6256 9089 9315 529 -227 -185 C ATOM 793 CD1 TYR A 132 46.411 4.642 21.901 1.00 65.17 C ANISOU 793 CD1 TYR A 132 6336 9158 9268 494 -269 -191 C ATOM 794 CD2 TYR A 132 45.746 2.350 21.892 1.00 65.45 C ANISOU 794 CD2 TYR A 132 6428 9075 9365 623 -209 -167 C ATOM 795 CE1 TYR A 132 46.844 4.517 23.220 1.00 65.98 C ANISOU 795 CE1 TYR A 132 6587 9219 9264 554 -301 -185 C ATOM 796 CE2 TYR A 132 46.174 2.214 23.212 1.00 66.26 C ANISOU 796 CE2 TYR A 132 6680 9136 9360 684 -235 -153 C ATOM 797 CZ TYR A 132 46.720 3.302 23.873 1.00 66.55 C ANISOU 797 CZ TYR A 132 6765 9213 9308 650 -284 -164 C ATOM 798 OH TYR A 132 47.136 3.174 25.177 1.00 67.45 O ANISOU 798 OH TYR A 132 7039 9283 9306 711 -321 -153 O ATOM 799 N PHE A 133 47.197 1.392 18.407 1.00 66.23 N ANISOU 799 N PHE A 133 6110 9477 9578 612 -357 -293 N ATOM 800 CA PHE A 133 48.036 0.199 18.504 1.00 66.87 C ANISOU 800 CA PHE A 133 6187 9589 9632 716 -420 -326 C ATOM 801 C PHE A 133 49.279 0.286 17.613 1.00 67.02 C ANISOU 801 C PHE A 133 6057 9775 9632 719 -503 -387 C ATOM 802 O PHE A 133 50.261 -0.405 17.882 1.00 67.70 O ANISOU 802 O PHE A 133 6131 9909 9683 803 -574 -417 O ATOM 803 CB PHE A 133 47.226 -1.079 18.233 1.00 66.92 C ANISOU 803 CB PHE A 133 6226 9489 9711 770 -370 -319 C ATOM 804 CG PHE A 133 46.515 -1.622 19.451 1.00 67.28 C ANISOU 804 CG PHE A 133 6434 9377 9752 818 -310 -262 C ATOM 805 CD1 PHE A 133 47.178 -2.444 20.356 1.00 68.07 C ANISOU 805 CD1 PHE A 133 6625 9450 9788 917 -358 -258 C ATOM 806 CD2 PHE A 133 45.180 -1.319 19.690 1.00 66.95 C ANISOU 806 CD2 PHE A 133 6453 9210 9774 765 -203 -209 C ATOM 807 CE1 PHE A 133 46.520 -2.944 21.484 1.00 68.51 C ANISOU 807 CE1 PHE A 133 6843 9359 9829 960 -296 -199 C ATOM 808 CE2 PHE A 133 44.522 -1.821 20.817 1.00 67.40 C ANISOU 808 CE2 PHE A 133 6661 9121 9827 808 -131 -152 C ATOM 809 CZ PHE A 133 45.196 -2.630 21.706 1.00 68.16 C ANISOU 809 CZ PHE A 133 6858 9194 9846 904 -175 -146 C ATOM 810 N ALA A 134 49.243 1.145 16.572 1.00 66.59 N ANISOU 810 N ALA A 134 5891 9807 9604 630 -492 -400 N ATOM 811 CA ALA A 134 50.360 1.371 15.652 1.00 66.80 C ANISOU 811 CA ALA A 134 5772 9995 9614 618 -548 -450 C ATOM 812 C ALA A 134 51.334 2.417 16.210 1.00 67.10 C ANISOU 812 C ALA A 134 5780 10118 9597 580 -610 -451 C ATOM 813 O ALA A 134 52.541 2.297 15.989 1.00 67.69 O ANISOU 813 O ALA A 134 5761 10307 9651 614 -677 -491 O ATOM 814 CB ALA A 134 49.844 1.807 14.290 1.00 66.22 C ANISOU 814 CB ALA A 134 5608 9967 9585 537 -504 -456 C ATOM 815 N ILE A 135 50.811 3.434 16.930 1.00 66.84 N ANISOU 815 N ILE A 135 5824 10025 9547 512 -589 -409 N ATOM 816 CA ILE A 135 51.611 4.503 17.537 1.00 67.17 C ANISOU 816 CA ILE A 135 5855 10127 9540 466 -652 -410 C ATOM 817 C ILE A 135 52.341 4.043 18.819 1.00 68.00 C ANISOU 817 C ILE A 135 6051 10205 9581 553 -731 -418 C ATOM 818 O ILE A 135 53.441 4.524 19.096 1.00 68.63 O ANISOU 818 O ILE A 135 6076 10372 9629 547 -821 -441 O ATOM 819 CB ILE A 135 50.801 5.829 17.696 1.00 66.61 C ANISOU 819 CB ILE A 135 5826 10006 9478 357 -603 -371 C ATOM 820 CG1 ILE A 135 51.725 7.065 17.726 1.00 66.95 C ANISOU 820 CG1 ILE A 135 5797 10146 9494 283 -671 -383 C ATOM 821 CG2 ILE A 135 49.821 5.803 18.884 1.00 66.49 C ANISOU 821 CG2 ILE A 135 5986 9832 9445 376 -547 -330 C ATOM 822 CD1 ILE A 135 51.123 8.343 17.129 1.00 66.45 C ANISOU 822 CD1 ILE A 135 5703 10080 9465 161 -624 -354 C ATOM 823 N THR A 136 51.734 3.104 19.578 1.00 68.60 N ANISOU 823 N THR A 136 6264 10159 9642 632 -700 -395 N ATOM 824 CA THR A 136 52.291 2.553 20.821 1.00 69.48 C ANISOU 824 CA THR A 136 6489 10227 9683 722 -771 -393 C ATOM 825 C THR A 136 53.249 1.381 20.564 1.00 70.12 C ANISOU 825 C THR A 136 6498 10371 9773 827 -845 -431 C ATOM 826 O THR A 136 54.052 1.045 21.438 1.00 70.87 O ANISOU 826 O THR A 136 6643 10469 9815 899 -940 -438 O ATOM 827 CB THR A 136 51.174 2.182 21.813 1.00 69.45 C ANISOU 827 CB THR A 136 6677 10058 9653 754 -694 -341 C ATOM 828 OG1 THR A 136 50.235 1.315 21.175 1.00 69.02 O ANISOU 828 OG1 THR A 136 6617 9935 9673 774 -603 -326 O ATOM 829 CG2 THR A 136 50.465 3.403 22.392 1.00 69.08 C ANISOU 829 CG2 THR A 136 6721 9948 9579 669 -639 -309 C ATOM 830 N SER A 137 53.159 0.767 19.366 1.00 70.32 N ANISOU 830 N SER A 137 6409 10443 9866 837 -806 -458 N ATOM 831 CA SER A 137 53.976 -0.361 18.908 1.00 70.93 C ANISOU 831 CA SER A 137 6404 10580 9967 936 -857 -503 C ATOM 832 C SER A 137 55.465 0.024 18.815 1.00 71.71 C ANISOU 832 C SER A 137 6370 10823 10053 945 -962 -544 C ATOM 833 O SER A 137 55.752 1.164 18.441 1.00 71.50 O ANISOU 833 O SER A 137 6257 10881 10029 848 -966 -549 O ATOM 834 CB SER A 137 53.482 -0.828 17.539 1.00 70.37 C ANISOU 834 CB SER A 137 6242 10533 9963 922 -784 -528 C ATOM 835 OG SER A 137 54.170 -1.970 17.055 1.00 70.95 O ANISOU 835 OG SER A 137 6246 10651 10061 1022 -819 -577 O ATOM 836 N PRO A 138 56.428 -0.899 19.114 1.00 74.45 N ANISOU 836 N PRO A 138 6690 11198 10399 1057 -1047 -574 N ATOM 837 CA PRO A 138 57.859 -0.546 18.981 1.00 75.31 C ANISOU 837 CA PRO A 138 6650 11445 10519 1066 -1146 -614 C ATOM 838 C PRO A 138 58.233 -0.189 17.541 1.00 75.10 C ANISOU 838 C PRO A 138 6434 11553 10548 1008 -1096 -654 C ATOM 839 O PRO A 138 59.136 0.618 17.317 1.00 75.54 O ANISOU 839 O PRO A 138 6361 11723 10618 957 -1141 -672 O ATOM 840 CB PRO A 138 58.589 -1.808 19.458 1.00 76.39 C ANISOU 840 CB PRO A 138 6799 11564 10662 1211 -1229 -635 C ATOM 841 CG PRO A 138 57.575 -2.582 20.229 1.00 76.14 C ANISOU 841 CG PRO A 138 6966 11370 10594 1265 -1193 -591 C ATOM 842 CD PRO A 138 56.271 -2.296 19.566 1.00 74.91 C ANISOU 842 CD PRO A 138 6843 11161 10458 1181 -1059 -569 C ATOM 843 N PHE A 139 57.508 -0.781 16.573 1.00 76.08 N ANISOU 843 N PHE A 139 6548 11656 10702 1014 -1001 -666 N ATOM 844 CA PHE A 139 57.633 -0.526 15.142 1.00 75.79 C ANISOU 844 CA PHE A 139 6368 11728 10701 962 -935 -699 C ATOM 845 C PHE A 139 56.537 0.509 14.835 1.00 74.66 C ANISOU 845 C PHE A 139 6273 11548 10546 833 -860 -656 C ATOM 846 O PHE A 139 55.465 0.162 14.327 1.00 73.96 O ANISOU 846 O PHE A 139 6242 11388 10472 820 -786 -645 O ATOM 847 CB PHE A 139 57.443 -1.827 14.322 1.00 75.87 C ANISOU 847 CB PHE A 139 6361 11723 10742 1051 -890 -742 C ATOM 848 CG PHE A 139 57.776 -3.118 15.039 1.00 76.71 C ANISOU 848 CG PHE A 139 6528 11761 10858 1192 -949 -758 C ATOM 849 CD1 PHE A 139 56.772 -3.911 15.580 1.00 76.47 C ANISOU 849 CD1 PHE A 139 6654 11576 10824 1238 -926 -728 C ATOM 850 CD2 PHE A 139 59.094 -3.537 15.175 1.00 77.84 C ANISOU 850 CD2 PHE A 139 6567 11988 11022 1279 -1027 -799 C ATOM 851 CE1 PHE A 139 57.080 -5.102 16.245 1.00 77.32 C ANISOU 851 CE1 PHE A 139 6825 11613 10940 1368 -981 -736 C ATOM 852 CE2 PHE A 139 59.401 -4.729 15.839 1.00 78.70 C ANISOU 852 CE2 PHE A 139 6734 12026 11143 1414 -1089 -810 C ATOM 853 CZ PHE A 139 58.393 -5.503 16.370 1.00 78.42 C ANISOU 853 CZ PHE A 139 6866 11836 11095 1457 -1066 -777 C ATOM 854 N LYS A 140 56.797 1.774 15.234 1.00 76.19 N ANISOU 854 N LYS A 140 6450 11778 10721 741 -889 -629 N ATOM 855 CA LYS A 140 55.898 2.930 15.115 1.00 75.32 C ANISOU 855 CA LYS A 140 6383 11632 10603 617 -834 -585 C ATOM 856 C LYS A 140 55.294 3.147 13.732 1.00 74.66 C ANISOU 856 C LYS A 140 6236 11586 10546 551 -747 -586 C ATOM 857 O LYS A 140 55.959 2.920 12.720 1.00 75.02 O ANISOU 857 O LYS A 140 6156 11744 10604 562 -734 -624 O ATOM 858 CB LYS A 140 56.588 4.214 15.605 1.00 75.64 C ANISOU 858 CB LYS A 140 6379 11732 10629 536 -893 -572 C ATOM 859 CG LYS A 140 56.175 4.645 17.008 1.00 75.48 C ANISOU 859 CG LYS A 140 6515 11599 10565 525 -932 -538 C ATOM 860 CD LYS A 140 57.187 4.223 18.066 1.00 76.49 C ANISOU 860 CD LYS A 140 6670 11731 10662 611 -1049 -557 C ATOM 861 CE LYS A 140 56.816 4.738 19.434 1.00 76.53 C ANISOU 861 CE LYS A 140 6839 11633 10606 594 -1090 -526 C ATOM 862 NZ LYS A 140 57.772 4.281 20.475 1.00 77.49 N ANISOU 862 NZ LYS A 140 7007 11749 10687 684 -1215 -542 N ATOM 863 N TYR A 141 54.014 3.579 13.710 1.00 75.53 N ANISOU 863 N TYR A 141 6438 11597 10663 487 -687 -544 N ATOM 864 CA TYR A 141 53.201 3.878 12.522 1.00 74.87 C ANISOU 864 CA TYR A 141 6323 11520 10604 416 -615 -532 C ATOM 865 C TYR A 141 52.919 2.690 11.583 1.00 74.96 C ANISOU 865 C TYR A 141 6315 11532 10634 482 -582 -571 C ATOM 866 O TYR A 141 52.399 2.884 10.480 1.00 74.59 O ANISOU 866 O TYR A 141 6235 11507 10599 429 -537 -570 O ATOM 867 CB TYR A 141 53.702 5.138 11.780 1.00 74.85 C ANISOU 867 CB TYR A 141 6210 11633 10596 307 -609 -521 C ATOM 868 CG TYR A 141 53.705 6.375 12.651 1.00 74.82 C ANISOU 868 CG TYR A 141 6242 11603 10583 230 -639 -483 C ATOM 869 CD1 TYR A 141 52.543 7.116 12.847 1.00 74.14 C ANISOU 869 CD1 TYR A 141 6243 11415 10511 157 -599 -434 C ATOM 870 CD2 TYR A 141 54.865 6.796 13.294 1.00 75.59 C ANISOU 870 CD2 TYR A 141 6285 11772 10665 233 -712 -498 C ATOM 871 CE1 TYR A 141 52.535 8.245 13.663 1.00 74.19 C ANISOU 871 CE1 TYR A 141 6292 11390 10507 92 -624 -406 C ATOM 872 CE2 TYR A 141 54.869 7.924 14.113 1.00 75.68 C ANISOU 872 CE2 TYR A 141 6338 11751 10666 162 -749 -470 C ATOM 873 CZ TYR A 141 53.701 8.646 14.294 1.00 74.95 C ANISOU 873 CZ TYR A 141 6343 11555 10579 93 -701 -426 C ATOM 874 OH TYR A 141 53.701 9.764 15.091 1.00 75.11 O ANISOU 874 OH TYR A 141 6413 11538 10588 26 -735 -404 O ATOM 875 N GLN A 142 53.215 1.462 12.046 1.00 74.72 N ANISOU 875 N GLN A 142 6317 11468 10606 599 -609 -604 N ATOM 876 CA GLN A 142 52.985 0.222 11.305 1.00 74.94 C ANISOU 876 CA GLN A 142 6340 11478 10655 675 -587 -648 C ATOM 877 C GLN A 142 51.904 -0.588 12.018 1.00 74.62 C ANISOU 877 C GLN A 142 6437 11269 10646 723 -571 -622 C ATOM 878 O GLN A 142 52.066 -0.934 13.192 1.00 74.98 O ANISOU 878 O GLN A 142 6560 11247 10681 781 -603 -605 O ATOM 879 CB GLN A 142 54.291 -0.580 11.156 1.00 75.94 C ANISOU 879 CB GLN A 142 6381 11701 10772 776 -629 -709 C ATOM 880 CG GLN A 142 55.279 0.042 10.174 1.00 76.39 C ANISOU 880 CG GLN A 142 6286 11927 10812 734 -620 -740 C ATOM 881 CD GLN A 142 56.681 -0.469 10.380 1.00 77.43 C ANISOU 881 CD GLN A 142 6323 12150 10947 824 -669 -786 C ATOM 882 OE1 GLN A 142 57.408 -0.020 11.273 1.00 77.70 O ANISOU 882 OE1 GLN A 142 6335 12207 10980 823 -731 -769 O ATOM 883 NE2 GLN A 142 57.102 -1.404 9.543 1.00 78.16 N ANISOU 883 NE2 GLN A 142 6353 12296 11048 903 -647 -848 N ATOM 884 N SER A 143 50.782 -0.846 11.317 1.00 73.05 N ANISOU 884 N SER A 143 6270 10999 10487 693 -523 -616 N ATOM 885 CA SER A 143 49.626 -1.581 11.838 1.00 72.76 C ANISOU 885 CA SER A 143 6348 10796 10502 722 -494 -588 C ATOM 886 C SER A 143 49.958 -3.041 12.148 1.00 73.39 C ANISOU 886 C SER A 143 6466 10824 10594 847 -519 -625 C ATOM 887 O SER A 143 50.634 -3.702 11.357 1.00 73.91 O ANISOU 887 O SER A 143 6461 10967 10654 904 -540 -688 O ATOM 888 CB SER A 143 48.454 -1.493 10.867 1.00 72.20 C ANISOU 888 CB SER A 143 6275 10673 10484 656 -452 -581 C ATOM 889 OG SER A 143 47.283 -2.085 11.406 1.00 72.03 O ANISOU 889 OG SER A 143 6352 10485 10531 671 -419 -545 O ATOM 890 N LEU A 144 49.479 -3.531 13.307 1.00 73.79 N ANISOU 890 N LEU A 144 6633 10741 10662 891 -512 -582 N ATOM 891 CA LEU A 144 49.695 -4.904 13.779 1.00 74.44 C ANISOU 891 CA LEU A 144 6774 10749 10761 1009 -535 -600 C ATOM 892 C LEU A 144 48.943 -5.943 12.942 1.00 74.43 C ANISOU 892 C LEU A 144 6780 10669 10831 1035 -510 -632 C ATOM 893 O LEU A 144 49.385 -7.090 12.856 1.00 74.99 O ANISOU 893 O LEU A 144 6859 10719 10916 1135 -539 -674 O ATOM 894 CB LEU A 144 49.323 -5.041 15.268 1.00 74.62 C ANISOU 894 CB LEU A 144 6935 10645 10772 1038 -526 -534 C ATOM 895 CG LEU A 144 50.222 -4.317 16.278 1.00 74.83 C ANISOU 895 CG LEU A 144 6981 10733 10718 1043 -576 -514 C ATOM 896 CD1 LEU A 144 49.486 -4.072 17.576 1.00 75.03 C ANISOU 896 CD1 LEU A 144 7158 10627 10723 1034 -539 -441 C ATOM 897 CD2 LEU A 144 51.509 -5.094 16.546 1.00 75.62 C ANISOU 897 CD2 LEU A 144 7046 10900 10786 1154 -662 -557 C ATOM 898 N LEU A 145 47.814 -5.540 12.329 1.00 74.31 N ANISOU 898 N LEU A 145 6763 10606 10865 947 -464 -613 N ATOM 899 CA LEU A 145 46.981 -6.401 11.489 1.00 74.37 C ANISOU 899 CA LEU A 145 6776 10532 10948 955 -450 -643 C ATOM 900 C LEU A 145 47.554 -6.536 10.076 1.00 74.69 C ANISOU 900 C LEU A 145 6719 10699 10961 961 -479 -725 C ATOM 901 O LEU A 145 48.012 -5.546 9.500 1.00 74.50 O ANISOU 901 O LEU A 145 6617 10807 10882 901 -481 -734 O ATOM 902 CB LEU A 145 45.542 -5.858 11.420 1.00 73.67 C ANISOU 902 CB LEU A 145 6719 10339 10933 856 -399 -587 C ATOM 903 CG LEU A 145 44.709 -5.957 12.697 1.00 73.54 C ANISOU 903 CG LEU A 145 6810 10166 10967 855 -346 -508 C ATOM 904 CD1 LEU A 145 43.808 -4.751 12.849 1.00 72.88 C ANISOU 904 CD1 LEU A 145 6727 10050 10914 747 -295 -447 C ATOM 905 CD2 LEU A 145 43.893 -7.240 12.727 1.00 74.00 C ANISOU 905 CD2 LEU A 145 6926 10068 11123 901 -329 -507 C ATOM 906 N THR A 146 47.522 -7.763 9.524 1.00 76.11 N ANISOU 906 N THR A 146 6908 10832 11178 1034 -497 -785 N ATOM 907 CA THR A 146 47.996 -8.066 8.166 1.00 76.57 C ANISOU 907 CA THR A 146 6895 10992 11206 1053 -517 -873 C ATOM 908 C THR A 146 46.876 -7.777 7.153 1.00 76.14 C ANISOU 908 C THR A 146 6840 10900 11190 964 -508 -875 C ATOM 909 O THR A 146 45.733 -7.571 7.566 1.00 75.66 O ANISOU 909 O THR A 146 6829 10715 11203 905 -489 -813 O ATOM 910 CB THR A 146 48.518 -9.514 8.071 1.00 77.51 C ANISOU 910 CB THR A 146 7032 11074 11344 1180 -545 -943 C ATOM 911 OG1 THR A 146 47.490 -10.423 8.468 1.00 77.62 O ANISOU 911 OG1 THR A 146 7137 10904 11451 1199 -542 -921 O ATOM 912 CG2 THR A 146 49.780 -9.745 8.898 1.00 77.98 C ANISOU 912 CG2 THR A 146 7073 11194 11362 1273 -568 -948 C ATOM 913 N LYS A 147 47.202 -7.754 5.838 1.00 78.23 N ANISOU 913 N LYS A 147 7049 11269 11406 956 -522 -945 N ATOM 914 CA LYS A 147 46.248 -7.486 4.749 1.00 77.99 C ANISOU 914 CA LYS A 147 7021 11217 11395 877 -532 -955 C ATOM 915 C LYS A 147 45.036 -8.421 4.771 1.00 78.05 C ANISOU 915 C LYS A 147 7098 11041 11516 884 -552 -957 C ATOM 916 O LYS A 147 43.907 -7.949 4.635 1.00 77.55 O ANISOU 916 O LYS A 147 7049 10898 11518 798 -553 -908 O ATOM 917 CB LYS A 147 46.930 -7.539 3.372 1.00 78.66 C ANISOU 917 CB LYS A 147 7056 11440 11391 893 -544 -1041 C ATOM 918 CG LYS A 147 47.841 -6.351 3.069 1.00 78.55 C ANISOU 918 CG LYS A 147 6962 11605 11278 846 -517 -1026 C ATOM 919 CD LYS A 147 48.078 -6.146 1.564 1.00 79.30 C ANISOU 919 CD LYS A 147 7026 11816 11288 822 -516 -1086 C ATOM 920 CE LYS A 147 49.118 -7.064 0.953 1.00 80.32 C ANISOU 920 CE LYS A 147 7133 12025 11360 930 -507 -1189 C ATOM 921 NZ LYS A 147 48.520 -8.333 0.456 1.00 80.80 N ANISOU 921 NZ LYS A 147 7266 11972 11462 989 -544 -1262 N ATOM 922 N ASN A 148 45.273 -9.736 4.960 1.00 81.04 N ANISOU 922 N ASN A 148 7516 11347 11929 986 -568 -1009 N ATOM 923 CA ASN A 148 44.228 -10.762 5.020 1.00 81.34 C ANISOU 923 CA ASN A 148 7619 11202 12084 1001 -588 -1014 C ATOM 924 C ASN A 148 43.385 -10.643 6.290 1.00 80.87 C ANISOU 924 C ASN A 148 7608 10999 12121 969 -550 -913 C ATOM 925 O ASN A 148 42.173 -10.852 6.233 1.00 80.79 O ANISOU 925 O ASN A 148 7625 10850 12222 917 -552 -883 O ATOM 926 CB ASN A 148 44.832 -12.161 4.902 1.00 82.29 C ANISOU 926 CB ASN A 148 7768 11288 12210 1124 -614 -1098 C ATOM 927 CG ASN A 148 45.459 -12.432 3.559 1.00 82.97 C ANISOU 927 CG ASN A 148 7821 11489 12215 1160 -643 -1208 C ATOM 928 OD1 ASN A 148 44.790 -12.842 2.604 1.00 83.44 O ANISOU 928 OD1 ASN A 148 7904 11497 12302 1138 -681 -1262 O ATOM 929 ND2 ASN A 148 46.760 -12.203 3.454 1.00 83.14 N ANISOU 929 ND2 ASN A 148 7787 11667 12135 1216 -624 -1244 N ATOM 930 N LYS A 149 44.025 -10.298 7.427 1.00 79.95 N ANISOU 930 N LYS A 149 7502 10914 11962 998 -516 -860 N ATOM 931 CA LYS A 149 43.358 -10.124 8.721 1.00 79.63 C ANISOU 931 CA LYS A 149 7521 10750 11985 975 -468 -762 C ATOM 932 C LYS A 149 42.513 -8.849 8.762 1.00 78.83 C ANISOU 932 C LYS A 149 7398 10646 11908 857 -432 -693 C ATOM 933 O LYS A 149 41.453 -8.852 9.388 1.00 78.70 O ANISOU 933 O LYS A 149 7425 10487 11990 818 -389 -625 O ATOM 934 CB LYS A 149 44.367 -10.160 9.879 1.00 79.79 C ANISOU 934 CB LYS A 149 7572 10810 11935 1049 -456 -735 C ATOM 935 CG LYS A 149 44.814 -11.570 10.244 1.00 80.67 C ANISOU 935 CG LYS A 149 7735 10847 12069 1169 -480 -770 C ATOM 936 CD LYS A 149 45.922 -11.570 11.284 1.00 80.95 C ANISOU 936 CD LYS A 149 7793 10939 12026 1247 -490 -750 C ATOM 937 CE LYS A 149 46.449 -12.962 11.533 1.00 81.90 C ANISOU 937 CE LYS A 149 7956 10995 12168 1372 -524 -789 C ATOM 938 NZ LYS A 149 47.599 -12.956 12.474 1.00 82.29 N ANISOU 938 NZ LYS A 149 8017 11109 12141 1453 -552 -775 N ATOM 939 N ALA A 150 42.972 -7.773 8.082 1.00 76.74 N ANISOU 939 N ALA A 150 7066 10533 11559 801 -446 -707 N ATOM 940 CA ALA A 150 42.269 -6.487 7.996 1.00 76.05 C ANISOU 940 CA ALA A 150 6951 10456 11489 691 -421 -647 C ATOM 941 C ALA A 150 40.982 -6.608 7.180 1.00 76.08 C ANISOU 941 C ALA A 150 6945 10362 11600 627 -441 -646 C ATOM 942 O ALA A 150 39.999 -5.940 7.505 1.00 75.75 O ANISOU 942 O ALA A 150 6904 10239 11638 553 -407 -578 O ATOM 943 CB ALA A 150 43.174 -5.428 7.389 1.00 75.75 C ANISOU 943 CB ALA A 150 6844 10602 11335 653 -437 -667 C ATOM 944 N ARG A 151 40.988 -7.469 6.133 1.00 76.74 N ANISOU 944 N ARG A 151 7020 10447 11690 658 -497 -726 N ATOM 945 CA ARG A 151 39.837 -7.743 5.262 1.00 76.99 C ANISOU 945 CA ARG A 151 7046 10384 11823 606 -541 -741 C ATOM 946 C ARG A 151 38.700 -8.388 6.058 1.00 77.12 C ANISOU 946 C ARG A 151 7103 10197 12002 602 -510 -688 C ATOM 947 O ARG A 151 37.532 -8.115 5.780 1.00 76.98 O ANISOU 947 O ARG A 151 7066 10085 12098 527 -520 -653 O ATOM 948 CB ARG A 151 40.237 -8.650 4.087 1.00 77.75 C ANISOU 948 CB ARG A 151 7143 10523 11875 658 -610 -849 C ATOM 949 CG ARG A 151 41.008 -7.941 2.982 1.00 77.79 C ANISOU 949 CG ARG A 151 7105 10712 11740 636 -638 -898 C ATOM 950 CD ARG A 151 41.537 -8.932 1.966 1.00 78.71 C ANISOU 950 CD ARG A 151 7237 10870 11799 706 -689 -1011 C ATOM 951 NE ARG A 151 42.780 -8.469 1.345 1.00 78.93 N ANISOU 951 NE ARG A 151 7228 11092 11670 732 -676 -1059 N ATOM 952 CZ ARG A 151 43.537 -9.205 0.535 1.00 79.79 C ANISOU 952 CZ ARG A 151 7344 11271 11701 807 -695 -1160 C ATOM 953 NH1 ARG A 151 43.187 -10.450 0.235 1.00 80.51 N ANISOU 953 NH1 ARG A 151 7487 11253 11851 864 -739 -1230 N ATOM 954 NH2 ARG A 151 44.651 -8.701 0.021 1.00 80.02 N ANISOU 954 NH2 ARG A 151 7329 11478 11597 825 -667 -1193 N ATOM 955 N VAL A 152 39.052 -9.232 7.055 1.00 76.27 N ANISOU 955 N VAL A 152 7050 10021 11908 681 -472 -678 N ATOM 956 CA VAL A 152 38.116 -9.916 7.955 1.00 76.55 C ANISOU 956 CA VAL A 152 7135 9864 12087 686 -424 -619 C ATOM 957 C VAL A 152 37.403 -8.868 8.828 1.00 75.94 C ANISOU 957 C VAL A 152 7057 9738 12059 615 -344 -515 C ATOM 958 O VAL A 152 36.176 -8.905 8.925 1.00 76.04 O ANISOU 958 O VAL A 152 7060 9612 12220 559 -317 -468 O ATOM 959 CB VAL A 152 38.814 -11.030 8.794 1.00 77.10 C ANISOU 959 CB VAL A 152 7274 9886 12134 795 -406 -629 C ATOM 960 CG1 VAL A 152 37.846 -11.690 9.775 1.00 77.37 C ANISOU 960 CG1 VAL A 152 7367 9719 12311 796 -341 -554 C ATOM 961 CG2 VAL A 152 39.453 -12.083 7.892 1.00 77.87 C ANISOU 961 CG2 VAL A 152 7371 10016 12200 869 -482 -737 C ATOM 962 N ILE A 153 38.171 -7.910 9.406 1.00 74.66 N ANISOU 962 N ILE A 153 6898 9692 11777 614 -308 -486 N ATOM 963 CA ILE A 153 37.678 -6.806 10.248 1.00 74.15 C ANISOU 963 CA ILE A 153 6841 9601 11731 554 -232 -398 C ATOM 964 C ILE A 153 36.625 -5.973 9.493 1.00 73.89 C ANISOU 964 C ILE A 153 6741 9543 11791 452 -243 -375 C ATOM 965 O ILE A 153 35.608 -5.604 10.082 1.00 73.88 O ANISOU 965 O ILE A 153 6744 9424 11903 406 -174 -303 O ATOM 966 CB ILE A 153 38.848 -5.934 10.818 1.00 73.67 C ANISOU 966 CB ILE A 153 6792 9686 11513 571 -219 -391 C ATOM 967 CG1 ILE A 153 39.974 -6.778 11.493 1.00 74.04 C ANISOU 967 CG1 ILE A 153 6897 9766 11469 678 -230 -419 C ATOM 968 CG2 ILE A 153 38.356 -4.800 11.736 1.00 73.25 C ANISOU 968 CG2 ILE A 153 6762 9598 11472 514 -140 -309 C ATOM 969 CD1 ILE A 153 39.592 -7.676 12.744 1.00 74.62 C ANISOU 969 CD1 ILE A 153 7072 9681 11600 737 -168 -366 C ATOM 970 N ILE A 154 36.862 -5.717 8.185 1.00 75.64 N ANISOU 970 N ILE A 154 6903 9870 11967 423 -328 -436 N ATOM 971 CA ILE A 154 35.953 -4.988 7.291 1.00 75.52 C ANISOU 971 CA ILE A 154 6826 9841 12027 333 -366 -422 C ATOM 972 C ILE A 154 34.623 -5.759 7.187 1.00 76.08 C ANISOU 972 C ILE A 154 6889 9728 12290 312 -372 -405 C ATOM 973 O ILE A 154 33.559 -5.164 7.376 1.00 76.01 O ANISOU 973 O ILE A 154 6847 9626 12407 246 -338 -341 O ATOM 974 CB ILE A 154 36.615 -4.723 5.902 1.00 75.50 C ANISOU 974 CB ILE A 154 6783 9993 11911 320 -459 -495 C ATOM 975 CG1 ILE A 154 37.822 -3.762 6.032 1.00 75.04 C ANISOU 975 CG1 ILE A 154 6713 10111 11688 322 -441 -495 C ATOM 976 CG2 ILE A 154 35.599 -4.189 4.881 1.00 75.49 C ANISOU 976 CG2 ILE A 154 6731 9960 11992 235 -520 -484 C ATOM 977 CD1 ILE A 154 38.910 -3.920 4.950 1.00 75.28 C ANISOU 977 CD1 ILE A 154 6722 10303 11578 352 -503 -578 C ATOM 978 N LEU A 155 34.699 -7.085 6.938 1.00 78.21 N ANISOU 978 N LEU A 155 7187 9938 12592 369 -413 -462 N ATOM 979 CA LEU A 155 33.545 -7.983 6.843 1.00 78.93 C ANISOU 979 CA LEU A 155 7272 9847 12871 354 -427 -455 C ATOM 980 C LEU A 155 32.819 -8.119 8.186 1.00 79.07 C ANISOU 980 C LEU A 155 7318 9711 13014 353 -308 -363 C ATOM 981 O LEU A 155 31.593 -8.225 8.199 1.00 79.55 O ANISOU 981 O LEU A 155 7341 9626 13258 301 -291 -319 O ATOM 982 CB LEU A 155 33.969 -9.362 6.313 1.00 79.63 C ANISOU 982 CB LEU A 155 7394 9915 12946 424 -497 -544 C ATOM 983 CG LEU A 155 33.717 -9.617 4.825 1.00 80.00 C ANISOU 983 CG LEU A 155 7408 9987 13001 397 -624 -627 C ATOM 984 CD1 LEU A 155 34.859 -9.090 3.964 1.00 79.63 C ANISOU 984 CD1 LEU A 155 7358 10147 12751 416 -673 -694 C ATOM 985 CD2 LEU A 155 33.530 -11.095 4.557 1.00 80.95 C ANISOU 985 CD2 LEU A 155 7563 9991 13203 447 -677 -692 C ATOM 986 N MET A 156 33.575 -8.083 9.310 1.00 79.85 N ANISOU 986 N MET A 156 7483 9844 13012 409 -225 -331 N ATOM 987 CA MET A 156 33.049 -8.152 10.680 1.00 80.04 C ANISOU 987 CA MET A 156 7559 9740 13112 418 -99 -241 C ATOM 988 C MET A 156 32.171 -6.934 10.982 1.00 79.65 C ANISOU 988 C MET A 156 7467 9657 13140 337 -29 -166 C ATOM 989 O MET A 156 31.161 -7.070 11.671 1.00 80.07 O ANISOU 989 O MET A 156 7523 9556 13344 314 64 -96 O ATOM 990 CB MET A 156 34.194 -8.236 11.706 1.00 79.88 C ANISOU 990 CB MET A 156 7628 9792 12931 496 -50 -232 C ATOM 991 CG MET A 156 34.816 -9.612 11.830 1.00 80.36 C ANISOU 991 CG MET A 156 7748 9824 12962 588 -84 -277 C ATOM 992 SD MET A 156 33.856 -10.753 12.849 1.00 81.42 S ANISOU 992 SD MET A 156 7953 9723 13260 612 12 -204 S ATOM 993 CE MET A 156 34.996 -12.115 12.951 1.00 81.68 C ANISOU 993 CE MET A 156 8061 9777 13197 732 -47 -265 C ATOM 994 N VAL A 157 32.556 -5.752 10.452 1.00 77.67 N ANISOU 994 N VAL A 157 7173 9545 12793 296 -69 -180 N ATOM 995 CA VAL A 157 31.838 -4.483 10.608 1.00 77.27 C ANISOU 995 CA VAL A 157 7077 9480 12803 222 -18 -118 C ATOM 996 C VAL A 157 30.495 -4.532 9.857 1.00 77.65 C ANISOU 996 C VAL A 157 7037 9411 13055 154 -55 -103 C ATOM 997 O VAL A 157 29.461 -4.244 10.460 1.00 77.92 O ANISOU 997 O VAL A 157 7049 9316 13242 118 35 -32 O ATOM 998 CB VAL A 157 32.729 -3.265 10.211 1.00 76.52 C ANISOU 998 CB VAL A 157 6964 9566 12544 199 -61 -139 C ATOM 999 CG1 VAL A 157 31.905 -1.998 9.977 1.00 76.24 C ANISOU 999 CG1 VAL A 157 6864 9514 12590 115 -46 -90 C ATOM 1000 CG2 VAL A 157 33.809 -3.012 11.260 1.00 76.27 C ANISOU 1000 CG2 VAL A 157 7013 9614 12353 252 -2 -130 C ATOM 1001 N TRP A 158 30.517 -4.925 8.563 1.00 76.60 N ANISOU 1001 N TRP A 158 6858 9319 12927 139 -188 -172 N ATOM 1002 CA TRP A 158 29.333 -5.027 7.700 1.00 77.09 C ANISOU 1002 CA TRP A 158 6838 9281 13172 77 -260 -171 C ATOM 1003 C TRP A 158 28.298 -6.058 8.170 1.00 77.93 C ANISOU 1003 C TRP A 158 6933 9185 13491 78 -213 -139 C ATOM 1004 O TRP A 158 27.100 -5.815 8.015 1.00 78.35 O ANISOU 1004 O TRP A 158 6909 9121 13740 16 -210 -95 O ATOM 1005 CB TRP A 158 29.732 -5.269 6.237 1.00 77.23 C ANISOU 1005 CB TRP A 158 6835 9397 13112 71 -418 -261 C ATOM 1006 CG TRP A 158 30.288 -4.054 5.554 1.00 76.62 C ANISOU 1006 CG TRP A 158 6736 9483 12893 35 -469 -271 C ATOM 1007 CD1 TRP A 158 31.599 -3.788 5.293 1.00 76.16 C ANISOU 1007 CD1 TRP A 158 6715 9601 12621 70 -489 -318 C ATOM 1008 CD2 TRP A 158 29.543 -2.937 5.049 1.00 76.50 C ANISOU 1008 CD2 TRP A 158 6652 9464 12950 -43 -504 -227 C ATOM 1009 NE1 TRP A 158 31.719 -2.576 4.653 1.00 75.77 N ANISOU 1009 NE1 TRP A 158 6629 9657 12502 14 -530 -304 N ATOM 1010 CE2 TRP A 158 30.472 -2.032 4.491 1.00 75.96 C ANISOU 1010 CE2 TRP A 158 6593 9573 12695 -54 -543 -248 C ATOM 1011 CE3 TRP A 158 28.176 -2.613 5.012 1.00 76.90 C ANISOU 1011 CE3 TRP A 158 6630 9374 13215 -104 -507 -170 C ATOM 1012 CZ2 TRP A 158 30.079 -0.824 3.902 1.00 75.79 C ANISOU 1012 CZ2 TRP A 158 6521 9590 12686 -124 -587 -211 C ATOM 1013 CZ3 TRP A 158 27.788 -1.416 4.428 1.00 76.73 C ANISOU 1013 CZ3 TRP A 158 6552 9392 13210 -169 -556 -137 C ATOM 1014 CH2 TRP A 158 28.733 -0.537 3.881 1.00 76.18 C ANISOU 1014 CH2 TRP A 158 6504 9497 12944 -178 -596 -156 C ATOM 1015 N ILE A 159 28.755 -7.195 8.745 1.00 77.70 N ANISOU 1015 N ILE A 159 6977 9111 13434 146 -175 -156 N ATOM 1016 CA ILE A 159 27.884 -8.257 9.272 1.00 78.59 C ANISOU 1016 CA ILE A 159 7092 9030 13739 151 -119 -121 C ATOM 1017 C ILE A 159 27.155 -7.768 10.537 1.00 78.68 C ANISOU 1017 C ILE A 159 7107 8932 13857 132 52 -12 C ATOM 1018 O ILE A 159 25.936 -7.937 10.637 1.00 79.33 O ANISOU 1018 O ILE A 159 7122 8856 14164 83 94 38 O ATOM 1019 CB ILE A 159 28.646 -9.610 9.442 1.00 79.03 C ANISOU 1019 CB ILE A 159 7231 9072 13725 233 -140 -173 C ATOM 1020 CG1 ILE A 159 28.904 -10.260 8.059 1.00 79.48 C ANISOU 1020 CG1 ILE A 159 7264 9172 13762 238 -307 -281 C ATOM 1021 CG2 ILE A 159 27.900 -10.590 10.372 1.00 79.83 C ANISOU 1021 CG2 ILE A 159 7361 8973 13998 246 -36 -110 C ATOM 1022 CD1 ILE A 159 30.083 -11.257 7.988 1.00 79.72 C ANISOU 1022 CD1 ILE A 159 7377 9267 13646 332 -349 -359 C ATOM 1023 N VAL A 160 27.895 -7.125 11.471 1.00 78.93 N ANISOU 1023 N VAL A 160 7213 9048 13728 168 149 20 N ATOM 1024 CA VAL A 160 27.360 -6.542 12.711 1.00 79.03 C ANISOU 1024 CA VAL A 160 7254 8979 13795 158 318 115 C ATOM 1025 C VAL A 160 26.384 -5.400 12.358 1.00 78.83 C ANISOU 1025 C VAL A 160 7123 8928 13901 78 329 154 C ATOM 1026 O VAL A 160 25.330 -5.283 12.990 1.00 79.32 O ANISOU 1026 O VAL A 160 7152 8847 14139 49 450 228 O ATOM 1027 CB VAL A 160 28.496 -6.125 13.695 1.00 78.52 C ANISOU 1027 CB VAL A 160 7307 9024 13504 219 388 125 C ATOM 1028 CG1 VAL A 160 28.002 -5.177 14.789 1.00 78.63 C ANISOU 1028 CG1 VAL A 160 7351 8986 13540 200 546 209 C ATOM 1029 CG2 VAL A 160 29.155 -7.353 14.318 1.00 78.92 C ANISOU 1029 CG2 VAL A 160 7462 9044 13480 300 407 115 C ATOM 1030 N SER A 161 26.712 -4.612 11.307 1.00 80.35 N ANISOU 1030 N SER A 161 7259 9251 14019 44 204 104 N ATOM 1031 CA SER A 161 25.874 -3.523 10.796 1.00 80.21 C ANISOU 1031 CA SER A 161 7140 9220 14116 -30 182 134 C ATOM 1032 C SER A 161 24.556 -4.071 10.239 1.00 81.10 C ANISOU 1032 C SER A 161 7147 9174 14493 -79 139 149 C ATOM 1033 O SER A 161 23.507 -3.481 10.484 1.00 81.38 O ANISOU 1033 O SER A 161 7105 9107 14708 -125 208 213 O ATOM 1034 CB SER A 161 26.610 -2.729 9.721 1.00 79.49 C ANISOU 1034 CB SER A 161 7028 9305 13870 -51 44 76 C ATOM 1035 OG SER A 161 27.775 -2.116 10.245 1.00 78.76 O ANISOU 1035 OG SER A 161 7015 9353 13557 -15 83 67 O ATOM 1036 N GLY A 162 24.626 -5.207 9.537 1.00 82.94 N ANISOU 1036 N GLY A 162 7377 9381 14756 -67 29 90 N ATOM 1037 CA GLY A 162 23.471 -5.893 8.964 1.00 83.93 C ANISOU 1037 CA GLY A 162 7408 9352 15129 -112 -35 92 C ATOM 1038 C GLY A 162 22.539 -6.473 10.010 1.00 84.78 C ANISOU 1038 C GLY A 162 7499 9267 15446 -115 120 170 C ATOM 1039 O GLY A 162 21.323 -6.509 9.807 1.00 85.59 O ANISOU 1039 O GLY A 162 7491 9229 15800 -171 119 209 O ATOM 1040 N LEU A 163 23.108 -6.921 11.142 1.00 86.43 N ANISOU 1040 N LEU A 163 7819 9467 15553 -54 257 199 N ATOM 1041 CA LEU A 163 22.372 -7.491 12.271 1.00 87.29 C ANISOU 1041 CA LEU A 163 7942 9403 15821 -47 430 282 C ATOM 1042 C LEU A 163 21.669 -6.390 13.081 1.00 87.29 C ANISOU 1042 C LEU A 163 7907 9355 15905 -76 592 369 C ATOM 1043 O LEU A 163 20.579 -6.622 13.608 1.00 88.18 O ANISOU 1043 O LEU A 163 7959 9299 16246 -104 711 441 O ATOM 1044 CB LEU A 163 23.338 -8.282 13.172 1.00 87.21 C ANISOU 1044 CB LEU A 163 8083 9416 15638 35 507 281 C ATOM 1045 CG LEU A 163 22.711 -9.264 14.161 1.00 88.21 C ANISOU 1045 CG LEU A 163 8247 9357 15912 50 657 355 C ATOM 1046 CD1 LEU A 163 22.782 -10.687 13.637 1.00 89.13 C ANISOU 1046 CD1 LEU A 163 8369 9398 16098 66 556 306 C ATOM 1047 CD2 LEU A 163 23.395 -9.180 15.510 1.00 87.89 C ANISOU 1047 CD2 LEU A 163 8356 9346 15691 117 812 405 C ATOM 1048 N THR A 164 22.298 -5.202 13.178 1.00 88.01 N ANISOU 1048 N THR A 164 8035 9589 15816 -67 600 362 N ATOM 1049 CA THR A 164 21.797 -4.052 13.941 1.00 87.98 C ANISOU 1049 CA THR A 164 8016 9559 15853 -85 747 432 C ATOM 1050 C THR A 164 20.905 -3.076 13.155 1.00 88.09 C ANISOU 1050 C THR A 164 7883 9554 16033 -154 685 444 C ATOM 1051 O THR A 164 20.128 -2.349 13.779 1.00 88.56 O ANISOU 1051 O THR A 164 7900 9532 16216 -173 822 511 O ATOM 1052 CB THR A 164 22.948 -3.329 14.667 1.00 87.08 C ANISOU 1052 CB THR A 164 8035 9588 15463 -35 804 424 C ATOM 1053 OG1 THR A 164 23.974 -2.998 13.729 1.00 86.11 O ANISOU 1053 OG1 THR A 164 7919 9644 15155 -32 633 344 O ATOM 1054 CG2 THR A 164 23.527 -4.148 15.817 1.00 87.28 C ANISOU 1054 CG2 THR A 164 8207 9586 15369 35 920 445 C ATOM 1055 N SER A 165 21.017 -3.043 11.810 1.00 87.97 N ANISOU 1055 N SER A 165 7797 9611 16016 -188 480 380 N ATOM 1056 CA SER A 165 20.225 -2.127 10.981 1.00 88.11 C ANISOU 1056 CA SER A 165 7683 9616 16178 -252 394 391 C ATOM 1057 C SER A 165 19.167 -2.811 10.116 1.00 89.18 C ANISOU 1057 C SER A 165 7688 9623 16574 -302 280 385 C ATOM 1058 O SER A 165 17.997 -2.437 10.195 1.00 89.98 O ANISOU 1058 O SER A 165 7669 9596 16923 -345 330 443 O ATOM 1059 CB SER A 165 21.129 -1.243 10.127 1.00 87.11 C ANISOU 1059 CB SER A 165 7580 9678 15839 -258 252 335 C ATOM 1060 OG SER A 165 21.789 -2.006 9.131 1.00 87.00 O ANISOU 1060 OG SER A 165 7591 9748 15717 -249 81 253 O ATOM 1061 N PHE A 166 19.574 -3.792 9.281 1.00 89.31 N ANISOU 1061 N PHE A 166 7724 9670 16539 -296 123 311 N ATOM 1062 CA PHE A 166 18.672 -4.511 8.376 1.00 90.39 C ANISOU 1062 CA PHE A 166 7751 9691 16902 -344 -16 289 C ATOM 1063 C PHE A 166 17.620 -5.358 9.091 1.00 91.63 C ANISOU 1063 C PHE A 166 7844 9637 17334 -359 107 351 C ATOM 1064 O PHE A 166 16.459 -5.327 8.685 1.00 92.62 O ANISOU 1064 O PHE A 166 7828 9634 17729 -417 61 380 O ATOM 1065 CB PHE A 166 19.450 -5.338 7.341 1.00 90.27 C ANISOU 1065 CB PHE A 166 7795 9764 16740 -326 -205 186 C ATOM 1066 CG PHE A 166 19.371 -4.808 5.928 1.00 90.20 C ANISOU 1066 CG PHE A 166 7731 9835 16706 -369 -419 132 C ATOM 1067 CD1 PHE A 166 18.387 -5.256 5.054 1.00 91.28 C ANISOU 1067 CD1 PHE A 166 7763 9856 17063 -422 -568 114 C ATOM 1068 CD2 PHE A 166 20.290 -3.874 5.465 1.00 89.14 C ANISOU 1068 CD2 PHE A 166 7654 9888 16327 -357 -475 102 C ATOM 1069 CE1 PHE A 166 18.318 -4.771 3.745 1.00 91.33 C ANISOU 1069 CE1 PHE A 166 7735 9936 17031 -459 -774 66 C ATOM 1070 CE2 PHE A 166 20.219 -3.387 4.156 1.00 89.17 C ANISOU 1070 CE2 PHE A 166 7620 9964 16296 -396 -667 59 C ATOM 1071 CZ PHE A 166 19.234 -3.841 3.304 1.00 90.28 C ANISOU 1071 CZ PHE A 166 7669 9991 16643 -444 -818 42 C ATOM 1072 N LEU A 167 18.012 -6.093 10.153 1.00 93.10 N ANISOU 1072 N LEU A 167 8131 9784 17458 -309 262 375 N ATOM 1073 CA LEU A 167 17.092 -6.933 10.927 1.00 94.36 C ANISOU 1073 CA LEU A 167 8247 9743 17862 -321 403 443 C ATOM 1074 C LEU A 167 15.970 -6.179 11.676 1.00 95.01 C ANISOU 1074 C LEU A 167 8228 9705 18167 -354 582 544 C ATOM 1075 O LEU A 167 14.817 -6.559 11.478 1.00 96.23 O ANISOU 1075 O LEU A 167 8243 9698 18622 -406 577 579 O ATOM 1076 CB LEU A 167 17.822 -7.938 11.838 1.00 94.39 C ANISOU 1076 CB LEU A 167 8398 9734 17733 -256 517 448 C ATOM 1077 CG LEU A 167 18.287 -9.237 11.175 1.00 94.63 C ANISOU 1077 CG LEU A 167 8472 9758 17725 -238 367 369 C ATOM 1078 CD1 LEU A 167 19.391 -9.886 11.976 1.00 94.54 C ANISOU 1078 CD1 LEU A 167 8630 9802 17489 -157 450 361 C ATOM 1079 CD2 LEU A 167 17.133 -10.220 10.995 1.00 96.04 C ANISOU 1079 CD2 LEU A 167 8542 9727 18222 -290 349 393 C ATOM 1080 N PRO A 168 16.220 -5.105 12.480 1.00 95.83 N ANISOU 1080 N PRO A 168 8385 9875 18151 -328 733 589 N ATOM 1081 CA PRO A 168 15.096 -4.430 13.161 1.00 96.63 C ANISOU 1081 CA PRO A 168 8385 9850 18480 -355 909 679 C ATOM 1082 C PRO A 168 14.107 -3.688 12.254 1.00 97.05 C ANISOU 1082 C PRO A 168 8252 9858 18764 -420 793 686 C ATOM 1083 O PRO A 168 12.990 -3.410 12.695 1.00 98.04 O ANISOU 1083 O PRO A 168 8259 9842 19150 -447 924 759 O ATOM 1084 CB PRO A 168 15.789 -3.484 14.152 1.00 95.78 C ANISOU 1084 CB PRO A 168 8406 9843 18142 -304 1070 705 C ATOM 1085 CG PRO A 168 17.204 -3.959 14.234 1.00 94.81 C ANISOU 1085 CG PRO A 168 8455 9864 17705 -247 1011 643 C ATOM 1086 CD PRO A 168 17.503 -4.489 12.873 1.00 94.52 C ANISOU 1086 CD PRO A 168 8372 9889 17652 -271 760 559 C ATOM 1087 N ILE A 169 14.501 -3.378 10.999 1.00 98.27 N ANISOU 1087 N ILE A 169 8382 10128 18828 -441 551 612 N ATOM 1088 CA ILE A 169 13.642 -2.685 10.030 1.00 98.66 C ANISOU 1088 CA ILE A 169 8270 10144 19072 -500 405 614 C ATOM 1089 C ILE A 169 12.831 -3.686 9.187 1.00 99.87 C ANISOU 1089 C ILE A 169 8301 10170 19475 -552 246 591 C ATOM 1090 O ILE A 169 11.606 -3.561 9.121 1.00101.05 O ANISOU 1090 O ILE A 169 8285 10170 19939 -599 261 644 O ATOM 1091 CB ILE A 169 14.410 -1.619 9.184 1.00 97.39 C ANISOU 1091 CB ILE A 169 8151 10170 18683 -499 247 562 C ATOM 1092 CG1 ILE A 169 15.108 -0.579 10.101 1.00 96.37 C ANISOU 1092 CG1 ILE A 169 8128 10145 18343 -456 413 590 C ATOM 1093 CG2 ILE A 169 13.472 -0.921 8.175 1.00 97.92 C ANISOU 1093 CG2 ILE A 169 8055 10192 18959 -559 87 573 C ATOM 1094 CD1 ILE A 169 16.200 0.283 9.443 1.00 95.03 C ANISOU 1094 CD1 ILE A 169 8042 10178 17887 -446 282 535 C ATOM 1095 N GLN A 170 13.509 -4.678 8.560 1.00102.06 N ANISOU 1095 N GLN A 170 8659 10500 19620 -541 96 511 N ATOM 1096 CA GLN A 170 12.867 -5.715 7.737 1.00103.20 C ANISOU 1096 CA GLN A 170 8714 10527 19971 -586 -72 474 C ATOM 1097 C GLN A 170 11.971 -6.616 8.594 1.00104.59 C ANISOU 1097 C GLN A 170 8818 10496 20426 -603 92 542 C ATOM 1098 O GLN A 170 10.820 -6.857 8.224 1.00105.97 O ANISOU 1098 O GLN A 170 8828 10516 20920 -663 31 568 O ATOM 1099 CB GLN A 170 13.904 -6.544 6.953 1.00102.60 C ANISOU 1099 CB GLN A 170 8763 10561 19660 -559 -248 366 C ATOM 1100 CG GLN A 170 14.651 -5.765 5.867 1.00101.57 C ANISOU 1100 CG GLN A 170 8682 10620 19291 -555 -438 295 C ATOM 1101 CD GLN A 170 13.894 -5.698 4.564 1.00102.44 C ANISOU 1101 CD GLN A 170 8678 10685 19560 -617 -681 259 C ATOM 1102 OE1 GLN A 170 12.933 -4.937 4.408 1.00103.20 O ANISOU 1102 OE1 GLN A 170 8636 10709 19866 -662 -701 314 O ATOM 1103 NE2 GLN A 170 14.337 -6.472 3.585 1.00102.42 N ANISOU 1103 NE2 GLN A 170 8735 10727 19452 -614 -876 162 N ATOM 1104 N MET A 171 12.490 -7.084 9.749 1.00108.36 N ANISOU 1104 N MET A 171 9418 10967 20788 -552 302 577 N ATOM 1105 CA MET A 171 11.743 -7.900 10.709 1.00109.64 C ANISOU 1105 CA MET A 171 9539 10939 21180 -562 496 655 C ATOM 1106 C MET A 171 11.219 -6.921 11.770 1.00109.76 C ANISOU 1106 C MET A 171 9516 10917 21271 -553 744 754 C ATOM 1107 O MET A 171 11.809 -6.772 12.844 1.00109.39 O ANISOU 1107 O MET A 171 9608 10921 21034 -496 938 788 O ATOM 1108 CB MET A 171 12.621 -9.017 11.324 1.00109.33 C ANISOU 1108 CB MET A 171 9670 10911 20960 -507 571 638 C ATOM 1109 CG MET A 171 13.354 -9.879 10.302 1.00109.19 C ANISOU 1109 CG MET A 171 9720 10963 20805 -497 335 527 C ATOM 1110 SD MET A 171 12.279 -10.970 9.339 1.00110.95 S ANISOU 1110 SD MET A 171 9788 10999 21369 -575 143 493 S ATOM 1111 CE MET A 171 13.478 -11.722 8.266 1.00110.31 C ANISOU 1111 CE MET A 171 9846 11055 21012 -536 -102 350 C ATOM 1112 N HIS A 172 10.139 -6.205 11.402 1.00113.06 N ANISOU 1112 N HIS A 172 9749 11252 21957 -606 719 792 N ATOM 1113 CA HIS A 172 9.427 -5.144 12.131 1.00113.24 C ANISOU 1113 CA HIS A 172 9689 11224 22113 -606 915 876 C ATOM 1114 C HIS A 172 9.543 -5.099 13.659 1.00113.50 C ANISOU 1114 C HIS A 172 9827 11218 22080 -557 1235 954 C ATOM 1115 O HIS A 172 9.052 -5.991 14.354 1.00114.82 O ANISOU 1115 O HIS A 172 9980 11237 22409 -564 1391 1011 O ATOM 1116 CB HIS A 172 7.963 -5.038 11.670 1.00114.68 C ANISOU 1116 CB HIS A 172 9625 11238 22710 -677 868 920 C ATOM 1117 CG HIS A 172 7.798 -5.043 10.182 1.00115.00 C ANISOU 1117 CG HIS A 172 9571 11308 22816 -725 544 846 C ATOM 1118 ND1 HIS A 172 8.125 -3.939 9.416 1.00114.02 N ANISOU 1118 ND1 HIS A 172 9450 11325 22547 -723 384 805 N ATOM 1119 CD2 HIS A 172 7.358 -6.028 9.365 1.00116.32 C ANISOU 1119 CD2 HIS A 172 9651 11379 23166 -776 357 808 C ATOM 1120 CE1 HIS A 172 7.872 -4.285 8.164 1.00114.75 C ANISOU 1120 CE1 HIS A 172 9465 11406 22729 -769 108 745 C ATOM 1121 NE2 HIS A 172 7.407 -5.531 8.085 1.00116.13 N ANISOU 1121 NE2 HIS A 172 9583 11439 23102 -803 77 741 N ATOM 1122 N TRP A 173 10.201 -4.038 14.164 1.00114.27 N ANISOU 1122 N TRP A 173 10037 11446 21934 -508 1328 955 N ATOM 1123 CA TRP A 173 10.418 -3.741 15.584 1.00114.39 C ANISOU 1123 CA TRP A 173 10178 11453 21832 -454 1615 1018 C ATOM 1124 C TRP A 173 10.467 -2.221 15.818 1.00113.70 C ANISOU 1124 C TRP A 173 10094 11447 21659 -433 1682 1028 C ATOM 1125 O TRP A 173 10.360 -1.770 16.961 1.00113.69 O ANISOU 1125 O TRP A 173 10165 11414 21618 -395 1929 1084 O ATOM 1126 CB TRP A 173 11.704 -4.413 16.111 1.00113.58 C ANISOU 1126 CB TRP A 173 10304 11454 21397 -393 1640 984 C ATOM 1127 CG TRP A 173 11.573 -5.878 16.428 1.00114.48 C ANISOU 1127 CG TRP A 173 10448 11450 21600 -396 1686 1006 C ATOM 1128 CD1 TRP A 173 10.575 -6.479 17.138 1.00116.13 C ANISOU 1128 CD1 TRP A 173 10584 11465 22075 -418 1880 1094 C ATOM 1129 CD2 TRP A 173 12.531 -6.905 16.136 1.00113.83 C ANISOU 1129 CD2 TRP A 173 10490 11434 21326 -370 1554 944 C ATOM 1130 NE1 TRP A 173 10.819 -7.828 17.250 1.00116.54 N ANISOU 1130 NE1 TRP A 173 10703 11453 22124 -414 1863 1092 N ATOM 1131 CE2 TRP A 173 12.018 -8.115 16.652 1.00115.15 C ANISOU 1131 CE2 TRP A 173 10650 11433 21668 -381 1663 998 C ATOM 1132 CE3 TRP A 173 13.770 -6.924 15.472 1.00112.34 C ANISOU 1132 CE3 TRP A 173 10412 11427 20845 -337 1358 848 C ATOM 1133 CZ2 TRP A 173 12.697 -9.333 16.519 1.00115.01 C ANISOU 1133 CZ2 TRP A 173 10737 11419 21542 -358 1573 957 C ATOM 1134 CZ3 TRP A 173 14.438 -8.131 15.336 1.00112.22 C ANISOU 1134 CZ3 TRP A 173 10494 11419 20726 -312 1274 804 C ATOM 1135 CH2 TRP A 173 13.904 -9.317 15.858 1.00113.54 C ANISOU 1135 CH2 TRP A 173 10656 11413 21070 -321 1378 858 C ATOM 1136 N TYR A 174 10.621 -1.442 14.727 1.00114.34 N ANISOU 1136 N TYR A 174 10105 11628 21711 -459 1462 974 N ATOM 1137 CA TYR A 174 10.695 0.022 14.734 1.00113.68 C ANISOU 1137 CA TYR A 174 10014 11624 21555 -448 1478 975 C ATOM 1138 C TYR A 174 9.314 0.695 14.716 1.00115.00 C ANISOU 1138 C TYR A 174 9975 11646 22074 -482 1552 1039 C ATOM 1139 O TYR A 174 9.208 1.860 15.104 1.00114.90 O ANISOU 1139 O TYR A 174 9963 11655 22039 -461 1655 1062 O ATOM 1140 CB TYR A 174 11.568 0.525 13.561 1.00112.30 C ANISOU 1140 CB TYR A 174 9874 11629 21166 -458 1206 893 C ATOM 1141 CG TYR A 174 10.901 0.475 12.200 1.00112.86 C ANISOU 1141 CG TYR A 174 9772 11664 21445 -519 961 868 C ATOM 1142 CD1 TYR A 174 10.373 1.624 11.618 1.00112.96 C ANISOU 1142 CD1 TYR A 174 9667 11681 21572 -546 876 881 C ATOM 1143 CD2 TYR A 174 10.819 -0.716 11.483 1.00113.32 C ANISOU 1143 CD2 TYR A 174 9795 11683 21578 -549 802 830 C ATOM 1144 CE1 TYR A 174 9.760 1.586 10.366 1.00113.59 C ANISOU 1144 CE1 TYR A 174 9597 11726 21836 -600 637 861 C ATOM 1145 CE2 TYR A 174 10.206 -0.767 10.232 1.00113.96 C ANISOU 1145 CE2 TYR A 174 9730 11729 21841 -605 564 802 C ATOM 1146 CZ TYR A 174 9.680 0.388 9.676 1.00114.11 C ANISOU 1146 CZ TYR A 174 9635 11754 21967 -630 479 820 C ATOM 1147 OH TYR A 174 9.080 0.344 8.440 1.00114.84 O ANISOU 1147 OH TYR A 174 9593 11811 22230 -684 230 796 O ATOM 1148 N ARG A 175 8.272 -0.031 14.248 1.00118.16 N ANISOU 1148 N ARG A 175 