HEADER MEMBRANE PROTEIN 12-JUL-19 6PS3 TITLE XFEL BETA2 AR STRUCTURE BY LIGAND EXCHANGE FROM TIMOLOL TO CARVEDILOL. COMPND MOL_ID: 1; COMPND 2 MOLECULE: FUSION PROTEIN OF BETA-2 ADRENERGIC RECEPTOR AND T4 COMPND 3 LYSOZYME; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: BETA-2 ADRENORECEPTOR,BETA-2 ADRENOCEPTOR,LYSIS PROTEIN, COMPND 6 LYSOZYME,MURAMIDASE; COMPND 7 ENGINEERED: 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, E, T4TP126; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS KEYWDS GPCR, COMPLEX-LCP METHOD, SBDD, DRUG DESIGN, XFEL, LCP-SFX, LIGAND KEYWDS 2 EXCHANGE, TIMOLOL, CAVEDILOL, B2AR, BETA2AR, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR A.ISHCHENKO,B.STAUCH,G.W.HAN,A.BATYUK,A.SHIRIAEVA,C.LI,N.A.ZATSEPIN, AUTHOR 2 U.WEIERSTALL,W.LIU,E.NANGO,T.NAKANE,R.TANAKA,K.TONO,Y.JOTI,S.IWATA, AUTHOR 3 I.MORAES,C.GATI,C.CHEREZOV REVDAT 3 01-JAN-20 6PS3 1 REMARK REVDAT 2 25-DEC-19 6PS3 1 JRNL REVDAT 1 13-NOV-19 6PS3 0 JRNL AUTH A.ISHCHENKO,B.STAUCH,G.W.HAN,A.BATYUK,A.SHIRIAEVA,C.LI, JRNL AUTH 2 N.ZATSEPIN,U.WEIERSTALL,W.LIU,E.NANGO,T.NAKANE,R.TANAKA, JRNL AUTH 3 K.TONO,Y.JOTI,S.IWATA,I.MORAES,C.GATI,V.CHEREZOV JRNL TITL TOWARD G PROTEIN-COUPLED RECEPTOR STRUCTURE-BASED DRUG JRNL TITL 2 DESIGN USING X-RAY LASERS. JRNL REF IUCRJ V. 6 1106 2019 JRNL REFN ESSN 2052-2525 JRNL PMID 31709066 JRNL DOI 10.1107/S2052252519013137 REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.10.2 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) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.40 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9 REMARK 3 NUMBER OF REFLECTIONS : 20415 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) : 0.205 REMARK 3 R VALUE (WORKING SET) : 0.203 REMARK 3 FREE R VALUE : 0.242 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010 REMARK 3 FREE R VALUE TEST SET COUNT : 1022 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 10 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.63 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.25 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2706 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2450 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2571 REMARK 3 BIN R VALUE (WORKING SET) : 0.2450 REMARK 3 BIN FREE R VALUE : 0.2510 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.99 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 135 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3459 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 203 REMARK 3 SOLVENT ATOMS : 13 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 95.64 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -12.26750 REMARK 3 B22 (A**2) : 8.24670 REMARK 3 B33 (A**2) : 4.02080 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) : 0.410 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.412 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.254 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.414 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.258 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 : 0.947 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3783 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 5136 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1730 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 62 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 553 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3783 ; 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 : 503 ; 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 : 4212 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.06 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.38 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.04 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|* } REMARK 3 ORIGIN FOR THE GROUP (A): 8.3717 2.9314 25.9283 REMARK 3 T TENSOR REMARK 3 T11: -0.0266 T22: -0.2243 REMARK 3 T33: -0.2482 T12: 0.0089 REMARK 3 T13: 0.0072 T23: 0.0135 REMARK 3 L TENSOR REMARK 3 L11: 0.5629 L22: 0.5252 REMARK 3 L33: 2.6017 L12: -0.2577 REMARK 3 L13: -0.8057 L23: 0.5148 REMARK 3 S TENSOR REMARK 3 S11: 0.0761 S12: -0.0024 S13: 0.0387 REMARK 3 S21: 0.0828 S22: -0.0304 S23: -0.0423 REMARK 3 S31: -0.3599 S32: 0.0447 S33: -0.0457 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6PS3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-19. REMARK 100 THE DEPOSITION ID IS D_1000242974. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-MAY-15 REMARK 200 TEMPERATURE (KELVIN) : 293 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : FREE ELECTRON LASER REMARK 200 BEAMLINE : BL3 REMARK 200 X-RAY GENERATOR MODEL : SACLA BEAMLINE BL3 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.76 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MPCCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL REMARK 200 DATA SCALING SOFTWARE : CRYSTFEL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20630 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 46.400 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 253.3 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.63 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 3D4S REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.38 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.0, 0.1 M AMMONIUM REMARK 280 SULFATE, 30% PEG 400, 2 MM OF TARGET LIGAND CARVEDILOL, LIPIDIC REMARK 280 CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 21.27500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 86.92500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.72000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 86.92500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.27500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.72000 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 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN 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 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 MET A -23 REMARK 465 LYS A -22 REMARK 465 THR A -21 REMARK 465 ILE A -20 REMARK 465 ILE A -19 REMARK 465 ALA A -18 REMARK 465 LEU A -17 REMARK 465 SER A -16 REMARK 465 TYR A -15 REMARK 465 ILE A -14 REMARK 465 PHE A -13 REMARK 465 CYS A -12 REMARK 465 LEU A -11 REMARK 465 VAL A -10 REMARK 465 PHE A -9 REMARK 465 ALA A -8 REMARK 465 ASP A -7 REMARK 465 TYR A -6 REMARK 465 LYS A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 ASP A -2 REMARK 465 ASP A -1 REMARK 465 ALA A 0 REMARK 465 MET A 1 REMARK 465 GLY A 2 REMARK 465 GLN A 3 REMARK 465 PRO A 4 REMARK 465 GLY A 5 REMARK 465 ASN A 6 REMARK 465 GLY A 7 REMARK 465 SER A 8 REMARK 465 ALA A 9 REMARK 465 PHE A 10 REMARK 465 LEU A 11 REMARK 465 LEU A 12 REMARK 465 ALA A 13 REMARK 465 PRO A 14 REMARK 465 ASN A 15 REMARK 465 ARG A 16 REMARK 465 SER A 17 REMARK 465 HIS A 18 REMARK 465 ALA A 19 REMARK 465 PRO A 20 REMARK 465 ASP A 21 REMARK 465 HIS A 22 REMARK 465 ASP A 23 REMARK 465 VAL A 24 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 LYS A 147 CE NZ REMARK 470 GLU A 180 CG CD OE1 OE2 REMARK 470 LYS A 227 CD CE NZ REMARK 470 ARG A1014 CG CD NE CZ NH1 NH2 REMARK 470 LYS A1016 CG CD CE NZ REMARK 470 ILE A1017 CD1 REMARK 470 LYS A1019 CG CD CE NZ REMARK 470 GLU A1022 CG CD OE1 OE2 REMARK 470 TYR A1024 CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS A1043 CD CE NZ REMARK 470 LYS A1048 CD CE NZ REMARK 470 ASN A1053 CG OD1 ND2 REMARK 470 ASN A1055 CG OD1 ND2 REMARK 470 LYS A1060 CG CD CE NZ REMARK 470 ASP A1061 CG OD1 OD2 REMARK 470 LYS A1065 CG CD CE NZ REMARK 470 GLN A1069 CD OE1 NE2 REMARK 470 LYS A1083 CD CE NZ REMARK 470 ASN A1144 CG OD1 ND2 REMARK 470 LYS A 267 CG CD CE NZ REMARK 470 GLN A 299 CG CD OE1 NE2 REMARK 470 ASN A 301 CG OD1 ND2 REMARK 470 LEU A 302 CG CD1 CD2 REMARK 470 ILE A 303 CG1 CG2 CD1 REMARK 470 ARG A 304 CD NE CZ NH1 NH2 REMARK 470 LYS A 305 CG CD CE NZ 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 VAL A 86 -61.60 -109.82 REMARK 500 LYS A 140 -56.20 59.59 REMARK 500 PHE A 208 -59.07 -123.06 REMARK 500 ASP A1020 -153.81 -82.86 REMARK 500 ARG A1125 71.30 -109.92 REMARK 500 LYS A1135 47.66 -96.75 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLC A 1207 REMARK 610 OLC A 1208 REMARK 610 OLC A 1209 REMARK 610 OLC A 1210 REMARK 610 OLC A 1211 REMARK 610 OLC A 1212 REMARK 610 OLA A 1213 REMARK 610 OLA A 1214 REMARK 610 OLA A 1215 REMARK 610 OLA A 1216 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CVD A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 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 CLR A 1206 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1207 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1208 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1209 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1210 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1211 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1212 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1213 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1214 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1215 DBREF 6PS3 A 1 230 UNP P07550 ADRB2_HUMAN 1 230 DBREF 6PS3 A 1002 1161 UNP D9IEF7 D9IEF7_BPT4 2 161 DBREF 6PS3 A 263 348 UNP P07550 ADRB2_HUMAN 263 348 SEQADV 6PS3 MET A -23 UNP P07550 INITIATING METHIONINE SEQADV 6PS3 LYS A -22 UNP P07550 EXPRESSION TAG SEQADV 6PS3 THR A -21 UNP P07550 EXPRESSION TAG SEQADV 6PS3 ILE A -20 UNP P07550 EXPRESSION TAG SEQADV 6PS3 ILE A -19 UNP P07550 EXPRESSION TAG SEQADV 6PS3 ALA A -18 UNP P07550 EXPRESSION TAG SEQADV 6PS3 LEU A -17 UNP P07550 EXPRESSION TAG SEQADV 6PS3 SER A -16 UNP P07550 EXPRESSION TAG SEQADV 6PS3 TYR A -15 UNP P07550 EXPRESSION TAG SEQADV 6PS3 ILE A -14 UNP P07550 EXPRESSION TAG SEQADV 6PS3 PHE A -13 UNP P07550 EXPRESSION TAG SEQADV 6PS3 CYS A -12 UNP P07550 EXPRESSION TAG SEQADV 6PS3 LEU A -11 UNP P07550 EXPRESSION TAG SEQADV 6PS3 VAL A -10 UNP P07550 EXPRESSION TAG SEQADV 6PS3 PHE A -9 UNP P07550 EXPRESSION TAG SEQADV 6PS3 ALA A -8 UNP P07550 EXPRESSION TAG SEQADV 6PS3 ASP A -7 UNP P07550 EXPRESSION TAG SEQADV 6PS3 TYR A -6 UNP P07550 EXPRESSION TAG SEQADV 6PS3 LYS A -5 UNP P07550 EXPRESSION TAG SEQADV 6PS3 ASP A -4 UNP P07550 EXPRESSION TAG SEQADV 6PS3 ASP A -3 UNP P07550 EXPRESSION TAG SEQADV 6PS3 ASP A -2 UNP P07550 EXPRESSION TAG SEQADV 6PS3 ASP A -1 UNP P07550 EXPRESSION TAG SEQADV 6PS3 ALA A 0 UNP P07550 EXPRESSION TAG SEQADV 6PS3 ARG A 16 UNP P07550 GLY 16 VARIANT SEQADV 6PS3 GLN A 27 UNP P07550 GLU 27 VARIANT SEQADV 6PS3 TRP A 122 UNP P07550 GLU 122 ENGINEERED MUTATION SEQADV 6PS3 GLU A 187 UNP P07550 ASN 187 ENGINEERED MUTATION SEQADV 6PS3 THR A 1054 UNP D9IEF7 CYS 54 ENGINEERED MUTATION SEQADV 6PS3 ALA A 1097 UNP D9IEF7 CYS 97 ENGINEERED MUTATION SEQADV 6PS3 HIS A 349 UNP P07550 EXPRESSION TAG SEQADV 6PS3 HIS A 350 UNP P07550 EXPRESSION TAG SEQADV 6PS3 HIS A 351 UNP P07550 EXPRESSION TAG SEQADV 6PS3 HIS A 352 UNP P07550 EXPRESSION TAG SEQADV 6PS3 HIS A 353 UNP P07550 EXPRESSION TAG SEQADV 6PS3 HIS A 354 UNP P07550 EXPRESSION TAG SEQRES 1 A 506 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 A 506 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP ALA MET GLY SEQRES 3 A 506 GLN PRO GLY ASN GLY SER ALA PHE LEU LEU ALA PRO ASN SEQRES 4 A 506 ARG SER HIS ALA PRO ASP HIS ASP VAL THR GLN GLN ARG SEQRES 5 A 506 ASP GLU VAL TRP VAL VAL GLY MET GLY ILE VAL MET SER SEQRES 6 A 506 LEU ILE VAL LEU ALA ILE VAL PHE GLY ASN VAL LEU VAL SEQRES 7 A 506 ILE THR ALA ILE ALA LYS PHE GLU ARG LEU GLN THR VAL SEQRES 8 A 506 THR ASN TYR PHE ILE THR SER LEU ALA CYS ALA ASP LEU SEQRES 9 A 506 VAL MET GLY LEU ALA VAL VAL PRO PHE GLY ALA ALA HIS SEQRES 10 A 506 ILE LEU MET LYS MET TRP THR PHE GLY ASN PHE TRP CYS SEQRES 11 A 506 GLU PHE TRP THR SER ILE ASP VAL LEU CYS VAL THR ALA SEQRES 12 A 506 SER ILE TRP THR LEU CYS VAL ILE ALA VAL ASP ARG TYR SEQRES 13 A 506 PHE ALA ILE THR SER PRO PHE LYS TYR GLN SER LEU LEU SEQRES 14 A 506 THR LYS ASN LYS ALA ARG VAL ILE ILE LEU MET VAL TRP SEQRES 15 A 506 ILE VAL SER GLY LEU THR SER PHE LEU PRO ILE GLN MET SEQRES 16 A 506 HIS TRP TYR ARG ALA THR HIS GLN GLU ALA ILE ASN CYS SEQRES 17 A 506 TYR ALA GLU GLU THR CYS CYS ASP PHE PHE THR ASN GLN SEQRES 18 A 506 ALA TYR ALA ILE ALA SER SER ILE VAL SER PHE TYR VAL SEQRES 19 A 506 PRO LEU VAL ILE MET VAL PHE VAL TYR SER ARG VAL PHE SEQRES 20 A 506 GLN GLU ALA LYS ARG GLN LEU ASN ILE PHE GLU MET LEU SEQRES 21 A 506 ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP SEQRES 22 A 506 THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU SEQRES 23 A 506 THR LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU SEQRES 24 A 506 ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR SEQRES 25 A 506 LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP SEQRES 26 A 506 ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS SEQRES 27 A 506 PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA SEQRES 28 A 506 LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL SEQRES 29 A 506 ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS SEQRES 30 A 506 ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG SEQRES 31 A 506 TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE SEQRES 32 A 506 THR THR PHE ARG THR GLY THR TRP ASP ALA TYR LYS PHE SEQRES 33 A 506 CYS LEU LYS GLU HIS LYS ALA LEU LYS THR LEU GLY ILE SEQRES 34 A 506 ILE MET GLY THR PHE THR LEU CYS TRP LEU PRO PHE PHE SEQRES 35 A 506 ILE VAL ASN ILE VAL HIS VAL ILE GLN ASP ASN LEU ILE SEQRES 36 A 506 ARG LYS GLU VAL TYR ILE LEU LEU ASN TRP ILE GLY TYR SEQRES 37 A 506 VAL ASN SER GLY PHE ASN PRO LEU ILE TYR CYS ARG SER SEQRES 38 A 506 PRO ASP PHE ARG ILE ALA PHE GLN GLU LEU LEU CYS LEU SEQRES 39 A 506 ARG ARG SER SER LEU LYS HIS HIS HIS HIS HIS HIS HET CVD A1201 30 HET SO4 A1202 5 HET SO4 A1203 5 HET SO4 A1204 5 HET SO4 A1205 5 HET CLR A1206 28 HET OLC A1207 16 HET OLC A1208 18 HET OLC A1209 12 HET OLC A1210 13 HET OLC A1211 10 HET OLC A1212 5 HET OLA A1213 14 HET OLA A1214 10 HET OLA A1215 13 HET OLA A1216 14 HETNAM CVD (2S)-1-(8H-CARBAZOL-4-YLOXY)-3-[2-(2-METHOXYPHENOXY) HETNAM 2 CVD ETHYLAMINO]PROPAN-2-OL HETNAM SO4 SULFATE ION HETNAM CLR CHOLESTEROL HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM OLA OLEIC ACID HETSYN CVD CARVEDILOL HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 CVD C24 H26 N2 O4 FORMUL 3 SO4 4(O4 S 2-) FORMUL 7 CLR C27 H46 O FORMUL 8 OLC 6(C21 H40 O4) FORMUL 14 OLA 4(C18 H34 O2) FORMUL 18 HOH *13(H2 O) HELIX 1 AA1 ASP A 29 PHE A 61 1 33 HELIX 2 AA2 GLU A 62 GLN A 65 5 4 HELIX 3 AA3 THR A 66 VAL A 86 1 21 HELIX 4 AA4 VAL A 86 LYS A 97 1 12 HELIX 5 AA5 PHE A 101 THR A 136 1 36 HELIX 6 AA6 THR A 146 MET A 171 1 26 HELIX 7 AA7 HIS A 178 GLU A 187 1 10 HELIX 8 AA8 ASN A 196 PHE A 208 1 13 HELIX 9 AA9 PHE A 208 GLN A 229 1 22 HELIX 10 AB1 ASN A 1002 GLY A 1012 1 11 HELIX 11 AB2 SER A 1038 GLY A 1051 1 14 HELIX 12 AB3 THR A 1059 ASN A 1081 1 23 HELIX 13 AB4 LEU A 1084 SER A 1090 1 7 HELIX 14 AB5 ASP A 1092 ALA A 1112 1 21 HELIX 15 AB6 PHE A 1114 GLN A 1123 1 10 HELIX 16 AB7 ARG A 1125 LYS A 1135 1 11 HELIX 17 AB8 SER A 1136 THR A 1142 1 7 HELIX 18 AB9 THR A 1142 GLY A 1156 1 15 HELIX 19 AC1 TRP A 1158 LYS A 263 5 5 HELIX 20 AC2 LEU A 266 GLN A 299 1 34 HELIX 21 AC3 ARG A 304 ASN A 318 1 15 HELIX 22 AC4 PHE A 321 TYR A 326 1 6 HELIX 23 AC5 SER A 329 LEU A 340 1 12 SHEET 1 AA1 3 ARG A1014 LYS A1019 0 SHEET 2 AA1 3 TYR A1025 GLY A1028 -1 O THR A1026 N TYR A1018 SHEET 3 AA1 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 2.03 SITE 1 AC1 12 HIS A 93 ILE A 94 ASP A 113 TYR A 199 SITE 2 AC1 12 SER A 203 SER A 207 PHE A 289 PHE A 290 SITE 3 AC1 12 ASN A 293 TYR A 308 ASN A 312 TYR A 316 SITE 1 AC2 5 THR A 66 VAL A 67 THR A 68 ARG A 131 SITE 2 AC2 5 SER A 143 SITE 1 AC3 3 LYS A 270 LYS A 273 ARG A 328 SITE 1 AC4 4 PHE A1114 THR A1115 ASN A1116 SER A1117 SITE 1 AC5 4 THR A1142 PRO A1143 ASN A1144 ARG A1145 SITE 1 AC6 5 THR A 73 CYS A 77 ARG A 151 TRP A 158 SITE 2 AC6 5 OLC A1207 SITE 1 AC7 3 ILE A 55 GLN A 65 CLR A1206 SITE 1 AC8 1 SER A 41 SITE 1 AC9 3 GLN A 197 LEU A 339 OLA A1213 SITE 1 AD1 3 TRP A 173 LEU A 340 LEU A 342 SITE 1 AD2 2 VAL A 126 PHE A 133 SITE 1 AD3 1 TRP A 122 SITE 1 AD4 1 OLC A1209 SITE 1 AD5 3 THR A 100 PHE A 217 VAL A 218 SITE 1 AD6 1 VAL A 216 CRYST1 42.550 77.440 173.850 90.00 90.00 90.00 P 21 21 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.023502 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012913 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005752 0.00000 ATOM 1 N ASP A 29 16.933 22.570 62.636 1.00162.35 N ANISOU 1 N ASP A 29 24268 20410 17006 -2835 237 -2155 N ATOM 2 CA ASP A 29 17.658 23.792 62.287 1.00164.36 C ANISOU 2 CA ASP A 29 24654 20605 17189 -3162 349 -2321 C ATOM 3 C ASP A 29 16.785 24.741 61.444 1.00167.11 C ANISOU 3 C ASP A 29 25316 20567 17611 -3166 521 -2261 C ATOM 4 O ASP A 29 15.837 24.292 60.796 1.00164.63 O ANISOU 4 O ASP A 29 25036 20093 17424 -2924 530 -2090 O ATOM 5 CB ASP A 29 18.961 23.450 61.543 1.00167.22 C ANISOU 5 CB ASP A 29 24768 21220 17547 -3326 290 -2401 C ATOM 6 CG ASP A 29 19.961 24.592 61.506 1.00182.15 C ANISOU 6 CG ASP A 29 26735 23152 19320 -3710 383 -2617 C ATOM 7 OD1 ASP A 29 19.912 25.392 60.546 1.00183.31 O ANISOU 7 OD1 ASP A 29 27067 23072 19511 -3850 523 -2631 O ATOM 8 OD2 ASP A 29 20.778 24.697 62.448 1.00190.24 O ANISOU 8 OD2 ASP A 29 27643 24437 20202 -3872 323 -2777 O ATOM 9 N GLU A 30 17.124 26.052 61.450 1.00165.02 N ANISOU 9 N GLU A 30 25285 20161 17256 -3442 662 -2407 N ATOM 10 CA GLU A 30 16.396 27.119 60.752 1.00164.72 C ANISOU 10 CA GLU A 30 25588 19748 17248 -3466 845 -2373 C ATOM 11 C GLU A 30 16.767 27.271 59.259 1.00167.26 C ANISOU 11 C GLU A 30 25915 19985 17652 -3547 912 -2346 C ATOM 12 O GLU A 30 15.950 27.797 58.501 1.00166.45 O ANISOU 12 O GLU A 30 26051 19584 17608 -3447 1033 -2251 O ATOM 13 CB GLU A 30 16.584 28.462 61.472 1.00168.62 C ANISOU 13 CB GLU A 30 26366 20106 17595 -3726 983 -2543 C ATOM 14 CG GLU A 30 15.740 28.585 62.732 1.00179.57 C ANISOU 14 CG GLU A 30 27880 21426 18924 -3584 976 -2525 C ATOM 15 CD GLU A 30 15.908 29.854 63.548 1.00201.62 C ANISOU 15 CD GLU A 30 30952 24092 21561 -3832 1107 -2697 C ATOM 16 OE1 GLU A 30 16.074 30.939 62.945 1.00198.04 O ANISOU 16 OE1 GLU A 30 30762 23411 21071 -4032 1277 -2772 O ATOM 17 OE2 GLU A 30 15.817 29.768 64.794 1.00194.27 O ANISOU 17 OE2 GLU A 30 29998 23273 20544 -3814 1048 -2752 O ATOM 18 N VAL A 31 17.968 26.834 58.831 1.00163.14 N ANISOU 18 N VAL A 31 25136 19726 17125 -3715 838 -2427 N ATOM 19 CA VAL A 31 18.347 26.936 57.414 1.00162.10 C ANISOU 19 CA VAL A 31 24998 19526 17068 -3792 900 -2401 C ATOM 20 C VAL A 31 17.914 25.656 56.667 1.00162.55 C ANISOU 20 C VAL A 31 24831 19654 17277 -3490 780 -2211 C ATOM 21 O VAL A 31 17.703 25.695 55.454 1.00161.25 O ANISOU 21 O VAL A 31 24720 19345 17204 -3440 840 -2126 O ATOM 22 CB VAL A 31 19.846 27.276 57.199 1.00167.82 C ANISOU 22 CB VAL A 31 25592 20467 17704 -4155 914 -2596 C ATOM 23 CG1 VAL A 31 20.752 26.053 57.342 1.00167.05 C ANISOU 23 CG1 VAL A 31 25075 20783 17615 -4119 722 -2614 C ATOM 24 CG2 VAL A 31 20.065 27.965 55.853 1.00168.07 C ANISOU 24 CG2 VAL A 31 25787 20296 17775 -4304 1064 -2601 C ATOM 25 N TRP A 32 17.761 24.544 57.402 1.00157.52 N ANISOU 25 N TRP A 32 23963 19229 16660 -3291 622 -2147 N ATOM 26 CA TRP A 32 17.350 23.256 56.857 1.00154.99 C ANISOU 26 CA TRP A 32 23434 18986 16468 -3011 509 -1977 C ATOM 27 C TRP A 32 15.856 23.258 56.494 1.00153.62 C ANISOU 27 C TRP A 32 23448 18525 16396 -2746 569 -1806 C ATOM 28 O TRP A 32 15.498 22.709 55.452 1.00151.92 O ANISOU 28 O TRP A 32 23169 18257 16297 -2597 558 -1684 O ATOM 29 CB TRP A 32 17.667 22.132 57.862 1.00154.24 C ANISOU 29 CB TRP A 32 23073 19193 16338 -2891 339 -1972 C ATOM 30 CG TRP A 32 17.082 20.793 57.510 1.00153.54 C ANISOU 30 CG TRP A 32 22816 19152 16371 -2587 237 -1793 C ATOM 31 CD1 TRP A 32 17.592 19.878 56.635 1.00155.69 C ANISOU 31 CD1 TRP A 32 22866 19571 16720 -2524 161 -1736 C ATOM 32 CD2 TRP A 32 15.871 20.222 58.030 1.00152.24 C ANISOU 32 CD2 TRP A 32 22701 18886 16258 -2317 211 -1656 C ATOM 33 NE1 TRP A 32 16.785 18.762 56.593 1.00153.46 N ANISOU 33 NE1 TRP A 32 22500 19278 16531 -2237 91 -1574 N ATOM 34 CE2 TRP A 32 15.713 18.953 57.428 1.00154.69 C ANISOU 34 CE2 TRP A 32 22817 19283 16675 -2112 122 -1524 C ATOM 35 CE3 TRP A 32 14.897 20.665 58.946 1.00153.64 C ANISOU 35 CE3 TRP A 32 23072 18907 16398 -2233 260 -1637 C ATOM 36 CZ2 TRP A 32 14.621 18.119 57.712 1.00152.55 C ANISOU 36 CZ2 TRP A 32 22541 18949 16473 -1845 88 -1381 C ATOM 37 CZ3 TRP A 32 13.820 19.838 59.228 1.00153.65 C ANISOU 37 CZ3 TRP A 32 23053 18857 16468 -1961 221 -1492 C ATOM 38 CH2 TRP A 32 13.689 18.581 58.618 1.00152.73 C ANISOU 38 CH2 TRP A 32 22744 18830 16456 -1778 139 -1369 C ATOM 39 N VAL A 33 14.995 23.860 57.351 1.00147.18 N ANISOU 39 N VAL A 33 22852 17542 15529 -2685 633 -1804 N ATOM 40 CA VAL A 33 13.536 23.914 57.168 1.00143.99 C ANISOU 40 CA VAL A 33 22619 16893 15197 -2428 691 -1657 C ATOM 41 C VAL A 33 13.152 24.782 55.931 1.00144.61 C ANISOU 41 C VAL A 33 22929 16700 15317 -2444 838 -1619 C ATOM 42 O VAL A 33 12.250 24.396 55.177 1.00143.24 O ANISOU 42 O VAL A 33 22760 16419 15243 -2217 844 -1475 O ATOM 43 CB VAL A 33 12.799 24.356 58.468 1.00148.03 C ANISOU 43 CB VAL A 33 23298 17319 15627 -2366 721 -1678 C ATOM 44 CG1 VAL A 33 13.170 25.773 58.903 1.00150.00 C ANISOU 44 CG1 VAL A 33 23815 17430 15747 -2619 853 -1831 C ATOM 