10195 11897 22803 -534 1493 1065 N ATOM 1149 CA ARG A 175 6.884 0.437 14.120 1.00119.66 C ANISOU 1149 CA ARG A 175 10157 11933 23376 -572 1537 1125 C ATOM 1150 C ARG A 175 6.315 0.949 15.448 1.00120.51 C ANISOU 1150 C ARG A 175 10261 11940 23587 -536 1872 1206 C ATOM 1151 O ARG A 175 6.390 0.249 16.460 1.00121.16 O ANISOU 1151 O ARG A 175 10437 11962 23636 -510 2088 1245 O ATOM 1152 CB ARG A 175 5.970 -0.667 13.538 1.00121.13 C ANISOU 1152 CB ARG A 175 10170 11967 23887 -634 1432 1137 C ATOM 1153 CG ARG A 175 6.475 -1.353 12.261 1.00120.54 C ANISOU 1153 CG ARG A 175 10112 11970 23717 -668 1111 1052 C ATOM 1154 CD ARG A 175 6.107 -0.614 10.986 1.00120.57 C ANISOU 1154 CD ARG A 175 9984 12009 23818 -708 843 1018 C ATOM 1155 NE ARG A 175 5.672 -1.537 9.935 1.00121.12 N ANISOU 1155 NE ARG A 175 9949 12012 24059 -766 598 978 N ATOM 1156 CZ ARG A 175 5.781 -1.303 8.631 1.00120.91 C ANISOU 1156 CZ ARG A 175 9884 12056 24000 -797 300 917 C ATOM 1157 NH1 ARG A 175 6.332 -0.177 8.194 1.00120.08 N ANISOU 1157 NH1 ARG A 175 9834 12094 23697 -778 210 895 N ATOM 1158 NH2 ARG A 175 5.351 -2.199 7.753 1.00121.60 N ANISOU 1158 NH2 ARG A 175 9887 12068 24247 -848 87 878 N ATOM 1159 N ALA A 176 5.769 2.180 15.440 1.00123.27 N ANISOU 1159 N ALA A 176 10512 12273 24053 -530 1914 1230 N ATOM 1160 CA ALA A 176 5.190 2.823 16.623 1.00124.15 C ANISOU 1160 CA ALA A 176 10613 12291 24267 -491 2227 1299 C ATOM 1161 C ALA A 176 3.714 2.465 16.813 1.00126.30 C ANISOU 1161 C ALA A 176 10652 12348 24989 -525 2359 1377 C ATOM 1162 O ALA A 176 2.990 2.276 15.833 1.00126.98 O ANISOU 1162 O ALA A 176 10535 12366 25346 -582 2163 1375 O ATOM 1163 CB ALA A 176 5.369 4.329 16.544 1.00123.43 C ANISOU 1163 CB ALA A 176 10537 12281 24080 -463 2213 1283 C ATOM 1164 N THR A 177 3.280 2.375 18.083 1.00128.90 N ANISOU 1164 N THR A 177 11012 12570 25394 -491 2693 1446 N ATOM 1165 CA THR A 177 1.918 2.005 18.490 1.00131.10 C ANISOU 1165 CA THR A 177 11083 12639 26090 -517 2885 1530 C ATOM 1166 C THR A 177 0.819 3.035 18.187 1.00132.33 C ANISOU 1166 C THR A 177 11002 12700 26577 -527 2898 1564 C ATOM 1167 O THR A 177 -0.334 2.637 18.009 1.00134.17 O ANISOU 1167 O THR A 177 11001 12768 27210 -570 2929 1618 O ATOM 1168 CB THR A 177 1.888 1.534 19.954 1.00131.98 C ANISOU 1168 CB THR A 177 11328 12674 26144 -474 3247 1595 C ATOM 1169 OG1 THR A 177 2.547 2.496 20.780 1.00131.01 O ANISOU 1169 OG1 THR A 177 11403 12648 25727 -401 3410 1581 O ATOM 1170 CG2 THR A 177 2.518 0.158 20.142 1.00131.81 C ANISOU 1170 CG2 THR A 177 11449 12666 25967 -485 3227 1589 C ATOM 1171 N HIS A 178 1.159 4.341 18.147 1.00132.06 N ANISOU 1171 N HIS A 178 11022 12761 26393 -486 2876 1534 N ATOM 1172 CA HIS A 178 0.185 5.411 17.890 1.00133.20 C ANISOU 1172 CA HIS A 178 10957 12820 26833 -484 2889 1564 C ATOM 1173 C HIS A 178 -0.341 5.454 16.450 1.00133.39 C ANISOU 1173 C HIS A 178 10761 12825 27096 -548 2549 1544 C ATOM 1174 O HIS A 178 0.389 5.115 15.516 1.00132.02 O ANISOU 1174 O HIS A 178 10658 12771 26732 -579 2261 1481 O ATOM 1175 CB HIS A 178 0.699 6.782 18.365 1.00132.54 C ANISOU 1175 CB HIS A 178 11009 12829 26521 -419 2987 1541 C ATOM 1176 CG HIS A 178 1.936 7.255 17.669 1.00130.43 C ANISOU 1176 CG HIS A 178 10908 12763 25886 -417 2729 1461 C ATOM 1177 ND1 HIS A 178 1.877 8.185 16.648 1.00130.19 N ANISOU 1177 ND1 HIS A 178 10781 12783 25902 -433 2491 1433 N ATOM 1178 CD2 HIS A 178 3.231 6.927 17.887 1.00128.61 C ANISOU 1178 CD2 HIS A 178 10927 12687 25252 -398 2687 1408 C ATOM 1179 CE1 HIS A 178 3.129 8.386 16.273 1.00128.28 C ANISOU 1179 CE1 HIS A 178 10731 12725 25284 -428 2322 1367 C ATOM 1180 NE2 HIS A 178 3.979 7.648 16.986 1.00127.28 N ANISOU 1180 NE2 HIS A 178 10810 12667 24884 -407 2429 1347 N ATOM 1181 N GLN A 179 -1.619 5.867 16.291 1.00134.98 N ANISOU 1181 N GLN A 179 10698 12871 27718 -564 2589 1599 N ATOM 1182 CA GLN A 179 -2.359 5.961 15.024 1.00135.68 C ANISOU 1182 CA GLN A 179 10545 12903 28104 -621 2290 1595 C ATOM 1183 C GLN A 179 -1.690 6.834 13.952 1.00134.04 C ANISOU 1183 C GLN A 179 10398 12850 27682 -623 1976 1531 C ATOM 1184 O GLN A 179 -1.748 6.484 12.771 1.00133.66 O ANISOU 1184 O GLN A 179 10269 12823 27693 -677 1658 1499 O ATOM 1185 CB GLN A 179 -3.816 6.405 15.280 1.00137.94 C ANISOU 1185 CB GLN A 179 10547 12993 28871 -620 2444 1672 C ATOM 1186 CG GLN A 179 -4.788 6.192 14.110 1.00139.07 C ANISOU 1186 CG GLN A 179 10405 13032 29403 -688 2161 1683 C ATOM 1187 CD GLN A 179 -4.981 4.739 13.738 1.00139.95 C ANISOU 1187 CD GLN A 179 10455 13079 29640 -759 2045 1680 C ATOM 1188 OE1 GLN A 179 -5.504 3.933 14.515 1.00141.38 O ANISOU 1188 OE1 GLN A 179 10574 13132 30012 -772 2282 1735 O ATOM 1189 NE2 GLN A 179 -4.582 4.382 12.527 1.00139.29 N ANISOU 1189 NE2 GLN A 179 10388 13077 29459 -808 1677 1618 N ATOM 1190 N GLU A 180 -1.052 7.952 14.364 1.00132.09 N ANISOU 1190 N GLU A 180 10301 12705 27183 -564 2065 1513 N ATOM 1191 CA GLU A 180 -0.352 8.896 13.481 1.00130.59 C ANISOU 1191 CA GLU A 180 10189 12663 26766 -562 1809 1462 C ATOM 1192 C GLU A 180 0.760 8.207 12.668 1.00128.86 C ANISOU 1192 C GLU A 180 10132 12607 26222 -596 1547 1390 C ATOM 1193 O GLU A 180 0.982 8.567 11.511 1.00128.25 O ANISOU 1193 O GLU A 180 10032 12608 26089 -625 1249 1355 O ATOM 1194 CB GLU A 180 0.221 10.064 14.300 1.00129.80 C ANISOU 1194 CB GLU A 180 10251 12636 26431 -493 2003 1455 C ATOM 1195 CG GLU A 180 0.531 11.310 13.488 1.00128.59 C ANISOU 1195 CG GLU A 180 10106 12574 26178 -488 1789 1429 C ATOM 1196 CD GLU A 180 1.339 12.354 14.232 1.00127.48 C ANISOU 1196 CD GLU A 180 10169 12531 25737 -429 1942 1405 C ATOM 1197 OE1 GLU A 180 2.525 12.547 13.880 1.00125.98 O ANISOU 1197 OE1 GLU A 180 10165 12513 25189 -434 1791 1350 O ATOM 1198 OE2 GLU A 180 0.793 12.974 15.173 1.00128.19 O ANISOU 1198 OE2 GLU A 180 10233 12523 25951 -378 2214 1440 O ATOM 1199 N ALA A 181 1.434 7.211 13.276 1.00125.53 N ANISOU 1199 N ALA A 181 9873 12229 25594 -590 1663 1370 N ATOM 1200 CA ALA A 181 2.505 6.430 12.656 1.00124.05 C ANISOU 1200 CA ALA A 181 9845 12186 25102 -613 1458 1302 C ATOM 1201 C ALA A 181 1.957 5.342 11.730 1.00124.95 C ANISOU 1201 C ALA A 181 9815 12225 25436 -678 1239 1292 C ATOM 1202 O ALA A 181 2.510 5.143 10.648 1.00124.12 O ANISOU 1202 O ALA A 181 9756 12225 25178 -708 951 1232 O ATOM 1203 CB ALA A 181 3.381 5.808 13.728 1.00123.30 C ANISOU 1203 CB ALA A 181 9972 12151 24725 -573 1675 1290 C ATOM 1204 N ILE A 182 0.874 4.646 12.158 1.00124.82 N ANISOU 1204 N ILE A 182 9626 12023 25777 -701 1378 1350 N ATOM 1205 CA ILE A 182 0.202 3.558 11.426 1.00126.01 C ANISOU 1205 CA ILE A 182 9619 12066 26193 -768 1200 1348 C ATOM 1206 C ILE A 182 -0.286 4.019 10.039 1.00126.51 C ANISOU 1206 C ILE A 182 9522 12125 26420 -812 860 1326 C ATOM 1207 O ILE A 182 -0.155 3.268 9.069 1.00126.50 O ANISOU 1207 O ILE A 182 9514 12146 26404 -860 593 1275 O ATOM 1208 CB ILE A 182 -0.915 2.882 12.286 1.00127.99 C ANISOU 1208 CB ILE A 182 9703 12107 26820 -783 1456 1427 C ATOM 1209 CG1 ILE A 182 -0.351 2.377 13.638 1.00127.46 C ANISOU 1209 CG1 ILE A 182 9827 12052 26550 -738 1782 1451 C ATOM 1210 CG2 ILE A 182 -1.611 1.734 11.527 1.00129.26 C ANISOU 1210 CG2 ILE A 182 9693 12146 27273 -859 1261 1424 C ATOM 1211 CD1 ILE A 182 -1.374 2.250 14.778 1.00129.29 C ANISOU 1211 CD1 ILE A 182 9932 12100 27093 -726 2132 1545 C ATOM 1212 N ASN A 183 -0.801 5.264 9.950 1.00128.80 N ANISOU 1212 N ASN A 183 9701 12390 26846 -792 866 1361 N ATOM 1213 CA ASN A 183 -1.286 5.879 8.709 1.00129.33 C ANISOU 1213 CA ASN A 183 9623 12450 27066 -825 557 1352 C ATOM 1214 C ASN A 183 -0.186 6.004 7.649 1.00127.58 C ANISOU 1214 C ASN A 183 9579 12420 26475 -835 262 1273 C ATOM 1215 O ASN A 183 -0.475 5.857 6.461 1.00128.04 O ANISOU 1215 O ASN A 183 9552 12472 26625 -881 -47 1247 O ATOM 1216 CB ASN A 183 -1.916 7.247 8.987 1.00129.98 C ANISOU 1216 CB ASN A 183 9587 12477 27323 -787 660 1407 C ATOM 1217 CG ASN A 183 -3.163 7.202 9.839 1.00131.92 C ANISOU 1217 CG ASN A 183 9615 12520 27989 -779 922 1487 C ATOM 1218 OD1 ASN A 183 -4.137 6.500 9.539 1.00133.68 O ANISOU 1218 OD1 ASN A 183 9625 12593 28574 -828 856 1515 O ATOM 1219 ND2 ASN A 183 -3.177 7.991 10.902 1.00131.75 N ANISOU 1219 ND2 ASN A 183 9637 12485 27938 -717 1223 1523 N ATOM 1220 N CYS A 184 1.068 6.259 8.078 1.00127.87 N ANISOU 1220 N CYS A 184 9863 12625 26097 -793 357 1235 N ATOM 1221 CA CYS A 184 2.218 6.386 7.182 1.00126.15 C ANISOU 1221 CA CYS A 184 9825 12599 25507 -798 119 1162 C ATOM 1222 C CYS A 184 2.680 5.037 6.626 1.00125.76 C ANISOU 1222 C CYS A 184 9851 12589 25343 -833 -39 1099 C ATOM 1223 O CYS A 184 3.029 4.963 5.446 1.00125.37 O ANISOU 1223 O CYS A 184 9838 12624 25173 -861 -329 1045 O ATOM 1224 CB CYS A 184 3.363 7.144 7.848 1.00124.45 C ANISOU 1224 CB CYS A 184 9827 12539 24919 -744 275 1145 C ATOM 1225 SG CYS A 184 4.734 7.545 6.731 1.00122.53 S ANISOU 1225 SG CYS A 184 9781 12531 24244 -750 -1 1068 S ATOM 1226 N TYR A 185 2.688 3.978 7.469 1.00125.21 N ANISOU 1226 N TYR A 185 9813 12454 25307 -828 154 1104 N ATOM 1227 CA TYR A 185 3.089 2.625 7.058 1.00125.01 C ANISOU 1227 CA TYR A 185 9858 12445 25196 -856 29 1046 C ATOM 1228 C TYR A 185 2.067 2.036 6.079 1.00126.67 C ANISOU 1228 C TYR A 185 9869 12521 25738 -922 -213 1041 C ATOM 1229 O TYR A 185 2.452 1.332 5.145 1.00126.41 O ANISOU 1229 O TYR A 185 9896 12541 25594 -951 -458 971 O ATOM 1230 CB TYR A 185 3.259 1.675 8.266 1.00125.07 C ANISOU 1230 CB TYR A 185 9940 12395 25185 -834 306 1066 C ATOM 1231 CG TYR A 185 4.019 2.225 9.457 1.00124.02 C ANISOU 1231 CG TYR A 185 9976 12348 24797 -768 587 1087 C ATOM 1232 CD1 TYR A 185 5.276 2.805 9.304 1.00122.17 C ANISOU 1232 CD1 TYR A 185 9941 12313 24165 -732 531 1035 C ATOM 1233 CD2 TYR A 185 3.529 2.069 10.751 1.00124.91 C ANISOU 1233 CD2 TYR A 185 10062 12343 25055 -744 907 1156 C ATOM 1234 CE1 TYR A 185 5.990 3.286 10.401 1.00121.30 C ANISOU 1234 CE1 TYR A 185 9990 12277 23821 -675 772 1049 C ATOM 1235 CE2 TYR A 185 4.233 2.545 11.855 1.00124.06 C ANISOU 1235 CE2 TYR A 185 10126 12311 24699 -682 1155 1171 C ATOM 1236 CZ TYR A 185 5.466 3.150 11.676 1.00122.24 C ANISOU 1236 CZ TYR A 185 10087 12276 24083 -648 1078 1114 C ATOM 1237 OH TYR A 185 6.165 3.613 12.764 1.00121.50 O ANISOU 1237 OH TYR A 185 10164 12252 23748 -590 1306 1124 O ATOM 1238 N ALA A 186 0.770 2.335 6.299 1.00128.05 N ANISOU 1238 N ALA A 186 9809 12520 26324 -943 -147 1114 N ATOM 1239 CA ALA A 186 -0.344 1.876 5.468 1.00129.93 C ANISOU 1239 CA ALA A 186 9825 12607 26935 -1007 -366 1121 C ATOM 1240 C ALA A 186 -0.363 2.554 4.097 1.00129.90 C ANISOU 1240 C ALA A 186 9793 12673 26890 -1029 -714 1085 C ATOM 1241 O ALA A 186 -0.701 1.907 3.105 1.00130.73 O ANISOU 1241 O ALA A 186 9831 12730 27110 -1081 -989 1043 O ATOM 1242 CB ALA A 186 -1.664 2.107 6.187 1.00131.78 C ANISOU 1242 CB ALA A 186 9814 12642 27615 -1016 -166 1215 C ATOM 1243 N GLU A 187 0.003 3.850 4.044 1.00130.82 N ANISOU 1243 N GLU A 187 9969 12897 26840 -991 -705 1100 N ATOM 1244 CA GLU A 187 0.037 4.641 2.814 1.00130.78 C ANISOU 1244 CA GLU A 187 9957 12964 26770 -1005 -1012 1079 C ATOM 1245 C GLU A 187 1.265 4.305 1.966 1.00129.41 C ANISOU 1245 C GLU A 187 10012 12978 26180 -1008 -1217 988 C ATOM 1246 O GLU A 187 2.375 4.197 2.495 1.00127.72 O ANISOU 1246 O GLU A 187 9998 12899 25631 -971 -1070 956 O ATOM 1247 CB GLU A 187 -0.013 6.146 3.141 1.00130.28 C ANISOU 1247 CB GLU A 187 9877 12937 26687 -962 -905 1135 C ATOM 1248 CG GLU A 187 -0.407 7.039 1.974 1.00130.84 C ANISOU 1248 CG GLU A 187 9867 13016 26830 -981 -1201 1146 C ATOM 1249 CD GLU A 187 -1.849 6.929 1.520 1.00133.11 C ANISOU 1249 CD GLU A 187 9878 13108 27589 -1021 -1350 1190 C ATOM 1250 OE1 GLU A 187 -2.744 7.405 2.255 1.00134.50 O ANISOU 1250 OE1 GLU A 187 9872 13146 28086 -1003 -1160 1263 O ATOM 1251 OE2 GLU A 187 -2.083 6.382 0.418 1.00133.59 O ANISOU 1251 OE2 GLU A 187 9906 13153 27699 -1069 -1662 1150 O ATOM 1252 N GLU A 188 1.056 4.149 0.646 1.00131.76 N ANISOU 1252 N GLU A 188 10279 13281 26503 -1050 -1558 948 N ATOM 1253 CA GLU A 188 2.109 3.845 -0.329 1.00130.84 C ANISOU 1253 CA GLU A 188 10365 13332 26016 -1055 -1780 860 C ATOM 1254 C GLU A 188 2.945 5.082 -0.697 1.00129.51 C ANISOU 1254 C GLU A 188 10337 13339 25531 -1024 -1827 862 C ATOM 1255 O GLU A 188 4.059 4.935 -1.206 1.00128.67 O ANISOU 1255 O GLU A 188 10429 13400 25060 -1014 -1920 796 O ATOM 1256 CB GLU A 188 1.531 3.149 -1.582 1.00132.50 C ANISOU 1256 CB GLU A 188 10500 13470 26374 -1111 -2124 812 C ATOM 1257 CG GLU A 188 0.506 3.961 -2.362 1.00134.11 C ANISOU 1257 CG GLU A 188 10529 13584 26843 -1139 -2349 860 C ATOM 1258 CD GLU A 188 -0.150 3.231 -3.518 1.00135.68 C ANISOU 1258 CD GLU A 188 10646 13692 27214 -1196 -2691 814 C ATOM 1259 OE1 GLU A 188 0.567 2.858 -4.475 1.00135.27 O ANISOU 1259 OE1 GLU A 188 10765 13756 26875 -1205 -2907 730 O ATOM 1260 OE2 GLU A 188 -1.390 3.060 -3.482 1.00137.39 O ANISOU 1260 OE2 GLU A 188 10625 13720 27856 -1231 -2747 859 O ATOM 1261 N THR A 189 2.406 6.290 -0.433 1.00128.92 N ANISOU 1261 N THR A 189 10157 13221 25606 -1008 -1755 939 N ATOM 1262 CA THR A 189 3.066 7.571 -0.716 1.00127.78 C ANISOU 1262 CA THR A 189 10122 13216 25212 -982 -1785 956 C ATOM 1263 C THR A 189 3.781 8.177 0.509 1.00126.29 C ANISOU 1263 C THR A 189 10037 13103 24844 -930 -1464 980 C ATOM 1264 O THR A 189 4.383 9.247 0.395 1.00125.16 O ANISOU 1264 O THR A 189 9991 13073 24492 -910 -1463 994 O ATOM 1265 CB THR A 189 2.104 8.553 -1.416 1.00129.13 C ANISOU 1265 CB THR A 189 10133 13300 25631 -998 -1975 1016 C ATOM 1266 OG1 THR A 189 0.922 8.711 -0.632 1.00130.35 O ANISOU 1266 OG1 THR A 189 10063 13267 26197 -992 -1814 1087 O ATOM 1267 CG2 THR A 189 1.746 8.119 -2.834 1.00130.44 C ANISOU 1267 CG2 THR A 189 10269 13446 25846 -1046 -2346 979 C ATOM 1268 N CYS A 190 3.733 7.487 1.667 1.00124.74 N ANISOU 1268 N CYS A 190 9831 12843 24722 -911 -1198 985 N ATOM 1269 CA CYS A 190 4.380 7.942 2.899 1.00123.50 C ANISOU 1269 CA CYS A 190 9781 12746 24397 -860 -892 1004 C ATOM 1270 C CYS A 190 5.547 7.032 3.276 1.00122.14 C ANISOU 1270 C CYS A 190 9807 12696 23904 -843 -803 938 C ATOM 1271 O CYS A 190 5.377 5.812 3.362 1.00122.64 O ANISOU 1271 O CYS A 190 9852 12698 24048 -859 -802 910 O ATOM 1272 CB CYS A 190 3.371 8.065 4.037 1.00124.59 C ANISOU 1272 CB CYS A 190 9758 12711 24869 -842 -629 1074 C ATOM 1273 SG CYS A 190 3.986 8.968 5.484 1.00123.36 S ANISOU 1273 SG CYS A 190 9726 12612 24533 -776 -273 1104 S ATOM 1274 N CYS A 191 6.730 7.632 3.493 1.00118.30 N ANISOU 1274 N CYS A 191 9505 12378 23065 -811 -735 915 N ATOM 1275 CA CYS A 191 7.957 6.923 3.864 1.00116.89 C ANISOU 1275 CA CYS A 191 9521 12332 22560 -787 -653 854 C ATOM 1276 C CYS A 191 8.698 7.645 5.015 1.00115.70 C ANISOU 1276 C CYS A 191 9492 12258 22212 -738 -397 872 C ATOM 1277 O CYS A 191 9.930 7.602 5.097 1.00114.37 O ANISOU 1277 O CYS A 191 9500 12247 21708 -717 -381 825 O ATOM 1278 CB CYS A 191 8.847 6.718 2.637 1.00116.14 C ANISOU 1278 CB CYS A 191 9548 12394 22186 -806 -909 783 C ATOM 1279 SG CYS A 191 10.012 5.332 2.774 1.00115.08 S ANISOU 1279 SG CYS A 191 9590 12368 21767 -786 -882 695 S ATOM 1280 N ASP A 192 7.929 8.290 5.919 1.00113.46 N ANISOU 1280 N ASP A 192 9110 11855 22145 -719 -196 939 N ATOM 1281 CA ASP A 192 8.464 9.001 7.084 1.00112.63 C ANISOU 1281 CA ASP A 192 9112 11794 21889 -671 55 957 C ATOM 1282 C ASP A 192 8.892 7.996 8.152 1.00112.24 C ANISOU 1282 C ASP A 192 9164 11738 21744 -640 265 940 C ATOM 1283 O ASP A 192 8.129 7.083 8.478 1.00113.24 O ANISOU 1283 O ASP A 192 9195 11731 22100 -649 339 961 O ATOM 1284 CB ASP A 192 7.436 10.001 7.649 1.00113.69 C ANISOU 1284 CB ASP A 192 9107 11791 22298 -656 198 1029 C ATOM 1285 CG ASP A 192 6.981 11.083 6.682 1.00114.32 C ANISOU 1285 CG ASP A 192 9085 11863 22489 -679 2 1055 C ATOM 1286 OD1 ASP A 192 7.815 11.550 5.873 1.00113.53 O ANISOU 1286 OD1 ASP A 192 9087 11907 22142 -694 -180 1023 O ATOM 1287 OD2 ASP A 192 5.806 11.497 6.768 1.00115.68 O ANISOU 1287 OD2 ASP A 192 9076 11882 22995 -680 39 1112 O ATOM 1288 N PHE A 193 10.118 8.153 8.677 1.00110.60 N ANISOU 1288 N PHE A 193 9149 11673 21201 -606 352 905 N ATOM 1289 CA PHE A 193 10.685 7.249 9.676 1.00110.19 C ANISOU 1289 CA PHE A 193 9221 11634 21012 -571 533 888 C ATOM 1290 C PHE A 193 10.143 7.472 11.093 1.00110.86 C ANISOU 1290 C PHE A 193 9298 11601 21223 -533 837 945 C ATOM 1291 O PHE A 193 10.808 8.080 11.938 1.00110.13 O ANISOU 1291 O PHE A 193 9340 11574 20930 -492 989 942 O ATOM 1292 CB PHE A 193 12.227 7.250 9.613 1.00108.56 C ANISOU 1292 CB PHE A 193 9217 11626 20405 -549 483 825 C ATOM 1293 CG PHE A 193 12.939 6.094 10.286 1.00108.14 C ANISOU 1293 CG PHE A 193 9292 11606 20190 -518 581 793 C ATOM 1294 CD1 PHE A 193 12.487 4.787 10.128 1.00108.84 C ANISOU 1294 CD1 PHE A 193 9325 11604 20425 -532 551 787 C ATOM 1295 CD2 PHE A 193 14.106 6.303 11.010 1.00107.07 C ANISOU 1295 CD2 PHE A 193 9335 11594 19752 -475 682 767 C ATOM 1296 CE1 PHE A 193 13.162 3.718 10.727 1.00108.51 C ANISOU 1296 CE1 PHE A 193 9407 11588 20234 -500 633 761 C ATOM 1297 CE2 PHE A 193 14.785 5.232 11.602 1.00106.76 C ANISOU 1297 CE2 PHE A 193 9416 11584 19564 -442 756 740 C ATOM 1298 CZ PHE A 193 14.312 3.947 11.450 1.00107.44 C ANISOU 1298 CZ PHE A 193 9448 11576 19798 -453 732 738 C ATOM 1299 N PHE A 194 8.918 6.974 11.339 1.00109.91 N ANISOU 1299 N PHE A 194 9018 11301 21442 -547 924 995 N ATOM 1300 CA PHE A 194 8.251 7.042 12.639 1.00110.89 C ANISOU 1300 CA PHE A 194 9116 11292 21725 -513 1225 1054 C ATOM 1301 C PHE A 194 8.759 5.874 13.483 1.00110.64 C ANISOU 1301 C PHE A 194 9218 11261 21559 -488 1372 1046 C ATOM 1302 O PHE A 194 8.630 4.717 13.072 1.00110.82 O ANISOU 1302 O PHE A 194 9202 11248 21656 -515 1278 1032 O ATOM 1303 CB PHE A 194 6.723 6.979 12.475 1.00112.72 C ANISOU 1303 CB PHE A 194 9104 11330 22394 -543 1250 1115 C ATOM 1304 CG PHE A 194 6.036 8.315 12.319 1.00113.38 C ANISOU 1304 CG PHE A 194 9065 11363 22651 -539 1254 1152 C ATOM 1305 CD1 PHE A 194 5.545 8.996 13.426 1.00114.05 C ANISOU 1305 CD1 PHE A 194 9137 11357 22840 -495 1532 1200 C ATOM 1306 CD2 PHE A 194 5.852 8.878 11.061 1.00113.48 C ANISOU 1306 CD2 PHE A 194 8979 11410 22728 -576 982 1139 C ATOM 1307 CE1 PHE A 194 4.899 10.228 13.281 1.00114.76 C ANISOU 1307 CE1 PHE A 194 9111 11391 23102 -486 1537 1231 C ATOM 1308 CE2 PHE A 194 5.207 10.110 10.917 1.00114.19 C ANISOU 1308 CE2 PHE A 194 8955 11444 22988 -569 980 1177 C ATOM 1309 CZ PHE A 194 4.734 10.776 12.027 1.00114.81 C ANISOU 1309 CZ PHE A 194 9015 11431 23177 -523 1258 1221 C ATOM 1310 N THR A 195 9.387 6.178 14.631 1.00108.24 N ANISOU 1310 N THR A 195 9081 11001 21044 -435 1585 1050 N ATOM 1311 CA THR A 195 9.972 5.162 15.513 1.00108.02 C ANISOU 1311 CA THR A 195 9207 10984 20852 -402 1727 1046 C ATOM 1312 C THR A 195 9.450 5.220 16.943 1.00109.05 C ANISOU 1312 C THR A 195 9377 10994 21063 -360 2054 1109 C ATOM 1313 O THR A 195 9.184 6.306 17.461 1.00109.30 O ANISOU 1313 O THR A 195 9409 11004 21116 -334 2188 1131 O ATOM 1314 CB THR A 195 11.508 5.240 15.494 1.00106.29 C ANISOU 1314 CB THR A 195 9198 10961 20226 -374 1637 979 C ATOM 1315 OG1 THR A 195 11.925 6.565 15.830 1.00105.59 O ANISOU 1315 OG1 THR A 195 9184 10947 19988 -349 1689 972 O ATOM 1316 CG2 THR A 195 12.102 4.825 14.159 1.00105.49 C ANISOU 1316 CG2 THR A 195 9082 10974 20026 -411 1341 916 C ATOM 1317 N ASN A 196 9.336 4.041 17.587 1.00106.51 N ANISOU 1317 N ASN A 196 9100 10595 20774 -350 2186 1137 N ATOM 1318 CA ASN A 196 8.905 3.915 18.981 1.00107.60 C ANISOU 1318 CA ASN A 196 9303 10621 20960 -308 2509 1200 C ATOM 1319 C ASN A 196 10.046 4.330 19.919 1.00106.55 C ANISOU 1319 C ASN A 196 9425 10607 20452 -246 2618 1173 C ATOM 1320 O ASN A 196 11.210 4.305 19.511 1.00105.13 O ANISOU 1320 O ASN A 196 9367 10587 19990 -240 2443 1109 O ATOM 1321 CB ASN A 196 8.411 2.491 19.287 1.00108.72 C ANISOU 1321 CB ASN A 196 9409 10636 21264 -325 2599 1246 C ATOM 1322 CG ASN A 196 9.418 1.394 19.034 1.00107.78 C ANISOU 1322 CG ASN A 196 9424 10609 20918 -322 2459 1199 C ATOM 1323 OD1 ASN A 196 10.358 1.183 19.805 1.00106.94 O ANISOU 1323 OD1 ASN A 196 9530 10582 20520 -272 2543 1185 O ATOM 1324 ND2 ASN A 196 9.209 0.634 17.974 1.00108.07 N ANISOU 1324 ND2 ASN A 196 9340 10627 21095 -374 2244 1173 N ATOM 1325 N GLN A 197 9.709 4.710 21.168 1.00105.07 N ANISOU 1325 N GLN A 197 9316 10341 20264 -200 2906 1221 N ATOM 1326 CA GLN A 197 10.672 5.155 22.185 1.00104.33 C ANISOU 1326 CA GLN A 197 9470 10339 19832 -138 3028 1199 C ATOM 1327 C GLN A 197 11.752 4.126 22.548 1.00103.47 C ANISOU 1327 C GLN A 197 9556 10315 19443 -112 2994 1176 C ATOM 1328 O GLN A 197 12.869 4.522 22.883 1.00102.23 O ANISOU 1328 O GLN A 197 9583 10291 18968 -76 2954 1128 O ATOM 1329 CB GLN A 197 9.958 5.696 23.434 1.00105.65 C ANISOU 1329 CB GLN A 197 9679 10384 20079 -93 3353 1256 C ATOM 1330 CG GLN A 197 9.351 7.085 23.222 1.00105.87 C ANISOU 1330 CG GLN A 197 9590 10383 20252 -95 3374 1253 C ATOM 1331 CD GLN A 197 8.724 7.661 24.469 1.00107.17 C ANISOU 1331 CD GLN A 197 9812 10433 20475 -42 3700 1298 C ATOM 1332 OE1 GLN A 197 9.375 7.841 25.505 1.00107.19 O ANISOU 1332 OE1 GLN A 197 10043 10474 20209 13 3850 1287 O ATOM 1333 NE2 GLN A 197 7.453 8.019 24.376 1.00108.36 N ANISOU 1333 NE2 GLN A 197 9755 10441 20976 -56 3811 1347 N ATOM 1334 N ALA A 198 11.433 2.819 22.452 1.00100.24 N ANISOU 1334 N ALA A 198 9101 9825 19160 -132 2996 1208 N ATOM 1335 CA ALA A 198 12.370 1.728 22.741 1.00 99.61 C ANISOU 1335 CA ALA A 198 9189 9806 18853 -107 2956 1192 C ATOM 1336 C ALA A 198 13.452 1.604 21.658 1.00 97.95 C ANISOU 1336 C ALA A 198 8997 9767 18453 -123 2650 1105 C ATOM 1337 O ALA A 198 14.625 1.433 21.994 1.00 96.97 O ANISOU 1337 O ALA A 198 9057 9763 18024 -82 2604 1065 O ATOM 1338 CB ALA A 198 11.619 0.414 22.896 1.00100.89 C ANISOU 1338 CB ALA A 198 9279 9816 19239 -128 3048 1255 C ATOM 1339 N TYR A 199 13.058 1.701 20.368 1.00 94.15 N ANISOU 1339 N TYR A 199 8328 9295 18150 -181 2441 1076 N ATOM 1340 CA TYR A 199 13.974 1.619 19.227 1.00 92.78 C ANISOU 1340 CA TYR A 199 8157 9276 17819 -200 2155 995 C ATOM 1341 C TYR A 199 14.815 2.888 19.091 1.00 91.55 C ANISOU 1341 C TYR A 199 8079 9276 17430 -185 2077 946 C ATOM 1342 O TYR A 199 16.003 2.786 18.790 1.00 90.43 O ANISOU 1342 O TYR A 199 8047 9286 17026 -170 1934 885 O ATOM 1343 CB TYR A 199 13.215 1.309 17.919 1.00 93.14 C ANISOU 1343 CB TYR A 199 7989 9270 18130 -267 1962 984 C ATOM 1344 CG TYR A 199 14.095 1.240 16.686 1.00 91.88 C ANISOU 1344 CG TYR A 199 7834 9266 17810 -286 1674 901 C ATOM 1345 CD1 TYR A 199 14.832 0.097 16.393 1.00 91.58 C ANISOU 1345 CD1 TYR A 199 7874 9281 17641 -276 1563 857 C ATOM 1346 CD2 TYR A 199 14.173 2.312 15.802 1.00 91.14 C ANISOU 1346 CD2 TYR A 199 7669 9260 17700 -314 1518 868 C ATOM 1347 CE1 TYR A 199 15.644 0.029 15.262 1.00 90.57 C ANISOU 1347 CE1 TYR A 199 7755 9296 17362 -289 1314 777 C ATOM 1348 CE2 TYR A 199 14.981 2.256 14.666 1.00 90.11 C ANISOU 1348 CE2 TYR A 199 7551 9273 17414 -332 1267 795 C ATOM 1349 CZ TYR A 199 15.713 1.111 14.398 1.00 89.86 C ANISOU 1349 CZ TYR A 199 7597 9297 17249 -319 1170 748 C ATOM 1350 OH TYR A 199 16.506 1.050 13.278 1.00 89.00 O ANISOU 1350 OH TYR A 199 7503 9329 16984 -332 939 674 O ATOM 1351 N ALA A 200 14.202 4.074 19.307 1.00 90.48 N ANISOU 1351 N ALA A 200 7882 9098 17399 -190 2173 972 N ATOM 1352 CA ALA A 200 14.855 5.387 19.216 1.00 89.55 C ANISOU 1352 CA ALA A 200 7826 9102 17097 -181 2116 932 C ATOM 1353 C ALA A 200 16.067 5.526 20.147 1.00 88.94 C ANISOU 1353 C ALA A 200 7981 9133 16679 -125 2184 903 C ATOM 1354 O ALA A 200 17.024 6.216 19.796 1.00 87.90 O ANISOU 1354 O ALA A 200 7915 9147 16336 -126 2052 849 O ATOM 1355 CB ALA A 200 13.851 6.494 19.488 1.00 90.37 C ANISOU 1355 CB ALA A 200 7829 9103 17404 -186 2249 975 C ATOM 1356 N ILE A 201 16.024 4.860 21.318 1.00 88.58 N ANISOU 1356 N ILE A 201 8059 9013 16584 -80 2385 941 N ATOM 1357 CA ILE A 201 17.110 4.845 22.302 1.00 88.23 C ANISOU 1357 CA ILE A 201 8246 9052 16225 -23 2453 919 C ATOM 1358 C ILE A 201 18.176 3.822 21.862 1.00 87.27 C ANISOU 1358 C ILE A 201 8194 9043 15922 -15 2278 874 C ATOM 1359 O ILE A 201 19.366 4.144 21.867 1.00 86.21 O ANISOU 1359 O ILE A 201 8176 9056 15524 6 2173 819 O ATOM 1360 CB ILE A 201 16.560 4.597 23.745 1.00 89.62 C ANISOU 1360 CB ILE A 201 8534 9094 16424 25 2748 985 C ATOM 1361 CG1 ILE A 201 15.736 5.815 24.238 1.00 90.62 C ANISOU 1361 CG1 ILE A 201 8624 9137 16671 30 2922 1012 C ATOM 1362 CG2 ILE A 201 17.682 4.250 24.743 1.00 89.34 C ANISOU 1362 CG2 ILE A 201 8748 9133 16064 87 2796 968 C ATOM 1363 CD1 ILE A 201 14.800 5.560 25.448 1.00 92.34 C ANISOU 1363 CD1 ILE A 201 8887 9186 17013 66 3234 1089 C ATOM 1364 N ALA A 202 17.738 2.609 21.458 1.00 88.62 N ANISOU 1364 N ALA A 202 8284 9140 16248 -32 2244 894 N ATOM 1365 CA ALA A 202 18.599 1.507 21.016 1.00 87.99 C ANISOU 1365 CA ALA A 202 8255 9139 16038 -21 2090 853 C ATOM 1366 C ALA A 202 19.378 1.805 19.729 1.00 86.70 C ANISOU 1366 C ALA A 202 8032 9134 15775 -51 1826 775 C ATOM 1367 O ALA A 202 20.583 1.558 19.690 1.00 85.79 O ANISOU 1367 O ALA A 202 8029 9151 15416 -21 1723 723 O ATOM 1368 CB ALA A 202 17.784 0.232 20.862 1.00 88.96 C ANISOU 1368 CB ALA A 202 8291 9121 16389 -40 2124 896 C ATOM 1369 N SER A 203 18.701 2.337 18.689 1.00 86.94 N ANISOU 1369 N SER A 203 7889 9151 15993 -109 1718 768 N ATOM 1370 CA SER A 203 19.316 2.671 17.398 1.00 85.92 C ANISOU 1370 CA SER A 203 7699 9162 15784 -142 1475 701 C ATOM 1371 C SER A 203 20.300 3.842 17.480 1.00 84.95 C ANISOU 1371 C SER A 203 7664 9190 15423 -131 1431 663 C ATOM 1372 O SER A 203 21.220 3.913 16.668 1.00 84.06 O ANISOU 1372 O SER A 203 7561 9222 15156 -141 1252 605 O ATOM 1373 CB SER A 203 18.252 2.935 16.336 1.00 86.41 C ANISOU 1373 CB SER A 203 7563 9154 16115 -204 1376 714 C ATOM 1374 OG SER A 203 17.397 4.004 16.709 1.00 86.87 O ANISOU 1374 OG SER A 203 7552 9130 16324 -218 1497 762 O ATOM 1375 N SER A 204 20.114 4.752 18.455 1.00 84.68 N ANISOU 1375 N SER A 204 7696 9118 15360 -111 1596 696 N ATOM 1376 CA SER A 204 20.998 5.903 18.649 1.00 83.90 C ANISOU 1376 CA SER A 204 7686 9143 15048 -102 1567 662 C ATOM 1377 C SER A 204 22.234 5.533 19.472 1.00 83.46 C ANISOU 1377 C SER A 204 7819 9181 14710 -47 1588 631 C ATOM 1378 O SER A 204 23.338 5.950 19.123 1.00 82.54 O ANISOU 1378 O SER A 204 7752 9215 14394 -49 1457 578 O ATOM 1379 CB SER A 204 20.248 7.061 19.298 1.00 84.53 C ANISOU 1379 CB SER A 204 7755 9135 15227 -104 1724 701 C ATOM 1380 OG SER A 204 19.192 7.515 18.467 1.00 84.90 O ANISOU 1380 OG SER A 204 7619 9107 15532 -153 1680 727 O ATOM 1381 N ILE A 205 22.052 4.747 20.552 1.00 81.96 N ANISOU 1381 N ILE A 205 7733 8899 14509 0 1750 668 N ATOM 1382 CA ILE A 205 23.137 4.320 21.436 1.00 81.75 C ANISOU 1382 CA ILE A 205 7894 8941 14226 59 1777 649 C ATOM 1383 C ILE A 205 24.055 3.266 20.797 1.00 81.15 C ANISOU 1383 C ILE A 205 7828 8965 14041 73 1608 603 C ATOM 1384 O ILE A 205 25.268 3.471 20.765 1.00 80.41 O ANISOU 1384 O ILE A 205 7815 9013 13724 93 1503 551 O ATOM 1385 CB ILE A 205 22.617 3.973 22.868 1.00 82.89 C ANISOU 1385 CB ILE A 205 8165 8950 14380 108 2017 710 C ATOM 1386 CG1 ILE A 205 22.359 5.272 23.668 1.00 83.13 C ANISOU 1386 CG1 ILE A 205 8262 8951 14372 116 2157 723 C ATOM 1387 CG2 ILE A 205 23.560 3.029 23.638 1.00 83.04 C ANISOU 1387 CG2 ILE A 205 8360 9006 14185 171 2026 704 C ATOM 1388 CD1 ILE A 205 21.373 5.160 24.835 1.00 84.44 C ANISOU 1388 CD1 ILE A 205 8492 8950 14641 147 2423 793 C ATOM 1389 N VAL A 206 23.481 2.168 20.270 1.00 79.93 N ANISOU 1389 N VAL A 206 7585 8734 14050 61 1580 618 N ATOM 1390 CA VAL A 206 24.240 1.071 19.652 1.00 79.55 C ANISOU 1390 CA VAL A 206 7544 8759 13922 78 1431 572 C ATOM 1391 C VAL A 206 24.879 1.467 18.307 1.00 78.53 C ANISOU 1391 C VAL A 206 7324 8779 13735 41 1215 502 C ATOM 1392 O VAL A 206 26.084 1.268 18.131 1.00 77.92 O ANISOU 1392 O VAL A 206 7313 8836 13456 70 1107 449 O ATOM 1393 CB VAL A 206 23.427 -0.258 19.574 1.00 80.40 C ANISOU 1393 CB VAL A 206 7600 8724 14224 78 1474 608 C ATOM 1394 CG1 VAL A 206 24.259 -1.397 18.985 1.00 80.02 C ANISOU 1394 CG1 VAL A 206 7574 8746 14083 105 1324 555 C ATOM 1395 CG2 VAL A 206 22.881 -0.656 20.944 1.00 81.48 C ANISOU 1395 CG2 VAL A 206 7841 8719 14400 116 1701 684 C ATOM 1396 N SER A 207 24.085 2.028 17.373 1.00 75.86 N ANISOU 1396 N SER A 207 6837 8415 13570 -20 1155 506 N ATOM 1397 CA SER A 207 24.569 2.400 16.041 1.00 75.07 C ANISOU 1397 CA SER A 207 6654 8445 13424 -59 956 449 C ATOM 1398 C SER A 207 25.223 3.793 15.887 1.00 74.32 C ANISOU 1398 C SER A 207 6576 8477 13186 -80 908 427 C ATOM 1399 O SER A 207 25.603 4.150 14.769 1.00 73.73 O ANISOU 1399 O SER A 207 6435 8508 13071 -116 753 388 O ATOM 1400 CB SER A 207 23.507 2.131 14.975 1.00 75.47 C ANISOU 1400 CB SER A 207 6546 8413 13716 -113 875 457 C ATOM 1401 OG SER A 207 22.728 3.273 14.660 1.00 75.63 O ANISOU 1401 OG SER A 207 6470 8401 13865 -163 878 486 O ATOM 1402 N PHE A 208 25.373 4.566 16.989 1.00 71.82 N ANISOU 1402 N PHE A 208 6354 8148 12786 -58 1039 452 N ATOM 1403 CA PHE A 208 26.013 5.889 16.939 1.00 71.22 C ANISOU 1403 CA PHE A 208 6303 8180 12577 -79 998 431 C ATOM 1404 C PHE A 208 26.773 6.307 18.203 1.00 71.25 C ANISOU 1404 C PHE A 208 6465 8217 12390 -34 1095 428 C ATOM 1405 O PHE A 208 27.973 6.558 18.110 1.00 70.66 O ANISOU 1405 O PHE A 208 6447 8282 12118 -25 1001 382 O ATOM 1406 CB PHE A 208 25.053 7.001 16.453 1.00 71.34 C ANISOU 1406 CB PHE A 208 6205 8138 12764 -136 1004 463 C ATOM 1407 CG PHE A 208 25.678 8.377 16.357 1.00 70.81 C ANISOU 1407 CG PHE A 208 6161 8170 12574 -162 959 445 C ATOM 1408 CD1 PHE A 208 26.489 8.719 15.281 1.00 70.08 C ANISOU 1408 CD1 PHE A 208 6027 8224 12377 -197 787 404 C ATOM 1409 CD2 PHE A 208 25.454 9.331 17.344 1.00 71.13 C ANISOU 1409 CD2 PHE A 208 6269 8154 12603 -151 1093 469 C ATOM 1410 CE1 PHE A 208 27.074 9.987 15.200 1.00 69.68 C ANISOU 1410 CE1 PHE A 208 5996 8258 12221 -227 748 393 C ATOM 1411 CE2 PHE A 208 26.035 10.600 17.259 1.00 70.72 C ANISOU 1411 CE2 PHE A 208 6241 8185 12445 -179 1046 450 C ATOM 1412 CZ PHE A 208 26.839 10.920 16.187 1.00 69.98 C ANISOU 1412 CZ PHE A 208 6098 8233 12258 -219 873 416 C ATOM 1413 N TYR A 209 26.079 6.425 19.357 1.00 70.19 N ANISOU 1413 N TYR A 209 6401 7954 12315 -7 1280 475 N ATOM 1414 CA TYR A 209 26.662 6.879 20.625 1.00 70.42 C ANISOU 1414 CA TYR A 209 6596 7994 12167 36 1382 474 C ATOM 1415 C TYR A 209 27.812 6.051 21.195 1.00 70.29 C ANISOU 1415 C TYR A 209 6715 8054 11938 94 1345 445 C ATOM 1416 O TYR A 209 28.852 6.630 21.511 1.00 69.95 O ANISOU 1416 O TYR A 209 6757 8118 11702 106 1288 407 O ATOM 1417 CB TYR A 209 25.586 7.207 21.671 1.00 71.42 C ANISOU 1417 CB TYR A 209 6769 7960 12408 53 1598 531 C ATOM 1418 CG TYR A 209 24.985 8.584 21.485 1.00 71.44 C ANISOU 1418 CG TYR A 209 6702 7930 12513 11 1631 540 C ATOM 1419 CD1 TYR A 209 23.952 8.800 20.577 1.00 71.54 C ANISOU 1419 CD1 TYR A 209 6539 7877 12766 -38 1607 566 C ATOM 1420 CD2 TYR A 209 25.459 9.676 22.206 1.00 71.44 C ANISOU 1420 CD2 TYR A 209 6812 7960 12372 21 1677 521 C ATOM 1421 CE1 TYR A 209 23.411 10.070 20.385 1.00 71.62 C ANISOU 1421 CE1 TYR A 209 6483 7854 12876 -73 1628 578 C ATOM 1422 CE2 TYR A 209 24.918 10.949 22.030 1.00 71.51 C ANISOU 1422 CE2 TYR A 209 6759 7931 12480 -15 1705 528 C ATOM 1423 CZ TYR A 209 23.893 11.141 21.118 1.00 71.60 C ANISOU 1423 CZ TYR A 209 6593 7878 12733 -60 1683 559 C ATOM 1424 OH TYR A 209 23.354 12.393 20.942 1.00 71.76 O ANISOU 1424 OH TYR A 209 6551 7855 12859 -91 1706 569 O ATOM 1425 N VAL A 210 27.642 4.714 21.315 1.00 67.84 N ANISOU 1425 N VAL A 210 6420 7687 11669 130 1370 463 N ATOM 1426 CA VAL A 210 28.685 3.802 21.815 1.00 67.81 C ANISOU 1426 CA VAL A 210 6538 7744 11483 192 1328 440 C ATOM 1427 C VAL A 210 29.960 3.854 20.931 1.00 66.87 C ANISOU 1427 C VAL A 210 6380 7805 11222 184 1127 370 C ATOM 1428 O VAL A 210 31.020 4.147 21.492 1.00 66.67 O ANISOU 1428 O VAL A 210 6459 7871 11002 215 1088 340 O ATOM 1429 CB VAL A 210 28.177 2.362 22.135 1.00 68.57 C ANISOU 1429 CB VAL A 210 6661 7725 11668 231 1403 481 C ATOM 1430 CG1 VAL A 210 29.330 1.383 22.360 1.00 68.65 C ANISOU 1430 CG1 VAL A 210 6769 7812 11503 293 1316 450 C ATOM 1431 CG2 VAL A 210 27.246 2.368 23.342 1.00 69.60 C ANISOU 1431 CG2 VAL A 210 6882 7696 11867 253 1624 552 C ATOM 1432 N PRO A 211 29.904 3.679 19.576 1.00 64.80 N ANISOU 1432 N PRO A 211 5973 7599 11049 142 999 340 N ATOM 1433 CA PRO A 211 31.142 3.785 18.779 1.00 64.04 C ANISOU 1433 CA PRO A 211 5846 7677 10810 137 830 275 C ATOM 1434 C PRO A 211 31.778 5.178 18.788 1.00 63.56 C ANISOU 1434 C PRO A 211 5794 7720 10636 102 788 254 C ATOM 1435 O PRO A 211 32.992 5.269 18.628 1.00 63.13 O ANISOU 1435 O PRO A 211 5761 7802 10423 115 686 207 O ATOM 1436 CB PRO A 211 30.705 3.367 17.370 1.00 63.82 C ANISOU 1436 CB PRO A 211 5673 7660 10916 96 729 257 C ATOM 1437 CG PRO A 211 29.410 2.657 17.551 1.00 64.52 C ANISOU 1437 CG PRO A 211 5730 7578 11206 95 829 307 C ATOM 1438 CD PRO A 211 28.759 3.337 18.707 1.00 65.02 C ANISOU 1438 CD PRO A 211 5863 7537 11305 99 996 363 C ATOM 1439 N LEU A 212 30.973 6.249 19.001 1.00 62.72 N ANISOU 1439 N LEU A 212 5669 7543 10618 60 870 287 N ATOM 1440 CA LEU A 212 31.444 7.640 19.070 1.00 62.40 C ANISOU 1440 CA LEU A 212 5641 7576 10492 23 842 272 C ATOM 1441 C LEU A 212 32.282 7.873 20.333 1.00 62.67 C ANISOU 1441 C LEU A 212 5835 7635 10342 69 884 258 C ATOM 1442 O LEU A 212 33.332 8.509 20.246 1.00 62.31 O ANISOU 1442 O LEU A 212 5806 7711 10158 55 790 219 O ATOM 1443 CB LEU A 212 30.266 8.630 19.019 1.00 62.66 C ANISOU 1443 CB LEU A 212 5616 7505 10687 -25 927 313 C ATOM 1444 CG LEU A 212 30.621 10.103 18.807 1.00 62.40 C ANISOU 1444 CG LEU A 212 5568 7538 10603 -76 881 299 C ATOM 1445 CD1 LEU A 212 30.371 10.523 17.372 1.00 61.89 C ANISOU 1445 CD1 LEU A 212 5353 7525 10638 -142 766 299 C ATOM 1446 CD2 LEU A 212 29.837 10.990 19.750 1.00 63.03 C ANISOU 1446 CD2 LEU A 212 5708 7495 10745 -75 1029 332 C ATOM 1447 N VAL A 213 31.814 7.357 21.498 1.00 63.37 N ANISOU 1447 N VAL A 213 6042 7607 10429 123 1023 292 N ATOM 1448 CA VAL A 213 32.489 7.456 22.802 1.00 63.88 C ANISOU 1448 CA VAL A 213 6283 7673 10315 176 1071 285 C ATOM 1449 C VAL A 213 33.886 6.813 22.715 1.00 63.60 C ANISOU 1449 C VAL A 213 6282 7771 10112 214 931 238 C ATOM 1450 O VAL A 213 34.860 7.408 23.181 1.00 63.60 O ANISOU 1450 O VAL A 213 6357 7854 9955 222 870 204 O ATOM 1451 CB VAL A 213 31.611 6.878 23.956 1.00 64.84 C ANISOU 1451 CB VAL A 213 6523 7635 10478 228 1256 340 C ATOM 1452 CG1 VAL A 213 32.413 6.661 25.240 1.00 65.43 C ANISOU 1452 CG1 VAL A 213 6796 7719 10345 296 1281 332 C ATOM 1453 CG2 VAL A 213 30.408 7.776 24.231 1.00 65.35 C ANISOU 1453 CG2 VAL A 213 6570 7579 10680 196 1405 378 C ATOM 1454 N ILE A 214 33.979 5.636 22.062 1.00 62.21 N ANISOU 1454 N ILE A 214 6040 7615 9981 236 873 233 N ATOM 1455 CA ILE A 214 35.235 4.909 21.855 1.00 62.00 C ANISOU 1455 CA ILE A 214 6024 7708 9825 279 743 188 C ATOM 1456 C ILE A 214 36.129 5.664 20.849 1.00 61.29 C ANISOU 1456 C ILE A 214 5826 7778 9684 227 599 135 C ATOM 1457 O ILE A 214 37.303 5.878 21.140 1.00 61.31 O ANISOU 1457 O ILE A 214 5872 7885 9538 247 516 98 O ATOM 1458 CB ILE A 214 35.000 3.415 21.468 1.00 62.15 C ANISOU 1458 CB ILE A 214 6011 7685 9918 321 734 195 C ATOM 1459 CG1 ILE A 214 33.995 2.727 22.428 1.00 62.95 C ANISOU 1459 CG1 ILE A 214 6209 7614 10095 359 893 259 C ATOM 1460 CG2 ILE A 214 36.328 2.638 21.413 1.00 62.16 C ANISOU 1460 CG2 ILE A 214 6039 7798 9780 380 612 149 C ATOM 1461 CD1 ILE A 214 33.216 1.539 21.828 1.00 63.08 C ANISOU 1461 CD1 ILE A 214 6148 7544 10276 364 912 281 C ATOM 1462 N MET A 215 35.561 6.096 19.697 1.00 60.98 N ANISOU 1462 N MET A 215 5648 7753 9769 161 571 136 N ATOM 1463 CA MET A 215 36.264 6.839 18.638 1.00 60.38 C ANISOU 1463 CA MET A 215 5466 7818 9658 104 450 98 C ATOM 1464 C MET A 215 36.906 8.136 19.155 1.00 60.36 C ANISOU 1464 C MET A 215 5510 7872 9551 72 433 86 C ATOM 1465 O MET A 215 38.055 8.414 18.814 1.00 60.15 O ANISOU 1465 O MET A 215 5453 7981 9420 61 328 46 O ATOM 1466 CB MET A 215 35.316 7.134 17.459 1.00 60.05 C ANISOU 1466 CB MET A 215 5293 7749 9774 40 440 116 C ATOM 1467 CG MET A 215 36.001 7.724 16.235 1.00 59.55 C ANISOU 1467 CG MET A 215 5124 7829 9673 -16 317 82 C ATOM 1468 SD MET A 215 34.840 8.470 15.062 1.00 59.35 S ANISOU 1468 SD MET A 215 4976 7759 9815 -99 307 115 S ATOM 1469 CE MET A 215 34.422 9.985 15.923 1.00 59.54 C ANISOU 1469 CE MET A 215 5052 7715 9856 -139 392 151 C ATOM 1470 N VAL A 216 36.171 8.915 19.974 1.00 61.96 N ANISOU 1470 N VAL A 216 5784 7969 9789 58 540 119 N ATOM 1471 CA VAL A 216 36.646 10.182 20.543 1.00 62.08 C ANISOU 1471 CA VAL A 216 5858 8013 9717 27 532 106 C ATOM 1472 C VAL A 216 37.741 9.951 21.601 1.00 62.51 C ANISOU 1472 C VAL A 216 6044 8114 9594 84 497 75 C ATOM 1473 O VAL A 216 38.799 10.574 21.509 1.00 62.43 O ANISOU 1473 O VAL A 216 6021 8214 9486 58 395 38 O ATOM 1474 CB VAL A 216 35.477 11.089 21.035 1.00 62.40 C ANISOU 1474 CB VAL A 216 5934 7918 9857 -1 660 144 C ATOM 1475 CG1 VAL A 216 35.978 12.279 21.856 1.00 62.77 C ANISOU 1475 CG1 VAL A 216 6079 7974 9798 -17 663 124 C ATOM 1476 CG2 VAL A 216 34.631 11.577 19.861 1.00 61.96 C ANISOU 1476 CG2 VAL A 216 5730 7845 9967 -68 651 169 C ATOM 1477 N PHE A 217 37.497 9.045 22.573 1.00 64.18 N ANISOU 1477 N PHE A 217 6377 8240 9769 158 574 94 N ATOM 1478 CA PHE A 217 38.432 8.724 23.659 1.00 64.73 C ANISOU 1478 CA PHE A 217 6589 8335 9670 221 540 72 C ATOM 1479 C PHE A 217 39.750 8.090 23.191 1.00 64.51 C ANISOU 1479 C PHE A 217 6506 8450 9555 247 389 29 C ATOM 1480 O PHE A 217 40.815 8.536 23.625 1.00 64.71 O ANISOU 1480 O PHE A 217 6574 8556 9456 251 298 -7 O ATOM 1481 CB PHE A 217 37.751 7.869 24.748 1.00 65.51 C ANISOU 1481 CB PHE A 217 6836 8298 9757 294 669 114 C ATOM 1482 CG PHE A 217 38.647 7.428 25.885 1.00 66.18 C ANISOU 1482 CG PHE A 217 7084 8398 9663 367 630 100 C ATOM 1483 CD1 PHE A 217 38.957 8.296 26.925 1.00 66.79 C ANISOU 1483 CD1 PHE A 217 7303 8459 9615 371 639 86 C ATOM 1484 CD2 PHE A 217 39.163 6.138 25.925 1.00 66.28 C ANISOU 1484 CD2 PHE A 217 7115 8434 9635 435 578 101 C ATOM 1485 CE1 PHE A 217 39.784 7.888 27.976 1.00 67.51 C ANISOU 1485 CE1 PHE A 217 7553 8563 9535 440 586 73 C ATOM 1486 CE2 PHE A 217 39.993 5.731 26.974 1.00 66.98 C ANISOU 1486 CE2 PHE A 217 7356 8533 9560 507 529 93 C ATOM 1487 CZ PHE A 217 40.296 6.608 27.993 1.00 67.59 C ANISOU 1487 CZ PHE A 217 7575 8598 9508 508 530 79 C ATOM 1488 N VAL A 218 39.678 7.044 22.341 1.00 63.86 N ANISOU 1488 N VAL A 218 6329 8392 9542 268 361 29 N ATOM 1489 CA VAL A 218 40.853 6.324 21.829 1.00 63.75 C ANISOU 1489 CA VAL A 218 6254 8505 9463 303 233 -14 C ATOM 1490 C VAL A 218 41.722 7.213 20.918 1.00 63.29 C ANISOU 1490 C VAL A 218 6070 8595 9383 237 124 -55 C ATOM 1491 O VAL A 218 42.944 7.235 21.091 1.00 63.54 O ANISOU 1491 O VAL A 218 6100 8731 9312 257 23 -92 O ATOM 1492 CB VAL A 218 40.503 4.932 21.218 1.00 63.66 C ANISOU 1492 CB VAL A 218 6190 8467 9531 348 241 -8 C ATOM 1493 CG1 VAL A 218 41.734 4.236 20.643 1.00 63.62 C ANISOU 1493 CG1 VAL A 218 6116 8594 9463 388 114 -59 C ATOM 1494 CG2 VAL A 218 39.831 4.032 22.253 1.00 64.29 C ANISOU 1494 CG2 VAL A 218 6407 8403 9617 416 344 36 C ATOM 1495 N TYR A 219 41.097 7.982 19.997 1.00 63.68 N ANISOU 1495 N TYR A 219 6016 8649 9530 157 143 -43 N ATOM 1496 CA TYR A 219 41.839 8.880 19.105 1.00 63.34 C ANISOU 1496 CA TYR A 219 5859 8737 9471 87 53 -70 C ATOM 1497 C TYR A 219 42.415 10.124 19.798 1.00 63.61 C ANISOU 1497 C TYR A 219 5947 8796 9426 47 25 -81 C ATOM 1498 O TYR A 219 43.321 10.757 19.252 1.00 63.56 O ANISOU 1498 O TYR A 219 5858 8908 9384 -1 -62 -107 O ATOM 1499 CB TYR A 219 41.063 9.217 17.822 1.00 62.78 C ANISOU 1499 CB TYR A 219 5667 8668 9519 19 67 -52 C ATOM 1500 CG TYR A 219 41.964 9.431 16.624 1.00 62.51 C ANISOU 1500 CG TYR A 219 5505 8788 9458 -22 -33 -84 C ATOM 1501 CD1 TYR A 219 42.584 8.356 15.992 1.00 62.56 C ANISOU 1501 CD1 TYR A 219 5454 8877 9439 26 -88 -118 C ATOM 1502 CD2 TYR A 219 42.189 10.705 16.114 1.00 62.31 C ANISOU 1502 CD2 TYR A 219 5418 8823 9434 -107 -65 -78 C ATOM 1503 CE1 TYR A 219 43.419 8.547 14.892 1.00 62.43 C ANISOU 1503 CE1 TYR A 219 5325 9003 9393 -7 -163 -147 C ATOM 1504 CE2 TYR A 219 43.021 10.908 15.014 1.00 62.19 C ANISOU 1504 CE2 TYR A 219 5289 8949 9391 -147 -142 -100 C ATOM 1505 CZ TYR A 219 43.633 9.825 14.405 1.00 62.27 C ANISOU 1505 CZ TYR A 219 5246 9044 9370 -96 -186 -135 C ATOM 1506 OH TYR A 219 44.453 10.017 13.320 1.00 62.26 O ANISOU 1506 OH TYR A 219 5137 9183 9337 -131 -246 -158 O ATOM 1507 N SER A 220 41.921 10.446 21.014 1.00 67.06 N ANISOU 1507 N SER A 220 6526 9120 9834 68 101 -62 N ATOM 1508 CA SER A 220 42.426 11.550 21.835 1.00 67.50 C ANISOU 1508 CA SER A 220 6662 9180 9805 40 74 -79 C ATOM 1509 C SER A 220 43.785 11.139 22.414 1.00 68.04 C ANISOU 1509 C SER A 220 6775 9336 9741 90 -37 -120 C ATOM 1510 O SER A 220 44.657 11.989 22.602 1.00 68.32 O ANISOU 1510 O SER A 220 6804 9440 9714 51 -122 -150 O ATOM 1511 CB SER A 220 41.454 11.872 22.966 1.00 67.95 C ANISOU 1511 CB SER A 220 6872 9083 9862 60 198 -52 C ATOM 1512 OG SER A 220 41.864 13.017 23.695 1.00 68.48 O ANISOU 1512 OG SER A 220 7024 9145 9850 29 171 -74 O ATOM 1513 N ARG A 221 43.957 9.824 22.675 1.00 69.05 N ANISOU 1513 N ARG A 221 6941 9457 9838 176 -41 -120 N ATOM 1514 CA ARG A 221 45.192 9.227 23.188 1.00 69.65 C ANISOU 1514 CA ARG A 221 7052 9608 9804 240 -149 -154 C ATOM 1515 C ARG A 221 46.241 9.121 22.074 1.00 69.36 C ANISOU 1515 C ARG A 221 6842 9729 9783 217 -260 -190 C ATOM 1516 O ARG A 221 47.437 9.084 22.368 1.00 69.90 O ANISOU 1516 O ARG A 221 6899 9884 9775 241 -371 -225 O ATOM 1517 CB ARG A 221 44.928 7.851 23.838 1.00 70.12 C ANISOU 1517 CB ARG A 221 7217 9591 9834 342 -108 -134 C ATOM 1518 CG ARG A 221 43.894 7.834 24.980 1.00 70.54 C ANISOU 1518 CG ARG A 221 7451 9485 9867 373 22 -91 C ATOM 1519 CD ARG A 221 44.337 8.573 26.236 1.00 71.28 C ANISOU 1519 CD ARG A 221 7703 9551 9829 381 -5 -105 C ATOM 1520 NE ARG A 221 43.783 9.929 26.289 1.00 71.01 N ANISOU 1520 NE ARG A 221 7678 9475 9827 302 55 -103 N ATOM 1521 CZ ARG A 221 42.990 10.382 27.256 1.00 71.61 C ANISOU 1521 CZ ARG A 221 7913 9428 9868 310 164 -83 C ATOM 1522 NH1 ARG A 221 42.662 9.602 28.279 1.00 72.55 N ANISOU 1522 NH1 ARG A 221 8203 9456 9907 391 230 -58 N ATOM 1523 NH2 ARG A 221 42.531 11.626 27.216 1.00 71.37 N ANISOU 1523 NH2 ARG A 221 7876 9362 9879 240 212 -87 N ATOM 1524 N VAL A 222 45.787 9.084 20.798 1.00 66.32 N ANISOU 1524 N VAL A 222 6322 9379 9498 171 -231 -181 N ATOM 1525 CA VAL A 222 46.637 9.037 19.599 1.00 66.09 C ANISOU 1525 CA VAL A 222 6128 9495 9488 143 -310 -211 C ATOM 1526 C VAL A 222 47.347 10.397 19.466 1.00 66.20 C ANISOU 1526 C VAL A 222 6085 9589 9478 56 -372 -225 C ATOM 1527 O VAL A 222 48.556 10.432 19.226 1.00 66.57 O ANISOU 1527 O VAL A 222 6051 9756 9486 55 -466 -259 O ATOM 1528 CB VAL A 222 45.836 8.646 18.320 1.00 65.41 C ANISOU 1528 CB VAL A 222 5942 9409 9502 118 -258 -196 C ATOM 1529 CG1 VAL A 222 46.712 8.681 17.069 1.00 65.29 C ANISOU 1529 CG1 VAL A 222 5771 9546 9490 87 -328 -228 C ATOM 1530 CG2 VAL A 222 45.191 7.273 18.471 1.00 65.42 C ANISOU 1530 CG2 VAL A 222 5996 9325 9536 200 -207 -186 C ATOM 1531 N PHE A 223 46.597 11.506 19.671 1.00 65.98 N ANISOU 1531 N PHE A 223 6100 9487 9482 -14 -317 -199 N ATOM 1532 CA PHE A 223 47.129 12.872 19.644 1.00 66.14 C ANISOU 1532 CA PHE A 223 6086 9555 9489 -101 -368 -207 C ATOM 1533 C PHE A 223 48.018 13.130 20.865 1.00 66.98 C ANISOU 1533 C PHE A 223 6289 9665 9495 -74 -446 -239 C ATOM 1534 O PHE A 223 48.945 13.937 20.781 1.00 67.30 O ANISOU 1534 O PHE A 223 6269 9786 9516 -132 -531 -262 O ATOM 1535 CB PHE A 223 45.998 13.914 19.583 1.00 65.78 C ANISOU 1535 CB PHE A 223 6072 9410 9511 -171 -285 -171 C ATOM 1536 CG PHE A 223 45.246 14.007 18.274 1.00 65.10 C ANISOU 1536 CG PHE A 223 5874 9334 9528 -222 -240 -139 C ATOM 1537 CD1 PHE A 223 45.912 14.300 17.089 1.00 64.93 C ANISOU 1537 CD1 PHE A 223 5710 9440 9521 -280 -299 -144 C ATOM 1538 CD2 PHE A 223 43.864 13.877 18.239 1.00 64.76 C ANISOU 1538 CD2 PHE A 223 5869 9169 9568 -215 -139 -102 C ATOM 1539 CE1 PHE A 223 45.213 14.403 15.883 1.00 64.43 C ANISOU 1539 CE1 PHE A 223 5559 9383 9538 -326 -266 -113 C ATOM 1540 CE2 PHE A 223 43.165 13.994 17.034 1.00 64.25 C ANISOU 1540 CE2 PHE A 223 5703 9110 9599 -263 -116 -72 C ATOM 1541 CZ PHE A 223 43.845 14.258 15.865 1.00 64.08 C ANISOU 1541 CZ PHE A 223 5556 9216 9575 -317 -184 -79 C ATOM 1542 N GLN A 224 47.733 12.440 21.992 1.00 69.10 N ANISOU 1542 N GLN A 224 6709 9844 9701 11 -419 -239 N ATOM 1543 CA GLN A 224 48.495 12.523 23.240 1.00 70.02 C ANISOU 1543 CA GLN A 224 6947 9950 9707 52 -499 -268 C ATOM 1544 C GLN A 224 49.875 11.873 23.047 1.00 70.44 C ANISOU 1544 C GLN A 224 6907 10133 9724 92 -629 -304 C ATOM 1545 O GLN A 224 50.865 12.376 23.581 1.00 71.22 O ANISOU 1545 O GLN A 224 7015 10279 9766 79 -740 -336 O ATOM 1546 CB GLN A 224 47.726 11.841 24.385 1.00 70.39 C ANISOU 1546 CB GLN A 224 7186 9864 9695 137 -421 -247 C ATOM 1547 CG GLN A 224 48.196 12.246 25.780 1.00 71.41 C ANISOU 1547 CG GLN A 224 7486 9946 9700 164 -479 -270 C ATOM 1548 CD GLN A 224 47.566 11.406 26.863 1.00 71.92 C ANISOU 1548 CD GLN A 224 7744 9892 9691 258 -402 -245 C ATOM 1549 OE1 GLN A 224 46.359 11.476 27.122 1.00 71.48 O ANISOU 1549 OE1 GLN A 224 7773 9719 9668 261 -257 -209 O ATOM 1550 NE2 GLN A 224 48.379 10.613 27.544 1.00 72.99 N ANISOU 1550 NE2 GLN A 224 7954 10051 9728 338 -497 -261 N ATOM 1551 N GLU A 225 49.932 10.767 22.270 1.00 70.07 N ANISOU 1551 N GLU A 225 6768 10137 9718 142 -616 -301 N ATOM 1552 CA GLU A 225 51.164 10.039 21.951 1.00 70.43 C ANISOU 1552 CA GLU A 225 6707 10304 9749 190 -720 -335 C ATOM 1553 C GLU A 225 52.018 10.796 20.938 1.00 70.32 C ANISOU 1553 C GLU A 225 6510 10426 9783 106 -777 -355 C ATOM 1554 O GLU A 225 53.242 10.648 20.938 1.00 70.79 O ANISOU 1554 O GLU A 225 6484 10587 9826 124 -881 -388 O ATOM 1555 CB GLU A 225 50.858 8.619 21.452 1.00 70.18 C ANISOU 1555 CB GLU A 225 6649 10267 9749 273 -675 -328 C ATOM 1556 CG GLU A 225 50.532 7.632 22.563 1.00 70.64 C ANISOU 1556 CG GLU A 225 6874 10219 9746 377 -659 -314 C ATOM 1557 CD GLU A 225 51.653 7.361 23.549 1.00 71.74 C ANISOU 1557 CD GLU A 225 7079 10386 9793 442 -784 -340 C ATOM 1558 OE1 GLU A 225 52.694 6.801 23.134 1.00 72.25 O ANISOU 1558 OE1 GLU A 225 7030 10556 9866 482 -877 -372 O ATOM 1559 OE2 GLU A 225 51.488 7.708 24.741 1.00 72.17 O ANISOU 1559 OE2 GLU A 225 7301 10355 9766 456 -791 -329 O ATOM 1560 N ALA A 226 51.368 11.604 20.076 1.00 68.61 N ANISOU 1560 N ALA A 226 6230 10208 9631 14 -707 -331 N ATOM 1561 CA ALA A 226 52.023 12.452 19.081 1.00 68.59 C ANISOU 1561 CA ALA A 226 6067 10320 9674 -79 -740 -336 C ATOM 1562 C ALA A 226 52.771 13.571 19.816 1.00 69.39 C ANISOU 1562 C ALA A 226 6181 10439 9745 -140 -830 -354 C ATOM 1563 O ALA A 226 53.853 13.969 19.385 1.00 69.93 O ANISOU 1563 O ALA A 226 6115 10623 9832 -183 -903 -373 O ATOM 1564 CB ALA A 226 50.987 13.041 18.136 1.00 67.80 C ANISOU 1564 CB ALA A 226 5932 10188 9641 -156 -646 -297 C ATOM 1565 N LYS A 227 52.205 14.044 20.949 1.00 69.61 N ANISOU 1565 N LYS A 227 6372 10349 9728 -141 -822 -350 N ATOM 1566 CA LYS A 227 52.808 15.072 21.794 1.00 70.45 C ANISOU 1566 CA LYS A 227 6524 10447 9796 -192 -913 -373 C ATOM 1567 C LYS A 227 53.925 14.475 22.664 1.00 71.45 C ANISOU 1567 C LYS A 227 6684 10612 9852 -117 -1040 -414 C ATOM 1568 O LYS A 227 54.871 15.185 23.008 1.00 72.32 O ANISOU 1568 O LYS A 227 6766 10764 9949 -161 -1153 -443 O ATOM 1569 CB LYS A 227 51.749 15.785 22.650 1.00 70.39 C ANISOU 1569 CB LYS A 227 6690 10293 9762 -215 -847 -359 C ATOM 1570 CG LYS A 227 52.124 17.224 22.988 1.00 70.97 C ANISOU 1570 CG LYS A 227 6776 10356 9833 -310 -914 -377 C ATOM 1571 CD LYS A 227 52.593 17.371 24.429 1.00 71.92 C ANISOU 1571 CD LYS A 227 7065 10412 9849 -267 -1000 -417 C ATOM 1572 CE LYS A 227 53.165 18.737 24.724 1.00 72.85 C ANISOU 1572 CE LYS A 227 7180 10531 9968 -360 -1097 -447 C ATOM 1573 NZ LYS A 227 54.612 18.814 24.399 1.00 73.61 N ANISOU 1573 NZ LYS A 227 7112 10762 10094 -393 -1237 -473 N ATOM 1574 N ARG A 228 53.813 13.171 23.000 1.00 71.31 N ANISOU 1574 N ARG A 228 6723 10576 9796 -5 -1027 -413 N ATOM 1575 CA ARG A 228 54.785 12.414 23.797 1.00 72.29 C ANISOU 1575 CA ARG A 228 6888 10726 9853 85 -1146 -444 C ATOM 1576 C ARG A 228 56.074 12.167 22.992 1.00 72.63 C ANISOU 1576 C ARG A 228 6725 10921 9951 83 -1241 -472 C ATOM 1577 O ARG A 228 57.170 12.144 23.565 1.00 73.65 O ANISOU 1577 O ARG A 228 6839 11093 10052 107 -1378 -504 O ATOM 1578 CB ARG A 228 54.167 11.074 24.237 1.00 72.18 C ANISOU 1578 CB ARG A 228 6998 10634 9793 202 -1086 -425 C ATOM 1579 CG ARG A 228 54.863 10.420 25.425 1.00 73.33 C ANISOU 1579 CG ARG A 228 7264 10755 9843 299 -1200 -445 C ATOM 1580 CD ARG A 228 54.796 8.906 25.363 1.00 73.35 C ANISOU 1580 CD ARG A 228 7283 10748 9839 416 -1176 -432 C ATOM 1581 NE ARG A 228 55.721 8.355 24.370 1.00 73.26 N ANISOU 1581 NE ARG A 228 7067 10868 9900 437 -1233 -457 N ATOM 1582 CZ ARG A 228 56.968 7.976 24.632 1.00 74.19 C ANISOU 1582 CZ ARG A 228 7125 11059 10005 494 -1373 -488 C ATOM 1583 NH1 ARG A 228 57.454 8.070 25.864 1.00 75.31 N ANISOU 1583 NH1 ARG A 228 7402 11155 10057 536 -1487 -498 N ATOM 1584 NH2 ARG A 228 57.739 7.497 23.665 1.00 74.15 N ANISOU 1584 NH2 ARG A 228 6927 11171 10076 514 -1401 -511 N ATOM 1585 N GLN A 229 55.925 11.981 21.664 1.00 70.61 N ANISOU 1585 N GLN A 229 6320 10738 9771 59 -1164 -459 N ATOM 1586 CA GLN A 229 57.000 11.718 20.707 1.00 70.87 C ANISOU 1586 CA GLN A 229 6148 10916 9863 52 -1215 -481 C ATOM 1587 C GLN A 229 57.959 12.898 20.508 1.00 71.32 C ANISOU 1587 C GLN A 229 6103 11040 9955 -55 -1295 -493 C ATOM 1588 O GLN A 229 59.073 12.691 20.028 1.00 71.82 O ANISOU 1588 O GLN A 229 6040 11201 10047 -46 -1396 -522 O ATOM 1589 CB GLN A 229 56.398 11.329 19.342 1.00 69.96 C ANISOU 1589 CB GLN A 229 5924 10852 9806 38 -1100 -462 C ATOM 1590 CG GLN A 229 56.185 9.834 19.131 1.00 70.05 C ANISOU 1590 CG GLN A 229 6018 10797 9801 138 -1026 -453 C ATOM 1591 CD GLN A 229 55.618 9.516 17.763 1.00 69.23 C ANISOU 1591 CD GLN A 229 5810 10742 9752 121 -929 -443 C ATOM 1592 OE1 GLN A 229 55.821 10.247 16.778 1.00 68.66 O ANISOU 1592 OE1 GLN A 229 5610 10757 9721 36 -911 -438 O ATOM 1593 NE2 GLN A 229 54.914 8.397 17.663 1.00 69.30 N ANISOU 1593 NE2 GLN A 229 5880 10691 9759 200 -869 -438 N ATOM 1594 N LEU A 230 57.525 14.127 20.840 1.00 68.01 N ANISOU 1594 N LEU A 230 5731 10566 9544 -157 -1257 -472 N ATOM 1595 CA LEU A 230 58.316 15.349 20.635 1.00 68.52 C ANISOU 1595 CA LEU A 230 5700 10685 9650 -264 -1338 -483 C ATOM 1596 C LEU A 230 59.638 15.430 21.425 1.00 69.65 C ANISOU 1596 C LEU A 230 5790 10887 9786 -226 -1499 -527 C ATOM 1597 O LEU A 230 59.643 15.678 22.634 1.00 70.30 O ANISOU 1597 O LEU A 230 6017 10901 9793 -151 -1577 -548 O ATOM 1598 CB LEU A 230 57.454 16.619 20.781 1.00 67.91 C ANISOU 1598 CB LEU A 230 5761 10493 9548 -342 -1324 -472 C ATOM 1599 CG LEU A 230 56.289 16.776 19.776 1.00 66.92 C ANISOU 1599 CG LEU A 230 5676 10302 9449 -391 -1178 -427 C ATOM 1600 CD1 LEU A 230 55.164 17.578 20.382 1.00 66.43 C ANISOU 1600 CD1 LEU A 230 5759 10117 9365 -453 -1172 -423 C ATOM 1601 CD2 LEU A 230 56.749 17.382 18.441 1.00 66.94 C ANISOU 1601 CD2 LEU A 230 5491 10409 9535 -474 -1128 -399 C ATOM 1602 N ASN A1002 60.760 15.186 20.714 1.00 61.00 N ANISOU 1602 N ASN A1002 6782 8730 7665 -812 1663 -397 N ATOM 1603 CA ASN A1002 62.130 15.178 21.242 1.00 60.37 C ANISOU 1603 CA ASN A1002 6954 8540 7444 -682 1568 -77 C ATOM 1604 C ASN A1002 63.042 16.170 20.508 1.00 58.32 C ANISOU 1604 C ASN A1002 6585 8393 7181 -500 1230 61 C ATOM 1605 O ASN A1002 62.578 16.881 19.610 1.00 57.50 O ANISOU 1605 O ASN A1002 6269 8431 7147 -471 1073 -61 O ATOM 1606 CB ASN A1002 62.725 13.761 21.132 1.00 61.53 C ANISOU 1606 CB ASN A1002 7285 8505 7588 -708 1736 29 C ATOM 1607 CG ASN A1002 61.995 12.682 21.896 1.00 61.28 C ANISOU 1607 CG ASN A1002 7481 8291 7512 -890 2103 -40 C ATOM 1608 OD1 ASN A1002 61.683 12.822 23.091 1.00 59.75 O ANISOU 1608 OD1 ASN A1002 7393 8080 7229 -967 2227 -85 O ATOM 1609 ND2 ASN A1002 61.778 11.548 21.233 1.00 63.05 N ANISOU 1609 ND2 ASN A1002 7803 8361 7792 -971 2302 -54 N ATOM 1610 N ILE A1003 64.342 16.206 20.899 1.00 58.09 N ANISOU 1610 N ILE A1003 6706 8294 7072 -375 1121 294 N ATOM 1611 CA ILE A1003 65.397 17.026 20.288 1.00 56.59 C ANISOU 1611 CA ILE A1003 6401 8202 6899 -242 847 394 C ATOM 1612 C ILE A1003 65.649 16.566 18.838 1.00 55.99 C ANISOU 1612 C ILE A1003 6202 8148 6923 -236 827 375 C ATOM 1613 O ILE A1003 65.808 17.414 17.955 1.00 55.01 O ANISOU 1613 O ILE A1003 5941 8124 6836 -194 668 360 O ATOM 1614 CB ILE A1003 66.698 17.097 21.172 1.00 56.75 C ANISOU 1614 CB ILE A1003 6574 8168 6820 -106 719 592 C ATOM 1615 CG1 ILE A1003 67.893 17.756 20.440 1.00 55.54 C ANISOU 1615 CG1 ILE A1003 6275 8122 6705 -17 470 643 C ATOM 1616 CG2 ILE A1003 67.110 15.734 21.744 1.00 58.05 C ANISOU 1616 CG2 ILE A1003 6900 8192 6964 -44 799 708 C ATOM 1617 CD1 ILE A1003 67.885 19.202 20.415 1.00 55.88 C ANISOU 1617 CD1 ILE A1003 6224 8265 6743 -37 358 561 C ATOM 1618 N PHE A1004 65.646 15.228 18.595 1.00 56.89 N ANISOU 1618 N PHE A1004 6400 8150 7066 -281 1005 376 N ATOM 1619 CA PHE A1004 65.834 14.632 17.263 1.00 56.58 C ANISOU 1619 CA PHE A1004 6263 8120 7115 -287 1025 334 C ATOM 1620 C PHE A1004 64.702 15.051 16.322 1.00 56.34 C ANISOU 1620 C PHE A1004 6043 8209 7154 -362 1020 115 C ATOM 1621 O PHE A1004 64.977 15.471 15.198 1.00 55.54 O ANISOU 1621 O PHE A1004 5836 8194 7073 -310 890 100 O ATOM 1622 CB PHE A1004 65.965 13.089 17.336 1.00 57.88 C ANISOU 1622 CB PHE A1004 6585 8112 7295 -320 1231 365 C ATOM 1623 CG PHE A1004 65.774 12.337 16.032 1.00 58.00 C ANISOU 1623 CG PHE A1004 6500 8125 7412 -376 1321 249 C ATOM 1624 CD1 PHE A1004 66.781 12.304 15.072 1.00 57.26 C ANISOU 1624 CD1 PHE A1004 6334 8071 7352 -285 1212 313 C ATOM 1625 CD2 PHE A1004 64.605 11.626 15.784 1.00 59.13 C ANISOU 1625 CD2 PHE A1004 6613 8230 7624 -531 1530 48 C ATOM 1626 CE1 PHE A1004 66.608 11.597 13.875 1.00 57.52 C ANISOU 1626 CE1 PHE A1004 6287 8106 7462 -333 1295 196 C ATOM 1627 CE2 PHE A1004 64.432 10.923 14.587 1.00 59.43 C ANISOU 1627 CE2 PHE A1004 6551 8273 7757 -578 1599 -85 C ATOM 1628 CZ PHE A1004 65.435 10.912 13.641 1.00 58.56 C ANISOU 1628 CZ PHE A1004 6393 8202 7655 -471 1475 -1 C ATOM 1629 N GLU A1005 63.442 14.964 16.797 1.00 56.40 N ANISOU 1629 N GLU A1005 6016 8224 7190 -475 1156 -71 N ATOM 1630 CA GLU A1005 62.245 15.334 16.032 1.00 56.69 C ANISOU 1630 CA GLU A1005 5845 8388 7307 -524 1133 -343 C ATOM 1631 C GLU A1005 62.184 16.835 15.733 1.00 55.69 C ANISOU 1631 C GLU A1005 5617 8399 7143 -407 866 -357 C ATOM 1632 O GLU A1005 61.659 17.223 14.688 1.00 55.67 O ANISOU 1632 O GLU A1005 5485 8498 7169 -355 740 -507 O ATOM 1633 CB GLU A1005 60.959 14.864 16.739 1.00 58.37 C ANISOU 1633 CB GLU A1005 6023 8574 7581 -687 1369 -571 C ATOM 1634 CG GLU A1005 60.878 13.364 17.001 1.00 59.82 C ANISOU 1634 CG GLU A1005 6344 8583 7801 -832 1676 -581 C ATOM 1635 CD GLU A1005 60.853 12.435 15.799 1.00 60.11 C ANISOU 1635 CD GLU A1005 6292 8608 7939 -870 1736 -698 C ATOM 1636 OE1 GLU A1005 60.314 12.829 14.739 1.00 59.59 O ANISOU 1636 OE1 GLU A1005 6004 8700 7937 -829 1586 -893 O ATOM 1637 OE2 GLU A1005 61.329 11.285 15.937 1.00 61.11 O ANISOU 1637 OE2 GLU A1005 6592 8558 8069 -928 1926 -604 O ATOM 1638 N MET A1006 62.731 17.668 16.645 1.00 54.46 N ANISOU 1638 N MET A1006 5547 8233 6912 -351 771 -203 N ATOM 1639 CA MET A1006 62.792 19.128 16.525 1.00 53.71 C ANISOU 1639 CA MET A1006 5406 8224 6777 -246 534 -186 C ATOM 1640 C MET A1006 63.683 19.526 15.343 1.00 52.87 C ANISOU 1640 C MET A1006 5316 8130 6642 -160 384 -63 C ATOM 1641 O MET A1006 63.246 20.285 14.477 1.00 52.92 O ANISOU 1641 O MET A1006 5272 8203 6632 -89 236 -154 O ATOM 1642 CB MET A1006 63.322 19.745 17.834 1.00 53.43 C ANISOU 1642 CB MET A1006 5476 8153 6673 -226 498 -43 C ATOM 1643 CG MET A1006 63.219 21.255 17.889 1.00 52.77 C ANISOU 1643 CG MET A1006 5354 8134 6562 -138 282 -52 C ATOM 1644 SD MET A1006 64.313 21.968 19.137 1.00 52.40 S ANISOU 1644 SD MET A1006 5429 8043 6438 -98 198 149 S ATOM 1645 CE MET A1006 63.300 23.301 19.716 1.00 52.83 C ANISOU 1645 CE MET A1006 5424 8163 6486 -75 110 -20 C ATOM 1646 N LEU A1007 64.918 18.993 15.304 1.00 52.40 N ANISOU 1646 N LEU A1007 5341 7999 6569 -158 430 128 N ATOM 1647 CA LEU A1007 65.896 19.262 14.251 1.00 51.92 C ANISOU 1647 CA LEU A1007 5296 7941 6490 -111 349 236 C ATOM 1648 C LEU A1007 65.555 18.552 12.936 1.00 52.30 C ANISOU 1648 C LEU A1007 5302 8013 6557 -122 400 133 C ATOM 1649 O LEU A1007 66.041 18.967 11.881 1.00 52.24 O ANISOU 1649 O LEU A1007 5320 8027 6502 -82 323 171 O ATOM 1650 CB LEU A1007 67.318 18.900 14.728 1.00 51.71 C ANISOU 1650 CB LEU A1007 5327 7849 6472 -97 378 418 C ATOM 1651 CG LEU A1007 68.182 19.986 15.418 1.00 51.40 C ANISOU 1651 CG LEU A1007 5310 7812 6408 -58 251 530 C ATOM 1652 CD1 LEU A1007 68.421 21.195 14.525 1.00 51.16 C ANISOU 1652 CD1 LEU A1007 5273 7813 6353 -50 135 539 C ATOM 1653 CD2 LEU A1007 67.642 20.385 16.784 1.00 51.54 C ANISOU 1653 CD2 LEU A1007 5369 7824 6390 -52 231 515 C ATOM 1654 N ARG A1008 64.708 17.499 12.998 1.00 54.61 N ANISOU 1654 N ARG A1008 5544 8296 6910 -188 542 -14 N ATOM 1655 CA ARG A1008 64.241 16.736 11.836 1.00 55.26 C ANISOU 1655 CA ARG A1008 5565 8408 7023 -206 595 -163 C ATOM 1656 C ARG A1008 63.351 17.620 10.949 1.00 55.74 C ANISOU 1656 C ARG A1008 5559 8582 7037 -127 417 -336 C ATOM 1657 O ARG A1008 63.373 17.477 9.726 1.00 56.20 O ANISOU 1657 O ARG A1008 5620 8680 7054 -83 368 -400 O ATOM 1658 CB ARG A1008 63.471 15.484 12.289 1.00 56.23 C ANISOU 1658 CB ARG A1008 5645 8478 7242 -321 808 -313 C ATOM 1659 CG ARG A1008 63.329 14.418 11.213 1.00 56.92 C ANISOU 1659 CG ARG A1008 5683 8561 7383 -360 904 -444 C ATOM 1660 CD ARG A1008 62.441 13.285 11.677 1.00 58.31 C ANISOU 1660 CD ARG A1008 5813 8672 7669 -505 1134 -636 C ATOM 1661 NE ARG A1008 61.673 12.718 10.569 1.00 59.31 N ANISOU 1661 NE ARG A1008 5801 8869 7865 -539 1155 -906 N ATOM 1662 CZ ARG A1008 60.712 11.809 10.706 1.00 60.87 C ANISOU 1662 CZ ARG A1008 5906 9035 8187 -686 1354 -1160 C ATOM 1663 NH1 ARG A1008 60.388 11.351 11.909 1.00 61.72 N ANISOU 1663 NH1 ARG A1008 6081 9022 8347 -825 1580 -1158 N ATOM 1664 NH2 ARG A1008 60.066 11.354 9.641 1.00 61.95 N ANISOU 1664 NH2 ARG A1008 5894 9255 8389 -702 1340 -1432 N ATOM 1665 N ILE A1009 62.579 18.533 11.573 1.00 56.79 N ANISOU 1665 N ILE A1009 5649 8763 7166 -91 312 -423 N ATOM 1666 CA ILE A1009 61.693 19.476 10.885 1.00 57.57 C ANISOU 1666 CA ILE A1009 5699 8958 7217 31 101 -602 C ATOM 1667 C ILE A1009 62.503 20.703 10.425 1.00 57.03 C ANISOU 1667 C ILE A1009 5799 8857 7013 142 -76 -406 C ATOM 1668 O ILE A1009 62.387 21.107 9.266 1.00 57.77 O ANISOU 1668 O ILE A1009 5972 8975 7003 247 -208 -445 O ATOM 1669 CB ILE A1009 60.460 19.866 11.765 1.00 58.36 C ANISOU 1669 CB ILE A1009 5659 9121 7394 28 76 -824 C ATOM 1670 CG1 ILE A1009 59.704 18.615 12.281 1.00 59.36 C ANISOU 1670 CG1 ILE A1009 5636 9256 7662 -130 317 -1039 C ATOM 1671 CG2 ILE A1009 59.505 20.809 11.011 1.00 59.53 C ANISOU 1671 CG2 ILE A1009 5754 9368 7496 207 -189 -1034 C ATOM 1672 CD1 ILE A1009 58.875 18.829 13.568 1.00 60.20 C ANISOU 1672 CD1 ILE A1009 5643 9382 7848 -213 418 -1191 C ATOM 1673 N ASP A1010 63.324 21.277 11.331 1.00 57.89 N ANISOU 1673 N ASP A1010 5982 8901 7113 112 -67 -207 N ATOM 1674 CA ASP A1010 64.145 22.465 11.082 1.00 57.64 C ANISOU 1674 CA ASP A1010 6105 8813 6983 169 -186 -33 C ATOM 1675 C ASP A1010 65.254 22.273 10.039 1.00 57.61 C ANISOU 1675 C ASP A1010 6219 8759 6911 144 -128 116 C ATOM 1676 O ASP A1010 65.242 22.966 9.019 1.00 58.45 O ANISOU 1676 O ASP A1010 6474 8843 6891 221 -230 130 O ATOM 1677 CB ASP A1010 64.696 23.045 12.398 1.00 56.91 C ANISOU 1677 CB ASP A1010 6021 8675 6927 125 -177 93 C ATOM 1678 CG ASP A1010 63.635 23.579 13.344 1.00 57.21 C ANISOU 1678 CG ASP A1010 5982 8755 6999 162 -250 -51 C ATOM 1679 OD1 ASP A1010 62.791 24.389 12.898 1.00 58.05 O ANISOU 1679 OD1 ASP A1010 6100 8892 7065 278 -416 -183 O ATOM 1680 OD2 ASP A1010 63.675 23.223 14.539 1.00 56.87 O ANISOU 1680 OD2 ASP A1010 5890 8708 7010 90 -151 -31 O ATOM 1681 N GLU A1011 66.204 21.347 10.288 1.00 60.95 N ANISOU 1681 N GLU A1011 6597 9156 7406 47 38 218 N ATOM 1682 CA GLU A1011 67.323 21.075 9.376 1.00 61.12 C ANISOU 1682 CA GLU A1011 6688 9142 7393 7 126 326 C ATOM 1683 C GLU A1011 66.918 20.188 8.197 1.00 61.76 C ANISOU 1683 C GLU A1011 6767 9263 7436 25 173 214 C ATOM 1684 O GLU A1011 67.221 20.524 7.051 1.00 62.45 O ANISOU 1684 O GLU A1011 6986 9340 7402 52 155 236 O ATOM 1685 CB GLU A1011 68.518 20.460 10.122 1.00 60.57 C ANISOU 1685 CB GLU A1011 6547 9037 7430 -66 252 442 C ATOM 1686 CG GLU A1011 69.281 21.436 10.998 1.00 60.33 C ANISOU 1686 CG GLU A1011 6529 8972 7422 -84 199 551 C ATOM 1687 CD GLU A1011 70.457 22.125 10.337 1.00 60.93 C ANISOU 1687 CD GLU A1011 6669 9007 7475 -139 238 636 C ATOM 1688 OE1 GLU A1011 71.608 21.843 10.741 1.00 61.00 O ANISOU 1688 OE1 GLU A1011 6590 9008 7579 -184 307 683 O ATOM 1689 OE2 GLU A1011 70.230 22.959 9.431 1.00 61.61 O ANISOU 1689 OE2 GLU A1011 6903 9061 7445 -133 201 642 O ATOM 1690 N GLY A1012 66.256 19.070 8.494 1.00 64.29 N ANISOU 1690 N GLY A1012 6960 9617 7851 0 247 86 N ATOM 1691 CA GLY A1012 65.805 18.107 7.497 1.00 65.03 C ANISOU 1691 CA GLY A1012 7018 9751 7939 3 300 -60 C ATOM 1692 C GLY A1012 66.731 16.917 7.372 1.00 64.81 C ANISOU 1692 C GLY A1012 6960 9675 7990 -72 486 5 C ATOM 1693 O GLY A1012 67.931 17.087 7.136 1.00 64.51 O ANISOU 1693 O GLY A1012 6978 9599 7933 -90 537 151 O ATOM 1694 N LEU A1013 66.178 15.702 7.536 1.00 68.54 N ANISOU 1694 N LEU A1013 7341 10139 8563 -119 598 -126 N ATOM 1695 CA LEU A1013 66.923 14.446 7.441 1.00 68.64 C ANISOU 1695 CA LEU A1013 7340 10081 8659 -170 771 -89 C ATOM 1696 C LEU A1013 67.160 14.095 5.968 1.00 69.41 C ANISOU 1696 C LEU A1013 7462 10220 8690 -153 792 -161 C ATOM 1697 O LEU A1013 66.201 13.969 5.201 1.00 70.23 O ANISOU 1697 O LEU A1013 7543 10394 8748 -130 735 -349 O ATOM 1698 CB LEU A1013 66.164 13.318 8.170 1.00 69.04 C ANISOU 1698 CB LEU A1013 7332 10070 8830 -243 907 -207 C ATOM 1699 CG LEU A1013 66.965 12.064 8.527 1.00 69.18 C ANISOU 1699 CG LEU A1013 7389 9958 8937 -273 1080 -127 C ATOM 1700 CD1 LEU A1013 66.676 11.621 9.944 1.00 69.60 C ANISOU 1700 CD1 LEU A1013 7499 9898 9048 -317 1175 -81 C ATOM 1701 CD2 LEU A1013 66.664 10.928 7.568 1.00 70.01 C ANISOU 1701 CD2 LEU A1013 7459 10047 9095 -316 1197 -293 C ATOM 1702 N ARG A1014 68.441 13.965 5.575 1.00 72.95 N ANISOU 1702 N ARG A1014 7951 10635 9132 -158 869 -35 N ATOM 1703 CA ARG A1014 68.849 13.630 4.207 1.00 73.84 C ANISOU 1703 CA ARG A1014 8106 10779 9170 -155 926 -89 C ATOM 1704 C ARG A1014 69.775 12.413 4.223 1.00 74.10 C ANISOU 1704 C ARG A1014 8082 10743 9330 -184 1095 -72 C ATOM 1705 O ARG A1014 70.870 12.475 4.785 1.00 73.86 O ANISOU 1705 O ARG A1014 8028 10667 9368 -181 1137 56 O ATOM 1706 CB ARG A1014 69.510 14.835 3.509 1.00 74.15 C ANISOU 1706 CB ARG A1014 8275 10846 9053 -140 874 18 C ATOM 1707 CG ARG A1014 68.553 15.992 3.230 1.00 74.56 C ANISOU 1707 CG ARG A1014 8442 10944 8943 -71 688 -16 C ATOM 1708 CD ARG A1014 69.289 17.240 2.783 1.00 74.88 C ANISOU 1708 CD ARG A1014 8664 10953 8834 -75 669 128 C ATOM 1709 NE ARG A1014 68.515 18.455 3.048 1.00 74.75 N ANISOU 1709 NE ARG A1014 8754 10934 8714 3 478 145 N ATOM 1710 CZ ARG A1014 68.600 19.175 4.164 1.00 73.78 C ANISOU 1710 CZ ARG A1014 8589 10776 8668 -12 423 236 C ATOM 1711 NH1 ARG A1014 69.425 18.810 5.138 1.00 72.91 N ANISOU 1711 NH1 ARG A1014 8340 10638 8725 -92 527 320 N ATOM 1712 NH2 ARG A1014 67.858 20.264 4.315 1.00 73.87 N ANISOU 1712 NH2 ARG A1014 8704 10780 8583 74 244 230 N ATOM 1713 N LEU A1015 69.312 11.299 3.630 1.00 76.97 N ANISOU 1713 N LEU A1015 8414 11097 9734 -200 1180 -227 N ATOM 1714 CA LEU A1015 70.037 10.024 3.582 1.00 77.52 C ANISOU 1714 CA LEU A1015 8444 11081 9929 -210 1337 -242 C ATOM 1715 C LEU A1015 71.280 10.040 2.686 1.00 78.20 C ANISOU 1715 C LEU A1015 8538 11195 9980 -200 1413 -207 C ATOM 1716 O LEU A1015 72.218 9.282 2.942 1.00 78.67 O ANISOU 1716 O LEU A1015 8545 11183 10163 -178 1511 -179 O ATOM 1717 CB LEU A1015 69.098 8.861 3.197 1.00 78.34 C ANISOU 1717 CB LEU A1015 8517 11152 10096 -249 1419 -445 C ATOM 1718 CG LEU A1015 67.827 8.670 4.042 1.00 78.20 C ANISOU 1718 CG LEU A1015 8468 11097 10147 -302 1411 -540 C ATOM 1719 CD1 LEU A1015 66.842 7.759 3.341 1.00 79.48 C ANISOU 1719 CD1 LEU A1015 8572 11265 10362 -364 1487 -804 C ATOM 1720 CD2 LEU A1015 68.143 8.132 5.432 1.00 77.71 C ANISOU 1720 CD2 LEU A1015 8450 10878 10198 -315 1500 -406 C ATOM 1721 N LYS A1016 71.287 10.892 1.643 1.00 80.02 N ANISOU 1721 N LYS A1016 8849 11519 10036 -208 1373 -221 N ATOM 1722 CA LYS A1016 72.403 11.027 0.702 1.00 81.02 C ANISOU 1722 CA LYS A1016 9010 11674 10100 -233 1487 -204 C ATOM 1723 C LYS A1016 73.387 12.124 1.121 1.00 80.76 C ANISOU 1723 C LYS A1016 8983 11640 10062 -265 1490 -54 C ATOM 1724 O LYS A1016 73.005 13.049 1.841 1.00 79.90 O ANISOU 1724 O LYS A1016 8909 11528 9921 -258 1365 39 O ATOM 1725 CB LYS A1016 71.886 11.294 -0.720 1.00 82.04 C ANISOU 1725 CB LYS A1016 9286 11880 10005 -230 1473 -306 C ATOM 1726 CG LYS A1016 71.515 10.033 -1.482 1.00 83.08 C ANISOU 1726 CG LYS A1016 9381 12024 10162 -219 1542 -496 C ATOM 1727 CD LYS A1016 71.457 10.291 -2.979 1.00 84.53 C ANISOU 1727 CD LYS A1016 9726 12283 10109 -212 1573 -581 C ATOM 1728 CE LYS A1016 71.364 9.011 -3.769 1.00 85.86 C ANISOU 1728 CE LYS A1016 9841 12463 10319 -209 1670 -778 C ATOM 1729 NZ LYS A1016 71.438 9.260 -5.232 1.00 87.48 N ANISOU 1729 NZ LYS A1016 10229 12742 10268 -199 1717 -856 N ATOM 1730 N ILE A1017 74.652 12.021 0.657 1.00 81.56 N ANISOU 1730 N ILE A1017 9035 11746 10208 -309 1645 -60 N ATOM 1731 CA ILE A1017 75.710 13.000 0.939 1.00 81.81 C ANISOU 1731 CA ILE A1017 9037 11781 10266 -374 1693 26 C ATOM 1732 C ILE A1017 75.423 14.274 0.133 1.00 82.52 C ANISOU 1732 C ILE A1017 9355 11887 10112 -444 1695 83 C ATOM 1733 O ILE A1017 75.269 14.211 -1.090 1.00 83.76 O ANISOU 1733 O ILE A1017 9667 12066 10092 -468 1780 24 O ATOM 1734 CB ILE A1017 77.143 12.440 0.676 1.00 83.05 C ANISOU 1734 CB ILE A1017 9029 11948 10578 -407 1877 -56 C ATOM 1735 CG1 ILE A1017 77.352 11.056 1.339 1.00 82.98 C ANISOU 1735 CG1 ILE A1017 8855 11894 10780 -290 1855 -120 C ATOM 1736 CG2 ILE A1017 78.219 13.443 1.133 1.00 83.29 C ANISOU 1736 CG2 ILE A1017 8970 11990 10686 -487 1922 -15 C ATOM 1737 CD1 ILE A1017 78.443 10.178 0.701 1.00 84.60 C ANISOU 1737 CD1 ILE A1017 8919 12112 11113 -281 2028 -263 C ATOM 1738 N TYR A1018 75.330 15.418 0.829 1.00 82.79 N ANISOU 1738 N TYR A1018 9439 11896 10121 -463 1593 195 N ATOM 1739 CA TYR A1018 75.033 16.716 0.224 1.00 83.61 C ANISOU 1739 CA TYR A1018 9805 11972 9992 -509 1574 270 C ATOM 1740 C TYR A1018 75.969 17.818 0.724 1.00 84.08 C ANISOU 1740 C TYR A1018 9855 11983 10109 -623 1646 352 C ATOM 1741 O TYR A1018 76.461 17.743 1.852 1.00 83.63 O ANISOU 1741 O TYR A1018 9576 11934 10265 -619 1601 360 O ATOM 1742 CB TYR A1018 73.556 17.100 0.474 1.00 82.65 C ANISOU 1742 CB TYR A1018 9803 11853 9747 -391 1331 291 C ATOM 1743 CG TYR A1018 73.221 17.414 1.919 1.00 80.95 C ANISOU 1743 CG TYR A1018 9454 11625 9678 -353 1178 350 C ATOM 1744 CD1 TYR A1018 73.163 18.729 2.372 1.00 80.76 C ANISOU 1744 CD1 TYR A1018 9539 11554 9592 -369 1091 449 C ATOM 1745 CD2 TYR A1018 72.929 16.399 2.826 1.00 79.81 C ANISOU 1745 CD2 TYR A1018 9109 11499 9715 -300 1131 304 C ATOM 1746 CE1 TYR A1018 72.861 19.025 3.701 1.00 79.35 C ANISOU 1746 CE1 TYR A1018 9242 11371 9536 -334 956 491 C ATOM 1747 CE2 TYR A1018 72.638 16.682 4.160 1.00 78.55 C ANISOU 1747 CE2 TYR A1018 8864 11323 9659 -268 1012 360 C ATOM 1748 CZ TYR A1018 72.593 17.998 4.591 1.00 78.27 C ANISOU 1748 CZ TYR A1018 8912 11265 9562 -283 918 446 C ATOM 1749 OH TYR A1018 72.285 18.283 5.900 1.00 77.17 O ANISOU 1749 OH TYR A1018 8695 11116 9511 -250 803 487 O ATOM 1750 N LYS A1019 76.185 18.852 -0.107 1.00 86.45 N ANISOU 1750 N LYS A1019 10420 12221 10206 -720 1753 406 N ATOM 1751 CA LYS A1019 77.003 20.012 0.248 1.00 87.26 C ANISOU 1751 CA LYS A1019 10556 12251 10348 -863 1853 468 C ATOM 1752 C LYS A1019 76.112 21.030 0.960 1.00 86.19 C ANISOU 1752 C LYS A1019 10556 12057 10136 -786 1622 577 C ATOM 1753 O LYS A1019 75.055 21.395 0.436 1.00 86.31 O ANISOU 1753 O LYS A1019 10834 12039 9920 -681 1484 621 O ATOM 1754 CB LYS A1019 77.661 20.632 -0.995 1.00 89.93 C ANISOU 1754 CB LYS A1019 11166 12511 10492 -1031 2130 473 C ATOM 1755 CG LYS A1019 78.908 19.895 -1.465 1.00 91.37 C ANISOU 1755 CG LYS A1019 11145 12749 10823 -1167 2419 334 C ATOM 1756 CD LYS A1019 79.565 20.608 -2.638 1.00 94.37 C ANISOU 1756 CD LYS A1019 11822 13035 11000 -1373 2742 335 C ATOM 1757 CE LYS A1019 80.829 19.918 -3.087 1.00 96.15 C ANISOU 1757 CE LYS A1019 11811 13327 11395 -1526 3057 157 C ATOM 1758 NZ LYS A1019 81.453 20.610 -4.244 1.00 99.34 N ANISOU 1758 NZ LYS A1019 12531 13628 11585 -1759 3424 147 N ATOM 1759 N ASP A1020 76.526 21.471 2.162 1.00 86.00 N ANISOU 1759 N ASP A1020 10342 12028 10306 -819 1561 597 N ATOM 1760 CA ASP A1020 75.774 22.433 2.976 1.00 85.02 C ANISOU 1760 CA ASP A1020 10308 11852 10143 -753 1351 682 C ATOM 1761 C ASP A1020 75.814 23.870 2.420 1.00 86.73 C ANISOU 1761 C ASP A1020 10869 11922 10163 -845 1417 770 C ATOM 1762 O ASP A1020 76.333 24.093 1.322 1.00 88.79 O ANISOU 1762 O ASP A1020 11342 12113 10281 -963 1638 776 O ATOM 1763 CB ASP A1020 76.217 22.368 4.458 1.00 83.95 C ANISOU 1763 CB ASP A1020 9871 11763 10263 -745 1260 662 C ATOM 1764 CG ASP A1020 77.683 22.662 4.757 1.00 85.44 C ANISOU 1764 CG ASP A1020 9877 11947 10639 -906 1432 599 C ATOM 1765 OD1 ASP A1020 78.433 23.002 3.813 1.00 87.37 O ANISOU 1765 OD1 ASP A1020 10220 12142 10834 -1068 1675 566 O ATOM 1766 OD2 ASP A1020 78.077 22.561 5.938 1.00 84.94 O ANISOU 1766 OD2 ASP A1020 9574 11932 10767 -871 1328 562 O ATOM 1767 N THR A1021 75.263 24.841 3.184 1.00 86.86 N ANISOU 1767 N THR A1021 10966 11874 10163 -791 1239 835 N ATOM 1768 CA THR A1021 75.220 26.268 2.832 1.00 88.56 C ANISOU 1768 CA THR A1021 11534 11913 10202 -854 1269 927 C ATOM 1769 C THR A1021 76.624 26.871 2.682 1.00 90.57 C ANISOU 1769 C THR A1021 11795 12072 10545 -1120 1574 914 C ATOM 1770 O THR A1021 76.806 27.807 1.902 1.00 92.68 O ANISOU 1770 O THR A1021 12434 12162 10618 -1229 1730 985 O ATOM 1771 CB THR A1021 74.370 27.058 3.841 1.00 87.43 C ANISOU 1771 CB THR A1021 11405 11737 10077 -730 1006 967 C ATOM 1772 OG1 THR A1021 74.869 26.838 5.161 1.00 85.74 O ANISOU 1772 OG1 THR A1021 10832 11609 10137 -776 971 917 O ATOM 1773 CG2 THR A1021 72.889 26.704 3.770 1.00 86.65 C ANISOU 1773 CG2 THR A1021 11356 11709 9858 -485 734 946 C ATOM 1774 N GLU A1022 77.609 26.320 3.420 1.00 91.21 N ANISOU 1774 N GLU A1022 11475 12263 10918 -1219 1662 806 N ATOM 1775 CA GLU A1022 79.010 26.751 3.396 1.00 93.31 C ANISOU 1775 CA GLU A1022 11626 12484 11344 -1476 1948 716 C ATOM 1776 C GLU A1022 79.751 26.154 2.191 1.00 95.22 C ANISOU 1776 C GLU A1022 11903 12739 11537 -1614 2258 645 C ATOM 1777 O GLU A1022 80.466 26.879 1.497 1.00 97.94 O ANISOU 1777 O GLU A1022 12447 12951 11815 -1846 2560 629 O ATOM 1778 CB GLU A1022 79.732 26.394 4.716 1.00 92.36 C ANISOU 1778 CB GLU A1022 11040 12495 11557 -1477 1861 589 C ATOM 1779 CG GLU A1022 78.995 26.763 5.999 1.00 90.31 C ANISOU 1779 CG GLU A1022 10712 12256 11346 -1320 1550 643 C ATOM 1780 CD GLU A1022 78.666 28.231 6.205 1.00 90.72 C ANISOU 1780 CD GLU A1022 11029 12142 11299 -1382 1511 724 C ATOM 1781 OE1 GLU A1022 79.606 29.057 6.249 1.00 93.01 O ANISOU 1781 OE1 GLU A1022 11315 12338 11686 -1601 1704 658 O ATOM 1782 OE2 GLU A1022 77.464 28.550 6.353 1.00 88.97 O ANISOU 1782 OE2 GLU A1022 11004 11882 10919 -1212 1289 830 O ATOM 1783 N GLY A1023 79.567 24.850 1.960 1.00 92.80 N ANISOU 1783 N GLY A1023 11420 12577 11263 -1482 2202 593 N ATOM 1784 CA GLY A1023 80.186 24.124 0.854 1.00 94.42 C ANISOU 1784 CA GLY A1023 11628 12818 11429 -1579 2469 506 C ATOM 1785 C GLY A1023 80.742 22.752 1.194 1.00 93.73 C ANISOU 1785 C GLY A1023 11113 12905 11595 -1508 2459 355 C ATOM 1786 O GLY A1023 81.020 21.963 0.286 1.00 94.84 O ANISOU 1786 O GLY A1023 11252 13091 11692 -1531 2628 281 O ATOM 1787 N TYR A1024 80.914 22.458 2.499 1.00 90.51 N ANISOU 1787 N TYR A1024 10368 12583 11439 -1405 2257 306 N ATOM 1788 CA TYR A1024 81.457 21.186 2.995 1.00 90.07 C ANISOU 1788 CA TYR A1024 9935 12664 11624 -1293 2203 170 C ATOM 1789 C TYR A1024 80.432 20.043 2.924 1.00 88.12 C ANISOU 1789 C TYR A1024 9730 12462 11290 -1077 2024 232 C ATOM 1790 O TYR A1024 79.228 20.300 2.872 1.00 86.81 O ANISOU 1790 O TYR A1024 9800 12253 10931 -989 1868 363 O ATOM 1791 CB TYR A1024 82.007 21.338 4.431 1.00 89.59 C ANISOU 1791 CB TYR A1024 9562 12659 11820 -1238 2033 97 C ATOM 1792 CG TYR A1024 82.732 22.641 4.704 1.00 91.05 C ANISOU 1792 CG TYR A1024 9723 12786 12086 -1444 2149 40 C ATOM 1793 CD1 TYR A1024 83.973 22.907 4.130 1.00 93.92 C ANISOU 1793 CD1 TYR A1024 9947 13154 12585 -1675 2461 -147 C ATOM 1794 CD2 TYR A1024 82.191 23.596 5.560 1.00 89.81 C ANISOU 1794 CD2 TYR A1024 9668 12567 11889 -1420 1964 144 C ATOM 1795 CE1 TYR A1024 84.646 24.102 4.382 1.00 95.57 C ANISOU 1795 CE1 TYR A1024 10126 13296 12890 -1898 2600 -231 C ATOM 1796 CE2 TYR A1024 82.859 24.792 5.825 1.00 91.32 C ANISOU 1796 CE2 TYR A1024 9839 12690 12168 -1620 2077 74 C ATOM 1797 CZ TYR A1024 84.086 25.041 5.232 1.00 94.24 C ANISOU 1797 CZ TYR A1024 10075 13054 12677 -1867 2401 -114 C ATOM 1798 OH TYR A1024 84.745 26.219 5.487 1.00 96.03 O ANISOU 1798 OH TYR A1024 10277 13199 13011 -2096 2545 -210 O ATOM 1799 N TYR A1025 80.913 18.781 2.922 1.00 84.82 N ANISOU 1799 N TYR A1025 9074 12126 11028 -993 2050 114 N ATOM 1800 CA TYR A1025 80.057 17.594 2.852 1.00 83.40 C ANISOU 1800 CA TYR A1025 8918 11969 10801 -816 1925 142 C ATOM 1801 C TYR A1025 79.346 17.305 4.171 1.00 81.31 C ANISOU 1801 C TYR A1025 8589 11703 10601 -645 1651 218 C ATOM 1802 O TYR A1025 79.989 17.210 5.218 1.00 81.32 O ANISOU 1802 O TYR A1025 8381 11729 10787 -584 1559 176 O ATOM 1803 CB TYR A1025 80.831 16.369 2.338 1.00 84.70 C ANISOU 1803 CB TYR A1025 8892 12189 11102 -788 2068 -14 C ATOM 1804 CG TYR A1025 81.340 16.537 0.923 1.00 86.68 C ANISOU 1804 CG TYR A1025 9252 12441 11241 -959 2363 -92 C ATOM 1805 CD1 TYR A1025 82.669 16.864 0.674 1.00 89.13 C ANISOU 1805 CD1 TYR A1025 9384 12782 11700 -1121 2600 -246 C ATOM 1806 CD2 TYR A1025 80.488 16.391 -0.168 1.00 86.44 C ANISOU 1806 CD2 TYR A1025 9509 12385 10950 -962 2411 -34 C ATOM 1807 CE1 TYR A1025 83.142 17.029 -0.626 1.00 91.28 C ANISOU 1807 CE1 TYR A1025 9785 13045 11852 -1304 2918 -323 C ATOM 1808 CE2 TYR A1025 80.946 16.566 -1.473 1.00 88.55 C ANISOU 1808 CE2 TYR A1025 9932 12644 11069 -1114 2690 -97 C ATOM 1809 CZ TYR A1025 82.277 16.876 -1.698 1.00 90.97 C ANISOU 1809 CZ TYR A1025 10082 12967 11516 -1296 2962 -233 C ATOM 1810 OH TYR A1025 82.736 17.040 -2.983 1.00 93.37 O ANISOU 1810 OH TYR A1025 10564 13253 11660 -1470 3282 -302 O ATOM 1811 N THR A1026 78.008 17.182 4.106 1.00 76.11 N ANISOU 1811 N THR A1026 8117 11019 9782 -567 1526 310 N ATOM 1812 CA THR A1026 77.119 16.945 5.248 1.00 74.33 C ANISOU 1812 CA THR A1026 7881 10781 9580 -437 1312 376 C ATOM 1813 C THR A1026 76.169 15.762 4.958 1.00 73.65 C ANISOU 1813 C THR A1026 7842 10690 9452 -346 1287 349 C ATOM 1814 O THR A1026 75.874 15.481 3.794 1.00 74.27 O ANISOU 1814 O THR A1026 8019 10781 9420 -378 1381 301 O ATOM 1815 CB THR A1026 76.367 18.259 5.584 1.00 73.59 C ANISOU 1815 CB THR A1026 7947 10657 9357 -467 1192 474 C ATOM 1816 OG1 THR A1026 77.296 19.346 5.606 1.00 74.58 O ANISOU 1816 OG1 THR A1026 8055 10764 9517 -589 1268 478 O ATOM 1817 CG2 THR A1026 75.626 18.211 6.916 1.00 72.04 C ANISOU 1817 CG2 THR A1026 7716 10455 9201 -362 999 524 C ATOM 1818 N ILE A1027 75.714 15.065 6.021 1.00 70.01 N ANISOU 1818 N ILE A1027 7325 10201 9075 -241 1176 368 N ATOM 1819 CA ILE A1027 74.785 13.929 5.951 1.00 69.56 C ANISOU 1819 CA ILE A1027 7308 10112 9010 -182 1176 327 C ATOM 1820 C ILE A1027 73.818 13.921 7.155 1.00 68.46 C ANISOU 1820 C ILE A1027 7209 9932 8870 -131 1052 378 C ATOM 1821 O ILE A1027 74.209 14.292 8.264 1.00 68.19 O ANISOU 1821 O ILE A1027 7139 9881 8889 -91 967 447 O ATOM 1822 CB ILE A1027 75.523 12.571 5.722 1.00 70.52 C ANISOU 1822 CB ILE A1027 7334 10199 9261 -127 1285 249 C ATOM 1823 CG1 ILE A1027 74.553 11.464 5.238 1.00 70.48 C ANISOU 1823 CG1 ILE A1027 7395 10153 9231 -114 1339 173 C ATOM 1824 CG2 ILE A1027 76.349 12.134 6.948 1.00 70.82 C ANISOU 1824 CG2 ILE A1027 7273 10187 9449 -14 1217 279 C ATOM 1825 CD1 ILE A1027 75.153 10.411 4.338 1.00 71.63 C ANISOU 1825 CD1 ILE A1027 7489 10285 9442 -101 1479 66 C ATOM 1826 N GLY A1028 72.571 13.518 6.908 1.00 67.38 N ANISOU 1826 N GLY A1028 7138 9788 8675 -139 1050 319 N ATOM 1827 CA GLY A1028 71.526 13.436 7.923 1.00 66.72 C ANISOU 1827 CA GLY A1028 7088 9669 8594 -125 986 324 C ATOM 1828 C GLY A1028 71.052 14.789 8.404 1.00 65.98 C ANISOU 1828 C GLY A1028 7026 9622 8421 -135 854 373 C ATOM 1829 O GLY A1028 70.533 15.583 7.614 1.00 66.02 O ANISOU 1829 O GLY A1028 7079 9684 8321 -152 798 335 O ATOM 1830 N ILE A1029 71.236 15.057 9.708 1.00 65.99 N ANISOU 1830 N ILE A1029 7024 9589 8460 -105 792 454 N ATOM 1831 CA ILE A1029 70.839 16.316 10.340 1.00 65.37 C ANISOU 1831 CA ILE A1029 6971 9544 8323 -109 667 495 C ATOM 1832 C ILE A1029 72.080 17.113 10.788 1.00 65.45 C ANISOU 1832 C ILE A1029 6944 9560 8364 -98 610 587 C ATOM 1833 O ILE A1029 72.626 16.869 11.869 1.00 65.60 O ANISOU 1833 O ILE A1029 6936 9549 8440 -44 574 634 O ATOM 1834 CB ILE A1029 69.783 16.103 11.472 1.00 65.09 C ANISOU 1834 CB ILE A1029 6964 9479 8288 -104 650 469 C ATOM 1835 CG1 ILE A1029 68.537 15.342 10.955 1.00 65.42 C ANISOU 1835 CG1 ILE A1029 6999 9525 8332 -146 731 318 C ATOM 1836 CG2 ILE A1029 69.379 17.437 12.110 1.00 64.57 C ANISOU 1836 CG2 ILE A1029 6914 9453 8167 -98 518 493 C ATOM 1837 CD1 ILE A1029 67.715 14.625 12.034 1.00 65.74 C ANISOU 1837 CD1 ILE A1029 7072 9497 8410 -184 824 269 C ATOM 1838 N GLY A1030 72.519 18.027 9.919 1.00 66.31 N ANISOU 1838 N GLY A1030 7068 9700 8427 -150 610 596 N ATOM 1839 CA GLY A1030 73.655 18.925 10.120 1.00 66.79 C ANISOU 1839 CA GLY A1030 7083 9764 8529 -189 594 639 C ATOM 1840 C GLY A1030 74.963 18.313 10.589 1.00 67.46 C ANISOU 1840 C GLY A1030 7024 9853 8754 -156 627 625 C ATOM 1841 O GLY A1030 75.736 18.984 11.281 1.00 67.84 O ANISOU 1841 O GLY A1030 6995 9915 8866 -160 563 629 O ATOM 1842 N HIS A1031 75.228 17.044 10.220 1.00 67.26 N ANISOU 1842 N HIS A1031 6954 9816 8786 -110 712 584 N ATOM 1843 CA HIS A1031 76.450 16.339 10.606 1.00 68.26 C ANISOU 1843 CA HIS A1031 6942 9942 9052 -32 718 542 C ATOM 1844 C HIS A1031 77.538 16.487 9.541 1.00 69.53 C ANISOU 1844 C HIS A1031 6984 10148 9286 -115 851 457 C ATOM 1845 O HIS A1031 77.458 15.868 8.476 1.00 69.91 O ANISOU 1845 O HIS A1031 7055 10194 9313 -150 982 415 O ATOM 1846 CB HIS A1031 76.162 14.864 10.954 1.00 68.41 C ANISOU 1846 CB HIS A1031 7004 9892 9097 87 731 542 C ATOM 1847 CG HIS A1031 77.390 14.017 11.095 1.00 69.84 C ANISOU 1847 CG HIS A1031 7063 10060 9413 205 731 478 C ATOM 1848 ND1 HIS A1031 78.210 14.114 12.203 1.00 70.66 N ANISOU 1848 ND1 HIS A1031 7090 10172 9586 334 584 468 N ATOM 1849 CD2 HIS A1031 77.903 13.094 10.250 1.00 70.82 C ANISOU 1849 CD2 HIS A1031 7125 10171 9612 230 844 398 C ATOM 1850 CE1 HIS A1031 79.188 13.247 12.003 1.00 72.20 C ANISOU 1850 CE1 HIS A1031 7171 10358 9903 449 596 375 C ATOM 1851 NE2 HIS A1031 79.047 12.611 10.840 1.00 72.31 N ANISOU 1851 NE2 HIS A1031 7188 10356 9930 385 761 333 N ATOM 1852 N LEU A1032 78.554 17.316 9.840 1.00 70.55 N ANISOU 1852 N LEU A1032 6981 10318 9507 -160 832 408 N ATOM 1853 CA LEU A1032 79.682 17.583 8.950 1.00 72.22 C ANISOU 1853 CA LEU A1032 7055 10572 9813 -277 994 292 C ATOM 1854 C LEU A1032 80.620 16.376 8.903 1.00 73.53 C ANISOU 1854 C LEU A1032 7033 10766 10139 -163 1026 166 C ATOM 1855 O LEU A1032 81.087 15.916 9.948 1.00 73.90 O ANISOU 1855 O LEU A1032 6969 10820 10290 5 868 128 O ATOM 1856 CB LEU A1032 80.436 18.842 9.411 1.00 73.10 C ANISOU 1856 CB LEU A1032 7061 10712 10002 -378 973 240 C ATOM 1857 CG LEU A1032 81.184 19.608 8.326 1.00 74.88 C ANISOU 1857 CG LEU A1032 7255 10942 10254 -598 1208 153 C ATOM 1858 CD1 LEU A1032 