45 CG2 VAL A 33 11.286 24.189 58.353 1.00146.32 C ANISOU 45 CG2 VAL A 33 23195 16916 15485 -2071 757 -1522 C ATOM 46 N VAL A 34 13.848 25.914 55.710 1.00139.31 N ANISOU 46 N VAL A 34 22442 15928 14562 -2713 957 -1748 N ATOM 47 CA VAL A 34 13.579 26.805 54.579 1.00137.76 C ANISOU 47 CA VAL A 34 22495 15466 14382 -2742 1111 -1720 C ATOM 48 C VAL A 34 14.129 26.177 53.295 1.00137.32 C ANISOU 48 C VAL A 34 22246 15506 14422 -2749 1066 -1670 C ATOM 49 O VAL A 34 13.419 26.139 52.290 1.00135.60 O ANISOU 49 O VAL A 34 22103 15135 14284 -2574 1111 -1547 O ATOM 50 CB VAL A 34 14.132 28.233 54.804 1.00143.86 C ANISOU 50 CB VAL A 34 23560 16078 15022 -3039 1274 -1879 C ATOM 51 CG1 VAL A 34 13.685 29.178 53.691 1.00144.07 C ANISOU 51 CG1 VAL A 34 23898 15790 15053 -3022 1450 -1830 C ATOM 52 CG2 VAL A 34 13.711 28.778 56.167 1.00144.69 C ANISOU 52 CG2 VAL A 34 23831 16122 15023 -3051 1306 -1945 C ATOM 53 N GLY A 35 15.370 25.684 53.361 1.00132.09 N ANISOU 53 N GLY A 35 21334 15110 13744 -2940 975 -1767 N ATOM 54 CA GLY A 35 16.068 25.030 52.256 1.00130.24 C ANISOU 54 CA GLY A 35 20886 15012 13589 -2970 921 -1740 C ATOM 55 C GLY A 35 15.348 23.819 51.691 1.00129.61 C ANISOU 55 C GLY A 35 20621 14980 13644 -2663 815 -1564 C ATOM 56 O GLY A 35 15.339 23.620 50.473 1.00128.40 O ANISOU 56 O GLY A 35 20439 14777 13571 -2614 834 -1493 O ATOM 57 N MET A 36 14.733 23.004 52.571 1.00123.58 N ANISOU 57 N MET A 36 19740 14312 12902 -2464 708 -1497 N ATOM 58 CA MET A 36 13.963 21.837 52.164 1.00120.44 C ANISOU 58 CA MET A 36 19185 13954 12624 -2182 619 -1339 C ATOM 59 C MET A 36 12.530 22.234 51.826 1.00120.40 C ANISOU 59 C MET A 36 19395 13690 12662 -1971 707 -1225 C ATOM 60 O MET A 36 11.889 21.543 51.038 1.00118.42 O ANISOU 60 O MET A 36 19061 13421 12513 -1776 676 -1103 O ATOM 61 CB MET A 36 13.999 20.732 53.214 1.00122.55 C ANISOU 61 CB MET A 36 19233 14444 12888 -2071 476 -1321 C ATOM 62 CG MET A 36 15.028 19.689 52.896 1.00126.48 C ANISOU 62 CG MET A 36 19434 15207 13414 -2102 355 -1331 C ATOM 63 SD MET A 36 14.984 18.298 54.038 1.00130.79 S ANISOU 63 SD MET A 36 19752 15992 13951 -1922 198 -1284 S ATOM 64 CE MET A 36 16.492 17.421 53.523 1.00127.94 C ANISOU 64 CE MET A 36 19084 15939 13587 -2011 87 -1333 C ATOM 65 N GLY A 37 12.064 23.352 52.386 1.00116.12 N ANISOU 65 N GLY A 37 19127 12957 12036 -2015 819 -1272 N ATOM 66 CA GLY A 37 10.743 23.906 52.109 1.00114.83 C ANISOU 66 CA GLY A 37 19195 12550 11886 -1816 918 -1178 C ATOM 67 C GLY A 37 10.621 24.370 50.667 1.00116.99 C ANISOU 67 C GLY A 37 19588 12663 12200 -1795 1011 -1127 C ATOM 68 O GLY A 37 9.622 24.073 50.006 1.00115.02 O ANISOU 68 O GLY A 37 19346 12338 12019 -1558 1017 -1004 O ATOM 69 N ILE A 38 11.668 25.067 50.158 1.00114.15 N ANISOU 69 N ILE A 38 19311 12270 11793 -2049 1085 -1225 N ATOM 70 CA ILE A 38 11.772 25.586 48.788 1.00113.78 C ANISOU 70 CA ILE A 38 19393 12072 11766 -2075 1185 -1194 C ATOM 71 C ILE A 38 11.827 24.420 47.784 1.00116.00 C ANISOU 71 C ILE A 38 19402 12500 12173 -1949 1078 -1096 C ATOM 72 O ILE A 38 11.107 24.476 46.786 1.00115.24 O ANISOU 72 O ILE A 38 19384 12278 12125 -1777 1124 -994 O ATOM 73 CB ILE A 38 12.993 26.552 48.626 1.00118.68 C ANISOU 73 CB ILE A 38 20152 12646 12297 -2419 1292 -1344 C ATOM 74 CG1 ILE A 38 12.813 27.832 49.466 1.00120.79 C ANISOU 74 CG1 ILE A 38 20750 12712 12434 -2537 1432 -1436 C ATOM 75 CG2 ILE A 38 13.258 26.915 47.151 1.00119.46 C ANISOU 75 CG2 ILE A 38 20344 12623 12423 -2461 1385 -1311 C ATOM 76 CD1 ILE A 38 14.115 28.510 49.912 1.00128.26 C ANISOU 76 CD1 ILE A 38 21744 13713 13275 -2919 1490 -1626 C ATOM 77 N VAL A 39 12.665 23.372 48.045 1.00111.64 N ANISOU 77 N VAL A 39 18539 12216 11663 -2023 938 -1128 N ATOM 78 CA VAL A 39 12.830 22.226 47.130 1.00109.73 C ANISOU 78 CA VAL A 39 18040 12120 11532 -1920 838 -1046 C ATOM 79 C VAL A 39 11.547 21.373 47.078 1.00111.25 C ANISOU 79 C VAL A 39 18155 12307 11810 -1612 775 -905 C ATOM 80 O VAL A 39 11.261 20.788 46.032 1.00110.07 O ANISOU 80 O VAL A 39 17909 12167 11746 -1487 750 -817 O ATOM 81 CB VAL A 39 14.099 21.339 47.357 1.00113.70 C ANISOU 81 CB VAL A 39 18244 12910 12045 -2063 714 -1116 C ATOM 82 CG1 VAL A 39 15.380 22.170 47.326 1.00115.44 C ANISOU 82 CG1 VAL A 39 18516 13168 12178 -2383 779 -1268 C ATOM 83 CG2 VAL A 39 14.022 20.497 48.629 1.00113.07 C ANISOU 83 CG2 VAL A 39 17996 13011 11955 -1984 591 -1119 C ATOM 84 N MET A 40 10.782 21.312 48.189 1.00106.35 N ANISOU 84 N MET A 40 17574 11674 11161 -1501 755 -891 N ATOM 85 CA MET A 40 9.524 20.570 48.235 1.00104.10 C ANISOU 85 CA MET A 40 17225 11387 10943 -1231 711 -773 C ATOM 86 C MET A 40 8.476 21.315 47.429 1.00106.52 C ANISOU 86 C MET A 40 17743 11481 11250 -1079 821 -702 C ATOM 87 O MET A 40 7.736 20.680 46.686 1.00105.78 O ANISOU 87 O MET A 40 17556 11404 11233 -892 793 -605 O ATOM 88 CB MET A 40 9.055 20.330 49.673 1.00106.53 C ANISOU 88 CB MET A 40 17520 11747 11210 -1171 668 -786 C ATOM 89 CG MET A 40 9.709 19.140 50.310 1.00109.98 C ANISOU 89 CG MET A 40 17696 12419 11671 -1198 534 -799 C ATOM 90 SD MET A 40 9.125 18.920 51.996 1.00115.20 S ANISOU 90 SD MET A 40 18372 13127 12273 -1121 496 -810 S ATOM 91 CE MET A 40 10.092 17.549 52.479 1.00111.49 C ANISOU 91 CE MET A 40 17609 12931 11819 -1153 348 -823 C ATOM 92 N SER A 41 8.463 22.665 47.528 1.00102.58 N ANISOU 92 N SER A 41 17532 10786 10656 -1163 952 -756 N ATOM 93 CA SER A 41 7.576 23.569 46.794 1.00102.09 C ANISOU 93 CA SER A 41 17723 10505 10562 -1020 1076 -698 C ATOM 94 C SER A 41 7.807 23.465 45.282 1.00103.91 C ANISOU 94 C SER A 41 17923 10712 10848 -1002 1096 -648 C ATOM 95 O SER A 41 6.844 23.549 44.519 1.00103.50 O ANISOU 95 O SER A 41 17936 10576 10812 -785 1134 -556 O ATOM 96 CB SER A 41 7.797 25.011 47.244 1.00107.79 C ANISOU 96 CB SER A 41 18774 11023 11160 -1160 1219 -783 C ATOM 97 OG SER A 41 7.550 25.162 48.631 1.00117.43 O ANISOU 97 OG SER A 41 20038 12258 12322 -1173 1207 -832 O ATOM 98 N LEU A 42 9.079 23.281 44.852 1.00 98.84 N ANISOU 98 N LEU A 42 17173 10156 10225 -1223 1070 -710 N ATOM 99 CA LEU A 42 9.426 23.153 43.433 1.00 97.78 C ANISOU 99 CA LEU A 42 17000 10012 10142 -1228 1087 -670 C ATOM 100 C LEU A 42 9.008 21.801 42.875 1.00 98.64 C ANISOU 100 C LEU A 42 16828 10285 10367 -1050 963 -576 C ATOM 101 O LEU A 42 8.700 21.717 41.687 1.00 97.94 O ANISOU 101 O LEU A 42 16741 10154 10317 -943 986 -507 O ATOM 102 CB LEU A 42 10.921 23.387 43.175 1.00 98.76 C ANISOU 102 CB LEU A 42 17090 10192 10244 -1528 1104 -774 C ATOM 103 CG LEU A 42 11.440 24.832 43.291 1.00105.59 C ANISOU 103 CG LEU A 42 18267 10862 10991 -1743 1264 -873 C ATOM 104 CD1 LEU A 42 12.921 24.887 42.995 1.00106.37 C ANISOU 104 CD1 LEU A 42 18275 11066 11076 -2046 1269 -983 C ATOM 105 CD2 LEU A 42 10.681 25.795 42.372 1.00108.66 C ANISOU 105 CD2 LEU A 42 18965 10986 11335 -1609 1413 -804 C ATOM 106 N ILE A 43 9.001 20.749 43.721 1.00 93.23 N ANISOU 106 N ILE A 43 15914 9782 9729 -1021 840 -575 N ATOM 107 CA ILE A 43 8.580 19.395 43.353 1.00 90.42 C ANISOU 107 CA ILE A 43 15303 9577 9476 -863 730 -493 C ATOM 108 C ILE A 43 7.054 19.431 43.088 1.00 93.49 C ANISOU 108 C ILE A 43 15764 9879 9877 -602 763 -401 C ATOM 109 O ILE A 43 6.623 18.946 42.047 1.00 92.33 O ANISOU 109 O ILE A 43 15533 9758 9792 -477 747 -332 O ATOM 110 CB ILE A 43 9.013 18.333 44.423 1.00 92.43 C ANISOU 110 CB ILE A 43 15335 10029 9756 -905 609 -521 C ATOM 111 CG1 ILE A 43 10.551 18.163 44.440 1.00 92.85 C ANISOU 111 CG1 ILE A 43 15269 10214 9797 -1133 563 -606 C ATOM 112 CG2 ILE A 43 8.352 16.959 44.182 1.00 91.68 C ANISOU 112 CG2 ILE A 43 15025 10053 9755 -723 518 -432 C ATOM 113 CD1 ILE A 43 11.142 17.423 45.696 1.00 99.56 C ANISOU 113 CD1 ILE A 43 15951 11251 10624 -1194 460 -657 C ATOM 114 N VAL A 44 6.267 20.072 43.990 1.00 90.77 N ANISOU 114 N VAL A 44 15582 9441 9466 -525 816 -408 N ATOM 115 CA VAL A 44 4.800 20.208 43.897 1.00 90.31 C ANISOU 115 CA VAL A 44 15597 9321 9398 -275 853 -334 C ATOM 116 C VAL A 44 4.400 20.909 42.606 1.00 94.35 C ANISOU 116 C VAL A 44 16258 9703 9887 -167 940 -286 C ATOM 117 O VAL A 44 3.471 20.444 41.949 1.00 93.69 O ANISOU 117 O VAL A 44 16088 9669 9842 33 920 -214 O ATOM 118 CB VAL A 44 4.168 20.931 45.122 1.00 95.32 C ANISOU 118 CB VAL A 44 16405 9865 9946 -229 908 -362 C ATOM 119 CG1 VAL A 44 2.643 21.021 45.004 1.00 94.71 C ANISOU 119 CG1 VAL A 44 16375 9756 9853 42 943 -289 C ATOM 120 CG2 VAL A 44 4.548 20.251 46.429 1.00 95.04 C ANISOU 120 CG2 VAL A 44 16231 9959 9922 -326 823 -408 C ATOM 121 N LEU A 45 5.077 22.023 42.254 1.00 92.23 N ANISOU 121 N LEU A 45 16220 9276 9548 -298 1042 -329 N ATOM 122 CA LEU A 45 4.778 22.806 41.048 1.00 92.40 C ANISOU 122 CA LEU A 45 16431 9151 9528 -198 1143 -283 C ATOM 123 C LEU A 45 5.081 22.009 39.764 1.00 94.22 C ANISOU 123 C LEU A 45 16469 9484 9846 -181 1084 -237 C ATOM 124 O LEU A 45 4.260 21.998 38.845 1.00 92.81 O ANISOU 124 O LEU A 45 16305 9290 9669 23 1102 -164 O ATOM 125 CB LEU A 45 5.539 24.142 41.055 1.00 94.50 C ANISOU 125 CB LEU A 45 17002 9212 9693 -378 1279 -350 C ATOM 126 CG LEU A 45 5.035 25.191 42.074 1.00101.70 C ANISOU 126 CG LEU A 45 18187 9962 10493 -348 1378 -384 C ATOM 127 CD1 LEU A 45 6.136 26.204 42.439 1.00103.39 C ANISOU 127 CD1 LEU A 45 18628 10031 10624 -633 1483 -490 C ATOM 128 CD2 LEU A 45 3.782 25.907 41.572 1.00105.15 C ANISOU 128 CD2 LEU A 45 18842 10255 10855 -59 1474 -302 C ATOM 129 N ALA A 46 6.231 21.313 39.731 1.00 90.12 N ANISOU 129 N ALA A 46 15762 9086 9392 -384 1008 -283 N ATOM 130 CA ALA A 46 6.681 20.507 38.602 1.00 89.11 C ANISOU 130 CA ALA A 46 15445 9064 9348 -396 948 -250 C ATOM 131 C ALA A 46 5.758 19.311 38.314 1.00 92.76 C ANISOU 131 C ALA A 46 15675 9675 9894 -193 851 -176 C ATOM 132 O ALA A 46 5.600 18.948 37.140 1.00 92.56 O ANISOU 132 O ALA A 46 15576 9682 9911 -109 839 -126 O ATOM 133 CB ALA A 46 8.094 20.012 38.852 1.00 89.71 C ANISOU 133 CB ALA A 46 15365 9258 9462 -645 885 -323 C ATOM 134 N ILE A 47 5.168 18.692 39.369 1.00 88.08 N ANISOU 134 N ILE A 47 14971 9174 9322 -128 787 -175 N ATOM 135 CA ILE A 47 4.265 17.540 39.220 1.00 86.56 C ANISOU 135 CA ILE A 47 14566 9121 9201 38 708 -119 C ATOM 136 C ILE A 47 2.931 17.995 38.594 1.00 91.42 C ANISOU 136 C ILE A 47 15277 9682 9776 277 766 -60 C ATOM 137 O ILE A 47 2.494 17.399 37.609 1.00 91.06 O ANISOU 137 O ILE A 47 15106 9716 9777 387 736 -15 O ATOM 138 CB ILE A 47 4.037 16.752 40.554 1.00 88.83 C ANISOU 138 CB ILE A 47 14724 9515 9513 29 638 -137 C ATOM 139 CG1 ILE A 47 5.339 16.101 41.066 1.00 88.77 C ANISOU 139 CG1 ILE A 47 14583 9605 9542 -169 564 -187 C ATOM 140 CG2 ILE A 47 2.953 15.685 40.398 1.00 87.73 C ANISOU 140 CG2 ILE A 47 14404 9496 9432 197 586 -85 C ATOM 141 CD1 ILE A 47 5.343 15.790 42.548 1.00 91.94 C ANISOU 141 CD1 ILE A 47 14950 10062 9922 -208 524 -220 C ATOM 142 N VAL A 48 2.305 19.043 39.164 1.00 88.61 N ANISOU 142 N VAL A 48 15139 9202 9326 362 849 -65 N ATOM 143 CA VAL A 48 1.007 19.600 38.759 1.00 88.80 C ANISOU 143 CA VAL A 48 15273 9181 9284 612 911 -15 C ATOM 144 C VAL A 48 1.058 20.152 37.306 1.00 93.82 C ANISOU 144 C VAL A 48 16019 9740 9889 691 970 25 C ATOM 145 O VAL A 48 0.232 19.748 36.485 1.00 93.09 O ANISOU 145 O VAL A 48 15822 9741 9808 875 947 74 O ATOM 146 CB VAL A 48 0.518 20.672 39.794 1.00 93.39 C ANISOU 146 CB VAL A 48 16094 9631 9761 667 995 -36 C ATOM 147 CG1 VAL A 48 -0.699 21.447 39.293 1.00 93.83 C ANISOU 147 CG1 VAL A 48 16306 9623 9723 940 1076 15 C ATOM 148 CG2 VAL A 48 0.210 20.025 41.144 1.00 92.32 C ANISOU 148 CG2 VAL A 48 15828 9595 9654 640 934 -63 C ATOM 149 N PHE A 49 2.014 21.057 36.996 1.00 91.33 N ANISOU 149 N PHE A 49 15912 9263 9526 548 1048 1 N ATOM 150 CA PHE A 49 2.124 21.676 35.670 1.00 90.89 C ANISOU 150 CA PHE A 49 16000 9107 9426 614 1122 39 C ATOM 151 C PHE A 49 2.445 20.670 34.592 1.00 91.68 C ANISOU 151 C PHE A 49 15866 9348 9621 597 1040 65 C ATOM 152 O PHE A 49 1.823 20.710 33.529 1.00 92.81 O ANISOU 152 O PHE A 49 16014 9509 9742 779 1055 120 O ATOM 153 CB PHE A 49 3.150 22.825 35.636 1.00 94.19 C ANISOU 153 CB PHE A 49 16699 9317 9773 425 1237 -4 C ATOM 154 CG PHE A 49 2.656 24.090 36.291 1.00 98.16 C ANISOU 154 CG PHE A 49 17522 9627 10148 502 1360 -12 C ATOM 155 CD1 PHE A 49 1.402 24.609 35.985 1.00102.52 C ANISOU 155 CD1 PHE A 49 18210 10131 10614 803 1417 53 C ATOM 156 CD2 PHE A 49 3.443 24.767 37.216 1.00101.69 C ANISOU 156 CD2 PHE A 49 18136 9951 10551 280 1421 -90 C ATOM 157 CE1 PHE A 49 0.943 25.771 36.607 1.00105.13 C ANISOU 157 CE1 PHE A 49 18848 10278 10818 891 1536 47 C ATOM 158 CE2 PHE A 49 2.987 25.942 37.822 1.00106.04 C ANISOU 158 CE2 PHE A 49 19002 10311 10978 348 1544 -101 C ATOM 159 CZ PHE A 49 1.740 26.434 37.517 1.00104.81 C ANISOU 159 CZ PHE A 49 18989 10095 10740 659 1603 -28 C ATOM 160 N GLY A 50 3.401 19.791 34.856 1.00 84.57 N ANISOU 160 N GLY A 50 14766 8550 8816 392 956 25 N ATOM 161 CA GLY A 50 3.796 18.768 33.897 1.00 82.58 C ANISOU 161 CA GLY A 50 14289 8430 8656 362 877 44 C ATOM 162 C GLY A 50 2.663 17.832 33.522 1.00 83.63 C ANISOU 162 C GLY A 50 14223 8719 8834 564 807 91 C ATOM 163 O GLY A 50 2.484 17.521 32.343 1.00 82.44 O ANISOU 163 O GLY A 50 14000 8620 8702 650 795 127 O ATOM 164 N ASN A 51 1.858 17.425 34.520 1.00 79.36 N ANISOU 164 N ASN A 51 13599 8254 8301 639 770 84 N ATOM 165 CA ASN A 51 0.770 16.476 34.327 1.00 78.52 C ANISOU 165 CA ASN A 51 13288 8311 8234 797 710 110 C ATOM 166 C ASN A 51 -0.500 17.085 33.740 1.00 83.22 C ANISOU 166 C ASN A 51 13970 8907 8744 1054 762 150 C ATOM 167 O ASN A 51 -1.243 16.339 33.106 1.00 81.50 O ANISOU 167 O ASN A 51 13575 8839 8554 1173 717 167 O ATOM 168 CB ASN A 51 0.466 15.726 35.611 1.00 77.12 C ANISOU 168 CB ASN A 51 12981 8224 8097 757 655 84 C ATOM 169 CG ASN A 51 1.436 14.602 35.754 1.00 82.26 C ANISOU 169 CG ASN A 51 13449 8960 8847 580 574 63 C ATOM 170 OD1 ASN A 51 1.298 13.566 35.116 1.00 75.40 O ANISOU 170 OD1 ASN A 51 12394 8210 8046 601 519 77 O ATOM 171 ND2 ASN A 51 2.533 14.856 36.428 1.00 74.45 N ANISOU 171 ND2 ASN A 51 12522 7909 7857 403 572 26 N ATOM 172 N VAL A 52 -0.738 18.414 33.899 1.00 82.76 N ANISOU 172 N VAL A 52 14182 8690 8573 1144 860 161 N ATOM 173 CA VAL A 52 -1.892 19.098 33.280 1.00 83.52 C ANISOU 173 CA VAL A 52 14386 8784 8564 1419 919 204 C ATOM 174 C VAL A 52 -1.583 19.305 31.802 1.00 88.09 C ANISOU 174 C VAL A 52 15010 9336 9126 1469 941 241 C ATOM 175 O VAL A 52 -2.492 19.321 30.974 1.00 88.48 O ANISOU 175 O VAL A 52 15022 9475 9121 1692 943 277 O ATOM 176 CB VAL A 52 -2.345 20.419 33.961 1.00 88.80 C ANISOU 176 CB VAL A 52 15344 9290 9105 1533 1024 209 C ATOM 177 CG1 VAL A 52 -2.788 20.183 35.394 1.00 88.03 C ANISOU 177 CG1 VAL A 52 15191 9239 9019 1510 1000 174 C ATOM 178 CG2 VAL A 52 -1.291 21.514 33.881 1.00 89.81 C ANISOU 178 CG2 VAL A 52 15766 9178 9180 1393 1121 201 C ATOM 179 N LEU A 53 -0.287 19.431 31.474 1.00 85.02 N ANISOU 179 N LEU A 53 14688 8839 8776 1258 956 228 N ATOM 180 CA LEU A 53 0.194 19.581 30.110 1.00 85.48 C ANISOU 180 CA LEU A 53 14789 8861 8827 1264 980 259 C ATOM 181 C LEU A 53 -0.037 18.286 29.315 1.00 88.28 C ANISOU 181 C LEU A 53 14843 9427 9274 1295 876 268 C ATOM 182 O LEU A 53 -0.545 18.360 28.207 1.00 89.26 O ANISOU 182 O LEU A 53 14963 9599 9354 1463 886 306 O ATOM 183 CB LEU A 53 1.677 19.961 30.120 1.00 85.87 C ANISOU 183 CB LEU A 53 14960 8766 8902 997 1022 227 C ATOM 184 CG LEU A 53 2.228 20.581 28.859 1.00 91.44 C ANISOU 184 CG LEU A 53 15825 9358 9559 994 1097 257 C ATOM 185 CD1 LEU A 53 1.702 22.002 28.661 1.00 93.28 C ANISOU 185 CD1 LEU A 53 16406 9397 9638 1166 1235 294 C ATOM 186 CD2 LEU A 53 3.732 20.568 28.893 1.00 94.46 C ANISOU 186 CD2 LEU A 53 16219 9674 9996 694 1108 208 C ATOM 187 N VAL A 54 0.286 17.115 29.895 1.00 83.17 N ANISOU 187 N VAL A 54 13956 8904 8742 1146 782 232 N ATOM 188 CA VAL A 54 0.078 15.787 29.291 1.00 81.70 C ANISOU 188 CA VAL A 54 13488 8908 8645 1152 689 231 C ATOM 189 C VAL A 54 -1.432 15.603 28.975 1.00 86.40 C ANISOU 189 C VAL A 54 13991 9648 9189 1400 677 247 C ATOM 190 O VAL A 54 -1.784 15.378 27.814 1.00 87.57 O ANISOU 190 O VAL A 54 14067 9885 9323 1512 664 268 O ATOM 191 CB VAL A 54 0.635 14.627 30.190 1.00 83.66 C ANISOU 191 CB VAL A 54 13540 9240 9006 962 608 191 C ATOM 192 CG1 VAL A 54 0.279 13.250 29.633 1.00 82.33 C ANISOU 192 CG1 VAL A 54 13108 9254 8918 980 529 188 C ATOM 193 CG2 VAL A 54 2.142 14.743 30.388 1.00 83.11 C ANISOU 193 CG2 VAL A 54 13525 9075 8977 732 610 168 C ATOM 194 N ILE A 55 -2.298 15.753 29.999 1.00 81.91 N ANISOU 194 N ILE A 55 13428 9112 8583 1485 686 233 N ATOM 195 CA ILE A 55 -3.759 15.581 29.952 1.00 81.68 C ANISOU 195 CA ILE A 55 13293 9245 8498 1705 677 232 C ATOM 196 C ILE A 55 -4.415 16.485 28.870 1.00 89.54 C ANISOU 196 C ILE A 55 14417 10237 9367 1956 731 274 C ATOM 197 O ILE A 55 -5.230 15.975 28.103 1.00 89.85 O ANISOU 197 O ILE A 55 14289 10462 9389 2095 694 271 O ATOM 198 CB ILE A 55 -4.386 15.779 31.385 1.00 83.79 C ANISOU 198 CB ILE A 55 13589 9510 8737 1730 694 209 C ATOM 199 CG1 ILE A 55 -3.946 14.625 32.332 1.00 81.86 C ANISOU 199 CG1 ILE A 55 13169 9323 8611 1519 629 169 C ATOM 200 CG2 ILE A 55 -5.916 15.866 31.341 1.00 84.11 C ANISOU 200 CG2 ILE A 55 13555 9713 8691 1980 703 206 C ATOM 201 CD1 ILE A 55 -4.128 14.853 33.847 1.00 84.46 C ANISOU 201 CD1 ILE A 55 13564 9602 8927 1478 647 147 C ATOM 202 N THR A 56 -4.052 17.789 28.791 1.00 88.28 N ANISOU 202 N THR A 56 14556 9872 9115 2010 822 309 N ATOM 203 CA THR A 56 -4.639 18.719 27.813 1.00 89.42 C ANISOU 203 CA THR A 56 14866 9990 9121 2268 887 358 C ATOM 204 C THR A 56 -4.086 18.478 26.397 1.00 92.07 C ANISOU 204 C THR A 56 15168 10339 9477 2250 872 383 C ATOM 205 O THR A 56 -4.828 18.687 25.429 1.00 93.65 O ANISOU 205 O THR A 56 15362 10635 9584 2483 880 413 O ATOM 206 CB THR A 56 -4.508 20.216 28.220 1.00100.64 C ANISOU 206 CB THR A 56 16653 11167 10419 2346 1009 389 C ATOM 207 OG1 THR A 56 -3.155 20.665 28.138 1.00107.23 O ANISOU 207 OG1 THR A 56 17671 11784 11286 2122 1061 390 O ATOM 208 CG2 THR A 56 -5.105 20.520 29.588 1.00 92.54 C ANISOU 208 CG2 THR A 56 15675 10125 9360 2384 1030 365 C ATOM 209 N ALA A 57 -2.820 18.042 26.261 1.00 86.21 N ANISOU 209 N ALA A 57 14395 9517 8843 1990 850 370 N ATOM 210 CA ALA A 57 -2.244 17.734 24.941 1.00 85.49 C ANISOU 210 CA ALA A 57 14257 9445 8779 1957 834 390 C ATOM 211 C ALA A 57 -3.024 16.599 24.269 1.00 89.64 C ANISOU 211 C ALA A 57 14485 10231 9344 2051 741 374 C ATOM 212 O ALA A 57 -3.367 16.717 23.099 1.00 90.49 O ANISOU 212 O ALA A 57 14590 10405 9388 2208 746 402 O ATOM 213 CB ALA A 57 -0.772 17.360 25.063 1.00 85.05 C ANISOU 213 CB ALA A 57 14187 9292 8837 1656 819 367 C ATOM 214 N ILE A 58 -3.350 15.530 25.023 1.00 85.42 N ANISOU 214 N ILE A 58 13712 9842 8901 1960 666 326 N ATOM 215 CA ILE A 58 -4.110 14.376 24.521 1.00 84.16 C ANISOU 215 CA ILE A 58 13266 9929 8781 2011 588 294 C ATOM 216 C ILE A 58 -5.594 14.791 24.247 1.00 91.50 C ANISOU 216 C ILE A 58 14171 11017 9579 2306 602 296 C ATOM 217 O ILE A 58 -6.158 14.372 23.230 1.00 92.58 O ANISOU 217 O ILE A 58 14163 11330 9683 2423 567 287 O ATOM 218 CB ILE A 58 -3.954 13.149 25.478 1.00 84.29 C ANISOU 218 CB ILE A 58 13075 10024 8926 1810 524 241 C ATOM 219 CG1 ILE A 58 -2.512 12.606 25.367 1.00 82.26 C ANISOU 219 CG1 ILE A 58 12804 9668 8784 1566 498 241 C ATOM 220 CG2 ILE A 58 -4.968 12.035 25.163 1.00 84.45 C ANISOU 220 CG2 ILE A 58 12823 10298 8968 1866 466 195 C ATOM 221 CD1 ILE A 58 -2.044 11.714 26.426 1.00 87.50 C ANISOU 221 CD1 ILE A 58 13358 10338 9553 1372 456 207 C ATOM 222 N ALA A 59 -6.174 15.659 25.099 1.00 88.78 N ANISOU 222 N ALA A 59 13973 10613 9147 2432 655 306 N ATOM 223 CA ALA A 59 -7.562 16.131 25.005 1.00 90.20 C ANISOU 223 CA ALA A 59 14138 10946 9188 2725 674 306 C ATOM 224 C ALA A 59 -7.829 17.021 23.780 1.00 98.03 C ANISOU 224 C ALA A 59 15283 11927 10036 2979 719 361 C ATOM 225 O ALA A 59 -8.950 16.990 23.256 1.00 99.84 O ANISOU 225 O ALA A 59 15393 12377 10163 3218 700 349 O ATOM 226 CB ALA A 59 -7.945 16.892 26.268 1.00 91.29 C ANISOU 226 CB ALA A 59 14429 10988 9270 2784 728 309 C ATOM 227 N LYS A 60 -6.828 17.820 23.338 1.00 94.26 N ANISOU 227 N LYS A 60 15069 11205 9540 2931 784 416 N ATOM 228 CA LYS A 60 -6.983 18.770 22.230 1.00 94.98 C ANISOU 228 CA LYS A 60 15365 11239 9485 3170 847 478 C ATOM 229 C LYS A 60 -6.426 18.277 20.882 1.00 98.58 C ANISOU 229 C LYS A 60 15739 11741 9977 3120 813 491 C ATOM 230 O LYS A 60 -6.918 18.716 19.840 1.00100.28 O ANISOU 230 O LYS A 60 16013 12024 10065 3363 833 528 O ATOM 231 CB LYS A 60 -6.319 20.116 22.586 1.00 98.30 C ANISOU 231 CB LYS A 60 16178 11339 9832 3168 970 531 C ATOM 232 CG LYS A 60 -7.174 21.041 23.459 1.00110.98 C ANISOU 232 CG LYS A 60 17958 12898 11311 3376 1037 545 C ATOM 233 CD LYS A 60 -8.198 21.859 22.648 1.00123.34 C ANISOU 233 CD LYS A 60 19651 14540 12673 3775 1087 597 C ATOM 234 CE LYS A 60 -9.220 22.576 23.509 1.00130.91 C ANISOU 234 CE LYS A 60 20716 15520 13505 4013 1136 601 C ATOM 235 NZ LYS A 60 -10.170 21.631 24.165 1.00133.46 N ANISOU 235 NZ LYS A 60 20692 16137 13882 4023 1039 532 N ATOM 236 N PHE A 61 -5.414 17.407 20.884 1.00 93.11 N ANISOU 236 N PHE A 61 14921 11013 9444 2826 764 463 N ATOM 237 CA PHE A 61 -4.800 16.951 19.647 1.00 92.39 C ANISOU 237 CA PHE A 61 14765 10949 9391 2764 736 474 C ATOM 238 C PHE A 61 -5.261 15.547 19.247 1.00 97.97 C ANISOU 238 C PHE A 61 15115 11928 10179 2719 628 415 C ATOM 239 O PHE A 61 -4.941 14.554 19.898 1.00 97.43 O ANISOU 239 O PHE A 61 14867 11904 10249 2500 572 366 O ATOM 240 CB PHE A 61 -3.268 17.025 19.740 1.00 93.15 C ANISOU 240 CB PHE A 61 14988 10817 9589 2483 769 486 C ATOM 241 CG PHE A 61 -2.750 18.439 19.806 1.00 96.07 C ANISOU 241 CG PHE A 61 15727 10916 9861 2517 893 539 C ATOM 242 CD1 PHE A 61 -2.533 19.173 18.644 1.00100.79 C ANISOU 242 CD1 PHE A 61 16524 11418 10355 2643 964 596 C ATOM 243 CD2 PHE A 61 -2.507 19.050 21.027 1.00 98.45 C ANISOU 243 CD2 PHE A 61 16191 11053 10163 2424 948 529 C ATOM 244 CE1 PHE A 61 -2.091 20.499 18.707 1.00103.08 C ANISOU 244 CE1 PHE A 61 17185 11441 10542 2671 1098 642 C ATOM 245 CE2 PHE A 61 -2.050 20.370 21.087 1.00102.81 C ANISOU 245 CE2 PHE A 61 17103 11345 10616 2443 1076 569 C ATOM 246 CZ PHE A 61 -1.848 21.087 19.927 1.00102.09 C ANISOU 246 CZ PHE A 61 17220 11150 10420 2564 1156 626 C ATOM 247 N GLU A 62 -5.995 15.497 18.133 1.00 96.49 N ANISOU 247 N GLU A 62 14847 11920 9896 2933 606 421 N ATOM 248 CA GLU A 62 -6.567 14.336 17.448 1.00 96.17 C ANISOU 248 CA GLU A 62 14496 12156 9889 2939 518 362 C ATOM 249 C GLU A 62 -5.544 13.200 17.215 1.00 98.26 C ANISOU 249 C GLU A 62 14615 12398 10322 2647 467 332 C ATOM 250 O GLU A 62 -5.880 12.027 17.404 1.00 96.57 O ANISOU 250 O GLU A 62 14143 12356 10192 2537 401 265 O ATOM 251 CB GLU A 62 -7.183 14.793 16.103 1.00 99.43 C ANISOU 251 CB GLU A 62 14934 12698 10146 3220 524 392 C ATOM 252 CG GLU A 62 -6.244 15.498 15.103 1.00114.13 C ANISOU 252 CG GLU A 62 17036 14361 11967 3240 584 467 C ATOM 253 CD GLU A 62 -5.723 16.901 15.403 1.00120.07 C ANISOU 253 CD GLU A 62 18165 14817 12637 3302 699 546 C ATOM 254 OE1 GLU A 62 -6.552 17.791 15.705 1.00107.68 O ANISOU 254 OE1 GLU A 62 16739 13249 10925 3552 748 574 O ATOM 255 OE2 GLU A 62 -4.493 17.119 15.283 1.00 90.20 O ANISOU 255 OE2 GLU A 62 14540 10807 8924 3105 745 576 O ATOM 256 N ARG A 63 -4.301 13.558 16.813 1.00 94.84 N ANISOU 256 N ARG A 63 14354 11751 9930 2523 506 380 N ATOM 257 CA ARG A 63 -3.181 12.641 16.541 1.00 93.04 C ANISOU 257 CA ARG A 63 14026 11479 9846 2266 468 363 C ATOM 258 C ARG A 63 -2.836 11.822 17.781 1.00 95.65 C ANISOU 258 C ARG A 63 14236 11794 10314 2038 432 317 C ATOM 259 O ARG A 63 -2.387 10.673 17.654 1.00 94.90 O ANISOU 259 O ARG A 63 13963 11764 10331 1869 377 280 O ATOM 260 CB ARG A 63 -1.923 13.418 16.096 1.00 93.97 C ANISOU 260 CB ARG A 63 14384 11358 9963 2180 536 421 C ATOM 261 CG ARG A 63 -2.205 14.719 15.346 1.00118.25 C ANISOU 261 CG ARG A 63 17712 14343 12874 2416 618 487 C ATOM 262 CD ARG A 63 -1.463 15.917 15.924 1.00137.52 C ANISOU 262 CD ARG A 63 20468 16504 15279 2356 722 531 C ATOM 263 NE ARG A 63 -0.576 16.535 14.933 1.00152.22 N ANISOU 263 NE ARG A 63 22529 18208 17098 2331 795 580 N ATOM 264 CZ ARG A 63 0.744 16.375 14.901 1.00169.72 C ANISOU 264 CZ ARG A 63 24780 20295 19413 2072 814 573 C ATOM 265 NH1 ARG A 63 1.467 16.966 13.959 1.00156.98 N ANISOU 265 NH1 ARG A 63 23348 18549 17747 2058 890 615 N ATOM 266 NH2 ARG A 63 1.353 15.627 15.814 1.00159.39 N ANISOU 266 NH2 ARG A 63 23322 18995 18243 1832 761 523 N ATOM 267 N LEU A 64 -3.020 12.440 18.980 1.00 90.65 N ANISOU 267 N LEU A 64 13719 11064 9661 2042 467 322 N ATOM 268 CA LEU A 64 -2.716 11.870 20.294 1.00 88.27 C ANISOU 268 CA LEU A 64 13348 10726 9464 1853 444 287 C ATOM 269 C LEU A 64 -3.912 11.086 20.923 1.00 88.67 C ANISOU 269 C LEU A 64 13187 10980 9523 1900 400 230 C ATOM 270 O LEU A 64 -3.727 10.465 21.973 1.00 87.45 O ANISOU 270 O LEU A 64 12960 10812 9455 1747 379 199 O ATOM 271 CB LEU A 64 -2.247 12.990 21.252 1.00 88.75 C ANISOU 271 CB LEU A 64 13656 10572 9493 1822 512 318 C ATOM 272 CG LEU A 64 -0.925 13.718 20.915 1.00 93.03 C ANISOU 272 CG LEU A 64 14409 10897 10039 1703 569 356 C ATOM 273 CD1 LEU A 64 -0.787 14.966 21.740 1.00 93.78 C ANISOU 273 CD1 LEU A 64 14767 10802 10063 1720 652 378 C ATOM 274 CD2 LEU A 64 0.287 12.840 21.186 1.00 93.52 C ANISOU 274 CD2 LEU A 64 14363 10932 10240 1436 525 329 C ATOM 275 N GLN A 65 -5.102 11.070 20.282 1.00 83.13 N ANISOU 275 N GLN A 65 12381 10477 8728 2103 386 210 N ATOM 276 CA GLN A 65 -6.264 10.352 20.834 1.00 81.91 C ANISOU 276 CA GLN A 65 12018 10535 8571 2136 354 143 C ATOM 277 C GLN A 65 -6.237 8.864 20.424 1.00 83.80 C ANISOU 277 C GLN A 65 12010 10923 8908 1980 297 80 C ATOM 278 O GLN A 65 -7.004 8.412 19.569 1.00 82.56 O ANISOU 278 O GLN A 65 11691 10975 8702 2069 270 36 O ATOM 279 CB GLN A 65 -7.586 11.034 20.448 1.00 84.63 C ANISOU 279 CB GLN A 65 12349 11051 8757 2425 369 137 C ATOM 280 CG GLN A 65 -7.584 12.535 20.748 1.00101.76 C ANISOU 280 CG GLN A 65 14798 13051 10814 2600 438 206 C ATOM 281 CD GLN A 65 -8.904 13.084 21.212 1.00125.93 C ANISOU 281 CD GLN A 65 17844 16256 13747 2836 458 190 C ATOM 282 OE1 GLN A 65 -9.702 12.403 21.868 1.00129.07 O ANISOU 282 OE1 GLN A 65 18045 16829 14167 2805 429 123 O ATOM 283 NE2 GLN A 65 -9.121 14.365 20.953 1.00111.02 N ANISOU 283 NE2 GLN A 65 16185 14279 11718 3072 517 251 N ATOM 284 N THR A 66 -5.325 8.107 21.067 1.00 80.18 N ANISOU 284 N THR A 66 11532 10353 8579 1746 284 73 N ATOM 285 CA THR A 66 -5.090 6.670 20.845 1.00 78.85 C ANISOU 285 CA THR A 66 11178 10268 8513 1573 244 22 C ATOM 286 C THR A 66 -5.356 5.875 22.136 1.00 82.81 C ANISOU 286 C THR A 66 11595 10788 9082 1440 244 -22 C ATOM 287 O THR A 66 -5.383 6.469 23.217 1.00 83.56 O ANISOU 287 O THR A 66 11796 10790 9165 1450 268 -1 O ATOM 288 CB THR A 66 -3.651 6.418 20.323 1.00 82.67 C ANISOU 288 CB THR A 66 11726 10604 9082 1432 233 61 C ATOM 289 OG1 THR A 66 -2.707 6.502 21.395 1.00 80.99 O ANISOU 289 OG1 THR A 66 11617 10216 8939 1290 243 87 O ATOM 290 CG2 THR A 66 -3.249 7.356 19.166 1.00 79.46 C ANISOU 290 CG2 THR A 66 11448 10136 8606 1550 249 114 C ATOM 291 N VAL A 67 -5.538 4.530 22.017 1.00 78.19 N ANISOU 291 N VAL A 67 10835 10312 8562 1312 225 -82 N ATOM 292 CA VAL A 67 -5.779 3.589 23.129 1.00 76.95 C ANISOU 292 CA VAL A 67 10600 10172 8467 1172 236 -127 C ATOM 293 C VAL A 67 -4.614 3.701 24.145 1.00 80.28 C ANISOU 293 C VAL A 67 11163 10378 8961 1054 239 -74 C ATOM 294 O VAL A 67 -4.874 3.894 25.329 1.00 80.56 O ANISOU 294 O VAL A 67 11242 10375 8992 1040 258 -75 O ATOM 295 CB VAL A 67 -6.009 2.118 22.625 1.00 79.86 C ANISOU 295 CB VAL A 67 10793 10663 8887 1044 229 -198 C ATOM 296 CG1 VAL A 67 -5.870 1.092 23.749 1.00 78.53 C ANISOU 296 CG1 VAL A 67 10603 10442 8795 874 251 -225 C ATOM 297 CG2 VAL A 67 -7.364 1.971 21.941 1.00 80.62 C ANISOU 297 CG2 VAL A 67 10723 11011 8898 1141 231 -276 C ATOM 298 N THR A 68 -3.348 3.639 23.674 1.00 76.31 N ANISOU 298 N THR A 68 10727 9752 8514 977 220 -31 N ATOM 299 CA THR A 68 -2.142 3.750 24.514 1.00 75.82 C ANISOU 299 CA THR A 68 10780 9516 8510 866 217 11 C ATOM 300 C THR A 68 -2.110 5.092 25.274 1.00 80.69 C ANISOU 300 C THR A 68 11559 10029 9071 937 240 47 C ATOM 301 O THR A 68 -1.694 5.136 26.437 1.00 80.36 O ANISOU 301 O THR A 68 11580 9898 9054 860 245 56 O ATOM 302 CB THR A 68 -0.880 3.574 23.647 1.00 80.93 C ANISOU 302 CB THR A 68 11454 10091 9207 796 195 42 C ATOM 303 OG1 THR A 68 -0.966 2.320 22.977 1.00 81.76 O ANISOU 303 OG1 THR A 68 11420 10287 9357 736 180 5 O ATOM 304 CG2 THR A 68 0.424 3.628 24.453 1.00 76.88 C ANISOU 304 CG2 THR A 68 11031 9435 8745 677 187 73 C ATOM 305 N ASN A 69 -2.563 6.174 24.619 1.00 77.92 N ANISOU 305 N ASN A 69 11284 9688 8635 1090 259 68 N ATOM 306 CA ASN A 69 -2.580 7.505 25.205 1.00 78.04 C ANISOU 306 CA ASN A 69 11479 9591 8581 1173 296 102 C ATOM 307 C ASN A 69 -3.750 7.714 26.173 1.00 82.39 C ANISOU 307 C ASN A 69 12013 10212 9080 1261 316 76 C ATOM 308 O ASN A 69 -3.698 8.674 26.948 1.00 83.23 O ANISOU 308 O ASN A 69 12273 10209 9142 1300 348 100 O ATOM 309 CB ASN A 69 -2.570 8.564 24.124 1.00 78.88 C ANISOU 309 CB ASN A 69 11703 9661 8606 1313 321 140 C ATOM 310 CG ASN A 69 -1.204 8.803 23.538 1.00 91.27 C ANISOU 310 CG ASN A 69 13369 11095 10214 1210 324 175 C ATOM 311 OD1 ASN A 69 -0.185 8.270 24.009 1.00 82.21 O ANISOU 311 OD1 ASN A 69 12205 9881 9149 1037 303 171 O ATOM 312 ND2 ASN A 69 -1.149 9.638 22.510 1.00 80.75 N ANISOU 312 ND2 ASN A 69 12145 9724 8810 1321 354 209 N ATOM 313 N TYR A 70 -4.786 6.833 26.145 1.00 78.23 N ANISOU 313 N TYR A 70 11304 9866 8554 1282 304 23 N ATOM 314 CA TYR A 70 -5.907 6.855 27.100 1.00 77.98 C ANISOU 314 CA TYR A 70 11225 9926 8479 1341 326 -13 C ATOM 315 C TYR A 70 -5.424 6.258 28.417 1.00 78.33 C ANISOU 315 C TYR A 70 11282 9881 8597 1178 327 -19 C ATOM 316 O TYR A 70 -5.846 6.686 29.489 1.00 78.13 O ANISOU 316 O TYR A 70 11315 9830 8539 1208 352 -21 O ATOM 317 CB TYR A 70 -7.120 6.073 26.572 1.00 80.71 C ANISOU 317 CB TYR A 70 11360 10510 8796 1391 320 -81 C ATOM 318 CG TYR A 70 -8.015 6.786 25.573 1.00 85.77 C ANISOU 318 CG TYR A 70 11969 11297 9323 1608 323 -88 C ATOM 319 CD1 TYR A 70 -7.643 8.007 25.011 1.00 88.72 C ANISOU 319 CD1 TYR A 70 12517 11565 9629 1752 334 -24 C ATOM 320 CD2 TYR A 70 -9.234 6.233 25.184 1.00 87.55 C ANISOU 320 CD2 TYR A 70 11993 11774 9496 1671 319 -163 C ATOM 321 CE1 TYR A 70 -8.462 8.658 24.087 1.00 90.87 C ANISOU 321 CE1 TYR A 70 12774 11972 9780 1977 339 -24 C ATOM 322 CE2 TYR A 70 -10.056 6.871 24.255 1.00 89.77 C ANISOU 322 CE2 TYR A 70 12232 12219 9658 1889 314 -173 C ATOM 323 CZ TYR A 70 -9.660 8.076 23.699 1.00 98.29 C ANISOU 323 CZ TYR A 70 13495 13182 10667 2054 323 -98 C ATOM 324 OH TYR A 70 -10.478 8.705 22.789 1.00100.73 O ANISOU 324 OH TYR A 70 13776 13655 10843 2294 321 -101 O ATOM 325 N PHE A 71 -4.517 5.270 28.324 1.00 73.16 N ANISOU 325 N PHE A 71 10580 9181 8035 1017 301 -19 N ATOM 326 CA PHE A 71 -3.897 4.608 29.462 1.00 72.54 C ANISOU 326 CA PHE A 71 10520 9020 8022 872 298 -18 C ATOM 327 C PHE A 71 -2.894 5.546 30.101 1.00 78.71 C ANISOU 327 C PHE A 71 11475 9634 8799 846 297 28 C ATOM 328 O PHE A 71 -2.813 5.611 31.329 1.00 79.99 O ANISOU 328 O PHE A 71 11692 9739 8961 801 307 28 O ATOM 329 CB PHE A 71 -3.233 3.285 29.049 1.00 73.52 C ANISOU 329 CB PHE A 71 10551 9154 8230 738 275 -29 C ATOM 330 CG PHE A 71 -4.167 2.164 28.635 1.00 75.33 C ANISOU 330 CG PHE A 71 10618 9535 8469 714 289 -89 C ATOM 331 CD1 PHE A 71 -5.291 1.849 29.400 1.00 79.09 C ANISOU 331 CD1 PHE A 71 11029 10105 8916 719 326 -136 C ATOM 332 CD2 PHE A 71 -3.885 1.376 27.524 1.00 76.97 C ANISOU 332 CD2 PHE A 71 10739 9790 8714 668 273 -105 C ATOM 333 CE1 PHE A 71 -6.156 0.816 29.015 1.00 80.25 C ANISOU 333 CE1 PHE A 71 11027 10400 9066 671 350 -206 C ATOM 334 CE2 PHE A 71 -4.733 0.323 27.159 1.00 79.97 C ANISOU 334 CE2 PHE A 71 10978 10308 9099 623 295 -172 C ATOM 335 CZ PHE A 71 -5.867 0.058 27.901 1.00 78.67 C ANISOU 335 CZ PHE A 71 10749 10242 8901 618 336 -225 C ATOM 336 N ILE A 72 -2.164 6.309 29.271 1.00 76.42 N ANISOU 336 N ILE A 72 11274 9268 8495 871 291 61 N ATOM 337 CA ILE A 72 -1.186 7.323 29.696 1.00 76.75 C ANISOU 337 CA ILE A 72 11489 9153 8520 832 302 93 C ATOM 338 C ILE A 72 -1.921 8.476 30.461 1.00 81.82 C ANISOU 338 C ILE A 72 12262 9749 9076 942 346 97 C ATOM 339 O ILE A 72 -1.330 9.048 31.380 1.00 80.79 O ANISOU 339 O ILE A 72 12256 9504 8935 879 359 104 O ATOM 340 CB ILE A 72 -0.337 7.806 28.469 1.00 79.30 C ANISOU 340 CB ILE A 72 11871 9418 8842 828 300 121 C ATOM 341 CG1 ILE A 72 0.878 6.854 28.259 1.00 78.13 C ANISOU 341 CG1 ILE A 72 11645 9260 8780 674 259 120 C ATOM 342 CG2 ILE A 72 0.085 9.301 28.564 1.00 79.37 C ANISOU 342 CG2 ILE A 72 12093 9282 8781 859 346 147 C ATOM 343 CD1 ILE A 72 1.770 7.129 27.021 1.00 83.37 C ANISOU 343 CD1 ILE A 72 12339 9886 9452 649 256 141 C ATOM 344 N THR A 73 -3.215 8.767 30.123 1.00 79.53 N ANISOU 344 N THR A 73 11936 9562 8719 1107 369 87 N ATOM 345 CA THR A 73 -3.974 9.804 30.835 1.00 80.23 C ANISOU 345 CA THR A 73 12145 9619 8719 1234 414 91 C ATOM 346 C THR A 73 -4.402 9.262 32.180 1.00 82.34 C ANISOU 346 C THR A 73 12356 9921 9007 1175 413 62 C ATOM 347 O THR A 73 -4.451 10.032 33.135 1.00 82.17 O ANISOU 347 O THR A 73 12467 9813 8942 1197 444 68 O ATOM 348 CB THR A 73 -5.152 10.425 30.036 1.00 92.32 C ANISOU 348 CB THR A 73 13670 11256 10150 1458 440 93 C ATOM 349 OG1 THR A 73 -6.156 9.469 29.741 1.00 99.86 O ANISOU 349 OG1 THR A 73 14409 12419 11113 1496 418 49 O ATOM 350 CG2 THR A 73 -4.710 11.093 28.780 1.00 89.08 C ANISOU 350 CG2 THR A 73 13356 10789 9702 1531 451 131 C ATOM 351 N SER A 74 -4.664 7.945 32.276 1.00 79.65 N ANISOU 351 N SER A 74 11837 9695 8731 1093 387 30 N ATOM 352 CA SER A 74 -4.998 7.278 33.550 1.00 79.58 C ANISOU 352 CA SER A 74 11779 9711 8746 1019 394 3 C ATOM 353 C SER A 74 -3.826 7.443 34.528 1.00 83.62 C ANISOU 353 C SER A 74 12412 10070 9290 895 382 26 C ATOM 354 O SER A 74 -4.019 7.865 35.665 1.00 83.91 O ANISOU 354 O SER A 74 12529 10059 9293 900 403 22 O ATOM 355 CB SER A 74 -5.313 5.804 33.316 1.00 81.95 C ANISOU 355 CB SER A 74 11896 10133 9108 933 380 -33 C ATOM 356 OG SER A 74 -5.604 5.132 34.529 1.00 90.09 O ANISOU 356 OG SER A 74 12900 11174 10157 857 398 -55 O ATOM 357 N LEU A 75 -2.606 7.212 34.028 1.00 80.39 N ANISOU 357 N LEU A 75 12018 9594 8934 794 348 45 N ATOM 358 CA LEU A 75 -1.332 7.360 34.727 1.00 80.60 C ANISOU 358 CA LEU A 75 12134 9506 8984 673 328 58 C ATOM 359 C LEU A 75 -1.068 8.828 35.174 1.00 85.74 C ANISOU 359 C LEU A 75 12976 10035 9565 702 360 68 C ATOM 360 O LEU A 75 -0.603 9.028 36.296 1.00 86.61 O ANISOU 360 O LEU A 75 13160 10084 9666 630 359 59 O ATOM 361 CB LEU A 75 -0.218 6.872 33.783 1.00 80.45 C ANISOU 361 CB LEU A 75 12068 9476 9023 587 291 71 C ATOM 362 CG LEU A 75 1.166 6.600 34.353 1.00 85.44 C ANISOU 362 CG LEU A 75 12724 10050 9688 451 256 74 C ATOM 363 CD1 LEU A 75 1.105 5.701 35.573 1.00 85.61 C ANISOU 363 CD1 LEU A 75 12700 10099 9727 402 243 64 C ATOM 364 CD2 LEU A 75 2.028 5.935 33.310 1.00 87.51 C ANISOU 364 CD2 LEU A 75 12906 10339 10006 393 223 84 C ATOM 365 N ALA A 76 -1.395 9.836 34.311 1.00 81.88 N ANISOU 365 N ALA A 76 12578 9512 9021 812 395 83 N ATOM 366 CA ALA A 76 -1.218 11.284 34.526 1.00 81.68 C ANISOU 366 CA ALA A 76 12765 9353 8917 854 446 93 C ATOM 367 C ALA A 76 -2.253 11.868 35.501 1.00 86.04 C ANISOU 367 C ALA A 76 13393 9900 9398 964 488 84 C ATOM 368 O ALA A 76 -1.962 12.878 36.155 1.00 87.30 O ANISOU 368 O ALA A 76 13734 9934 9501 952 528 83 O ATOM 369 CB ALA A 76 -1.286 12.023 33.200 1.00 82.95 C ANISOU 369 CB ALA A 76 13002 9481 9035 955 477 119 C ATOM 370 N CYS A 77 -3.456 11.250 35.596 1.00 81.23 N ANISOU 370 N CYS A 77 12647 9432 8787 1064 484 72 N ATOM 371 CA CYS A 77 -4.489 11.631 36.575 1.00 80.79 C ANISOU 371 CA CYS A 77 12628 9402 8667 1165 521 58 C ATOM 372 C CYS A 77 -4.014 11.265 37.999 1.00 83.08 C ANISOU 372 C CYS A 77 12935 9643 8987 1029 508 41 C ATOM 373 O CYS A 77 -4.179 12.080 38.904 1.00 83.93 O ANISOU 373 O CYS A 77 13182 9673 9034 1061 545 36 O ATOM 374 CB CYS A 77 -5.823 10.967 36.261 1.00 80.74 C ANISOU 374 CB CYS A 77 12443 9584 8650 1280 521 37 C ATOM 375 SG CYS A 77 -6.705 11.692 34.865 1.00 85.37 S ANISOU 375 SG CYS A 77 13032 10255 9150 1508 546 51 S ATOM 376 N ALA A 78 -3.440 10.039 38.187 1.00 76.77 N ANISOU 376 N ALA A 78 12004 8891 8273 890 459 33 N ATOM 377 CA ALA A 78 -2.895 9.541 39.460 1.00 76.09 C ANISOU 377 CA ALA A 78 11924 8775 8212 769 440 21 C ATOM 378 C ALA A 78 -1.750 10.433 39.947 1.00 80.93 C ANISOU 378 C ALA A 78 12700 9252 8799 681 438 21 C ATOM 379 O ALA A 78 -1.668 10.748 41.135 1.00 81.27 O ANISOU 379 O ALA A 78 12826 9248 8807 649 449 7 O ATOM 380 CB ALA A 78 -2.407 8.104 39.303 1.00 75.90 C ANISOU 380 CB ALA A 78 11750 8819 8271 664 394 21 C ATOM 381 N ASP A 79 -0.907 10.888 39.009 1.00 77.41 N ANISOU 381 N ASP A 79 12303 8746 8361 641 431 31 N ATOM 382 CA ASP A 79 0.213 11.780 39.266 1.00 77.25 C ANISOU 382 CA ASP A 79 12433 8607 8311 536 440 19 C ATOM 383 C ASP A 79 -0.243 13.220 39.615 1.00 81.88 C ANISOU 383 C ASP A 79 13231 9077 8802 615 513 14 C ATOM 384 O ASP A 79 0.440 13.905 40.379 1.00 82.41 O ANISOU 384 O ASP A 79 13431 9050 8830 518 531 -13 O ATOM 385 CB ASP A 79 1.135 11.789 38.047 1.00 78.71 C ANISOU 385 CB ASP A 79 12600 8774 8531 472 424 29 C ATOM 386 CG ASP A 79 1.855 10.474 37.842 1.00 85.18 C ANISOU 386 CG ASP A 79 13244 9687 9434 377 355 30 C ATOM 387 OD1 ASP A 79 2.240 9.846 38.846 1.00 86.42 O ANISOU 387 OD1 ASP A 79 13352 9878 9606 304 320 16 O ATOM 388 OD2 ASP A 79 2.066 10.093 36.679 1.00 90.32 O ANISOU 388 OD2 ASP A 79 13819 10373 10127 383 339 46 O ATOM 389 N LEU A 80 -1.393 13.663 39.070 1.00 77.95 N ANISOU 389 N LEU A 80 12764 8594 8260 793 557 35 N ATOM 390 CA LEU A 80 -1.984 14.972 39.350 1.00 78.35 C ANISOU 390 CA LEU A 80 13021 8540 8208 911 634 37 C ATOM 391 C LEU A 80 -2.671 14.979 40.738 1.00 82.51 C ANISOU 391 C LEU A 80 13564 9084 8700 946 648 17 C ATOM 392 O LEU A 80 -2.593 15.987 41.436 1.00 83.41 O ANISOU 392 O LEU A 80 13872 9079 8741 948 701 3 O ATOM 393 CB LEU A 80 -2.979 15.339 38.234 1.00 78.95 C ANISOU 393 CB LEU A 80 13103 8657 8238 1118 670 69 C ATOM 394 CG LEU A 80 -3.538 16.771 38.192 1.00 84.86 C ANISOU 394 CG LEU A 80 14092 9286 8864 1280 760 84 C ATOM 395 CD1 LEU A 80 -2.430 17.816 38.061 1.00 85.33 C ANISOU 395 CD1 LEU A 80 14392 9145 8886 1167 815 81 C ATOM 396 CD2 LEU A 80 -4.532 16.912 37.068 1.00 87.06 C ANISOU 396 CD2 LEU A 80 14332 9653 9095 1503 778 116 C ATOM 397 N VAL A 81 -3.334 13.852 41.132 1.00 79.05 N ANISOU 397 N VAL A 81 12934 8791 8310 965 608 13 N ATOM 398 CA VAL A 81 -4.010 13.656 42.431 1.00 79.05 C ANISOU 398 CA VAL A 81 12922 8829 8286 988 619 -5 C ATOM 399 C VAL A 81 -2.911 13.559 43.517 1.00 85.20 C ANISOU 399 C VAL A 81 13756 9536 9078 811 591 -28 C ATOM 400 O VAL A 81 -3.075 14.103 44.616 1.00 86.10 O ANISOU 400 O VAL A 81 13984 9595 9136 814 621 -47 O ATOM 401 CB VAL A 81 -5.009 12.449 42.438 1.00 81.84 C ANISOU 401 CB VAL A 81 13059 9355 8681 1040 599 -9 C ATOM 402 CG1 VAL A 81 -5.611 12.211 43.818 1.00 81.62 C ANISOU 402 CG1 VAL A 81 13025 9359 8628 1043 617 -29 C ATOM 403 CG2 VAL A 81 -6.137 12.650 41.426 1.00 81.92 C ANISOU 403 CG2 VAL A 81 13007 9464 8656 1221 626 0 C ATOM 404 N MET A 82 -1.776 12.932 43.170 1.00 82.70 N ANISOU 404 N MET A 82 13364 9229 8828 668 535 -29 N ATOM 405 CA MET A 82 -0.588 12.796 44.007 1.00 83.52 C ANISOU 405 CA MET A 82 13496 9300 8940 504 497 -55 C ATOM 406 C MET A 82 0.016 14.184 44.274 1.00 87.12 C ANISOU 406 C MET A 82 14166 9614 9321 448 543 -83 C ATOM 407 O MET A 82 0.342 14.491 45.413 1.00 87.25 O ANISOU 407 O MET A 82 14261 9595 9294 377 546 -116 O ATOM 408 CB MET A 82 0.433 11.877 43.298 1.00 86.37 C ANISOU 408 CB MET A 82 13720 9719 9379 397 432 -47 C ATOM 409 CG MET A 82 1.440 11.203 44.216 1.00 91.82 C ANISOU 409 CG MET A 82 14357 10449 10083 267 375 -68 C ATOM 410 SD MET A 82 0.717 9.933 45.282 1.00 97.56 S ANISOU 410 SD MET A 82 14971 11269 10828 310 356 -54 S ATOM 411 CE MET A 82 2.118 8.919 45.554 1.00 94.25 C ANISOU 411 CE MET A 82 14455 10915 10442 189 278 -58 C ATOM 412 N GLY A 83 0.096 15.016 43.233 1.00 83.74 N ANISOU 412 N GLY A 83 13841 9105 8870 483 587 -73 N ATOM 413 CA GLY A 83 0.642 16.369 43.306 1.00 83.69 C ANISOU 413 CA GLY A 83 14067 8944 8788 424 653 -101 C ATOM 414 C GLY A 83 -0.176 17.378 44.082 1.00 87.18 C ANISOU 414 C GLY A 83 14700 9289 9135 527 730 -110 C ATOM 415 O GLY A 83 0.401 18.203 44.790 1.00 87.33 O ANISOU 415 O GLY A 83 14888 9200 9093 422 769 -154 O ATOM 416 N LEU A 84 -1.518 17.354 43.938 1.00 83.38 N ANISOU 416 N LEU A 84 14196 8852 8633 732 757 -75 N ATOM 417 CA LEU A 84 -2.418 18.303 44.608 1.00 84.04 C ANISOU 417 CA LEU A 84 14456 8857 8618 868 834 -78 C ATOM 418 C LEU A 84 -2.871 17.851 45.998 1.00 88.13 C ANISOU 418 C LEU A 84 14914 9440 9130 863 813 -99 C ATOM 419 O LEU A 84 -2.847 18.650 46.935 1.00 88.39 O ANISOU 419 O LEU A 84 15121 9374 9089 845 861 -129 O ATOM 420 CB LEU A 84 -3.671 18.540 43.752 1.00 84.61 C ANISOU 420 CB LEU A 84 14523 8971 8652 1112 875 -34 C ATOM 421 CG LEU A 84 -3.515 19.378 42.477 1.00 90.69 C ANISOU 421 CG LEU A 84 15438 9641 9379 1188 930 -6 C ATOM 422 CD1 LEU A 84 -4.659 19.112 41.515 1.00 91.02 C ANISOU 422 CD1 LEU A 84 15366 9809 9410 1416 928 36 C ATOM 423 CD2 LEU A 84 -3.424 20.866 42.790 1.00 94.68 C ANISOU 423 CD2 LEU A 84 16268 9939 9766 1223 1038 -16 C ATOM 424 N ALA A 85 -3.335 16.588 46.128 1.00 83.96 N ANISOU 424 N ALA A 85 14154 9072 8673 882 751 -86 N ATOM 425 CA ALA A 85 -3.895 16.067 47.377 1.00 82.42 C ANISOU 425 CA ALA A 85 13897 8947 8471 893 741 -99 C ATOM 426 C ALA A 85 -2.934 15.202 48.222 1.00 82.72 C ANISOU 426 C ALA A 85 13848 9025 8559 712 672 -121 C ATOM 427 O ALA A 85 -3.252 14.952 49.384 1.00 81.96 O ANISOU 427 O ALA A 85 13748 8956 8438 709 673 -136 O ATOM 428 CB ALA A 85 -5.144 15.264 47.068 1.00 82.59 C ANISOU 428 CB ALA A 85 13741 9120 8520 1033 738 -77 C ATOM 429 N VAL A 86 -1.795 14.738 47.689 1.00 77.18 N ANISOU 429 N VAL A 86 13075 8335 7916 577 615 -124 N ATOM 430 CA VAL A 86 -0.949 13.866 48.518 1.00 75.96 C ANISOU 430 CA VAL A 86 12830 8241 7792 442 549 -141 C ATOM 431 C VAL A 86 0.378 14.565 48.955 1.00 81.79 C ANISOU 431 C VAL A 86 13683 8906 8487 280 535 -191 C ATOM 432 O VAL A 86 0.617 14.703 50.164 1.00 81.42 O ANISOU 432 O VAL A 86 13692 8854 8389 224 529 -225 O ATOM 433 CB VAL A 86 -0.681 12.484 47.866 1.00 76.57 C ANISOU 433 CB VAL A 86 12700 8431 7961 413 486 -112 C ATOM 434 CG1 VAL A 86 0.122 11.595 48.794 1.00 76.00 C ANISOU 434 CG1 VAL A 86 12555 8420 7901 310 425 -124 C ATOM 435 CG2 VAL A 86 -1.983 11.804 47.470 1.00 75.42 C ANISOU 435 CG2 VAL A 86 12440 8366 7849 544 507 -82 C ATOM 436 N VAL A 87 1.238 14.957 47.987 1.00 78.50 N ANISOU 436 N VAL A 87 13292 8447 8087 198 532 -200 N ATOM 437 CA