80.375 20.802 7.847 1.00 74.49 C ANISOU 1858 CD1 LEU A1032 7477 10813 10012 -737 1257 278 C ATOM 1859 CD2 LEU A1032 82.532 20.075 8.831 1.00 76.82 C ANISOU 1859 CD2 LEU A1032 7220 11248 10720 -655 1224 -29 C ATOM 1860 N LEU A1033 80.866 15.851 7.691 1.00 76.44 N ANISOU 1860 N LEU A1033 7388 11144 10511 -232 1218 95 N ATOM 1861 CA LEU A1033 81.732 14.692 7.468 1.00 77.95 C ANISOU 1861 CA LEU A1033 7402 11358 10858 -125 1270 -47 C ATOM 1862 C LEU A1033 83.200 15.116 7.421 1.00 80.26 C ANISOU 1862 C LEU A1033 7408 11736 11351 -185 1345 -248 C ATOM 1863 O LEU A1033 83.988 14.687 8.267 1.00 81.63 O ANISOU 1863 O LEU A1033 7377 11945 11694 -13 1197 -364 O ATOM 1864 CB LEU A1033 81.336 13.948 6.177 1.00 77.91 C ANISOU 1864 CB LEU A1033 7500 11332 10770 -179 1452 -61 C ATOM 1865 CG LEU A1033 80.004 13.204 6.195 1.00 76.15 C ANISOU 1865 CG LEU A1033 7487 11033 10413 -102 1388 57 C ATOM 1866 CD1 LEU A1033 79.368 13.203 4.823 1.00 75.83 C ANISOU 1866 CD1 LEU A1033 7595 10999 10217 -225 1547 55 C ATOM 1867 CD2 LEU A1033 80.174 11.784 6.706 1.00 76.61 C ANISOU 1867 CD2 LEU A1033 7499 11027 10583 94 1325 16 C ATOM 1868 N THR A1034 83.559 15.964 6.435 1.00 84.45 N ANISOU 1868 N THR A1034 7937 12295 11856 -426 1579 -306 N ATOM 1869 CA THR A1034 84.909 16.498 6.226 1.00 87.02 C ANISOU 1869 CA THR A1034 7991 12697 12375 -563 1732 -531 C ATOM 1870 C THR A1034 84.871 17.876 5.558 1.00 87.41 C ANISOU 1870 C THR A1034 8188 12711 12313 -856 1946 -492 C ATOM 1871 O THR A1034 83.961 18.161 4.775 1.00 86.26 O ANISOU 1871 O THR A1034 8356 12491 11927 -945 2037 -327 O ATOM 1872 CB THR A1034 85.832 15.479 5.509 1.00 89.06 C ANISOU 1872 CB THR A1034 8028 13016 12796 -527 1889 -751 C ATOM 1873 OG1 THR A1034 87.171 15.975 5.511 1.00 91.90 O ANISOU 1873 OG1 THR A1034 8059 13468 13391 -644 2015 -1022 O ATOM 1874 CG2 THR A1034 85.390 15.163 4.075 1.00 88.81 C ANISOU 1874 CG2 THR A1034 8200 12949 12594 -660 2146 -705 C ATOM 1875 N LYS A1035 85.867 18.723 5.867 1.00 91.64 N ANISOU 1875 N LYS A1035 8506 13289 13023 -998 2023 -662 N ATOM 1876 CA LYS A1035 85.989 20.069 5.302 1.00 92.68 C ANISOU 1876 CA LYS A1035 8786 13353 13075 -1299 2261 -649 C ATOM 1877 C LYS A1035 86.617 20.041 3.898 1.00 94.91 C ANISOU 1877 C LYS A1035 9090 13628 13343 -1533 2659 -778 C ATOM 1878 O LYS A1035 86.575 21.048 3.188 1.00 95.65 O ANISOU 1878 O LYS A1035 9427 13622 13294 -1790 2909 -724 O ATOM 1879 CB LYS A1035 86.779 20.991 6.248 1.00 94.33 C ANISOU 1879 CB LYS A1035 8751 13598 13492 -1380 2200 -804 C ATOM 1880 CG LYS A1035 86.037 21.338 7.536 1.00 92.34 C ANISOU 1880 CG LYS A1035 8576 13326 13183 -1204 1852 -646 C ATOM 1881 CD LYS A1035 85.817 22.837 7.680 1.00 92.10 C ANISOU 1881 CD LYS A1035 8715 13198 13081 -1415 1915 -578 C ATOM 1882 CE LYS A1035 85.065 23.176 8.943 1.00 90.65 C ANISOU 1882 CE LYS A1035 8601 13003 12839 -1241 1582 -440 C ATOM 1883 NZ LYS A1035 84.839 24.639 9.076 1.00 90.46 N ANISOU 1883 NZ LYS A1035 8751 12869 12751 -1435 1639 -383 N ATOM 1884 N SER A1036 87.178 18.877 3.502 1.00 99.15 N ANISOU 1884 N SER A1036 9406 14255 14011 -1437 2724 -945 N ATOM 1885 CA SER A1036 87.830 18.636 2.214 1.00101.57 C ANISOU 1885 CA SER A1036 9691 14579 14323 -1631 3102 -1105 C ATOM 1886 C SER A1036 86.851 18.709 1.028 1.00100.81 C ANISOU 1886 C SER A1036 10062 14376 13865 -1715 3256 -881 C ATOM 1887 O SER A1036 85.751 18.159 1.121 1.00 98.22 O ANISOU 1887 O SER A1036 9934 14020 13365 -1514 3027 -682 O ATOM 1888 CB SER A1036 88.548 17.289 2.228 1.00102.36 C ANISOU 1888 CB SER A1036 9439 14799 14654 -1443 3064 -1336 C ATOM 1889 OG SER A1036 89.305 17.082 1.046 1.00104.53 O ANISOU 1889 OG SER A1036 9637 15109 14971 -1641 3448 -1542 O ATOM 1890 N PRO A1037 87.242 19.352 -0.103 1.00106.20 N ANISOU 1890 N PRO A1037 10931 14996 14424 -2009 3648 -931 N ATOM 1891 CA PRO A1037 86.325 19.448 -1.254 1.00105.97 C ANISOU 1891 CA PRO A1037 11389 14863 14012 -2055 3767 -727 C ATOM 1892 C PRO A1037 86.143 18.150 -2.049 1.00106.01 C ANISOU 1892 C PRO A1037 11389 14936 13954 -1927 3804 -778 C ATOM 1893 O PRO A1037 85.272 18.096 -2.920 1.00105.60 O ANISOU 1893 O PRO A1037 11721 14820 13582 -1906 3825 -621 O ATOM 1894 CB PRO A1037 86.940 20.566 -2.112 1.00109.25 C ANISOU 1894 CB PRO A1037 12026 15169 14315 -2414 4196 -778 C ATOM 1895 CG PRO A1037 88.040 21.169 -1.275 1.00110.88 C ANISOU 1895 CG PRO A1037 11848 15416 14866 -2570 4274 -997 C ATOM 1896 CD PRO A1037 88.497 20.072 -0.379 1.00109.79 C ANISOU 1896 CD PRO A1037 11197 15457 15061 -2319 4011 -1183 C ATOM 1897 N SER A1038 86.948 17.108 -1.752 1.00108.56 N ANISOU 1897 N SER A1038 11287 15384 14577 -1820 3791 -1012 N ATOM 1898 CA SER A1038 86.870 15.803 -2.413 1.00108.76 C ANISOU 1898 CA SER A1038 11266 15467 14591 -1686 3821 -1093 C ATOM 1899 C SER A1038 85.788 14.933 -1.764 1.00105.49 C ANISOU 1899 C SER A1038 10899 15044 14138 -1378 3434 -927 C ATOM 1900 O SER A1038 85.770 14.786 -0.538 1.00104.14 O ANISOU 1900 O SER A1038 10530 14891 14148 -1209 3156 -907 O ATOM 1901 CB SER A1038 88.222 15.097 -2.372 1.00111.36 C ANISOU 1901 CB SER A1038 11127 15915 15270 -1690 3972 -1436 C ATOM 1902 OG SER A1038 89.213 15.840 -3.062 1.00114.76 O ANISOU 1902 OG SER A1038 11500 16357 15747 -2014 4390 -1631 O ATOM 1903 N LEU A1039 84.880 14.374 -2.590 1.00105.30 N ANISOU 1903 N LEU A1039 11152 14989 13868 -1316 3428 -824 N ATOM 1904 CA LEU A1039 83.768 13.518 -2.157 1.00102.57 C ANISOU 1904 CA LEU A1039 10878 14622 13471 -1072 3126 -698 C ATOM 1905 C LEU A1039 84.245 12.173 -1.583 1.00102.24 C ANISOU 1905 C LEU A1039 10517 14621 13709 -868 3017 -845 C ATOM 1906 O LEU A1039 83.616 11.652 -0.660 1.00100.11 O ANISOU 1906 O LEU A1039 10231 14312 13494 -674 2745 -746 O ATOM 1907 CB LEU A1039 82.760 13.318 -3.316 1.00102.45 C ANISOU 1907 CB LEU A1039 11218 14576 13132 -1081 3175 -613 C ATOM 1908 CG LEU A1039 81.536 12.406 -3.088 1.00 99.84 C ANISOU 1908 CG LEU A1039 10965 14227 12743 -875 2918 -536 C ATOM 1909 CD1 LEU A1039 80.536 13.023 -2.120 1.00100.03 C ANISOU 1909 CD1 LEU A1039 11085 14205 12717 -793 2637 -350 C ATOM 1910 CD2 LEU A1039 80.846 12.100 -4.391 1.00 99.22 C ANISOU 1910 CD2 LEU A1039 11162 14151 12386 -893 3003 -549 C ATOM 1911 N ASN A1040 85.364 11.632 -2.114 1.00105.29 N ANISOU 1911 N ASN A1040 10666 15071 14268 -910 3236 -1088 N ATOM 1912 CA ASN A1040 85.962 10.363 -1.678 1.00105.65 C ANISOU 1912 CA ASN A1040 10414 15143 14585 -695 3144 -1262 C ATOM 1913 C ASN A1040 86.404 10.381 -0.209 1.00105.25 C ANISOU 1913 C ASN A1040 10118 15097 14776 -518 2876 -1276 C ATOM 1914 O ASN A1040 86.386 9.334 0.442 1.00104.82 O ANISOU 1914 O ASN A1040 9968 15002 14856 -265 2676 -1301 O ATOM 1915 CB ASN A1040 87.117 9.964 -2.594 1.00108.67 C ANISOU 1915 CB ASN A1040 10576 15607 15106 -792 3452 -1554 C ATOM 1916 CG ASN A1040 86.678 9.610 -3.992 1.00109.24 C ANISOU 1916 CG ASN A1040 10895 15672 14940 -899 3683 -1563 C ATOM 1917 OD1 ASN A1040 86.202 8.502 -4.261 1.00108.25 O ANISOU 1917 OD1 ASN A1040 10821 15514 14795 -746 3610 -1575 O ATOM 1918 ND2 ASN A1040 86.826 10.548 -4.915 1.00111.11 N ANISOU 1918 ND2 ASN A1040 11315 15925 14977 -1166 3974 -1562 N ATOM 1919 N ALA A1041 86.780 11.569 0.309 1.00106.31 N ANISOU 1919 N ALA A1041 10183 15263 14947 -646 2871 -1260 N ATOM 1920 CA ALA A1041 87.197 11.777 1.698 1.00106.16 C ANISOU 1920 CA ALA A1041 9949 15263 15124 -493 2607 -1283 C ATOM 1921 C ALA A1041 86.008 11.651 2.659 1.00103.21 C ANISOU 1921 C ALA A1041 9807 14794 14614 -320 2297 -1011 C ATOM 1922 O ALA A1041 86.188 11.194 3.790 1.00103.10 O ANISOU 1922 O ALA A1041 9676 14764 14733 -87 2041 -1019 O ATOM 1923 CB ALA A1041 87.850 13.142 1.849 1.00107.36 C ANISOU 1923 CB ALA A1041 9986 15470 15336 -721 2726 -1357 C ATOM 1924 N ALA A1042 84.800 12.051 2.206 1.00101.61 N ANISOU 1924 N ALA A1042 9939 14529 14139 -425 2322 -791 N ATOM 1925 CA ALA A1042 83.563 11.983 2.987 1.00 99.03 C ANISOU 1925 CA ALA A1042 9830 14120 13677 -304 2080 -563 C ATOM 1926 C ALA A1042 83.084 10.540 3.167 1.00 98.71 C ANISOU 1926 C ALA A1042 9833 14006 13666 -96 1978 -553 C ATOM 1927 O ALA A1042 82.588 10.200 4.243 1.00 98.01 O ANISOU 1927 O ALA A1042 9804 13846 13589 64 1764 -445 O ATOM 1928 CB ALA A1042 82.478 12.823 2.331 1.00 97.57 C ANISOU 1928 CB ALA A1042 9950 13906 13217 -465 2139 -396 C ATOM 1929 N LYS A1043 83.243 9.696 2.121 1.00100.32 N ANISOU 1929 N LYS A1043 10028 14214 13875 -109 2151 -671 N ATOM 1930 CA LYS A1043 82.859 8.280 2.129 1.00100.43 C ANISOU 1930 CA LYS A1043 10091 14137 13931 63 2101 -692 C ATOM 1931 C LYS A1043 83.701 7.461 3.108 1.00101.79 C ANISOU 1931 C LYS A1043 10078 14264 14334 312 1947 -786 C ATOM 1932 O LYS A1043 83.173 6.547 3.742 1.00101.39 O ANISOU 1932 O LYS A1043 10154 14081 14289 487 1814 -709 O ATOM 1933 CB LYS A1043 82.933 7.681 0.718 1.00101.70 C ANISOU 1933 CB LYS A1043 10272 14324 14045 -22 2333 -826 C ATOM 1934 CG LYS A1043 81.572 7.567 0.044 1.00100.39 C ANISOU 1934 CG LYS A1043 10378 14118 13648 -95 2354 -722 C ATOM 1935 CD LYS A1043 81.662 6.927 -1.341 1.00101.75 C ANISOU 1935 CD LYS A1043 10580 14322 13758 -162 2568 -873 C ATOM 1936 CE LYS A1043 81.681 7.937 -2.468 1.00101.93 C ANISOU 1936 CE LYS A1043 10731 14437 13562 -370 2747 -874 C ATOM 1937 NZ LYS A1043 80.347 8.559 -2.686 1.00100.12 N ANISOU 1937 NZ LYS A1043 10776 14194 13071 -420 2643 -719 N ATOM 1938 N SER A1044 85.001 7.801 3.238 1.00104.35 N ANISOU 1938 N SER A1044 10115 14688 14845 332 1966 -967 N ATOM 1939 CA SER A1044 85.941 7.147 4.153 1.00106.18 C ANISOU 1939 CA SER A1044 10137 14903 15303 606 1779 -1104 C ATOM 1940 C SER A1044 85.600 7.478 5.612 1.00104.98 C ANISOU 1940 C SER A1044 10084 14691 15113 754 1492 -937 C ATOM 1941 O SER A1044 85.796 6.637 6.492 1.00105.75 O ANISOU 1941 O SER A1044 10211 14688 15282 1038 1285 -938 O ATOM 1942 CB SER A1044 87.373 7.568 3.836 1.00108.78 C ANISOU 1942 CB SER A1044 10091 15389 15851 555 1886 -1393 C ATOM 1943 OG SER A1044 88.315 6.842 4.608 1.00110.93 O ANISOU 1943 OG SER A1044 10134 15659 16355 864 1680 -1580 O ATOM 1944 N GLU A1045 85.081 8.699 5.857 1.00103.28 N ANISOU 1944 N GLU A1045 9953 14523 14766 572 1482 -793 N ATOM 1945 CA GLU A1045 84.674 9.182 7.179 1.00102.11 C ANISOU 1945 CA GLU A1045 9910 14333 14554 670 1239 -636 C ATOM 1946 C GLU A1045 83.302 8.631 7.577 1.00100.05 C ANISOU 1946 C GLU A1045 9987 13918 14109 718 1175 -405 C ATOM 1947 O GLU A1045 83.083 8.353 8.758 1.00 99.85 O ANISOU 1947 O GLU A1045 10083 13801 14054 902 974 -305 O ATOM 1948 CB GLU A1045 84.670 10.720 7.226 1.00101.34 C ANISOU 1948 CB GLU A1045 9763 14338 14404 445 1275 -599 C ATOM 1949 CG GLU A1045 86.053 11.352 7.249 1.00103.76 C ANISOU 1949 CG GLU A1045 9721 14781 14922 404 1302 -845 C ATOM 1950 CD GLU A1045 86.754 11.319 8.593 1.00105.30 C ANISOU 1950 CD GLU A1045 9749 15004 15257 655 1007 -937 C ATOM 1951 OE1 GLU A1045 86.611 12.297 9.361 1.00105.71 O ANISOU 1951 OE1 GLU A1045 9815 15085 15265 605 886 -869 O ATOM 1952 OE2 GLU A1045 87.455 10.320 8.875 1.00106.42 O ANISOU 1952 OE2 GLU A1045 9755 15135 15545 920 882 -1090 O ATOM 1953 N LEU A1046 82.385 8.480 6.594 1.00 98.89 N ANISOU 1953 N LEU A1046 9996 13745 13833 551 1353 -341 N ATOM 1954 CA LEU A1046 81.025 7.962 6.787 1.00 97.25 C ANISOU 1954 CA LEU A1046 10063 13409 13478 548 1341 -184 C ATOM 1955 C LEU A1046 81.033 6.495 7.235 1.00 98.36 C ANISOU 1955 C LEU A1046 10308 13380 13685 764 1293 -194 C ATOM 1956 O LEU A1046 80.254 6.129 8.118 1.00 97.77 O ANISOU 1956 O LEU A1046 10452 13168 13529 834 1210 -59 O ATOM 1957 CB LEU A1046 80.185 8.156 5.505 1.00 96.25 C ANISOU 1957 CB LEU A1046 10027 13324 13220 338 1524 -183 C ATOM 1958 CG LEU A1046 78.685 7.801 5.547 1.00 94.80 C ANISOU 1958 CG LEU A1046 10072 13049 12899 290 1526 -82 C ATOM 1959 CD1 LEU A1046 77.920 8.673 6.536 1.00 93.29 C ANISOU 1959 CD1 LEU A1046 9984 12854 12609 261 1391 65 C ATOM 1960 CD2 LEU A1046 78.063 7.945 4.175 1.00 94.39 C ANISOU 1960 CD2 LEU A1046 10070 13064 12730 131 1671 -141 C ATOM 1961 N ASP A1047 81.921 5.670 6.641 1.00101.80 N ANISOU 1961 N ASP A1047 10605 13809 14265 867 1359 -362 N ATOM 1962 CA ASP A1047 82.080 4.254 6.987 1.00103.43 C ANISOU 1962 CA ASP A1047 10921 13830 14548 1100 1313 -391 C ATOM 1963 C ASP A1047 82.729 4.117 8.368 1.00104.80 C ANISOU 1963 C ASP A1047 11117 13930 14772 1379 1059 -357 C ATOM 1964 O ASP A1047 82.416 3.180 9.102 1.00105.72 O ANISOU 1964 O ASP A1047 11487 13833 14849 1564 979 -268 O ATOM 1965 CB ASP A1047 82.924 3.516 5.929 1.00105.36 C ANISOU 1965 CB ASP A1047 10982 14106 14944 1144 1445 -610 C ATOM 1966 CG ASP A1047 82.354 3.504 4.520 1.00105.21 C ANISOU 1966 CG ASP A1047 10970 14151 14853 904 1688 -665 C ATOM 1967 OD1 ASP A1047 81.116 3.393 4.376 1.00103.42 O ANISOU 1967 OD1 ASP A1047 10957 13855 14483 780 1744 -550 O ATOM 1968 OD2 ASP A1047 83.151 3.545 3.559 1.00107.15 O ANISOU 1968 OD2 ASP A1047 11009 14516 15187 850 1824 -848 O ATOM 1969 N LYS A1048 83.626 5.063 8.713 1.00105.39 N ANISOU 1969 N LYS A1048 10947 14173 14924 1406 938 -439 N ATOM 1970 CA LYS A1048 84.340 5.120 9.990 1.00106.90 C ANISOU 1970 CA LYS A1048 11112 14345 15161 1679 659 -451 C ATOM 1971 C LYS A1048 83.399 5.520 11.135 1.00105.37 C ANISOU 1971 C LYS A1048 11208 14059 14769 1677 540 -212 C ATOM 1972 O LYS A1048 83.601 5.083 12.269 1.00106.80 O ANISOU 1972 O LYS A1048 11557 14117 14905 1946 326 -154 O ATOM 1973 CB LYS A1048 85.513 6.107 9.893 1.00107.78 C ANISOU 1973 CB LYS A1048 10831 14688 15433 1648 602 -658 C ATOM 1974 CG LYS A1048 86.697 5.750 10.780 1.00110.77 C ANISOU 1974 CG LYS A1048 11045 15080 15963 2006 320 -833 C ATOM 1975 CD LYS A1048 87.863 6.708 10.562 1.00112.37 C ANISOU 1975 CD LYS A1048 10798 15527 16370 1929 311 -1106 C ATOM 1976 CE LYS A1048 89.116 6.281 11.289 1.00115.81 C ANISOU 1976 CE LYS A1048 10994 16009 17000 2304 23 -1365 C ATOM 1977 NZ LYS A1048 89.796 5.141 10.616 1.00118.29 N ANISOU 1977 NZ LYS A1048 11172 16285 17487 2483 76 -1578 N ATOM 1978 N ALA A1049 82.377 6.348 10.832 1.00102.08 N ANISOU 1978 N ALA A1049 10864 13698 14224 1388 674 -86 N ATOM 1979 CA ALA A1049 81.387 6.836 11.796 1.00100.55 C ANISOU 1979 CA ALA A1049 10910 13442 13852 1338 603 112 C ATOM 1980 C ALA A1049 80.289 5.813 12.108 1.00 99.97 C ANISOU 1980 C ALA A1049 11191 13138 13655 1355 689 251 C ATOM 1981 O ALA A1049 79.781 5.799 13.231 1.00 99.32 O ANISOU 1981 O ALA A1049 11354 12942 13441 1426 601 390 O ATOM 1982 CB ALA A1049 80.767 8.131 11.297 1.00 98.41 C ANISOU 1982 CB ALA A1049 10555 13323 13513 1047 702 152 C ATOM 1983 N ILE A1050 79.919 4.970 11.122 1.00100.45 N ANISOU 1983 N ILE A1050 11285 13125 13757 1271 882 198 N ATOM 1984 CA ILE A1050 78.877 3.948 11.272 1.00100.31 C ANISOU 1984 CA ILE A1050 11576 12880 13658 1242 1013 283 C ATOM 1985 C ILE A1050 79.478 2.580 11.641 1.00102.91 C ANISOU 1985 C ILE A1050 12082 12977 14042 1517 967 264 C ATOM 1986 O ILE A1050 79.184 2.054 12.715 1.00103.71 O ANISOU 1986 O ILE A1050 12507 12864 14035 1654 911 393 O ATOM 1987 CB ILE A1050 77.926 3.893 10.029 1.00 98.67 C ANISOU 1987 CB ILE A1050 11321 12723 13446 972 1242 221 C ATOM 1988 CG1 ILE A1050 77.263 5.270 9.714 1.00 96.43 C ANISOU 1988 CG1 ILE A1050 10921 12641 13077 745 1252 248 C ATOM 1989 CG2 ILE A1050 76.890 2.758 10.129 1.00 99.08 C ANISOU 1989 CG2 ILE A1050 11651 12537 13458 920 1404 250 C ATOM 1990 CD1 ILE A1050 76.224 5.842 10.761 1.00 95.46 C ANISOU 1990 CD1 ILE A1050 10973 12478 12819 670 1210 382 C ATOM 1991 N GLY A1051 80.300 2.030 10.747 1.00104.34 N ANISOU 1991 N GLY A1051 12075 13191 14378 1599 1001 102 N ATOM 1992 CA GLY A1051 80.947 0.734 10.923 1.00107.12 C ANISOU 1992 CA GLY A1051 12565 13328 14808 1882 950 49 C ATOM 1993 C GLY A1051 80.561 -0.293 9.876 1.00107.58 C ANISOU 1993 C GLY A1051 12669 13268 14938 1788 1177 -42 C ATOM 1994 O GLY A1051 80.656 -1.498 10.128 1.00109.87 O ANISOU 1994 O GLY A1051 13200 13293 15253 1978 1187 -40 O ATOM 1995 N ARG A1052 80.125 0.178 8.690 1.00105.40 N ANISOU 1995 N ARG A1052 12188 13175 14684 1505 1355 -128 N ATOM 1996 CA ARG A1052 79.709 -0.652 7.552 1.00105.63 C ANISOU 1996 CA ARG A1052 12221 13142 14771 1383 1572 -247 C ATOM 1997 C ARG A1052 79.943 0.070 6.215 1.00104.40 C ANISOU 1997 C ARG A1052 11747 13266 14655 1193 1673 -394 C ATOM 1998 O ARG A1052 80.114 1.291 6.204 1.00102.91 O ANISOU 1998 O ARG A1052 11391 13289 14421 1094 1612 -366 O ATOM 1999 CB ARG A1052 78.230 -1.085 7.693 1.00104.85 C ANISOU 1999 CB ARG A1052 12400 12871 14568 1188 1737 -161 C ATOM 2000 CG ARG A1052 77.209 0.043 7.516 1.00102.21 C ANISOU 2000 CG ARG A1052 11991 12726 14118 913 1781 -114 C ATOM 2001 CD ARG A1052 75.806 -0.488 7.307 1.00101.90 C ANISOU 2001 CD ARG A1052 12122 12561 14035 704 1972 -138 C ATOM 2002 NE ARG A1052 74.884 0.558 6.857 1.00 99.78 N ANISOU 2002 NE ARG A1052 11725 12508 13679 474 1993 -161 N ATOM 2003 CZ ARG A1052 74.590 0.807 5.584 1.00 99.27 C ANISOU 2003 CZ ARG A1052 11492 12615 13612 335 2063 -306 C ATOM 2004 NH1 ARG A1052 75.143 0.089 4.614 1.00100.57 N ANISOU 2004 NH1 ARG A1052 11580 12773 13860 376 2144 -445 N ATOM 2005 NH2 ARG A1052 73.740 1.776 5.271 1.00 97.68 N ANISOU 2005 NH2 ARG A1052 11215 12588 13311 175 2041 -321 N ATOM 2006 N ASN A1053 79.923 -0.681 5.093 1.00105.28 N ANISOU 2006 N ASN A1053 11809 13358 14834 1135 1839 -549 N ATOM 2007 CA ASN A1053 80.085 -0.121 3.749 1.00104.58 C ANISOU 2007 CA ASN A1053 11491 13504 14741 955 1965 -689 C ATOM 2008 C ASN A1053 78.781 0.581 3.348 1.00102.38 C ANISOU 2008 C ASN A1053 11290 13316 14294 694 2038 -622 C ATOM 2009 O ASN A1053 77.797 -0.076 2.997 1.00102.26 O ANISOU 2009 O ASN A1053 11412 13198 14245 598 2145 -659 O ATOM 2010 CB ASN A1053 80.485 -1.206 2.739 1.00106.47 C ANISOU 2010 CB ASN A1053 11675 13687 15092 1001 2109 -889 C ATOM 2011 CG ASN A1053 81.834 -1.824 3.009 1.00108.94 C ANISOU 2011 CG ASN A1053 11865 13940 15587 1279 2025 -1004 C ATOM 2012 OD1 ASN A1053 81.945 -2.886 3.630 1.00110.85 O ANISOU 2012 OD1 ASN A1053 12282 13933 15903 1494 1964 -990 O ATOM 2013 ND2 ASN A1053 82.892 -1.179 2.538 1.00109.30 N ANISOU 2013 ND2 ASN A1053 11613 14203 15713 1285 2025 -1138 N ATOM 2014 N THR A1054 78.769 1.921 3.466 1.00101.00 N ANISOU 2014 N THR A1054 11026 13325 14025 594 1967 -540 N ATOM 2015 CA THR A1054 77.609 2.776 3.188 1.00 99.11 C ANISOU 2015 CA THR A1054 10853 13184 13621 393 1981 -477 C ATOM 2016 C THR A1054 77.387 3.045 1.700 1.00 99.19 C ANISOU 2016 C THR A1054 10805 13343 13540 243 2107 -605 C ATOM 2017 O THR A1054 76.237 3.063 1.256 1.00 98.63 O ANISOU 2017 O THR A1054 10828 13286 13361 130 2136 -634 O ATOM 2018 CB THR A1054 77.701 4.092 3.976 1.00 97.77 C ANISOU 2018 CB THR A1054 10650 13116 13383 373 1841 -334 C ATOM 2019 OG1 THR A1054 78.916 4.757 3.630 1.00 98.55 O ANISOU 2019 OG1 THR A1054 10555 13356 13534 386 1840 -389 O ATOM 2020 CG2 THR A1054 77.620 3.885 5.486 1.00 97.53 C ANISOU 2020 CG2 THR A1054 10737 12939 13381 507 1706 -198 C ATOM 2021 N ASN A1055 78.483 3.301 0.947 1.00101.53 N ANISOU 2021 N ASN A1055 10949 13758 13870 245 2182 -700 N ATOM 2022 CA ASN A1055 78.505 3.610 -0.493 1.00102.08 C ANISOU 2022 CA ASN A1055 10997 13967 13822 113 2324 -818 C ATOM 2023 C ASN A1055 77.838 4.942 -0.902 1.00100.75 C ANISOU 2023 C ASN A1055 10920 13930 13431 -34 2291 -732 C ATOM 2024 O ASN A1055 77.864 5.297 -2.084 1.00101.25 O ANISOU 2024 O ASN A1055 11026 14096 13349 -130 2400 -809 O ATOM 2025 CB ASN A1055 78.028 2.421 -1.355 1.00103.12 C ANISOU 2025 CB ASN A1055 11186 14033 13961 108 2438 -976 C ATOM 2026 CG ASN A1055 78.935 1.206 -1.344 1.00104.89 C ANISOU 2026 CG ASN A1055 11319 14146 14389 250 2512 -1103 C ATOM 2027 OD1 ASN A1055 79.947 1.136 -0.633 1.00105.62 O ANISOU 2027 OD1 ASN A1055 11294 14204 14632 387 2456 -1087 O ATOM 2028 ND2 ASN A1055 78.585 0.210 -2.144 1.00105.89 N ANISOU 2028 ND2 ASN A1055 11492 14213 14528 237 2623 -1256 N ATOM 2029 N GLY A1056 77.288 5.671 0.071 1.00 97.30 N ANISOU 2029 N GLY A1056 10536 13477 12957 -35 2142 -577 N ATOM 2030 CA GLY A1056 76.643 6.960 -0.158 1.00 96.15 C ANISOU 2030 CA GLY A1056 10489 13429 12615 -138 2077 -490 C ATOM 2031 C GLY A1056 75.342 7.193 0.586 1.00 94.62 C ANISOU 2031 C GLY A1056 10391 13196 12364 -137 1930 -408 C ATOM 2032 O GLY A1056 75.082 8.317 1.025 1.00 93.74 O ANISOU 2032 O GLY A1056 10321 13131 12165 -168 1826 -297 O ATOM 2033 N VAL A1057 74.504 6.145 0.713 1.00 92.08 N ANISOU 2033 N VAL A1057 10102 12783 12101 -115 1939 -485 N ATOM 2034 CA VAL A1057 73.190 6.225 1.367 1.00 91.05 C ANISOU 2034 CA VAL A1057 10038 12616 11942 -142 1846 -466 C ATOM 2035 C VAL A1057 73.180 5.495 2.722 1.00 90.93 C ANISOU 2035 C VAL A1057 10042 12432 12076 -84 1843 -392 C ATOM 2036 O VAL A1057 73.674 4.370 2.822 1.00 92.05 O ANISOU 2036 O VAL A1057 10188 12445 12341 -22 1932 -434 O ATOM 2037 CB VAL A1057 72.034 5.743 0.435 1.00 91.56 C ANISOU 2037 CB VAL A1057 10137 12717 11934 -200 1872 -655 C ATOM 2038 CG1 VAL A1057 70.662 6.098 1.009 1.00 91.08 C ANISOU 2038 CG1 VAL A1057 10097 12661 11848 -242 1773 -684 C ATOM 2039 CG2 VAL A1057 72.177 6.307 -0.978 1.00 91.76 C ANISOU 2039 CG2 VAL A1057 10203 12889 11772 -219 1872 -728 C ATOM 2040 N ILE A1058 72.602 6.146 3.752 1.00 86.68 N ANISOU 2040 N ILE A1058 9545 11881 11508 -96 1743 -283 N ATOM 2041 CA ILE A1058 72.444 5.616 5.115 1.00 86.75 C ANISOU 2041 CA ILE A1058 9635 11726 11600 -51 1741 -195 C ATOM 2042 C ILE A1058 70.945 5.418 5.447 1.00 86.58 C ANISOU 2042 C ILE A1058 9676 11659 11561 -160 1781 -274 C ATOM 2043 O ILE A1058 70.108 5.528 4.548 1.00 86.57 O ANISOU 2043 O ILE A1058 9622 11758 11513 -242 1791 -430 O ATOM 2044 CB ILE A1058 73.207 6.468 6.180 1.00 86.12 C ANISOU 2044 CB ILE A1058 9549 11662 11511 33 1612 -20 C ATOM 2045 CG1 ILE A1058 72.763 7.953 6.175 1.00 84.82 C ANISOU 2045 CG1 ILE A1058 9349 11650 11228 -35 1497 30 C ATOM 2046 CG2 ILE A1058 74.724 6.322 6.023 1.00 87.19 C ANISOU 2046 CG2 ILE A1058 9593 11807 11729 150 1599 -4 C ATOM 2047 CD1 ILE A1058 72.783 8.636 7.545 1.00 83.93 C ANISOU 2047 CD1 ILE A1058 9276 11514 11100 7 1381 170 C ATOM 2048 N THR A1059 70.611 5.108 6.718 1.00 85.34 N ANISOU 2048 N THR A1059 9635 11353 11437 -158 1809 -191 N ATOM 2049 CA THR A1059 69.223 4.913 7.159 1.00 85.59 C ANISOU 2049 CA THR A1059 9714 11332 11474 -290 1892 -289 C ATOM 2050 C THR A1059 68.800 5.886 8.273 1.00 84.69 C ANISOU 2050 C THR A1059 9633 11254 11292 -302 1802 -180 C ATOM 2051 O THR A1059 69.662 6.493 8.911 1.00 84.15 O ANISOU 2051 O THR A1059 9594 11198 11181 -195 1684 -4 O ATOM 2052 CB THR A1059 68.904 3.425 7.420 1.00 87.37 C ANISOU 2052 CB THR A1059 10078 11317 11802 -344 2104 -367 C ATOM 2053 OG1 THR A1059 67.493 3.274 7.578 1.00 87.92 O ANISOU 2053 OG1 THR A1059 10136 11370 11900 -520 2221 -537 O ATOM 2054 CG2 THR A1059 69.628 2.857 8.638 1.00 88.22 C ANISOU 2054 CG2 THR A1059 10406 11197 11917 -231 2137 -173 C ATOM 2055 N LYS A1060 67.471 6.031 8.488 1.00 84.03 N ANISOU 2055 N LYS A1060 9522 11196 11210 -435 1857 -318 N ATOM 2056 CA LYS A1060 66.839 6.897 9.496 1.00 83.48 C ANISOU 2056 CA LYS A1060 9467 11165 11086 -471 1801 -272 C ATOM 2057 C LYS A1060 67.376 6.627 10.913 1.00 83.81 C ANISOU 2057 C LYS A1060 9716 11029 11099 -414 1845 -68 C ATOM 2058 O LYS A1060 67.648 7.574 11.654 1.00 82.87 O ANISOU 2058 O LYS A1060 9610 10973 10904 -350 1709 64 O ATOM 2059 CB LYS A1060 65.303 6.737 9.437 1.00 84.51 C ANISOU 2059 CB LYS A1060 9514 11324 11273 -637 1915 -527 C ATOM 2060 CG LYS A1060 64.511 7.589 10.432 1.00 84.28 C ANISOU 2060 CG LYS A1060 9474 11342 11207 -691 1888 -535 C ATOM 2061 CD LYS A1060 63.886 6.727 11.527 1.00 86.01 C ANISOU 2061 CD LYS A1060 9849 11354 11477 -837 2154 -573 C ATOM 2062 CE LYS A1060 63.321 7.551 12.656 1.00 85.90 C ANISOU 2062 CE LYS A1060 9864 11370 11404 -877 2146 -542 C ATOM 2063 NZ LYS A1060 62.836 6.694 13.769 1.00 87.79 N ANISOU 2063 NZ LYS A1060 10324 11377 11655 -1026 2444 -547 N ATOM 2064 N ASP A1061 67.525 5.338 11.272 1.00 86.07 N ANISOU 2064 N ASP A1061 10188 11082 11433 -425 2027 -49 N ATOM 2065 CA ASP A1061 68.025 4.885 12.572 1.00 87.07 C ANISOU 2065 CA ASP A1061 10588 10995 11500 -339 2073 141 C ATOM 2066 C ASP A1061 69.512 5.210 12.748 1.00 86.55 C ANISOU 2066 C ASP A1061 10531 10959 11394 -106 1859 325 C ATOM 2067 O ASP A1061 69.927 5.576 13.849 1.00 86.58 O ANISOU 2067 O ASP A1061 10671 10918 11308 1 1763 477 O ATOM 2068 CB ASP A1061 67.758 3.381 12.763 1.00 89.41 C ANISOU 2068 CB ASP A1061 11123 11001 11848 -407 2334 99 C ATOM 2069 CG ASP A1061 66.325 2.955 12.483 1.00 90.46 C ANISOU 2069 CG ASP A1061 11202 11104 12065 -669 2578 -146 C ATOM 2070 OD1 ASP A1061 65.395 3.579 13.046 1.00 90.13 O ANISOU 2070 OD1 ASP A1061 11118 11134 11993 -798 2625 -215 O ATOM 2071 OD2 ASP A1061 66.134 1.977 11.727 1.00 91.92 O ANISOU 2071 OD2 ASP A1061 11377 11192 12357 -746 2730 -293 O ATOM 2072 N GLU A1062 70.304 5.090 11.660 1.00 84.36 N ANISOU 2072 N GLU A1062 10096 10769 11188 -32 1791 281 N ATOM 2073 CA GLU A1062 71.737 5.404 11.649 1.00 84.17 C ANISOU 2073 CA GLU A1062 10006 10805 11170 164 1611 385 C ATOM 2074 C GLU A1062 71.960 6.917 11.694 1.00 82.47 C ANISOU 2074 C GLU A1062 9619 10813 10902 163 1430 429 C ATOM 2075 O GLU A1062 72.950 7.369 12.272 1.00 82.53 O ANISOU 2075 O GLU A1062 9610 10851 10896 304 1278 526 O ATOM 2076 CB GLU A1062 72.430 4.783 10.428 1.00 84.66 C ANISOU 2076 CB GLU A1062 9945 10889 11333 207 1646 287 C ATOM 2077 CG GLU A1062 72.779 3.314 10.618 1.00 86.76 C ANISOU 2077 CG GLU A1062 10404 10901 11660 308 1757 288 C ATOM 2078 CD GLU A1062 73.228 2.547 9.387 1.00 87.47 C ANISOU 2078 CD GLU A1062 10385 10991 11859 324 1833 154 C ATOM 2079 OE1 GLU A1062 73.036 3.047 8.254 1.00 86.40 O ANISOU 2079 OE1 GLU A1062 10044 11050 11734 215 1844 39 O ATOM 2080 OE2 GLU A1062 73.750 1.422 9.559 1.00 89.34 O ANISOU 2080 OE2 GLU A1062 10770 11020 12155 458 1884 160 O ATOM 2081 N ALA A1063 71.029 7.695 11.095 1.00 80.90 N ANISOU 2081 N ALA A1063 9300 10763 10676 14 1439 338 N ATOM 2082 CA ALA A1063 71.049 9.161 11.084 1.00 79.47 C ANISOU 2082 CA ALA A1063 9000 10762 10434 -2 1286 372 C ATOM 2083 C ALA A1063 70.726 9.691 12.484 1.00 79.26 C ANISOU 2083 C ALA A1063 9078 10699 10338 14 1223 469 C ATOM 2084 O ALA A1063 71.262 10.725 12.887 1.00 78.57 O ANISOU 2084 O ALA A1063 8936 10703 10214 68 1072 546 O ATOM 2085 CB ALA A1063 70.042 9.693 10.077 1.00 78.78 C ANISOU 2085 CB ALA A1063 8809 10805 10319 -123 1298 235 C ATOM 2086 N GLU A1064 69.860 8.965 13.224 1.00 80.64 N ANISOU 2086 N GLU A1064 9416 10731 10493 -47 1362 453 N ATOM 2087 CA GLU A1064 69.466 9.267 14.600 1.00 80.92 C ANISOU 2087 CA GLU A1064 9604 10702 10440 -46 1356 534 C ATOM 2088 C GLU A1064 70.654 8.981 15.529 1.00 81.80 C ANISOU 2088 C GLU A1064 9872 10707 10502 149 1250 696 C ATOM 2089 O GLU A1064 70.864 9.719 16.493 1.00 81.49 O ANISOU 2089 O GLU A1064 9882 10702 10378 215 1124 781 O ATOM 2090 CB GLU A1064 68.241 8.424 14.998 1.00 82.18 C ANISOU 2090 CB GLU A1064 9913 10714 10598 -196 1598 444 C ATOM 2091 CG GLU A1064 67.556 8.874 16.280 1.00 82.60 C ANISOU 2091 CG GLU A1064 10106 10727 10551 -250 1641 482 C ATOM 2092 CD GLU A1064 66.298 8.120 16.670 1.00 84.08 C ANISOU 2092 CD GLU A1064 10417 10779 10750 -448 1930 351 C ATOM 2093 OE1 GLU A1064 66.228 6.893 16.427 1.00 85.29 O ANISOU 2093 OE1 GLU A1064 10699 10751 10956 -504 2126 312 O ATOM 2094 OE2 GLU A1064 65.393 8.754 17.260 1.00 84.25 O ANISOU 2094 OE2 GLU A1064 10411 10864 10736 -555 1978 275 O ATOM 2095 N LYS A1065 71.434 7.920 15.217 1.00 83.05 N ANISOU 2095 N LYS A1065 10100 10741 10715 261 1283 715 N ATOM 2096 CA LYS A1065 72.631 7.506 15.954 1.00 84.44 C ANISOU 2096 CA LYS A1065 10410 10813 10860 498 1149 827 C ATOM 2097 C LYS A1065 73.748 8.546 15.784 1.00 83.62 C ANISOU 2097 C LYS A1065 10062 10908 10802 607 916 828 C ATOM 2098 O LYS A1065 74.451 8.842 16.752 1.00 84.31 O ANISOU 2098 O LYS A1065 10214 10990 10830 773 743 899 O ATOM 2099 CB LYS A1065 73.099 6.116 15.487 1.00 86.20 C ANISOU 2099 CB LYS A1065 10739 10857 11155 592 1244 805 C ATOM 2100 CG LYS A1065 74.085 5.442 16.436 1.00 88.42 C ANISOU 2100 CG LYS A1065 11258 10963 11375 871 1117 913 C ATOM 2101 CD LYS A1065 74.681 4.184 15.824 1.00 90.22 C ANISOU 2101 CD LYS A1065 11539 11038 11703 996 1171 867 C ATOM 2102 CE LYS A1065 75.760 3.592 16.696 1.00 92.41 C ANISOU 2102 CE LYS A1065 12024 11162 11925 1333 980 948 C ATOM 2103 NZ LYS A1065 76.393 2.409 16.057 1.00 94.35 N ANISOU 2103 NZ LYS A1065 12299 11264 12286 1482 1012 881 N ATOM 2104 N LEU A1066 73.900 9.101 14.558 1.00 81.22 N ANISOU 2104 N LEU A1066 9495 10772 10593 507 921 735 N ATOM 2105 CA LEU A1066 74.888 10.138 14.243 1.00 80.69 C ANISOU 2105 CA LEU A1066 9195 10881 10582 545 768 710 C ATOM 2106 C LEU A1066 74.523 11.454 14.922 1.00 79.49 C ANISOU 2106 C LEU A1066 9019 10831 10352 486 661 755 C ATOM 2107 O LEU A1066 75.417 12.182 15.354 1.00 79.73 O ANISOU 2107 O LEU A1066 8946 10943 10405 568 504 760 O ATOM 2108 CB LEU A1066 75.011 10.354 12.725 1.00 80.11 C ANISOU 2108 CB LEU A1066 8926 10923 10589 426 855 609 C ATOM 2109 CG LEU A1066 76.019 9.486 11.972 1.00 81.35 C ANISOU 2109 CG LEU A1066 8986 11060 10863 518 897 532 C ATOM 2110 CD1 LEU A1066 75.814 9.608 10.476 1.00 80.85 C ANISOU 2110 CD1 LEU A1066 8802 11091 10826 371 1026 436 C ATOM 2111 CD2 LEU A1066 77.458 9.859 12.320 1.00 82.01 C ANISOU 2111 CD2 LEU A1066 8911 11216 11033 663 744 501 C ATOM 2112 N PHE A1067 73.207 11.754 15.011 1.00 77.67 N ANISOU 2112 N PHE A1067 8866 10598 10046 344 745 756 N ATOM 2113 CA PHE A1067 72.674 12.959 15.650 1.00 76.65 C ANISOU 2113 CA PHE A1067 8729 10552 9843 286 659 780 C ATOM 2114 C PHE A1067 72.944 12.943 17.155 1.00 77.48 C ANISOU 2114 C PHE A1067 8994 10585 9859 412 558 868 C ATOM 2115 O PHE A1067 73.273 13.987 17.716 1.00 77.12 O ANISOU 2115 O PHE A1067 8887 10629 9786 440 411 885 O ATOM 2116 CB PHE A1067 71.169 13.119 15.364 1.00 75.85 C ANISOU 2116 CB PHE A1067 8653 10464 9703 128 776 713 C ATOM 2117 CG PHE A1067 70.568 14.394 15.912 1.00 75.15 C ANISOU 2117 CG PHE A1067 8540 10463 9551 79 684 711 C ATOM 2118 CD1 PHE A1067 70.673 15.589 15.211 1.00 74.19 C ANISOU 2118 CD1 PHE A1067 8281 10466 9442 41 585 683 C ATOM 2119 CD2 PHE A1067 69.899 14.399 17.131 1.00 75.73 C ANISOU 2119 CD2 PHE A1067 8755 10478 9541 73 710 735 C ATOM 2120 CE1 PHE A1067 70.130 16.770 15.725 1.00 73.71 C ANISOU 2120 CE1 PHE A1067 8212 10466 9329 14 490 675 C ATOM 2121 CE2 PHE A1067 69.363 15.581 17.647 1.00 75.24 C ANISOU 2121 CE2 PHE A1067 8659 10500 9429 37 624 715 C ATOM 2122 CZ PHE A1067 69.473 16.757 16.937 1.00 74.18 C ANISOU 2122 CZ PHE A1067 8374 10485 9326 16 504 682 C ATOM 2123 N ASN A1068 72.805 11.763 17.799 1.00 77.00 N ANISOU 2123 N ASN A1068 9168 10349 9739 490 641 920 N ATOM 2124 CA ASN A1068 73.053 11.578 19.231 1.00 78.34 C ANISOU 2124 CA ASN A1068 9575 10416 9775 640 553 1015 C ATOM 2125 C ASN A1068 74.532 11.767 19.578 1.00 79.36 C ANISOU 2125 C ASN A1068 9623 10596 9935 868 309 1026 C ATOM 2126 O ASN A1068 74.846 12.224 20.678 1.00 80.02 O ANISOU 2126 O ASN A1068 9801 10689 9914 990 149 1067 O ATOM 2127 CB ASN A1068 72.529 10.227 19.717 1.00 80.01 C ANISOU 2127 CB ASN A1068 10117 10387 9896 658 736 1072 C ATOM 2128 CG ASN A1068 71.023 10.161 19.826 1.00 79.64 C ANISOU 2128 CG ASN A1068 10166 10291 9803 427 977 1030 C ATOM 2129 OD1 ASN A1068 70.381 10.964 20.517 1.00 78.99 O ANISOU 2129 OD1 ASN A1068 10100 10274 9639 349 971 1024 O ATOM 2130 ND2 ASN A1068 70.425 9.176 19.176 1.00 80.36 N ANISOU 2130 ND2 ASN A1068 10313 10263 9957 312 1200 970 N ATOM 2131 N GLN A1069 75.431 11.444 18.627 1.00 78.19 N ANISOU 2131 N GLN A1069 9278 10494 9937 922 282 956 N ATOM 2132 CA GLN A1069 76.879 11.620 18.749 1.00 79.45 C ANISOU 2132 CA GLN A1069 9270 10732 10185 1118 68 895 C ATOM 2133 C GLN A1069 77.200 13.120 18.644 1.00 78.36 C ANISOU 2133 C GLN A1069 8873 10793 10108 1016 -38 829 C ATOM 2134 O GLN A1069 78.064 13.616 19.369 1.00 79.46 O ANISOU 2134 O GLN A1069 8932 11001 10258 1157 -244 783 O ATOM 2135 CB GLN A1069 77.602 10.831 17.640 1.00 80.09 C ANISOU 2135 CB GLN A1069 9197 10808 10426 1159 130 806 C ATOM 2136 CG GLN A1069 79.123 10.783 17.780 1.00 81.60 C ANISOU 2136 CG GLN A1069 9195 11071 10739 1385 -77 692 C ATOM 2137 CD GLN A1069 79.818 11.221 16.514 1.00 81.44 C ANISOU 2137 CD GLN A1069 8825 11206 10913 1260 -5 544 C ATOM 2138 OE1 GLN A1069 79.843 10.507 15.505 1.00 81.93 O ANISOU 2138 OE1 GLN A1069 8843 11233 11054 1214 147 500 O ATOM 2139 NE2 GLN A1069 80.415 12.404 16.544 1.00 80.99 N ANISOU 2139 NE2 GLN A1069 8527 11313 10932 1192 -94 454 N ATOM 2140 N ASP A1070 76.486 13.831 17.746 1.00 74.73 N ANISOU 2140 N ASP A1070 8301 10412 9681 781 98 812 N ATOM 2141 CA ASP A1070 76.634 15.266 17.499 1.00 73.75 C ANISOU 2141 CA ASP A1070 7990 10430 9601 654 43 764 C ATOM 2142 C ASP A1070 76.023 16.125 18.603 1.00 73.35 C ANISOU 2142 C ASP A1070 8046 10394 9430 642 -52 815 C ATOM 2143 O ASP A1070 76.587 17.173 18.923 1.00 73.55 O ANISOU 2143 O ASP A1070 7941 10511 9493 637 -180 766 O ATOM 2144 CB ASP A1070 76.040 15.644 16.133 1.00 72.25 C ANISOU 2144 CB ASP A1070 7720 10285 9446 450 207 740 C ATOM 2145 CG ASP A1070 76.952 15.372 14.952 1.00 72.68 C ANISOU 2145 CG ASP A1070 7600 10384 9631 422 285 654 C ATOM 2146 OD1 ASP A1070 77.533 14.264 14.889 1.00 73.93 O ANISOU 2146 OD1 ASP A1070 7751 10489 9850 547 299 624 O ATOM 2147 OD2 ASP A1070 77.056 16.251 14.070 1.00 71.97 O ANISOU 2147 OD2 ASP A1070 7407 10367 9571 276 348 615 O ATOM 2148 N VAL A1071 74.875 15.696 19.174 1.00 70.85 N ANISOU 2148 N VAL A1071 7958 9983 8979 621 30 892 N ATOM 2149 CA VAL A1071 74.187 16.422 20.247 1.00 70.60 C ANISOU 2149 CA VAL A1071 8045 9959 8821 603 -26 926 C ATOM 2150 C VAL A1071 75.015 16.468 21.545 1.00 72.17 C ANISOU 2150 C VAL A1071 8329 10151 8941 803 -229 943 C ATOM 2151 O VAL A1071 74.999 17.487 22.233 1.00 71.96 O ANISOU 2151 O VAL A1071 8273 10197 8871 795 -346 922 O ATOM 2152 CB VAL A1071 72.697 16.001 20.434 1.00 70.17 C ANISOU 2152 CB VAL A1071 8177 9820 8664 490 159 955 C ATOM 2153 CG1 VAL A1071 72.552 14.717 21.250 1.00 71.87 C ANISOU 2153 CG1 VAL A1071 8682 9864 8762 592 240 1030 C ATOM 2154 CG2 VAL A1071 71.869 17.130 21.038 1.00 69.21 C ANISOU 2154 CG2 VAL A1071 8060 9764 8473 401 130 932 C ATOM 2155 N ASP A1072 75.774 15.388 21.839 1.00 75.14 N ANISOU 2155 N ASP A1072 8808 10440 9302 1002 -292 965 N ATOM 2156 CA ASP A1072 76.653 15.299 23.008 1.00 77.18 C ANISOU 2156 CA ASP A1072 9163 10690 9472 1254 -530 960 C ATOM 2157 C ASP A1072 77.855 16.226 22.830 1.00 77.42 C ANISOU 2157 C ASP A1072 8858 10892 9667 1296 -729 814 C ATOM 2158 O ASP A1072 78.273 16.870 23.791 1.00 78.21 O ANISOU 2158 O ASP A1072 8952 11056 9708 1404 -930 766 O ATOM 2159 CB ASP A1072 77.115 13.850 23.247 1.00 79.34 C ANISOU 2159 CB ASP A1072 9656 10803 9686 1485 -555 1011 C ATOM 2160 CG ASP A1072 76.016 12.876 23.644 1.00 79.81 C ANISOU 2160 CG ASP A1072 10107 10651 9566 1446 -341 1148 C ATOM 2161 OD1 ASP A1072 75.049 13.306 24.316 1.00 78.57 O ANISOU 2161 OD1 ASP A1072 10117 10471 9265 1324 -245 1202 O ATOM 2162 OD2 ASP A1072 76.150 11.674 23.329 1.00 81.69 O ANISOU 2162 OD2 ASP A1072 10492 10735 9812 1536 -259 1186 O ATOM 2163 N ALA A1073 78.385 16.314 21.590 1.00 74.17 N ANISOU 2163 N ALA A1073 8171 10551 9459 1191 -650 726 N ATOM 2164 CA ALA A1073 79.507 17.181 21.224 1.00 74.69 C ANISOU 2164 CA ALA A1073 7898 10767 9715 1162 -756 558 C ATOM 2165 C ALA A1073 79.082 18.653 21.250 1.00 73.26 C ANISOU 2165 C ALA A1073 7633 10665 9538 956 -737 542 C ATOM 2166 O ALA A1073 79.901 19.518 21.566 1.00 74.21 O ANISOU 2166 O ALA A1073 7555 10886 9755 959 -873 408 O ATOM 2167 CB ALA A1073 80.026 16.811 19.845 1.00 74.56 C ANISOU 2167 CB ALA A1073 7672 10777 9881 1070 -607 481 C ATOM 2168 N ALA A1074 77.797 18.927 20.930 1.00 68.63 N ANISOU 2168 N ALA A1074 7192 10028 8856 786 -575 656 N ATOM 2169 CA ALA A1074 77.207 20.267 20.929 1.00 67.33 C ANISOU 2169 CA ALA A1074 6999 9908 8676 615 -558 654 C ATOM 2170 C ALA A1074 77.052 20.794 22.358 1.00 67.94 C ANISOU 2170 C ALA A1074 7184 10000 8630 712 -727 654 C ATOM 2171 O ALA A1074 77.427 21.938 22.616 1.00 68.18 O ANISOU 2171 O ALA A1074 7087 10101 8718 655 -822 568 O ATOM 2172 CB ALA A1074 75.861 20.251 20.220 1.00 65.59 C ANISOU 2172 CB ALA A1074 6899 9634 8388 465 -373 740 C ATOM 2173 N VAL A1075 76.528 19.952 23.284 1.00 67.81 N ANISOU 2173 N VAL A1075 7423 9906 8437 851 -749 743 N ATOM 2174 CA VAL A1075 76.326 20.273 24.706 1.00 68.77 C ANISOU 2174 CA VAL A1075 7715 10027 8388 963 -891 755 C ATOM 2175 C VAL A1075 77.679 20.565 25.380 1.00 70.85 C ANISOU 2175 C VAL A1075 7840 10378 8702 1147 -1159 628 C ATOM 2176 O VAL A1075 77.796 21.565 26.092 1.00 71.29 O ANISOU 2176 O VAL A1075 7848 10505 8734 1143 -1293 552 O ATOM 2177 CB VAL A1075 75.487 19.184 25.445 1.00 69.35 C ANISOU 2177 CB VAL A1075 8145 9964 8241 1052 -798 883 C ATOM 2178 CG1 VAL A1075 75.480 19.394 26.960 1.00 70.81 C ANISOU 2178 CG1 VAL A1075 8552 10140 8213 1203 -952 895 C ATOM 2179 CG2 VAL A1075 74.057 19.140 24.915 1.00 67.60 C ANISOU 2179 CG2 VAL A1075 8001 9688 7995 841 -540 938 C ATOM 2180 N ARG A1076 78.705 19.726 25.106 1.00 72.28 N ANISOU 2180 N ARG A1076 7928 10561 8974 1309 -1243 571 N ATOM 2181 CA ARG A1076 80.062 19.898 25.639 1.00 74.67 C ANISOU 2181 CA ARG A1076 8041 10966 9364 1509 -1517 392 C ATOM 2182 C ARG A1076 80.740 21.146 25.068 1.00 74.48 C ANISOU 2182 C ARG A1076 7643 11075 9581 1323 -1525 208 C ATOM 2183 O ARG A1076 81.540 21.773 25.763 1.00 76.29 O ANISOU 2183 O ARG A1076 7715 11407 9865 1414 -1742 32 O ATOM 2184 CB ARG A1076 80.932 18.644 25.419 1.00 76.57 C ANISOU 2184 CB ARG A1076 8264 11171 9658 1746 -1602 351 C ATOM 2185 CG ARG A1076 80.484 17.396 26.193 1.00 77.92 C ANISOU 2185 CG ARG A1076 8861 11176 9569 1984 -1638 517 C ATOM 2186 CD ARG A1076 80.606 17.522 27.706 1.00 79.43 C ANISOU 2186 CD ARG A1076 9299 11361 9520 2226 -1894 518 C ATOM 2187 NE ARG A1076 80.020 16.371 28.397 1.00 80.92 N ANISOU 2187 NE ARG A1076 9980 11345 9421 2405 -1857 711 N ATOM 2188 CZ ARG A1076 78.743 16.275 28.758 1.00 79.75 C ANISOU 2188 CZ ARG A1076 10162 11072 9068 2253 -1628 889 C ATOM 2189 NH1 ARG A1076 77.894 17.261 28.495 1.00 76.98 N ANISOU 2189 NH1 ARG A1076 9684 10794 8772 1952 -1453 894 N ATOM 2190 NH2 ARG A1076 78.305 15.189 29.380 1.00 81.67 N ANISOU 2190 NH2 ARG A1076 10872 11105 9054 2400 -1563 1049 N ATOM 2191 N GLY A1077 80.391 21.500 23.829 1.00 71.09 N ANISOU 2191 N GLY A1077 7102 10632 9277 1062 -1282 241 N ATOM 2192 CA GLY A1077 80.881 22.693 23.146 1.00 70.94 C ANISOU 2192 CA GLY A1077 6812 10685 9457 837 -1213 103 C ATOM 2193 C GLY A1077 80.326 23.963 23.763 1.00 70.28 C ANISOU 2193 C GLY A1077 6786 10610 9308 726 -1256 104 C ATOM 2194 O GLY A1077 81.015 24.987 23.809 1.00 71.12 O ANISOU 2194 O GLY A1077 6683 10780 9560 626 -1309 -65 O ATOM 2195 N ILE A1078 79.070 23.891 24.256 1.00 66.92 N ANISOU 2195 N ILE A1078 6639 10114 8673 737 -1221 271 N ATOM 2196 CA ILE A1078 78.362 24.978 24.939 1.00 66.37 C ANISOU 2196 CA ILE A1078 6661 10044 8513 663 -1262 278 C ATOM 2197 C ILE A1078 78.973 25.169 26.342 1.00 68.43 C ANISOU 2197 C ILE A1078 6923 10377 8700 855 -1527 164 C ATOM 2198 O ILE A1078 79.248 26.304 26.737 1.00 69.11 O ANISOU 2198 O ILE A1078 6894 10515 8850 786 -1619 35 O ATOM 2199 CB ILE A1078 76.823 24.705 24.967 1.00 64.52 C ANISOU 2199 CB ILE A1078 6690 9726 8099 616 -1119 451 C ATOM 2200 CG1 ILE A1078 76.200 24.874 23.562 1.00 62.79 C ANISOU 2200 CG1 ILE A1078 6440 9457 7960 425 -906 513 C ATOM 2201 CG2 ILE A1078 76.097 25.593 25.987 1.00 64.40 C ANISOU 2201 CG2 ILE A1078 6793 9718 7958 607 -1191 438 C ATOM 2202 CD1 ILE A1078 74.886 24.088 23.325 1.00 61.45 C ANISOU 2202 CD1 ILE A1078 6464 9220 7663 411 -754 637 C ATOM 2203 N LEU A1079 79.198 24.053 27.073 1.00 70.06 N ANISOU 2203 N LEU A1079 7281 10575 8763 1107 -1655 203 N ATOM 2204 CA LEU A1079 79.781 24.036 28.421 1.00 72.49 C ANISOU 2204 CA LEU A1079 7653 10944 8946 1355 -1940 103 C ATOM 2205 C LEU A1079 81.225 24.551 28.448 1.00 74.71 C ANISOU 2205 C LEU A1079 7577 11359 9451 1413 -2147 -170 C ATOM 2206 O LEU A1079 81.618 25.201 29.418 1.00 76.59 O ANISOU 2206 O LEU A1079 7772 11679 9650 1509 -2369 -319 O ATOM 2207 CB LEU A1079 79.693 22.632 29.047 1.00 73.71 C ANISOU 2207 CB LEU A1079 8114 11017 8876 1627 -2011 228 C ATOM 2208 CG LEU A1079 78.293 22.140 29.432 1.00 72.36 C ANISOU 2208 CG LEU A1079 8337 10712 8444 1588 -1825 450 C ATOM 2209 CD1 LEU A1079 78.219 20.632 29.385 1.00 73.58 C ANISOU 2209 CD1 LEU A1079 8750 10734 8473 1752 -1764 588 C ATOM 2210 CD2 LEU A1079 77.879 22.647 30.808 1.00 72.86 C ANISOU 2210 CD2 LEU A1079 8628 10789 8266 1675 -1949 444 C ATOM 2211 N ARG A1080 82.004 24.270 27.382 1.00 76.56 N ANISOU 2211 N ARG A1080 7543 11621 9926 1343 -2062 -262 N ATOM 2212 CA ARG A1080 83.391 24.727 27.243 1.00 78.82 C ANISOU 2212 CA ARG A1080 7432 12039 10477 1349 -2198 -568 C ATOM 2213 C ARG A1080 83.453 26.224 26.919 1.00 78.35 C ANISOU 2213 C ARG A1080 7172 12006 10592 1043 -2088 -695 C ATOM 2214 O ARG A1080 84.427 26.884 27.285 1.00 80.60 O ANISOU 2214 O ARG A1080 7174 12401 11049 1043 -2239 -979 O ATOM 2215 CB ARG A1080 84.141 23.907 26.181 1.00 79.16 C ANISOU 2215 CB ARG A1080 7264 12094 10718 1353 -2096 -637 C ATOM 2216 CG ARG A1080 84.699 22.591 26.715 1.00 81.32 C ANISOU 2216 CG ARG A1080 7611 12381 10906 1732 -2329 -667 C ATOM 2217 CD ARG A1080 85.333 21.740 25.628 1.00 81.54 C ANISOU 2217 CD ARG A1080 7444 12409 11128 1737 -2209 -730 C ATOM 2218 NE ARG A1080 84.334 21.020 24.833 1.00 79.14 N ANISOU 2218 NE ARG A1080 7400 11958 10711 1629 -1938 -443 N ATOM 2219 CZ ARG A1080 84.617 20.057 23.960 1.00 79.63 C ANISOU 2219 CZ ARG A1080 7406 11983 10867 1666 -1823 -433 C ATOM 2220 NH1 ARG A1080 85.874 19.678 23.761 1.00 82.49 N ANISOU 2220 NH1 ARG A1080 7456 12445 11441 1815 -1949 -694 N ATOM 2221 NH2 ARG A1080 83.644 19.461 23.284 1.00 77.50 N ANISOU 2221 NH2 ARG A1080 7373 11583 10490 1557 -1584 -192 N ATOM 2222 N ASN A1081 82.411 26.753 26.240 1.00 73.66 N ANISOU 2222 N ASN A1081 6732 11303 9953 794 -1832 -503 N ATOM 2223 CA ASN A1081 82.292 28.164 25.862 1.00 73.14 C ANISOU 2223 CA ASN A1081 6574 11205 10011 510 -1702 -571 C ATOM 2224 C ASN A1081 82.013 29.019 27.101 1.00 73.81 C ANISOU 2224 C ASN A1081 6737 11319 9989 566 -1891 -639 C ATOM 2225 O ASN A1081 81.180 28.646 27.928 1.00 73.14 O ANISOU 2225 O ASN A1081 6920 11216 9655 724 -1982 -492 O ATOM 2226 CB ASN A1081 81.188 28.346 24.816 1.00 70.46 C ANISOU 2226 CB ASN A1081 6428 10732 9612 306 -1425 -340 C ATOM 2227 CG ASN A1081 81.285 29.633 24.039 1.00 70.62 C ANISOU 2227 CG ASN A1081 6365 10680 9787 13 -1246 -406 C ATOM 2228 OD1 ASN A1081 80.987 30.721 24.544 1.00 70.82 O ANISOU 2228 OD1 ASN A1081 6434 10671 9803 -69 -1290 -454 O ATOM 2229 ND2 ASN A1081 81.677 29.533 22.779 1.00 70.79 N ANISOU 2229 ND2 ASN A1081 6302 10657 9937 -151 -1026 -404 N ATOM 2230 N ALA A1082 82.724 30.153 27.231 1.00 72.75 N ANISOU 2230 N ALA A1082 6372 11225 10044 423 -1931 -879 N ATOM 2231 CA ALA A1082 82.617 31.071 28.369 1.00 73.83 C ANISOU 2231 CA ALA A1082 6535 11399 10118 458 -2115 -999 C ATOM 2232 C ALA A1082 81.287 31.826 28.466 1.00 71.73 C ANISOU 2232 C ALA A1082 6545 11013 9696 341 -2003 -810 C ATOM 2233 O ALA A1082 80.811 32.064 29.578 1.00 72.03 O ANISOU 2233 O ALA A1082 6728 11081 9559 468 -2164 -813 O ATOM 2234 CB ALA A1082 83.778 32.053 28.359 1.00 76.50 C ANISOU 2234 CB ALA A1082 6525 11799 10742 302 -2153 -1339 C ATOM 2235 N LYS A1083 80.700 32.213 27.317 1.00 67.65 N ANISOU 2235 N LYS A1083 6104 10364 9237 117 -1739 -668 N ATOM 2236 CA LYS A1083 79.444 32.972 27.258 1.00 65.92 C ANISOU 2236 CA LYS A1083 6121 10026 8900 21 -1641 -520 C ATOM 2237 C LYS A1083 78.183 32.107 27.224 1.00 63.71 C ANISOU 2237 C LYS A1083 6097 9715 8394 134 -1582 -276 C ATOM 2238 O LYS A1083 77.155 32.518 27.766 1.00 62.86 O ANISOU 2238 O LYS A1083 6166 9573 8145 157 -1597 -215 O ATOM 2239 CB LYS A1083 79.449 33.950 26.071 1.00 65.69 C ANISOU 2239 CB LYS A1083 6080 9850 9029 -253 -1417 -516 C ATOM 2240 CG LYS A1083 80.330 35.174 26.285 1.00 68.04 C ANISOU 2240 CG LYS A1083 6204 10121 9527 -422 -1432 -760 C ATOM 2241 CD LYS A1083 80.230 36.148 25.123 1.00 68.06 C ANISOU 2241 CD LYS A1083 6297 9925 9638 -693 -1179 -719 C ATOM 2242 CE LYS A1083 81.090 37.368 25.339 1.00 70.78 C ANISOU 2242 CE LYS A1083 6492 10209 10192 -897 -1150 -972 C ATOM 2243 NZ LYS A1083 80.954 38.343 24.226 1.00 71.09 N ANISOU 2243 NZ LYS A1083 6706 10005 10300 -1162 -880 -908 N ATOM 2244 N LEU A1084 78.251 30.932 26.574 1.00 61.61 N ANISOU 2244 N LEU A1084 5838 9459 8112 190 -1498 -164 N ATOM 2245 CA LEU A1084 77.115 30.017 26.425 1.00 59.79 C ANISOU 2245 CA LEU A1084 5824 9192 7702 265 -1406 37 C ATOM 2246 C LEU A1084 76.784 29.203 27.680 1.00 60.25 C ANISOU 2246 C LEU A1084 6044 9303 7546 480 -1536 79 C ATOM 2247 O LEU A1084 75.609 28.905 27.906 1.00 59.11 O ANISOU 2247 O LEU A1084 6102 9116 7241 496 -1451 196 O ATOM 2248 CB LEU A1084 77.309 29.080 25.218 1.00 59.04 C ANISOU 2248 CB LEU A1084 5687 9070 7675 229 -1251 128 C ATOM 2249 CG LEU A1084 77.373 29.716 23.824 1.00 58.59 C ANISOU 2249 CG LEU A1084 5571 8932 7758 16 -1067 140 C ATOM 2250 CD1 LEU A1084 77.924 28.734 22.816 1.00 58.28 C ANISOU 2250 CD1 LEU A1084 5448 8901 7794 5 -947 175 C ATOM 2251 CD2 LEU A1084 76.007 30.212 23.367 1.00 57.14 C ANISOU 2251 CD2 LEU A1084 5581 8655 7474 -53 -970 257 C ATOM 2252 N LYS A1085 77.810 28.829 28.475 1.00 61.23 N ANISOU 2252 N LYS A1085 6090 9513 7662 649 -1735 -33 N ATOM 2253 CA LYS A1085 77.671 28.035 29.703 1.00 62.28 C ANISOU 2253 CA LYS A1085 6433 9676 7554 887 -1881 7 C ATOM 2254 C LYS A1085 76.751 28.644 30.795 1.00 62.34 C ANISOU 2254 C LYS A1085 6645 9680 7361 905 -1919 14 C ATOM 2255 O LYS A1085 75.900 27.899 31.285 1.00 61.95 O ANISOU 2255 O LYS A1085 6865 9583 7090 980 -1840 147 O ATOM 2256 CB LYS A1085 79.045 27.631 30.271 1.00 64.89 C ANISOU 2256 CB LYS A1085 6630 10103 7922 1101 -2136 -151 C ATOM 2257 CG LYS A1085 78.990 26.522 31.316 1.00 66.37 C ANISOU 2257 CG LYS A1085 7105 10282 7831 1391 -2278 -68 C ATOM 2258 CD LYS A1085 80.091 26.687 32.353 1.00 69.36 C ANISOU 2258 CD LYS A1085 7404 10777 8173 1632 -2623 -280 C ATOM 2259 CE LYS A1085 79.744 26.048 33.677 1.00 70.70 C ANISOU 2259 CE LYS A1085 7970 10918 7975 1895 -2768 -193 C ATOM 2260 NZ LYS A1085 78.689 26.803 34.411 1.00 69.83 N ANISOU 2260 NZ LYS A1085 8054 10788 7691 1782 -2685 -147 N ATOM 2261 N PRO A1086 76.866 29.941 31.209 1.00 62.35 N ANISOU 2261 N PRO A1086 6541 9719 7430 827 -2012 -135 N ATOM 2262 CA PRO A1086 75.962 30.450 32.262 1.00 62.53 C ANISOU 2262 CA PRO A1086 6764 9741 7254 854 -2037 -139 C ATOM 2263 C PRO A1086 74.496 30.554 31.836 1.00 60.48 C ANISOU 2263 C PRO A1086 6642 9398 6940 719 -1802 -13 C ATOM 2264 O PRO A1086 73.609 30.442 32.684 1.00 60.72 O ANISOU 2264 O PRO A1086 6884 9424 6764 765 -1760 16 O ATOM 2265 CB PRO A1086 76.549 31.825 32.613 1.00 63.64 C ANISOU 2265 CB PRO A1086 6716 9930 7534 786 -2186 -352 C ATOM 2266 CG PRO A1086 77.909 31.856 31.990 1.00 64.85 C ANISOU 2266 CG PRO A1086 6581 10128 7930 760 -2267 -484 C ATOM 2267 CD PRO A1086 77.803 30.997 30.778 1.00 63.27 C ANISOU 2267 CD PRO A1086 6366 9867 7806 697 -2075 -323 C ATOM 2268 N VAL A1087 74.249 30.750 30.526 1.00 59.11 N ANISOU 2268 N VAL A1087 6352 9162 6946 560 -1648 41 N ATOM 2269 CA VAL A1087 72.912 30.862 29.930 1.00 57.37 C ANISOU 2269 CA VAL A1087 6215 8873 6709 453 -1458 121 C ATOM 2270 C VAL A1087 72.242 29.478 29.877 1.00 56.84 C ANISOU 2270 C VAL A1087 6307 8786 6503 505 -1310 254 C ATOM 2271 O VAL A1087 71.063 29.359 30.217 1.00 56.49 O ANISOU 2271 O VAL A1087 6396 8724 6344 481 -1188 267 O ATOM 2272 CB VAL A1087 72.952 31.549 28.533 1.00 56.28 C ANISOU 2272 CB VAL A1087 5940 8666 6778 300 -1375 127 C ATOM 2273 CG1 VAL A1087 71.546 31.854 28.022 1.00 54.91 C ANISOU 2273 CG1 VAL A1087 5849 8434 6580 238 -1248 160 C ATOM 2274 CG2 VAL A1087 73.793 32.825 28.563 1.00 57.27 C ANISOU 2274 CG2 VAL A1087 5931 8777 7053 223 -1484 -7 C ATOM 2275 N TYR A1088 73.005 28.442 29.465 1.00 57.71 N ANISOU 2275 N TYR A1088 6396 8893 6638 568 -1309 327 N ATOM 2276 CA TYR A1088 72.561 27.049 29.342 1.00 57.52 C ANISOU 2276 CA TYR A1088 6530 8821 6504 615 -1166 451 C ATOM 2277 C TYR A1088 72.108 26.447 30.677 1.00 58.92 C ANISOU 2277 C TYR A1088 6988 8981 6418 728 -1156 484 C ATOM 2278 O TYR A1088 71.157 25.663 30.694 1.00 58.65 O ANISOU 2278 O TYR A1088 7124 8882 6278 685 -953 556 O ATOM 2279 CB TYR A1088 73.672 26.194 28.713 1.00 57.96 C ANISOU 2279 CB TYR A1088 6494 8873 6655 687 -1210 492 C ATOM 2280 CG TYR A1088 73.218 24.835 28.226 1.00 57.53 C ANISOU 2280 CG TYR A1088 6571 8743 6545 699 -1036 615 C ATOM 2281 CD1 TYR A1088 72.612 24.686 26.981 1.00 55.91 C ANISOU 2281 CD1 TYR A1088 6281 8505 6458 557 -860 650 C ATOM 2282 CD2 TYR A1088 73.440 23.691 28.985 1.00 59.08 C ANISOU 2282 CD2 TYR A1088 6995 8887 6565 863 -1057 688 C ATOM 2283 CE1 TYR A1088 72.205 23.434 26.520 1.00 55.68 C ANISOU 2283 CE1 TYR A1088 6356 8405 6395 557 -697 736 C ATOM 2284 CE2 TYR A1088 73.039 22.435 28.534 1.00 58.94 C ANISOU 2284 CE2 TYR A1088 7117 8770 6508 861 -878 794 C ATOM 2285 CZ TYR A1088 72.422 22.311 27.301 1.00 57.17 C ANISOU 2285 CZ TYR A1088 6768 8527 6427 697 -694 807 C ATOM 2286 OH TYR A1088 72.024 21.073 26.857 1.00 57.20 O ANISOU 2286 OH TYR A1088 6896 8432 6405 683 -515 886 O ATOM 2287 N ASP A1089 72.782 26.821 31.785 1.00 62.37 N ANISOU 2287 N ASP A1089 7484 9471 6742 865 -1363 416 N ATOM 2288 CA ASP A1089 72.475 26.360 33.144 1.00 64.25 C ANISOU 2288 CA ASP A1089 8040 9689 6683 994 -1377 444 C ATOM 2289 C ASP A1089 71.125 26.887 33.651 1.00 63.93 C ANISOU 2289 C ASP A1089 8116 9639 6536 868 -1203 406 C ATOM 2290 O ASP A1089 70.548 26.303 34.571 1.00 65.48 O ANISOU 2290 O ASP A1089 8617 9785 6478 910 -1088 450 O ATOM 2291 CB ASP A1089 73.607 26.751 34.115 1.00 66.38 C ANISOU 2291 CB ASP A1089 8313 10039 6869 1191 -1688 344 C ATOM 2292 CG ASP A1089 74.951 26.081 33.863 1.00 67.64 C ANISOU 2292 CG ASP A1089 8382 10219 7099 1371 -1884 338 C ATOM 2293 OD1 ASP A1089 75.105 25.425 32.807 1.00 66.39 O ANISOU 2293 OD1 ASP A1089 8119 10015 7092 1320 -1774 413 O ATOM 2294 OD2 ASP A1089 75.852 26.226 34.716 1.00 70.09 O ANISOU 2294 OD2 ASP A1089 8712 10600 7319 1575 -2160 233 O ATOM 2295 N SER A1090 70.625 27.982 33.044 1.00 63.22 N ANISOU 2295 N SER A1090 7800 9585 6636 719 -1173 313 N ATOM 2296 CA SER A1090 69.352 28.617 33.388 1.00 62.91 C ANISOU 2296 CA SER A1090 7798 9552 6552 611 -1031 229 C ATOM 2297 C SER A1090 68.249 28.318 32.345 1.00 61.29 C ANISOU 2297 C SER A1090 7507 9307 6474 464 -799 239 C ATOM 2298 O SER A1090 67.329 29.121 32.164 1.00 60.61 O ANISOU 2298 O SER A1090 7316 9242 6471 378 -745 125 O ATOM 2299 CB SER A1090 69.548 30.119 33.581 1.00 62.89 C ANISOU 2299 CB SER A1090 7634 9608 6654 593 -1202 86 C ATOM 2300 OG SER A1090 70.496 30.387 34.602 1.00 64.50 O ANISOU 2300 OG SER A1090 7903 9864 6740 727 -1420 34 O ATOM 2301 N LEU A1091 68.335 27.144 31.684 1.00 62.00 N ANISOU 2301 N LEU A1091 7640 9340 6578 454 -679 353 N ATOM 2302 CA LEU A1091 67.368 26.689 30.678 1.00 60.81 C ANISOU 2302 CA LEU A1091 7406 9158 6542 329 -472 345 C ATOM 2303 C LEU A1091 66.891 25.268 30.984 1.00 61.76 C ANISOU 2303 C LEU A1091 7750 9196 6521 301 -234 417 C ATOM 2304 O LEU A1091 67.712 24.402 31.295 1.00 62.35 O ANISOU 2304 O LEU A1091 7991 9210 6489 405 -271 544 O ATOM 2305 CB LEU A1091 67.971 26.747 29.257 1.00 59.28 C ANISOU 2305 CB LEU A1091 7005 8962 6557 313 -549 393 C ATOM 2306 CG LEU A1091 68.244 28.133 28.656 1.00 58.41 C ANISOU 2306 CG LEU A1091 6700 8886 6607 289 -707 322 C ATOM 2307 CD1 LEU A1091 69.294 28.053 27.570 1.00 57.77 C ANISOU 2307 CD1 LEU A1091 6493 8788 6669 288 -780 395 C ATOM 2308 CD2 LEU A1091 66.979 28.760 28.093 1.00 57.67 C ANISOU 2308 CD2 LEU A1091 6523 8797 6592 214 -630 212 C ATOM 2309 N ASP A1092 65.567 25.032 30.901 1.00 61.79 N ANISOU 2309 N ASP A1092 7756 9188 6533 165 13 315 N ATOM 2310 CA ASP A1092 64.957 23.718 31.144 1.00 63.00 C ANISOU 2310 CA ASP A1092 8119 9241 6577 81 305 348 C ATOM 2311 C ASP A1092 65.118 22.800 29.923 1.00 61.94 C ANISOU 2311 C ASP A1092 7893 9055 6587 47 371 415 C ATOM 2312 O ASP A1092 65.447 23.289 28.844 1.00 60.24 O ANISOU 2312 O ASP A1092 7431 8900 6557 63 222 404 O ATOM 2313 CB ASP A1092 63.476 23.865 31.546 1.00 63.90 C ANISOU 2313 CB ASP A1092 8224 9376 6679 -80 568 154 C ATOM 2314 CG ASP A1092 62.602 24.524 30.497 1.00 62.61 C ANISOU 2314 CG ASP A1092 7720 9307 6762 -161 562 -34 C ATOM 2315 OD1 ASP A1092 61.773 23.816 29.887 1.00 63.39 O ANISOU 2315 OD1 ASP A1092 7742 9387 6957 -284 778 -133 O ATOM 2316 OD2 ASP A1092 62.738 25.750 30.298 1.00 61.15 O ANISOU 2316 OD2 ASP A1092 7360 9205 6669 -91 336 -94 O ATOM 2317 N ALA A1093 64.876 21.477 30.095 1.00 61.71 N ANISOU 2317 N ALA A1093 8091 8897 6460 -6 610 482 N ATOM 2318 CA ALA A1093 64.992 20.427 29.067 1.00 61.15 C ANISOU 2318 CA ALA A1093 7986 8749 6498 -42 712 540 C ATOM 2319 C ALA A1093 64.446 20.785 27.674 1.00 59.30 C ANISOU 2319 C ALA A1093 7411 8607 6513 -131 702 411 C ATOM 2320 O ALA A1093 65.092 20.472 26.673 1.00 58.24 O ANISOU 2320 O ALA A1093 7173 8468 6487 -83 609 486 O ATOM 2321 CB ALA A1093 64.363 19.134 29.564 1.00 63.17 C ANISOU 2321 CB ALA A1093 8540 8839 6622 -153 1051 558 C ATOM 2322 N VAL A1094 63.273 21.446 27.616 1.00 56.64 N ANISOU 2322 N VAL A1094 6908 8356 6257 -242 787 205 N ATOM 2323 CA VAL A1094 62.622 21.867 26.367 1.00 55.39 C ANISOU 2323 CA VAL A1094 6451 8290 6305 -287 744 50 C ATOM 2324 C VAL A1094 63.338 23.099 25.788 1.00 53.78 C ANISOU 2324 C VAL A1094 6095 8165 6174 -161 428 105 C ATOM 2325 O VAL A1094 63.559 23.164 24.576 1.00 52.71 O ANISOU 2325 O VAL A1094 5838 8043 6146 -134 338 137 O ATOM 2326 CB VAL A1094 61.093 22.104 26.555 1.00 56.38 C ANISOU 2326 CB VAL A1094 6439 8484 6499 -414 915 -232 C ATOM 2327 CG1 VAL A1094 60.397 22.381 25.222 1.00 55.50 C ANISOU 2327 CG1 VAL A1094 6037 8466 6585 -417 837 -412 C ATOM 2328 CG2 VAL A1094 60.429 20.925 27.264 1.00 58.38 C ANISOU 2328 CG2 VAL A1094 6870 8638 6675 -584 1286 -301 C ATOM 2329 N ARG A1095 63.703 24.063 26.656 1.00 52.67 N ANISOU 2329 N ARG A1095 5985 8062 5965 -96 282 111 N ATOM 2330 CA ARG A1095 64.387 25.295 26.256 1.00 51.60 C ANISOU 2330 CA ARG A1095 5740 7972 5894 -5 17 149 C ATOM 2331 C ARG A1095 65.870 25.089 25.943 1.00 51.16 C ANISOU 2331 C ARG A1095 5723 7879 5837 71 -115 335 C ATOM 2332 O ARG A1095 66.435 25.863 25.166 1.00 50.43 O ANISOU 2332 O ARG A1095 5522 7805 5834 102 -275 358 O ATOM 2333 CB ARG A1095 64.158 26.419 27.272 1.00 52.13 C ANISOU 2333 CB ARG A1095 5824 8081 5902 27 -77 65 C ATOM 2334 CG ARG A1095 62.761 27.019 27.180 1.00 52.50 C ANISOU 2334 CG ARG A1095 5745 8187 6015 -17 -18 -165 C ATOM 2335 CD ARG A1095 62.657 28.300 27.972 1.00 52.92 C ANISOU 2335 CD ARG A1095 5797 8276 6034 34 -149 -248 C ATOM 2336 NE ARG A1095 61.271 28.742 28.132 1.00 53.91 N ANISOU 2336 NE ARG A1095 5805 8462 6216 5 -73 -501 N ATOM 2337 CZ ARG A1095 60.557 28.591 29.244 1.00 55.36 C ANISOU 2337 CZ ARG A1095 6047 8676 6311 -63 105 -635 C ATOM 2338 NH1 ARG A1095 61.089 28.003 30.309 1.00 56.00 N ANISOU 2338 NH1 ARG A1095 6354 8716 6208 -96 219 -511 N ATOM 2339 NH2 ARG A1095 59.306 29.027 29.300 1.00 56.47 N ANISOU 2339 NH2 ARG A1095 6030 8887 6539 -86 170 -907 N ATOM 2340 N ARG A1096 66.486 24.029 26.519 1.00 53.20 N ANISOU 2340 N ARG A1096 6145 8076 5994 101 -38 449 N ATOM 2341 CA ARG A1096 67.877 23.630 26.278 1.00 53.19 C ANISOU 2341 CA ARG A1096 6161 8047 6001 196 -160 586 C ATOM 2342 C ARG A1096 68.001 23.234 24.808 1.00 52.12 C ANISOU 2342 C ARG A1096 5884 7906 6013 158 -132 606 C ATOM 2343 O ARG A1096 68.951 23.644 24.142 1.00 51.54 O ANISOU 2343 O ARG A1096 5698 7857 6028 189 -263 641 O ATOM 2344 CB ARG A1096 68.262 22.421 27.149 1.00 54.67 C ANISOU 2344 CB ARG A1096 6597 8146 6030 268 -79 686 C ATOM 2345 CG ARG A1096 68.770 22.749 28.542 1.00 56.11 C ANISOU 2345 CG ARG A1096 6945 8334 6040 385 -212 711 C ATOM 2346 CD ARG A1096 69.209 21.471 29.235 1.00 57.93 C ANISOU 2346 CD ARG A1096 7473 8449 6088 500 -161 828 C ATOM 2347 NE ARG A1096 69.688 21.688 30.603 1.00 59.65 N ANISOU 2347 NE ARG A1096 7890 8673 6101 648 -316 847 N ATOM 2348 CZ ARG A1096 68.964 21.473 31.698 1.00 61.23 C ANISOU 2348 CZ ARG A1096 8381 8813 6070 636 -183 852 C ATOM 2349 NH1 ARG A1096 67.706 21.060 31.600 1.00 61.39 N ANISOU 2349 NH1 ARG A1096 8502 8763 6061 459 132 820 N ATOM 2350 NH2 ARG A1096 69.488 21.681 32.898 1.00 62.96 N ANISOU 2350 NH2 ARG A1096 8793 9046 6083 796 -356 865 N ATOM 2351 N ALA A1097 67.012 22.459 24.307 1.00 51.57 N ANISOU 2351 N ALA A1097 5818 7808 5968 74 57 558 N ATOM 2352 CA ALA A1097 66.919 21.977 22.930 1.00 50.83 C ANISOU 2352 CA ALA A1097 5612 7712 5989 34 108 549 C ATOM 2353 C ALA A1097 66.829 23.115 21.904 1.00 49.84 C ANISOU 2353 C ALA A1097 5331 7651 5955 25 -21 491 C ATOM 2354 O ALA A1097 67.387 22.982 20.813 1.00 49.30 O ANISOU 2354 O ALA A1097 5198 7580 5953 27 -48 533 O ATOM 2355 CB ALA A1097 65.731 21.047 22.790 1.00 51.44 C ANISOU 2355 CB ALA A1097 5714 7757 6074 -64 331 450 C ATOM 2356 N ALA A1098 66.148 24.232 22.253 1.00 49.43 N ANISOU 2356 N ALA A1098 5246 7642 5893 23 -91 391 N ATOM 2357 CA ALA A1098 66.023 25.400 21.372 1.00 48.95 C ANISOU 2357 CA ALA A1098 5103 7607 5889 42 -228 337 C ATOM 2358 C ALA A1098 67.372 26.106 21.178 1.00 48.67 C ANISOU 2358 C ALA A1098 5070 7545 5878 65 -357 448 C ATOM 2359 O ALA A1098 67.621 26.645 20.099 1.00 48.40 O ANISOU 2359 O ALA A1098 5017 7488 5885 58 -408 463 O ATOM 2360 CB ALA A1098 64.982 26.367 21.912 1.00 49.39 C ANISOU 2360 CB ALA A1098 5139 7699 5928 57 -276 194 C ATOM 2361 N LEU A1099 68.248 26.078 22.211 1.00 50.15 N ANISOU 2361 N LEU A1099 5291 7730 6033 90 -400 509 N ATOM 2362 CA LEU A1099 69.591 26.664 22.151 1.00 50.32 C ANISOU 2362 CA LEU A1099 5270 7741 6108 96 -509 562 C ATOM 2363 C LEU A1099 70.528 25.767 21.331 1.00 50.28 C ANISOU 2363 C LEU A1099 5218 7724 6162 88 -449 634 C ATOM 2364 O LEU A1099 71.370 26.286 20.599 1.00 50.38 O ANISOU 2364 O LEU A1099 5166 7722 6254 44 -473 645 O ATOM 2365 CB LEU A1099 70.162 26.909 23.559 1.00 51.10 C ANISOU 2365 CB LEU A1099 5399 7864 6152 152 -608 553 C ATOM 2366 CG LEU A1099 71.275 27.959 23.657 1.00 51.66 C ANISOU 2366 CG LEU A1099 5388 7938 6303 140 -741 528 C ATOM 2367 CD1 LEU A1099 70.702 29.363 23.814 1.00 51.64 C ANISOU 2367 CD1 LEU A1099 5400 7911 6310 103 -811 454 C ATOM 2368 CD2 LEU A1099 72.204 27.659 24.814 1.00 52.78 C ANISOU 2368 CD2 LEU A1099 5528 8123 6403 232 -849 515 C ATOM 2369 N ILE A1100 70.368 24.426 21.444 1.00 51.70 N ANISOU 2369 N ILE A1100 5443 7897 6304 120 -349 670 N ATOM 2370 CA ILE A1100 71.142 23.418 20.698 1.00 51.80 C ANISOU 2370 CA ILE A1100 5418 7892 6372 131 -283 722 C ATOM 2371 C ILE A1100 70.774 23.509 19.201 1.00 51.12 C ANISOU 2371 C ILE A1100 5286 7800 6338 56 -206 707 C ATOM 2372 O ILE A1100 71.647 23.345 18.343 1.00 51.27 O ANISOU 2372 O ILE A1100 5241 7814 6424 33 -179 730 O ATOM 2373 CB ILE A1100 70.952 21.988 21.303 1.00 52.39 C ANISOU 2373 CB ILE A1100 5606 7923 6377 194 -193 763 C ATOM 2374 CG1 ILE A1100 71.487 21.921 22.755 1.00 53.54 C ANISOU 2374 CG1 ILE A1100 5851 8061 6430 308 -300 791 C ATOM 2375 CG2 ILE A1100 71.614 20.897 20.439 1.00 52.55 C ANISOU 2375 CG2 ILE A1100 5591 7911 6464 213 -116 800 C ATOM 2376 CD1 ILE A1100 70.833 20.852 23.649 1.00 54.41 C ANISOU 2376 CD1 ILE A1100 6185 8091 6397 352 -187 835 C ATOM 2377 N ASN A1101 69.490 23.822 18.906 1.00 52.34 N ANISOU 2377 N ASN A1101 5472 7960 6455 28 -182 646 N ATOM 2378 CA ASN A1101 68.938 24.010 17.559 1.00 52.03 C ANISOU 2378 CA ASN A1101 5424 7920 6425 -3 -155 608 C ATOM 2379 C ASN A1101 69.664 25.155 16.833 1.00 52.23 C ANISOU 2379 C ASN A1101 5463 7915 6467 -32 -222 644 C ATOM 2380 O ASN A1101 69.889 25.066 15.625 1.00 52.37 O ANISOU 2380 O ASN A1101 5504 7912 6482 -61 -171 663 O ATOM 2381 CB ASN A1101 67.435 24.301 17.644 1.00 52.01 C ANISOU 2381 CB ASN A1101 5430 7945 6386 13 -173 488 C ATOM 2382 CG ASN A1101 66.697 24.216 16.329 1.00 52.07 C ANISOU 2382 CG ASN A1101 5429 7968 6387 23 -165 409 C ATOM 2383 OD1 ASN A1101 66.849 25.058 15.437 1.00 52.29 O ANISOU 2383 OD1 ASN A1101 5513 7971 6384 49 -248 425 O ATOM 2384 ND2 ASN A1101 65.829 23.226 16.208 1.00 52.19 N ANISOU 2384 ND2 ASN A1101 5395 8014 6420 6 -64 308 N ATOM 2385 N MET A1102 70.035 26.215 17.580 1.00 53.38 N ANISOU 2385 N MET A1102 5616 8044 6621 -35 -318 647 N ATOM 2386 CA MET A1102 70.762 27.381 17.072 1.00 53.95 C ANISOU 2386 CA MET A1102 5724 8055 6719 -94 -352 669 C ATOM 2387 C MET A1102 72.226 27.026 16.788 1.00 54.50 C ANISOU 2387 C MET A1102 5706 8125 6876 -161 -277 702 C ATOM 2388 O MET A1102 72.770 27.463 15.772 1.00 55.09 O ANISOU 2388 O MET A1102 5821 8144 6967 -246 -201 720 O ATOM 2389 CB MET A1102 70.673 28.554 18.064 1.00 54.25 C ANISOU 2389 CB MET A1102 5782 8072 6759 -84 -469 632 C ATOM 2390 CG MET A1102 69.303 29.209 18.115 1.00 54.11 C ANISOU 2390 CG MET A1102 5848 8038 6673 -18 -549 570 C ATOM 2391 SD MET A1102 69.190 30.545 19.333 1.00 54.64 S ANISOU 2391 SD MET A1102 5936 8076 6748 0 -680 508 S ATOM 2392 CE MET A1102 70.026 31.863 18.453 1.00 55.69 C ANISOU 2392 CE MET A1102 6189 8059 6912 -87 -683 554 C ATOM 2393 N VAL A1103 72.856 26.228 17.683 1.00 55.85 N ANISOU 2393 N VAL A1103 5771 8354 7096 -115 -294 694 N ATOM 2394 CA VAL A1103 74.249 25.765 17.572 1.00 56.70 C ANISOU 2394 CA VAL A1103 5747 8487 7310 -136 -256 676 C ATOM 2395 C VAL A1103 74.398 24.839 16.345 1.00 56.63 C ANISOU 2395 C VAL A1103 5729 8473 7314 -162 -115 701 C ATOM 2396 O VAL A1103 75.404 24.915 15.639 1.00 57.51 O ANISOU 2396 O VAL A1103 5759 8581 7511 -242 -29 670 O ATOM 2397 CB VAL A1103 74.763 25.118 18.896 1.00 57.21 C ANISOU 2397 CB VAL A1103 5739 8608 7390 -17 -362 651 C ATOM 2398 CG1 VAL A1103 76.200 24.614 18.763 1.00 58.51 C ANISOU 2398 CG1 VAL A1103 5736 8812 7683 1 -360 588 C ATOM 2399 CG2 VAL A1103 74.659 26.095 20.064 1.00 57.43 C ANISOU 2399 CG2 VAL A1103 5783 8648 7390 4 -502 610 C ATOM 2400 N PHE A1104 73.371 24.012 16.069 1.00 57.79 N ANISOU 2400 N PHE A1104 5954 8620 7384 -113 -76 732 N ATOM 2401 CA PHE A1104 73.334 23.104 14.920 1.00 57.73 C ANISOU 2401 CA PHE A1104 5951 8609 7375 -130 48 739 C ATOM 2402 C PHE A1104 73.213 23.856 13.586 1.00 58.00 C ANISOU 2402 C PHE A1104 6072 8605 7360 -218 114 745 C ATOM 2403 O PHE A1104 73.535 23.291 12.539 1.00 58.43 O ANISOU 2403 O PHE A1104 6126 8659 7416 -253 230 741 O ATOM 2404 CB PHE A1104 72.183 22.097 15.069 1.00 57.01 C ANISOU 2404 CB PHE A1104 5915 8522 7225 -70 75 735 C ATOM 2405 CG PHE A1104 72.605 20.733 15.560 1.00 57.28 C ANISOU 2405 CG PHE A1104 5917 8547 7300 -3 123 748 C ATOM 2406 CD1 PHE A1104 72.680 20.459 16.921 1.00 57.63 C ANISOU 2406 CD1 PHE A1104 5993 8579 7324 79 54 770 C ATOM 2407 CD2 PHE A1104 72.910 19.717 14.663 1.00 57.41 C ANISOU 2407 CD2 PHE A1104 5906 8552 7355 -7 234 737 C ATOM 2408 CE1 PHE A1104 73.067 19.195 17.376 1.00 58.28 C ANISOU 2408 CE1 PHE A1104 6111 8617 7415 169 89 795 C ATOM 2409 CE2 PHE A1104 73.296 18.453 15.119 1.00 57.90 C ANISOU 2409 CE2 PHE A1104 5970 8576 7453 75 272 749 C ATOM 2410 CZ PHE A1104 73.372 18.201 16.472 1.00 58.39 C ANISOU 2410 CZ PHE A1104 6095 8606 7484 170 195 785 C ATOM 2411 N GLN A1105 72.760 25.126 13.630 1.00 60.52 N ANISOU 2411 N GLN A1105 6495 8880 7620 -242 41 753 N ATOM 2412 CA GLN A1105 72.569 25.977 12.457 1.00 61.18 C ANISOU 2412 CA GLN A1105 6746 8888 7612 -296 81 774 C ATOM 2413 C GLN A1105 73.765 26.894 12.165 1.00 62.47 C ANISOU 2413 C GLN A1105 6932 8978 7826 -434 172 786 C ATOM 2414 O GLN A1105 74.207 26.952 11.015 1.00 63.45 O ANISOU 2414 O GLN A1105 7158 9048 7903 -519 313 804 O ATOM 2415 CB GLN A1105 71.274 26.799 12.599 1.00 60.89 C ANISOU 2415 CB GLN A1105 6846 8819 7471 -213 -60 761 C ATOM 2416 CG GLN A1105 70.814 27.474 11.304 1.00 61.80 C ANISOU 2416 CG GLN A1105 7194 8848 7440 -196 -64 782 C ATOM 2417 CD GLN A1105 69.615 28.381 11.477 1.00 61.94 C ANISOU 2417 CD GLN A1105 7338 8828 7368 -75 -241 741 C ATOM 2418 OE1 GLN A1105 68.856 28.298 12.453 1.00 61.18 O ANISOU 2418 OE1 GLN A1105 7127 8798 7320 -5 -343 671 O ATOM 2419 NE2 GLN A1105 69.403 29.260 10.509 1.00 63.22 N ANISOU 2419 NE2 GLN A1105 7760 8874 7386 -37 -277 773 N ATOM 2420 N MET A1106 74.267 27.625 13.183 1.00 64.59 N ANISOU 2420 N MET A1106 7116 9239 8187 -468 108 757 N ATOM 2421 CA MET A1106 75.367 28.583 13.010 1.00 66.15 C ANISOU 2421 CA MET A1106 7313 9358 8463 -628 208 726 C ATOM 2422 C MET A1106 76.688 28.276 13.735 1.00 66.93 C ANISOU 2422 C MET A1106 7138 9537 8755 -684 231 621 C ATOM 2423 O MET A1106 77.737 28.766 13.311 1.00 68.57 O ANISOU 2423 O MET A1106 7292 9699 9062 -849 374 549 O ATOM 2424 CB MET A1106 74.891 30.030 13.257 1.00 66.66 C ANISOU 2424 CB MET A1106 7567 9298 8463 -653 134 749 C ATOM 2425 CG MET A1106 74.402 30.294 14.668 1.00 65.77 C ANISOU 2425 CG MET A1106 7369 9239 8382 -551 -59 713 C ATOM 2426 SD MET A1106 73.100 31.545 14.714 1.00 65.87 S ANISOU 2426 SD MET A1106 7643 9126 8258 -473 -193 745 S ATOM 2427 CE MET A1106 71.673 30.509 14.728 1.00 64.17 C ANISOU 2427 CE MET A1106 7402 9029 7950 -284 -307 742 C ATOM 2428 N GLY A1107 76.624 27.488 14.807 1.00 67.46 N ANISOU 2428 N GLY A1107 7049 9714 8868 -544 95 595 N ATOM 2429 CA GLY A1107 77.798 27.117 15.592 1.00 68.46 C ANISOU 2429 CA GLY A1107 6927 9929 9156 -525 49 478 C ATOM 2430 C GLY A1107 77.928 27.877 16.895 1.00 68.81 C ANISOU 2430 C GLY A1107 6912 9994 9238 -488 -120 415 C ATOM 2431 O GLY A1107 77.296 28.922 17.070 1.00 68.61 O ANISOU 2431 O GLY A1107 7031 9894 9144 -529 -160 451 O ATOM 2432 N GLU A1108 78.769 27.355 17.810 1.00 71.36 N ANISOU 2432 N GLU A1108 7030 10418 9666 -390 -237 305 N ATOM 2433 CA GLU A1108 79.047 27.915 19.142 1.00 72.04 C ANISOU 2433 CA GLU A1108 7039 10551 9782 -323 -428 213 C ATOM 2434 C GLU A1108 79.498 29.383 19.141 1.00 73.29 C ANISOU 2434 C GLU A1108 7160 10648 10038 -507 -390 107 C ATOM 2435 O GLU A1108 79.072 30.145 20.009 1.00 72.99 O ANISOU 2435 O GLU A1108 7189 10593 9950 -480 -517 99 O ATOM 2436 CB GLU A1108 80.018 27.019 19.941 1.00 73.22 C ANISOU 2436 CB GLU A1108 6984 10820 10017 -153 -577 90 C ATOM 2437 CG GLU A1108 81.326 26.688 19.231 1.00 75.49 C ANISOU 2437 CG GLU A1108 7011 11161 10511 -225 -480 -81 C ATOM 2438 CD GLU A1108 81.975 25.362 19.585 1.00 75.82 C ANISOU 2438 CD GLU A1108 6923 11289 10596 -12 -579 -139 C ATOM 2439 OE1 GLU A1108 81.248 24.409 19.949 1.00 74.75 O ANISOU 2439 OE1 GLU A1108 6966 11134 10301 168 -655 11 O ATOM 2440 OE2 GLU A1108 83.215 25.262 19.442 1.00 77.45 O ANISOU 2440 OE2 GLU A1108 6853 11572 11003 -30 -563 -349 O ATOM 2441 N THR A1109 80.335 29.778 18.160 1.00 73.68 N ANISOU 2441 N THR A1109 7122 10651 10222 -708 -192 21 N ATOM 2442 CA THR A1109 80.842 31.147 18.015 1.00 75.39 C ANISOU 2442 CA THR A1109 7329 10770 10546 -930 -89 -90 C ATOM 2443 C THR A1109 79.728 32.097 17.538 1.00 74.51 C ANISOU 2443 C THR A1109 7555 10483 10273 -1002 -27 76 C ATOM 2444 O THR A1109 79.683 33.252 17.967 1.00 75.31 O ANISOU 2444 O THR A1109 7720 10494 10400 -1087 -57 26 O ATOM 2445 CB THR A1109 82.091 31.174 17.111 1.00 77.81 C ANISOU 2445 CB THR A1109 7449 11071 11044 -1141 151 -252 C ATOM 2446 OG1 THR A1109 82.917 30.042 17.398 1.00 78.49 O ANISOU 2446 OG1 THR A1109 7242 11328 11252 -1006 69 -388 O ATOM 2447 CG2 THR A1109 82.909 32.452 17.274 1.00 80.23 C ANISOU 2447 CG2 THR A1109 7651 11306 11526 -1378 249 -452 C ATOM 2448 N GLY A1110 78.846 31.588 16.676 1.00 70.67 N ANISOU 2448 N GLY A1110 7275 9951 9625 -947 38 251 N ATOM 2449 CA GLY A1110 77.715 32.327 16.122 1.00 70.02 C ANISOU 2449 CA GLY A1110 7516 9717 9371 -952 56 395 C ATOM 2450 C GLY A1110 76.641 32.660 17.139 1.00 68.75 C ANISOU 2450 C GLY A1110 7433 9572 9117 -792 -163 433 C ATOM 2451 O GLY A1110 76.144 33.790 17.159 1.00 69.28 O ANISOU 2451 O GLY A1110 7686 9505 9132 -826 -190 452 O ATOM 2452 N VAL A1111 76.276 31.677 17.990 1.00 67.09 N ANISOU 2452 N VAL A1111 7102 9510 8879 -620 -307 436 N ATOM 2453 CA VAL A1111 75.259 31.823 19.043 1.00 66.04 C ANISOU 2453 CA VAL A1111 7025 9414 8653 -476 -483 451 C ATOM 2454 C VAL A1111 75.769 32.747 20.167 1.00 67.14 C ANISOU 2454 C VAL A1111 7078 9559 8873 -503 -596 329 C ATOM 2455 O VAL A1111 74.980 33.503 20.736 1.00 66.93 O ANISOU 2455 O VAL A1111 7160 9489 8781 -457 -693 325 O ATOM 2456 CB VAL A1111 74.723 30.456 19.570 1.00 64.66 C ANISOU 2456 CB VAL A1111 6800 9364 8404 -314 -545 494 C ATOM 2457 CG1 VAL A1111 73.527 30.643 20.503 1.00 63.82 C ANISOU 2457 CG1 VAL A1111 6782 9279 8188 -203 -664 499 C ATOM 2458 CG2 VAL A1111 74.338 29.534 18.417 1.00 63.86 C ANISOU 2458 CG2 VAL A1111 6758 9256 8250 -307 -424 580 C ATOM 2459 N ALA A1112 77.093 32.721 20.442 1.00 69.26 N ANISOU 2459 N ALA A1112 7137 9883 9296 -578 -585 201 N ATOM 2460 CA ALA A1112 77.750 33.559 21.455 1.00 70.75 C ANISOU 2460 CA ALA A1112 7200 10093 9588 -615 -697 37 C ATOM 2461 C ALA A1112 77.682 35.060 21.117 1.00 71.84 C ANISOU 2461 C ALA A1112 7473 10052 9771 -789 -617 3 C ATOM 2462 O ALA A1112 77.784 35.895 22.019 1.00 72.79 O ANISOU 2462 O ALA A1112 7557 10162 9938 -801 -727 -113 O ATOM 2463 CB ALA A1112 79.197 33.127 21.635 1.00 72.49 C ANISOU 2463 CB ALA A1112 7132 10423 9987 -651 -700 -137 C ATOM 2464 N GLY A1113 77.492 35.372 19.833 1.00 72.71 N ANISOU 2464 N GLY A1113 7769 10008 9849 -910 -430 106 N ATOM 2465 CA GLY A1113 77.382 36.732 19.317 1.00 74.04 C ANISOU 2465 CA GLY A1113 8159 9951 10022 -1066 -325 112 C ATOM 2466 C GLY A1113 76.114 37.469 19.708 1.00 73.07 C ANISOU 2466 C GLY A1113 8264 9737 9762 -938 -467 183 C ATOM 2467 O GLY A1113 76.076 38.701 19.634 1.00 74.30 O ANISOU 2467 O GLY A1113 8598 9699 9933 -1034 -431 158 O ATOM 2468 N PHE A1114 75.065 36.729 20.131 1.00 71.14 N ANISOU 2468 N PHE A1114 8019 9620 9391 -725 -615 252 N ATOM 2469 CA PHE A1114 73.777 37.288 20.557 1.00 70.37 C ANISOU 2469 CA PHE A1114 8082 9476 9179 -582 -754 276 C ATOM 2470 C PHE A1114 73.850 37.754 22.026 1.00 70.82 C ANISOU 2470 C PHE A1114 8018 9606 9284 -542 -905 141 C ATOM 2471 O PHE A1114 73.109 37.254 22.877 1.00 69.98 O ANISOU 2471 O PHE A1114 7865 9629 9095 -390 -1025 129 O ATOM 2472 CB PHE A1114 72.642 36.264 20.347 1.00 68.46 C ANISOU 2472 CB PHE A1114 7864 9344 8804 -409 -803 363 C ATOM 2473 CG PHE A1114 72.406 35.838 18.917 1.00 68.14 C ANISOU 2473 CG PHE A1114 7961 9237 8691 -416 -691 475 C ATOM 2474 CD1 PHE A1114 71.559 36.564 18.089 1.00 68.37 C ANISOU 2474 CD1 PHE A1114 8252 9111 8614 -354 -716 525 C ATOM 2475 CD2 PHE A1114 72.999 34.689 18.411 1.00 67.86 C ANISOU 2475 CD2 PHE A1114 7808 9297 8679 -456 -582 519 C ATOM 2476 CE1 PHE A1114 71.334 36.162 16.769 1.00 68.34 C ANISOU 2476 CE1 PHE A1114 8401 9054 8512 -337 -635 619 C ATOM 2477 CE2 PHE A1114 72.773 34.288 17.092 1.00 67.70 C ANISOU 2477 CE2 PHE A1114 7922 9223 8578 -460 -479 610 C ATOM 2478 CZ PHE A1114 71.940 35.027 16.280 1.00 67.95 C ANISOU 2478 CZ PHE A1114 8224 9108 8486 -401 -509 660 C ATOM 2479 N THR A1115 74.747 38.726 22.305 1.00 71.22 N ANISOU 2479 N THR A1115 8028 9565 9467 -693 -879 24 N ATOM 2480 CA THR A1115 75.022 39.303 23.630 1.00 72.13 C ANISOU 2480 CA THR A1115 8023 9737 9646 -683 -1017 -140 C ATOM 2481 C THR A1115 73.765 39.799 24.361 1.00 71.44 C ANISOU 2481 C THR A1115 8062 9639 9443 -528 -1162 -147 C ATOM 2482 O THR A1115 73.592 39.485 25.539 1.00 71.16 O ANISOU 2482 O THR A1115 7915 9760 9363 -421 -1294 -226 O ATOM 2483 CB THR A1115 76.134 40.367 23.538 1.00 74.52 C ANISOU 2483 CB THR A1115 8286 9899 10129 -910 -922 -282 C ATOM 2484 OG1 THR A1115 77.179 39.894 22.684 1.00 75.29 O ANISOU 2484 OG1 THR A1115 8276 9996 10335 -1069 -742 -285 O ATOM 2485 CG2 THR A1115 76.717 40.732 24.901 1.00 75.74 C ANISOU 2485 CG2 THR A1115 8233 10166 10379 -908 -1074 -499 C ATOM 2486 N ASN A1116 72.892 40.551 23.662 1.00 69.37 N ANISOU 2486 N ASN A1116 8043 9193 9122 -501 -1141 -77 N ATOM 2487 CA ASN A1116 71.649 41.090 24.224 1.00 69.06 C ANISOU 2487 CA ASN A1116 8111 9133 8996 -343 -1274 -117 C ATOM 2488 C ASN A1116 70.601 40.001 24.474 1.00 67.27 C ANISOU 2488 C ASN A1116 7824 9090 8645 -170 -1327 -76 C ATOM 2489 O ASN A1116 69.872 40.078 25.464 1.00 67.04 O ANISOU 2489 O ASN A1116 7756 9152 8564 -64 -1424 -168 O ATOM 2490 CB ASN A1116 71.076 42.190 23.330 1.00 70.13 C ANISOU 2490 CB ASN A1116 8536 9003 9107 -331 -1260 -72 C ATOM 2491 CG ASN A1116 71.949 43.414 23.242 1.00 72.34 C ANISOU 2491 CG ASN A1116 8927 9056 9502 -514 -1187 -133 C ATOM 2492 OD1 ASN A1116 71.943 44.277 24.126 1.00 73.60 O ANISOU 2492 OD1 ASN A1116 9077 9168 9720 -520 -1272 -268 O ATOM 2493 ND2 ASN A1116 72.716 43.517 22.169 1.00 73.09 N ANISOU 2493 ND2 ASN A1116 9139 8998 9634 -684 -1006 -49 N ATOM 2494 N SER A1117 70.530 38.995 23.579 1.00 64.69 N ANISOU 2494 N SER A1117 7492 8812 8275 -160 -1240 44 N ATOM 2495 CA SER A1117 69.585 37.879 23.668 1.00 63.27 C ANISOU 2495 CA SER A1117 7255 8786 7999 -33 -1246 73 C ATOM 2496 C SER A1117 69.924 36.927 24.817 1.00 62.70 C ANISOU 2496 C SER A1117 7020 8902 7901 -16 -1256 41 C ATOM 2497 O SER A1117 69.033 36.576 25.589 1.00 62.32 O ANISOU 2497 O SER A1117 6957 8952 7770 77 -1286 -14 O ATOM 2498 CB SER A1117 69.529 37.113 22.349 1.00 62.59 C ANISOU 2498 CB SER A1117 7215 8682 7884 -41 -1147 194 C ATOM 2499 OG SER A1117 69.233 37.962 21.253 1.00 63.50 O ANISOU 2499 OG SER A1117 7540 8610 7977 -32 -1147 236 O ATOM 2500 N LEU A1118 71.210 36.523 24.929 1.00 60.83 N ANISOU 2500 N LEU A1118 6676 8708 7728 -99 -1229 59 N ATOM 2501 CA LEU A1118 71.723 35.598 25.948 1.00 60.79 C ANISOU 2501 CA LEU A1118 6555 8860 7682 -49 -1270 36 C ATOM 2502 C LEU A1118 71.572 36.109 27.384 1.00 61.66 C ANISOU 2502 C LEU A1118 6662 9031 7734 13 -1394 -87 C ATOM 2503 O LEU A1118 71.277 35.312 28.277 1.00 61.50 O ANISOU 2503 O LEU A1118 6655 9124 7588 108 -1416 -87 O ATOM 2504 CB LEU A1118 73.192 35.226 25.668 1.00 61.46 C ANISOU 2504 CB LEU A1118 6504 8970 7877 -127 -1249 33 C ATOM 2505 CG LEU A1118 73.476 34.347 24.444 1.00 60.99 C ANISOU 2505 CG LEU A1118 6425 8898 7851 -170 -1116 146 C ATOM 2506 CD1 LEU A1118 74.895 34.548 23.957 1.00 62.33 C ANISOU 2506 CD1 LEU A1118 6458 9044 8180 -300 -1065 87 C ATOM 2507 CD2 LEU A1118 73.226 32.873 24.736 1.00 59.71 C ANISOU 2507 CD2 LEU A1118 6247 8851 7590 -54 -1103 218 C ATOM 2508 N ARG A1119 71.778 37.427 27.603 1.00 62.06 N ANISOU 2508 N ARG A1119 6724 8991 7865 -46 -1460 -193 N ATOM 2509 CA ARG A1119 71.669 38.083 28.914 1.00 63.14 C ANISOU 2509 CA ARG A1119 6860 9174 7957 3 -1583 -336 C ATOM 2510 C ARG A1119 70.253 38.012 29.488 1.00 62.60 C ANISOU 2510 C ARG A1119 6888 9148 7750 110 -1581 -358 C ATOM 2511 O ARG A1119 70.094 37.856 30.700 1.00 63.25 O ANISOU 2511 O ARG A1119 6981 9333 7718 180 -1641 -437 O ATOM 2512 CB ARG A1119 72.145 39.541 28.840 1.00 64.53 C ANISOU 2512 CB ARG A1119 7039 9208 8272 -104 -1626 -451 C ATOM 2513 CG ARG A1119 73.656 39.689 28.905 1.00 66.15 C ANISOU 2513 CG ARG A1119 7088 9428 8618 -216 -1651 -542 C ATOM 2514 CD ARG A1119 74.096 41.095 28.557 1.00 67.76 C ANISOU 2514 CD ARG A1119 7319 9443 8984 -377 -1621 -646 C ATOM 2515 NE ARG A1119 75.555 41.208 28.524 1.00 68.84 N ANISOU 2515 NE ARG A1119 7265 9598 9293 -520 -1605 -774 N ATOM 2516 CZ ARG A1119 76.218 42.309 28.186 1.00 70.88 C ANISOU 2516 CZ ARG A1119 7512 9691 9728 -715 -1532 -896 C ATOM 2517 NH1 ARG A1119 75.561 43.410 27.841 1.00 72.03 N ANISOU 2517 NH1 ARG A1119 7872 9615 9881 -769 -1482 -877 N ATOM 2518 NH2 ARG A1119 77.545 42.317 28.187 1.00 72.07 N ANISOU 2518 NH2 ARG A1119 7439 9887 10057 -856 -1502 -1058 N ATOM 2519 N MET A1120 69.232 38.121 28.615 1.00 64.84 N ANISOU 2519 N MET A1120 7240 9357 8040 127 -1511 -310 N ATOM 2520 CA MET A1120 67.820 38.058 28.997 1.00 64.56 C ANISOU 2520 CA MET A1120 7248 9367 7915 218 -1490 -378 C ATOM 2521 C MET A1120 67.325 36.614 29.141 1.00 63.63 C ANISOU 2521 C MET A1120 7116 9373 7688 250 -1373 -314 C ATOM 2522 O MET A1120 66.406 36.366 29.924 1.00 63.85 O ANISOU 2522 O MET A1120 7164 9477 7619 294 -1323 -403 O ATOM 2523 CB MET A1120 66.945 38.863 28.024 1.00 64.66 C ANISOU 2523 CB MET A1120 7326 9248 7994 255 -1507 -406 C ATOM 2524 CG MET A1120 67.069 40.360 28.215 1.00 66.01 C ANISOU 2524 CG MET A1120 7565 9277 8238 253 -1613 -507 C ATOM 2525 SD MET A1120 66.185 41.308 26.957 1.00 66.66 S ANISOU 2525 SD MET A1120 7801 9153 8373 338 -1664 -510 S ATOM 2526 CE MET A1120 66.589 42.963 27.469 1.00 68.48 C ANISOU 2526 CE MET A1120 8135 9200 8683 311 -1767 -625 C ATOM 2527 N LEU A1121 67.943 35.665 28.402 1.00 63.76 N ANISOU 2527 N LEU A1121 7106 9398 7722 214 -1308 -176 N ATOM 2528 CA LEU A1121 67.611 34.237 28.466 1.00 63.09 C ANISOU 2528 CA LEU A1121 7031 9396 7544 231 -1185 -104 C ATOM 2529 C LEU A1121 68.130 33.623 29.768 1.00 63.87 C ANISOU 2529 C LEU A1121 7183 9578 7507 271 -1201 -100 C ATOM 2530 O LEU A1121 67.486 32.731 30.323 1.00 64.08 O ANISOU 2530 O LEU A1121 7291 9654 7403 293 -1085 -93 O ATOM 2531 CB LEU A1121 68.175 33.473 27.254 1.00 62.23 C ANISOU 2531 CB LEU A1121 6886 9256 7502 192 -1123 31 C ATOM 2532 CG LEU A1121 67.448 33.653 25.918 1.00 61.57 C ANISOU 2532 CG LEU A1121 6802 9107 7485 182 -1080 43 C ATOM 2533 CD1 LEU A1121 68.352 33.294 24.756 1.00 61.10 C ANISOU 2533 CD1 LEU A1121 6725 8996 7494 126 -1044 165 C ATOM 2534 CD2 LEU A1121 66.163 32.841 25.861 1.00 61.30 C ANISOU 2534 CD2 LEU A1121 6758 9135 7398 213 -971 -11 C ATOM 2535 N GLN A1122 69.292 34.112 30.252 1.00 66.43 N ANISOU 2535 N GLN A1122 7475 9909 7856 281 -1342 -121 N ATOM 2536 CA GLN A1122 69.939 33.689 31.498 1.00 67.67 C ANISOU 2536 CA GLN A1122 7695 10146 7871 363 -1426 -141 C ATOM 2537 C GLN A1122 69.117 34.166 32.705 1.00 68.62 C ANISOU 2537 C GLN A1122 7921 10306 7845 401 -1432 -258 C ATOM 2538 O GLN A1122 69.045 33.464 33.714 1.00 69.54 O ANISOU 2538 O GLN A1122 8185 10478 7759 474 -1410 -246 O ATOM 2539 CB GLN A1122 71.366 34.258 31.567 1.00 68.59 C ANISOU 2539 CB GLN A1122 7691 10270 8099 361 -1598 -199 C ATOM 2540 CG GLN A1122 72.262 33.584 32.600 1.00 70.33 C ANISOU 2540 CG GLN A1122 7954 10583 8185 491 -1732 -219 C ATOM 2541 CD GLN A1122 73.548 34.343 32.804 1.00 71.61 C ANISOU 2541 CD GLN A1122 7948 10778 8483 488 -1920 -361 C ATOM 2542 OE1 GLN A1122 74.418 34.398 31.926 1.00 72.03 O ANISOU 2542 OE1 GLN A1122 7832 10803 8734 407 -1915 -369 O ATOM 2543 NE2 GLN A1122 73.704 34.936 33.977 1.00 72.50 N ANISOU 2543 NE2 GLN A1122 8097 10955 8494 568 -2079 -501 N ATOM 2544 N GLN A1123 68.490 35.354 32.583 1.00 68.55 N ANISOU 2544 N GLN A1123 7864 10254 7928 360 -1454 -372 N ATOM 2545 CA GLN A1123 67.640 35.976 33.603 1.00 69.47 C ANISOU 2545 CA GLN A1123 8048 10404 7943 388 -1451 -519 C ATOM 2546 C GLN A1123 66.226 35.366 33.626 1.00 69.22 C ANISOU 2546 C GLN A1123 8070 10399 7832 374 -1249 -544 C ATOM 2547 O GLN A1123 65.398 35.769 34.448 1.00 70.10 O ANISOU 2547 O GLN A1123 8227 10548 7860 385 -1200 -687 O ATOM 2548 CB GLN A1123 67.546 37.488 33.351 1.00 69.63 C ANISOU 2548 CB GLN A1123 7991 10345 8120 361 -1558 -644 C ATOM 2549 CG GLN A1123 68.748 38.286 33.835 1.00 71.00 C ANISOU 2549 CG GLN A1123 8123 10508 8346 354 -1734 -717 C ATOM 2550 CD GLN A1123 68.577 39.761 33.562 1.00 71.64 C ANISOU 2550 CD GLN A1123 8171 10472 8577 313 -1805 -841 C ATOM 2551 OE1 GLN A1123 69.299 40.354 32.755 1.00 71.79 O ANISOU 2551 OE1 GLN A1123 8137 10376 8764 236 -1846 -821 O ATOM 2552 NE2 GLN A1123 67.609 40.385 34.219 1.00 72.29 N ANISOU 2552 NE2 GLN A1123 8301 10564 8602 360 -1802 -979 N ATOM 2553 N LYS A1124 65.959 34.403 32.714 1.00 67.86 N ANISOU 2553 N LYS A1124 7876 10210 7698 340 -1120 -433 N ATOM 2554 CA LYS A1124 64.687 33.695 32.521 1.00 67.77 C ANISOU 2554 CA LYS A1124 7871 10221 7658 300 -909 -479 C ATOM 2555 C LYS A1124 63.538 34.582 31.999 1.00 67.76 C ANISOU 2555 C LYS A1124 7744 10209 7793 302 -909 -654 C ATOM 2556 O LYS A1124 62.364 34.218 32.117 1.00 68.39 O ANISOU 2556 O LYS A1124 7790 10336 7859 273 -746 -787 O ATOM 2557 CB LYS A1124 64.301 32.809 33.727 1.00 69.15 C ANISOU 2557 CB LYS A1124 8223 10445 7606 286 -735 -492 C ATOM 2558 CG LYS A1124 65.198 31.587 33.891 1.00 69.31 C ANISOU 2558 CG LYS A1124 8396 10444 7495 313 -708 -299 C ATOM 2559 CD LYS A1124 64.687 30.638 34.964 1.00 70.75 C ANISOU 2559 CD LYS A1124 8828 10627 7427 293 -494 -292 C ATOM 2560 CE LYS A1124 65.542 29.398 35.059 1.00 71.16 C ANISOU 2560 CE LYS A1124 9070 10625 7343 354 -485 -95 C ATOM 2561 NZ LYS A1124 65.000 28.427 36.044 1.00 72.78 N ANISOU 2561 NZ LYS A1124 9593 10782 7278 328 -242 -65 N ATOM 2562 N ARG A1125 63.894 35.728 31.380 1.00 68.02 N ANISOU 2562 N ARG A1125 7713 10169 7963 339 -1090 -668 N ATOM 2563 CA ARG A1125 62.960 36.670 30.759 1.00 68.26 C ANISOU 2563 CA ARG A1125 7663 10153 8119 393 -1152 -817 C ATOM 2564 C ARG A1125 