VAL A 87 2.552 15.579 48.215 1.00 78.77 C ANISOU 437 CA VAL A 87 13411 8435 8082 20 524 -259 C ATOM 438 C VAL A 87 2.450 16.855 49.102 1.00 84.82 C ANISOU 438 C VAL A 87 14405 9078 8746 -10 595 -310 C ATOM 439 O VAL A 87 3.250 16.933 50.037 1.00 85.52 O ANISOU 439 O VAL A 87 14509 9191 8792 -144 567 -367 O ATOM 440 CB VAL A 87 3.330 15.847 46.894 1.00 82.15 C ANISOU 440 CB VAL A 87 13838 8832 8542 -54 529 -260 C ATOM 441 CG1 VAL A 87 4.618 16.624 47.146 1.00 82.90 C ANISOU 441 CG1 VAL A 87 14034 8881 8582 -253 540 -335 C ATOM 442 CG2 VAL A 87 3.637 14.538 46.173 1.00 80.41 C ANISOU 442 CG2 VAL A 87 13395 8741 8416 -50 451 -222 C ATOM 443 N PRO A 88 1.503 17.823 48.914 1.00 82.52 N ANISOU 443 N PRO A 88 14288 8664 8402 115 686 -294 N ATOM 444 CA PRO A 88 1.490 19.004 49.791 1.00 83.83 C ANISOU 444 CA PRO A 88 14685 8703 8465 77 759 -346 C ATOM 445 C PRO A 88 1.279 18.707 51.274 1.00 87.17 C ANISOU 445 C PRO A 88 15089 9180 8852 69 732 -373 C ATOM 446 O PRO A 88 1.895 19.408 52.081 1.00 88.04 O ANISOU 446 O PRO A 88 15333 9231 8888 -59 755 -441 O ATOM 447 CB PRO A 88 0.330 19.838 49.244 1.00 86.16 C ANISOU 447 CB PRO A 88 15138 8884 8715 272 854 -304 C ATOM 448 CG PRO A 88 0.214 19.432 47.846 1.00 89.57 C ANISOU 448 CG PRO A 88 15465 9354 9215 342 838 -252 C ATOM 449 CD PRO A 88 0.459 17.956 47.879 1.00 83.85 C ANISOU 449 CD PRO A 88 14465 8806 8588 300 730 -234 C ATOM 450 N PHE A 89 0.450 17.691 51.647 1.00 82.08 N ANISOU 450 N PHE A 89 14287 8649 8252 188 690 -326 N ATOM 451 CA PHE A 89 0.198 17.373 53.065 1.00 82.16 C ANISOU 451 CA PHE A 89 14286 8708 8223 190 671 -345 C ATOM 452 C PHE A 89 1.362 16.574 53.714 1.00 86.54 C ANISOU 452 C PHE A 89 14716 9373 8790 35 579 -379 C ATOM 453 O PHE A 89 1.534 16.634 54.936 1.00 86.64 O ANISOU 453 O PHE A 89 14772 9405 8742 -11 567 -418 O ATOM 454 CB PHE A 89 -1.144 16.655 53.262 1.00 83.19 C ANISOU 454 CB PHE A 89 14316 8911 8382 365 679 -290 C ATOM 455 CG PHE A 89 -2.322 17.479 52.801 1.00 85.21 C ANISOU 455 CG PHE A 89 14687 9090 8601 538 766 -266 C ATOM 456 CD1 PHE A 89 -2.879 18.455 53.628 1.00 89.20 C ANISOU 456 CD1 PHE A 89 15380 9501 9010 603 839 -291 C ATOM 457 CD2 PHE A 89 -2.851 17.313 51.522 1.00 86.36 C ANISOU 457 CD2 PHE A 89 14758 9260 8794 646 776 -221 C ATOM 458 CE1 PHE A 89 -3.953 19.240 53.188 1.00 90.56 C ANISOU 458 CE1 PHE A 89 15666 9610 9132 788 922 -266 C ATOM 459 CE2 PHE A 89 -3.938 18.080 51.090 1.00 89.80 C ANISOU 459 CE2 PHE A 89 15294 9647 9178 830 853 -199 C ATOM 460 CZ PHE A 89 -4.481 19.040 51.925 1.00 89.54 C ANISOU 460 CZ PHE A 89 15450 9523 9046 907 926 -220 C ATOM 461 N GLY A 90 2.151 15.880 52.893 1.00 82.62 N ANISOU 461 N GLY A 90 14076 8952 8363 -33 518 -366 N ATOM 462 CA GLY A 90 3.339 15.156 53.333 1.00 82.15 C ANISOU 462 CA GLY A 90 13895 9012 8307 -161 430 -397 C ATOM 463 C GLY A 90 4.458 16.141 53.610 1.00 87.18 C ANISOU 463 C GLY A 90 14643 9611 8869 -338 439 -486 C ATOM 464 O GLY A 90 5.228 15.963 54.554 1.00 85.65 O ANISOU 464 O GLY A 90 14417 9505 8621 -436 387 -539 O ATOM 465 N ALA A 91 4.525 17.212 52.780 1.00 87.20 N ANISOU 465 N ALA A 91 14789 9485 8859 -381 512 -507 N ATOM 466 CA ALA A 91 5.487 18.324 52.850 1.00 89.26 C ANISOU 466 CA ALA A 91 15195 9675 9045 -568 553 -599 C ATOM 467 C ALA A 91 5.287 19.120 54.139 1.00 96.10 C ANISOU 467 C ALA A 91 16231 10476 9808 -604 598 -661 C ATOM 468 O ALA A 91 6.265 19.369 54.840 1.00 97.50 O ANISOU 468 O ALA A 91 16416 10711 9918 -775 572 -751 O ATOM 469 CB ALA A 91 5.335 19.231 51.637 1.00 90.24 C ANISOU 469 CB ALA A 91 15464 9646 9177 -565 643 -588 C ATOM 470 N ALA A 92 4.018 19.451 54.485 1.00 93.14 N ANISOU 470 N ALA A 92 15974 10003 9413 -439 661 -618 N ATOM 471 CA ALA A 92 3.642 20.160 55.713 1.00 94.21 C ANISOU 471 CA ALA A 92 16275 10069 9451 -440 710 -665 C ATOM 472 C ALA A 92 3.999 19.355 56.968 1.00100.38 C ANISOU 472 C ALA A 92 16927 11005 10208 -480 622 -691 C ATOM 473 O ALA A 92 4.465 19.942 57.939 1.00102.06 O ANISOU 473 O ALA A 92 17242 11209 10328 -594 633 -774 O ATOM 474 CB ALA A 92 2.153 20.456 55.708 1.00 94.67 C ANISOU 474 CB ALA A 92 16437 10028 9505 -222 784 -599 C ATOM 475 N HIS A 93 3.770 18.017 56.939 1.00 96.89 N ANISOU 475 N HIS A 93 16272 10700 9841 -383 541 -621 N ATOM 476 CA HIS A 93 4.024 17.069 58.036 1.00 96.86 C ANISOU 476 CA HIS A 93 16143 10844 9816 -381 460 -624 C ATOM 477 C HIS A 93 5.507 17.059 58.455 1.00102.00 C ANISOU 477 C HIS A 93 16733 11613 10409 -568 388 -711 C ATOM 478 O HIS A 93 5.785 17.064 59.651 1.00102.61 O ANISOU 478 O HIS A 93 16828 11757 10403 -609 359 -761 O ATOM 479 CB HIS A 93 3.569 15.650 57.627 1.00 96.48 C ANISOU 479 CB HIS A 93 15900 10894 9864 -253 406 -530 C ATOM 480 CG HIS A 93 3.604 14.637 58.737 1.00100.24 C ANISOU 480 CG HIS A 93 16280 11493 10313 -213 345 -513 C ATOM 481 ND1 HIS A 93 4.752 13.912 59.021 1.00102.26 N ANISOU 481 ND1 HIS A 93 16409 11894 10549 -289 254 -535 N ATOM 482 CD2 HIS A 93 2.628 14.253 59.590 1.00101.94 C ANISOU 482 CD2 HIS A 93 16517 11706 10511 -98 370 -476 C ATOM 483 CE1 HIS A 93 4.443 13.129 60.041 1.00101.50 C ANISOU 483 CE1 HIS A 93 16278 11867 10420 -210 228 -506 C ATOM 484 NE2 HIS A 93 3.178 13.294 60.416 1.00101.75 N ANISOU 484 NE2 HIS A 93 16396 11811 10455 -104 298 -471 N ATOM 485 N ILE A 94 6.442 17.058 57.479 1.00 99.13 N ANISOU 485 N ILE A 94 16294 11289 10083 -678 362 -734 N ATOM 486 CA ILE A 94 7.900 17.034 57.682 1.00 99.99 C ANISOU 486 CA ILE A 94 16313 11539 10137 -860 294 -824 C ATOM 487 C ILE A 94 8.410 18.379 58.254 1.00105.83 C ANISOU 487 C ILE A 94 17234 12212 10766 -1042 354 -949 C ATOM 488 O ILE A 94 9.235 18.372 59.173 1.00106.82 O ANISOU 488 O ILE A 94 17313 12472 10801 -1156 300 -1035 O ATOM 489 CB ILE A 94 8.615 16.657 56.339 1.00102.55 C ANISOU 489 CB ILE A 94 16507 11916 10542 -912 264 -807 C ATOM 490 CG1 ILE A 94 8.549 15.142 56.110 1.00101.89 C ANISOU 490 CG1 ILE A 94 16214 11964 10535 -776 178 -716 C ATOM 491 CG2 ILE A 94 10.079 17.157 56.259 1.00103.96 C ANISOU 491 CG2 ILE A 94 16651 12195 10656 -1141 239 -925 C ATOM 492 CD1 ILE A 94 8.384 14.760 54.713 1.00112.70 C ANISOU 492 CD1 ILE A 94 17512 13298 12012 -725 187 -649 C ATOM 493 N LEU A 95 7.942 19.512 57.690 1.00102.40 N ANISOU 493 N LEU A 95 17007 11573 10327 -1069 468 -960 N ATOM 494 CA LEU A 95 8.352 20.860 58.093 1.00103.54 C ANISOU 494 CA LEU A 95 17365 11610 10365 -1249 553 -1077 C ATOM 495 C LEU A 95 7.823 21.248 59.474 1.00108.38 C ANISOU 495 C LEU A 95 18106 12188 10887 -1216 577 -1113 C ATOM 496 O LEU A 95 8.468 22.052 60.157 1.00110.05 O ANISOU 496 O LEU A 95 18427 12396 10990 -1398 606 -1234 O ATOM 497 CB LEU A 95 7.891 21.913 57.065 1.00103.76 C ANISOU 497 CB LEU A 95 17609 11405 10409 -1248 683 -1062 C ATOM 498 CG LEU A 95 8.401 21.822 55.622 1.00107.48 C ANISOU 498 CG LEU A 95 18014 11869 10956 -1299 689 -1037 C ATOM 499 CD1 LEU A 95 7.751 22.885 54.765 1.00107.92 C ANISOU 499 CD1 LEU A 95 18320 11677 11006 -1253 827 -1009 C ATOM 500 CD2 LEU A 95 9.917 21.961 55.542 1.00111.15 C ANISOU 500 CD2 LEU A 95 18394 12462 11377 -1563 655 -1155 C ATOM 501 N MET A 96 6.660 20.693 59.884 1.00103.50 N ANISOU 501 N MET A 96 17474 11548 10304 -998 570 -1016 N ATOM 502 CA MET A 96 6.024 21.014 61.168 1.00103.62 C ANISOU 502 CA MET A 96 17610 11524 10237 -942 598 -1037 C ATOM 503 C MET A 96 6.261 19.947 62.235 1.00107.77 C ANISOU 503 C MET A 96 17960 12248 10737 -903 488 -1030 C ATOM 504 O MET A 96 5.941 20.185 63.403 1.00108.07 O ANISOU 504 O MET A 96 18086 12282 10693 -884 500 -1062 O ATOM 505 CB MET A 96 4.520 21.253 60.985 1.00105.18 C ANISOU 505 CB MET A 96 17933 11561 10469 -727 684 -945 C ATOM 506 CG MET A 96 4.233 22.542 60.259 1.00109.82 C ANISOU 506 CG MET A 96 18763 11932 11032 -749 811 -965 C ATOM 507 SD MET A 96 2.525 23.084 60.386 1.00114.22 S ANISOU 507 SD MET A 96 19506 12318 11574 -495 920 -888 S ATOM 508 CE MET A 96 1.811 22.178 59.058 1.00109.18 C ANISOU 508 CE MET A 96 18686 11724 11072 -308 890 -760 C ATOM 509 N LYS A 97 6.826 18.781 61.840 1.00104.25 N ANISOU 509 N LYS A 97 17282 11972 10356 -882 386 -986 N ATOM 510 CA LYS A 97 7.143 17.621 62.703 1.00104.12 C ANISOU 510 CA LYS A 97 17095 12152 10316 -824 280 -965 C ATOM 511 C LYS A 97 5.892 17.116 63.486 1.00108.07 C ANISOU 511 C LYS A 97 17631 12610 10821 -631 302 -882 C ATOM 512 O LYS A 97 6.034 16.526 64.560 1.00108.38 O ANISOU 512 O LYS A 97 17617 12767 10796 -595 246 -886 O ATOM 513 CB LYS A 97 8.308 17.945 63.677 1.00107.84 C ANISOU 513 CB LYS A 97 17549 12770 10654 -994 224 -1094 C ATOM 514 CG LYS A 97 9.545 18.582 63.033 1.00123.68 C ANISOU 514 CG LYS A 97 19530 14828 12633 -1218 218 -1203 C ATOM 515 CD LYS A 97 10.494 17.560 62.421 1.00135.63 C ANISOU 515 CD LYS A 97 20800 16542 14191 -1226 114 -1183 C ATOM 516 CE LYS A 97 11.581 18.208 61.599 1.00150.74 C ANISOU 516 CE LYS A 97 22689 18492 16094 -1442 126 -1282 C ATOM 517 NZ LYS A 97 12.625 18.847 62.446 1.00164.99 N ANISOU 517 NZ LYS A 97 24497 20437 17755 -1653 103 -1443 N ATOM 518 N MET A 98 4.676 17.339 62.923 1.00103.64 N ANISOU 518 N MET A 98 17155 11894 10331 -505 385 -808 N ATOM 519 CA MET A 98 3.372 16.985 63.506 1.00102.37 C ANISOU 519 CA MET A 98 17031 11686 10180 -330 426 -736 C ATOM 520 C MET A 98 2.243 17.021 62.457 1.00100.95 C ANISOU 520 C MET A 98 16867 11393 10096 -197 497 -655 C ATOM 521 O MET A 98 2.426 17.581 61.367 1.00101.51 O ANISOU 521 O MET A 98 16973 11387 10208 -239 528 -661 O ATOM 522 CB MET A 98 3.030 17.953 64.656 1.00106.59 C ANISOU 522 CB MET A 98 17756 12142 10601 -351 485 -802 C ATOM 523 CG MET A 98 2.731 19.370 64.183 1.00112.35 C ANISOU 523 CG MET A 98 18697 12686 11307 -394 590 -846 C ATOM 524 SD MET A 98 2.072 20.454 65.470 1.00119.61 S ANISOU 524 SD MET A 98 19860 13486 12099 -376 679 -906 S ATOM 525 CE MET A 98 0.483 19.667 65.784 1.00115.67 C ANISOU 525 CE MET A 98 19307 12991 11650 -123 707 -791 C ATOM 526 N TRP A 99 1.055 16.484 62.826 1.00 91.86 N ANISOU 526 N TRP A 99 15698 10238 8967 -39 528 -586 N ATOM 527 CA TRP A 99 -0.145 16.479 61.980 1.00 88.47 C ANISOU 527 CA TRP A 99 15266 9738 8611 103 594 -518 C ATOM 528 C TRP A 99 -1.157 17.555 62.489 1.00 92.30 C ANISOU 528 C TRP A 99 15942 10100 9026 189 695 -536 C ATOM 529 O TRP A 99 -1.580 17.539 63.652 1.00 91.94 O ANISOU 529 O TRP A 99 15949 10067 8915 227 712 -548 O ATOM 530 CB TRP A 99 -0.760 15.071 61.923 1.00 84.45 C ANISOU 530 CB TRP A 99 14585 9329 8174 207 567 -439 C ATOM 531 CG TRP A 99 -1.873 14.938 60.937 1.00 83.45 C ANISOU 531 CG TRP A 99 14412 9173 8123 331 622 -381 C ATOM 532 CD1 TRP A 99 -3.203 14.845 61.215 1.00 86.02 C ANISOU 532 CD1 TRP A 99 14744 9494 8444 466 688 -349 C ATOM 533 CD2 TRP A 99 -1.760 14.937 59.507 1.00 82.39 C ANISOU 533 CD2 TRP A 99 14213 9023 8069 334 617 -356 C ATOM 534 NE1 TRP A 99 -3.928 14.790 60.051 1.00 84.53 N ANISOU 534 NE1 TRP A 99 14491 9303 8324 554 720 -311 N ATOM 535 CE2 TRP A 99 -3.064 14.806 58.985 1.00 85.50 C ANISOU 535 CE2 TRP A 99 14570 9416 8502 478 676 -311 C ATOM 536 CE3 TRP A 99 -0.676 15.005 58.611 1.00 83.17 C ANISOU 536 CE3 TRP A 99 14271 9122 8206 228 568 -371 C ATOM 537 CZ2 TRP A 99 -3.316 14.713 57.610 1.00 83.68 C ANISOU 537 CZ2 TRP A 99 14264 9188 8344 525 682 -278 C ATOM 538 CZ3 TRP A 99 -0.931 14.932 57.250 1.00 83.49 C ANISOU 538 CZ3 TRP A 99 14250 9148 8324 273 580 -334 C ATOM 539 CH2 TRP A 99 -2.237 14.793 56.763 1.00 83.66 C ANISOU 539 CH2 TRP A 99 14238 9168 8379 423 634 -288 C ATOM 540 N THR A 100 -1.501 18.506 61.607 1.00 88.45 N ANISOU 540 N THR A 100 15569 9491 8545 227 764 -538 N ATOM 541 CA THR A 100 -2.367 19.646 61.931 1.00 89.26 C ANISOU 541 CA THR A 100 15880 9464 8572 321 867 -555 C ATOM 542 C THR A 100 -3.714 19.642 61.174 1.00 93.04 C ANISOU 542 C THR A 100 16335 9926 9091 525 930 -487 C ATOM 543 O THR A 100 -4.377 20.687 61.132 1.00 93.02 O ANISOU 543 O THR A 100 16511 9807 9023 626 1020 -495 O ATOM 544 CB THR A 100 -1.611 20.955 61.614 1.00 93.74 C ANISOU 544 CB THR A 100 16654 9886 9077 201 916 -625 C ATOM 545 OG1 THR A 100 -1.187 20.917 60.250 1.00 93.86 O ANISOU 545 OG1 THR A 100 16611 9885 9164 169 904 -601 O ATOM 546 CG2 THR A 100 -0.409 21.176 62.509 1.00 90.78 C ANISOU 546 CG2 THR A 100 16324 9536 8633 -3 873 -716 C ATOM 547 N PHE A 101 -4.132 18.470 60.618 1.00 89.12 N ANISOU 547 N PHE A 101 15623 9551 8688 590 886 -424 N ATOM 548 CA PHE A 101 -5.339 18.344 59.781 1.00 89.05 C ANISOU 548 CA PHE A 101 15548 9568 8720 767 933 -370 C ATOM 549 C PHE A 101 -6.424 17.385 60.354 1.00 94.33 C ANISOU 549 C PHE A 101 16074 10361 9406 871 941 -336 C ATOM 550 O PHE A 101 -7.427 17.113 59.683 1.00 93.69 O ANISOU 550 O PHE A 101 15896 10344 9358 1003 972 -300 O ATOM 551 CB PHE A 101 -4.933 17.907 58.347 1.00 89.74 C ANISOU 551 CB PHE A 101 15510 9686 8900 742 890 -337 C ATOM 552 CG PHE A 101 -3.849 18.772 57.729 1.00 91.44 C ANISOU 552 CG PHE A 101 15854 9788 9101 625 889 -371 C ATOM 553 CD1 PHE A 101 -4.132 20.063 57.281 1.00 94.65 C ANISOU 553 CD1 PHE A 101 16468 10051 9444 695 976 -383 C ATOM 554 CD2 PHE A 101 -2.537 18.316 57.641 1.00 92.73 C ANISOU 554 CD2 PHE A 101 15943 9989 9303 445 811 -396 C ATOM 555 CE1 PHE A 101 -3.126 20.872 56.742 1.00 95.80 C ANISOU 555 CE1 PHE A 101 16753 10079 9568 567 992 -421 C ATOM 556 CE2 PHE A 101 -1.528 19.131 57.106 1.00 95.93 C ANISOU 556 CE2 PHE A 101 16463 10300 9688 316 819 -440 C ATOM 557 CZ PHE A 101 -1.831 20.401 56.653 1.00 94.62 C ANISOU 557 CZ PHE A 101 16512 9979 9463 368 914 -453 C ATOM 558 N GLY A 102 -6.225 16.906 61.579 1.00 92.83 N ANISOU 558 N GLY A 102 15875 10211 9184 810 918 -352 N ATOM 559 CA GLY A 102 -7.179 16.026 62.251 1.00 92.72 C ANISOU 559 CA GLY A 102 15755 10300 9175 885 939 -326 C ATOM 560 C GLY A 102 -7.106 14.578 61.826 1.00 95.42 C ANISOU 560 C GLY A 102 15890 10757 9609 846 889 -285 C ATOM 561 O GLY A 102 -6.521 14.251 60.792 1.00 93.70 O ANISOU 561 O GLY A 102 15589 10551 9463 796 842 -268 O ATOM 562 N ASN A 103 -7.729 13.709 62.624 1.00 92.59 N ANISOU 562 N ASN A 103 15460 10477 9244 870 911 -269 N ATOM 563 CA ASN A 103 -7.707 12.263 62.447 1.00 91.54 C ANISOU 563 CA ASN A 103 15163 10437 9180 827 883 -233 C ATOM 564 C ASN A 103 -8.503 11.788 61.227 1.00 95.31 C ANISOU 564 C ASN A 103 15493 10985 9735 885 909 -210 C ATOM 565 O ASN A 103 -8.185 10.722 60.698 1.00 94.06 O ANISOU 565 O ASN A 103 15213 10878 9649 826 875 -185 O ATOM 566 CB ASN A 103 -8.193 11.557 63.721 1.00 91.39 C ANISOU 566 CB ASN A 103 15145 10465 9115 832 920 -227 C ATOM 567 CG ASN A 103 -7.097 11.220 64.724 1.00107.33 C ANISOU 567 CG ASN A 103 17227 12467 11087 743 861 -230 C ATOM 568 OD1 ASN A 103 -5.895 11.151 64.415 1.00 98.03 O ANISOU 568 OD1 ASN A 103 16043 11277 9927 661 781 -233 O ATOM 569 ND2 ASN A 103 -7.499 10.972 65.956 1.00101.36 N ANISOU 569 ND2 ASN A 103 16524 11726 10262 762 899 -231 N ATOM 570 N PHE A 104 -9.503 12.563 60.770 1.00 93.03 N ANISOU 570 N PHE A 104 15216 10705 9424 1007 969 -221 N ATOM 571 CA PHE A 104 -10.302 12.198 59.597 1.00 92.70 C ANISOU 571 CA PHE A 104 15026 10755 9440 1074 991 -210 C ATOM 572 C PHE A 104 -9.493 12.338 58.312 1.00 96.80 C ANISOU 572 C PHE A 104 15519 11238 10024 1036 931 -196 C ATOM 573 O PHE A 104 -9.448 11.378 57.543 1.00 96.61 O ANISOU 573 O PHE A 104 15348 11284 10075 994 906 -178 O ATOM 574 CB PHE A 104 -11.598 13.027 59.496 1.00 95.64 C ANISOU 574 CB PHE A 104 15416 11172 9751 1240 1068 -228 C ATOM 575 CG PHE A 104 -12.360 12.803 58.206 1.00 97.33 C ANISOU 575 CG PHE A 104 15475 11498 10007 1323 1082 -224 C ATOM 576 CD1 PHE A 104 -13.219 11.716 58.065 1.00100.56 C ANISOU 576 CD1 PHE A 104 15698 12060 10451 1313 1114 -233 C ATOM 577 CD2 PHE A 104 -12.194 13.661 57.121 1.00 99.58 C ANISOU 577 CD2 PHE A 104 15807 11739 10291 1403 1067 -217 C ATOM 578 CE1 PHE A 104 -13.894 11.491 56.867 1.00101.46 C ANISOU 578 CE1 PHE A 104 15657 12298 10597 1378 1122 -241 C ATOM 579 CE2 PHE A 104 -12.867 13.434 55.922 1.00102.50 C ANISOU 579 CE2 PHE A 104 16030 12226 10691 1486 1074 -215 C ATOM 580 CZ PHE A 104 -13.714 12.352 55.804 1.00100.74 C ANISOU 580 CZ PHE A 104 15606 12172 10501 1472 1097 -230 C ATOM 581 N TRP A 105 -8.902 13.536 58.054 1.00 93.94 N ANISOU 581 N TRP A 105 15306 10763 9626 1050 919 -207 N ATOM 582 CA TRP A 105 -8.111 13.789 56.846 1.00 93.50 C ANISOU 582 CA TRP A 105 15245 10660 9620 1011 873 -196 C ATOM 583 C TRP A 105 -6.867 12.892 56.820 1.00 94.39 C ANISOU 583 C TRP A 105 15292 10777 9796 853 793 -187 C ATOM 584 O TRP A 105 -6.454 12.490 55.737 1.00 94.49 O ANISOU 584 O TRP A 105 15212 10812 9878 820 755 -169 O ATOM 585 CB TRP A 105 -7.729 15.272 56.664 1.00 93.86 C ANISOU 585 CB TRP A 105 15492 10568 9602 1042 896 -215 C ATOM 586 CG TRP A 105 -6.939 15.524 55.402 1.00 95.20 C ANISOU 586 CG TRP A 105 15663 10689 9819 996 861 -205 C ATOM 587 CD1 TRP A 105 -5.607 15.815 55.316 1.00 98.13 C ANISOU 587 CD1 TRP A 105 16111 10976 10199 852 816 -223 C ATOM 588 CD2 TRP A 105 -7.402 15.366 54.047 1.00 94.95 C ANISOU 588 CD2 TRP A 105 15530 10713 9836 1082 864 -178 C ATOM 589 NE1 TRP A 105 -5.222 15.902 53.995 1.00 97.21 N ANISOU 589 NE1 TRP A 105 15959 10844 10133 844 798 -205 N ATOM 590 CE2 TRP A 105 -6.302 15.619 53.195 1.00 98.64 C ANISOU 590 CE2 TRP A 105 16034 11107 10339 988 824 -175 C ATOM 591 CE3 TRP A 105 -8.648 15.049 53.469 1.00 96.31 C ANISOU 591 CE3 TRP A 105 15576 11003 10015 1228 897 -163 C ATOM 592 CZ2 TRP A 105 -6.408 15.565 51.795 1.00 97.97 C ANISOU 592 CZ2 TRP A 105 15878 11049 10299 1042 817 -150 C ATOM 593 CZ3 TRP A 105 -8.757 15.012 52.087 1.00 97.77 C ANISOU 593 CZ3 TRP A 105 15683 11227 10238 1284 886 -143 C ATOM 594 CH2 TRP A 105 -7.647 15.261 51.265 1.00 98.14 C ANISOU 594 CH2 TRP A 105 15781 11185 10323 1194 846 -133 C ATOM 595 N CYS A 106 -6.318 12.526 57.996 1.00 87.51 N ANISOU 595 N CYS A 106 14457 9898 8894 772 769 -196 N ATOM 596 CA CYS A 106 -5.166 11.629 58.108 1.00 85.05 C ANISOU 596 CA CYS A 106 14083 9612 8622 650 693 -186 C ATOM 597 C CYS A 106 -5.465 10.286 57.433 1.00 88.84 C ANISOU 597 C CYS A 106 14390 10179 9184 649 684 -149 C ATOM 598 O CYS A 106 -4.660 9.851 56.607 1.00 87.92 O ANISOU 598 O CYS A 106 14205 10073 9127 589 630 -135 O ATOM 599 CB CYS A 106 -4.753 11.442 59.568 1.00 84.31 C ANISOU 599 CB CYS A 106 14059 9516 8460 601 678 -201 C ATOM 600 SG CYS A 106 -3.587 10.083 59.839 1.00 86.64 S ANISOU 600 SG CYS A 106 14260 9877 8783 504 596 -177 S ATOM 601 N GLU A 107 -6.622 9.648 57.763 1.00 86.36 N ANISOU 601 N GLU A 107 14010 9931 8870 707 745 -140 N ATOM 602 CA GLU A 107 -7.029 8.354 57.184 1.00 86.43 C ANISOU 602 CA GLU A 107 13869 10022 8949 691 757 -117 C ATOM 603 C GLU A 107 -7.434 8.492 55.711 1.00 90.18 C ANISOU 603 C GLU A 107 14247 10535 9483 733 760 -116 C ATOM 604 O GLU A 107 -7.187 7.576 54.935 1.00 89.47 O ANISOU 604 O GLU A 107 14049 10484 9460 686 737 -100 O ATOM 605 CB GLU A 107 -8.169 7.690 57.973 1.00 88.47 C ANISOU 605 CB GLU A 107 14091 10343 9180 720 836 -120 C ATOM 606 CG GLU A 107 -7.773 7.238 59.370 1.00 99.11 C ANISOU 606 CG GLU A 107 15522 11663 10473 677 837 -111 C ATOM 607 CD GLU A 107 -8.632 6.164 60.012 1.00114.65 C ANISOU 607 CD GLU A 107 17447 13685 12430 667 915 -103 C ATOM 608 OE1 GLU A 107 -8.049 5.152 60.465 1.00104.85 O ANISOU 608 OE1 GLU A 107 16219 12430 11189 609 904 -75 O ATOM 609 OE2 GLU A 107 -9.870 6.341 60.098 1.00103.50 O ANISOU 609 OE2 GLU A 107 15995 12332 11000 720 993 -128 O ATOM 610 N PHE A 108 -8.045 9.625 55.333 1.00 87.16 N ANISOU 610 N PHE A 108 13911 10141 9067 831 790 -134 N ATOM 611 CA PHE A 108 -8.473 9.894 53.962 1.00 87.01 C ANISOU 611 CA PHE A 108 13815 10163 9083 899 794 -133 C ATOM 612 C PHE A 108 -7.255 10.117 53.044 1.00 85.73 C ANISOU 612 C PHE A 108 13674 9932 8966 835 726 -118 C ATOM 613 O PHE A 108 -7.220 9.566 51.950 1.00 84.04 O ANISOU 613 O PHE A 108 13347 9769 8816 825 706 -106 O ATOM 614 CB PHE A 108 -9.438 11.099 53.918 1.00 91.03 C ANISOU 614 CB PHE A 108 14394 10673 9519 1049 850 -151 C ATOM 615 CG PHE A 108 -10.428 11.006 52.783 1.00 94.45 C ANISOU 615 CG PHE A 108 14694 11225 9967 1153 877 -156 C ATOM 616 CD1 PHE A 108 -11.532 10.162 52.866 1.00 99.75 C ANISOU 616 CD1 PHE A 108 15209 12046 10643 1174 922 -178 C ATOM 617 CD2 PHE A 108 -10.234 11.725 51.611 1.00 98.00 C ANISOU 617 CD2 PHE A 108 15170 11647 10420 1223 859 -146 C ATOM 618 CE1 PHE A 108 -12.425 10.042 51.795 1.00101.55 C ANISOU 618 CE1 PHE A 108 15293 12413 10877 1262 941 -195 C ATOM 619 CE2 PHE A 108 -11.127 11.608 50.541 1.00101.90 C ANISOU 619 CE2 PHE A 108 15531 12269 10918 1329 876 -153 C ATOM 620 CZ PHE A 108 -12.214 10.762 50.638 1.00100.61 C ANISOU 620 CZ PHE A 108 15195 12273 10757 1346 913 -181 C ATOM 621 N TRP A 109 -6.255 10.876 53.521 1.00 80.30 N ANISOU 621 N TRP A 109 13127 9139 8244 781 695 -125 N ATOM 622 CA TRP A 109 -4.995 11.210 52.866 1.00 79.21 C ANISOU 622 CA TRP A 109 13028 8935 8132 698 638 -123 C ATOM 623 C TRP A 109 -4.159 9.945 52.565 1.00 82.75 C ANISOU 623 C TRP A 109 13352 9435 8653 598 576 -103 C ATOM 624 O TRP A 109 -3.605 9.839 51.479 1.00 82.02 O ANISOU 624 O TRP A 109 13207 9344 8613 568 542 -93 O ATOM 625 CB TRP A 109 -4.214 12.189 53.767 1.00 78.65 C ANISOU 625 CB TRP A 109 13129 8765 7991 640 631 -152 C ATOM 626 CG TRP A 109 -2.809 12.503 53.343 1.00 79.60 C ANISOU 626 CG TRP A 109 13287 8834 8124 521 576 -167 C ATOM 627 CD1 TRP A 109 -2.420 13.224 52.253 1.00 82.36 C ANISOU 627 CD1 TRP A 109 13682 9124 8487 511 580 -170 C ATOM 628 CD2 TRP A 109 -1.610 12.196 54.072 1.00 79.43 C ANISOU 628 CD2 TRP A 109 13271 8824 8087 395 516 -188 C ATOM 629 NE1 TRP A 