62.755 36.164 29.331 1.00 67.30 C ANISOU 2564 C ARG A1125 7491 9993 8087 397 -1130 -735 C ATOM 2565 O ARG A1125 63.663 36.275 28.504 1.00 66.70 O ANISOU 2565 O ARG A1125 7448 9833 8063 383 -1207 -582 O ATOM 2566 CB ARG A1125 63.544 38.099 30.758 1.00 68.79 C ANISOU 2566 CB ARG A1125 7759 10114 8263 430 -1345 -844 C ATOM 2567 CG ARG A1125 63.652 38.737 32.141 1.00 69.90 C ANISOU 2567 CG ARG A1125 7937 10296 8326 439 -1389 -971 C ATOM 2568 CD ARG A1125 64.770 39.762 32.211 1.00 70.30 C ANISOU 2568 CD ARG A1125 8022 10246 8443 424 -1553 -944 C ATOM 2569 NE ARG A1125 64.446 41.001 31.500 1.00 70.92 N ANISOU 2569 NE ARG A1125 8116 10171 8660 469 -1659 -1015 N ATOM 2570 CZ ARG A1125 65.320 41.968 31.240 1.00 71.47 C ANISOU 2570 CZ ARG A1125 8237 10096 8822 429 -1765 -992 C ATOM 2571 NH1 ARG A1125 66.587 41.849 31.619 1.00 71.46 N ANISOU 2571 NH1 ARG A1125 8219 10114 8819 339 -1790 -933 N ATOM 2572 NH2 ARG A1125 64.937 43.058 30.591 1.00 72.35 N ANISOU 2572 NH2 ARG A1125 8425 10032 9033 483 -1846 -1045 N ATOM 2573 N TRP A1126 61.594 35.543 29.062 1.00 68.95 N ANISOU 2573 N TRP A1126 7616 10271 8311 403 -1007 -854 N ATOM 2574 CA TRP A1126 61.305 34.933 27.762 1.00 68.26 C ANISOU 2574 CA TRP A1126 7472 10172 8292 414 -984 -810 C ATOM 2575 C TRP A1126 60.735 35.869 26.705 1.00 68.54 C ANISOU 2575 C TRP A1126 7478 10135 8429 543 -1155 -903 C ATOM 2576 O TRP A1126 61.217 35.851 25.571 1.00 67.85 O ANISOU 2576 O TRP A1126 7448 9967 8365 563 -1223 -764 O ATOM 2577 CB TRP A1126 60.468 33.649 27.912 1.00 68.49 C ANISOU 2577 CB TRP A1126 7423 10303 8297 340 -759 -898 C ATOM 2578 CG TRP A1126 60.916 32.745 29.028 1.00 68.61 C ANISOU 2578 CG TRP A1126 7544 10353 8172 236 -581 -806 C ATOM 2579 CD1 TRP A1126 60.197 32.396 30.133 1.00 69.90 C ANISOU 2579 CD1 TRP A1126 7728 10582 8249 171 -393 -948 C ATOM 2580 CD2 TRP A1126 62.205 32.128 29.176 1.00 67.83 C ANISOU 2580 CD2 TRP A1126 7572 10214 7986 204 -585 -563 C ATOM 2581 NE1 TRP A1126 60.946 31.579 30.948 1.00 70.02 N ANISOU 2581 NE1 TRP A1126 7926 10581 8098 112 -284 -782 N ATOM 2582 CE2 TRP A1126 62.185 31.404 30.389 1.00 68.75 C ANISOU 2582 CE2 TRP A1126 7817 10363 7942 149 -422 -554 C ATOM 2583 CE3 TRP A1126 63.376 32.109 28.397 1.00 66.74 C ANISOU 2583 CE3 TRP A1126 7456 10014 7888 221 -705 -370 C ATOM 2584 CZ2 TRP A1126 63.285 30.663 30.837 1.00 68.66 C ANISOU 2584 CZ2 TRP A1126 7962 10321 7804 151 -420 -357 C ATOM 2585 CZ3 TRP A1126 64.470 31.389 28.851 1.00 66.59 C ANISOU 2585 CZ3 TRP A1126 7536 9987 7779 205 -689 -206 C ATOM 2586 CH2 TRP A1126 64.420 30.678 30.057 1.00 67.56 C ANISOU 2586 CH2 TRP A1126 7792 10140 7737 191 -571 -199 C ATOM 2587 N ASP A1127 59.719 36.677 27.065 1.00 70.29 N ANISOU 2587 N ASP A1127 7630 10379 8698 643 -1226 -1145 N ATOM 2588 CA ASP A1127 59.067 37.628 26.158 1.00 71.11 C ANISOU 2588 CA ASP A1127 7734 10402 8882 821 -1427 -1266 C ATOM 2589 C ASP A1127 59.998 38.758 25.704 1.00 71.17 C ANISOU 2589 C ASP A1127 7942 10215 8885 869 -1599 -1100 C ATOM 2590 O ASP A1127 59.885 39.218 24.566 1.00 71.64 O ANISOU 2590 O ASP A1127 8104 10157 8958 986 -1735 -1063 O ATOM 2591 CB ASP A1127 57.782 38.194 26.791 1.00 72.84 C ANISOU 2591 CB ASP A1127 7812 10699 9164 929 -1462 -1599 C ATOM 2592 CG ASP A1127 56.602 37.234 26.830 1.00 73.32 C ANISOU 2592 CG ASP A1127 7648 10933 9277 900 -1299 -1844 C ATOM 2593 OD1 ASP A1127 56.832 36.002 26.836 1.00 74.76 O ANISOU 2593 OD1 ASP A1127 7807 11179 9420 751 -1104 -1737 O ATOM 2594 OD2 ASP A1127 55.450 37.715 26.889 1.00 72.57 O ANISOU 2594 OD2 ASP A1127 7395 10906 9273 1021 -1356 -2164 O ATOM 2595 N GLU A1128 60.918 39.190 26.587 1.00 70.72 N ANISOU 2595 N GLU A1128 7956 10115 8800 774 -1585 -1012 N ATOM 2596 CA GLU A1128 61.889 40.253 26.312 1.00 71.07 C ANISOU 2596 CA GLU A1128 8174 9968 8861 764 -1700 -884 C ATOM 2597 C GLU A1128 63.022 39.775 25.401 1.00 70.05 C ANISOU 2597 C GLU A1128 8132 9766 8718 656 -1645 -637 C ATOM 2598 O GLU A1128 63.442 40.522 24.515 1.00 70.63 O ANISOU 2598 O GLU A1128 8374 9655 8807 676 -1718 -546 O ATOM 2599 CB GLU A1128 62.440 40.843 27.619 1.00 71.55 C ANISOU 2599 CB GLU A1128 8237 10034 8915 694 -1704 -930 C ATOM 2600 CG GLU A1128 61.425 41.689 28.366 1.00 72.96 C ANISOU 2600 CG GLU A1128 8375 10227 9119 813 -1782 -1180 C ATOM 2601 CD GLU A1128 61.811 42.021 29.792 1.00 73.42 C ANISOU 2601 CD GLU A1128 8412 10346 9138 742 -1757 -1258 C ATOM 2602 OE1 GLU A1128 62.241 43.171 30.035 1.00 74.47 O ANISOU 2602 OE1 GLU A1128 8637 10344 9315 754 -1868 -1292 O ATOM 2603 OE2 GLU A1128 61.685 41.134 30.666 1.00 72.99 O ANISOU 2603 OE2 GLU A1128 8275 10462 8996 675 -1621 -1289 O ATOM 2604 N ALA A1129 63.505 38.531 25.611 1.00 68.34 N ANISOU 2604 N ALA A1129 7821 9680 8465 543 -1504 -538 N ATOM 2605 CA ALA A1129 64.567 37.914 24.810 1.00 67.45 C ANISOU 2605 CA ALA A1129 7748 9530 8350 442 -1434 -335 C ATOM 2606 C ALA A1129 64.067 37.551 23.410 1.00 67.25 C ANISOU 2606 C ALA A1129 7768 9468 8316 509 -1436 -292 C ATOM 2607 O ALA A1129 64.858 37.542 22.465 1.00 67.20 O ANISOU 2607 O ALA A1129 7863 9362 8308 452 -1410 -141 O ATOM 2608 CB ALA A1129 65.099 36.674 25.507 1.00 66.56 C ANISOU 2608 CB ALA A1129 7533 9562 8195 350 -1310 -271 C ATOM 2609 N ALA A1130 62.754 37.261 23.285 1.00 65.44 N ANISOU 2609 N ALA A1130 7456 9325 8083 627 -1462 -450 N ATOM 2610 CA ALA A1130 62.073 36.909 22.036 1.00 65.62 C ANISOU 2610 CA ALA A1130 7495 9344 8093 729 -1502 -475 C ATOM 2611 C ALA A1130 62.152 38.033 21.001 1.00 66.82 C ANISOU 2611 C ALA A1130 7879 9294 8215 848 -1660 -423 C ATOM 2612 O ALA A1130 62.276 37.750 19.809 1.00 66.86 O ANISOU 2612 O ALA A1130 7992 9244 8168 879 -1668 -328 O ATOM 2613 CB ALA A1130 60.621 36.569 22.318 1.00 66.25 C ANISOU 2613 CB ALA A1130 7398 9566 8207 835 -1517 -734 C ATOM 2614 N VAL A1131 62.085 39.300 21.462 1.00 67.23 N ANISOU 2614 N VAL A1131 8039 9219 8286 915 -1777 -483 N ATOM 2615 CA VAL A1131 62.163 40.504 20.626 1.00 68.88 C ANISOU 2615 CA VAL A1131 8537 9182 8451 1032 -1920 -431 C ATOM 2616 C VAL A1131 63.589 40.643 20.062 1.00 68.75 C ANISOU 2616 C VAL A1131 8709 9007 8406 846 -1798 -187 C ATOM 2617 O VAL A1131 63.746 40.920 18.872 1.00 69.74 O ANISOU 2617 O VAL A1131 9083 8969 8446 894 -1821 -76 O ATOM 2618 CB VAL A1131 61.697 41.782 21.388 1.00 70.41 C ANISOU 2618 CB VAL A1131 8791 9274 8688 1147 -2062 -582 C ATOM 2619 CG1 VAL A1131 61.623 42.992 20.457 1.00 72.48 C ANISOU 2619 CG1 VAL A1131 9407 9246 8885 1308 -2221 -534 C ATOM 2620 CG2 VAL A1131 60.350 41.560 22.074 1.00 70.87 C ANISOU 2620 CG2 VAL A1131 8605 9523 8799 1295 -2137 -863 C ATOM 2621 N ASN A1132 64.615 40.417 20.915 1.00 68.64 N ANISOU 2621 N ASN A1132 8575 9048 8458 639 -1666 -126 N ATOM 2622 CA ASN A1132 66.036 40.478 20.554 1.00 68.71 C ANISOU 2622 CA ASN A1132 8673 8948 8486 435 -1528 41 C ATOM 2623 C ASN A1132 66.415 39.397 19.536 1.00 67.92 C ANISOU 2623 C ASN A1132 8562 8905 8340 375 -1410 171 C ATOM 2624 O ASN A1132 67.192 39.672 18.619 1.00 68.81 O ANISOU 2624 O ASN A1132 8863 8859 8423 278 -1320 298 O ATOM 2625 CB ASN A1132 66.918 40.370 21.799 1.00 68.03 C ANISOU 2625 CB ASN A1132 8398 8960 8490 278 -1462 11 C ATOM 2626 CG ASN A1132 66.840 41.567 22.709 1.00 69.17 C ANISOU 2626 CG ASN A1132 8585 9013 8684 295 -1557 -108 C ATOM 2627 OD1 ASN A1132 67.504 42.586 22.495 1.00 70.54 O ANISOU 2627 OD1 ASN A1132 8926 8976 8901 206 -1541 -82 O ATOM 2628 ND2 ASN A1132 66.039 41.461 23.759 1.00 68.81 N ANISOU 2628 ND2 ASN A1132 8394 9114 8636 393 -1632 -254 N ATOM 2629 N LEU A1133 65.859 38.176 19.696 1.00 64.07 N ANISOU 2629 N LEU A1133 7867 8632 7844 418 -1387 129 N ATOM 2630 CA LEU A1133 66.097 37.038 18.802 1.00 63.24 C ANISOU 2630 CA LEU A1133 7727 8599 7702 376 -1281 224 C ATOM 2631 C LEU A1133 65.422 37.243 17.441 1.00 64.27 C ANISOU 2631 C LEU A1133 8064 8630 7725 520 -1360 239 C ATOM 2632 O LEU A1133 65.952 36.789 16.426 1.00 64.35 O ANISOU 2632 O LEU A1133 8170 8601 7679 461 -1266 356 O ATOM 2633 CB LEU A1133 65.634 35.719 19.444 1.00 61.75 C ANISOU 2633 CB LEU A1133 7287 8636 7539 377 -1224 157 C ATOM 2634 CG LEU A1133 66.472 35.183 20.610 1.00 60.95 C ANISOU 2634 CG LEU A1133 7031 8635 7493 252 -1136 182 C ATOM 2635 CD1 LEU A1133 65.634 34.314 21.523 1.00 60.27 C ANISOU 2635 CD1 LEU A1133 6791 8713 7396 293 -1106 78 C ATOM 2636 CD2 LEU A1133 67.686 34.410 20.118 1.00 60.45 C ANISOU 2636 CD2 LEU A1133 6936 8579 7453 127 -1010 317 C ATOM 2637 N ALA A1134 64.260 37.931 17.425 1.00 64.68 N ANISOU 2637 N ALA A1134 8189 8644 7742 727 -1546 103 N ATOM 2638 CA ALA A1134 63.515 38.253 16.204 1.00 66.23 C ANISOU 2638 CA ALA A1134 8607 8741 7816 931 -1690 82 C ATOM 2639 C ALA A1134 64.224 39.374 15.439 1.00 68.02 C ANISOU 2639 C ALA A1134 9230 8672 7942 911 -1687 241 C ATOM 2640 O ALA A1134 64.146 39.422 14.211 1.00 69.31 O ANISOU 2640 O ALA A1134 9655 8722 7957 1003 -1719 319 O ATOM 2641 CB ALA A1134 62.096 38.673 16.550 1.00 67.22 C ANISOU 2641 CB ALA A1134 8657 8924 7959 1179 -1909 -156 C ATOM 2642 N LYS A1135 64.917 40.270 16.174 1.00 68.43 N ANISOU 2642 N LYS A1135 9343 8591 8066 784 -1634 278 N ATOM 2643 CA LYS A1135 65.682 41.389 15.624 1.00 70.35 C ANISOU 2643 CA LYS A1135 9959 8526 8245 702 -1573 412 C ATOM 2644 C LYS A1135 67.136 40.944 15.396 1.00 69.68 C ANISOU 2644 C LYS A1135 9837 8429 8210 397 -1300 554 C ATOM 2645 O LYS A1135 68.046 41.386 16.106 1.00 69.70 O ANISOU 2645 O LYS A1135 9767 8381 8335 198 -1187 553 O ATOM 2646 CB LYS A1135 65.606 42.615 16.556 1.00 71.33 C ANISOU 2646 CB LYS A1135 10145 8509 8448 720 -1658 328 C ATOM 2647 CG LYS A1135 64.272 43.345 16.535 1.00 72.76 C ANISOU 2647 CG LYS A1135 10461 8618 8566 1042 -1930 189 C ATOM 2648 CD LYS A1135 64.230 44.422 17.606 1.00 73.43 C ANISOU 2648 CD LYS A1135 10544 8600 8756 1042 -1997 83 C ATOM 2649 CE LYS A1135 62.936 45.196 17.594 1.00 74.94 C ANISOU 2649 CE LYS A1135 10863 8709 8902 1379 -2274 -80 C ATOM 2650 NZ LYS A1135 62.901 46.219 18.672 1.00 75.77 N ANISOU 2650 NZ LYS A1135 10952 8720 9117 1374 -2330 -198 N ATOM 2651 N SER A1136 67.342 40.039 14.416 1.00 70.04 N ANISOU 2651 N SER A1136 9904 8537 8171 368 -1201 642 N ATOM 2652 CA SER A1136 68.658 39.483 14.076 1.00 69.56 C ANISOU 2652 CA SER A1136 9779 8489 8161 102 -941 746 C ATOM 2653 C SER A1136 68.745 38.984 12.624 1.00 70.51 C ANISOU 2653 C SER A1136 10124 8553 8114 113 -846 858 C ATOM 2654 O SER A1136 67.727 38.922 11.929 1.00 71.36 O ANISOU 2654 O SER A1136 10402 8648 8063 349 -1013 846 O ATOM 2655 CB SER A1136 69.016 38.350 15.036 1.00 67.12 C ANISOU 2655 CB SER A1136 9027 8465 8011 12 -891 680 C ATOM 2656 OG SER A1136 68.105 37.269 14.926 1.00 65.91 O ANISOU 2656 OG SER A1136 8715 8511 7816 165 -979 633 O ATOM 2657 N ARG A1137 69.971 38.620 12.181 1.00 71.23 N ANISOU 2657 N ARG A1137 10198 8621 8245 -136 -585 938 N ATOM 2658 CA ARG A1137 70.263 38.079 10.850 1.00 72.18 C ANISOU 2658 CA ARG A1137 10509 8700 8216 -176 -439 1038 C ATOM 2659 C ARG A1137 69.642 36.681 10.711 1.00 70.22 C ANISOU 2659 C ARG A1137 9996 8722 7962 -44 -525 987 C ATOM 2660 O ARG A1137 69.142 36.339 9.639 1.00 70.95 O ANISOU 2660 O ARG A1137 10282 8800 7875 83 -564 1021 O ATOM 2661 CB ARG A1137 71.785 38.015 10.623 1.00 72.93 C ANISOU 2661 CB ARG A1137 10564 8735 8412 -502 -114 1081 C ATOM 2662 CG ARG A1137 72.196 37.704 9.186 1.00 74.37 C ANISOU 2662 CG ARG A1137 11019 8819 8419 -582 91 1183 C ATOM 2663 CD ARG A1137 73.571 37.071 9.126 1.00 74.46 C ANISOU 2663 CD ARG A1137 10780 8915 8596 -873 390 1152 C ATOM 2664 NE ARG A1137 73.907 36.627 7.773 1.00 75.76 N ANISOU 2664 NE ARG A1137 11169 9022 8594 -945 597 1230 N ATOM 2665 CZ ARG A1137 75.045 36.024 7.439 1.00 76.47 C ANISOU 2665 CZ ARG A1137 11082 9178 8795 -1182 878 1191 C ATOM 2666 NH1 ARG A1137 75.976 35.790 8.357 1.00 76.13 N ANISOU 2666 NH1 ARG A1137 10625 9263 9038 -1351 961 1067 N ATOM 2667 NH2 ARG A1137 75.264 35.657 6.183 1.00 77.81 N ANISOU 2667 NH2 ARG A1137 11486 9291 8788 -1237 1069 1256 N ATOM 2668 N TRP A1138 69.669 35.893 11.808 1.00 66.85 N ANISOU 2668 N TRP A1138 9153 8526 7721 -71 -554 899 N ATOM 2669 CA TRP A1138 69.126 34.535 11.921 1.00 64.98 C ANISOU 2669 CA TRP A1138 8642 8530 7517 17 -602 836 C ATOM 2670 C TRP A1138 67.643 34.464 11.523 1.00 65.23 C ANISOU 2670 C TRP A1138 8754 8605 7425 278 -821 753 C ATOM 2671 O TRP A1138 67.245 33.515 10.846 1.00 65.18 O ANISOU 2671 O TRP A1138 8695 8709 7362 343 -821 725 O ATOM 2672 CB TRP A1138 69.373 33.991 13.345 1.00 63.19 C ANISOU 2672 CB TRP A1138 8054 8476 7479 -43 -605 764 C ATOM 2673 CG TRP A1138 68.637 32.733 13.711 1.00 61.52 C ANISOU 2673 CG TRP A1138 7602 8472 7301 50 -654 688 C ATOM 2674 CD1 TRP A1138 68.677 31.535 13.058 1.00 60.83 C ANISOU 2674 CD1 TRP A1138 7434 8482 7197 42 -566 699 C ATOM 2675 CD2 TRP A1138 67.825 32.529 14.874 1.00 60.60 C ANISOU 2675 CD2 TRP A1138 7302 8476 7247 134 -763 580 C ATOM 2676 NE1 TRP A1138 67.905 30.609 13.720 1.00 59.63 N ANISOU 2676 NE1 TRP A1138 7074 8485 7097 111 -611 606 N ATOM 2677 CE2 TRP A1138 67.371 31.192 14.840 1.00 59.53 C ANISOU 2677 CE2 TRP A1138 7000 8490 7128 162 -719 533 C ATOM 2678 CE3 TRP A1138 67.416 33.355 15.935 1.00 60.81 C ANISOU 2678 CE3 TRP A1138 7303 8489 7313 180 -876 507 C ATOM 2679 CZ2 TRP A1138 66.531 30.661 15.827 1.00 58.81 C ANISOU 2679 CZ2 TRP A1138 6737 8522 7086 214 -756 419 C ATOM 2680 CZ3 TRP A1138 66.583 32.829 16.910 1.00 60.00 C ANISOU 2680 CZ3 TRP A1138 7018 8528 7251 245 -924 391 C ATOM 2681 CH2 TRP A1138 66.148 31.498 16.850 1.00 59.09 C ANISOU 2681 CH2 TRP A1138 6757 8548 7146 252 -852 351 C ATOM 2682 N TYR A1139 66.845 35.477 11.915 1.00 67.80 N ANISOU 2682 N TYR A1139 9196 8845 7720 431 -1012 688 N ATOM 2683 CA TYR A1139 65.424 35.559 11.574 1.00 68.53 C ANISOU 2683 CA TYR A1139 9343 8978 7717 707 -1253 557 C ATOM 2684 C TYR A1139 65.221 36.008 10.120 1.00 70.86 C ANISOU 2684 C TYR A1139 10047 9102 7774 850 -1326 626 C ATOM 2685 O TYR A1139 64.263 35.572 9.482 1.00 71.42 O ANISOU 2685 O TYR A1139 10121 9264 7751 1059 -1490 513 O ATOM 2686 CB TYR A1139 64.666 36.474 12.557 1.00 68.78 C ANISOU 2686 CB TYR A1139 9333 8986 7815 837 -1437 433 C ATOM 2687 CG TYR A1139 63.180 36.581 12.281 1.00 69.82 C ANISOU 2687 CG TYR A1139 9461 9182 7885 1136 -1700 238 C ATOM 2688 CD1 TYR A1139 62.322 35.517 12.549 1.00 68.81 C ANISOU 2688 CD1 TYR A1139 8998 9301 7845 1191 -1733 51 C ATOM 2689 CD2 TYR A1139 62.630 37.745 11.753 1.00 72.20 C ANISOU 2689 CD2 TYR A1139 10097 9288 8048 1369 -1915 215 C ATOM 2690 CE1 TYR A1139 60.958 35.602 12.280 1.00 70.15 C ANISOU 2690 CE1 TYR A1139 9112 9551 7990 1459 -1972 -187 C ATOM 2691 CE2 TYR A1139 61.265 37.846 11.489 1.00 73.56 C ANISOU 2691 CE2 TYR A1139 10236 9536 8178 1681 -2193 -9 C ATOM 2692 CZ TYR A1139 60.431 36.772 11.757 1.00 72.54 C ANISOU 2692 CZ TYR A1139 9715 9684 8164 1719 -2220 -228 C ATOM 2693 OH TYR A1139 59.084 36.864 11.503 1.00 74.19 O ANISOU 2693 OH TYR A1139 9837 9988 8364 2018 -2491 -507 O ATOM 2694 N ASN A1140 66.116 36.872 9.602 1.00 73.78 N ANISOU 2694 N ASN A1140 10773 9220 8040 735 -1199 794 N ATOM 2695 CA ASN A1140 66.051 37.379 8.228 1.00 76.44 C ANISOU 2695 CA ASN A1140 11596 9344 8104 853 -1229 895 C ATOM 2696 C ASN A1140 66.381 36.290 7.196 1.00 76.17 C ANISOU 2696 C ASN A1140 11562 9409 7970 790 -1090 942 C ATOM 2697 O ASN A1140 65.749 36.245 6.140 1.00 77.75 O ANISOU 2697 O ASN A1140 12029 9571 7942 1004 -1231 928 O ATOM 2698 CB ASN A1140 66.967 38.591 8.053 1.00 78.57 C ANISOU 2698 CB ASN A1140 12262 9290 8301 694 -1066 1056 C ATOM 2699 CG ASN A1140 66.747 39.334 6.760 1.00 81.89 C ANISOU 2699 CG ASN A1140 13289 9429 8396 856 -1122 1168 C ATOM 2700 OD1 ASN A1140 67.347 39.024 5.725 1.00 82.83 O ANISOU 2700 OD1 ASN A1140 13651 9471 8350 746 -926 1286 O ATOM 2701 ND2 ASN A1140 65.875 40.331 6.790 1.00 84.00 N ANISOU 2701 ND2 ASN A1140 13837 9530 8549 1135 -1394 1127 N ATOM 2702 N GLN A1141 67.364 35.419 7.507 1.00 73.40 N ANISOU 2702 N GLN A1141 10917 9188 7784 521 -834 979 N ATOM 2703 CA GLN A1141 67.794 34.325 6.630 1.00 73.01 C ANISOU 2703 CA GLN A1141 10822 9240 7678 435 -672 1010 C ATOM 2704 C GLN A1141 66.801 33.157 6.677 1.00 71.51 C ANISOU 2704 C GLN A1141 10322 9309 7540 596 -829 849 C ATOM 2705 O GLN A1141 66.323 32.724 5.626 1.00 72.60 O ANISOU 2705 O GLN A1141 10601 9478 7506 733 -899 814 O ATOM 2706 CB GLN A1141 69.222 33.849 6.980 1.00 71.84 C ANISOU 2706 CB GLN A1141 10458 9128 7710 112 -357 1077 C ATOM 2707 CG GLN A1141 70.317 34.915 6.864 1.00 73.32 C ANISOU 2707 CG GLN A1141 10907 9069 7883 -107 -141 1190 C ATOM 2708 CD GLN A1141 70.708 35.226 5.441 1.00 76.20 C ANISOU 2708 CD GLN A1141 11734 9230 7988 -160 30 1306 C ATOM 2709 OE1 GLN A1141 70.099 36.068 4.771 1.00 78.30 O ANISOU 2709 OE1 GLN A1141 12456 9293 8002 13 -94 1369 O ATOM 2710 NE2 GLN A1141 71.757 34.577 4.960 1.00 76.72 N ANISOU 2710 NE2 GLN A1141 11716 9334 8100 -394 326 1331 N ATOM 2711 N THR A1142 66.491 32.656 7.893 1.00 66.80 N ANISOU 2711 N THR A1142 9321 8889 7171 573 -872 740 N ATOM 2712 CA THR A1142 65.559 31.545 8.118 1.00 65.52 C ANISOU 2712 CA THR A1142 8845 8955 7095 675 -968 566 C ATOM 2713 C THR A1142 64.364 32.004 8.987 1.00 65.38 C ANISOU 2713 C THR A1142 8689 9000 7152 850 -1199 393 C ATOM 2714 O THR A1142 64.405 31.843 10.210 1.00 63.84 O ANISOU 2714 O THR A1142 8235 8888 7134 757 -1151 352 O ATOM 2715 CB THR A1142 66.289 30.303 8.676 1.00 63.47 C ANISOU 2715 CB THR A1142 8259 8839 7018 470 -753 583 C ATOM 2716 OG1 THR A1142 66.983 30.657 9.874 1.00 62.27 O ANISOU 2716 OG1 THR A1142 7974 8667 7019 331 -676 640 O ATOM 2717 CG2 THR A1142 67.251 29.677 7.670 1.00 63.80 C ANISOU 2717 CG2 THR A1142 8391 8857 6993 342 -550 687 C ATOM 2718 N PRO A1143 63.298 32.587 8.381 1.00 65.24 N ANISOU 2718 N PRO A1143 8849 8945 6994 1118 -1455 273 N ATOM 2719 CA PRO A1143 62.161 33.068 9.189 1.00 65.45 C ANISOU 2719 CA PRO A1143 8720 9037 7111 1293 -1672 67 C ATOM 2720 C PRO A1143 61.272 31.977 9.782 1.00 64.30 C ANISOU 2720 C PRO A1143 8151 9141 7139 1294 -1675 -175 C ATOM 2721 O PRO A1143 60.901 32.086 10.950 1.00 63.52 O ANISOU 2721 O PRO A1143 7828 9113 7194 1258 -1671 -279 O ATOM 2722 CB PRO A1143 61.391 33.985 8.225 1.00 68.27 C ANISOU 2722 CB PRO A1143 9419 9268 7253 1607 -1960 2 C ATOM 2723 CG PRO A1143 62.269 34.136 7.009 1.00 69.52 C ANISOU 2723 CG PRO A1143 9985 9248 7181 1558 -1854 228 C ATOM 2724 CD PRO A1143 63.091 32.893 6.954 1.00 67.63 C ANISOU 2724 CD PRO A1143 9523 9136 7037 1295 -1574 304 C ATOM 2725 N ASN A1144 60.930 30.938 8.987 1.00 63.75 N ANISOU 2725 N ASN A1144 7986 9193 7043 1321 -1661 -277 N ATOM 2726 CA ASN A1144 60.079 29.819 9.415 1.00 63.08 C ANISOU 2726 CA ASN A1144 7520 9323 7125 1292 -1623 -527 C ATOM 2727 C ASN A1144 60.705 29.012 10.553 1.00 60.81 C ANISOU 2727 C ASN A1144 7002 9091 7012 1021 -1347 -440 C ATOM 2728 O ASN A1144 59.992 28.609 11.472 1.00 60.42 O ANISOU 2728 O ASN A1144 6689 9157 7111 982 -1305 -623 O ATOM 2729 CB ASN A1144 59.741 28.896 8.238 1.00 63.87 C ANISOU 2729 CB ASN A1144 7602 9513 7152 1357 -1649 -642 C ATOM 2730 CG ASN A1144 59.019 29.556 7.087 1.00 66.36 C ANISOU 2730 CG ASN A1144 8155 9793 7266 1667 -1955 -761 C ATOM 2731 OD1 ASN A1144 58.110 30.378 7.263 1.00 68.22 O ANISOU 2731 OD1 ASN A1144 8388 10036 7496 1900 -2214 -951 O ATOM 2732 ND2 ASN A1144 59.378 29.163 5.876 1.00 66.78 N ANISOU 2732 ND2 ASN A1144 8421 9812 7141 1696 -1944 -674 N ATOM 2733 N ARG A1145 62.034 28.789 10.491 1.00 57.08 N ANISOU 2733 N ARG A1145 6642 8532 6513 845 -1159 -177 N ATOM 2734 CA ARG A1145 62.793 28.047 11.497 1.00 55.31 C ANISOU 2734 CA ARG A1145 6253 8341 6422 630 -933 -74 C ATOM 2735 C ARG A1145 62.881 28.828 12.812 1.00 54.88 C ANISOU 2735 C ARG A1145 6159 8255 6438 597 -951 -49 C ATOM 2736 O ARG A1145 62.623 28.252 13.870 1.00 54.23 O ANISOU 2736 O ARG A1145 5886 8255 6464 517 -855 -121 O ATOM 2737 CB ARG A1145 64.194 27.684 10.969 1.00 54.71 C ANISOU 2737 CB ARG A1145 6292 8190 6306 491 -767 153 C ATOM 2738 CG ARG A1145 64.989 26.792 11.913 1.00 53.28 C ANISOU 2738 CG ARG A1145 5945 8046 6253 320 -574 237 C ATOM 2739 CD ARG A1145 66.298 26.338 11.314 1.00 53.03 C ANISOU 2739 CD ARG A1145 5975 7965 6209 208 -423 398 C ATOM 2740 NE ARG A1145 67.097 25.602 12.294 1.00 52.02 N ANISOU 2740 NE ARG A1145 5702 7864 6200 96 -291 465 N ATOM 2741 CZ ARG A1145 68.197 24.916 12.003 1.00 51.83 C ANISOU 2741 CZ ARG A1145 5650 7829 6214 10 -155 554 C ATOM 2742 NH1 ARG A1145 68.640 24.855 10.753 1.00 52.47 N ANISOU 2742 NH1 ARG A1145 5831 7878 6227 -10 -95 591 N ATOM 2743 NH2 ARG A1145 68.860 24.280 12.959 1.00 51.26 N ANISOU 2743 NH2 ARG A1145 5461 7777 6238 -40 -83 595 N ATOM 2744 N ALA A1146 63.234 30.131 12.739 1.00 53.62 N ANISOU 2744 N ALA A1146 6206 7962 6205 653 -1061 49 N ATOM 2745 CA ALA A1146 63.361 31.013 13.902 1.00 53.48 C ANISOU 2745 CA ALA A1146 6176 7899 6245 631 -1095 64 C ATOM 2746 C ALA A1146 62.040 31.197 14.650 1.00 54.07 C ANISOU 2746 C ALA A1146 6087 8072 6386 746 -1210 -177 C ATOM 2747 O ALA A1146 62.048 31.179 15.879 1.00 53.47 O ANISOU 2747 O ALA A1146 5883 8041 6392 666 -1143 -206 O ATOM 2748 CB ALA A1146 63.933 32.359 13.491 1.00 54.53 C ANISOU 2748 CB ALA A1146 6592 7841 6286 667 -1179 193 C ATOM 2749 N LYS A1147 60.910 31.323 13.913 1.00 54.70 N ANISOU 2749 N LYS A1147 6161 8195 6428 937 -1380 -374 N ATOM 2750 CA LYS A1147 59.562 31.481 14.477 1.00 55.73 C ANISOU 2750 CA LYS A1147 6092 8438 6645 1061 -1494 -672 C ATOM 2751 C LYS A1147 59.187 30.343 15.430 1.00 54.89 C ANISOU 2751 C LYS A1147 5699 8484 6673 896 -1283 -799 C ATOM 2752 O LYS A1147 58.572 30.601 16.462 1.00 55.45 O ANISOU 2752 O LYS A1147 5630 8613 6825 888 -1267 -955 O ATOM 2753 CB LYS A1147 58.509 31.629 13.368 1.00 57.69 C ANISOU 2753 CB LYS A1147 6355 8728 6836 1308 -1725 -892 C ATOM 2754 CG LYS A1147 58.337 33.061 12.882 1.00 59.62 C ANISOU 2754 CG LYS A1147 6875 8819 6959 1553 -1997 -879 C ATOM 2755 CD LYS A1147 57.352 33.154 11.720 1.00 62.05 C ANISOU 2755 CD LYS A1147 7236 9166 7175 1843 -2264 -1096 C ATOM 2756 CE LYS A1147 56.022 33.750 12.118 1.00 64.07 C ANISOU 2756 CE LYS A1147 7321 9504 7519 2089 -2508 -1448 C ATOM 2757 NZ LYS A1147 56.091 35.230 12.257 1.00 65.37 N ANISOU 2757 NZ LYS A1147 7778 9468 7591 2275 -2710 -1365 N ATOM 2758 N ARG A1148 59.580 29.099 15.096 1.00 51.62 N ANISOU 2758 N ARG A1148 5227 8114 6273 759 -1103 -730 N ATOM 2759 CA ARG A1148 59.327 27.912 15.914 1.00 51.09 C ANISOU 2759 CA ARG A1148 4963 8141 6308 588 -867 -815 C ATOM 2760 C ARG A1148 60.228 27.878 17.154 1.00 49.89 C ANISOU 2760 C ARG A1148 4864 7936 6156 442 -719 -617 C ATOM 2761 O ARG A1148 59.742 27.574 18.244 1.00 50.15 O ANISOU 2761 O ARG A1148 4791 8022 6242 361 -592 -727 O ATOM 2762 CB ARG A1148 59.510 26.633 15.084 1.00 50.81 C ANISOU 2762 CB ARG A1148 4890 8136 6280 510 -738 -797 C ATOM 2763 CG ARG A1148 58.228 26.134 14.421 1.00 52.28 C ANISOU 2763 CG ARG A1148 4886 8443 6536 582 -785 -1129 C ATOM 2764 CD ARG A1148 58.336 26.048 12.907 1.00 52.99 C ANISOU 2764 CD ARG A1148 5071 8527 6535 705 -926 -1120 C ATOM 2765 NE ARG A1148 59.397 25.138 12.468 1.00 51.75 N ANISOU 2765 NE ARG A1148 5018 8310 6335 572 -758 -879 N ATOM 2766 CZ ARG A1148 59.724 24.919 11.198 1.00 51.83 C ANISOU 2766 CZ ARG A1148 5143 8302 6248 636 -820 -823 C ATOM 2767 NH1 ARG A1148 59.069 25.534 10.220 1.00 53.19 N ANISOU 2767 NH1 ARG A1148 5375 8505 6329 846 -1062 -976 N ATOM 2768 NH2 ARG A1148 60.708 24.083 10.895 1.00 50.81 N ANISOU 2768 NH2 ARG A1148 5083 8123 6100 507 -648 -625 N ATOM 2769 N VAL A1149 61.532 28.194 16.983 1.00 46.73 N ANISOU 2769 N VAL A1149 4630 7435 5690 409 -730 -348 N ATOM 2770 CA VAL A1149 62.552 28.209 18.043 1.00 45.86 C ANISOU 2770 CA VAL A1149 4570 7280 5574 303 -640 -171 C ATOM 2771 C VAL A1149 62.274 29.312 19.085 1.00 46.26 C ANISOU 2771 C VAL A1149 4628 7322 5627 344 -732 -235 C ATOM 2772 O VAL A1149 62.340 29.038 20.286 1.00 46.16 O ANISOU 2772 O VAL A1149 4582 7339 5618 272 -633 -238 O ATOM 2773 CB VAL A1149 63.998 28.259 17.459 1.00 45.17 C ANISOU 2773 CB VAL A1149 4605 7106 5451 257 -631 65 C ATOM 2774 CG1 VAL A1149 65.054 28.358 18.559 1.00 44.69 C ANISOU 2774 CG1 VAL A1149 4562 7018 5400 181 -587 195 C ATOM 2775 CG2 VAL A1149 64.275 27.048 16.571 1.00 44.85 C ANISOU 2775 CG2 VAL A1149 4542 7084 5414 209 -513 111 C ATOM 2776 N ILE A1150 61.944 30.538 18.623 1.00 46.98 N ANISOU 2776 N ILE A1150 4791 7358 5701 472 -922 -290 N ATOM 2777 CA ILE A1150 61.626 31.691 19.479 1.00 47.59 C ANISOU 2777 CA ILE A1150 4884 7410 5788 534 -1032 -372 C ATOM 2778 C ILE A1150 60.374 31.413 20.338 1.00 48.32 C ANISOU 2778 C ILE A1150 4796 7626 5938 545 -976 -630 C ATOM 2779 O ILE A1150 60.381 31.718 21.534 1.00 48.43 O ANISOU 2779 O ILE A1150 4790 7657 5954 498 -931 -661 O ATOM 2780 CB ILE A1150 61.560 33.014 18.649 1.00 48.62 C ANISOU 2780 CB ILE A1150 5182 7415 5877 686 -1246 -365 C ATOM 2781 CG1 ILE A1150 62.971 33.413 18.151 1.00 48.24 C ANISOU 2781 CG1 ILE A1150 5328 7222 5779 603 -1225 -110 C ATOM 2782 CG2 ILE A1150 60.913 34.170 19.430 1.00 49.64 C ANISOU 2782 CG2 ILE A1150 5307 7520 6034 790 -1380 -516 C ATOM 2783 CD1 ILE A1150 63.014 34.279 16.874 1.00 49.52 C ANISOU 2783 CD1 ILE A1150 5734 7228 5854 719 -1358 -51 C ATOM 2784 N THR A1151 59.336 30.784 19.738 1.00 52.20 N ANISOU 2784 N THR A1151 5148 8208 6478 590 -959 -834 N ATOM 2785 CA THR A1151 58.087 30.406 20.417 1.00 53.32 C ANISOU 2785 CA THR A1151 5080 8475 6704 567 -860 -1133 C ATOM 2786 C THR A1151 58.352 29.315 21.472 1.00 52.84 C ANISOU 2786 C THR A1151 4998 8445 6634 358 -570 -1072 C ATOM 2787 O THR A1151 57.698 29.312 22.519 1.00 53.85 O ANISOU 2787 O THR A1151 5044 8631 6786 296 -448 -1240 O ATOM 2788 CB THR A1151 56.992 30.051 19.391 1.00 54.60 C ANISOU 2788 CB THR A1151 5081 8727 6938 671 -935 -1399 C ATOM 2789 OG1 THR A1151 56.891 31.112 18.439 1.00 55.43 O ANISOU 2789 OG1 THR A1151 5294 8769 6998 901 -1231 -1409 O ATOM 2790 CG2 THR A1151 55.622 29.831 20.030 1.00 56.26 C ANISOU 2790 CG2 THR A1151 5027 9076 7273 650 -840 -1785 C ATOM 2791 N THR A1152 59.336 28.421 21.210 1.00 53.88 N ANISOU 2791 N THR A1152 5232 8524 6715 261 -461 -831 N ATOM 2792 CA THR A1152 59.755 27.360 22.135 1.00 53.70 C ANISOU 2792 CA THR A1152 5267 8488 6649 103 -217 -726 C ATOM 2793 C THR A1152 60.421 27.996 23.371 1.00 53.58 C ANISOU 2793 C THR A1152 5373 8436 6549 96 -243 -604 C ATOM 2794 O THR A1152 60.196 27.529 24.487 1.00 54.37 O ANISOU 2794 O THR A1152 5515 8548 6595 7 -67 -640 O ATOM 2795 CB THR A1152 60.624 26.308 21.412 1.00 52.82 C ANISOU 2795 CB THR A1152 5228 8324 6518 49 -140 -527 C ATOM 2796 OG1 THR A1152 59.922 25.836 20.261 1.00 53.43 O ANISOU 2796 OG1 THR A1152 5187 8446 6668 69 -142 -676 O ATOM 2797 CG2 THR A1152 60.983 25.117 22.301 1.00 52.81 C ANISOU 2797 CG2 THR A1152 5323 8282 6461 -80 101 -430 C ATOM 2798 N PHE A1153 61.197 29.085 23.168 1.00 55.40 N ANISOU 2798 N PHE A1153 5674 8613 6762 186 -451 -480 N ATOM 2799 CA PHE A1153 61.847 29.836 24.247 1.00 55.45 C ANISOU 2799 CA PHE A1153 5771 8591 6707 191 -514 -401 C ATOM 2800 C PHE A1153 60.804 30.605 25.067 1.00 56.61 C ANISOU 2800 C PHE A1153 5852 8790 6867 225 -529 -629 C ATOM 2801 O PHE A1153 60.974 30.760 26.275 1.00 57.09 O ANISOU 2801 O PHE A1153 5977 8862 6853 190 -478 -628 O ATOM 2802 CB PHE A1153 62.882 30.831 23.687 1.00 54.87 C ANISOU 2802 CB PHE A1153 5771 8433 6644 249 -705 -253 C ATOM 2803 CG PHE A1153 64.253 30.289 23.348 1.00 54.04 C ANISOU 2803 CG PHE A1153 5729 8281 6523 198 -683 -36 C ATOM 2804 CD1 PHE A1153 65.054 29.710 24.327 1.00 53.98 C ANISOU 2804 CD1 PHE A1153 5769 8287 6454 157 -621 60 C ATOM 2805 CD2 PHE A1153 64.781 30.443 22.072 1.00 53.63 C ANISOU 2805 CD2 PHE A1153 5700 8170 6507 208 -738 58 C ATOM 2806 CE1 PHE A1153 66.336 29.243 24.020 1.00 53.54 C ANISOU 2806 CE1 PHE A1153 5737 8200 6406 137 -627 217 C ATOM 2807 CE2 PHE A1153 66.065 29.978 21.766 1.00 53.12 C ANISOU 2807 CE2 PHE A1153 5661 8073 6449 153 -702 220 C ATOM 2808 CZ PHE A1153 66.836 29.387 22.744 1.00 53.07 C ANISOU 2808 CZ PHE A1153 5656 8095 6414 125 -657 285 C ATOM 2809 N ARG A1154 59.737 31.091 24.399 1.00 59.50 N ANISOU 2809 N ARG A1154 6093 9193 7321 312 -613 -842 N ATOM 2810 CA ARG A1154 58.642 31.863 24.992 1.00 60.92 C ANISOU 2810 CA ARG A1154 6165 9433 7549 374 -650 -1115 C ATOM 2811 C ARG A1154 57.771 31.055 25.955 1.00 62.04 C ANISOU 2811 C ARG A1154 6214 9670 7688 244 -382 -1308 C ATOM 2812 O ARG A1154 57.484 31.529 27.056 1.00 63.06 O ANISOU 2812 O ARG A1154 6352 9827 7781 226 -333 -1415 O ATOM 2813 CB ARG A1154 57.758 32.476 23.891 1.00 61.78 C ANISOU 2813 CB ARG A1154 6161 9557 7756 540 -840 -1311 C ATOM 2814 CG ARG A1154 58.296 33.772 23.307 1.00 61.73 C ANISOU 2814 CG ARG A1154 6298 9426 7731 695 -1109 -1197 C ATOM 2815 CD ARG A1154 57.383 34.952 23.595 1.00 63.33 C ANISOU 2815 CD ARG A1154 6441 9631 7990 860 -1278 -1448 C ATOM 2816 NE ARG A1154 56.184 34.949 22.752 1.00 64.97 N ANISOU 2816 NE ARG A1154 6493 9911 8281 1021 -1394 -1726 N ATOM 2817 CZ ARG A1154 55.241 35.886 22.782 1.00 66.75 C ANISOU 2817 CZ ARG A1154 6637 10150 8575 1220 -1581 -1997 C ATOM 2818 NH1 ARG A1154 55.344 36.918 23.612 1.00 67.01 N ANISOU 2818 NH1 ARG A1154 6742 10116 8602 1266 -1655 -2014 N ATOM 2819 NH2 ARG A1154 54.187 35.800 21.981 1.00 68.51 N ANISOU 2819 NH2 ARG A1154 6698 10456 8877 1391 -1712 -2277 N ATOM 2820 N THR A1155 57.330 29.855 25.530 1.00 64.09 N ANISOU 2820 N THR A1155 6398 9968 7985 143 -190 -1368 N ATOM 2821 CA THR A1155 56.432 28.993 26.308 1.00 65.58 C ANISOU 2821 CA THR A1155 6511 10221 8185 -21 123 -1575 C ATOM 2822 C THR A1155 57.112 27.893 27.118 1.00 65.48 C ANISOU 2822 C THR A1155 6716 10137 8026 -182 378 -1356 C ATOM 2823 O THR A1155 56.652 27.581 28.219 1.00 66.98 O ANISOU 2823 O THR A1155 6970 10336 8143 -306 622 -1456 O ATOM 2824 CB THR A1155 55.321 28.416 25.418 1.00 66.55 C ANISOU 2824 CB THR A1155 6391 10428 8467 -42 195 -1863 C ATOM 2825 OG1 THR A1155 55.905 27.760 24.290 1.00 65.43 O ANISOU 2825 OG1 THR A1155 6290 10240 8331 -23 131 -1684 O ATOM 2826 CG2 THR A1155 54.321 29.473 24.961 1.00 67.22 C ANISOU 2826 CG2 THR A1155 6244 10607 8689 134 -26 -2189 C ATOM 2827 N GLY A1156 58.168 27.303 26.565 1.00 65.30 N ANISOU 2827 N GLY A1156 6820 10036 7955 -172 329 -1077 N ATOM 2828 CA GLY A1156 58.887 26.200 27.194 1.00 65.38 C ANISOU 2828 CA GLY A1156 7057 9958 7827 -274 523 -861 C ATOM 2829 C GLY A1156 58.230 24.866 26.901 1.00 66.37 C ANISOU 2829 C GLY A1156 7157 10061 8000 -427 814 -960 C ATOM 2830 O GLY A1156 58.406 23.904 27.654 1.00 67.39 O ANISOU 2830 O GLY A1156 7500 10100 8005 -541 1060 -863 O ATOM 2831 N THR A1157 57.450 24.815 25.801 1.00 67.84 N ANISOU 2831 N THR A1157 7101 10316 8359 -423 781 -1165 N ATOM 2832 CA THR A1157 56.718 23.633 25.326 1.00 68.96 C ANISOU 2832 CA THR A1157 7151 10454 8596 -574 1039 -1332 C ATOM 2833 C THR A1157 57.055 23.326 23.858 1.00 67.70 C ANISOU 2833 C THR A1157 6897 10299 8527 -499 888 -1274 C ATOM 2834 O THR A1157 57.545 24.204 23.144 1.00 66.26 O ANISOU 2834 O THR A1157 6679 10144 8353 -329 586 -1177 O ATOM 2835 CB THR A1157 55.200 23.817 25.515 1.00 70.91 C ANISOU 2835 CB THR A1157 7136 10819 8987 -661 1185 -1764 C ATOM 2836 OG1 THR A1157 54.778 25.034 24.897 1.00 70.32 O ANISOU 2836 OG1 THR A1157 6845 10859 9015 -465 860 -1926 O ATOM 2837 CG2 THR A1157 54.772 23.782 26.979 1.00 72.60 C ANISOU 2837 CG2 THR A1157 7469 11012 9104 -807 1464 -1851 C ATOM 2838 N TRP A1158 56.775 22.084 23.409 1.00 68.77 N ANISOU 2838 N TRP A1158 7009 10396 8725 -638 1118 -1347 N ATOM 2839 CA TRP A1158 57.010 21.636 22.031 1.00 67.96 C ANISOU 2839 CA TRP A1158 6819 10301 8702 -585 1011 -1325 C ATOM 2840 C TRP A1158 55.790 21.910 21.119 1.00 68.95 C ANISOU 2840 C TRP A1158 6626 10572 9000 -540 914 -1705 C ATOM 2841 O TRP A1158 55.751 21.411 19.990 1.00 68.75 O ANISOU 2841 O TRP A1158 6513 10569 9041 -510 852 -1757 O ATOM 2842 CB TRP A1158 57.352 20.136 21.995 1.00 68.65 C ANISOU 2842 CB TRP A1158 7051 10260 8772 -743 1293 -1224 C ATOM 2843 CG TRP A1158 58.513 19.710 22.842 1.00 67.87 C ANISOU 2843 CG TRP A1158 7276 10012 8499 -740 1354 -873 C ATOM 2844 CD1 TRP A1158 58.457 19.203 24.106 1.00 69.21 C ANISOU 2844 CD1 TRP A1158 7679 10072 8545 -855 1606 -810 C ATOM 2845 CD2 TRP A1158 59.890 19.658 22.446 1.00 65.97 C ANISOU 2845 CD2 TRP A1158 7169 9715 8182 -605 1159 -562 C ATOM 2846 NE1 TRP A1158 59.718 18.871 24.539 1.00 68.28 N ANISOU 2846 NE1 TRP A1158 7837 9836 8270 -763 1536 -478 N ATOM 2847 CE2 TRP A1158 60.618 19.142 23.542 1.00 66.30 C ANISOU 2847 CE2 TRP A1158 7499 9626 8066 -615 1265 -339 C ATOM 2848 CE3 TRP A1158 60.587 20.021 21.280 1.00 64.37 C ANISOU 2848 CE3 TRP A1158 6877 9558 8023 -475 912 -468 C ATOM 2849 CZ2 TRP A1158 62.006 18.981 23.507 1.00 65.07 C ANISOU 2849 CZ2 TRP A1158 7492 9404 7828 -485 1106 -58 C ATOM 2850 CZ3 TRP A1158 61.963 19.855 21.246 1.00 63.12 C ANISOU 2850 CZ3 TRP A1158 6867 9328 7787 -387 804 -186 C ATOM 2851 CH2 TRP A1158 62.656 19.334 22.348 1.00 63.47 C ANISOU 2851 CH2 TRP A1158 7145 9263 7708 -386 889 -1 C ATOM 2852 N ASP A1159 54.811 22.711 21.604 1.00 71.21 N ANISOU 2852 N ASP A1159 6738 10964 9355 -514 880 -1988 N ATOM 2853 CA ASP A1159 53.571 23.067 20.898 1.00 72.80 C ANISOU 2853 CA ASP A1159 6610 11322 9728 -432 753 -2412 C ATOM 2854 C ASP A1159 53.774 23.767 19.545 1.00 71.94 C ANISOU 2854 C ASP A1159 6459 11263 9612 -168 353 -2376 C ATOM 2855 O ASP A1159 52.868 23.747 18.708 1.00 73.56 O ANISOU 2855 O ASP A1159 6424 11585 9941 -81 236 -2708 O ATOM 2856 CB ASP A1159 52.627 23.877 21.807 1.00 74.62 C ANISOU 2856 CB ASP A1159 6690 11644 10018 -424 773 -2692 C ATOM 2857 CG ASP A1159 52.255 23.214 23.124 1.00 76.04 C ANISOU 2857 CG ASP A1159 6913 11783 10196 -701 1207 -2793 C ATOM 2858 OD1 ASP A1159 52.113 21.969 23.148 1.00 76.64 O ANISOU 2858 OD1 ASP A1159 7014 11796 10310 -921 1528 -2838 O ATOM 2859 OD2 ASP A1159 52.057 23.945 24.120 1.00 76.81 O ANISOU 2859 OD2 ASP A1159 7037 11901 10247 -702 1240 -2840 O ATOM 2860 N ALA A1160 54.963 24.367 19.328 1.00 67.83 N ANISOU 2860 N ALA A1160 6180 10649 8943 -44 154 -1996 N ATOM 2861 CA ALA A1160 55.336 25.051 18.087 1.00 67.18 C ANISOU 2861 CA ALA A1160 6151 10567 8808 181 -179 -1904 C ATOM 2862 C ALA A1160 55.547 24.060 16.929 1.00 67.05 C ANISOU 2862 C ALA A1160 6128 10548 8800 156 -149 -1881 C ATOM 2863 O ALA A1160 55.409 24.441 15.764 1.00 67.57 O ANISOU 2863 O ALA A1160 6182 10652 8840 339 -398 -1944 O ATOM 2864 CB ALA A1160 56.597 25.874 18.305 1.00 65.33 C ANISOU 2864 CB ALA A1160 6176 10217 8430 252 -313 -1524 C ATOM 2865 N TYR A1161 55.875 22.793 17.255 1.00 68.17 N ANISOU 2865 N TYR A1161 6305 10633 8963 -57 152 -1796 N ATOM 2866 CA TYR A1161 56.126 21.726 16.283 1.00 68.01 C ANISOU 2866 CA TYR A1161 6284 10595 8962 -110 227 -1775 C ATOM 2867 C TYR A1161 54.946 20.745 16.126 1.00 70.00 C ANISOU 2867 C TYR A1161 6289 10926 9382 -252 431 -2166 C ATOM 2868 O TYR A1161 55.136 19.620 15.653 1.00 70.32 O ANISOU 2868 O TYR A1161 6344 10918 9456 -373 604 -2152 O ATOM 2869 CB TYR A1161 57.448 20.999 16.607 1.00 66.36 C ANISOU 2869 CB TYR A1161 6314 10240 8660 -218 390 -1396 C ATOM 2870 CG TYR A1161 58.664 21.896 16.527 1.00 64.69 C ANISOU 2870 CG TYR A1161 6298 9965 8316 -92 191 -1063 C ATOM 2871 CD1 TYR A1161 59.329 22.097 15.321 1.00 64.01 C ANISOU 2871 CD1 TYR A1161 6288 9867 8166 22 19 -933 C ATOM 2872 CD2 TYR A1161 59.149 22.549 17.657 1.00 64.11 C ANISOU 2872 CD2 TYR A1161 6335 9843 8181 -99 189 -901 C ATOM 2873 CE1 TYR A1161 60.442 22.933 15.239 1.00 62.87 C ANISOU 2873 CE1 TYR A1161 6314 9654 7919 99 -118 -660 C ATOM 2874 CE2 TYR A1161 60.255 23.393 17.586 1.00 62.90 C ANISOU 2874 CE2 TYR A1161 6330 9634 7935 -6 20 -641 C ATOM 2875 CZ TYR A1161 60.905 23.575 16.376 1.00 62.33 C ANISOU 2875 CZ TYR A1161 6321 9541 7821 79 -118 -525 C ATOM 2876 OH TYR A1161 62.003 24.399 16.304 1.00 61.51 O ANISOU 2876 OH TYR A1161 6357 9370 7643 132 -237 -297 O ATOM 2877 N LYS A 263 53.723 21.190 16.491 1.00 74.29 N ANISOU 2877 N LYS A 263 6364 11204 10659 -847 -867 -228 N ATOM 2878 CA LYS A 263 52.497 20.396 16.379 1.00 73.51 C ANISOU 2878 CA LYS A 263 6349 11033 10548 -771 -775 -212 C ATOM 2879 C LYS A 263 52.092 20.231 14.915 1.00 72.97 C ANISOU 2879 C LYS A 263 6176 11027 10522 -802 -705 -166 C ATOM 2880 O LYS A 263 51.997 21.224 14.187 1.00 73.03 O ANISOU 2880 O LYS A 263 6125 11047 10576 -901 -691 -125 O ATOM 2881 CB LYS A 263 51.348 21.035 17.174 1.00 73.19 C ANISOU 2881 CB LYS A 263 6464 10831 10514 -780 -729 -200 C ATOM 2882 CG LYS A 263 51.328 20.676 18.652 1.00 73.71 C ANISOU 2882 CG LYS A 263 6685 10811 10510 -702 -759 -244 C ATOM 2883 CD LYS A 263 49.937 20.912 19.241 1.00 73.42 C ANISOU 2883 CD LYS A 263 6797 10619 10480 -673 -663 -226 C ATOM 2884 CE LYS A 263 49.932 21.015 20.748 1.00 74.05 C ANISOU 2884 CE LYS A 263 7052 10597 10487 -630 -687 -265 C ATOM 2885 NZ LYS A 263 50.171 19.704 21.411 1.00 74.17 N ANISOU 2885 NZ LYS A 263 7132 10630 10419 -520 -716 -296 N ATOM 2886 N PHE A 264 51.865 18.968 14.491 1.00 74.11 N ANISOU 2886 N PHE A 264 6303 11208 10647 -716 -667 -175 N ATOM 2887 CA PHE A 264 51.464 18.556 13.136 1.00 73.69 C ANISOU 2887 CA PHE A 264 6169 11212 10617 -724 -608 -144 C ATOM 2888 C PHE A 264 52.394 19.078 12.018 1.00 74.19 C ANISOU 2888 C PHE A 264 6083 11412 10693 -806 -622 -124 C ATOM 2889 O PHE A 264 51.924 19.468 10.945 1.00 74.00 O ANISOU 2889 O PHE A 264 6020 11403 10694 -864 -577 -77 O ATOM 2890 CB PHE A 264 49.976 18.876 12.856 1.00 72.95 C ANISOU 2890 CB PHE A 264 6149 11001 10568 -744 -538 -98 C ATOM 2891 CG PHE A 264 49.004 18.502 13.951 1.00 72.56 C ANISOU 2891 CG PHE A 264 6241 10808 10520 -675 -503 -108 C ATOM 2892 CD1 PHE A 264 48.650 17.175 14.167 1.00 72.28 C ANISOU 2892 CD1 PHE A 264 6246 10753 10464 -572 -477 -131 C ATOM 2893 CD2 PHE A 264 48.416 19.480 14.744 1.00 72.55 C ANISOU 2893 CD2 PHE A 264 6334 10686 10545 -713 -487 -93 C ATOM 2894 CE1 PHE A 264 47.744 16.831 15.174 1.00 72.04 C ANISOU 2894 CE1 PHE A 264 6347 10588 10437 -512 -431 -132 C ATOM 2895 CE2 PHE A 264 47.506 19.135 15.749 1.00 72.32 C ANISOU 2895 CE2 PHE A 264 6437 10525 10516 -647 -436 -100 C ATOM 2896 CZ PHE A 264 47.176 17.814 15.957 1.00 72.07 C ANISOU 2896 CZ PHE A 264 6442 10479 10462 -549 -406 -116 C ATOM 2897 N CYS A 265 53.714 19.073 12.280 1.00 77.00 N ANISOU 2897 N CYS A 265 6357 11865 11034 -809 -684 -157 N ATOM 2898 CA CYS A 265 54.736 19.526 11.333 1.00 77.68 C ANISOU 2898 CA CYS A 265 6292 12085 11138 -883 -689 -140 C ATOM 2899 C CYS A 265 55.420 18.358 10.618 1.00 77.91 C ANISOU 2899 C CYS A 265 6219 12243 11140 -810 -673 -172 C ATOM 2900 O CYS A 265 55.905 18.529 9.498 1.00 78.25 O ANISOU 2900 O CYS A 265 6148 12394 11189 -859 -637 -150 O ATOM 2901 CB CYS A 265 55.749 20.436 12.021 1.00 78.60 C ANISOU 2901 CB CYS A 265 6365 12217 11283 -957 -766 -149 C ATOM 2902 SG CYS A 265 55.811 22.118 11.350 1.00 78.60 S ANISOU 2902 SG CYS A 265 6309 12214 11341 -1120 -748 -79 S ATOM 2903 N LEU A 266 55.465 17.181 11.268 1.00 75.13 N ANISOU 2903 N LEU A 266 5915 11874 10757 -692 -693 -221 N ATOM 2904 CA LEU A 266 56.071 15.966 10.720 1.00 75.36 C ANISOU 2904 CA LEU A 266 5862 12008 10764 -605 -680 -259 C ATOM 2905 C LEU A 266 55.157 15.287 9.699 1.00 74.66 C ANISOU 2905 C LEU A 266 5798 11914 10656 -572 -602 -247 C ATOM 2906 O LEU A 266 53.938 15.467 9.747 1.00 73.87 O ANISOU 2906 O LEU A 266 5800 11705 10563 -586 -572 -217 O ATOM 2907 CB LEU A 266 56.431 14.983 11.847 1.00 75.48 C ANISOU 2907 CB LEU A 266 5929 11993 10757 -490 -741 -314 C ATOM 2908 CG LEU A 266 57.687 15.309 12.652 1.00 76.42 C ANISOU 2908 CG LEU A 266 5988 12157 10892 -498 -838 -342 C ATOM 2909 CD1 LEU A 266 57.580 14.779 14.061 1.00 76.39 C ANISOU 2909 CD1 LEU A 266 6109 12061 10854 -409 -907 -376 C ATOM 2910 CD2 LEU A 266 58.937 14.767 11.976 1.00 77.39 C ANISOU 2910 CD2 LEU A 266 5939 12430 11035 -471 -846 -371 C ATOM 2911 N LYS A 267 55.757 14.495 8.783 1.00 73.69 N ANISOU 2911 N LYS A 267 5581 11905 10513 -527 -570 -272 N ATOM 2912 CA LYS A 267 55.080 13.733 7.726 1.00 73.26 C ANISOU 2912 CA LYS A 267 5542 11862 10431 -489 -507 -273 C ATOM 2913 C LYS A 267 54.029 12.778 8.316 1.00 72.45 C ANISOU 2913 C LYS A 267 5565 11636 10326 -398 -509 -293 C ATOM 2914 O LYS A 267 52.924 12.675 7.779 1.00 71.83 O ANISOU 2914 O LYS A 267 5547 11494 10251 -408 -472 -270 O ATOM 2915 CB LYS A 267 56.124 12.965 6.889 1.00 74.06 C ANISOU 2915 CB LYS A 267 5524 12107 10508 -437 -481 -315 