109 -1.046 13.309 52.208 1.00 81.67 N ANISOU 629 NE1 TRP A 109 13611 9016 8403 371 528 -194 N ATOM 630 CE2 TRP A 109 -0.522 12.686 53.312 1.00 82.94 C ANISOU 630 CE2 TRP A 109 13739 9232 8544 302 483 -208 C ATOM 631 CE3 TRP A 109 -1.347 11.538 55.291 1.00 80.72 C ANISOU 631 CE3 TRP A 109 13417 9037 8217 359 487 -193 C ATOM 632 CZ2 TRP A 109 0.809 12.533 53.723 1.00 82.23 C ANISOU 632 CZ2 TRP A 109 13637 9173 8435 170 419 -240 C ATOM 633 CZ3 TRP A 109 -0.028 11.393 55.700 1.00 82.42 C ANISOU 633 CZ3 TRP A 109 13629 9279 8408 246 420 -219 C ATOM 634 CH2 TRP A 109 1.033 11.891 54.922 1.00 83.05 C ANISOU 634 CH2 TRP A 109 13714 9341 8501 151 385 -246 C ATOM 635 N THR A 110 -4.078 8.994 53.517 1.00 79.99 N ANISOU 635 N THR A 110 12969 9125 8300 558 567 -95 N ATOM 636 CA THR A 110 -3.325 7.741 53.386 1.00 79.30 C ANISOU 636 CA THR A 110 12788 9080 8261 486 519 -72 C ATOM 637 C THR A 110 -3.986 6.842 52.322 1.00 84.69 C ANISOU 637 C THR A 110 13336 9826 9018 510 541 -53 C ATOM 638 O THR A 110 -3.283 6.175 51.557 1.00 84.86 O ANISOU 638 O THR A 110 13286 9864 9095 463 499 -36 O ATOM 639 CB THR A 110 -3.225 7.028 54.752 1.00 84.06 C ANISOU 639 CB THR A 110 13421 9698 8819 465 523 -65 C ATOM 640 OG1 THR A 110 -2.839 7.956 55.766 1.00 84.55 O ANISOU 640 OG1 THR A 110 13608 9715 8803 453 512 -92 O ATOM 641 CG2 THR A 110 -2.234 5.891 54.746 1.00 80.46 C ANISOU 641 CG2 THR A 110 12910 9273 8388 409 470 -38 C ATOM 642 N SER A 111 -5.337 6.837 52.283 1.00 81.37 N ANISOU 642 N SER A 111 12875 9453 8591 581 609 -64 N ATOM 643 CA SER A 111 -6.168 6.079 51.346 1.00 80.30 C ANISOU 643 CA SER A 111 12603 9399 8507 600 642 -65 C ATOM 644 C SER A 111 -5.964 6.540 49.892 1.00 82.61 C ANISOU 644 C SER A 111 12848 9698 8842 626 612 -64 C ATOM 645 O SER A 111 -5.853 5.686 49.014 1.00 81.90 O ANISOU 645 O SER A 111 12653 9653 8813 590 598 -56 O ATOM 646 CB SER A 111 -7.640 6.202 51.722 1.00 83.90 C ANISOU 646 CB SER A 111 13028 9927 8925 673 721 -91 C ATOM 647 OG SER A 111 -7.956 5.483 52.902 1.00 88.07 O ANISOU 647 OG SER A 111 13574 10464 9424 635 764 -92 O ATOM 648 N ILE A 112 -5.905 7.875 49.646 1.00 78.67 N ANISOU 648 N ILE A 112 12440 9146 8304 689 607 -70 N ATOM 649 CA ILE A 112 -5.687 8.478 48.316 1.00 77.85 C ANISOU 649 CA ILE A 112 12326 9030 8224 726 587 -65 C ATOM 650 C ILE A 112 -4.267 8.134 47.817 1.00 79.59 C ANISOU 650 C ILE A 112 12540 9204 8496 620 520 -48 C ATOM 651 O ILE A 112 -4.104 7.791 46.653 1.00 81.09 O ANISOU 651 O ILE A 112 12647 9426 8738 615 500 -38 O ATOM 652 CB ILE A 112 -5.963 10.011 48.315 1.00 81.93 C ANISOU 652 CB ILE A 112 12984 9477 8669 824 617 -74 C ATOM 653 CG1 ILE A 112 -7.456 10.318 48.561 1.00 82.65 C ANISOU 653 CG1 ILE A 112 13054 9645 8705 962 683 -90 C ATOM 654 CG2 ILE A 112 -5.495 10.669 47.012 1.00 83.39 C ANISOU 654 CG2 ILE A 112 13198 9619 8868 849 600 -62 C ATOM 655 CD1 ILE A 112 -7.739 11.755 49.027 1.00 86.82 C ANISOU 655 CD1 ILE A 112 13758 10087 9141 1065 725 -97 C ATOM 656 N ASP A 113 -3.269 8.209 48.694 1.00 73.68 N ANISOU 656 N ASP A 113 11869 8398 7727 540 486 -49 N ATOM 657 CA ASP A 113 -1.865 7.865 48.458 1.00 72.51 C ANISOU 657 CA ASP A 113 11708 8232 7610 439 421 -42 C ATOM 658 C ASP A 113 -1.738 6.403 47.944 1.00 76.64 C ANISOU 658 C ASP A 113 12095 8824 8202 410 400 -18 C ATOM 659 O ASP A 113 -1.199 6.162 46.861 1.00 75.06 O ANISOU 659 O ASP A 113 11832 8635 8052 385 369 -8 O ATOM 660 CB ASP A 113 -1.116 8.034 49.801 1.00 74.18 C ANISOU 660 CB ASP A 113 12007 8414 7765 379 396 -56 C ATOM 661 CG ASP A 113 0.397 8.117 49.777 1.00 80.10 C ANISOU 661 CG ASP A 113 12767 9156 8510 279 330 -68 C ATOM 662 OD1 ASP A 113 1.022 7.475 48.903 1.00 79.52 O ANISOU 662 OD1 ASP A 113 12602 9119 8493 247 292 -51 O ATOM 663 OD2 ASP A 113 0.962 8.735 50.691 1.00 84.67 O ANISOU 663 OD2 ASP A 113 13436 9708 9025 231 316 -98 O ATOM 664 N VAL A 114 -2.275 5.443 48.725 1.00 74.29 N ANISOU 664 N VAL A 114 11765 8563 7899 414 428 -11 N ATOM 665 CA VAL A 114 -2.272 4.010 48.440 1.00 73.49 C ANISOU 665 CA VAL A 114 11570 8507 7847 385 432 8 C ATOM 666 C VAL A 114 -2.964 3.767 47.091 1.00 78.80 C ANISOU 666 C VAL A 114 12138 9228 8575 409 454 2 C ATOM 667 O VAL A 114 -2.389 3.060 46.264 1.00 79.13 O ANISOU 667 O VAL A 114 12115 9283 8667 372 426 16 O ATOM 668 CB VAL A 114 -2.912 3.203 49.611 1.00 76.94 C ANISOU 668 CB VAL A 114 12026 8957 8250 386 484 12 C ATOM 669 CG1 VAL A 114 -3.222 1.772 49.209 1.00 76.37 C ANISOU 669 CG1 VAL A 114 11876 8919 8222 356 520 24 C ATOM 670 CG2 VAL A 114 -2.009 3.211 50.842 1.00 76.96 C ANISOU 670 CG2 VAL A 114 12120 8925 8196 364 448 24 C ATOM 671 N LEU A 115 -4.155 4.394 46.858 1.00 75.68 N ANISOU 671 N LEU A 115 11726 8869 8160 479 501 -21 N ATOM 672 CA LEU A 115 -4.978 4.299 45.633 1.00 74.84 C ANISOU 672 CA LEU A 115 11513 8839 8085 522 524 -37 C ATOM 673 C LEU A 115 -4.231 4.803 44.403 1.00 77.44 C ANISOU 673 C LEU A 115 11835 9144 8446 528 474 -24 C ATOM 674 O LEU A 115 -4.377 4.215 43.332 1.00 76.60 O ANISOU 674 O LEU A 115 11627 9093 8385 521 471 -28 O ATOM 675 CB LEU A 115 -6.309 5.087 45.791 1.00 75.41 C ANISOU 675 CB LEU A 115 11582 8967 8102 624 578 -65 C ATOM 676 CG LEU A 115 -7.144 5.408 44.521 1.00 78.75 C ANISOU 676 CG LEU A 115 11909 9485 8527 710 592 -86 C ATOM 677 CD1 LEU A 115 -7.743 4.160 43.913 1.00 78.59 C ANISOU 677 CD1 LEU A 115 11734 9577 8549 660 617 -113 C ATOM 678 CD2 LEU A 115 -8.235 6.398 44.822 1.00 78.52 C ANISOU 678 CD2 LEU A 115 11908 9504 8423 838 636 -107 C ATOM 679 N CYS A 116 -3.445 5.886 44.552 1.00 74.19 N ANISOU 679 N CYS A 116 11534 8649 8006 531 444 -15 N ATOM 680 CA CYS A 116 -2.678 6.481 43.449 1.00 73.52 C ANISOU 680 CA CYS A 116 11466 8527 7942 526 408 -5 C ATOM 681 C CYS A 116 -1.538 5.558 43.018 1.00 78.26 C ANISOU 681 C CYS A 116 12005 9131 8601 434 357 11 C ATOM 682 O CYS A 116 -1.322 5.421 41.818 1.00 78.82 O ANISOU 682 O CYS A 116 12015 9222 8712 434 340 18 O ATOM 683 CB CYS A 116 -2.167 7.877 43.807 1.00 73.51 C ANISOU 683 CB CYS A 116 11618 8429 7884 532 408 -9 C ATOM 684 SG CYS A 116 -3.402 9.188 43.611 1.00 77.45 S ANISOU 684 SG CYS A 116 12204 8911 8311 683 471 -18 S ATOM 685 N VAL A 117 -0.844 4.903 43.977 1.00 74.96 N ANISOU 685 N VAL A 117 11600 8701 8179 369 333 18 N ATOM 686 CA VAL A 117 0.264 3.976 43.693 1.00 74.19 C ANISOU 686 CA VAL A 117 11451 8618 8122 304 285 35 C ATOM 687 C VAL A 117 -0.300 2.675 43.100 1.00 78.95 C ANISOU 687 C VAL A 117 11950 9273 8776 308 310 44 C ATOM 688 O VAL A 117 0.276 2.150 42.139 1.00 78.88 O ANISOU 688 O VAL A 117 11878 9280 8813 284 284 54 O ATOM 689 CB VAL A 117 1.169 3.707 44.933 1.00 77.69 C ANISOU 689 CB VAL A 117 11946 9048 8526 259 252 40 C ATOM 690 CG1 VAL A 117 2.257 2.665 44.631 1.00 77.15 C ANISOU 690 CG1 VAL A 117 11816 9012 8485 222 206 61 C ATOM 691 CG2 VAL A 117 1.797 4.997 45.443 1.00 77.61 C ANISOU 691 CG2 VAL A 117 12032 8995 8461 230 230 17 C ATOM 692 N THR A 118 -1.428 2.173 43.657 1.00 75.23 N ANISOU 692 N THR A 118 11464 8830 8292 330 368 33 N ATOM 693 CA THR A 118 -2.067 0.939 43.198 1.00 74.24 C ANISOU 693 CA THR A 118 11253 8753 8204 311 411 26 C ATOM 694 C THR A 118 -2.570 1.090 41.754 1.00 77.25 C ANISOU 694 C THR A 118 11541 9190 8622 334 414 7 C ATOM 695 O THR A 118 -2.226 0.241 40.932 1.00 77.07 O ANISOU 695 O THR A 118 11456 9182 8644 298 406 11 O ATOM 696 CB THR A 118 -3.174 0.493 44.154 1.00 78.89 C ANISOU 696 CB THR A 118 11850 9364 8760 312 483 7 C ATOM 697 OG1 THR A 118 -2.621 0.395 45.465 1.00 76.03 O ANISOU 697 OG1 THR A 118 11584 8947 8356 300 475 29 O ATOM 698 CG2 THR A 118 -3.763 -0.856 43.769 1.00 77.71 C ANISOU 698 CG2 THR A 118 11631 9255 8642 262 542 -9 C ATOM 699 N ALA A 119 -3.333 2.168 41.432 1.00 73.33 N ANISOU 699 N ALA A 119 11041 8723 8097 405 425 -12 N ATOM 700 CA ALA A 119 -3.852 2.401 40.065 1.00 72.16 C ANISOU 700 CA ALA A 119 10808 8644 7966 451 426 -29 C ATOM 701 C ALA A 119 -2.725 2.647 39.043 1.00 74.69 C ANISOU 701 C ALA A 119 11135 8922 8323 436 370 -4 C ATOM 702 O ALA A 119 -2.890 2.267 37.891 1.00 75.16 O ANISOU 702 O ALA A 119 11108 9035 8412 441 367 -13 O ATOM 703 CB ALA A 119 -4.833 3.567 40.049 1.00 73.08 C ANISOU 703 CB ALA A 119 10943 8799 8025 560 451 -47 C ATOM 704 N SER A 120 -1.581 3.232 39.468 1.00 70.19 N ANISOU 704 N SER A 120 10659 8266 7744 407 330 21 N ATOM 705 CA SER A 120 -0.424 3.527 38.614 1.00 69.56 C ANISOU 705 CA SER A 120 10590 8150 7690 376 283 39 C ATOM 706 C SER A 120 0.290 2.263 38.086 1.00 74.52 C ANISOU 706 C SER A 120 11138 8801 8374 315 258 50 C ATOM 707 O SER A 120 0.529 2.186 36.884 1.00 75.94 O ANISOU 707 O SER A 120 11265 9001 8586 317 243 53 O ATOM 708 CB SER A 120 0.583 4.410 39.347 1.00 72.28 C ANISOU 708 CB SER A 120 11046 8419 8000 338 256 46 C ATOM 709 OG SER A 120 0.096 5.735 39.496 1.00 77.28 O ANISOU 709 OG SER A 120 11776 9007 8580 394 284 37 O ATOM 710 N ILE A 121 0.639 1.296 38.953 1.00 70.08 N ANISOU 710 N ILE A 121 10579 8233 7817 273 257 59 N ATOM 711 CA ILE A 121 1.339 0.070 38.542 1.00 68.75 C ANISOU 711 CA ILE A 121 10359 8075 7688 234 242 75 C ATOM 712 C ILE A 121 0.370 -0.891 37.830 1.00 74.85 C ANISOU 712 C ILE A 121 11053 8895 8493 232 290 55 C ATOM 713 O ILE A 121 0.810 -1.669 36.975 1.00 75.02 O ANISOU 713 O ILE A 121 11024 8928 8553 209 282 61 O ATOM 714 CB ILE A 121 2.082 -0.608 39.742 1.00 71.11 C ANISOU 714 CB ILE A 121 10710 8349 7961 212 229 96 C ATOM 715 CG1 ILE A 121 2.922 -1.855 39.330 1.00 70.74 C ANISOU 715 CG1 ILE A 121 10629 8308 7940 197 214 118 C ATOM 716 CG2 ILE A 121 1.137 -0.945 40.888 1.00 71.15 C ANISOU 716 CG2 ILE A 121 10758 8344 7932 222 283 89 C ATOM 717 CD1 ILE A 121 4.159 -1.600 38.550 1.00 70.74 C ANISOU 717 CD1 ILE A 121 10595 8324 7957 185 154 128 C ATOM 718 N TRP A 122 -0.928 -0.853 38.181 1.00 72.61 N ANISOU 718 N TRP A 122 10753 8647 8189 249 344 26 N ATOM 719 CA TRP A 122 -1.894 -1.729 37.530 1.00 73.08 C ANISOU 719 CA TRP A 122 10726 8773 8269 227 397 -10 C ATOM 720 C TRP A 122 -2.151 -1.254 36.086 1.00 77.16 C ANISOU 720 C TRP A 122 11160 9353 8803 263 376 -28 C ATOM 721 O TRP A 122 -2.296 -2.108 35.211 1.00 77.22 O ANISOU 721 O TRP A 122 11095 9402 8842 227 392 -49 O ATOM 722 CB TRP A 122 -3.184 -1.881 38.346 1.00 73.00 C ANISOU 722 CB TRP A 122 10706 8806 8223 224 465 -46 C ATOM 723 CG TRP A 122 -3.110 -2.988 39.366 1.00 75.08 C ANISOU 723 CG TRP A 122 11029 9020 8480 163 515 -38 C ATOM 724 CD1 TRP A 122 -2.973 -2.849 40.717 1.00 78.27 C ANISOU 724 CD1 TRP A 122 11524 9370 8844 171 524 -16 C ATOM 725 CD2 TRP A 122 -3.065 -4.402 39.103 1.00 75.40 C ANISOU 725 CD2 TRP A 122 11061 9045 8544 92 564 -47 C ATOM 726 NE1 TRP A 122 -2.886 -4.083 41.318 1.00 77.89 N ANISOU 726 NE1 TRP A 122 11527 9277 8790 119 578 -7 N ATOM 727 CE2 TRP A 122 -2.952 -5.057 40.353 1.00 80.01 C ANISOU 727 CE2 TRP A 122 11743 9560 9095 68 609 -26 C ATOM 728 CE3 TRP A 122 -3.136 -5.185 37.930 1.00 76.85 C ANISOU 728 CE3 TRP A 122 11174 9262 8765 48 583 -73 C ATOM 729 CZ2 TRP A 122 -2.918 -6.463 40.467 1.00 80.01 C ANISOU 729 CZ2 TRP A 122 11791 9512 9097 5 681 -26 C ATOM 730 CZ3 TRP A 122 -3.102 -6.575 38.044 1.00 78.66 C ANISOU 730 CZ3 TRP A 122 11444 9443 8999 -25 652 -79 C ATOM 731 CH2 TRP A 122 -3.004 -7.200 39.299 1.00 79.82 C ANISOU 731 CH2 TRP A 122 11706 9511 9111 -45 704 -54 C ATOM 732 N THR A 123 -2.120 0.084 35.819 1.00 73.42 N ANISOU 732 N THR A 123 10715 8877 8305 333 345 -18 N ATOM 733 CA THR A 123 -2.276 0.642 34.460 1.00 73.33 C ANISOU 733 CA THR A 123 10651 8915 8297 387 326 -26 C ATOM 734 C THR A 123 -1.021 0.367 33.633 1.00 76.51 C ANISOU 734 C THR A 123 11053 9272 8744 347 281 3 C ATOM 735 O THR A 123 -1.140 0.171 32.420 1.00 77.19 O ANISOU 735 O THR A 123 11069 9411 8849 360 275 -9 O ATOM 736 CB THR A 123 -2.615 2.140 34.435 1.00 81.63 C ANISOU 736 CB THR A 123 11764 9957 9294 485 321 -18 C ATOM 737 OG1 THR A 123 -1.653 2.864 35.191 1.00 84.22 O ANISOU 737 OG1 THR A 123 12212 10176 9611 465 297 14 O ATOM 738 CG2 THR A 123 -4.004 2.435 34.941 1.00 78.61 C ANISOU 738 CG2 THR A 123 11354 9653 8859 554 366 -52 C ATOM 739 N LEU A 124 0.168 0.329 34.275 1.00 71.15 N ANISOU 739 N LEU A 124 10443 8515 8076 301 250 35 N ATOM 740 CA LEU A 124 1.424 0.005 33.581 1.00 70.12 C ANISOU 740 CA LEU A 124 10301 8359 7981 263 209 58 C ATOM 741 C LEU A 124 1.405 -1.447 33.161 1.00 76.32 C ANISOU 741 C LEU A 124 11020 9174 8806 225 226 50 C ATOM 742 O LEU A 124 1.928 -1.781 32.102 1.00 77.31 O ANISOU 742 O LEU A 124 11100 9312 8962 214 208 54 O ATOM 743 CB LEU A 124 2.672 0.303 34.437 1.00 69.30 C ANISOU 743 CB LEU A 124 10269 8198 7864 227 171 83 C ATOM 744 CG LEU A 124 3.064 1.775 34.574 1.00 72.20 C ANISOU 744 CG LEU A 124 10714 8522 8195 234 154 86 C ATOM 745 CD1 LEU A 124 4.152 1.949 35.611 1.00 71.64 C ANISOU 745 CD1 LEU A 124 10699 8422 8100 182 122 92 C ATOM 746 CD2 LEU A 124 3.470 2.371 33.227 1.00 71.70 C ANISOU 746 CD2 LEU A 124 10639 8457 8145 240 143 90 C ATOM 747 N CYS A 125 0.763 -2.299 33.980 1.00 73.45 N ANISOU 747 N CYS A 125 10660 8813 8435 201 272 35 N ATOM 748 CA CYS A 125 0.581 -3.726 33.730 1.00 73.24 C ANISOU 748 CA CYS A 125 10600 8795 8433 155 313 21 C ATOM 749 C CYS A 125 -0.357 -3.942 32.511 1.00 77.60 C ANISOU 749 C CYS A 125 11054 9431 9001 148 341 -27 C ATOM 750 O CYS A 125 -0.055 -4.763 31.652 1.00 77.71 O ANISOU 750 O CYS A 125 11031 9452 9045 117 347 -35 O ATOM 751 CB CYS A 125 0.042 -4.409 34.981 1.00 73.50 C ANISOU 751 CB CYS A 125 10685 8800 8440 126 370 14 C ATOM 752 SG CYS A 125 0.159 -6.209 34.943 1.00 77.52 S ANISOU 752 SG CYS A 125 11219 9270 8965 64 436 10 S ATOM 753 N VAL A 126 -1.454 -3.175 32.433 1.00 73.92 N ANISOU 753 N VAL A 126 10545 9036 8505 188 355 -60 N ATOM 754 CA VAL A 126 -2.453 -3.197 31.364 1.00 73.84 C ANISOU 754 CA VAL A 126 10428 9140 8488 203 374 -113 C ATOM 755 C VAL A 126 -1.793 -2.786 30.016 1.00 78.46 C ANISOU 755 C VAL A 126 10983 9735 9093 241 323 -95 C ATOM 756 O VAL A 126 -2.077 -3.423 28.987 1.00 78.65 O ANISOU 756 O VAL A 126 10926 9827 9132 217 335 -130 O ATOM 757 CB VAL A 126 -3.668 -2.299 31.741 1.00 77.52 C ANISOU 757 CB VAL A 126 10864 9690 8900 271 393 -144 C ATOM 758 CG1 VAL A 126 -4.595 -2.068 30.554 1.00 77.48 C ANISOU 758 CG1 VAL A 126 10740 9830 8868 323 396 -195 C ATOM 759 CG2 VAL A 126 -4.449 -2.896 32.918 1.00 77.41 C ANISOU 759 CG2 VAL A 126 10857 9688 8867 216 458 -176 C ATOM 760 N ILE A 127 -0.879 -1.781 30.038 1.00 73.82 N ANISOU 760 N ILE A 127 10466 9079 8503 286 274 -44 N ATOM 761 CA ILE A 127 -0.132 -1.313 28.859 1.00 72.69 C ANISOU 761 CA ILE A 127 10317 8929 8374 314 233 -21 C ATOM 762 C ILE A 127 0.784 -2.448 28.340 1.00 75.44 C ANISOU 762 C ILE A 127 10641 9251 8773 247 224 -12 C ATOM 763 O ILE A 127 0.865 -2.629 27.129 1.00 76.05 O ANISOU 763 O ILE A 127 10662 9369 8864 254 214 -23 O ATOM 764 CB ILE A 127 0.651 0.014 29.136 1.00 75.90 C ANISOU 764 CB ILE A 127 10823 9257 8759 351 201 22 C ATOM 765 CG1 ILE A 127 -0.333 1.185 29.380 1.00 77.00 C ANISOU 765 CG1 ILE A 127 10999 9420 8838 442 219 14 C ATOM 766 CG2 ILE A 127 1.641 0.378 27.993 1.00 75.72 C ANISOU 766 CG2 ILE A 127 10806 9210 8752 352 169 47 C ATOM 767 CD1 ILE A 127 0.271 2.424 30.112 1.00 82.94 C ANISOU 767 CD1 ILE A 127 11883 10073 9559 458 210 46 C ATOM 768 N ALA A 128 1.418 -3.236 29.236 1.00 71.36 N ANISOU 768 N ALA A 128 10168 8671 8272 195 230 6 N ATOM 769 CA ALA A 128 2.307 -4.352 28.863 1.00 70.61 C ANISOU 769 CA ALA A 128 10068 8547 8212 154 228 19 C ATOM 770 C ALA A 128 1.552 -5.490 28.155 1.00 73.48 C ANISOU 770 C ALA A 128 10371 8958 8592 113 278 -28 C ATOM 771 O ALA A 128 2.020 -6.001 27.138 1.00 72.04 O ANISOU 771 O ALA A 128 10155 8783 8433 101 270 -30 O ATOM 772 CB ALA A 128 3.018 -4.895 30.097 1.00 71.46 C ANISOU 772 CB ALA A 128 10251 8589 8314 136 229 51 C ATOM 773 N VAL A 129 0.385 -5.869 28.700 1.00 71.56 N ANISOU 773 N VAL A 129 10114 8748 8329 82 335 -72 N ATOM 774 CA VAL A 129 -0.490 -6.934 28.198 1.00 72.22 C ANISOU 774 CA VAL A 129 10142 8885 8415 15 399 -136 C ATOM 775 C VAL A 129 -1.101 -6.489 26.850 1.00 77.55 C ANISOU 775 C VAL A 129 10706 9677 9083 42 380 -179 C ATOM 776 O VAL A 129 -1.111 -7.296 25.913 1.00 77.82 O ANISOU 776 O VAL A 129 10695 9741 9133 -4 400 -214 O ATOM 777 CB VAL A 129 -1.552 -7.332 29.275 1.00 76.44 C ANISOU 777 CB VAL A 129 10691 9431 8920 -36 471 -176 C ATOM 778 CG1 VAL A 129 -2.609 -8.292 28.728 1.00 76.92 C ANISOU 778 CG1 VAL A 129 10680 9572 8972 -127 548 -263 C ATOM 779 CG2 VAL A 129 -0.874 -7.951 30.497 1.00 75.93 C ANISOU 779 CG2 VAL A 129 10749 9245 8854 -55 495 -129 C ATOM 780 N ASP A 130 -1.529 -5.199 26.735 1.00 73.83 N ANISOU 780 N ASP A 130 10204 9265 8581 126 343 -174 N ATOM 781 CA ASP A 130 -2.102 -4.609 25.507 1.00 73.19 C ANISOU 781 CA ASP A 130 10032 9301 8475 187 320 -205 C ATOM 782 C ASP A 130 -1.081 -4.557 24.341 1.00 74.87 C ANISOU 782 C ASP A 130 10247 9483 8716 206 276 -171 C ATOM 783 O ASP A 130 -1.448 -4.861 23.205 1.00 74.23 O ANISOU 783 O ASP A 130 10085 9492 8628 207 278 -213 O ATOM 784 CB ASP A 130 -2.665 -3.200 25.772 1.00 74.65 C ANISOU 784 CB ASP A 130 10226 9530 8609 297 297 -192 C ATOM 785 CG ASP A 130 -3.180 -2.508 24.528 1.00 79.67 C ANISOU 785 CG ASP A 130 10789 10281 9202 394 273 -211 C ATOM 786 OD1 ASP A 130 -4.175 -3.004 23.938 1.00 78.42 O ANISOU 786 OD1 ASP A 130 10513 10270 9015 384 296 -285 O ATOM 787 OD2 ASP A 130 -2.563 -1.498 24.115 1.00 85.13 O ANISOU 787 OD2 ASP A 130 11545 10920 9881 475 235 -157 O ATOM 788 N ARG A 131 0.177 -4.160 24.625 1.00 70.02 N ANISOU 788 N ARG A 131 9720 8758 8128 218 239 -103 N ATOM 789 CA ARG A 131 1.271 -4.118 23.646 1.00 68.91 C ANISOU 789 CA ARG A 131 9586 8584 8014 226 203 -69 C ATOM 790 C ARG A 131 1.665 -5.525 23.227 1.00 73.41 C ANISOU 790 C ARG A 131 10132 9140 8620 155 226 -88 C ATOM 791 O ARG A 131 2.091 -5.702 22.090 1.00 72.86 O ANISOU 791 O ARG A 131 10028 9092 8564 161 211 -89 O ATOM 792 CB ARG A 131 2.509 -3.369 24.196 1.00 67.10 C ANISOU 792 CB ARG A 131 9444 8258 7793 238 166 -6 C ATOM 793 CG ARG A 131 2.382 -1.852 24.326 1.00 67.93 C ANISOU 793 CG ARG A 131 9601 8351 7859 304 148 17 C ATOM 794 CD ARG A 131 2.065 -1.159 23.009 1.00 68.58 C ANISOU 794 CD ARG A 131 9656 8488 7914 373 140 13 C ATOM 795 NE ARG A 131 0.621 -0.972 22.885 1.00 72.05 N ANISOU 795 NE ARG A 131 10040 9028 8307 439 161 -29 N ATOM 796 CZ ARG A 131 -0.026 -0.765 21.749 1.00 76.85 C ANISOU 796 CZ ARG A 131 10587 9734 8879 508 159 -53 C ATOM 797 NH1 ARG A 131 0.638 -0.693 20.602 1.00 66.48 N ANISOU 797 NH1 ARG A 131 9271 8414 7574 520 141 -34 N ATOM 798 NH2 ARG A 131 -1.344 -0.630 21.748 1.00 58.97 N ANISOU 798 NH2 ARG A 131 8256 7588 6562 572 176 -99 N ATOM 799 N TYR A 132 1.529 -6.525 24.136 1.00 71.77 N ANISOU 799 N TYR A 132 9958 8889 8422 94 271 -101 N ATOM 800 CA TYR A 132 1.845 -7.931 23.831 1.00 72.12 C ANISOU 800 CA TYR A 132 10014 8900 8490 30 312 -119 C ATOM 801 C TYR A 132 0.865 -8.478 22.812 1.00 74.94 C ANISOU 801 C TYR A 132 10284 9353 8838 -14 349 -197 C ATOM 802 O TYR A 132 1.289 -9.136 21.875 1.00 75.16 O ANISOU 802 O TYR A 132 10296 9378 8882 -36 355 -208 O ATOM 803 CB TYR A 132 1.871 -8.832 25.097 1.00 73.94 C ANISOU 803 CB TYR A 132 10329 9047 8717 -16 365 -112 C ATOM 804 CG TYR A 132 2.092 -10.296 24.772 1.00 76.84 C ANISOU 804 CG TYR A 132 10735 9364 9095 -75 426 -132 C ATOM 805 CD1 TYR A 132 3.371 -10.791 24.533 1.00 78.92 C ANISOU 805 CD1 TYR A 132 11051 9560 9375 -42 406 -82 C ATOM 806 CD2 TYR A 132 1.012 -11.169 24.621 1.00 78.42 C ANISOU 806 CD2 TYR A 132 10919 9595 9283 -165 509 -209 C ATOM 807 CE1 TYR A 132 3.573 -12.121 24.151 1.00 79.42 C ANISOU 807 CE1 TYR A 132 11166 9568 9440 -81 469 -99 C ATOM 808 CE2 TYR A 132 1.202 -12.495 24.229 1.00 79.64 C ANISOU 808 CE2 TYR A 132 11129 9690 9441 -228 577 -234 C ATOM 809 CZ TYR A 132 2.487 -12.968 24.007 1.00 87.96 C ANISOU 809 CZ TYR A 132 12253 10659 10510 -177 558 -174 C ATOM 810 OH TYR A 132 2.692 -14.283 23.669 1.00 93.10 O ANISOU 810 OH TYR A 132 12982 11235 11156 -224 634 -194 O ATOM 811 N PHE A 133 -0.436 -8.244 23.012 1.00 71.51 N ANISOU 811 N PHE A 133 9788 9014 8370 -29 377 -256 N ATOM 812 CA PHE A 133 -1.481 -8.709 22.107 1.00 72.51 C ANISOU 812 CA PHE A 133 9809 9270 8473 -78 412 -347 C ATOM 813 C PHE A 133 -1.397 -8.036 20.732 1.00 76.99 C ANISOU 813 C PHE A 133 10298 9927 9027 -3 356 -349 C ATOM 814 O PHE A 133 -1.760 -8.649 19.740 1.00 77.04 O ANISOU 814 O PHE A 133 10234 10015 9024 -46 374 -412 O ATOM 815 CB PHE A 133 -2.863 -8.488 22.730 1.00 75.44 C ANISOU 815 CB PHE A 133 10117 9748 8799 -98 450 -412 C ATOM 816 CG PHE A 133 -3.234 -9.578 23.710 1.00 78.40 C ANISOU 816 CG PHE A 133 10548 10065 9177 -217 539 -449 C ATOM 817 CD1 PHE A 133 -3.447 -10.886 23.276 1.00 82.37 C ANISOU 817 CD1 PHE A 133 11050 10563 9683 -341 614 -516 C ATOM 818 CD2 PHE A 133 -3.376 -9.300 25.066 1.00 80.81 C ANISOU 818 CD2 PHE A 133 10919 10310 9474 -210 556 -417 C ATOM 819 CE1 PHE A 133 -3.792 -11.892 24.182 1.00 83.85 C ANISOU 819 CE1 PHE A 133 11317 10678 9865 -455 713 -550 C ATOM 820 CE2 PHE A 133 -3.734 -10.306 25.969 1.00 84.22 C ANISOU 820 CE2 PHE A 133 11416 10681 9900 -317 648 -449 C ATOM 821 CZ PHE A 133 -3.931 -11.595 25.523 1.00 83.03 C ANISOU 821 CZ PHE A 133 11279 10517 9752 -440 729 -513 C ATOM 822 N ALA A 134 -0.913 -6.793 20.685 1.00 74.36 N ANISOU 822 N ALA A 134 9991 9574 8688 103 294 -283 N ATOM 823 CA ALA A 134 -0.731 -6.021 19.469 1.00 74.61 C ANISOU 823 CA ALA A 134 9982 9666 8699 188 246 -268 C ATOM 824 C ALA A 134 0.440 -6.592 18.640 1.00 81.55 C ANISOU 824 C ALA A 134 10888 10476 