C ATOM 2916 CG LYS A 267 55.568 12.228 5.667 1.00 73.80 C ANISOU 2916 CG LYS A 267 5505 12102 10434 -401 -419 -325 C ATOM 2917 CD LYS A 267 56.662 11.552 4.827 1.00 74.70 C ANISOU 2917 CD LYS A 267 5502 12361 10519 -350 -380 -370 C ATOM 2918 CE LYS A 267 57.066 10.175 5.315 1.00 74.89 C ANISOU 2918 CE LYS A 267 5523 12387 10545 -214 -405 -442 C ATOM 2919 NZ LYS A 267 58.129 10.237 6.355 1.00 75.93 N ANISOU 2919 NZ LYS A 267 5585 12548 10717 -192 -467 -461 N ATOM 2920 N GLU A 268 54.375 12.108 9.431 1.00 71.14 N ANISOU 2920 N GLU A 268 5438 11434 10158 -314 -555 -332 N ATOM 2921 CA GLU A 268 53.506 11.172 10.146 1.00 70.60 C ANISOU 2921 CA GLU A 268 5490 11246 10089 -225 -555 -347 C ATOM 2922 C GLU A 268 52.367 11.870 10.901 1.00 69.96 C ANISOU 2922 C GLU A 268 5530 11021 10031 -269 -545 -305 C ATOM 2923 O GLU A 268 51.241 11.368 10.892 1.00 69.37 O ANISOU 2923 O GLU A 268 5536 10847 9974 -238 -507 -293 O ATOM 2924 CB GLU A 268 54.320 10.245 11.076 1.00 71.14 C ANISOU 2924 CB GLU A 268 5564 11325 10141 -119 -609 -397 C ATOM 2925 CG GLU A 268 55.296 10.950 12.010 1.00 71.79 C ANISOU 2925 CG GLU A 268 5620 11435 10223 -145 -683 -402 C ATOM 2926 CD GLU A 268 56.762 10.693 11.724 1.00 72.82 C ANISOU 2926 CD GLU A 268 5605 11705 10358 -119 -725 -440 C ATOM 2927 OE1 GLU A 268 57.240 11.098 10.639 1.00 73.14 O ANISOU 2927 OE1 GLU A 268 5525 11854 10411 -176 -686 -433 O ATOM 2928 OE2 GLU A 268 57.441 10.112 12.600 1.00 73.40 O ANISOU 2928 OE2 GLU A 268 5686 11777 10426 -42 -796 -473 O ATOM 2929 N HIS A 269 52.660 13.022 11.546 1.00 68.57 N ANISOU 2929 N HIS A 269 5362 10830 9862 -342 -577 -284 N ATOM 2930 CA HIS A 269 51.688 13.805 12.317 1.00 68.14 C ANISOU 2930 CA HIS A 269 5420 10641 9828 -385 -565 -249 C ATOM 2931 C HIS A 269 50.629 14.490 11.455 1.00 67.57 C ANISOU 2931 C HIS A 269 5352 10523 9798 -462 -509 -198 C ATOM 2932 O HIS A 269 49.510 14.700 11.930 1.00 67.10 O ANISOU 2932 O HIS A 269 5390 10335 9770 -464 -476 -172 O ATOM 2933 CB HIS A 269 52.388 14.809 13.249 1.00 68.70 C ANISOU 2933 CB HIS A 269 5503 10709 9891 -435 -625 -251 C ATOM 2934 CG HIS A 269 53.109 14.179 14.403 1.00 69.22 C ANISOU 2934 CG HIS A 269 5613 10771 9917 -352 -691 -296 C ATOM 2935 ND1 HIS A 269 54.200 14.794 14.990 1.00 69.92 N ANISOU 2935 ND1 HIS A 269 5663 10908 9995 -384 -774 -315 N ATOM 2936 CD2 HIS A 269 52.870 13.012 15.048 1.00 69.24 C ANISOU 2936 CD2 HIS A 269 5696 10722 9890 -241 -691 -320 C ATOM 2937 CE1 HIS A 269 54.586 13.989 15.967 1.00 70.34 C ANISOU 2937 CE1 HIS A 269 5778 10940 10008 -289 -828 -351 C ATOM 2938 NE2 HIS A 269 53.818 12.903 16.037 1.00 69.93 N ANISOU 2938 NE2 HIS A 269 5801 10828 9941 -201 -777 -352 N ATOM 2939 N LYS A 270 50.973 14.833 10.195 1.00 64.99 N ANISOU 2939 N LYS A 270 4922 10299 9472 -522 -498 -180 N ATOM 2940 CA LYS A 270 50.048 15.455 9.241 1.00 64.59 C ANISOU 2940 CA LYS A 270 4871 10217 9453 -594 -459 -128 C ATOM 2941 C LYS A 270 48.998 14.436 8.790 1.00 64.06 C ANISOU 2941 C LYS A 270 4849 10090 9401 -531 -425 -133 C ATOM 2942 O LYS A 270 47.841 14.804 8.581 1.00 63.60 O ANISOU 2942 O LYS A 270 4837 9936 9392 -564 -400 -93 O ATOM 2943 CB LYS A 270 50.798 16.031 8.029 1.00 65.07 C ANISOU 2943 CB LYS A 270 4819 10410 9495 -671 -456 -107 C ATOM 2944 CG LYS A 270 51.520 17.341 8.318 1.00 65.59 C ANISOU 2944 CG LYS A 270 4841 10506 9574 -767 -484 -81 C ATOM 2945 CD LYS A 270 52.224 17.882 7.077 1.00 66.08 C ANISOU 2945 CD LYS A 270 4794 10693 9621 -846 -465 -48 C ATOM 2946 CE LYS A 270 53.259 18.939 7.396 1.00 66.92 C ANISOU 2946 CE LYS A 270 4829 10852 9745 -929 -497 -35 C ATOM 2947 NZ LYS A 270 52.646 20.229 7.816 1.00 66.93 N ANISOU 2947 NZ LYS A 270 4889 10746 9794 -1017 -512 12 N ATOM 2948 N ALA A 271 49.406 13.153 8.668 1.00 63.02 N ANISOU 2948 N ALA A 271 4699 10009 9236 -439 -428 -183 N ATOM 2949 CA ALA A 271 48.546 12.028 8.287 1.00 62.68 C ANISOU 2949 CA ALA A 271 4696 9911 9208 -371 -405 -199 C ATOM 2950 C ALA A 271 47.534 11.715 9.395 1.00 62.21 C ANISOU 2950 C ALA A 271 4745 9694 9197 -327 -387 -191 C ATOM 2951 O ALA A 271 46.393 11.363 9.092 1.00 61.84 O ANISOU 2951 O ALA A 271 4737 9557 9202 -318 -361 -173 O ATOM 2952 CB ALA A 271 49.393 10.801 7.986 1.00 63.10 C ANISOU 2952 CB ALA A 271 4703 10057 9215 -283 -416 -260 C ATOM 2953 N LEU A 272 47.953 11.859 10.674 1.00 60.48 N ANISOU 2953 N LEU A 272 4577 9441 8962 -301 -401 -201 N ATOM 2954 CA LEU A 272 47.105 11.642 11.852 1.00 60.22 C ANISOU 2954 CA LEU A 272 4660 9262 8959 -258 -373 -190 C ATOM 2955 C LEU A 272 46.075 12.764 11.967 1.00 59.90 C ANISOU 2955 C LEU A 272 4661 9120 8979 -335 -336 -138 C ATOM 2956 O LEU A 272 44.950 12.518 12.406 1.00 59.63 O ANISOU 2956 O LEU A 272 4700 8957 9000 -311 -286 -117 O ATOM 2957 CB LEU A 272 47.940 11.572 13.144 1.00 60.66 C ANISOU 2957 CB LEU A 272 4768 9320 8960 -212 -408 -217 C ATOM 2958 CG LEU A 272 48.940 10.423 13.285 1.00 61.11 C ANISOU 2958 CG LEU A 272 4797 9454 8968 -120 -450 -267 C ATOM 2959 CD1 LEU A 272 49.956 10.735 14.359 1.00 61.73 C ANISOU 2959 CD1 LEU A 272 4898 9563 8994 -104 -511 -288 C ATOM 2960 CD2 LEU A 272 48.243 9.101 13.589 1.00 60.97 C ANISOU 2960 CD2 LEU A 272 4855 9344 8967 -25 -417 -276 C ATOM 2961 N LYS A 273 46.470 13.996 11.573 1.00 59.37 N ANISOU 2961 N LYS A 273 4541 9108 8908 -427 -357 -115 N ATOM 2962 CA LYS A 273 45.616 15.184 11.571 1.00 59.16 C ANISOU 2962 CA LYS A 273 4541 8995 8942 -505 -331 -65 C ATOM 2963 C LYS A 273 44.527 15.025 10.507 1.00 58.80 C ANISOU 2963 C LYS A 273 4469 8909 8964 -525 -305 -31 C ATOM 2964 O LYS A 273 43.380 15.389 10.763 1.00 58.54 O ANISOU 2964 O LYS A 273 4483 8751 9009 -539 -266 4 O ATOM 2965 CB LYS A 273 46.447 16.451 11.306 1.00 59.50 C ANISOU 2965 CB LYS A 273 4526 9116 8965 -599 -369 -49 C ATOM 2966 CG LYS A 273 45.719 17.748 11.649 1.00 59.41 C ANISOU 2966 CG LYS A 273 4561 9000 9012 -671 -348 -5 C ATOM 2967 CD LYS A 273 46.537 18.969 11.266 1.00 59.84 C ANISOU 2967 CD LYS A 273 4552 9130 9055 -770 -389 15 C ATOM 2968 CE LYS A 273 45.857 20.254 11.668 1.00 59.85 C ANISOU 2968 CE LYS A 273 4606 9019 9116 -836 -373 52 C ATOM 2969 NZ LYS A 273 46.697 21.439 11.356 1.00 60.38 N ANISOU 2969 NZ LYS A 273 4615 9151 9176 -934 -416 71 N ATOM 2970 N THR A 274 44.890 14.461 9.330 1.00 58.10 N ANISOU 2970 N THR A 274 4305 8925 8845 -521 -329 -44 N ATOM 2971 CA THR A 274 43.987 14.208 8.201 1.00 57.90 C ANISOU 2971 CA THR A 274 4256 8878 8866 -536 -326 -20 C ATOM 2972 C THR A 274 42.875 13.237 8.616 1.00 57.63 C ANISOU 2972 C THR A 274 4279 8716 8902 -468 -294 -27 C ATOM 2973 O THR A 274 41.704 13.531 8.376 1.00 57.45 O ANISOU 2973 O THR A 274 4268 8591 8969 -496 -277 13 O ATOM 2974 CB THR A 274 44.775 13.739 6.960 1.00 58.20 C ANISOU 2974 CB THR A 274 4219 9062 8833 -536 -356 -45 C ATOM 2975 OG1 THR A 274 45.892 14.606 6.749 1.00 58.58 O ANISOU 2975 OG1 THR A 274 4210 9224 8824 -597 -373 -37 O ATOM 2976 CG2 THR A 274 43.918 13.700 5.696 1.00 58.20 C ANISOU 2976 CG2 THR A 274 4202 9049 8863 -566 -369 -18 C ATOM 2977 N LEU A 275 43.242 12.114 9.277 1.00 56.15 N ANISOU 2977 N LEU A 275 4125 8527 8682 -381 -285 -73 N ATOM 2978 CA LEU A 275 42.309 11.096 9.778 1.00 56.01 C ANISOU 2978 CA LEU A 275 4165 8388 8729 -312 -249 -78 C ATOM 2979 C LEU A 275 41.437 11.636 10.917 1.00 55.89 C ANISOU 2979 C LEU A 275 4226 8228 8782 -319 -189 -41 C ATOM 2980 O LEU A 275 40.308 11.173 11.096 1.00 55.81 O ANISOU 2980 O LEU A 275 4246 8095 8865 -295 -145 -22 O ATOM 2981 CB LEU A 275 43.062 9.835 10.237 1.00 56.20 C ANISOU 2981 CB LEU A 275 4210 8451 8692 -218 -257 -132 C ATOM 2982 CG LEU A 275 43.647 8.945 9.140 1.00 56.40 C ANISOU 2982 CG LEU A 275 4173 8585 8671 -185 -298 -178 C ATOM 2983 CD1 LEU A 275 44.882 8.221 9.631 1.00 56.73 C ANISOU 2983 CD1 LEU A 275 4213 8709 8633 -111 -319 -229 C ATOM 2984 CD2 LEU A 275 42.618 7.948 8.623 1.00 56.34 C ANISOU 2984 CD2 LEU A 275 4178 8493 8736 -151 -292 -184 C ATOM 2985 N GLY A 276 41.974 12.605 11.661 1.00 54.86 N ANISOU 2985 N GLY A 276 4124 8110 8610 -350 -186 -34 N ATOM 2986 CA GLY A 276 41.291 13.277 12.761 1.00 54.89 C ANISOU 2986 CA GLY A 276 4209 7987 8660 -359 -127 -6 C ATOM 2987 C GLY A 276 40.146 14.149 12.287 1.00 54.73 C ANISOU 2987 C GLY A 276 4165 7880 8750 -423 -98 46 C ATOM 2988 O GLY A 276 39.126 14.255 12.974 1.00 54.76 O ANISOU 2988 O GLY A 276 4224 7747 8836 -408 -27 71 O ATOM 2989 N ILE A 277 40.306 14.774 11.098 1.00 54.26 N ANISOU 2989 N ILE A 277 4023 7899 8694 -492 -152 64 N ATOM 2990 CA ILE A 277 39.284 15.623 10.477 1.00 54.21 C ANISOU 2990 CA ILE A 277 3985 7820 8792 -555 -146 117 C ATOM 2991 C ILE A 277 38.117 14.753 9.979 1.00 54.12 C ANISOU 2991 C ILE A 277 3954 7725 8884 -524 -132 130 C ATOM 2992 O ILE A 277 36.968 15.150 10.155 1.00 54.14 O ANISOU 2992 O ILE A 277 3962 7601 9008 -539 -91 170 O ATOM 2993 CB ILE A 277 39.861 16.597 9.398 1.00 54.30 C ANISOU 2993 CB ILE A 277 3928 7938 8765 -640 -210 140 C ATOM 2994 CG1 ILE A 277 40.974 17.490 9.997 1.00 54.51 C ANISOU 2994 CG1 ILE A 277 3970 8030 8712 -677 -222 129 C ATOM 2995 CG2 ILE A 277 38.756 17.479 8.784 1.00 54.33 C ANISOU 2995 CG2 ILE A 277 3906 7856 8881 -700 -213 202 C ATOM 2996 CD1 ILE A 277 42.023 17.991 9.004 1.00 54.71 C ANISOU 2996 CD1 ILE A 277 3921 8203 8663 -741 -281 134 C ATOM 2997 N ILE A 278 38.408 13.546 9.425 1.00 57.29 N ANISOU 2997 N ILE A 278 4333 8188 9246 -478 -164 94 N ATOM 2998 CA ILE A 278 37.397 12.583 8.944 1.00 57.29 C ANISOU 2998 CA ILE A 278 4315 8111 9342 -446 -165 96 C ATOM 2999 C ILE A 278 36.443 12.210 10.095 1.00 57.34 C ANISOU 2999 C ILE A 278 4378 7959 9450 -401 -76 112 C ATOM 3000 O ILE A 278 35.227 12.162 9.896 1.00 57.45 O ANISOU 3000 O ILE A 278 4368 7857 9603 -411 -54 145 O ATOM 3001 CB ILE A 278 38.027 11.307 8.286 1.00 57.36 C ANISOU 3001 CB ILE A 278 4305 8213 9276 -396 -212 42 C ATOM 3002 CG1 ILE A 278 39.284 11.596 7.414 1.00 57.47 C ANISOU 3002 CG1 ILE A 278 4276 8402 9158 -424 -274 16 C ATOM 3003 CG2 ILE A 278 36.983 10.465 7.537 1.00 57.49 C ANISOU 3003 CG2 ILE A 278 4295 8155 9394 -382 -238 43 C ATOM 3004 CD1 ILE A 278 39.098 12.430 6.105 1.00 57.57 C ANISOU 3004 CD1 ILE A 278 4234 8469 9171 -504 -329 50 C ATOM 3005 N MET A 279 37.009 11.978 11.298 1.00 58.56 N ANISOU 3005 N MET A 279 4607 8107 9536 -352 -24 90 N ATOM 3006 CA MET A 279 36.280 11.647 12.526 1.00 58.73 C ANISOU 3006 CA MET A 279 4705 7989 9621 -304 76 105 C ATOM 3007 C MET A 279 35.516 12.870 13.048 1.00 58.84 C ANISOU 3007 C MET A 279 4738 7902 9716 -347 139 150 C ATOM 3008 O MET A 279 34.402 12.725 13.555 1.00 59.07 O ANISOU 3008 O MET A 279 4787 7791 9866 -329 225 180 O ATOM 3009 CB MET A 279 37.242 11.116 13.602 1.00 58.86 C ANISOU 3009 CB MET A 279 4808 8043 9513 -241 95 69 C ATOM 3010 CG MET A 279 37.867 9.787 13.246 1.00 58.88 C ANISOU 3010 CG MET A 279 4798 8117 9457 -183 47 27 C ATOM 3011 SD MET A 279 39.230 9.340 14.338 1.00 59.11 S ANISOU 3011 SD MET A 279 4911 8218 9330 -114 36 -15 S ATOM 3012 CE MET A 279 39.885 7.942 13.459 1.00 59.04 C ANISOU 3012 CE MET A 279 4847 8304 9281 -60 -35 -65 C ATOM 3013 N GLY A 280 36.124 14.049 12.909 1.00 58.01 N ANISOU 3013 N GLY A 280 4624 7865 9552 -403 101 153 N ATOM 3014 CA GLY A 280 35.551 15.324 13.325 1.00 58.17 C ANISOU 3014 CA GLY A 280 4663 7800 9639 -447 149 188 C ATOM 3015 C GLY A 280 34.396 15.778 12.456 1.00 58.18 C ANISOU 3015 C GLY A 280 4584 7727 9795 -492 140 237 C ATOM 3016 O GLY A 280 33.423 16.337 12.970 1.00 58.45 O ANISOU 3016 O GLY A 280 4633 7630 9945 -496 217 270 O ATOM 3017 N THR A 281 34.496 15.540 11.129 1.00 59.58 N ANISOU 3017 N THR A 281 4679 7985 9974 -524 46 240 N ATOM 3018 CA THR A 281 33.470 15.894 10.141 1.00 59.68 C ANISOU 3018 CA THR A 281 4614 7939 10122 -567 8 285 C ATOM 3019 C THR A 281 32.221 15.034 10.347 1.00 59.92 C ANISOU 3019 C THR A 281 4628 7833 10306 -525 63 299 C ATOM 3020 O THR A 281 31.117 15.578 10.359 1.00 60.19 O ANISOU 3020 O THR A 281 4627 7747 10496 -543 97 343 O ATOM 3021 CB THR A 281 34.027 15.828 8.701 1.00 59.57 C ANISOU 3021 CB THR A 281 4539 8057 10038 -608 -110 280 C ATOM 3022 OG1 THR A 281 35.286 16.502 8.647 1.00 59.50 O ANISOU 3022 OG1 THR A 281 4544 8176 9887 -643 -142 265 O ATOM 3023 CG2 THR A 281 33.087 16.452 7.674 1.00 59.78 C ANISOU 3023 CG2 THR A 281 4499 8032 10183 -661 -169 332 C ATOM 3024 N PHE A 282 32.399 13.705 10.537 1.00 61.99 N ANISOU 3024 N PHE A 282 4911 8107 10536 -467 74 263 N ATOM 3025 CA PHE A 282 31.306 12.752 10.769 1.00 62.29 C ANISOU 3025 CA PHE A 282 4933 8016 10718 -427 128 275 C ATOM 3026 C PHE A 282 30.538 13.071 12.054 1.00 62.59 C ANISOU 3026 C PHE A 282 5020 7909 10852 -402 270 305 C ATOM 3027 O PHE A 282 29.321 12.892 12.090 1.00 62.98 O ANISOU 3027 O PHE A 282 5023 7826 11081 -399 321 340 O ATOM 3028 CB PHE A 282 31.826 11.302 10.798 1.00 62.24 C ANISOU 3028 CB PHE A 282 4954 8056 10639 -369 114 228 C ATOM 3029 CG PHE A 282 30.748 10.253 10.642 1.00 62.62 C ANISOU 3029 CG PHE A 282 4964 7986 10842 -344 132 239 C ATOM 3030 CD1 PHE A 282 30.345 9.828 9.381 1.00 62.74 C ANISOU 3030 CD1 PHE A 282 4903 8015 10921 -369 26 232 C ATOM 3031 CD2 PHE A 282 30.141 9.681 11.755 1.00 62.96 C ANISOU 3031 CD2 PHE A 282 5053 7902 10968 -298 255 256 C ATOM 3032 CE1 PHE A 282 29.339 8.869 9.236 1.00 63.20 C ANISOU 3032 CE1 PHE A 282 4921 7956 11136 -351 32 239 C ATOM 3033 CE2 PHE A 282 29.135 8.721 11.607 1.00 63.40 C ANISOU 3033 CE2 PHE A 282 5064 7841 11184 -281 275 270 C ATOM 3034 CZ PHE A 282 28.747 8.315 10.350 1.00 63.51 C ANISOU 3034 CZ PHE A 282 4993 7867 11271 -310 158 259 C ATOM 3035 N THR A 283 31.248 13.547 13.097 1.00 64.23 N ANISOU 3035 N THR A 283 5321 8141 10943 -384 332 290 N ATOM 3036 CA THR A 283 30.660 13.919 14.384 1.00 64.63 C ANISOU 3036 CA THR A 283 5444 8065 11048 -355 474 311 C ATOM 3037 C THR A 283 29.804 15.185 14.229 1.00 64.86 C ANISOU 3037 C THR A 283 5425 8008 11211 -402 500 354 C ATOM 3038 O THR A 283 28.612 15.137 14.515 1.00 65.34 O ANISOU 3038 O THR A 283 5455 7928 11443 -389 590 390 O ATOM 3039 CB THR A 283 31.747 14.020 15.474 1.00 64.58 C ANISOU 3039 CB THR A 283 5562 8116 10859 -321 508 275 C ATOM 3040 OG1 THR A 283 32.515 12.815 15.486 1.00 64.44 O ANISOU 3040 OG1 THR A 283 5573 8177 10734 -275 469 239 O ATOM 3041 CG2 THR A 283 31.167 14.266 16.866 1.00 65.11 C ANISOU 3041 CG2 THR A 283 5730 8052 10956 -282 662 291 C ATOM 3042 N LEU A 284 30.395 16.288 13.721 1.00 67.44 N ANISOU 3042 N LEU A 284 5736 8415 11473 -458 421 353 N ATOM 3043 CA LEU A 284 29.710 17.570 13.519 1.00 67.72 C ANISOU 3043 CA LEU A 284 5729 8376 11625 -503 431 393 C ATOM 3044 C LEU A 284 28.565 17.567 12.486 1.00 67.89 C ANISOU 3044 C LEU A 284 5629 8328 11838 -532 381 439 C ATOM 3045 O LEU A 284 27.779 18.517 12.455 1.00 68.11 O ANISOU 3045 O LEU A 284 5618 8262 11999 -556 407 478 O ATOM 3046 CB LEU A 284 30.716 18.700 13.246 1.00 67.61 C ANISOU 3046 CB LEU A 284 5737 8465 11487 -557 356 383 C ATOM 3047 CG LEU A 284 31.194 19.467 14.480 1.00 67.88 C ANISOU 3047 CG LEU A 284 5883 8473 11435 -544 435 359 C ATOM 3048 CD1 LEU A 284 32.435 18.825 15.090 1.00 67.63 C ANISOU 3048 CD1 LEU A 284 5936 8550 11210 -512 418 305 C ATOM 3049 CD2 LEU A 284 31.482 20.914 14.137 1.00 68.16 C ANISOU 3049 CD2 LEU A 284 5908 8522 11468 -609 386 375 C ATOM 3050 N CYS A 285 28.458 16.502 11.665 1.00 71.41 N ANISOU 3050 N CYS A 285 6016 8812 12304 -526 307 432 N ATOM 3051 CA CYS A 285 27.396 16.358 10.664 1.00 71.71 C ANISOU 3051 CA CYS A 285 5943 8785 12518 -551 240 469 C ATOM 3052 C CYS A 285 26.269 15.434 11.130 1.00 72.19 C ANISOU 3052 C CYS A 285 5969 8705 12754 -508 329 484 C ATOM 3053 O CYS A 285 25.118 15.646 10.743 1.00 72.68 O ANISOU 3053 O CYS A 285 5939 8658 13018 -524 321 526 O ATOM 3054 CB CYS A 285 27.959 15.921 9.315 1.00 71.39 C ANISOU 3054 CB CYS A 285 5861 8875 12389 -582 82 452 C ATOM 3055 SG CYS A 285 28.903 17.204 8.454 1.00 71.08 S ANISOU 3055 SG CYS A 285 5824 8971 12213 -652 -27 463 S ATOM 3056 N TRP A 286 26.595 14.412 11.950 1.00 74.01 N ANISOU 3056 N TRP A 286 6270 8935 12916 -454 410 453 N ATOM 3057 CA TRP A 286 25.611 13.456 12.461 1.00 74.53 C ANISOU 3057 CA TRP A 286 6312 8867 13139 -414 508 470 C ATOM 3058 C TRP A 286 25.104 13.735 13.874 1.00 74.99 C ANISOU 3058 C TRP A 286 6434 8802 13257 -374 698 491 C ATOM 3059 O TRP A 286 23.930 13.470 14.138 1.00 75.69 O ANISOU 3059 O TRP A 286 6463 8747 13549 -362 789 528 O ATOM 3060 CB TRP A 286 26.074 12.003 12.291 1.00 74.33 C ANISOU 3060 CB TRP A 286 6308 8895 13038 -381 468 432 C ATOM 3061 CG TRP A 286 25.871 11.476 10.902 1.00 74.31 C ANISOU 3061 CG TRP A 286 6213 8931 13090 -413 313 422 C ATOM 3062 CD1 TRP A 286 26.832 11.260 9.959 1.00 73.83 C ANISOU 3062 CD1 TRP A 286 6158 9020 12874 -429 176 381 C ATOM 3063 CD2 TRP A 286 24.619 11.145 10.283 1.00 74.91 C ANISOU 3063 CD2 TRP A 286 6178 8891 13394 -432 278 454 C ATOM 3064 NE1 TRP A 286 26.261 10.793 8.798 1.00 74.10 N ANISOU 3064 NE1 TRP A 286 6107 9039 13008 -455 57 382 N ATOM 3065 CE2 TRP A 286 24.903 10.705 8.972 1.00 74.77 C ANISOU 3065 CE2 TRP A 286 6117 8960 13332 -459 108 425 C ATOM 3066 CE3 TRP A 286 23.282 11.165 10.716 1.00 75.68 C ANISOU 3066 CE3 TRP A 286 6205 8816 13734 -429 374 503 C ATOM 3067 CZ2 TRP A 286 23.897 10.321 8.077 1.00 75.36 C ANISOU 3067 CZ2 TRP A 286 6088 8955 13590 -484 14 442 C ATOM 3068 CZ3 TRP A 286 22.289 10.761 9.837 1.00 76.26 C ANISOU 3068 CZ3 TRP A 286 6159 8809 14007 -455 285 522 C ATOM 3069 CH2 TRP A 286 22.599 10.340 8.537 1.00 76.09 C ANISOU 3069 CH2 TRP A 286 6105 8876 13930 -483 99 490 C ATOM 3070 N LEU A 287 25.964 14.274 14.773 1.00 74.16 N ANISOU 3070 N LEU A 287 6449 8748 12980 -355 760 467 N ATOM 3071 CA LEU A 287 25.580 14.613 16.152 1.00 74.71 C ANISOU 3071 CA LEU A 287 6607 8709 13070 -315 941 480 C ATOM 3072 C LEU A 287 24.404 15.613 16.230 1.00 75.33 C ANISOU 3072 C LEU A 287 6615 8652 13354 -332 1020 526 C ATOM 3073 O LEU A 287 23.483 15.319 16.993 1.00 76.08 O ANISOU 3073 O LEU A 287 6711 8610 13585 -296 1175 554 O ATOM 3074 CB LEU A 287 26.775 15.069 17.014 1.00 74.44 C ANISOU 3074 CB LEU A 287 6721 8760 12803 -296 963 440 C ATOM 3075 CG LEU A 287 26.557 15.121 18.530 1.00 75.09 C ANISOU 3075 CG LEU A 287 6934 8744 12853 -240 1146 442 C ATOM 3076 CD1 LEU A 287 26.871 13.781 19.181 1.00 75.38 C ANISOU 3076 CD1 LEU A 287 7055 8783 12803 -183 1201 431 C ATOM 3077 CD2 LEU A 287 27.404 16.206 19.159 1.00 74.92 C ANISOU 3077 CD2 LEU A 287 7025 8775 12666 -246 1145 408 C ATOM 3078 N PRO A 288 24.337 16.728 15.436 1.00 77.39 N ANISOU 3078 N PRO A 288 6807 8938 13660 -384 922 539 N ATOM 3079 CA PRO A 288 23.164 17.624 15.532 1.00 78.12 C ANISOU 3079 CA PRO A 288 6826 8889 13968 -392 998 583 C ATOM 3080 C PRO A 288 21.821 16.954 15.222 1.00 78.82 C ANISOU 3080 C PRO A 288 6784 8848 14316 -384 1038 627 C ATOM 3081 O PRO A 288 20.784 17.458 15.651 1.00 79.65 O ANISOU 3081 O PRO A 288 6840 8812 14611 -369 1155 663 O ATOM 3082 CB PRO A 288 23.485 18.744 14.536 1.00 77.76 C ANISOU 3082 CB PRO A 288 6727 8913 13905 -453 847 591 C ATOM 3083 CG PRO A 288 24.958 18.707 14.378 1.00 76.97 C ANISOU 3083 CG PRO A 288 6715 8983 13547 -470 751 545 C ATOM 3084 CD PRO A 288 25.312 17.258 14.459 1.00 76.68 C ANISOU 3084 CD PRO A 288 6705 8997 13433 -436 749 518 C ATOM 3085 N PHE A 289 21.844 15.813 14.499 1.00 78.81 N ANISOU 3085 N PHE A 289 6727 8888 14329 -391 942 621 N ATOM 3086 CA PHE A 289 20.656 15.024 14.173 1.00 79.51 C ANISOU 3086 CA PHE A 289 6692 8859 14659 -388 960 657 C ATOM 3087 C PHE A 289 20.323 14.071 15.330 1.00 80.01 C ANISOU 3087 C PHE A 289 6815 8832 14753 -333 1146 662 C ATOM 3088 O PHE A 289 19.170 14.022 15.761 1.00 80.96 O ANISOU 3088 O PHE A 289 6865 8801 15095 -317 1278 704 O ATOM 3089 CB PHE A 289 20.845 14.253 12.846 1.00 79.17 C ANISOU 3089 CB PHE A 289 6572 8897 14611 -423 761 643 C ATOM 3090 CG PHE A 289 19.856 13.133 12.602 1.00 79.88 C ANISOU 3090 CG PHE A 289 6561 8881 14909 -418 767 663 C ATOM 3091 CD1 PHE A 289 18.539 13.408 12.251 1.00 80.82 C ANISOU 3091 CD1 PHE A 289 6534 8863 15311 -437 768 712 C ATOM 3092 CD2 PHE A 289 20.244 11.803 12.720 1.00 79.69 C ANISOU 3092 CD2 PHE A 289 6582 8889 14808 -394 766 634 C ATOM 3093 CE1 PHE A 289 17.624 12.373 12.035 1.00 81.59 C ANISOU 3093 CE1 PHE A 289 6529 8856 15615 -437 767 731 C ATOM 3094 CE2 PHE A 289 19.328 10.768 12.502 1.00 80.44 C ANISOU 3094 CE2 PHE A 289 6584 8876 15104 -394 769 652 C ATOM 3095 CZ PHE A 289 18.026 11.061 12.160 1.00 81.39 C ANISOU 3095 CZ PHE A 289 6555 8861 15508 -418 768 700 C ATOM 3096 N PHE A 290 21.332 13.314 15.816 1.00 78.33 N ANISOU 3096 N PHE A 290 6728 8711 14323 -304 1156 622 N ATOM 3097 CA PHE A 290 21.184 12.350 16.908 1.00 78.81 C ANISOU 3097 CA PHE A 290 6871 8701 14372 -251 1320 629 C ATOM 3098 C PHE A 290 20.881 12.991 18.262 1.00 79.46 C ANISOU 3098 C PHE A 290 7051 8689 14450 -210 1533 647 C ATOM 3099 O PHE A 290 20.174 12.381 19.065 1.00 80.34 O ANISOU 3099 O PHE A 290 7180 8682 14663 -173 1703 678 O ATOM 3100 CB PHE A 290 22.393 11.407 16.994 1.00 78.14 C ANISOU 3100 CB PHE A 290 6896 8742 14053 -228 1252 583 C ATOM 3101 CG PHE A 290 22.380 10.289 15.978 1.00 77.88 C ANISOU 3101 CG PHE A 290 6778 8743 14069 -245 1114 571 C ATOM 3102 CD1 PHE A 290 23.075 10.406 14.781 1.00 77.11 C ANISOU 3102 CD1 PHE A 290 6641 8782 13876 -283 914 534 C ATOM 3103 CD2 PHE A 290 21.686 9.109 16.226 1.00 78.52 C ANISOU 3103 CD2 PHE A 290 6828 8717 14289 -224 1187 594 C ATOM 3104 CE1 PHE A 290 23.068 9.369 13.844 1.00 76.98 C ANISOU 3104 CE1 PHE A 290 6560 8794 13895 -295 788 514 C ATOM 3105 CE2 PHE A 290 21.677 8.073 15.287 1.00 78.37 C ANISOU 3105 CE2 PHE A 290 6738 8722 14317 -241 1052 576 C ATOM 3106 CZ PHE A 290 22.369 8.210 14.103 1.00 77.60 C ANISOU 3106 CZ PHE A 290 6609 8761 14115 -273 852 532 C ATOM 3107 N ILE A 291 21.395 14.215 18.512 1.00 80.35 N ANISOU 3107 N ILE A 291 7231 8850 14448 -216 1529 626 N ATOM 3108 CA ILE A 291 21.141 14.944 19.760 1.00 81.04 C ANISOU 3108 CA ILE A 291 7424 8850 14518 -177 1722 632 C ATOM 3109 C ILE A 291 19.693 15.474 19.807 1.00 82.04 C ANISOU 3109 C ILE A 291 7427 8811 14933 -177 1844 683 C ATOM 3110 O ILE A 291 19.120 15.601 20.889 1.00 82.99 O ANISOU 3110 O ILE A 291 7610 8816 15107 -132 2054 702 O ATOM 3111 CB ILE A 291 22.235 16.014 20.069 1.00 80.47 C ANISOU 3111 CB ILE A 291 7476 8879 14220 -183 1671 586 C ATOM 3112 CG1 ILE A 291 22.370 16.271 21.583 1.00 81.02 C ANISOU 3112 CG1 ILE A 291 7724 8888 14171 -126 1862 572 C ATOM 3113 CG2 ILE A 291 22.057 17.317 19.267 1.00 80.43 C ANISOU 3113 CG2 ILE A 291 7376 8883 14301 -235 1569 591 C ATOM 3114 CD1 ILE A 291 23.804 16.324 22.087 1.00 80.29 C ANISOU 3114 CD1 ILE A 291 7801 8925 13781 -114 1795 516 C ATOM 3115 N VAL A 292 19.108 15.745 18.622 1.00 84.18 N ANISOU 3115 N VAL A 292 7524 9070 15390 -226 1710 707 N ATOM 3116 CA VAL A 292 17.737 16.225 18.434 1.00 85.13 C ANISOU 3116 CA VAL A 292 7492 9041 15812 -232 1780 757 C ATOM 3117 C VAL A 292 16.749 15.039 18.479 1.00 85.98 C ANISOU 3117 C VAL A 292 7497 9036 16135 -220 1863 798 C ATOM 3118 O VAL A 292 15.639 15.187 18.999 1.00 87.13 O ANISOU 3118 O VAL A 292 7572 9030 16504 -197 2033 841 O ATOM 3119 CB VAL A 292 17.641 17.107 17.151 1.00 84.69 C ANISOU 3119 CB VAL A 292 7311 9029 15838 -289 1578 764 C ATOM 3120 CG1 VAL A 292 16.242 17.113 16.536 1.00 85.30 C ANISOU 3120 CG1 VAL A 292 7187 8973 16250 -305 1565 818 C ATOM 3121 CG2 VAL A 292 18.108 18.530 17.440 1.00 84.80 C ANISOU 3121 CG2 VAL A 292 7404 9068 15748 -291 1587 745 C ATOM 3122 N ASN A 293 17.183 13.858 17.985 1.00 88.11 N ANISOU 3122 N ASN A 293 7763 9377 16337 -234 1753 784 N ATOM 3123 CA ASN A 293 16.404 12.615 17.958 1.00 88.86 C ANISOU 3123 CA ASN A 293 7771 9377 16614 -230 1804 817 C ATOM 3124 C ASN A 293 16.016 12.129 19.365 1.00 89.77 C ANISOU 3124 C ASN A 293 7979 9382 16748 -175 2070 845 C ATOM 3125 O ASN A 293 14.942 11.549 19.529 1.00 90.89 O ANISOU 3125 O ASN A 293 8014 9385 17135 -172 2183 894 O ATOM 3126 CB ASN A 293 17.165 11.525 17.202 1.00 88.08 C ANISOU 3126 CB ASN A 293 7687 9392 16388 -250 1626 783 C ATOM 3127 CG ASN A 293 16.304 10.364 16.778 1.00 88.87 C ANISOU 3127 CG ASN A 293 7660 9396 16710 -265 1610 812 C ATOM 3128 OD1 ASN A 293 15.591 10.422 15.772 1.00 89.36 O ANISOU 3128 OD1 ASN A 293 7559 9417 16977 -308 1482 828 O ATOM 3129 ND2 ASN A 293 16.362 9.277 17.532 1.00 89.09 N ANISOU 3129 ND2 ASN A 293 7765 9383 16702 -232 1730 820 N ATOM 3130 N ILE A 294 16.883 12.376 20.369 1.00 90.90 N ANISOU 3130 N ILE A 294 8321 9583 16634 -133 2168 816 N ATOM 3131 CA ILE A 294 16.658 12.000 21.772 1.00 91.79 C ANISOU 3131 CA ILE A 294 8563 9604 16709 -75 2420 839 C ATOM 3132 C ILE A 294 15.591 12.907 22.419 1.00 92.96 C ANISOU 3132 C ILE A 294 8670 9606 17044 -52 2629 876 C ATOM 3133 O ILE A 294 14.839 12.441 23.277 1.00 94.04 O ANISOU 3133 O ILE A 294 8823 9616 17291 -16 2853 919 O ATOM 3134 CB ILE A 294 17.998 11.936 22.575 1.00 91.04 C ANISOU 3134 CB ILE A 294 8702 9626 16263 -37 2425 792 C ATOM 3135 CG1 ILE A 294 18.986 10.937 21.924 1.00 90.23 C ANISOU 3135 CG1 ILE A 294 8621 9653 16009 -52 2233 760 C ATOM 3136 CG2 ILE A 294 17.770 11.579 24.061 1.00 92.05 C ANISOU 3136 CG2 ILE A 294 8990 9658 16327 27 2686 818 C ATOM 3137 CD1 ILE A 294 20.452 11.152 22.272 1.00 89.25 C ANISOU 3137 CD1 ILE A 294 8676 9680 15555 -32 2150 702 C ATOM 3138 N VAL A 295 15.504 14.183 21.981 1.00 97.27 N ANISOU 3138 N VAL A 295 9157 10165 17637 -72 2559 860 N ATOM 3139 CA VAL A 295 14.529 15.168 22.481 1.00 98.43 C ANISOU 3139 CA VAL A 295 9253 10177 17969 -48 2737 887 C ATOM 3140 C VAL A 295 13.080 14.723 22.171 1.00 99.75 C ANISOU 3140 C VAL A 295 9206 10188 18506 -58 2821 953 C ATOM 3141 O VAL A 295 12.178 14.995 22.967 1.00101.11 O ANISOU 3141 O VAL A 295 9359 10220 18839 -19 3057 988 O ATOM 3142 CB VAL A 295 14.831 16.622 22.006 1.00 97.96 C ANISOU 3142 CB VAL A 295 9180 10168 17873 -68 2619 855 C ATOM 3143 CG1 VAL A 295 13.996 17.647 22.772 1.00 99.23 C ANISOU 3143 CG1 VAL A 295 9336 10190 18177 -27 2829 871 C ATOM 3144 CG2 VAL A 295 16.314 16.956 22.135 1.00 96.66 C ANISOU 3144 CG2 VAL A 295 9200 10165 17362 -72 2502 792 C ATOM 3145 N HIS A 296 12.877 13.996 21.046 1.00102.80 N ANISOU 3145 N HIS A 296 9437 10598 19025 -109 2633 967 N ATOM 3146 CA HIS A 296 11.578 13.455 20.627 1.00104.03 C ANISOU 3146 CA HIS A 296 9377 10614 19535 -129 2667 1025 C ATOM 3147 C HIS A 296 11.066 12.384 21.604 1.00105.08 C ANISOU 3147 C HIS A 296 9546 10638 19741 -97 2903 1067 C ATOM 3148 O HIS A 296 9.854 12.215 21.743 1.00106.54 O ANISOU 3148 O HIS A 296 9577 10670 20234 -96 3041 1123 O ATOM 3149 CB HIS A 296 11.653 12.899 19.198 1.00103.44 C ANISOU 3149 CB HIS A 296 9164 10605 19533 -192 2385 1017 C ATOM 3150 CG HIS A 296 10.642 13.495 18.269 1.00103.80 C ANISOU 3150 CG HIS A 296 8987 10572 19881 -227 2277 1047 C ATOM 3151 ND1 HIS A 296 10.825 14.749 17.712 1.00104.73 N ANISOU 3151 ND1 HIS A 296 9086 10737 19970 -239 2162 1031 N ATOM 3152 CD2 HIS A 296 9.471 12.987 17.822 1.00103.45 C ANISOU 3152 CD2 HIS A 296 8735 10402 20169 -253 2261 1094 C ATOM 3153 CE1 HIS A 296 9.763 14.964 16.953 1.00104.89 C ANISOU 3153 CE1 HIS A 296 8893 10661 20299 -267 2078 1071 C ATOM 3154 NE2 HIS A 296 8.920 13.932 16.987 1.00104.15 N ANISOU 3154 NE2 HIS A 296 8676 10462 20434 -277 2130 1107 N ATOM 3155 N VAL A 297 11.994 11.680 22.286 1.00107.34 N ANISOU 3155 N VAL A 297 10033 11001 19750 -70 2949 1044 N ATOM 3156 CA VAL A 297 11.700 10.653 23.294 1.00108.29 C ANISOU 3156 CA VAL A 297 10233 11033 19879 -35 3171 1085 C ATOM 3157 C VAL A 297 11.239 11.359 24.586 1.00109.49 C ANISOU 3157 C VAL A 297 10485 11084 20033 25 3470 1108 C ATOM 3158 O VAL A 297 10.264 10.925 25.205 1.00111.01 O ANISOU 3158 O VAL A 297 10622 11129 20428 44 3699 1168 O ATOM 3159 CB VAL A 297 12.919 9.711 23.537 1.00107.23 C ANISOU 3159 CB VAL A 297 10288 11020 19434 -22 3094 1052 C ATOM 3160 CG1 VAL A 297 12.592 8.611 24.545 1.00108.31 C ANISOU 3160 CG1 VAL A 297 10511 11057 19584 12 3317 1104 C ATOM 3161 CG2 VAL A 297 13.421 9.102 22.230 1.00106.21 C ANISOU 3161 CG2 VAL A 297 10068 10996 19291 -75 2802 1019 C ATOM 3162 N ILE A 298 11.932 12.457 24.965 1.00111.73 N ANISOU 3162 N ILE A 298 10912 11443 20097 52 3467 1057 N ATOM 3163 CA ILE A 298 11.645 13.273 26.154 1.00112.82 C ANISOU 3163 CA ILE A 298 11174 11500 20192 113 3726 1060 C ATOM 3164 C ILE A 298 10.310 14.021 25.984 1.00114.13 C ANISOU 3164 C ILE A 298 11136 11518 20710 113 3845 1099 C ATOM 3165 O ILE A 298 9.432 13.898 26.840 1.00115.64 O ANISOU 3165 O ILE A 298 11319 11569 21051 153 4120 1146 O ATOM 3166 CB ILE A 298 12.833 14.234 26.503 1.00111.84 C ANISOU 3166 CB ILE A 298 11257 11502 19735 134 3649 985 C ATOM 3167 CG1 ILE A 298 14.230 13.535 26.471 1.00110.47 C ANISOU 3167 CG1 ILE A 298 11251 11490 19233 128 3483 942 C ATOM 3168 CG2 ILE A 298 12.594 15.017 27.807 1.00113.09 C ANISOU 3168 CG2 ILE A 298 11574 11575 19820 202 3916 978 C ATOM 3169 CD1 ILE A 298 14.504 12.358 27.496 1.00111.06 C ANISOU 3169 CD1 ILE A 298 11503 11544 19151 172 3639 967 C ATOM 3170 N GLN A 299 10.164 14.784 24.881 1.00116.38 N ANISOU 3170 N GLN A 299 11258 11834 21127 71 3639 1082 N ATOM 3171 CA GLN A 299 8.958 15.547 24.561 1.00117.56 C ANISOU 3171 CA GLN A 299 11198 11852 21618 70 3702 1117 C ATOM 3172 C GLN A 299 8.468 15.195 23.153 1.00117.14 C ANISOU 3172 C GLN A 299 10895 11799 21814 3 3461 1142 C ATOM 3173 O GLN A 299 9.188 15.408 22.174 1.00115.75 O ANISOU 3173 O GLN A 299 10711 11751 21519 -41 3188 1105 O ATOM 3174 CB GLN A 299 9.207 17.063 24.719 1.00117.66 C ANISOU 3174 CB GLN A 299 11278 11882 21546 96 3703 1073 C ATOM 3175 CG GLN A 299 7.983 17.954 24.474 1.00118.59 C ANISOU 3175 CG GLN A 299 11189 11857 22012 106 3777 1107 C ATOM 3176 CD GLN A 299 6.958 17.890 25.581 1.00120.62 C ANISOU 3176 CD GLN A 299 11432 11945 22454 168 4127 1149 C ATOM 3177 OE1 GLN A 299 7.165 18.400 26.687 1.00121.23 O ANISOU 3177 OE1 GLN A 299 11697 11995 22369 229 4340 1122 O ATOM 3178 NE2 GLN A 299 5.815 17.287 25.294 1.00121.81 N ANISOU 3178 NE2 GLN A 299 11355 11973 22954 152 4193 1215 N ATOM 3179 N ASP A 300 7.245 14.644 23.065 1.00120.30 N ANISOU 3179 N ASP A 300 11095 12053 22560 -6 3565 1206 N ATOM 3180 CA ASP A 300 6.615 14.245 21.807 1.00120.33 C ANISOU 3180 CA ASP A 300 10852 12028 22839 -68 3352 1234 C ATOM 3181 C ASP A 300 6.113 15.466 21.035 1.00120.47 C ANISOU 3181 C ASP A 300 10713 12017 23044 -79 3225 1234 C ATOM 3182 O ASP A 300 5.507 16.364 21.627 1.00121.46 O ANISOU 3182 O ASP A 300 10811 12042 23296 -34 3411 1248 O ATOM 3183 CB ASP A 300 5.468 13.249 22.068 1.00122.03 C ANISOU 3183 CB ASP A 300 10907 12086 23373 -74 3517 1303 C ATOM 3184 CG ASP A 300 4.796 12.715 20.816 1.00122.63 C ANISOU 3184 CG ASP A 300 10731 12120 23742 -140 3292 1329 C ATOM 3185 OD1 ASP A 300 5.469 12.002 20.038 1.00121.53 O ANISOU 3185 OD1 ASP A 300 10617 12088 23470 -186 3055 1300 O ATOM 3186 OD2 ASP A 300 3.590 12.984 20.631 1.00124.32 O ANISOU 3186 OD2 ASP A 300 10723 12190 24323 -144 3356 1378 O ATOM 3187 N ASN A 301 6.368 15.482 19.709 1.00120.25 N ANISOU 3187 N ASN A 301 10588 12074 23028 -138 2910 1218 N ATOM 3188 CA ASN A 301 5.983 16.533 18.756 1.00120.33 C ANISOU 3188 CA ASN A 301 10451 12072 23197 -159 2728 1222 C ATOM 3189 C ASN A 301 6.485 17.944 19.138 1.00119.94 C ANISOU 3189 C ASN A 301 10529 12063 22980 -122 2772 1188 C ATOM 3190 O ASN A 301 5.708 18.904 19.156 1.00120.99 O ANISOU 3190 O ASN A 301 10550 12090 23331 -98 2836 1211 O ATOM 3191 CB ASN A 301 4.469 16.497 18.445 1.00122.22 C ANISOU 3191 CB ASN A 301 10413 12133 23893 -165 2771 1286 C ATOM 3192 CG ASN A 301 3.966 15.185 17.883 1.00122.77 C ANISOU 3192 CG ASN A 301 10337 12160 24150 -214 2679 1316 C ATOM 3193 OD1 ASN A 301 4.483 14.654 16.892 1.00121.73 O ANISOU 3193 OD1 ASN A 301 10203 12130 23918 -267 2413 1292 O ATOM 3194 ND2 ASN A 301 2.911 14.655 18.482 1.00124.58 N ANISOU 3194 ND2 ASN A 301 10435 12229 24671 -198 2897 1370 N ATOM 3195 N LEU A 302 7.793 18.056 19.439 1.00117.48 N ANISOU 3195 N LEU A 302 10449 11900 22287 -118 2733 1132 N ATOM 3196 CA LEU A 302 8.437 19.320 19.802 1.00117.03 C ANISOU 3196 CA LEU A 302 10537 11894 22035 -92 2753 1091 C ATOM 3197 C LEU A 302 9.237 19.879 18.618 1.00115.66 C ANISOU 3197 C LEU A 302 10367 11860 21719 -146 2444 1064 C ATOM 3198 O LEU A 302 9.072 21.050 18.273 1.00115.91 O ANISOU 3198 O LEU A 302 10353 11867 21820 -147 2381 1067 O ATOM 3199 CB LEU A 302 9.321 19.152 21.056 1.00116.63 C ANISOU 3199 CB LEU A 302 10746 11901 21668 -48 2936 1048 C ATOM 3200 CG LEU A 302 9.851 20.434 21.715 1.00116.64 C ANISOU 3200 CG LEU A 302 10909 11920 21489 -10 3014 1003 C ATOM 3201 CD1 LEU A 302 8.774 21.127 22.545 1.00118.41 C ANISOU 3201 CD1 LEU A 302 11082 11968 21940 51 3279 1027 C ATOM 3202 CD2 LEU A 302 11.047 20.133 22.591 1.00116.05 C ANISOU 3202 CD2 LEU A 302 11098 11953 21044 12 3077 951 C ATOM 3203 N ILE A 303 10.087 19.038 17.993 1.00113.05 N ANISOU 3203 N ILE A 303 10090 11670 21193 -190 2259 1041 N ATOM 3204 CA ILE A 303 10.898 19.404 16.830 1.00111.77 C ANISOU 3204 CA ILE A 303 9938 11650 20880 -244 1973 1017 C ATOM 3205 C ILE A 303 10.058 19.260 15.556 1.00112.25 C ANISOU 3205 C ILE A 303 9777 11664 21209 -289 1774 1059 C ATOM 3206 O ILE A 303 9.422 18.223 15.351 1.00112.84 O ANISOU 3206 O ILE A 303 9740 11681 21454 -301 1771 1084 O ATOM 3207 CB ILE A 303 12.239 18.602 16.800 1.00110.32 C ANISOU 3207 CB ILE A 303 9922 11639 20355 -263 1882 967 C ATOM 3208 CG1 ILE A 303 13.261 19.203 17.781 1.00109.59 C ANISOU 3208 CG1 ILE A 303 10048 11620 19971 -231 1987 919 C ATOM 3209 CG2 ILE A 303 12.852 18.501 15.397 1.00109.34 C ANISOU 3209 CG2 ILE A 303 9757 11648 20139 -325 1583 954 C ATOM 3210 CD1 ILE A 303 13.380 18.473 19.067 1.00109.00 C ANISOU 3210 CD1 ILE A 303 10113 11525 19777 -183 2200 904 C ATOM 3211 N ARG A 304 10.057 20.313 14.714 1.00111.98 N ANISOU 3211 N ARG A 304 9686 11649 21212 -315 1604 1070 N ATOM 3212 CA ARG A 304 9.328 20.378 13.441 1.00112.48 C ANISOU 3212 CA ARG A 304 9557 11674 21506 -357 1386 1111 C ATOM 3213 C ARG A 304 9.858 19.342 12.444 1.00111.68 C ANISOU 3213 C ARG A 304 9456 11692 21285 -409 1163 1092 C ATOM 3214 O ARG A 304 11.032 18.967 12.518 1.00110.40 O ANISOU 3214 O ARG A 304 9455 11676 20816 -419 1129 1045 O ATOM 3215 CB ARG A 304 9.433 21.788 12.830 1.00112.20 C ANISOU 3215 CB ARG A 304 9510 11653 21468 -371 1253 1124 C ATOM 3216 CG ARG A 304 8.815 22.898 13.677 1.00113.00 C ANISOU 3216 CG ARG A 304 9597 11623 21715 -317 1450 1140 C ATOM 3217 CD ARG A 304 9.350 24.265 13.292 1.00112.55 C ANISOU 3217 CD ARG A 304 9605 11616 21543 -332 1336 1136 C ATOM 3218 NE ARG A 304 8.702 24.798 12.092 1.00113.81 N ANISOU 3218 NE ARG A 304 9599 11724 21920 -361 1126 1189 N ATOM 3219 CZ ARG A 304 9.086 25.902 11.457 1.00113.70 C ANISOU 3219 CZ ARG A 304 9613 11749 21838 -385 975 1203 C ATOM 3220 NH1 ARG A 304 10.127 26.601 11.894 1.00112.40 N ANISOU 3220 NH1 ARG A 304 9628 11676 21402 -388 1010 1163 N ATOM 3221 NH2 ARG A 304 8.435 26.313 10.376 1.00114.99 N ANISOU 3221 NH2 ARG A 304 9627 11857 22207 -407 782 1257 N ATOM 3222 N LYS A 305 8.992 18.890 11.508 1.00111.83 N ANISOU 3222 N LYS A 305 9294 11644 21552 -440 1008 1127 N ATOM 3223 CA LYS A 305 9.334 17.908 10.471 1.00111.29 C ANISOU 3223 CA LYS A 305 9212 11668 21405 -488 785 1108 C ATOM 3224 C LYS A 305 10.451 18.425 9.555 1.00110.02 C ANISOU 3224 C LYS A 305 9163 11680 20960 -525 569 1079 C ATOM 3225 O LYS A 305 11.329 17.650 9.174 1.00109.09 O ANISOU 3225 O LYS A 305 9140 11693 20616 -547 471 1036 O ATOM 3226 CB LYS A 305 8.092 17.514 9.653 1.00112.65 C ANISOU 3226 CB LYS A 305 9164 11717 21921 -514 651 1151 C ATOM 3227 CG LYS A 305 8.245 16.187 8.918 1.00112.52 C ANISOU 3227 CG LYS A 305 9132 11752 21869 -552 491 1124 C ATOM 3228 CD LYS A 305 7.116 15.947 7.932 1.00113.16 C ANISOU 3228 CD LYS A 305 9007 11727 22262 -586 298 1161 C ATOM 3229 CE LYS A 305 7.349 14.695 7.124 1.00113.15 C ANISOU 3229 CE LYS A 305 9011 11784 22196 -626 117 1123 C ATOM 3230 NZ LYS A 305 6.272 14.474 6.125 1.00113.77 N ANISOU 3230 NZ LYS A 305 8897 11759 22572 -663 -94 1153 N ATOM 3231 N GLU A 306 10.427 19.738 9.234 1.00108.28 N ANISOU 3231 N GLU A 306 8933 11455 20753 -530 507 1105 N ATOM 3232 CA GLU A 306 11.429 20.418 8.406 1.00107.28 C ANISOU 3232 CA GLU A 306 8908 11477 20377 -568 322 1091 C ATOM 3233 C GLU A 306 12.803 20.419 9.083 1.00105.91 C ANISOU 3233 C GLU A 306 8936 11446 19859 -559 419 1036 C ATOM 3234 O GLU A 306 13.817 20.311 8.396 1.00104.95 O ANISOU 3234 O GLU A 306 8906 11479 19492 -594 272 1007 O ATOM 3235 CB GLU A 306 10.994 21.859 8.100 1.00107.89 C ANISOU 3235 CB GLU A 306 8927 11488 20578 -569 271 1138 C ATOM 3236 CG GLU A 306 9.935 21.969 7.017 1.00109.15 C ANISOU 3236 CG GLU A 306 8907 11555 21011 -592 78 1193 C ATOM 3237 CD GLU A 306 9.485 23.387 6.724 1.00109.90 C ANISOU 3237 CD GLU A 306 8943 11574 21240 -587 25 1246 C ATOM 3238 OE1 GLU A 306 10.295 24.168 6.173 1.00109.22 O ANISOU 3238 OE1 GLU A 306 8958 11591 20950 -617 -94 1249 O ATOM 3239 OE2 GLU A 306 8.316 23.712 7.030 1.00111.26 O ANISOU 3239 OE2 GLU A 306 8965 11578 21731 -554 104 1287 O ATOM 3240 N VAL A 307 12.825 20.532 10.429 1.00103.72 N ANISOU 3240 N VAL A 307 8728 11114 19567 -511 665 1021 N ATOM 3241 CA VAL A 307 14.037 20.538 11.258 1.00102.65 C ANISOU 3241 CA VAL A 307 8783 11091 19128 -494 774 968 C ATOM 3242 C VAL A 307 14.670 19.131 11.278 1.00101.93 C ANISOU 3242 C VAL A 307 8757 11095 18877 -497 757 927 C ATOM 3243 O VAL A 307 15.884 19.012 11.104 1.00100.83 O ANISOU 3243 O VAL A 307 8742 11110 18459 -513 684 885 O ATOM 3244 CB VAL A 307 13.762 21.103 12.685 1.00103.18 C ANISOU 3244 CB VAL A 307 8910 11055 19239 -438 1037 966 C ATOM 3245 CG1 VAL A 307 15.026 21.117 13.544 1.00102.21 C ANISOU 3245 CG1 VAL A 307 8991 11046 18799 -422 1130 909 C ATOM 3246 CG2 VAL A 307 13.157 22.504 12.619 1.00103.77 C ANISOU 3246 CG2 VAL A 307 8922 11033 19473 -432 1046 1001 C ATOM 3247 N TYR A 308 13.840 18.078 11.459 1.00 99.86 N ANISOU 3247 N TYR A 308 8403 10736 18803 -481 820 941 N ATOM 3248 CA TYR A 308 14.263 16.672 11.492 1.00 99.39 C ANISOU 3248 CA TYR A 308 8389 10736 18638 -480 810 907 C ATOM 3249 C TYR A 308 14.875 16.219 10.158 1.00 98.70 C ANISOU 3249 C TYR A 308 8299 10780 18423 -527 554 882 C ATOM 3250 O TYR A 308 15.891 15.523 10.167 1.00 97.74 O ANISOU 3250 O TYR A 308 8289 10783 18064 -526 525 834 O ATOM 3251 CB TYR A 308 13.086 15.761 11.900 1.00100.53 C ANISOU 3251 CB TYR A 308 8414 10723 19060 -461 928 938 C ATOM 3252 CG TYR A 308 13.450 14.302 12.093 1.00100.22 C ANISOU 3252 CG TYR A 308 8427 10720 18932 -455 946 908 C ATOM 3253 CD1 TYR A 308 13.213 13.365 11.091 1.00100.09 C ANISOU 3253 CD1 TYR A 308 8323 10711 18995 -490 768 901 C ATOM 3254 CD2 TYR A 308 13.994 13.851 13.293 1.00100.20 C ANISOU 3254 CD2 TYR A 308 8566 10733 18773 -411 1139 888 C ATOM 3255 CE1 TYR A 308 13.537 12.020 11.266 1.00 99.89 C ANISOU 3255 CE1 TYR A 308 8347 10708 18898 -482 783 872 C ATOM 3256 CE2 TYR A 308 14.318 12.508 13.481 1.00100.02 C ANISOU 3256 CE2 TYR A 308 8593 10734 18676 -402 1154 866 C ATOM 3257 CZ TYR A 308 14.088 11.596 12.464 1.00 99.84 C ANISOU 3257 CZ TYR A 308 8478 10716 18740 -437 978 857 C ATOM 3258 OH TYR A 308 14.404 10.270 12.643 1.00 99.74 O ANISOU 3258 OH TYR A 308 8516 10718 18662 -427 990 833 O ATOM 3259 N ILE A 309 14.258 16.616 9.024 1.00 94.99 N ANISOU 3259 N ILE A 309 7705 10280 18106 -565 372 914 N ATOM 3260 CA ILE A 309 14.713 16.276 7.669 1.00 94.57 C ANISOU 3260 CA ILE A 309 7649 10340 17943 -610 123 894 C ATOM 3261 C ILE A 309 16.029 16.998 7.322 1.00 93.50 C ANISOU 3261 C ILE A 309 7648 10377 17501 -630 44 868 C ATOM 3262 O ILE A 309 16.951 16.355 6.815 1.00 92.81 O ANISOU 3262 O ILE A 309 7639 10425 17200 -643 -53 823 O ATOM 3263 CB ILE A 309 13.576 16.471 6.612 1.00 95.67 C ANISOU 3263 CB ILE A 309 7621 10381 18349 -642 -50 940 C ATOM 3264 CG1 ILE A 309 12.432 15.450 6.844 1.00 96.71 C ANISOU 3264 CG1 ILE A 309 7618 10362 18765 -631 3 955 C ATOM 3265 CG2 ILE A 309 14.100 16.377 5.165 1.00 95.35 C ANISOU 3265 CG2 ILE A 309 7603 10464 18162 -688 -314 923 C ATOM 3266 CD1 ILE A 309 11.044 15.853 6.291 1.00 98.16 C ANISOU 3266 CD1 ILE A 309 7608 10391 19297 -647 -88 1014 C ATOM 3267 N LEU A 310 16.119 18.315 7.625 1.00 90.49 N ANISOU 3267 N LEU A 310 7291 9984 17108 -630 95 894 N ATOM 3268 CA LEU A 310 17.304 19.146 7.370 1.00 89.63 C ANISOU 