9622 161 232 -239 C ATOM 825 O ALA A 134 0.259 -6.856 17.449 1.00 82.80 O ANISOU 825 O ALA A 134 10980 10713 9767 164 228 -276 O ATOM 826 CB ALA A 134 -0.484 -4.555 19.814 1.00 74.55 C ANISOU 826 CB ALA A 134 10034 9622 8669 294 205 -203 C ATOM 827 N ILE A 135 1.618 -6.822 19.281 1.00 76.96 N ANISOU 827 N ILE A 135 10396 9762 9084 137 225 -177 N ATOM 828 CA ILE A 135 2.858 -7.317 18.666 1.00 75.10 C ANISOU 828 CA ILE A 135 10188 9461 8884 124 211 -142 C ATOM 829 C ILE A 135 2.739 -8.784 18.225 1.00 78.80 C ANISOU 829 C ILE A 135 10641 9931 9368 48 261 -193 C ATOM 830 O ILE A 135 3.525 -9.217 17.381 1.00 78.98 O ANISOU 830 O ILE A 135 10665 9933 9409 48 253 -181 O ATOM 831 CB ILE A 135 4.067 -7.070 19.627 1.00 77.40 C ANISOU 831 CB ILE A 135 10565 9644 9199 133 188 -70 C ATOM 832 CG1 ILE A 135 5.388 -6.933 18.858 1.00 78.06 C ANISOU 832 CG1 ILE A 135 10657 9699 9302 153 154 -27 C ATOM 833 CG2 ILE A 135 4.184 -8.071 20.777 1.00 77.17 C ANISOU 833 CG2 ILE A 135 10594 9545 9182 84 227 -69 C ATOM 834 CD1 ILE A 135 5.797 -5.504 18.579 1.00 85.03 C ANISOU 834 CD1 ILE A 135 11553 10585 10168 201 114 11 C ATOM 835 N THR A 136 1.770 -9.544 18.761 1.00 75.25 N ANISOU 835 N THR A 136 10183 9502 8906 -23 320 -254 N ATOM 836 CA THR A 136 1.620 -10.952 18.372 1.00 75.07 C ANISOU 836 CA THR A 136 10169 9463 8889 -113 386 -311 C ATOM 837 C THR A 136 0.364 -11.130 17.492 1.00 81.37 C ANISOU 837 C THR A 136 10856 10411 9651 -163 412 -414 C ATOM 838 O THR A 136 -0.133 -12.246 17.344 1.00 83.20 O ANISOU 838 O THR A 136 11088 10649 9874 -269 484 -488 O ATOM 839 CB THR A 136 1.628 -11.875 19.592 1.00 75.96 C ANISOU 839 CB THR A 136 10383 9471 9009 -177 454 -308 C ATOM 840 OG1 THR A 136 0.513 -11.554 20.423 1.00 75.20 O ANISOU 840 OG1 THR A 136 10259 9426 8886 -208 480 -347 O ATOM 841 CG2 THR A 136 2.934 -11.806 20.378 1.00 72.57 C ANISOU 841 CG2 THR A 136 10053 8920 8601 -115 424 -213 C ATOM 842 N SER A 137 -0.119 -10.030 16.881 1.00 77.16 N ANISOU 842 N SER A 137 10231 9998 9086 -83 356 -420 N ATOM 843 CA SER A 137 -1.262 -10.030 15.971 1.00 76.92 C ANISOU 843 CA SER A 137 10075 10147 9005 -98 362 -515 C ATOM 844 C SER A 137 -0.801 -9.573 14.558 1.00 79.73 C ANISOU 844 C SER A 137 10387 10558 9349 -19 308 -497 C ATOM 845 O SER A 137 0.284 -8.976 14.417 1.00 77.09 O ANISOU 845 O SER A 137 10117 10130 9042 55 263 -407 O ATOM 846 CB SER A 137 -2.397 -9.150 16.512 1.00 80.30 C ANISOU 846 CB SER A 137 10433 10697 9382 -47 351 -543 C ATOM 847 OG SER A 137 -2.211 -7.761 16.282 1.00 87.98 O ANISOU 847 OG SER A 137 11405 11694 10331 100 282 -477 O ATOM 848 N PRO A 138 -1.607 -9.835 13.498 1.00 78.09 N ANISOU 848 N PRO A 138 10068 10510 9092 -37 313 -587 N ATOM 849 CA PRO A 138 -1.213 -9.389 12.153 1.00 78.68 C ANISOU 849 CA PRO A 138 10106 10642 9147 47 263 -569 C ATOM 850 C PRO A 138 -1.196 -7.864 11.994 1.00 85.20 C ANISOU 850 C PRO A 138 10933 11504 9935 207 200 -500 C ATOM 851 O PRO A 138 -0.651 -7.376 11.002 1.00 85.72 O ANISOU 851 O PRO A 138 11007 11576 9988 285 164 -461 O ATOM 852 CB PRO A 138 -2.275 -10.017 11.242 1.00 81.14 C ANISOU 852 CB PRO A 138 10288 11142 9399 -13 287 -696 C ATOM 853 CG PRO A 138 -2.959 -11.028 12.055 1.00 85.56 C ANISOU 853 CG PRO A 138 10840 11704 9966 -164 364 -780 C ATOM 854 CD PRO A 138 -2.896 -10.549 13.454 1.00 80.58 C ANISOU 854 CD PRO A 138 10281 10973 9361 -140 368 -715 C ATOM 855 N PHE A 139 -1.776 -7.117 12.959 1.00 82.79 N ANISOU 855 N PHE A 139 10634 11215 9606 257 195 -484 N ATOM 856 CA PHE A 139 -1.857 -5.650 12.932 1.00 83.48 C ANISOU 856 CA PHE A 139 10749 11322 9647 412 151 -421 C ATOM 857 C PHE A 139 -0.549 -4.998 13.457 1.00 88.16 C ANISOU 857 C PHE A 139 11483 11720 10294 437 134 -308 C ATOM 858 O PHE A 139 -0.290 -3.822 13.189 1.00 87.50 O ANISOU 858 O PHE A 139 11457 11614 10177 548 107 -248 O ATOM 859 CB PHE A 139 -3.089 -5.176 13.728 1.00 85.93 C ANISOU 859 CB PHE A 139 11005 11744 9901 456 161 -461 C ATOM 860 CG PHE A 139 -4.374 -5.864 13.307 1.00 88.79 C ANISOU 860 CG PHE A 139 11209 12323 10204 410 183 -588 C ATOM 861 CD1 PHE A 139 -4.998 -5.540 12.102 1.00 93.29 C ANISOU 861 CD1 PHE A 139 11673 13085 10689 507 153 -636 C ATOM 862 CD2 PHE A 139 -4.943 -6.855 14.098 1.00 91.29 C ANISOU 862 CD2 PHE A 139 11484 12660 10543 262 240 -665 C ATOM 863 CE1 PHE A 139 -6.182 -6.184 11.710 1.00 95.34 C ANISOU 863 CE1 PHE A 139 11767 13573 10883 453 173 -768 C ATOM 864 CE2 PHE A 139 -6.129 -7.493 13.710 1.00 95.60 C ANISOU 864 CE2 PHE A 139 11877 13418 11028 193 270 -797 C ATOM 865 CZ PHE A 139 -6.741 -7.152 12.518 1.00 94.59 C ANISOU 865 CZ PHE A 139 11625 13500 10814 286 233 -852 C ATOM 866 N LYS A 140 0.259 -5.801 14.179 1.00 85.09 N ANISOU 866 N LYS A 140 11153 11199 9979 330 155 -288 N ATOM 867 CA LYS A 140 1.586 -5.552 14.761 1.00 83.90 C ANISOU 867 CA LYS A 140 11111 10885 9883 317 143 -203 C ATOM 868 C LYS A 140 1.633 -4.376 15.786 1.00 88.08 C ANISOU 868 C LYS A 140 11715 11352 10398 374 130 -148 C ATOM 869 O LYS A 140 2.094 -4.604 16.909 1.00 87.56 O ANISOU 869 O LYS A 140 11706 11194 10370 321 139 -123 O ATOM 870 CB LYS A 140 2.659 -5.362 13.672 1.00 85.18 C ANISOU 870 CB LYS A 140 11296 11010 10058 343 120 -160 C ATOM 871 CG LYS A 140 4.039 -5.801 14.144 1.00 93.87 C ANISOU 871 CG LYS A 140 12464 11981 11220 285 120 -109 C ATOM 872 CD LYS A 140 4.951 -6.125 12.986 1.00102.31 C ANISOU 872 CD LYS A 140 13525 13042 12305 283 111 -94 C ATOM 873 CE LYS A 140 6.308 -6.559 13.466 1.00111.60 C ANISOU 873 CE LYS A 140 14752 14120 13530 241 110 -49 C ATOM 874 NZ LYS A 140 7.174 -6.989 12.342 1.00120.30 N ANISOU 874 NZ LYS A 140 15838 15225 14646 240 107 -41 N ATOM 875 N TYR A 141 1.218 -3.146 15.423 1.00 84.41 N ANISOU 875 N TYR A 141 11267 10931 9874 485 112 -127 N ATOM 876 CA TYR A 141 1.339 -1.999 16.339 1.00 83.59 C ANISOU 876 CA TYR A 141 11258 10749 9752 535 109 -76 C ATOM 877 C TYR A 141 -0.006 -1.346 16.692 1.00 86.49 C ANISOU 877 C TYR A 141 11600 11214 10049 628 117 -104 C ATOM 878 O TYR A 141 -0.034 -0.244 17.243 1.00 86.57 O ANISOU 878 O TYR A 141 11699 11168 10024 698 118 -63 O ATOM 879 CB TYR A 141 2.316 -0.960 15.759 1.00 84.50 C ANISOU 879 CB TYR A 141 11470 10782 9855 583 96 -10 C ATOM 880 CG TYR A 141 3.634 -1.573 15.338 1.00 85.86 C ANISOU 880 CG TYR A 141 11649 10887 10087 499 88 13 C ATOM 881 CD1 TYR A 141 4.464 -2.203 16.271 1.00 87.54 C ANISOU 881 CD1 TYR A 141 11880 11021 10359 406 87 25 C ATOM 882 CD2 TYR A 141 4.014 -1.608 14.001 1.00 86.09 C ANISOU 882 CD2 TYR A 141 11657 10946 10106 524 82 18 C ATOM 883 CE1 TYR A 141 5.656 -2.815 15.882 1.00 87.83 C ANISOU 883 CE1 TYR A 141 11912 11020 10441 348 80 43 C ATOM 884 CE2 TYR A 141 5.223 -2.180 13.606 1.00 86.45 C ANISOU 884 CE2 TYR A 141 11702 10941 10202 454 78 36 C ATOM 885 CZ TYR A 141 6.035 -2.791 14.549 1.00 92.83 C ANISOU 885 CZ TYR A 141 12523 11682 11067 370 76 47 C ATOM 886 OH TYR A 141 7.215 -3.373 14.162 1.00 93.09 O ANISOU 886 OH TYR A 141 12546 11685 11138 320 70 63 O ATOM 887 N GLN A 142 -1.105 -2.046 16.424 1.00 82.38 N ANISOU 887 N GLN A 142 10957 10841 9502 622 127 -181 N ATOM 888 CA GLN A 142 -2.428 -1.543 16.747 1.00 82.57 C ANISOU 888 CA GLN A 142 10928 10994 9452 711 135 -222 C ATOM 889 C GLN A 142 -3.058 -2.408 17.817 1.00 84.90 C ANISOU 889 C GLN A 142 11167 11318 9774 607 167 -279 C ATOM 890 O GLN A 142 -3.017 -3.639 17.722 1.00 84.54 O ANISOU 890 O GLN A 142 11064 11287 9772 483 189 -329 O ATOM 891 CB GLN A 142 -3.318 -1.493 15.497 1.00 84.90 C ANISOU 891 CB GLN A 142 11109 11482 9667 805 122 -277 C ATOM 892 CG GLN A 142 -3.272 -0.163 14.742 1.00103.86 C ANISOU 892 CG GLN A 142 13584 13889 11988 985 101 -219 C ATOM 893 CD GLN A 142 -4.259 -0.073 13.588 1.00129.91 C ANISOU 893 CD GLN A 142 16766 17407 15188 1108 85 -275 C ATOM 894 OE1 GLN A 142 -4.099 0.742 12.676 1.00126.97 O ANISOU 894 OE1 GLN A 142 16451 17043 14751 1245 71 -231 O ATOM 895 NE2 GLN A 142 -5.319 -0.881 13.600 1.00125.34 N ANISOU 895 NE2 GLN A 142 16022 17020 14583 1063 90 -378 N ATOM 896 N SER A 143 -3.638 -1.758 18.841 1.00 80.60 N ANISOU 896 N SER A 143 10654 10774 9197 657 178 -271 N ATOM 897 CA SER A 143 -4.339 -2.426 19.935 1.00 80.04 C ANISOU 897 CA SER A 143 10538 10736 9138 570 216 -323 C ATOM 898 C SER A 143 -5.535 -3.186 19.379 1.00 84.30 C ANISOU 898 C SER A 143 10912 11485 9633 536 239 -433 C ATOM 899 O SER A 143 -6.127 -2.764 18.384 1.00 84.27 O ANISOU 899 O SER A 143 10825 11636 9559 641 216 -464 O ATOM 900 CB SER A 143 -4.792 -1.416 20.990 1.00 82.44 C ANISOU 900 CB SER A 143 10904 11019 9402 657 221 -294 C ATOM 901 OG SER A 143 -5.694 -2.001 21.917 1.00 86.41 O ANISOU 901 OG SER A 143 11342 11594 9897 589 263 -356 O ATOM 902 N LEU A 144 -5.883 -4.304 20.013 1.00 80.87 N ANISOU 902 N LEU A 144 10436 11059 9231 388 289 -495 N ATOM 903 CA LEU A 144 -7.029 -5.098 19.584 1.00 81.47 C ANISOU 903 CA LEU A 144 10354 11337 9263 317 326 -617 C ATOM 904 C LEU A 144 -8.301 -4.611 20.291 1.00 87.50 C ANISOU 904 C LEU A 144 11036 12256 9954 372 347 -670 C ATOM 905 O LEU A 144 -9.398 -5.100 20.005 1.00 87.70 O ANISOU 905 O LEU A 144 10908 12491 9923 323 378 -783 O ATOM 906 CB LEU A 144 -6.770 -6.598 19.821 1.00 81.00 C ANISOU 906 CB LEU A 144 10308 11202 9265 116 389 -665 C ATOM 907 CG LEU A 144 -5.593 -7.211 19.039 1.00 84.08 C ANISOU 907 CG LEU A 144 10764 11464 9717 68 375 -625 C ATOM 908 CD1 LEU A 144 -5.372 -8.643 19.446 1.00 84.41 C ANISOU 908 CD1 LEU A 144 10854 11412 9808 -109 449 -664 C ATOM 909 CD2 LEU A 144 -5.807 -7.128 17.539 1.00 84.56 C ANISOU 909 CD2 LEU A 144 10722 11671 9735 119 340 -669 C ATOM 910 N LEU A 145 -8.143 -3.601 21.177 1.00 85.11 N ANISOU 910 N LEU A 145 10833 11861 9644 476 331 -593 N ATOM 911 CA LEU A 145 -9.222 -2.960 21.928 1.00 86.02 C ANISOU 911 CA LEU A 145 10897 12098 9688 558 347 -623 C ATOM 912 C LEU A 145 -9.744 -1.744 21.216 1.00 91.24 C ANISOU 912 C LEU A 145 11519 12897 10251 777 302 -610 C ATOM 913 O LEU A 145 -8.981 -1.015 20.577 1.00 90.45 O ANISOU 913 O LEU A 145 11514 12701 10151 883 259 -530 O ATOM 914 CB LEU A 145 -8.755 -2.509 23.333 1.00 85.43 C ANISOU 914 CB LEU A 145 10971 11837 9652 558 359 -547 C ATOM 915 CG LEU A 145 -8.361 -3.557 24.362 1.00 88.56 C ANISOU 915 CG LEU A 145 11429 12096 10123 378 411 -550 C ATOM 916 CD1 LEU A 145 -7.509 -2.924 25.453 1.00 87.26 C ANISOU 916 CD1 LEU A 145 11431 11728 9995 410 396 -451 C ATOM 917 CD2 LEU A 145 -9.582 -4.268 24.927 1.00 89.69 C ANISOU 917 CD2 LEU A 145 11458 12388 10230 279 481 -656 C ATOM 918 N THR A 146 -11.042 -1.494 21.382 1.00 90.02 N ANISOU 918 N THR A 146 11233 12968 10004 852 318 -686 N ATOM 919 CA THR A 146 -11.692 -0.291 20.885 1.00 91.10 C ANISOU 919 CA THR A 146 11337 13252 10023 1095 283 -673 C ATOM 920 C THR A 146 -11.507 0.802 21.958 1.00 93.64 C ANISOU 920 C THR A 146 11821 13424 10336 1208 288 -584 C ATOM 921 O THR A 146 -11.240 0.472 23.122 1.00 93.33 O ANISOU 921 O THR A 146 11849 13247 10363 1086 321 -569 O ATOM 922 CB THR A 146 -13.150 -0.563 20.506 1.00106.33 C ANISOU 922 CB THR A 146 13034 15522 11844 1133 295 -804 C ATOM 923 OG1 THR A 146 -13.638 0.587 19.818 1.00119.84 O ANISOU 923 OG1 THR A 146 14725 17376 13431 1400 253 -780 O ATOM 924 CG2 THR A 146 -14.040 -0.878 21.700 1.00100.98 C ANISOU 924 CG2 THR A 146 12281 14935 11153 1052 351 -874 C ATOM 925 N LYS A 147 -11.627 2.089 21.573 1.00 89.21 N ANISOU 925 N LYS A 147 11334 12878 9685 1442 261 -524 N ATOM 926 CA LYS A 147 -11.462 3.220 22.497 1.00 88.51 C ANISOU 926 CA LYS A 147 11417 12640 9572 1560 273 -443 C ATOM 927 C LYS A 147 -12.525 3.197 23.619 1.00 93.48 C ANISOU 927 C LYS A 147 11967 13392 10159 1568 311 -501 C ATOM 928 O LYS A 147 -12.284 3.767 24.681 1.00 93.05 O ANISOU 928 O LYS A 147 12052 13182 10119 1584 332 -446 O ATOM 929 CB LYS A 147 -11.475 4.558 21.743 1.00 90.96 C ANISOU 929 CB LYS A 147 11834 12950 9777 1818 253 -376 C ATOM 930 CG LYS A 147 -10.117 4.927 21.141 1.00 95.62 C ANISOU 930 CG LYS A 147 12601 13304 10424 1797 235 -282 C ATOM 931 CD LYS A 147 -10.170 6.215 20.314 1.00102.99 C ANISOU 931 CD LYS A 147 13658 14233 11241 2049 230 -218 C ATOM 932 N ASN A 148 -13.648 2.464 23.401 1.00 90.99 N ANISOU 932 N ASN A 148 11426 13354 9794 1531 326 -620 N ATOM 933 CA ASN A 148 -14.772 2.261 24.326 1.00 91.54 C ANISOU 933 CA ASN A 148 11374 13593 9815 1513 369 -700 C ATOM 934 C ASN A 148 -14.450 1.154 25.364 1.00 94.30 C ANISOU 934 C ASN A 148 11737 13812 10279 1244 418 -727 C ATOM 935 O ASN A 148 -14.890 1.240 26.516 1.00 94.15 O ANISOU 935 O ASN A 148 11734 13786 10253 1222 459 -738 O ATOM 936 CB ASN A 148 -16.020 1.889 23.516 1.00 96.51 C ANISOU 936 CB ASN A 148 11743 14588 10337 1564 367 -828 C ATOM 937 CG ASN A 148 -17.357 2.009 24.215 1.00139.12 C ANISOU 937 CG ASN A 148 16988 20235 15636 1624 404 -917 C ATOM 938 OD1 ASN A 148 -17.493 1.853 25.437 1.00139.39 O ANISOU 938 OD1 ASN A 148 17063 20189 15708 1529 452 -920 O ATOM 939 ND2 ASN A 148 -18.402 2.225 23.428 1.00136.19 N ANISOU 939 ND2 ASN A 148 16420 20197 15129 1779 385 -1002 N ATOM 940 N LYS A 149 -13.693 0.113 24.954 1.00 89.25 N ANISOU 940 N LYS A 149 11102 13072 9738 1050 419 -735 N ATOM 941 CA LYS A 149 -13.307 -0.980 25.845 1.00 87.64 C ANISOU 941 CA LYS A 149 10937 12729 9632 813 470 -751 C ATOM 942 C LYS A 149 -12.160 -0.528 26.741 1.00 89.51 C ANISOU 942 C LYS A 149 11397 12667 9944 809 459 -631 C ATOM 943 O LYS A 149 -12.121 -0.906 27.910 1.00 88.55 O ANISOU 943 O LYS A 149 11333 12452 9861 705 502 -628 O ATOM 944 CB LYS A 149 -12.940 -2.244 25.056 1.00 89.78 C ANISOU 944 CB LYS A 149 11145 13003 9966 629 482 -805 C ATOM 945 CG LYS A 149 -14.158 -3.070 24.633 1.00108.84 C ANISOU 945 CG LYS A 149 13335 15702 12319 532 527 -957 C ATOM 946 CD LYS A 149 -13.782 -4.318 23.824 1.00124.13 C ANISOU 946 CD LYS A 149 15228 17626 14310 343 548 -1014 C ATOM 947 CE LYS A 149 -13.608 -5.543 24.704 1.00140.94 C ANISOU 947 CE LYS A 149 17418 19622 16512 101 636 -1047 C ATOM 948 NZ LYS A 149 -13.105 -6.723 23.948 1.00151.10 N ANISOU 948 NZ LYS A 149 18708 20850 17852 -70 662 -1088 N ATOM 949 N ALA A 150 -11.257 0.318 26.201 1.00 85.58 N ANISOU 949 N ALA A 150 11025 12034 9457 925 404 -537 N ATOM 950 CA ALA A 150 -10.112 0.889 26.917 1.00 84.43 C ANISOU 950 CA ALA A 150 11084 11626 9367 926 389 -432 C ATOM 951 C ALA A 150 -10.580 1.749 28.096 1.00 89.30 C ANISOU 951 C ALA A 150 11776 12218 9935 1017 411 -410 C ATOM 952 O ALA A 150 -9.980 1.671 29.169 1.00 89.10 O ANISOU 952 O ALA A 150 11867 12025 9963 933 425 -368 O ATOM 953 CB ALA A 150 -9.252 1.713 25.968 1.00 84.65 C ANISOU 953 CB ALA A 150 11212 11559 9393 1034 339 -356 C ATOM 954 N ARG A 151 -11.671 2.536 27.903 1.00 86.26 N ANISOU 954 N ARG A 151 11322 12013 9442 1195 415 -441 N ATOM 955 CA ARG A 151 -12.294 3.383 28.925 1.00 86.40 C ANISOU 955 CA ARG A 151 11395 12040 9394 1309 442 -430 C ATOM 956 C ARG A 151 -12.883 2.518 30.043 1.00 90.77 C ANISOU 956 C ARG A 151 11871 12645 9971 1162 495 -494 C ATOM 957 O ARG A 151 -12.764 2.878 31.210 1.00 91.69 O ANISOU 957 O ARG A 151 12099 12645 10095 1158 518 -459 O ATOM 958 CB ARG A 151 -13.385 4.274 28.311 1.00 88.14 C ANISOU 958 CB ARG A 151 11534 12476 9478 1548 436 -458 C ATOM 959 CG ARG A 151 -12.855 5.473 27.541 1.00 99.43 C ANISOU 959 CG ARG A 151 13115 13807 10858 1739 404 -374 C ATOM 960 CD ARG A 151 -13.986 6.314 26.982 1.00112.62 C ANISOU 960 CD ARG A 151 14713 15699 12376 2002 404 -399 C ATOM 961 NE ARG A 151 -13.488 7.360 26.086 1.00125.56 N ANISOU 961 NE ARG A 151 16505 17244 13958 2185 382 -319 N ATOM 962 CZ ARG A 151 -13.587 7.328 24.760 1.00143.88 C ANISOU 962 CZ ARG A 151 18748 19688 16230 2275 350 -330 C ATOM 963 NH1 ARG A 151 -14.188 6.308 24.156 1.00131.52 N ANISOU 963 NH1 ARG A 151 16944 18362 14667 2197 332 -426 N ATOM 964 NH2 ARG A 151 -13.103 8.323 24.027 1.00132.48 N ANISOU 964 NH2 ARG A 151 17475 18132 14729 2441 343 -250 N ATOM 965 N VAL A 152 -13.483 1.368 29.689 1.00 86.95 N ANISOU 965 N VAL A 152 11209 12328 9498 1030 522 -589 N ATOM 966 CA VAL A 152 -14.065 0.412 30.640 1.00 86.55 C ANISOU 966 CA VAL A 152 11087 12330 9468 864 590 -660 C ATOM 967 C VAL A 152 -12.942 -0.204 31.501 1.00 87.47 C ANISOU 967 C VAL A 152 11364 12180 9689 700 605 -597 C ATOM 968 O VAL A 152 -13.105 -0.254 32.716 1.00 86.56 O ANISOU 968 O VAL A 152 11309 12004 9577 656 647 -591 O ATOM 969 CB VAL A 152 -14.921 -0.662 29.918 1.00 91.20 C ANISOU 969 CB VAL A 152 11460 13157 10036 745 626 -786 C ATOM 970 CG1 VAL A 152 -15.301 -1.809 30.853 1.00 91.24 C ANISOU 970 CG1 VAL A 152 11431 13163 10075 526 713 -855 C ATOM 971 CG2 VAL A 152 -16.172 -0.038 29.313 1.00 92.45 C ANISOU 971 CG2 VAL A 152 11438 13623 10068 917 615 -862 C ATOM 972 N ILE A 153 -11.806 -0.620 30.882 1.00 82.18 N ANISOU 972 N ILE A 153 10765 11364 9097 630 568 -548 N ATOM 973 CA ILE A 153 -10.633 -1.180 31.576 1.00 80.96 C ANISOU 973 CA ILE A 153 10758 10975 9030 505 571 -484 C ATOM 974 C ILE A 153 -10.103 -0.156 32.615 1.00 85.52 C ANISOU 974 C ILE A 153 11497 11395 9601 590 551 -402 C ATOM 975 O ILE A 153 -9.873 -0.542 33.760 1.00 85.45 O ANISOU 975 O ILE A 153 11567 11285 9618 506 583 -386 O ATOM 976 CB ILE A 153 -9.496 -1.620 30.579 1.00 83.17 C ANISOU 976 CB ILE A 153 11071 11151 9376 455 527 -445 C ATOM 977 CG1 ILE A 153 -9.981 -2.625 29.479 1.00 84.47 C ANISOU 977 CG1 ILE A 153 11086 11465 9544 367 548 -531 C ATOM 978 CG2 ILE A 153 -8.249 -2.150 31.293 1.00 81.54 C ANISOU 978 CG2 ILE A 153 11009 10726 9245 354 524 -378 C ATOM 979 CD1 ILE A 153 -10.562 -3.957 29.920 1.00 97.73 C ANISOU 979 CD1 ILE A 153 12703 13194 11236 186 633 -614 C ATOM 980 N ILE A 154 -9.931 1.135 32.216 1.00 82.14 N ANISOU 980 N ILE A 154 11129 10950 9131 754 504 -354 N ATOM 981 CA ILE A 154 -9.421 2.226 33.065 1.00 81.82 C ANISOU 981 CA ILE A 154 11254 10760 9074 834 489 -284 C ATOM 982 C ILE A 154 -10.358 2.450 34.264 1.00 86.77 C ANISOU 982 C ILE A 154 11877 11443 9648 863 538 -313 C ATOM 983 O ILE A 154 -9.865 2.559 35.386 1.00 86.15 O ANISOU 983 O ILE A 154 11919 11226 9589 817 547 -276 O ATOM 984 CB ILE A 154 -9.172 3.553 32.267 1.00 85.21 C ANISOU 984 CB ILE A 154 11761 11162 9454 1003 451 -236 C ATOM 985 CG1 ILE A 154 -8.049 3.380 31.228 1.00 84.58 C ANISOU 985 CG1 ILE A 154 11712 10993 9431 957 406 -197 C ATOM 986 CG2 ILE A 154 -8.851 4.738 33.202 1.00 86.27 C ANISOU 986 CG2 ILE A 154 12073 11154 9552 1081 455 -181 C ATOM 987 CD1 ILE A 154 -8.113 4.343 30.069 1.00 90.47 C ANISOU 987 CD1 ILE A 154 12480 11775 10119 1113 383 -175 C ATOM 988 N LEU A 155 -11.689 2.504 34.041 1.00 84.59 N ANISOU 988 N LEU A 155 11460 11382 9301 939 570 -384 N ATOM 989 CA LEU A 155 -12.647 2.684 35.142 1.00 85.30 C ANISOU 989 CA LEU A 155 11528 11549 9335 968 622 -420 C ATOM 990 C LEU A 155 -12.662 1.451 36.062 1.00 88.77 C ANISOU 990 C LEU A 155 11948 11953 9826 770 677 -453 C ATOM 991 O LEU A 155 -12.814 1.616 37.273 1.00 88.39 O ANISOU 991 O LEU A 155 11975 11847 9764 759 711 -442 O ATOM 992 CB LEU A 155 -14.061 3.015 34.640 1.00 86.80 C ANISOU 992 CB LEU A 155 11550 12008 9424 1102 643 -496 C ATOM 993 CG LEU A 155 -14.211 4.345 33.890 1.00 92.34 C ANISOU 993 CG LEU A 155 12293 12749 10042 1342 603 -458 C ATOM 994 CD1 LEU A 155 -15.464 4.356 33.069 1.00 94.44 C ANISOU 994 CD1 LEU A 155 12354 13315 10213 1460 610 -541 C ATOM 995 CD2 LEU A 155 -14.191 5.536 34.828 1.00 94.00 C ANISOU 995 CD2 LEU A 155 12673 12844 10200 1477 615 -402 C ATOM 996 N AMET A 156 -12.469 0.237 35.481 0.50 85.17 N ANISOU 996 N AMET A 156 11414 11520 9427 620 690 -491 N ATOM 997 N BMET A 156 -12.469 0.241 35.499 0.50 84.96 N ANISOU 997 N BMET A 156 11388 11491 9400 620 690 -490 N ATOM 998 CA AMET A 156 -12.389 -1.065 36.163 0.50 84.87 C ANISOU 998 CA AMET A 156 11383 11427 9437 426 753 -519 C ATOM 999 CA BMET A 156 -12.425 -1.009 36.260 0.50 84.54 C ANISOU 999 CA BMET A 156 11345 11384 9391 432 755 -518 C ATOM 1000 C AMET A 156 -11.140 -1.124 37.061 0.50 86.57 C ANISOU 1000 C AMET A 156 11788 11397 9707 380 733 -429 C ATOM 1001 C BMET A 156 -11.136 -1.103 37.098 0.50 86.38 C ANISOU 1001 C BMET A 156 11768 11370 9683 382 733 -428 C ATOM 1002 O AMET A 156 -11.226 -1.633 38.178 0.50 86.53 O ANISOU 1002 O AMET A 156 11842 11332 9705 298 787 -430 O ATOM 1003 O BMET A 156 -11.196 -1.604 38.222 0.50 86.27 O ANISOU 1003 O BMET A 156 11815 11291 9671 300 786 -427 O ATOM 1004 CB AMET A 156 -12.368 -2.215 35.127 0.50 87.51 C ANISOU 1004 CB AMET A 156 11614 11826 9810 299 769 -575 C ATOM 1005 CB BMET A 156 -12.583 -2.227 35.340 0.50 87.23 C ANISOU 1005 CB BMET A 156 11570 11809 9764 294 784 -586 C ATOM 1006 CG AMET A 156 -12.703 -3.596 35.688 0.50 92.20 C ANISOU 1006 CG AMET A 156 12192 12417 10424 101 865 -635 C ATOM 1007 CG BMET A 156 -13.533 -3.285 35.890 0.50 92.24 C ANISOU 1007 CG BMET A 156 12121 12547 10379 137 889 -680 C ATOM 1008 SD AMET A 156 -12.269 -4.966 34.562 0.50 96.72 S ANISOU 1008 SD AMET A 156 12721 12974 11053 -58 886 -676 S ATOM 1009 SD BMET A 156 -15.245 -2.727 36.156 0.50 98.32 S ANISOU 1009 SD BMET A 156 12714 13604 11042 213 937 -782 S ATOM 1010 CE AMET A 156 -13.585 -4.844 33.359 0.50 94.52 C ANISOU 1010 CE AMET A 156 12196 13011 10707 -33 891 -801 C ATOM 1011 CE BMET A 156 -15.927 -4.172 36.928 0.50 96.03 C ANISOU 1011 CE BMET A 156 12385 13349 10752 -34 1074 -877 C ATOM 1012 N VAL A 157 -9.991 -0.598 36.584 1.00 81.34 N ANISOU 1012 N VAL A 157 11217 10607 9082 433 658 -356 N ATOM 1013 CA VAL A 157 -8.740 -0.590 37.361 1.00 79.81 C ANISOU 1013 CA VAL A 157 11183 10212 8929 396 629 -279 C ATOM 1014 C VAL A 157 -8.894 0.460 38.485 1.00 85.42 C ANISOU 1014 C VAL A 157 11991 10874 9590 482 629 -251 C ATOM 1015 O VAL A 157 -8.465 0.193 39.599 1.00 86.47 O ANISOU 1015 O VAL A 157 12221 10904 9731 426 644 -224 O ATOM 1016 CB VAL A 157 -7.376 -0.445 36.588 1.00 81.60 C ANISOU 1016 CB VAL A 157 11472 10326 9208 400 557 -219 C ATOM 1017 CG1 VAL A 157 -7.322 -1.260 35.296 1.00 80.12 C ANISOU 1017 CG1 VAL A 157 11183 10203 9058 347 553 -249 C ATOM 1018 CG2 VAL A 157 -6.982 1.000 36.344 1.00 81.46 C ANISOU 1018 CG2 VAL A 157 11526 10263 9162 524 503 -176 C ATOM 1019 N TRP A 158 -9.575 1.599 38.216 1.00 81.77 N ANISOU 1019 N TRP A 158 11507 10495 9068 622 620 -262 N ATOM 1020 CA TRP A 158 -9.769 2.662 39.197 1.00 81.96 C ANISOU 1020 CA TRP A 158 11634 10471 9037 715 626 -239 C ATOM 1021 C TRP A 158 -10.807 2.298 40.286 1.00 85.79 C ANISOU 1021 C TRP A 158 12078 11035 9482 688 697 -285 C ATOM 1022 O TRP A 158 -10.615 2.686 41.439 1.00 84.65 O ANISOU 1022 O TRP A 158 12049 10798 9318 695 708 -258 O ATOM 1023 CB TRP A 158 -10.130 3.986 38.504 1.00 81.42 C ANISOU 1023 CB TRP A 158 11580 10451 8907 891 603 -230 C ATOM 1024 CG TRP A 158 -8.910 4.756 38.090 1.00 81.90 C ANISOU 1024 CG TRP A 158 11776 10355 8989 917 548 -165 C ATOM 1025 CD1 TRP A 158 -8.217 4.624 36.923 1.00 84.30 C ANISOU 1025 CD1 TRP A 158 12059 10638 9334 900 507 -147 C ATOM 1026 CD2 TRP A 158 -8.153 5.663 38.904 1.00 81.83 C ANISOU 1026 CD2 TRP A 158 11944 10185 8964 932 536 -119 C ATOM 1027 NE1 TRP A 158 -7.111 5.442 36.932 1.00 83.31 N ANISOU 1027 NE1 TRP A 158 12083 10355 9215 906 473 -93 N ATOM 1028 CE2 TRP A 158 -7.043 6.088 38.137 1.00 85.15 C ANISOU 1028 CE2 TRP A 158 12439 10501 9413 919 491 -79 C ATOM 1029 CE3 TRP A 158 -8.314 6.173 40.206 1.00 83.53 C ANISOU 1029 CE3 TRP A 158 12262 10339 9137 948 562 -114 C ATOM 1030 CZ2 TRP A 158 -6.114 7.023 38.614 1.00 84.51 C ANISOU 1030 CZ2 TRP A 158 12528 10264 9316 912 476 -42 C ATOM 1031 CZ3 TRP A 158 -7.390 7.093 40.682 1.00 85.05 C ANISOU 1031 CZ3 TRP A 158 12626 10374 9315 948 543 -75 C ATOM 1032 CH2 TRP A 158 -6.305 7.509 39.892 1.00 85.44 C ANISOU 1032 CH2 TRP A 158 12743 10329 9391 923 502 -43 C ATOM 1033 N ILE A 159 -11.872 1.548 39.939 1.00 83.30 N ANISOU 1033 N ILE A 159 11604 10895 9152 646 749 -360 N ATOM 1034 CA ILE A 159 -12.905 1.123 40.895 1.00 83.97 C ANISOU 1034 CA ILE A 159 11636 11074 9197 600 830 -416 C ATOM 1035 C ILE A 159 -12.356 0.000 41.805 1.00 87.04 C ANISOU 1035 C ILE A 159 12106 11333 9633 434 871 -400 C ATOM 1036 O ILE A 159 -12.590 0.057 43.012 1.00 86.48 O ANISOU 1036 O ILE A 159 12105 11221 9533 422 914 -394 O ATOM 1037 CB ILE A 159 -14.239 0.713 40.181 1.00 88.11 C ANISOU 1037 CB ILE A 159 11948 11852 9677 596 877 -517 C ATOM 1038 CG1 ILE A 159 -15.007 1.956 39.687 1.00 89.35 C ANISOU 1038 CG1 ILE A 159 12040 12160 9749 806 851 -532 C ATOM 1039 CG2 ILE A 159 -15.154 -0.152 41.083 1.00 89.70 C ANISOU 1039 CG2 ILE A 159 12084 12143 9854 471 979 -589 C ATOM 1040 CD1 ILE A 159 -16.030 1.671 38.541 1.00 99.82 C ANISOU 1040 CD1 ILE A 159 13143 13754 11030 835 862 -624 C ATOM 1041 N VAL A 160 -11.648 -1.013 41.239 1.00 83.46 N ANISOU 1041 N VAL A 160 11652 10815 9244 319 864 -391 N ATOM 1042 CA VAL A 160 -11.116 -2.132 42.034 1.00 84.09 C ANISOU 1042 CA VAL A 160 11826 10769 9357 183 911 -371 C ATOM 1043 C VAL A 160 -10.016 -1.610 42.977 1.00 89.62 C ANISOU 1043 C VAL A 160 12697 11294 10062 228 859 -285 C ATOM 1044 O VAL A 160 -10.065 -1.948 44.172 1.00 90.65 O ANISOU 1044 O VAL A 160 12912 11362 10169 186 907 -274 O ATOM 1045 CB VAL A 160 -10.670 -3.376 41.214 1.00 88.11 C ANISOU 1045 CB VAL A 160 12307 11251 9921 62 927 -384 C ATOM 1046 CG1 VAL A 160 -10.061 -4.455 42.115 1.00 87.78 C ANISOU 1046 CG1 VAL A 160 12399 11059 9895 -44 980 -349 C ATOM 1047 CG2 VAL A 160 -11.852 -3.970 40.450 1.00 88.85 C ANISOU 1047 CG2 VAL A 160 12232 11531 9997 -12 994 -487 C ATOM 1048 N SER A 161 -9.066 -0.761 42.468 1.00 85.73 N ANISOU 1048 N SER A 161 12253 10730 9589 308 767 -232 N ATOM 1049 CA ASER A 161 -8.004 -0.189 43.305 0.50 85.23 C ANISOU 1049 CA ASER A 161 12336 10525 9522 338 716 -166 C ATOM 1050 CA BSER A 161 -8.000 -0.168 43.288 0.50 84.56 C ANISOU 1050 CA BSER A 161 12252 10441 9438 340 715 -166 C ATOM 1051 C SER A 161 -8.594 0.705 44.409 1.00 89.54 C ANISOU 1051 C SER A 161 12942 11075 10004 407 739 -171 C ATOM 1052 O SER A 161 -7.959 0.890 45.440 1.00 89.54 O ANISOU 1052 O SER A 161 13060 10973 9987 401 724 -134 O ATOM 1053 CB ASER A 161 -6.985 0.583 42.471 0.50 88.42 C ANISOU 1053 CB ASER A 161 12770 10873 9952 391 629 -127 C ATOM 1054 CB BSER A 161 -7.034 0.654 42.433 0.50 85.64 C ANISOU 1054 CB BSER A 161 12415 10526 9599 397 628 -128 C ATOM 1055 OG ASER A 161 -7.586 1.631 41.730 0.50 98.70 O ANISOU 1055 OG ASER A 161 14025 12251 11228 495 614 -145 O ATOM 1056 OG BSER A 161 -6.364 -0.138 41.464 0.50 86.96 O ANISOU 1056 OG BSER A 161 12537 10681 9823 339 603 -119 O ATOM 1057 N GLY A 162 -9.813 1.211 44.200 1.00 86.89 N ANISOU 1057 N GLY A 162 12519 10868 9626 476 776 -219 N ATOM 1058 CA GLY A 162 -10.526 2.031 45.178 1.00 87.46 C ANISOU 1058 CA GLY A 162 12636 10964 9631 554 808 -230 C ATOM 1059 C GLY A 162 -11.018 1.196 46.351 1.00 92.99 C ANISOU 1059 C GLY A 162 13353 11668 10312 468 886 -251 C ATOM 1060 O GLY A 162 -10.935 1.624 47.508 1.00 92.36 O ANISOU 1060 O GLY A 162 13379 11521 10193 493 896 -229 O ATOM 1061 N LEU A 163 -11.518 -0.022 46.039 1.00 90.75 N ANISOU 1061 N LEU A 163 12973 11456 10051 358 948 -295 N ATOM 1062 CA ALEU A 163 -12.028 -0.969 47.021 0.50 90.88 C ANISOU 1062 CA ALEU A 163 13011 11473 10048 255 1043 -320 C ATOM 1063 CA BLEU A 163 -12.024 -0.991 47.015 0.50 91.25 C ANISOU 1063 CA BLEU A 163 13057 11519 10095 253 1044 -320 C ATOM 1064 C LEU A 163 -10.877 -1.501 47.896 1.00 93.70 C ANISOU 1064 C LEU A 163 13531 11650 10420 203 1029 -251 C ATOM 1065 O LEU A 163 -10.957 -1.418 49.117 1.00 94.12 O ANISOU 1065 O LEU A 163 13679 11653 10430 207 1062 -235 O ATOM 1066 CB ALEU A 163 -12.769 -2.112 46.292 0.50 91.33 C ANISOU 1066 CB ALEU A 163 12935 11643 10122 136 1119 -392 C ATOM 1067 CB BLEU A 163 -12.725 -2.168 46.293 0.50 91.99 C ANISOU 1067 CB BLEU A 163 13023 11721 10209 130 1119 -390 C ATOM 1068 CG ALEU A 163 -14.310 -2.043 46.219 0.50 96.91 C ANISOU 1068 CG ALEU A 163 13484 12562 10776 131 1197 -488 C ATOM 1069 CG BLEU A 163 -13.521 -3.152 47.166 0.50 98.10 C ANISOU 1069 CG BLEU A 163 13802 12522 10950 4 1247 -439 C ATOM 1070 CD1ALEU A 163 -14.811 -0.798 45.486 0.50 96.93 C ANISOU 1070 CD1ALEU A 163 13382 12702 10745 294 1136 -507 C ATOM 1071 CD1BLEU A 163 -14.853 -3.486 46.523 0.50 99.62 C ANISOU 1071 CD1BLEU A 163 13804 12929 11118 -58 1323 -548 C ATOM 1072 CD2ALEU A 163 -14.866 -3.268 45.526 0.50 99.87 C ANISOU 1072 CD2ALEU A 163 13743 13035 11168 -23 1275 -567 C ATOM 1073 CD2BLEU A 163 -12.727 -4.429 47.450 0.50 99.97 C ANISOU 1073 CD2BLEU A 163 14162 12604 11220 -118 1289 -402 C ATOM 1074 N THR A 164 -9.797 -2.008 47.273 1.00 87.69 N ANISOU 1074 N THR A 164 12802 10805 9712 169 976 -211 N ATOM 1075 CA THR A 164 -8.633 -2.547 47.984 1.00 86.37 C ANISOU 1075 CA THR A 164 12774 10492 9549 142 953 -146 C ATOM 1076 C THR A 164 -7.852 -1.476 48.784 1.00 87.59 C ANISOU 1076 C THR A 164 13034 10573 9673 227 876 -98 C ATOM 1077 O THR A 164 -7.072 -1.854 49.664 1.00 87.12 O ANISOU 1077 O THR A 164 13088 10424 9592 216 866 -55 O ATOM 1078 CB THR A 164 -7.675 -3.263 47.007 1.00 93.44 C ANISOU 1078 CB THR A 164 13661 11339 10502 105 910 -120 C ATOM 1079 OG1 THR A 164 -6.961 -2.299 46.235 1.00 93.21 O ANISOU 1079 OG1 THR A 164 13605 11309 10501 176 807 -98 O ATOM 1080 CG2 THR A 164 -8.378 -4.280 46.106 1.00 90.34 C ANISOU 1080 CG2 THR A 164 13171 11015 10140 12 984 -175 C ATOM 1081 N SER A 165 -8.040 -0.168 48.473 1.00 82.65 N ANISOU 1081 N SER A 165 12380 9986 9036 313 827 -109 N ATOM 1082 CA SER A 165 -7.330 0.933 49.133 1.00 81.84 C ANISOU 1082 CA SER A 165 12383 9812 8901 376 763 -77 C ATOM 1083 C SER A 165 -8.129 1.621 50.237 1.00 85.16 C ANISOU 1083 C SER A 165 12855 10247 9254 426 808 -95 C ATOM 1084 O SER A 165 -7.619 1.731 51.350 1.00 82.98 O ANISOU 1084 O SER A 165 12690 9900 8938 423 798 -70 O ATOM 1085 CB SER A 165 -6.897 1.985 48.120 1.00 84.73 C ANISOU 1085 CB SER A 165 12728 10178 9287 436 692 -72 C ATOM 1086 OG SER A 165 -5.986 1.432 47.185 1.00 91.03 O ANISOU 1086 OG SER A 165 13491 10952 10143 392 643 -51 O ATOM 1087 N PHE A 166 -9.349 2.107 49.935 1.00 83.97 N ANISOU 1087 N PHE A 166 12624 10200 9081 481 854 -139 N ATOM 1088 CA PHE A 166 -10.181 2.840 50.905 1.00 85.37 C ANISOU 1088 CA PHE A 166 12843 10405 9189 546 900 -160 C ATOM 1089 C PHE A 166 -10.811 1.941 51.972 1.00 92.47 C ANISOU 1089 C PHE A 166 13753 11324 10058 480 988 -176 C ATOM 1090 O PHE A 166 -10.860 2.338 53.144 1.00 92.43 O ANISOU 1090 O PHE A 166 13847 11275 9998 506 1005 -166 O ATOM 1091 CB PHE A 166 -11.287 3.650 50.199 1.00 87.32 C ANISOU 1091 CB PHE A 166 12992 10777 9409 651 921 -203 C ATOM 1092 CG PHE A 166 -10.862 5.045 49.810 1.00 88.56 C ANISOU 1092 CG PHE A 166 13226 10879 9545 763 861 -182 C ATOM 1093 CD1 PHE A 166 -10.228 5.284 48.596 1.00 90.72 C ANISOU 1093 CD1 PHE A 166 13476 11132 9862 776 801 -165 C ATOM 1094 CD2 PHE A 166 -11.096 6.122 50.657 1.00 91.43 C ANISOU 1094 CD2 PHE A 166 13700 11202 9838 851 874 -180 C ATOM 1095 CE1 PHE A 166 -9.815 6.575 48.246 1.00 91.71 C ANISOU 1095 CE1 PHE A 166 13697 11188 9959 869 762 -145 C ATOM 1096 CE2 PHE A 166 -10.693 7.415 50.300 1.00 94.48 C ANISOU 1096 CE2 PHE A 166 14186 11517 10197 946 836 -163 C ATOM 1097 CZ PHE A 166 -10.047 7.631 49.099 1.00 91.85 C ANISOU 1097 CZ PHE A 166 13838 11155 9905 950 783 -145 C ATOM 1098 N LEU A 167 -11.289 0.746 51.573 1.00 90.93 N ANISOU 1098 N LEU A 167 13467 11189 9893 387 1050 -204 N ATOM 1099 CA LEU A 167 -11.997 -0.180 52.452 1.00 92.27 C ANISOU 1099 CA LEU A 167 13647 11380 10031 305 1157 -229 C ATOM 1100 C LEU A 167 -11.121 -0.714 53.632 1.00 95.53 C ANISOU 1100 C LEU A 167 14225 11651 10421 268 1159 -171 C ATOM 1101 O LEU A 167 -11.551 -0.477 54.762 1.00 96.27 O ANISOU 1101 O LEU A 167 14385 11738 10455 286 1206 -174 O ATOM 1102 CB LEU A 167 -12.642 -1.331 51.650 1.00 93.14 C ANISOU 1102 CB LEU A 167 13635 11579 10175 196 1231 -280 C ATOM 1103 CG LEU A 167 -13.815 -2.099 52.290 1.00 99.89 C ANISOU 1103 CG LEU A 167 14451 12515 10988 102 1368 -341 C ATOM 1104 CD1 LEU A 167 -14.975 -1.164 52.662 1.00101.56 C ANISOU 1104 CD1 LEU A 167 14582 12867 11138 184 1400 -393 C ATOM 1105 CD2 LEU A 167 -14.312 -3.184 51.352 1.00102.22 C ANISOU 1105 CD2 LEU A 167 14630 12892 11316 -25 1436 -401 C ATOM 1106 N PRO A 168 -9.930 -1.366 53.481 1.00 89.80 N ANISOU 1106 N PRO A 168 13570 10823 9727 233 1110 -119 N ATOM 1107 CA PRO A 168 -9.194 -1.815 54.689 1.00 89.58 C ANISOU 1107 CA PRO A 168 13695 10687 9653 227 1114 -68 C ATOM 1108 C PRO A 168 -8.799 -0.688 55.653 1.00 94.10 C ANISOU 1108 C PRO A 168 14358 11226 10172 308 1054 -48 C ATOM 1109 O PRO A 168 -8.730 -0.930 56.857 1.00 95.04 O ANISOU 1109 O PRO A 168 14585 11298 10229 310 1089 -27 O ATOM 1110 CB PRO A 168 -7.940 -2.485 54.124 1.00 90.73 C ANISOU 1110 CB PRO A 168 13872 10761 9839 210 1051 -20 C ATOM 1111 CG PRO A 168 -8.283 -2.821 52.708 1.00 94.83 C ANISOU 1111 CG PRO A 168 14261 11342 10428 165 1058 -54 C ATOM 1112 CD PRO A 168 -9.213 -1.749 52.248 1.00 90.28 C ANISOU 1112 CD PRO A 168 13575 10872 9856 209 1052 -106 C ATOM 1113 N ILE A 169 -8.561 0.542 55.137 1.00 89.75 N ANISOU 1113 N ILE A 169 13774 10693 9635 374 974 -57 N ATOM 1114 CA ILE A 169 -8.150 1.702 55.932 1.00 88.86 C ANISOU 1114 CA ILE A 169 13755 10539 9469 438 921 -48 C ATOM 1115 C ILE A 169 -9.344 2.264 56.739 1.00 96.36 C ANISOU 1115 C ILE A 169 14718 11534 10359 481 995 -83 C ATOM 1116 O ILE A 169 -9.239 2.377 57.966 1.00 97.19 O ANISOU 1116 O ILE A 169 14930 11597 10401 492 1011 -71 O ATOM 1117 CB ILE A 169 -7.423 2.787 55.075 1.00 89.86 C ANISOU 1117 CB ILE A 169 13869 10649 9624 478 825 -47 C ATOM 1118 CG1 ILE A 169 -6.054 2.244 54.591 1.00 88.32 C ANISOU 1118 CG1 ILE A 169 13680 10409 9469 434 748 -12 C ATOM 1119 CG2 ILE A 169 -7.232 4.092 55.881 1.00 90.70 C ANISOU 1119 CG2 ILE A 169 14083 10714 9667 533 796 -56 C ATOM 1120 CD1 ILE A 169 -5.352 3.022 53.529 1.00 89.13 C ANISOU 1120 CD1 ILE A 169 13751 10503 9612 445 671 -14 C ATOM 1121 N GLN A 170 -10.462 2.591 56.068 1.00 94.27 N ANISOU 1121 N GLN A 170 14343 11366 10108 512 1041 -127 N ATOM 1122 CA GLN A 170 -11.652 3.153 56.713 1.00 95.62 C ANISOU 1122 CA GLN A 170 14506 11607 10219 569 1113 -165 C ATOM 1123 C GLN A 170 -12.346 2.128 57.655 1.00101.72 C ANISOU 1123 C GLN A 170 15287 12404 10956 497 1219 -177 C ATOM 1124 O GLN A 170 -13.021 2.538 58.605 1.00101.27 O ANISOU 1124 O GLN A 170 15272 12371 10835 536 1273 -196 O ATOM 1125 CB GLN A 170 -12.628 3.704 55.655 1.00 97.35 C ANISOU 1125 CB GLN A 170 14588 11952 10450 637 1129 -211 C ATOM 1126 CG GLN A 170 -12.820 5.239 55.711 1.00112.60 C ANISOU 1126 CG GLN A 170 16574 13877 12330 774 1100 -217 C ATOM 1127 CD GLN A 170 -11.705 6.126 55.161 1.00124.40 C ANISOU 1127 CD GLN A 170 18154 15267 13845 812 1004 -184 C ATOM 1128 OE1 GLN A 170 -10.637 5.676 54.733 1.00115.45 O ANISOU 1128 OE1 GLN A 170 17033 14067 12766 739 943 -154 O ATOM 1129 NE2 GLN A 170 -11.945 7.435 55.163 1.00118.27 N ANISOU 1129 NE2 GLN A 170 17447 14474 13018 929 999 -192 N ATOM 1130 N MET A 171 -12.126 0.812 57.427 1.00 99.77 N ANISOU 1130 N MET A 171 15023 12139 10747 394 1255 -166 N ATOM 1131 CA MET A 171 -12.658 -0.279 58.255 1.00100.36 C ANISOU 1131 CA MET A 171 15136 12209 10787 308 1369 -173 C ATOM 1132 C MET A 171 -11.665 -0.638 59.378 1.00102.77 C ANISOU 1132 C MET A 171 15616 12382 11048 308 1348 -110 C ATOM 1133 O MET A 171 -11.958 -1.498 60.213 1.00104.22 O ANISOU 1133 O MET A 171 15876 12534 11189 252 1442 -102 O ATOM 1134 CB MET A 171 -12.980 -1.515 57.400 1.00103.32 C ANISOU 1134 CB MET A 171 15423 12622 11213 195 1436 -199 C ATOM 1135 CG MET A 171 -14.099 -1.308 56.393 1.00108.19 C ANISOU 1135 CG MET A 171 15851 13402 11854 185 1472 -275 C ATOM 1136 SD MET A 171 -15.697 -0.974 57.160 1.00114.74 S ANISOU 1136 SD MET A 171 16608 14380 12608 193 1589 -349 S ATOM 1137 CE MET A 171 -16.202 -2.668 57.614 1.00112.47 C ANISOU 1137 CE MET A 171 16349 14078 12307 0 1752 -380 C ATOM 1138 N HIS A 172 -10.497 0.047 59.399 1.00 96.41 N ANISOU 1138 N HIS A 172 14876 11510 10245 370 1228 -70 N ATOM 1139 CA HIS A 172 -9.404 -0.055 60.379 1.00 95.12 C ANISOU 1139 CA HIS A 172 14858 11254 10030 392 1177 -17 C ATOM 1140 C HIS A 172 -8.771 -1.468 60.462 1.00 96.77 C ANISOU 1140 C HIS A 172 15129 11399 10239 342 1203 29 C ATOM 1141 O HIS A 172 -8.156 -1.800 61.474 1.00 96.74 O ANISOU 1141 O HIS A 172 15252 11337 10167 367 1197 71 O ATOM 1142 CB HIS A 172 -9.861 0.427 61.773 1.00 96.70 C ANISOU 1142 CB HIS A 172 15154 11445 10141 430 1221 -23 C ATOM 1143 CG HIS A 172 -10.301 1.865 61.817 1.00100.25 C ANISOU 1143 CG HIS A 172 15582 11934 10574 500 1190 -61 C ATOM 1144 ND1 HIS A 172 -11.007 2.366 62.891 1.00102.72 N ANISOU 1144 ND1 HIS A 172 15955 12260 10813 538 1247 -80 N ATOM 1145 CD2 HIS A 172 -10.130 2.858 60.910 1.00101.75 C ANISOU 1145 CD2 HIS A 172 15712 12143 10804 543 1119 -79 C ATOM 1146 CE1 HIS A 172 -11.243 3.638 62.609 1.00102.26 C ANISOU 1146 CE1 HIS A 172 15877 12226 10751 608 1210 -109 C ATOM 1147 NE2 HIS A 172 -10.736 3.979 61.425 1.00101.96 N ANISOU 1147 NE2 HIS A 172 15773 12188 10778 615 1135 -109 N ATOM 1148 N TRP A 173 -8.837 -2.244 59.356 1.00 91.01 N ANISOU 1148 N TRP A 173 14318 10682 9579 283 1225 23 N ATOM 1149 CA TRP A 173 -8.257 -3.582 59.230 1.00 89.89 C ANISOU 1149 CA TRP A 173 14240 10472 9441 242 1258 65 C ATOM 1150 C TRP A 173 -6.733 -3.537 59.235 1.00 87.20 C ANISOU 1150 C TRP A 173 13959 10084 9091 306 1137 120 C ATOM 1151 O TRP A 173 -6.083 -4.509 59.601 1.00 85.54 O ANISOU 1151 O TRP A 173 13850 9810 8841 319 1154 170 O ATOM 1152 CB TRP A 173 -8.734 -4.238 57.925 1.00 89.70 C ANISOU 1152 CB TRP A 173 14102 10484 9496 162 1305 31 C ATOM 1153 CG TRP A 173 -10.221 -4.442 57.794 1.00 92.43 C ANISOU 1153 CG TRP A 173 14362 10909 9847 81 1429 -38 C ATOM 1154 CD1 TRP A 173 -11.161 -4.356 58.783 1.00 96.36 C ANISOU 1154 CD1 TRP A 173 14895 11433 10284 63 1525 -65 C ATOM 1155 CD2 TRP A 173 -10.926 -4.825 56.601 1.00 92.74 C ANISOU 1155 CD2 TRP A 173 14260 11028 9948 0 1475 -96 C ATOM 1156 NE1 TRP A 173 -12.406 -4.655 58.280 1.00 96.79 N ANISOU 1156 NE1 TRP A 173 14828 11589 10357 -27 1628 -140 N ATOM 1157 CE2 TRP A 173 -12.292 -4.945 56.943 1.00 97.65 C ANISOU 1157 CE2 TRP A 173 14825 11737 10539 -68 1599 -163 C ATOM 1158 CE3 TRP A 173 -10.527 -5.117 55.279 1.00 93.72 C ANISOU 1158 CE3 TRP A 173 14298 11167 10146 -26 1428 -102 C ATOM 1159 CZ2 TRP A 173 -13.272 -5.284 56.001 1.00 97.46 C ANISOU 1159 CZ2 TRP A 173 14647 11833 10551 -160 1668 -243 C ATOM 1160 CZ3 TRP A 173 -11.495 -5.464 54.349 1.00 95.69 C ANISOU 1160 CZ3 TRP A 173 14407 11520 10432 -113 1496 -176 C ATOM 1161 CH2 TRP A 173 -12.850 -5.544 54.711 1.00 97.37 C ANISOU 1161 CH2 TRP A 173 14554 11835 10609 -181 1613 -249 C ATOM 1162 N TYR A 174 -6.169 -2.407 58.807 1.00 81.33 N ANISOU 1162 N TYR A 174 13153 9374 8373 348 1020 109 N ATOM 1163 CA TYR A 174 -4.731 -2.151 58.713 1.00 79.83 C ANISOU 1163 CA TYR A 174 12985 9171 8174 394 897 141 C ATOM 1164 C TYR A 174 -4.049 -1.980 60.080 1.00 84.70 C ANISOU 1164 C TYR A 174 13724 9770 8689 452 860 169 C ATOM 1165 O TYR A 174 -2.845 -2.217 60.177 1.00 83.73 O ANISOU 1165 O TYR A 174 13630 9648 8534 491 780 201 O ATOM 1166 CB TYR A 174 -4.496 -0.866 57.876 1.00 79.16 C ANISOU 1166 CB TYR A 174 12807 9128 8142 400 806 107 C ATOM 1167 CG TYR A 174 -4.744 0.439 58.611 1.00 79.95 C ANISOU 1167 CG TYR A 174 12946 9238 8194 432 783 77 C ATOM 1168 CD1 TYR A 174 -6.019 0.988 58.689 1.00 81.75 C ANISOU 1168 CD1 TYR A 174 13146 9491 8423 437 854 39 C ATOM 1169 CD2 TYR A 174 -3.702 1.113 59.246 1.00 80.51 C ANISOU 1169 CD2 TYR A 174 13081 9302 8208 458 695 80 C ATOM 1170 CE1 TYR A 174 -6.251 2.188 59.366 1.00 82.10 C ANISOU 1170 CE1 TYR A 174 13243 9535 8417 478 841 13 C ATOM 1171 CE2 TYR A 174 -3.924 2.305 59.934 1.00 81.22 C ANISOU 1171 CE2 TYR A 174 13224 9389 8248 478 684 47 C ATOM 1172 CZ TYR A 174 -5.198 2.847 59.981 1.00 89.46 C ANISOU 1172 CZ TYR A 174 14255 10438 9296 493 758 18 C ATOM 1173 OH TYR A 174 -5.414 4.026 60.662 1.00 93.00 O ANISOU 1173 OH TYR A 174 14774 10874 9689 524 753 -13 O ATOM 1174 N ARG A 175 -4.807 -1.509 61.099 1.00 81.97 N ANISOU 1174 N ARG A 175 13436 9422 8285 462 913 150 N ATOM 1175 CA ARG A 175 -4.365 -1.082 62.421 1.00 82.83 C ANISOU 1175 CA ARG A 175 13651 9527 8292 513 879 161 C ATOM 1176 C ARG A 175 -3.584 -2.128 63.287 1.00 89.21 C ANISOU 1176 C ARG A 175 14577 10307 9011 565 882 219 C ATOM 1177 O ARG A 175 -4.009 -3.273 63.476 1.00 89.15 O ANISOU 1177 O ARG A 175 14635 10251 8987 558 983 253 O ATOM 1178 CB ARG A 175 -5.564 -0.553 63.228 1.00 84.08 C ANISOU 1178 CB ARG A 175 13846 9687 8414 510 963 129 C ATOM 1179 CG ARG A 175 -5.981 0.847 62.794 1.00 87.00 C ANISOU 1179 CG ARG A 175 14146 10089 8820 511 927 76 C ATOM 1180 CD ARG A 175 -6.751 1.621 63.844 1.00 89.71 C ANISOU 1180 CD ARG A 175 14554 10436 9096 539 974 48 C ATOM 1181 NE ARG A 175 -7.178 2.924 63.316 1.00100.85 N ANISOU 1181 NE ARG A 175 15913 11869 10538 557 951 2 N ATOM 1182 CZ ARG A 175 -7.840 3.847 64.008 1.00112.45 C ANISOU 1182 CZ ARG A 175 17431 13340 11954 595 984 -30 C ATOM 1183 NH1 ARG A 175 -8.160 3.637 65.276 1.00103.60 N ANISOU 1183 NH1 ARG A 175 16403 12210 10752 611 1037 -24 N ATOM 1184 NH2 ARG A 175 -8.175 4.997 63.436 1.00 98.75 N ANISOU 1184 NH2 ARG A 175 15666 11613 10240 627 967 -66 N ATOM 1185 N ALA A 176 -2.427 -1.652 63.838 1.00 86.57 N ANISOU 1185 N ALA A 176 14275 10011 8607 619 771 225 N ATOM 1186 CA ALA A 176 -1.498 -2.343 64.746 1.00 86.64 C ANISOU 1186 CA ALA A 176 14384 10030 8504 701 739 273 C ATOM 1187 C ALA A 176 -2.030 -2.259 66.166 1.00 92.46 C ANISOU 1187 C ALA A 176 15244 10749 9139 735 799 278 C ATOM 1188 O ALA A 176 -2.768 -1.320 66.485 1.00 92.99 O ANISOU 1188 O ALA A 176 15301 10818 9214 699 820 232 O ATOM 1189 CB ALA A 176 -0.115 -1.713 64.662 1.00 86.99 C ANISOU 1189 CB ALA A 176 14377 10159 8515 730 592 255 C ATOM 1190 N THR A 177 -1.655 -3.210 67.027 1.00 89.83 N ANISOU 1190 N THR A 177 15034 10397 8700 814 829 335 N ATOM 1191 CA THR A 177 -2.199 -3.240 68.381 1.00 90.34 C ANISOU 1191 CA THR A 177 15228 10438 8661 849 899 346 C ATOM 1192 C THR A 177 -1.195 -2.814 69.483 1.00 94.95 C ANISOU 1192 C THR A 177 15871 11097 9107 940 797 347 C ATOM 1193 O THR A 177 -1.624 -2.662 70.629 1.00 94.88 O ANISOU 1193 O THR A 177 15965 11077 9009 968 843 348 O ATOM 1194 CB THR A 177 -2.811 -4.611 68.682 1.00 97.64 C ANISOU 1194 CB THR A 177 16278 11268 9551 864 1047 405 C ATOM 1195 OG1 THR A 177 -1.864 -5.634 68.367 1.00100.37 O ANISOU 1195 OG1 THR A 177 16670 11603 9864 940 1022 464 O ATOM 1196 CG2 THR A 177 -4.118 -4.845 67.918 1.00 93.24 C ANISOU 1196 CG2 THR A 177 15666 10655 9105 747 1173 377 C ATOM 1197 N HIS A 178 0.089 -2.538 69.150 1.00 92.15 N ANISOU 1197 N HIS A 178 15443 10835 8734 975 659 335 N ATOM 1198 CA HIS A 178 1.061 -2.081 70.166 1.00 93.02 C ANISOU 1198 CA HIS A 178 15586 11051 8706 1048 555 318 C ATOM 1199 C HIS A 178 0.767 -0.627 70.597 1.00 94.30 C ANISOU 1199 C HIS A 178 15721 11241 8866 974 518 237 C ATOM 1200 O HIS A 178 0.202 0.152 69.828 1.00 92.73 O ANISOU 1200 O HIS A 178 15446 11006 8781 878 531 192 O ATOM 1201 CB HIS A 178 2.517 -2.251 69.714 1.00 