3268 CA LEU A 310 7298 10020 16738 -654 34 878 C ATOM 3269 C LEU A 310 18.541 18.634 8.118 1.00 88.58 C ANISOU 3269 C LEU A 310 7312 10008 16336 -634 131 818 C ATOM 3270 O LEU A 310 19.607 18.535 7.511 1.00 87.85 O ANISOU 3270 O LEU A 310 7293 10069 16017 -660 21 788 O ATOM 3271 CB LEU A 310 17.032 20.621 7.718 1.00 89.99 C ANISOU 3271 CB LEU A 310 7336 9996 16860 -654 93 918 C ATOM 3272 CG LEU A 310 18.040 21.642 7.186 1.00 89.36 C ANISOU 3272 CG LEU A 310 7343 10041 16569 -694 -8 919 C ATOM 3273 CD1 LEU A 310 17.529 22.308 5.921 1.00 89.88 C ANISOU 3273 CD1 LEU A 310 7323 10087 16740 -737 -201 975 C ATOM 3274 CD2 LEU A 310 18.349 22.691 8.234 1.00 89.37 C ANISOU 3274 CD2 LEU A 310 7422 10010 16525 -675 146 915 C ATOM 3275 N LEU A 311 18.393 18.294 9.419 1.00 86.29 N ANISOU 3275 N LEU A 311 7064 9648 16074 -585 335 804 N ATOM 3276 CA LEU A 311 19.482 17.773 10.255 1.00 85.45 C ANISOU 3276 CA LEU A 311 7100 9638 15729 -558 431 751 C ATOM 3277 C LEU A 311 19.943 16.389 9.802 1.00 85.07 C ANISOU 3277 C LEU A 311 7067 9673 15583 -556 352 712 C ATOM 3278 O LEU A 311 21.124 16.065 9.942 1.00 84.25 O ANISOU 3278 O LEU A 311 7071 9702 15238 -550 339 666 O ATOM 3279 CB LEU A 311 19.105 17.766 11.745 1.00 85.78 C ANISOU 3279 CB LEU A 311 7192 9571 15829 -504 667 752 C ATOM 3280 CG LEU A 311 18.982 19.132 12.428 1.00 86.14 C ANISOU 3280 CG LEU A 311 7273 9557 15900 -495 770 768 C ATOM 3281 CD1 LEU A 311 18.186 19.024 13.701 1.00 86.90 C ANISOU 3281 CD1 LEU A 311 7380 9506 16132 -440 1002 780 C ATOM 3282 CD2 LEU A 311 20.346 19.751 12.710 1.00 85.36 C ANISOU 3282 CD2 LEU A 311 7317 9593 15523 -507 749 728 C ATOM 3283 N ASN A 312 19.013 15.586 9.245 1.00 83.57 N ANISOU 3283 N ASN A 312 6765 9401 15587 -561 292 729 N ATOM 3284 CA ASN A 312 19.294 14.260 8.694 1.00 83.41 C ANISOU 3284 CA ASN A 312 6746 9438 15508 -562 200 692 C ATOM 3285 C ASN A 312 20.074 14.452 7.389 1.00 82.97 C ANISOU 3285 C ASN A 312 6709 9531 15285 -604 -8 669 C ATOM 3286 O ASN A 312 21.031 13.720 7.137 1.00 82.43 O ANISOU 3286 O ASN A 312 6714 9585 15020 -598 -59 619 O ATOM 3287 CB ASN A 312 17.984 13.499 8.423 1.00 84.45 C ANISOU 3287 CB ASN A 312 6743 9422 15922 -564 183 719 C ATOM 3288 CG ASN A 312 18.063 11.986 8.499 1.00 84.52 C ANISOU 3288 CG ASN A 312 6766 9426 15921 -545 188 684 C ATOM 3289 OD1 ASN A 312 17.129 11.324 8.962 1.00 85.26 O ANISOU 3289 OD1 ASN A 312 6786 9381 16228 -530 278 707 O ATOM 3290 ND2 ASN A 312 19.147 11.389 8.016 1.00 83.88 N ANISOU 3290 ND2 ASN A 312 6773 9490 15608 -545 92 628 N ATOM 3291 N TRP A 313 19.686 15.474 6.591 1.00 80.93 N ANISOU 3291 N TRP A 313 6389 9261 15100 -644 -118 710 N ATOM 3292 CA TRP A 313 20.311 15.827 5.315 1.00 80.68 C ANISOU 3292 CA TRP A 313 6376 9358 14921 -688 -309 704 C ATOM 3293 C TRP A 313 21.732 16.384 5.427 1.00 79.75 C ANISOU 3293 C TRP A 313 6377 9401 14523 -697 -297 676 C ATOM 3294 O TRP A 313 22.469 16.337 4.442 1.00 79.47 O ANISOU 3294 O TRP A 313 6375 9496 14324 -726 -431 657 O ATOM 3295 CB TRP A 313 19.404 16.742 4.485 1.00 81.47 C ANISOU 3295 CB TRP A 313 6377 9381 15196 -725 -428 765 C ATOM 3296 CG TRP A 313 18.559 15.979 3.514 1.00 82.22 C ANISOU 3296 CG TRP A 313 6378 9419 15443 -740 -582 769 C ATOM 3297 CD1 TRP A 313 17.304 15.492 3.727 1.00 83.13 C ANISOU 3297 CD1 TRP A 313 6375 9374 15837 -727 -558 792 C ATOM 3298 CD2 TRP A 313 18.944 15.541 2.205 1.00 82.23 C ANISOU 3298 CD2 TRP A 313 6402 9523 15319 -770 -781 745 C ATOM 3299 NE1 TRP A 313 16.867 14.807 2.618 1.00 83.69 N ANISOU 3299 NE1 TRP A 313 6390 9436 15972 -751 -746 782 N ATOM 3300 CE2 TRP A 313 17.855 14.821 1.667 1.00 83.16 C ANISOU 3300 CE2 TRP A 313 6415 9530 15651 -776 -885 751 C ATOM 3301 CE3 TRP A 313 20.100 15.704 1.423 1.00 81.65 C ANISOU 3301 CE3 TRP A 313 6427 9623 14974 -794 -879 718 C ATOM 3302 CZ2 TRP A 313 17.888 14.260 0.386 1.00 83.53 C ANISOU 3302 CZ2 TRP A 313 6467 9633 15638 -801 -1091 726 C ATOM 3303 CZ3 TRP A 313 20.131 15.152 0.151 1.00 82.03 C ANISOU 3303 CZ3 TRP A 313 6479 9729 14959 -817 -1067 697 C ATOM 3304 CH2 TRP A 313 19.034 14.443 -0.356 1.00 82.96 C ANISOU 3304 CH2 TRP A 313 6506 9733 15282 -819 -1176 698 C ATOM 3305 N ILE A 314 22.124 16.893 6.617 1.00 76.50 N ANISOU 3305 N ILE A 314 6030 8979 14057 -673 -137 673 N ATOM 3306 CA ILE A 314 23.479 17.400 6.879 1.00 75.72 C ANISOU 3306 CA ILE A 314 6040 9021 13709 -681 -118 643 C ATOM 3307 C ILE A 314 24.453 16.201 6.854 1.00 75.13 C ANISOU 3307 C ILE A 314 6031 9067 13448 -657 -132 580 C ATOM 3308 O ILE A 314 25.548 16.304 6.295 1.00 74.65 O ANISOU 3308 O ILE A 314 6020 9156 13187 -678 -210 554 O ATOM 3309 CB ILE A 314 23.541 18.246 8.193 1.00 75.67 C ANISOU 3309 CB ILE A 314 6089 8953 13709 -659 48 652 C ATOM 3310 CG1 ILE A 314 22.751 19.568 8.029 1.00 76.21 C ANISOU 3310 CG1 ILE A 314 6097 8923 13936 -687 38 711 C ATOM 3311 CG2 ILE A 314 24.992 18.538 8.625 1.00 74.92 C ANISOU 3311 CG2 ILE A 314 6110 8998 13359 -661 73 610 C ATOM 3312 CD1 ILE A 314 22.278 20.238 9.335 1.00 76.54 C ANISOU 3312 CD1 ILE A 314 6164 8839 14079 -652 219 722 C ATOM 3313 N GLY A 315 23.999 15.070 7.394 1.00 74.13 N ANISOU 3313 N GLY A 315 5895 8868 13404 -613 -60 560 N ATOM 3314 CA GLY A 315 24.744 13.818 7.416 1.00 73.75 C ANISOU 3314 CA GLY A 315 5900 8904 13218 -581 -69 503 C ATOM 3315 C GLY A 315 24.814 13.126 6.066 1.00 73.83 C ANISOU 3315 C GLY A 315 5873 8981 13198 -602 -236 479 C ATOM 3316 O GLY A 315 25.692 12.287 5.849 1.00 73.45 O ANISOU 3316 O GLY A 315 5877 9039 12992 -581 -270 425 O ATOM 3317 N TYR A 316 23.878 13.465 5.151 1.00 75.25 N ANISOU 3317 N TYR A 316 5965 9096 13531 -640 -345 517 N ATOM 3318 CA TYR A 316 23.816 12.934 3.783 1.00 75.52 C ANISOU 3318 CA TYR A 316 5970 9182 13543 -664 -521 498 C ATOM 3319 C TYR A 316 24.953 13.539 2.946 1.00 75.08 C ANISOU 3319 C TYR A 316 5974 9298 13255 -696 -613 485 C ATOM 3320 O TYR A 316 25.559 12.834 2.137 1.00 74.93 O ANISOU 3320 O TYR A 316 5988 9384 13099 -694 -705 437 O ATOM 3321 CB TYR A 316 22.452 13.262 3.138 1.00 76.43 C ANISOU 3321 CB TYR A 316 5976 9166 13898 -695 -615 550 C ATOM 3322 CG TYR A 316 21.351 12.241 3.351 1.00 77.15 C ANISOU 3322 CG TYR A 316 5989 9110 14215 -674 -600 547 C ATOM 3323 CD1 TYR A 316 20.556 11.812 2.293 1.00 78.01 C ANISOU 3323 CD1 TYR A 316 6023 9163 14454 -699 -763 551 C ATOM 3324 CD2 TYR A 316 21.062 11.750 4.623 1.00 77.10 C ANISOU 3324 CD2 TYR A 316 5983 9011 14301 -633 -424 547 C ATOM 3325 CE1 TYR A 316 19.520 10.899 2.487 1.00 78.79 C ANISOU 3325 CE1 TYR A 316 6037 9117 14782 -687 -754 551 C ATOM 3326 CE2 TYR A 316 20.034 10.830 4.827 1.00 77.87 C ANISOU 3326 CE2 TYR A 316 6001 8966 14620 -620 -400 553 C ATOM 3327 CZ TYR A 316 19.264 10.409 3.757 1.00 78.71 C ANISOU 3327 CZ TYR A 316 6021 9017 14867 -649 -567 554 C ATOM 3328 OH TYR A 316 18.246 9.509 3.958 1.00 79.56 O ANISOU 3328 OH TYR A 316 6042 8978 15210 -643 -548 560 O ATOM 3329 N VAL A 317 25.242 14.844 3.161 1.00 74.96 N ANISOU 3329 N VAL A 317 5974 9308 13199 -725 -580 526 N ATOM 3330 CA VAL A 317 26.299 15.611 2.484 1.00 74.64 C ANISOU 3330 CA VAL A 317 5984 9419 12957 -764 -645 529 C ATOM 3331 C VAL A 317 27.691 15.135 2.958 1.00 73.94 C ANISOU 3331 C VAL A 317 5975 9468 12650 -736 -578 468 C ATOM 3332 O VAL A 317 28.646 15.173 2.178 1.00 73.82 O ANISOU 3332 O VAL A 317 5995 9597 12456 -756 -647 447 O ATOM 3333 CB VAL A 317 26.099 17.152 2.645 1.00 74.75 C ANISOU 3333 CB VAL A 317 5985 9393 13024 -804 -625 595 C ATOM 3334 CG1 VAL A 317 27.113 17.945 1.822 1.00 74.53 C ANISOU 3334 CG1 VAL A 317 6002 9511 12804 -854 -700 608 C ATOM 3335 CG2 VAL A 317 24.681 17.571 2.265 1.00 75.56 C ANISOU 3335 CG2 VAL A 317 5999 9347 13364 -821 -688 655 C ATOM 3336 N ASN A 318 27.783 14.644 4.219 1.00 74.66 N ANISOU 3336 N ASN A 318 6094 9512 12762 -687 -446 443 N ATOM 3337 CA ASN A 318 29.004 14.125 4.855 1.00 74.09 C ANISOU 3337 CA ASN A 318 6094 9547 12510 -651 -381 387 C ATOM 3338 C ASN A 318 29.667 12.985 4.059 1.00 74.06 C ANISOU 3338 C ASN A 318 6107 9653 12379 -629 -460 328 C ATOM 3339 O ASN A 318 30.885 12.810 4.149 1.00 73.68 O ANISOU 3339 O ASN A 318 6106 9736 12153 -615 -447 287 O ATOM 3340 CB ASN A 318 28.710 13.679 6.290 1.00 73.99 C ANISOU 3340 CB ASN A 318 6110 9433 12569 -598 -238 378 C ATOM 3341 CG ASN A 318 29.943 13.396 7.109 1.00 73.51 C ANISOU 3341 CG ASN A 318 6131 9469 12331 -561 -171 333 C ATOM 3342 OD1 ASN A 318 30.497 14.281 7.760 1.00 73.22 O ANISOU 3342 OD1 ASN A 318 6136 9462 12222 -573 -118 341 O ATOM 3343 ND2 ASN A 318 30.411 12.159 7.077 1.00 73.50 N ANISOU 3343 ND2 ASN A 318 6153 9515 12259 -515 -182 282 N ATOM 3344 N SER A 319 28.867 12.219 3.288 1.00 73.62 N ANISOU 3344 N SER A 319 6010 9541 12422 -626 -543 320 N ATOM 3345 CA SER A 319 29.331 11.116 2.443 1.00 73.75 C ANISOU 3345 CA SER A 319 6044 9641 12337 -604 -627 258 C ATOM 3346 C SER A 319 30.248 11.615 1.315 1.00 73.82 C ANISOU 3346 C SER A 319 6077 9810 12162 -641 -718 249 C ATOM 3347 O SER A 319 31.183 10.912 0.930 1.00 73.80 O ANISOU 3347 O SER A 319 6111 9924 12005 -614 -738 190 O ATOM 3348 CB SER A 319 28.142 10.351 1.870 1.00 74.38 C ANISOU 3348 CB SER A 319 6073 9603 12585 -602 -707 257 C ATOM 3349 OG SER A 319 27.354 9.781 2.901 1.00 74.38 O ANISOU 3349 OG SER A 319 6049 9458 12754 -568 -611 265 O ATOM 3350 N GLY A 320 29.978 12.825 0.824 1.00 72.45 N ANISOU 3350 N GLY A 320 5882 9636 12010 -700 -763 311 N ATOM 3351 CA GLY A 320 30.758 13.479 -0.221 1.00 72.62 C ANISOU 3351 CA GLY A 320 5928 9796 11869 -745 -837 321 C ATOM 3352 C GLY A 320 31.826 14.418 0.308 1.00 72.17 C ANISOU 3352 C GLY A 320 5896 9835 11691 -767 -760 337 C ATOM 3353 O GLY A 320 32.610 14.960 -0.476 1.00 72.37 O ANISOU 3353 O GLY A 320 5940 9984 11573 -805 -802 348 O ATOM 3354 N PHE A 321 31.864 14.617 1.644 1.00 70.11 N ANISOU 3354 N PHE A 321 5639 9514 11485 -744 -648 340 N ATOM 3355 CA PHE A 321 32.835 15.476 2.326 1.00 69.71 C ANISOU 3355 CA PHE A 321 5615 9535 11337 -762 -577 348 C ATOM 3356 C PHE A 321 34.223 14.832 2.362 1.00 69.48 C ANISOU 3356 C PHE A 321 5617 9657 11125 -732 -557 285 C ATOM 3357 O PHE A 321 35.200 15.488 2.000 1.00 69.53 O ANISOU 3357 O PHE A 321 5629 9783 11006 -770 -567 292 O ATOM 3358 CB PHE A 321 32.366 15.815 3.754 1.00 69.41 C ANISOU 3358 CB PHE A 321 5586 9375 11412 -741 -469 364 C ATOM 3359 CG PHE A 321 31.818 17.210 3.939 1.00 69.57 C ANISOU 3359 CG PHE A 321 5590 9315 11528 -792 -456 431 C ATOM 3360 CD1 PHE A 321 30.449 17.446 3.909 1.00 69.89 C ANISOU 3360 CD1 PHE A 321 5587 9204 11764 -796 -463 475 C ATOM 3361 CD2 PHE A 321 32.669 18.284 4.174 1.00 69.47 C ANISOU 3361 CD2 PHE A 321 5602 9371 11423 -834 -437 448 C ATOM 3362 CE1 PHE A 321 29.942 18.735 4.096 1.00 70.10 C ANISOU 3362 CE1 PHE A 321 5598 9150 11887 -835 -448 535 C ATOM 3363 CE2 PHE A 321 32.161 19.574 4.356 1.00 69.68 C ANISOU 3363 CE2 PHE A 321 5619 9314 11543 -879 -426 507 C ATOM 3364 CZ PHE A 321 30.800 19.790 4.316 1.00 69.99 C ANISOU 3364 CZ PHE A 321 5618 9203 11772 -876 -431 550 C ATOM 3365 N ASN A 322 34.297 13.545 2.789 1.00 66.29 N ANISOU 3365 N ASN A 322 5228 9241 10718 -663 -529 226 N ATOM 3366 CA ASN A 322 35.520 12.738 2.912 1.00 66.14 C ANISOU 3366 CA ASN A 322 5234 9345 10551 -616 -509 159 C ATOM 3367 C ASN A 322 36.479 12.784 1.700 1.00 66.46 C ANISOU 3367 C ASN A 322 5268 9549 10435 -640 -570 139 C ATOM 3368 O ASN A 322 37.655 13.074 1.932 1.00 66.35 O ANISOU 3368 O ASN A 322 5257 9648 10305 -644 -537 123 O ATOM 3369 CB ASN A 322 35.211 11.289 3.334 1.00 66.15 C ANISOU 3369 CB ASN A 322 5251 9284 10599 -539 -489 107 C ATOM 3370 CG ASN A 322 34.389 11.148 4.596 1.00 65.95 C ANISOU 3370 CG ASN A 322 5239 9107 10712 -510 -408 127 C ATOM 3371 OD1 ASN A 322 34.592 11.848 5.596 1.00 65.70 O ANISOU 3371 OD1 ASN A 322 5230 9052 10681 -516 -336 150 O ATOM 3372 ND2 ASN A 322 33.454 10.211 4.586 1.00 66.16 N ANISOU 3372 ND2 ASN A 322 5257 9025 10856 -477 -413 117 N ATOM 3373 N PRO A 323 36.038 12.562 0.422 1.00 64.06 N ANISOU 3373 N PRO A 323 4958 9260 10122 -659 -657 141 N ATOM 3374 CA PRO A 323 36.989 12.627 -0.709 1.00 64.48 C ANISOU 3374 CA PRO A 323 5018 9472 10010 -680 -697 122 C ATOM 3375 C PRO A 323 37.727 13.957 -0.865 1.00 64.54 C ANISOU 3375 C PRO A 323 5014 9568 9940 -750 -679 176 C ATOM 3376 O PRO A 323 38.889 13.955 -1.271 1.00 64.73 O ANISOU 3376 O PRO A 323 5036 9736 9823 -753 -661 152 O ATOM 3377 CB PRO A 323 36.114 12.313 -1.926 1.00 65.08 C ANISOU 3377 CB PRO A 323 5103 9513 10111 -694 -799 127 C ATOM 3378 CG PRO A 323 34.964 11.554 -1.375 1.00 64.94 C ANISOU 3378 CG PRO A 323 5076 9338 10260 -654 -808 115 C ATOM 3379 CD PRO A 323 34.688 12.201 -0.061 1.00 64.38 C ANISOU 3379 CD PRO A 323 4987 9177 10297 -661 -724 157 C ATOM 3380 N LEU A 324 37.064 15.080 -0.522 1.00 62.70 N ANISOU 3380 N LEU A 324 4771 9245 9808 -804 -678 248 N ATOM 3381 CA LEU A 324 37.652 16.421 -0.577 1.00 62.79 C ANISOU 3381 CA LEU A 324 4773 9313 9771 -877 -662 305 C ATOM 3382 C LEU A 324 38.677 16.622 0.543 1.00 62.38 C ANISOU 3382 C LEU A 324 4715 9309 9677 -864 -582 280 C ATOM 3383 O LEU A 324 39.642 17.366 0.356 1.00 62.57 O ANISOU 3383 O LEU A 324 4726 9434 9613 -913 -568 299 O ATOM 3384 CB LEU A 324 36.566 17.505 -0.523 1.00 62.94 C ANISOU 3384 CB LEU A 324 4785 9204 9925 -930 -690 385 C ATOM 3385 CG LEU A 324 35.841 17.780 -1.840 1.00 63.62 C ANISOU 3385 CG LEU A 324 4876 9277 10020 -971 -790 434 C ATOM 3386 CD1 LEU A 324 34.373 18.069 -1.605 1.00 63.76 C ANISOU 3386 CD1 LEU A 324 4875 9122 10229 -974 -827 479 C ATOM 3387 CD2 LEU A 324 36.499 18.917 -2.609 1.00 64.06 C ANISOU 3387 CD2 LEU A 324 4939 9426 9975 -1049 -809 496 C ATOM 3388 N ILE A 325 38.474 15.948 1.697 1.00 61.62 N ANISOU 3388 N ILE A 325 4632 9138 9643 -801 -532 238 N ATOM 3389 CA ILE A 325 39.386 16.004 2.845 1.00 61.31 C ANISOU 3389 CA ILE A 325 4600 9133 9563 -778 -469 208 C ATOM 3390 C ILE A 325 40.596 15.081 2.594 1.00 61.46 C ANISOU 3390 C ILE A 325 4606 9294 9451 -731 -465 141 C ATOM 3391 O ILE A 325 41.684 15.357 3.104 1.00 61.46 O ANISOU 3391 O ILE A 325 4593 9375 9384 -735 -437 124 O ATOM 3392 CB ILE A 325 38.677 15.738 4.212 1.00 60.90 C ANISOU 3392 CB ILE A 325 4581 8939 9619 -730 -414 199 C ATOM 3393 CG1 ILE A 325 37.341 16.513 4.326 1.00 60.89 C ANISOU 3393 CG1 ILE A 325 4582 8788 9766 -766 -413 261 C ATOM 3394 CG2 ILE A 325 39.600 16.092 5.391 1.00 60.73 C ANISOU 3394 CG2 ILE A 325 4582 8946 9546 -721 -364 178 C ATOM 3395 CD1 ILE A 325 36.272 15.861 5.231 1.00 60.71 C ANISOU 3395 CD1 ILE A 325 4581 8613 9873 -709 -361 253 C ATOM 3396 N TYR A 326 40.417 14.018 1.771 1.00 62.76 N ANISOU 3396 N TYR A 326 4772 9488 9586 -688 -498 102 N ATOM 3397 CA TYR A 326 41.491 13.082 1.407 1.00 63.03 C ANISOU 3397 CA TYR A 326 4794 9652 9503 -636 -493 35 C ATOM 3398 C TYR A 326 42.567 13.744 0.528 1.00 63.56 C ANISOU 3398 C TYR A 326 4826 9874 9450 -690 -495 49 C ATOM 3399 O TYR A 326 43.688 13.235 0.450 1.00 63.85 O ANISOU 3399 O TYR A 326 4836 10028 9396 -654 -471 -1 O ATOM 3400 CB TYR A 326 40.936 11.813 0.725 1.00 63.24 C ANISOU 3400 CB TYR A 326 4840 9654 9535 -577 -530 -14 C ATOM 3401 CG TYR A 326 40.149 10.877 1.623 1.00 62.88 C ANISOU 3401 CG TYR A 326 4821 9474 9596 -511 -516 -40 C ATOM 3402 CD1 TYR A 326 38.996 10.247 1.166 1.00 63.07 C ANISOU 3402 CD1 TYR A 326 4861 9396 9707 -496 -560 -44 C ATOM 3403 CD2 TYR A 326 40.592 10.574 2.909 1.00 62.47 C ANISOU 3403 CD2 TYR A 326 4782 9398 9555 -462 -461 -62 C ATOM 3404 CE1 TYR A 326 38.272 9.379 1.982 1.00 62.83 C ANISOU 3404 CE1 TYR A 326 4850 9239 9784 -440 -538 -63 C ATOM 3405 CE2 TYR A 326 39.879 9.703 3.733 1.00 62.25 C ANISOU 3405 CE2 TYR A 326 4787 9246 9619 -402 -438 -79 C ATOM 3406 CZ TYR A 326 38.718 9.109 3.265 1.00 62.44 C ANISOU 3406 CZ TYR A 326 4819 9167 9739 -393 -471 -78 C ATOM 3407 OH TYR A 326 38.012 8.247 4.069 1.00 62.32 O ANISOU 3407 OH TYR A 326 4831 9024 9824 -339 -439 -89 O ATOM 3408 N CYS A 327 42.229 14.890 -0.107 1.00 66.61 N ANISOU 3408 N CYS A 327 5209 10255 9845 -776 -519 121 N ATOM 3409 CA CYS A 327 43.123 15.682 -0.959 1.00 67.19 C ANISOU 3409 CA CYS A 327 5254 10459 9816 -843 -513 155 C ATOM 3410 C CYS A 327 44.272 16.332 -0.170 1.00 67.18 C ANISOU 3410 C CYS A 327 5210 10525 9791 -870 -466 158 C ATOM 3411 O CYS A 327 45.261 16.746 -0.778 1.00 67.76 O ANISOU 3411 O CYS A 327 5244 10724 9777 -913 -446 171 O ATOM 3412 CB CYS A 327 42.334 16.716 -1.758 1.00 67.44 C ANISOU 3412 CB CYS A 327 5304 10444 9876 -924 -558 239 C ATOM 3413 SG CYS A 327 41.328 16.014 -3.092 1.00 68.17 S ANISOU 3413 SG CYS A 327 5441 10514 9946 -906 -635 234 S ATOM 3414 N ARG A 328 44.137 16.415 1.175 1.00 71.16 N ANISOU 3414 N ARG A 328 5723 10942 10372 -847 -448 146 N ATOM 3415 CA ARG A 328 45.126 16.971 2.108 1.00 71.15 C ANISOU 3415 CA ARG A 328 5693 10980 10361 -866 -420 139 C ATOM 3416 C ARG A 328 46.454 16.209 2.053 1.00 71.54 C ANISOU 3416 C ARG A 328 5692 11170 10320 -817 -400 77 C ATOM 3417 O ARG A 328 47.516 16.832 2.105 1.00 71.88 O ANISOU 3417 O ARG A 328 5681 11305 10326 -863 -386 86 O ATOM 3418 CB ARG A 328 44.578 16.939 3.541 1.00 70.57 C ANISOU 3418 CB ARG A 328 5664 10775 10374 -829 -409 127 C ATOM 3419 CG ARG A 328 43.982 18.257 4.017 1.00 70.42 C ANISOU 3419 CG ARG A 328 5669 10654 10434 -901 -409 189 C ATOM 3420 CD ARG A 328 43.380 18.147 5.411 1.00 70.00 C ANISOU 3420 CD ARG A 328 5674 10467 10456 -855 -383 171 C ATOM 3421 NE ARG A 328 44.334 17.638 6.402 1.00 70.00 N ANISOU 3421 NE ARG A 328 5680 10512 10405 -802 -371 114 N ATOM 3422 CZ ARG A 328 45.155 18.396 7.122 1.00 70.24 C ANISOU 3422 CZ ARG A 328 5707 10567 10414 -837 -375 110 C ATOM 3423 NH1 ARG A 328 45.151 19.716 6.977 1.00 70.44 N ANISOU 3423 NH1 ARG A 328 5722 10575 10467 -927 -384 161 N ATOM 3424 NH2 ARG A 328 45.986 17.842 7.994 1.00 70.33 N ANISOU 3424 NH2 ARG A 328 5726 10616 10380 -781 -379 57 N ATOM 3425 N SER A 329 46.385 14.866 1.954 1.00 76.27 N ANISOU 3425 N SER A 329 6304 11779 10896 -725 -400 13 N ATOM 3426 CA SER A 329 47.548 13.985 1.879 1.00 76.72 C ANISOU 3426 CA SER A 329 6315 11957 10879 -661 -381 -53 C ATOM 3427 C SER A 329 48.216 14.088 0.497 1.00 77.51 C ANISOU 3427 C SER A 329 6368 12197 10885 -694 -363 -48 C ATOM 3428 O SER A 329 47.509 14.038 -0.515 1.00 77.61 O ANISOU 3428 O SER A 329 6416 12198 10874 -712 -378 -28 O ATOM 3429 CB SER A 329 47.143 12.542 2.170 1.00 76.47 C ANISOU 3429 CB SER A 329 6322 11873 10861 -553 -387 -118 C ATOM 3430 OG SER A 329 48.259 11.666 2.153 1.00 77.01 O ANISOU 3430 OG SER A 329 6345 12048 10867 -482 -371 -184 O ATOM 3431 N PRO A 330 49.564 14.230 0.425 1.00 83.26 N ANISOU 3431 N PRO A 330 7018 13058 11559 -702 -331 -65 N ATOM 3432 CA PRO A 330 50.226 14.326 -0.890 1.00 84.14 C ANISOU 3432 CA PRO A 330 7087 13305 11577 -732 -294 -57 C ATOM 3433 C PRO A 330 50.214 13.015 -1.676 1.00 84.53 C ANISOU 3433 C PRO A 330 7157 13402 11559 -642 -282 -127 C ATOM 3434 O PRO A 330 50.280 13.050 -2.904 1.00 85.21 O ANISOU 3434 O PRO A 330 7251 13564 11561 -664 -260 -117 O ATOM 3435 CB PRO A 330 51.657 14.769 -0.547 1.00 84.79 C ANISOU 3435 CB PRO A 330 7068 13500 11649 -758 -258 -60 C ATOM 3436 CG PRO A 330 51.635 15.139 0.912 1.00 84.16 C ANISOU 3436 CG PRO A 330 6991 13331 11655 -761 -294 -59 C ATOM 3437 CD PRO A 330 50.552 14.315 1.518 1.00 83.34 C ANISOU 3437 CD PRO A 330 6974 13098 11593 -685 -327 -90 C ATOM 3438 N ASP A 331 50.119 11.867 -0.968 1.00 87.13 N ANISOU 3438 N ASP A 331 7503 13682 11920 -540 -298 -198 N ATOM 3439 CA ASP A 331 50.074 10.519 -1.546 1.00 87.44 C ANISOU 3439 CA ASP A 331 7568 13744 11911 -443 -294 -274 C ATOM 3440 C ASP A 331 48.807 10.318 -2.387 1.00 87.31 C ANISOU 3440 C ASP A 331 7638 13650 11886 -455 -334 -262 C ATOM 3441 O ASP A 331 48.876 9.702 -3.452 1.00 87.96 O ANISOU 3441 O ASP A 331 7742 13792 11886 -423 -326 -302 O ATOM 3442 CB ASP A 331 50.160 9.455 -0.438 1.00 87.01 C ANISOU 3442 CB ASP A 331 7521 13627 11913 -340 -310 -338 C ATOM 3443 CG ASP A 331 51.089 8.301 -0.759 1.00 87.63 C ANISOU 3443 CG ASP A 331 7561 13798 11937 -240 -282 -423 C ATOM 3444 OD1 ASP A 331 50.759 7.507 -1.668 1.00 88.36 O ANISOU 3444 OD1 ASP A 331 7694 13901 11978 -197 -280 -467 O ATOM 3445 OD2 ASP A 331 52.130 8.172 -0.081 1.00 87.45 O ANISOU 3445 OD2 ASP A 331 7470 13831 11927 -200 -267 -450 O ATOM 3446 N PHE A 332 47.662 10.851 -1.911 1.00 88.70 N ANISOU 3446 N PHE A 332 7861 13691 12150 -500 -378 -207 N ATOM 3447 CA PHE A 332 46.373 10.780 -2.601 1.00 88.55 C ANISOU 3447 CA PHE A 332 7912 13581 12152 -519 -430 -186 C ATOM 3448 C PHE A 332 46.271 11.815 -3.723 1.00 89.04 C ANISOU 3448 C PHE A 332 7983 13698 12150 -613 -438 -117 C ATOM 3449 O PHE A 332 45.643 11.534 -4.744 1.00 89.43 O ANISOU 3449 O PHE A 332 8086 13737 12156 -614 -478 -120 O ATOM 3450 CB PHE A 332 45.207 10.946 -1.613 1.00 87.64 C ANISOU 3450 CB PHE A 332 7831 13297 12171 -526 -465 -153 C ATOM 3451 CG PHE A 332 44.662 9.652 -1.058 1.00 87.36 C ANISOU 3451 CG PHE A 332 7830 13166 12197 -434 -481 -214 C ATOM 3452 CD1 PHE A 332 45.089 9.169 0.173 1.00 87.05 C ANISOU 3452 CD1 PHE A 332 7779 13099 12196 -374 -453 -246 C ATOM 3453 CD2 PHE A 332 43.707 8.923 -1.759 1.00 87.52 C ANISOU 3453 CD2 PHE A 332 7898 13118 12238 -410 -531 -238 C ATOM 3454 CE1 PHE A 332 44.576 7.975 0.691 1.00 86.88 C ANISOU 3454 CE1 PHE A 332 7795 12983 12232 -291 -463 -295 C ATOM 3455 CE2 PHE A 332 43.199 7.727 -1.243 1.00 87.36 C ANISOU 3455 CE2 PHE A 332 7906 13001 12285 -330 -544 -291 C ATOM 3456 CZ PHE A 332 43.637 7.261 -0.022 1.00 87.02 C ANISOU 3456 CZ PHE A 332 7853 12932 12279 -272 -505 -316 C ATOM 3457 N ARG A 333 46.889 13.005 -3.531 1.00 90.98 N ANISOU 3457 N ARG A 333 8181 13998 12389 -691 -404 -54 N ATOM 3458 CA ARG A 333 46.904 14.116 -4.493 1.00 91.54 C ANISOU 3458 CA ARG A 333 8258 14120 12403 -788 -403 25 C ATOM 3459 C ARG A 333 47.509 13.722 -5.845 1.00 92.65 C ANISOU 3459 C ARG A 333 8410 14395 12398 -777 -372 -1 C ATOM 3460 O ARG A 333 47.000 14.148 -6.882 1.00 93.25 O ANISOU 3460 O ARG A 333 8541 14475 12415 -826 -401 47 O ATOM 3461 CB ARG A 333 47.639 15.331 -3.912 1.00 91.42 C ANISOU 3461 CB ARG A 333 8180 14140 12416 -867 -366 85 C ATOM 3462 CG ARG A 333 46.807 16.608 -3.931 1.00 91.55 C ANISOU 3462 CG ARG A 333 8226 14064 12495 -962 -404 182 C ATOM 3463 CD ARG A 333 47.661 17.860 -3.816 1.00 91.92 C ANISOU 3463 CD ARG A 333 8217 14172 12537 -1055 -365 246 C ATOM 3464 NE ARG A 333 48.287 17.998 -2.498 1.00 91.47 N ANISOU 3464 NE ARG A 333 8105 14101 12548 -1044 -346 219 N ATOM 3465 CZ ARG A 333 47.766 18.680 -1.482 1.00 90.74 C ANISOU 3465 CZ ARG A 333 8027 13891 12559 -1073 -372 247 C ATOM 3466 NH1 ARG A 333 46.598 19.297 -1.617 1.00 90.36 N ANISOU 3466 NH1 ARG A 333 8035 13725 12573 -1113 -413 306 N ATOM 3467 NH2 ARG A 333 48.408 18.749 -0.324 1.00 90.51 N ANISOU 3467 NH2 ARG A 333 7961 13857 12572 -1059 -360 216 N ATOM 3468 N ILE A 334 48.585 12.905 -5.829 1.00 94.28 N ANISOU 3468 N ILE A 334 8569 14709 12545 -707 -312 -76 N ATOM 3469 CA ILE A 334 49.262 12.404 -7.032 1.00 95.45 C ANISOU 3469 CA ILE A 334 8725 14989 12552 -679 -262 -116 C ATOM 3470 C ILE A 334 48.363 11.360 -7.726 1.00 95.58 C ANISOU 3470 C ILE A 334 8837 14950 12530 -613 -321 -175 C ATOM 3471 O ILE A 334 48.264 11.362 -8.956 1.00 96.48 O ANISOU 3471 O ILE A 334 9011 15120 12527 -628 -322 -171 O ATOM 3472 CB ILE A 334 50.694 11.866 -6.707 1.00 95.83 C ANISOU 3472 CB ILE A 334 8679 15159 12573 -619 -177 -180 C ATOM 3473 CG1 ILE A 334 51.571 12.963 -6.050 1.00 96.09 C ANISOU 3473 CG1 ILE A 334 8614 15242 12654 -695 -133 -119 C ATOM 3474 CG2 ILE A 334 51.390 11.295 -7.960 1.00 96.99 C ANISOU 3474 CG2 ILE A 334 8836 15440 12576 -578 -110 -230 C ATOM 3475 CD1 ILE A 334 52.746 12.453 -5.182 1.00 96.15 C ANISOU 3475 CD1 ILE A 334 8516 15314 12702 -633 -90 -179 C ATOM 3476 N ALA A 335 47.689 10.501 -6.928 1.00 95.78 N ANISOU 3476 N ALA A 335 8880 14859 12653 -545 -373 -228 N ATOM 3477 CA ALA A 335 46.782 9.451 -7.404 1.00 95.87 C ANISOU 3477 CA ALA A 335 8972 14793 12661 -483 -439 -288 C ATOM 3478 C ALA A 335 45.559 10.005 -8.144 1.00 96.00 C ANISOU 3478 C ALA A 335 9065 14729 12682 -550 -526 -226 C ATOM 3479 O ALA A 335 45.172 9.439 -9.168 1.00 96.83 O ANISOU 3479 O ALA A 335 9244 14841 12706 -525 -570 -265 O ATOM 3480 CB ALA A 335 46.345 8.566 -6.247 1.00 94.97 C ANISOU 3480 CB ALA A 335 8850 14562 12672 -411 -467 -338 C ATOM 3481 N PHE A 336 44.963 11.110 -7.640 1.00 96.45 N ANISOU 3481 N PHE A 336 9106 14707 12834 -630 -554 -134 N ATOM 3482 CA PHE A 336 43.803 11.752 -8.267 1.00 96.59 C ANISOU 3482 CA PHE A 336 9184 14640 12877 -694 -642 -64 C ATOM 3483 C PHE A 336 44.187 12.489 -9.553 1.00 97.68 C ANISOU 3483 C PHE A 336 9361 14887 12866 -758 -632 -11 C ATOM 3484 O PHE A 336 43.386 12.532 -10.488 1.00 98.26 O ANISOU 3484 O PHE A 336 9512 14924 12899 -779 -714 10 O ATOM 3485 CB PHE A 336 43.085 12.710 -7.293 1.00 95.66 C ANISOU 3485 CB PHE A 336 9033 14400 12913 -753 -665 16 C ATOM 3486 CG PHE A 336 42.428 12.088 -6.079 1.00 94.68 C ANISOU 3486 CG PHE A 336 8891 14143 12941 -700 -679 -19 C ATOM 3487 CD1 PHE A 336 41.537 11.027 -6.213 1.00 94.64 C ANISOU 3487 CD1 PHE A 336 8925 14045 12989 -641 -741 -74 C ATOM 3488 CD2 PHE A 336 42.631 12.619 -4.811 1.00 93.90 C ANISOU 3488 CD2 PHE A 336 8742 14001 12935 -714 -632 9 C ATOM 3489 CE1 PHE A 336 40.919 10.464 -5.092 1.00 93.85 C ANISOU 3489 CE1 PHE A 336 8809 13818 13032 -596 -742 -97 C ATOM 3490 CE2 PHE A 336 42.008 12.058 -3.691 1.00 93.12 C ANISOU 3490 CE2 PHE A 336 8639 13777 12965 -664 -635 -17 C ATOM 3491 CZ PHE A 336 41.154 10.988 -3.839 1.00 93.11 C ANISOU 3491 CZ PHE A 336 8672 13689 13017 -607 -684 -66 C ATOM 3492 N GLN A 337 45.408 13.064 -9.596 1.00 98.72 N ANISOU 3492 N GLN A 337 9440 15150 12919 -789 -534 12 N ATOM 3493 CA GLN A 337 45.939 13.804 -10.745 1.00 99.88 C ANISOU 3493 CA GLN A 337 9617 15412 12921 -853 -497 70 C ATOM 3494 C GLN A 337 46.205 12.907 -11.956 1.00101.05 C ANISOU 3494 C GLN A 337 9841 15650 12903 -797 -487 0 C ATOM 3495 O GLN A 337 45.836 13.277 -13.070 1.00101.96 O ANISOU 3495 O GLN A 337 10044 15784 12913 -838 -528 45 O ATOM 3496 CB GLN A 337 47.207 14.582 -10.362 1.00100.02 C ANISOU 3496 CB GLN A 337 9542 15538 12923 -900 -386 110 C ATOM 3497 CG GLN A 337 46.930 15.951 -9.761 1.00 99.78 C ANISOU 3497 CG GLN A 337 9477 15441 12994 -999 -403 217 C ATOM 3498 CD GLN A 337 48.209 16.690 -9.460 1.00100.24 C ANISOU 3498 CD GLN A 337 9444 15605 13037 -1051 -303 252 C ATOM 3499 OE1 GLN A 337 48.783 16.573 -8.373 1.00 99.67 O ANISOU 3499 OE1 GLN A 337 9289 15533 13048 -1028 -269 217 O ATOM 3500 NE2 GLN A 337 48.688 17.467 -10.421 1.00101.40 N ANISOU 3500 NE2 GLN A 337 9606 15843 13078 -1124 -256 323 N ATOM 3501 N GLU A 338 46.843 11.738 -11.739 1.00101.46 N ANISOU 3501 N GLU A 338 9867 15754 12929 -701 -435 -109 N ATOM 3502 CA GLU A 338 47.172 10.773 -12.796 1.00102.65 C ANISOU 3502 CA GLU A 338 10088 15987 12926 -632 -414 -195 C ATOM 3503 C GLU A 338 45.933 10.065 -13.353 1.00102.75 C ANISOU 3503 C GLU A 338 10212 15892 12936 -599 -544 -237 C ATOM 3504 O GLU A 338 45.924 9.693 -14.528 1.00103.91 O ANISOU 3504 O GLU A 338 10457 16093 12931 -579 -559 -272 O ATOM 3505 CB GLU A 338 48.207 9.744 -12.306 1.00102.82 C ANISOU 3505 CB GLU A 338 10040 16082 12945 -533 -325 -300 C ATOM 3506 CG GLU A 338 49.616 10.294 -12.125 1.00103.42 C ANISOU 3506 CG GLU A 338 10012 16299 12984 -557 -190 -274 C ATOM 3507 CD GLU A 338 50.386 10.661 -13.383 1.00105.06 C ANISOU 3507 CD GLU A 338 10251 16654 13013 -586 -97 -252 C ATOM 3508 OE1 GLU A 338 51.117 11.677 -13.348 1.00105.57 O ANISOU 3508 OE1 GLU A 338 10242 16800 13070 -660 -15 -175 O ATOM 3509 OE2 GLU A 338 50.278 9.929 -14.394 1.00105.94 O ANISOU 3509 OE2 GLU A 338 10463 16799 12990 -536 -103 -313 O ATOM 3510 N LEU A 339 44.898 9.879 -12.511 1.00100.39 N ANISOU 3510 N LEU A 339 9899 15438 12806 -593 -636 -234 N ATOM 3511 CA LEU A 339 43.642 9.221 -12.879 1.00100.40 C ANISOU 3511 CA LEU A 339 9983 15315 12850 -568 -769 -269 C ATOM 3512 C LEU A 339 42.741 10.137 -13.716 1.00100.97 C ANISOU 3512 C LEU A 339 10128 15341 12894 -652 -870 -177 C ATOM 3513 O LEU A 339 42.158 9.681 -14.701 1.00101.96 O ANISOU 3513 O LEU A 339 10356 15446 12939 -637 -962 -211 O ATOM 3514 CB LEU A 339 42.903 8.748 -11.617 1.00 99.06 C ANISOU 3514 CB LEU A 339 9757 14996 12885 -537 -813 -289 C ATOM 3515 CG LEU A 339 42.214 7.391 -11.712 1.00 99.05 C ANISOU 3515 CG LEU A 339 9806 14900 12928 -458 -892 -388 C ATOM 3516 CD1 LEU A 339 42.396 6.602 -10.434 1.00 98.00 C ANISOU 3516 CD1 LEU A 339 9603 14707 12925 -391 -847 -441 C ATOM 3517 CD2 LEU A 339 40.737 7.542 -12.042 1.00 99.09 C ANISOU 3517 CD2 LEU A 339 9862 14762 13026 -499 -1037 -350 C ATOM 3518 N LEU A 340 42.631 11.422 -13.322 1.00 99.82 N ANISOU 3518 N LEU A 340 9935 15176 12815 -738 -859 -63 N ATOM 3519 CA LEU A 340 41.809 12.432 -13.999 1.00100.33 C ANISOU 3519 CA LEU A 340 10058 15190 12873 -821 -952 40 C ATOM 3520 C LEU A 340 42.553 13.159 -15.129 1.00101.62 C ANISOU 3520 C LEU A 340 10282 15493 12836 -873 -900 97 C ATOM 3521 O LEU A 340 41.939 13.957 -15.844 1.00102.33 O ANISOU 3521 O LEU A 340 10438 15552 12890 -938 -981 184 O ATOM 3522 CB LEU A 340 41.261 13.454 -12.981 1.00 99.25 C ANISOU 3522 CB LEU A 340 9843 14947 12920 -884 -967 134 C ATOM 3523 CG LEU A 340 40.226 12.944 -11.980 1.00 98.03 C ANISOU 3523 CG LEU A 340 9645 14629 12973 -849 -1031 105 C ATOM 3524 CD1 LEU A 340 40.196 13.813 -10.741 1.00 97.04 C ANISOU 3524 CD1 LEU A 340 9431 14441 12998 -890 -980 171 C ATOM 3525 CD2 LEU A 340 38.843 12.857 -12.603 1.00 98.30 C ANISOU 3525 CD2 LEU A 340 9741 14540 13069 -860 -1186 123 C ATOM 3526 N CYS A 341 43.868 12.870 -15.292 1.00102.67 N ANISOU 3526 N CYS A 341 10390 15776 12843 -843 -763 51 N ATOM 3527 CA CYS A 341 44.783 13.458 -16.283 1.00103.95 C ANISOU 3527 CA CYS A 341 10595 16088 12813 -885 -672 98 C ATOM 3528 C CYS A 341 44.899 14.983 -16.115 1.00103.87 C ANISOU 3528 C CYS A 341 10543 16080 12843 -996 -646 239 C ATOM 3529 O CYS A 341 44.222 15.749 -16.809 1.00104.46 O ANISOU 3529 O CYS A 341 10697 16114 12879 -1060 -728 329 O ATOM 3530 CB CYS A 341 44.421 13.052 -17.713 1.00105.45 C ANISOU 3530 CB CYS A 341 10939 16309 12818 -867 -739 73 C ATOM 3531 SG CYS A 341 44.327 11.261 -17.977 1.00105.71 S ANISOU 3531 SG CYS A 341 11031 16334 12799 -738 -773 -101 S ATOM 3532 N LEU A 342 45.735 15.409 -15.149 1.00 99.02 N ANISOU 3532 N LEU A 342 9805 15502 12316 -1016 -542 256 N ATOM 3533 CA LEU A 342 45.967 16.818 -14.818 1.00 98.86 C ANISOU 3533 CA LEU A 342 9730 15478 12354 -1119 -508 378 C ATOM 3534 C LEU A 342 47.457 17.150 -14.872 1.00 99.41 C ANISOU 3534 C LEU A 342 9725 15703 12343 -1145 -349 391 C ATOM 3535 O LEU A 342 47.826 18.298 -15.108 1.00 99.61 O ANISOU 3535 O LEU A 342 9736 15764 12347 -1238 -305 497 O ATOM 3536 CB LEU A 342 45.401 17.150 -13.422 1.00 97.36 C ANISOU 3536 CB LEU A 342 9455 15154 12383 -1131 -554 393 C ATOM 3537 CG LEU A 342 43.880 17.063 -13.252 1.00 96.53 C ANISOU 3537 CG LEU A 342 9399 14881 12398 -1122 -700 403 C ATOM 3538 CD1 LEU A 342 43.515 16.624 -11.850 1.00 95.17 C ANISOU 3538 CD1 LEU A 342 9147 14603 12410 -1077 -709 353 C ATOM 3539 CD2 LEU A 342 43.205 18.385 -13.589 1.00 97.11 C ANISOU 3539 CD2 LEU A 342 9510 14883 12504 -1216 -771 533 C TER 3540 LEU A 342 HETATM 3541 C1 ERC A1201 16.744 6.627 14.839 1.00102.14 C ANISOU 3541 C1 ERC A1201 9251 11141 18416 -309 1242 751 C HETATM 3542 N1 ERC A1201 17.920 6.004 14.627 1.00101.26 N ANISOU 3542 N1 ERC A1201 9251 11164 18059 -293 1141 695 N HETATM 3543 O1 ERC A1201 16.123 6.418 15.904 1.00102.98 O ANISOU 3543 O1 ERC A1201 9373 11123 18631 -281 1456 798 O HETATM 3544 S1 ERC A1201 10.549 10.024 2.057 1.00107.77 S ANISOU 3544 S1 ERC A1201 8703 11656 20588 -785 -968 822 S HETATM 3545 C2 ERC A1201 16.202 7.506 13.893 1.00102.23 C ANISOU 3545 C2 ERC A1201 9130 11147 18565 -354 1116 759 C HETATM 3546 N2 ERC A1201 16.595 8.351 8.486 1.00101.42 N ANISOU 3546 N2 ERC A1201 8769 11331 18435 -525 195 658 N HETATM 3547 O2 ERC A1201 20.449 4.675 14.148 1.00 99.57 O ANISOU 3547 O2 ERC A1201 9256 11233 17343 -249 928 574 O HETATM 3548 C3 ERC A1201 16.870 7.769 12.695 1.00101.42 C ANISOU 3548 C3 ERC A1201 9019 11181 18335 -386 885 713 C HETATM 3549 O3 ERC A1201 19.433 8.718 9.313 1.00 99.15 O ANISOU 3549 O3 ERC A1201 8798 11363 17512 -469 266 575 O HETATM 3550 C4 ERC A1201 18.083 7.128 12.457 1.00100.53 C ANISOU 3550 C4 ERC A1201 9021 11210 17966 -371 792 654 C HETATM 3551 O4 ERC A1201 14.751 12.345 4.248 1.00102.93 O ANISOU 3551 O4 ERC A1201 8623 11529 18956 -693 -498 776 O HETATM 3552 C5 ERC A1201 18.615 6.204 13.495 1.00100.46 C ANISOU 3552 C5 ERC A1201 9138 11199 17833 -321 927 644 C HETATM 3553 O5 ERC A1201 12.068 12.466 4.982 1.00105.23 O ANISOU 3553 O5 ERC A1201 8605 11453 19924 -688 -364 880 O HETATM 3554 C6 ERC A1201 19.918 5.529 13.230 1.00 99.60 C ANISOU 3554 C6 ERC A1201 9141 11238 17464 -299 822 581 C HETATM 3555 C7 ERC A1201 20.594 5.781 12.034 1.00 98.93 C ANISOU 3555 C7 ERC A1201 9040 11291 17258 -328 618 531 C HETATM 3556 C8 ERC A1201 20.089 6.645 11.055 1.00 99.03 C ANISOU 3556 C8 ERC A1201 8944 11308 17375 -379 497 543 C HETATM 3557 C9 ERC A1201 18.886 7.343 11.217 1.00 99.75 C ANISOU 3557 C9 ERC A1201 8927 11265 17708 -401 567 602 C HETATM 3558 C10 ERC A1201 18.374 8.233 10.148 1.00 99.95 C ANISOU 3558 C10 ERC A1201 8841 11292 17843 -451 421 618 C HETATM 3559 C11 ERC A1201 17.377 7.449 9.306 1.00101.03 C ANISOU 3559 C11 ERC A1201 8843 11326 18217 -482 306 625 C HETATM 3560 C12 ERC A1201 15.312 7.912 7.979 1.00102.47 C ANISOU 3560 C12 ERC A1201 8746 11320 18867 -555 120 685 C HETATM 3561 C13 ERC A1201 15.234 7.998 6.461 1.00102.54 C ANISOU 3561 C13 ERC A1201 8700 11386 18875 -601 -144 662 C HETATM 3562 C14 ERC A1201 14.390 9.188 6.071 1.00103.18 C ANISOU 3562 C14 ERC A1201 8666 11400 19137 -629 -196 718 C HETATM 3563 C15 ERC A1201 13.043 9.243 6.434 1.00104.35 C ANISOU 3563 C15 ERC A1201 8662 11365 19622 -635 -120 775 C HETATM 3564 C16 ERC A1201 12.268 10.345 6.067 1.00105.02 C ANISOU 3564 C16 ERC A1201 8635 11384 19884 -655 -173 827 C HETATM 3565 C17 ERC A1201 12.838 11.387 5.332 1.00104.50 C ANISOU 3565 C17 ERC A1201 8619 11434 19652 -672 -307 825 C HETATM 3566 C18 ERC A1201 14.182 11.331 4.972 1.00103.35 C ANISOU 3566 C18 ERC A1201 8628 11472 19169 -672 -376 772 C HETATM 3567 C19 ERC A1201 14.959 10.232 5.341 1.00102.69 C ANISOU 3567 C19 ERC A1201 8646 11456 18915 -649 -321 716 C HETATM 3568 C20 ERC A1201 14.982 12.166 2.852 1.00102.88 C ANISOU 3568 C20 ERC A1201 8627 11607 18856 -729 -743 751 C HETATM 3569 C21 ERC A1201 11.626 12.627 3.636 1.00105.97 C ANISOU 3569 C21 ERC A1201 8620 11543 20101 -730 -622 890 C HETATM 3570 C22 ERC A1201 10.153 12.248 3.534 1.00107.53 C ANISOU 3570 C22 ERC A1201 8621 11550 20685 -742 -656 930 C HETATM 3571 C23 ERC A1201 9.965 10.735 3.561 1.00107.73 C ANISOU 3571 C23 ERC A1201 8626 11531 20776 -748 -664 889 C HETATM 3572 C1 CLR A1202 39.658 -2.701 -0.557 1.00115.50 C HETATM 3573 C2 CLR A1202 40.909 -2.876 -1.441 1.00115.50 C HETATM 3574 C3 CLR A1202 41.633 -4.185 -1.094 1.00115.50 C HETATM 3575 C4 CLR A1202 40.704 -5.385 -1.323 1.00115.50 C HETATM 3576 C5 CLR A1202 39.462 -5.165 -0.480 1.00115.50 C HETATM 3577 C6 CLR A1202 39.118 -6.071 0.390 1.00115.50 C HETATM 3578 C7 CLR A1202 37.909 -5.914 1.267 1.00115.50 C HETATM 3579 C8 CLR A1202 36.850 -5.088 0.523 1.00115.50 C HETATM 3580 C9 CLR A1202 37.451 -3.717 0.159 1.00115.50 C HETATM 3581 C10 CLR A1202 38.698 -3.891 -0.723 1.00115.50 C HETATM 3582 C11 CLR A1202 36.425 -2.815 -0.538 1.00115.50 C HETATM 3583 C12 CLR A1202 35.165 -2.651 0.335 1.00115.50 C HETATM 3584 C13 CLR A1202 34.565 -4.043 0.589 1.00115.50 C HETATM 3585 C14 CLR A1202 35.619 -4.863 1.393 1.00115.50 C HETATM 3586 C15 CLR A1202 34.827 -6.093 1.847 1.00115.50 C HETATM 3587 C16 CLR A1202 33.465 -5.470 2.267 1.00115.50 C HETATM 3588 C17 CLR A1202 33.311 -4.143 1.471 1.00115.50 C HETATM 3589 C18 CLR A1202 34.337 -4.770 -0.749 1.00115.50 C HETATM 3590 C19 CLR A1202 38.223 -3.917 -2.182 1.00115.50 C HETATM 3591 C20 CLR A1202 31.999 -4.122 0.667 1.00115.50 C HETATM 3592 C21 CLR A1202 31.884 -2.798 -0.099 1.00115.50 C HETATM 3593 C22 CLR A1202 30.809 -4.243 1.627 1.00115.50 C HETATM 3594 C23 CLR A1202 29.497 -4.230 0.837 1.00115.50 C HETATM 3595 C24 CLR A1202 28.313 -4.351 1.802 1.00115.50 C HETATM 3596 C25 CLR A1202 26.969 -4.340 1.056 1.00115.50 C HETATM 3597 C26 CLR A1202 27.163 -4.209 -0.459 1.00115.50 C HETATM 3598 C27 CLR A1202 26.203 -5.629 1.362 1.00115.50 C HETATM 3599 O1 CLR A1202 42.805 -4.337 -1.899 1.00115.50 O HETATM 3600 S SO4 A1203 49.758 0.847 7.689 1.00 82.96 S HETATM 3601 O1 SO4 A1203 50.187 -0.524 7.396 1.00 82.96 O HETATM 3602 O2 SO4 A1203 50.604 1.792 6.956 1.00 82.96 O HETATM 3603 O3 SO4 A1203 48.364 1.026 7.281 1.00 82.96 O HETATM 3604 O4 SO4 A1203 49.878 1.099 9.127 1.00 82.96 O HETATM 3605 S SO4 A1204 48.605 20.525 8.156 1.00133.14 S HETATM 3606 O1 SO4 A1204 48.459 19.094 8.422 1.00133.14 O HETATM 3607 O2 SO4 A1204 49.281 20.715 6.871 1.00133.14 O HETATM 3608 O3 SO4 A1204 47.284 21.153 8.110 1.00133.14 O HETATM 3609 O4 SO4 A1204 49.398 21.142 9.222 1.00133.14 O HETATM 3610 S SO4 A1205 50.730 -8.380 4.800 1.00 91.32 S HETATM 3611 O1 SO4 A1205 51.285 -8.275 3.447 1.00 91.32 O HETATM 3612 O2 SO4 A1205 50.364 -7.045 5.281 1.00 91.32 O HETATM 3613 O3 SO4 A1205 49.541 -9.236 4.776 1.00 91.32 O HETATM 3614 O4 SO4 A1205 51.730 -8.964 5.696 1.00 91.32 O HETATM 3615 S SO4 A1206 71.558 40.764 19.797 1.00 93.38 S HETATM 3616 O1 SO4 A1206 71.705 39.828 18.681 1.00 93.38 O HETATM 3617 O2 SO4 A1206 71.676 42.136 19.300 1.00 93.38 O HETATM 3618 O3 SO4 A1206 70.244 40.579 20.417 1.00 93.38 O HETATM 3619 O4 SO4 A1206 72.609 40.513 20.787 1.00 93.38 O HETATM 3620 S SO4 A1207 63.375 28.582 6.643 1.00 77.81 S HETATM 3621 O1 SO4 A1207 62.236 27.754 6.232 1.00 77.81 O HETATM 3622 O2 SO4 A1207 63.509 29.719 5.727 1.00 77.81 O HETATM 3623 O3 SO4 A1207 63.155 29.073 7.999 1.00 77.81 O HETATM 3624 O4 SO4 A1207 64.600 27.777 6.612 1.00 77.81 O HETATM 3625 S SO4 A1208 76.564 40.267 31.750 1.00 77.81 S HETATM 3626 O1 SO4 A1208 75.798 39.169 32.348 1.00 77.81 O HETATM 3627 O2 SO4 A1208 75.696 41.433 31.576 1.00 77.81 O HETATM 3628 O3 SO4 A1208 77.682 40.618 32.629 1.00 77.81 O HETATM 3629 O4 SO4 A1208 77.083 39.845 30.447 1.00 77.81 O CONECT 477 3544 CONECT 593 1279 CONECT 1225 1273 CONECT 1273 1225 CONECT 1279 593 CONECT 3541 3542 3543 3545 CONECT 3542 3541 3552 CONECT 3543 3541 CONECT 3544 477 3571 CONECT 3545 3541 3548 CONECT 3546 3559 3560 CONECT 3547 3554 CONECT 3548 3545 3550 CONECT 3549 3558 CONECT 3550 3548 3552 3557 CONECT 3551 3566 3568 CONECT 3552 3542 3550 3554 CONECT 3553 3565 3569 CONECT 3554 3547 3552 3555 CONECT 3555 3554 3556 CONECT 3556 3555 3557 CONECT 3557 3550 3556 3558 CONECT 3558 3549 3557 3559 CONECT 3559 3546 3558 CONECT 3560 3546 3561 CONECT 3561 3560 3562 CONECT 3562 3561 3563 3567 CONECT 3563 3562 3564 CONECT 3564 3563 3565 CONECT 3565 3553 3564 3566 CONECT 3566 3551 3565 3567 CONECT 3567 3562 3566 CONECT 3568 3551 CONECT 3569 3553 3570 CONECT 3570 3569 3571 CONECT 3571 3544 3570 CONECT 3572 3573 3581 CONECT 3573 3572 3574 CONECT 3574 3573 3575 3599 CONECT 3575 3574 3576 CONECT 3576 3575 3577 3581 CONECT 3577 3576 3578 CONECT 3578 3577 3579 CONECT 3579 3578 3580 3585 CONECT 3580 3579 3581 3582 CONECT 3581 3572 3576 3580 3590 CONECT 3582 3580 3583 CONECT 3583 3582 3584 CONECT 3584 3583 3585 3588 3589 CONECT 3585 3579 3584 3586 CONECT 3586 3585 3587 CONECT 3587 3586 3588 CONECT 3588 3584 3587 3591 CONECT 3589 3584 CONECT 3590 3581 CONECT 3591 3588 3592 3593 CONECT 3592 3591 CONECT 3593 3591 3594 CONECT 3594 3593 3595 CONECT 3595 3594 3596 CONECT 3596 3595 3597 3598 CONECT 3597 3596 CONECT 3598 3596 CONECT 3599 3574 CONECT 3600 3601 3602 3603 3604 CONECT 3601 3600 CONECT 3602 3600 CONECT 3603 3600 CONECT 3604 3600 CONECT 3605 3606 3607 3608 3609 CONECT 3606 3605 CONECT 3607 3605 CONECT 3608 3605 CONECT 3609 3605 CONECT 3610 3611 3612 3613 3614 CONECT 3611 3610 CONECT 3612 3610 CONECT 3613 3610 CONECT 3614 3610 CONECT 3615 3616 3617 3618 3619 CONECT 3616 3615 CONECT 3617 3615 CONECT 3618 3615 CONECT 3619 3615 CONECT 3620 3621 3622 3623 3624 CONECT 3621 3620 CONECT 3622 3620 CONECT 3623 3620 CONECT 3624 3620 CONECT 3625 3626 3627 3628 3629 CONECT 3626 3625 CONECT 3627 3625 CONECT 3628 3625 CONECT 3629 3625 MASTER 337 0 8 26 3 0 16 6 3628 1 94 36 END