94.60 C ANISOU 1201 CB HIS A 178 15703 11367 8873 1103 425 319 C ATOM 1202 CG HIS A 178 2.863 -1.570 68.431 1.00 97.63 C ANISOU 1202 CG HIS A 178 15931 11780 9382 1004 355 268 C ATOM 1203 ND1 HIS A 178 3.573 -0.380 68.417 1.00 99.91 N ANISOU 1203 ND1 HIS A 178 16136 12169 9656 944 246 189 N ATOM 1204 CD2 HIS A 178 2.621 -1.953 67.157 1.00 98.69 C ANISOU 1204 CD2 HIS A 178 15994 11858 9647 957 387 285 C ATOM 1205 CE1 HIS A 178 3.730 -0.071 67.142 1.00 98.44 C ANISOU 1205 CE1 HIS A 178 15836 11976 9592 865 218 165 C ATOM 1206 NE2 HIS A 178 3.167 -0.985 66.344 1.00 98.16 N ANISOU 1206 NE2 HIS A 178 15798 11851 9647 875 296 222 N ATOM 1207 N GLN A 179 1.120 -0.298 71.841 1.00 91.11 N ANISOU 1207 N GLN A 179 15393 10899 8324 1028 480 221 N ATOM 1208 CA GLN A 179 0.843 0.969 72.522 1.00 90.94 C ANISOU 1208 CA GLN A 179 15391 10896 8267 973 461 148 C ATOM 1209 C GLN A 179 1.310 2.232 71.738 1.00 92.97 C ANISOU 1209 C GLN A 179 15535 11195 8596 866 373 63 C ATOM 1210 O GLN A 179 0.577 3.226 71.747 1.00 92.82 O ANISOU 1210 O GLN A 179 15529 11120 8618 798 410 14 O ATOM 1211 CB GLN A 179 1.443 0.951 73.949 1.00 93.91 C ANISOU 1211 CB GLN A 179 15860 11360 8463 1061 414 145 C ATOM 1212 CG GLN A 179 0.685 1.796 75.000 1.00105.93 C ANISOU 1212 CG GLN A 179 17473 12851 9926 1035 461 102 C ATOM 1213 CD GLN A 179 -0.735 1.354 75.306 1.00118.64 C ANISOU 1213 CD GLN A 179 19174 14335 11568 1042 615 148 C ATOM 1214 OE1 GLN A 179 -1.014 0.182 75.601 1.00112.96 O ANISOU 1214 OE1 GLN A 179 18537 13571 10814 1114 694 225 O ATOM 1215 NE2 GLN A 179 -1.663 2.305 75.270 1.00108.37 N ANISOU 1215 NE2 GLN A 179 17870 12979 10326 968 667 97 N ATOM 1216 N GLU A 180 2.475 2.198 71.054 1.00 88.10 N ANISOU 1216 N GLU A 180 14816 10669 7988 855 268 47 N ATOM 1217 CA GLU A 180 2.966 3.350 70.271 1.00 87.00 C ANISOU 1217 CA GLU A 180 14582 10563 7912 741 197 -34 C ATOM 1218 C GLU A 180 2.035 3.636 69.069 1.00 89.30 C ANISOU 1218 C GLU A 180 14828 10736 8365 673 268 -29 C ATOM 1219 O GLU A 180 1.774 4.799 68.767 1.00 89.94 O ANISOU 1219 O GLU A 180 14905 10781 8488 592 269 -91 O ATOM 1220 CB GLU A 180 4.410 3.128 69.802 1.00 88.71 C ANISOU 1220 CB GLU A 180 14692 10917 8098 745 80 -52 C ATOM 1221 N ALA A 181 1.508 2.578 68.420 1.00 83.45 N ANISOU 1221 N ALA A 181 14067 9937 7703 711 332 42 N ATOM 1222 CA ALA A 181 0.544 2.679 67.332 1.00 81.50 C ANISOU 1222 CA ALA A 181 13770 9600 7596 661 404 48 C ATOM 1223 C ALA A 181 -0.822 3.206 67.855 1.00 84.48 C ANISOU 1223 C ALA A 181 14218 9903 7978 653 505 33 C ATOM 1224 O ALA A 181 -1.337 4.200 67.342 1.00 82.56 O ANISOU 1224 O ALA A 181 13951 9624 7794 604 520 -11 O ATOM 1225 CB ALA A 181 0.374 1.324 66.664 1.00 81.60 C ANISOU 1225 CB ALA A 181 13753 9584 7668 698 452 118 C ATOM 1226 N ILE A 182 -1.361 2.556 68.905 1.00 82.41 N ANISOU 1226 N ILE A 182 14050 9621 7641 709 575 70 N ATOM 1227 CA ILE A 182 -2.627 2.855 69.593 1.00 82.80 C ANISOU 1227 CA ILE A 182 14170 9616 7672 714 679 61 C ATOM 1228 C ILE A 182 -2.692 4.338 70.045 1.00 86.17 C ANISOU 1228 C ILE A 182 14634 10047 8061 687 649 -11 C ATOM 1229 O ILE A 182 -3.731 4.980 69.866 1.00 84.99 O ANISOU 1229 O ILE A 182 14486 9853 7955 674 718 -36 O ATOM 1230 CB ILE A 182 -2.812 1.859 70.792 1.00 86.89 C ANISOU 1230 CB ILE A 182 14802 10127 8085 783 742 113 C ATOM 1231 CG1 ILE A 182 -3.069 0.399 70.315 1.00 86.99 C ANISOU 1231 CG1 ILE A 182 14813 10099 8140 799 818 182 C ATOM 1232 CG2 ILE A 182 -3.871 2.308 71.805 1.00 87.54 C ANISOU 1232 CG2 ILE A 182 14972 10176 8112 792 831 94 C ATOM 1233 CD1 ILE A 182 -4.363 0.161 69.450 1.00 98.11 C ANISOU 1233 CD1 ILE A 182 16159 11454 9666 736 931 177 C ATOM 1234 N ASN A 183 -1.597 4.874 70.605 1.00 83.76 N ANISOU 1234 N ASN A 183 14356 9800 7668 679 551 -48 N ATOM 1235 CA ASN A 183 -1.582 6.269 71.052 1.00 84.73 C ANISOU 1235 CA ASN A 183 14533 9915 7744 637 529 -124 C ATOM 1236 C ASN A 183 -1.624 7.231 69.878 1.00 89.06 C ANISOU 1236 C ASN A 183 15025 10423 8389 571 516 -167 C ATOM 1237 O ASN A 183 -2.299 8.244 69.976 1.00 89.72 O ANISOU 1237 O ASN A 183 15167 10449 8472 560 563 -208 O ATOM 1238 CB ASN A 183 -0.385 6.582 71.952 1.00 84.27 C ANISOU 1238 CB ASN A 183 14514 9946 7557 627 432 -167 C ATOM 1239 CG ASN A 183 -0.406 5.870 73.269 1.00 98.40 C ANISOU 1239 CG ASN A 183 16388 11774 9224 708 448 -132 C ATOM 1240 OD1 ASN A 183 -1.454 5.696 73.914 1.00 90.51 O ANISOU 1240 OD1 ASN A 183 15468 10715 8206 751 545 -106 O ATOM 1241 ND2 ASN A 183 0.768 5.446 73.696 1.00 91.42 N ANISOU 1241 ND2 ASN A 183 15488 11001 8246 738 355 -133 N ATOM 1242 N CYS A 184 -0.932 6.917 68.780 1.00 86.00 N ANISOU 1242 N CYS A 184 14537 10062 8077 537 459 -156 N ATOM 1243 CA CYS A 184 -0.897 7.728 67.555 1.00 85.43 C ANISOU 1243 CA CYS A 184 14412 9950 8097 478 448 -188 C ATOM 1244 C CYS A 184 -2.285 7.871 66.902 1.00 88.50 C ANISOU 1244 C CYS A 184 14787 10265 8572 512 546 -168 C ATOM 1245 O CYS A 184 -2.594 8.938 66.382 1.00 88.49 O ANISOU 1245 O CYS A 184 14810 10213 8598 494 564 -207 O ATOM 1246 CB CYS A 184 0.105 7.146 66.568 1.00 85.32 C ANISOU 1246 CB CYS A 184 14287 9991 8141 446 373 -171 C ATOM 1247 SG CYS A 184 0.367 8.168 65.104 1.00 88.73 S ANISOU 1247 SG CYS A 184 14666 10379 8667 365 352 -213 S ATOM 1248 N TYR A 185 -3.089 6.797 66.885 1.00 85.24 N ANISOU 1248 N TYR A 185 14337 9854 8195 561 611 -113 N ATOM 1249 CA TYR A 185 -4.446 6.806 66.326 1.00 85.00 C ANISOU 1249 CA TYR A 185 14270 9793 8234 592 706 -103 C ATOM 1250 C TYR A 185 -5.388 7.713 67.134 1.00 90.32 C ANISOU 1250 C TYR A 185 15035 10436 8848 632 774 -137 C ATOM 1251 O TYR A 185 -6.283 8.318 66.550 1.00 90.91 O ANISOU 1251 O TYR A 185 15087 10491 8962 663 826 -153 O ATOM 1252 CB TYR A 185 -5.050 5.383 66.278 1.00 86.25 C ANISOU 1252 CB TYR A 185 14376 9970 8426 610 772 -49 C ATOM 1253 CG TYR A 185 -4.249 4.322 65.556 1.00 87.33 C ANISOU 1253 CG TYR A 185 14441 10126 8613 587 725 -8 C ATOM 1254 CD1 TYR A 185 -3.770 4.535 64.265 1.00 88.38 C ANISOU 1254 CD1 TYR A 185 14484 10266 8831 554 671 -15 C ATOM 1255 CD2 TYR A 185 -4.080 3.054 66.112 1.00 88.16 C ANISOU 1255 CD2 TYR A 185 14577 10238 8680 607 752 42 C ATOM 1256 CE1 TYR A 185 -3.068 3.544 63.579 1.00 88.41 C ANISOU 1256 CE1 TYR A 185 14422 10289 8881 540 633 22 C ATOM 1257 CE2 TYR A 185 -3.378 2.054 65.436 1.00 88.36 C ANISOU 1257 CE2 TYR A 185 14553 10275 8746 601 719 82 C ATOM 1258 CZ TYR A 185 -2.879 2.300 64.166 1.00 92.27 C ANISOU 1258 CZ TYR A 185 14948 10784 9328 566 658 70 C ATOM 1259 OH TYR A 185 -2.183 1.318 63.498 1.00 89.23 O ANISOU 1259 OH TYR A 185 14515 10411 8979 567 628 109 O ATOM 1260 N ALA A 186 -5.207 7.776 68.471 1.00 87.66 N ANISOU 1260 N ALA A 186 14799 10102 8406 644 774 -146 N ATOM 1261 CA ALA A 186 -6.031 8.574 69.383 1.00 88.21 C ANISOU 1261 CA ALA A 186 14968 10144 8405 685 839 -177 C ATOM 1262 C ALA A 186 -5.767 10.066 69.234 1.00 92.69 C ANISOU 1262 C ALA A 186 15610 10661 8947 670 812 -238 C ATOM 1263 O ALA A 186 -6.725 10.831 69.092 1.00 93.99 O ANISOU 1263 O ALA A 186 15808 10789 9114 723 880 -257 O ATOM 1264 CB ALA A 186 -5.791 8.146 70.818 1.00 89.72 C ANISOU 1264 CB ALA A 186 15247 10355 8486 700 840 -168 C ATOM 1265 N GLU A 187 -4.482 10.482 69.253 1.00 88.17 N ANISOU 1265 N GLU A 187 15067 10092 8343 599 720 -271 N ATOM 1266 CA GLU A 187 -4.104 11.880 69.119 1.00 88.28 C ANISOU 1266 CA GLU A 187 15173 10046 8325 556 704 -337 C ATOM 1267 C GLU A 187 -4.181 12.350 67.692 1.00 94.29 C ANISOU 1267 C GLU A 187 15884 10763 9178 547 708 -337 C ATOM 1268 O GLU A 187 -3.609 11.743 66.782 1.00 93.97 O ANISOU 1268 O GLU A 187 15734 10758 9213 510 656 -312 O ATOM 1269 CB GLU A 187 -2.726 12.189 69.713 1.00 90.16 C ANISOU 1269 CB GLU A 187 15457 10320 8482 463 614 -389 C ATOM 1270 CG GLU A 187 -1.610 11.234 69.360 1.00 98.27 C ANISOU 1270 CG GLU A 187 16368 11438 9533 417 522 -366 C ATOM 1271 CD GLU A 187 -0.516 11.155 70.400 1.00114.99 C ANISOU 1271 CD GLU A 187 18514 13643 11534 371 444 -406 C ATOM 1272 OE1 GLU A 187 -0.805 10.714 71.535 1.00 95.71 O ANISOU 1272 OE1 GLU A 187 16122 11231 9012 429 461 -389 O ATOM 1273 OE2 GLU A 187 0.635 11.531 70.080 1.00116.29 O ANISOU 1273 OE2 GLU A 187 18647 13857 11681 278 366 -460 O ATOM 1274 N GLU A 188 -4.911 13.464 67.515 1.00 93.46 N ANISOU 1274 N GLU A 188 15872 10579 9058 594 774 -365 N ATOM 1275 CA GLU A 188 -5.162 14.174 66.258 1.00 93.69 C ANISOU 1275 CA GLU A 188 15901 10549 9148 616 798 -369 C ATOM 1276 C GLU A 188 -3.866 14.727 65.634 1.00 97.82 C ANISOU 1276 C GLU A 188 16450 11036 9679 498 731 -408 C ATOM 1277 O GLU A 188 -3.798 14.907 64.416 1.00 97.14 O ANISOU 1277 O GLU A 188 16321 10924 9663 497 729 -395 O ATOM 1278 CB GLU A 188 -6.147 15.333 66.519 1.00 96.20 C ANISOU 1278 CB GLU A 188 16358 10786 9406 711 889 -395 C ATOM 1279 CG GLU A 188 -7.608 15.002 66.228 1.00108.52 C ANISOU 1279 CG GLU A 188 17842 12389 11000 850 966 -355 C ATOM 1280 CD GLU A 188 -8.341 14.100 67.204 1.00133.27 C ANISOU 1280 CD GLU A 188 20922 15604 14113 888 1001 -333 C ATOM 1281 OE1 GLU A 188 -8.008 14.117 68.412 1.00139.43 O ANISOU 1281 OE1 GLU A 188 21787 16375 14814 853 993 -352 O ATOM 1282 OE2 GLU A 188 -9.294 13.416 66.766 1.00124.62 O ANISOU 1282 OE2 GLU A 188 19700 14580 13068 953 1046 -301 O ATOM 1283 N THR A 189 -2.848 14.998 66.479 1.00 95.28 N ANISOU 1283 N THR A 189 16197 10726 9279 396 680 -461 N ATOM 1284 CA THR A 189 -1.529 15.545 66.120 1.00 94.85 C ANISOU 1284 CA THR A 189 16167 10662 9207 255 620 -519 C ATOM 1285 C THR A 189 -0.539 14.442 65.657 1.00 94.91 C ANISOU 1285 C THR A 189 16005 10786 9271 195 524 -493 C ATOM 1286 O THR A 189 0.637 14.745 65.418 1.00 95.03 O ANISOU 1286 O THR A 189 16009 10831 9266 73 465 -546 O ATOM 1287 CB THR A 189 -0.945 16.346 67.298 1.00106.75 C ANISOU 1287 CB THR A 189 17816 12155 10590 168 613 -604 C ATOM 1288 OG1 THR A 189 -0.769 15.478 68.424 1.00108.29 O ANISOU 1288 OG1 THR A 189 17957 12458 10731 185 567 -592 O ATOM 1289 CG2 THR A 189 -1.807 17.541 67.683 1.00106.60 C ANISOU 1289 CG2 THR A 189 17989 12004 10509 222 713 -636 C ATOM 1290 N CYS A 190 -1.014 13.185 65.527 1.00 87.87 N ANISOU 1290 N CYS A 190 14988 9960 8441 277 516 -418 N ATOM 1291 CA CYS A 190 -0.190 12.072 65.060 1.00 86.46 C ANISOU 1291 CA CYS A 190 14662 9878 8311 247 439 -383 C ATOM 1292 C CYS A 190 -0.813 11.426 63.831 1.00 89.69 C ANISOU 1292 C CYS A 190 14964 10276 8840 305 465 -320 C ATOM 1293 O CYS A 190 -2.015 11.124 63.817 1.00 89.01 O ANISOU 1293 O CYS A 190 14868 10167 8784 396 534 -280 O ATOM 1294 CB CYS A 190 0.038 11.044 66.160 1.00 86.74 C ANISOU 1294 CB CYS A 190 14667 10006 8286 281 404 -357 C ATOM 1295 SG CYS A 190 1.328 9.817 65.791 1.00 90.01 S ANISOU 1295 SG CYS A 190 14934 10547 8717 255 300 -327 S ATOM 1296 N CYS A 191 0.018 11.233 62.794 1.00 85.07 N ANISOU 1296 N CYS A 191 14291 9718 8315 246 410 -317 N ATOM 1297 CA CYS A 191 -0.391 10.579 61.567 1.00 83.87 C ANISOU 1297 CA CYS A 191 14028 9567 8272 287 422 -263 C ATOM 1298 C CYS A 191 0.767 9.775 61.001 1.00 88.92 C ANISOU 1298 C CYS A 191 14553 10286 8948 232 340 -249 C ATOM 1299 O CYS A 191 1.294 10.077 59.936 1.00 90.17 O ANISOU 1299 O CYS A 191 14668 10435 9158 181 315 -261 O ATOM 1300 CB CYS A 191 -0.952 11.567 60.552 1.00 83.76 C ANISOU 1300 CB CYS A 191 14056 9467 8303 303 473 -275 C ATOM 1301 SG CYS A 191 -1.805 10.786 59.160 1.00 86.65 S ANISOU 1301 SG CYS A 191 14286 9849 8788 379 503 -214 S ATOM 1302 N ASP A 192 1.183 8.748 61.749 1.00 84.50 N ANISOU 1302 N ASP A 192 13951 9805 8349 253 301 -224 N ATOM 1303 CA ASP A 192 2.204 7.815 61.311 1.00 83.39 C ANISOU 1303 CA ASP A 192 13703 9751 8230 236 229 -200 C ATOM 1304 C ASP A 192 1.445 6.576 60.911 1.00 86.30 C ANISOU 1304 C ASP A 192 14010 10112 8669 314 272 -126 C ATOM 1305 O ASP A 192 0.577 6.122 61.663 1.00 86.85 O ANISOU 1305 O ASP A 192 14125 10161 8713 373 331 -98 O ATOM 1306 CB ASP A 192 3.263 7.571 62.395 1.00 86.02 C ANISOU 1306 CB ASP A 192 14044 10187 8452 221 156 -226 C ATOM 1307 CG ASP A 192 4.225 8.723 62.633 1.00102.01 C ANISOU 1307 CG ASP A 192 16103 12249 10408 110 105 -317 C ATOM 1308 OD1 ASP A 192 4.077 9.778 61.972 1.00103.82 O ANISOU 1308 OD1 ASP A 192 16375 12398 10674 40 136 -358 O ATOM 1309 OD2 ASP A 192 5.128 8.573 63.478 1.00111.76 O ANISOU 1309 OD2 ASP A 192 17326 13596 11543 92 40 -351 O ATOM 1310 N PHE A 193 1.657 6.117 59.677 1.00 81.56 N ANISOU 1310 N PHE A 193 13314 9519 8157 303 257 -101 N ATOM 1311 CA PHE A 193 0.931 4.978 59.132 1.00 80.33 C ANISOU 1311 CA PHE A 193 13099 9350 8072 356 306 -42 C ATOM 1312 C PHE A 193 1.504 3.671 59.704 1.00 85.48 C ANISOU 1312 C PHE A 193 13741 10057 8681 398 282 3 C ATOM 1313 O PHE A 193 2.408 3.051 59.120 1.00 85.72 O ANISOU 1313 O PHE A 193 13703 10137 8732 396 228 21 O ATOM 1314 CB PHE A 193 0.942 5.007 57.579 1.00 80.59 C ANISOU 1314 CB PHE A 193 13041 9370 8208 330 301 -36 C ATOM 1315 CG PHE A 193 0.092 4.013 56.814 1.00 80.55 C ANISOU 1315 CG PHE A 193 12969 9354 8284 364 358 6 C ATOM 1316 CD1 PHE A 193 -1.145 3.605 57.299 1.00 82.98 C ANISOU 1316 CD1 PHE A 193 13302 9641 8587 402 444 20 C ATOM 1317 CD2 PHE A 193 0.502 3.534 55.572 1.00 81.87 C ANISOU 1317 CD2 PHE A 193 13043 9536 8526 346 332 23 C ATOM 1318 CE1 PHE A 193 -1.929 2.690 56.581 1.00 83.68 C ANISOU 1318 CE1 PHE A 193 13323 9731 8742 409 504 44 C ATOM 1319 CE2 PHE A 193 -0.287 2.626 54.853 1.00 83.61 C ANISOU 1319 CE2 PHE A 193 13203 9751 8814 363 389 51 C ATOM 1320 CZ PHE A 193 -1.495 2.210 55.362 1.00 81.66 C ANISOU 1320 CZ PHE A 193 12979 9489 8559 388 476 57 C ATOM 1321 N PHE A 194 0.998 3.301 60.898 1.00 81.49 N ANISOU 1321 N PHE A 194 13316 9542 8105 445 327 20 N ATOM 1322 CA PHE A 194 1.302 2.050 61.580 1.00 80.87 C ANISOU 1322 CA PHE A 194 13267 9491 7968 508 332 72 C ATOM 1323 C PHE A 194 0.364 1.011 61.025 1.00 86.11 C ANISOU 1323 C PHE A 194 13914 10099 8703 525 423 118 C ATOM 1324 O PHE A 194 -0.822 1.310 60.821 1.00 85.37 O ANISOU 1324 O PHE A 194 13819 9960 8657 504 500 105 O ATOM 1325 CB PHE A 194 1.147 2.168 63.106 1.00 82.62 C ANISOU 1325 CB PHE A 194 13598 9722 8074 548 348 68 C ATOM 1326 CG PHE A 194 2.138 3.072 63.796 1.00 83.76 C ANISOU 1326 CG PHE A 194 13762 9939 8127 525 258 13 C ATOM 1327 CD1 PHE A 194 3.448 2.655 64.021 1.00 86.39 C ANISOU 1327 CD1 PHE A 194 14060 10377 8387 553 167 15 C ATOM 1328 CD2 PHE A 194 1.760 4.339 64.238 1.00 84.50 C ANISOU 1328 CD2 PHE A 194 13909 10003 8194 478 268 -46 C ATOM 1329 CE1 PHE A 194 4.366 3.502 64.655 1.00 87.57 C ANISOU 1329 CE1 PHE A 194 14211 10619 8443 515 84 -52 C ATOM 1330 CE2 PHE A 194 2.670 5.167 64.905 1.00 86.97 C ANISOU 1330 CE2 PHE A 194 14248 10383 8414 437 194 -108 C ATOM 1331 CZ PHE A 194 3.968 4.752 65.096 1.00 85.48 C ANISOU 1331 CZ PHE A 194 14007 10315 8157 446 101 -116 C ATOM 1332 N THR A 195 0.899 -0.184 60.700 1.00 83.67 N ANISOU 1332 N THR A 195 13590 9802 8399 560 418 167 N ATOM 1333 CA THR A 195 0.104 -1.281 60.145 1.00 82.94 C ANISOU 1333 CA THR A 195 13494 9653 8368 559 513 205 C ATOM 1334 C THR A 195 0.448 -2.584 60.865 1.00 88.48 C ANISOU 1334 C THR A 195 14291 10337 8989 631 549 265 C ATOM 1335 O THR A 195 1.540 -2.718 61.430 1.00 89.94 O ANISOU 1335 O THR A 195 14507 10579 9088 698 473 282 O ATOM 1336 CB THR A 195 0.289 -1.414 58.600 1.00 87.06 C ANISOU 1336 CB THR A 195 13902 10178 8999 518 490 200 C ATOM 1337 OG1 THR A 195 1.601 -1.875 58.288 1.00 88.52 O ANISOU 1337 OG1 THR A 195 14058 10410 9164 553 409 224 O ATOM 1338 CG2 THR A 195 -0.009 -0.123 57.835 1.00 78.81 C ANISOU 1338 CG2 THR A 195 12781 9144 8021 463 460 147 C ATOM 1339 N ASN A 196 -0.496 -3.539 60.870 1.00 84.08 N ANISOU 1339 N ASN A 196 13789 9708 8451 620 670 292 N ATOM 1340 CA ASN A 196 -0.241 -4.873 61.405 1.00 83.55 C ANISOU 1340 CA ASN A 196 13840 9596 8310 687 730 355 C ATOM 1341 C ASN A 196 0.566 -5.606 60.322 1.00 86.95 C ANISOU 1341 C ASN A 196 14219 10031 8786 707 693 383 C ATOM 1342 O ASN A 196 0.476 -5.247 59.149 1.00 86.27 O ANISOU 1342 O ASN A 196 14013 9960 8805 642 665 351 O ATOM 1343 CB ASN A 196 -1.538 -5.602 61.816 1.00 81.04 C ANISOU 1343 CB ASN A 196 13614 9191 7988 646 889 366 C ATOM 1344 CG ASN A 196 -2.577 -5.832 60.736 1.00 94.97 C ANISOU 1344 CG ASN A 196 15295 10925 9864 540 975 332 C ATOM 1345 OD1 ASN A 196 -2.365 -6.553 59.745 1.00 86.40 O ANISOU 1345 OD1 ASN A 196 14175 9817 8836 518 989 344 O ATOM 1346 ND2 ASN A 196 -3.769 -5.298 60.961 1.00 81.44 N ANISOU 1346 ND2 ASN A 196 13553 9219 8172 477 1043 286 N ATOM 1347 N GLN A 197 1.372 -6.587 60.707 1.00 84.52 N ANISOU 1347 N GLN A 197 14004 9715 8394 809 690 441 N ATOM 1348 CA GLN A 197 2.253 -7.321 59.799 1.00 83.34 C ANISOU 1348 CA GLN A 197 13821 9576 8266 855 653 473 C ATOM 1349 C GLN A 197 1.489 -8.046 58.685 1.00 85.33 C ANISOU 1349 C GLN A 197 14056 9741 8623 771 753 471 C ATOM 1350 O GLN A 197 2.006 -8.133 57.574 1.00 84.31 O ANISOU 1350 O GLN A 197 13833 9638 8563 759 703 465 O ATOM 1351 CB GLN A 197 3.134 -8.292 60.591 1.00 85.68 C ANISOU 1351 CB GLN A 197 14251 9876 8426 1009 650 542 C ATOM 1352 CG GLN A 197 4.127 -7.543 61.497 1.00101.29 C ANISOU 1352 CG GLN A 197 16203 11988 10296 1095 521 531 C ATOM 1353 CD GLN A 197 5.114 -8.406 62.250 1.00130.88 C ANISOU 1353 CD GLN A 197 20058 15781 13890 1275 496 595 C ATOM 1354 OE1 GLN A 197 5.051 -9.639 62.251 1.00132.04 O ANISOU 1354 OE1 GLN A 197 20340 15834 13993 1357 589 662 O ATOM 1355 NE2 GLN A 197 6.054 -7.766 62.923 1.00122.63 N ANISOU 1355 NE2 GLN A 197 18962 14886 12747 1345 372 573 N ATOM 1356 N ALA A 198 0.254 -8.504 58.950 1.00 81.54 N ANISOU 1356 N ALA A 198 13654 9172 8156 701 894 466 N ATOM 1357 CA ALA A 198 -0.554 -9.197 57.942 1.00 80.78 C ANISOU 1357 CA ALA A 198 13536 9008 8149 601 999 448 C ATOM 1358 C ALA A 198 -1.021 -8.244 56.814 1.00 83.38 C ANISOU 1358 C ALA A 198 13676 9403 8603 502 948 380 C ATOM 1359 O ALA A 198 -1.059 -8.667 55.664 1.00 82.67 O ANISOU 1359 O ALA A 198 13520 9302 8588 453 963 368 O ATOM 1360 CB ALA A 198 -1.753 -9.881 58.589 1.00 82.19 C ANISOU 1360 CB ALA A 198 13839 9096 8295 536 1168 445 C ATOM 1361 N TYR A 199 -1.365 -6.976 57.137 1.00 79.47 N ANISOU 1361 N TYR A 199 13105 8970 8120 481 893 338 N ATOM 1362 CA TYR A 199 -1.793 -5.966 56.148 1.00 77.77 C ANISOU 1362 CA TYR A 199 12733 8813 8002 414 845 280 C ATOM 1363 C TYR A 199 -0.588 -5.541 55.292 1.00 81.80 C ANISOU 1363 C TYR A 199 13155 9374 8550 446 716 285 C ATOM 1364 O TYR A 199 -0.691 -5.486 54.063 1.00 80.28 O ANISOU 1364 O TYR A 199 12861 9197 8443 400 704 263 O ATOM 1365 CB TYR A 199 -2.452 -4.731 56.842 1.00 77.59 C ANISOU 1365 CB TYR A 199 12691 8828 7961 404 833 240 C ATOM 1366 CG TYR A 199 -2.743 -3.575 55.903 1.00 76.98 C ANISOU 1366 CG TYR A 199 12480 8807 7962 370 776 190 C ATOM 1367 CD1 TYR A 199 -3.931 -3.517 55.181 1.00 78.35 C ANISOU 1367 CD1 TYR A 199 12570 9001 8198 310 847 147 C ATOM 1368 CD2 TYR A 199 -1.819 -2.548 55.723 1.00 76.77 C ANISOU 1368 CD2 TYR A 199 12415 8817 7937 397 658 182 C ATOM 1369 CE1 TYR A 199 -4.180 -2.479 54.276 1.00 77.51 C ANISOU 1369 CE1 TYR A 199 12354 8948 8150 304 797 108 C ATOM 1370 CE2 TYR A 199 -2.052 -1.512 54.821 1.00 76.52 C ANISOU 1370 CE2 TYR A 199 12290 8818 7968 373 618 142 C ATOM 1371 CZ TYR A 199 -3.242 -1.470 54.110 1.00 81.56 C ANISOU 1371 CZ TYR A 199 12855 9471 8662 339 687 111 C ATOM 1372 OH TYR A 199 -3.473 -0.426 53.235 1.00 76.12 O ANISOU 1372 OH TYR A 199 12088 8815 8020 340 650 77 O ATOM 1373 N ALA A 200 0.542 -5.218 55.960 1.00 79.86 N ANISOU 1373 N ALA A 200 12943 9167 8232 521 621 308 N ATOM 1374 CA ALA A 200 1.787 -4.788 55.328 1.00 79.68 C ANISOU 1374 CA ALA A 200 12838 9212 8224 546 500 306 C ATOM 1375 C ALA A 200 2.227 -5.789 54.254 1.00 85.81 C ANISOU 1375 C ALA A 200 13584 9972 9050 555 509 334 C ATOM 1376 O ALA A 200 2.494 -5.361 53.135 1.00 86.50 O ANISOU 1376 O ALA A 200 13560 10092 9213 515 458 309 O ATOM 1377 CB ALA A 200 2.879 -4.610 56.370 1.00 80.82 C ANISOU 1377 CB ALA A 200 13032 9418 8258 628 418 323 C ATOM 1378 N ILE A 201 2.227 -7.110 54.565 1.00 82.31 N ANISOU 1378 N ILE A 201 13250 9465 8559 606 587 383 N ATOM 1379 CA ILE A 201 2.591 -8.167 53.621 1.00 81.56 C ANISOU 1379 CA ILE A 201 13157 9334 8497 621 615 411 C ATOM 1380 C ILE A 201 1.530 -8.284 52.517 1.00 83.79 C ANISOU 1380 C ILE A 201 13370 9577 8889 506 690 371 C ATOM 1381 O ILE A 201 1.870 -8.119 51.352 1.00 83.45 O ANISOU 1381 O ILE A 201 13221 9567 8920 480 641 355 O ATOM 1382 CB ILE A 201 2.832 -9.534 54.323 1.00 85.94 C ANISOU 1382 CB ILE A 201 13885 9814 8956 714 696 476 C ATOM 1383 CG1 ILE A 201 3.984 -9.473 55.350 1.00 87.82 C ANISOU 1383 CG1 ILE A 201 14178 10120 9068 856 610 517 C ATOM 1384 CG2 ILE A 201 3.049 -10.665 53.313 1.00 86.63 C ANISOU 1384 CG2 ILE A 201 13998 9840 9079 721 750 501 C ATOM 1385 CD1 ILE A 201 5.411 -9.140 54.808 1.00100.36 C ANISOU 1385 CD1 ILE A 201 15652 11833 10648 926 469 517 C ATOM 1386 N ALA A 202 0.265 -8.562 52.880 1.00 79.71 N ANISOU 1386 N ALA A 202 12906 9004 8377 437 809 351 N ATOM 1387 CA ALA A 202 -0.850 -8.768 51.953 1.00 78.89 C ANISOU 1387 CA ALA A 202 12732 8886 8357 324 892 301 C ATOM 1388 C ALA A 202 -1.063 -7.617 50.937 1.00 80.79 C ANISOU 1388 C ALA A 202 12801 9211 8685 279 813 250 C ATOM 1389 O ALA A 202 -1.081 -7.905 49.745 1.00 80.05 O ANISOU 1389 O ALA A 202 12629 9127 8658 239 814 232 O ATOM 1390 CB ALA A 202 -2.140 -9.036 52.719 1.00 80.30 C ANISOU 1390 CB ALA A 202 12980 9026 8507 257 1023 276 C ATOM 1391 N SER A 203 -1.192 -6.347 51.378 1.00 77.83 N ANISOU 1391 N SER A 203 12381 8888 8302 292 750 228 N ATOM 1392 CA SER A 203 -1.398 -5.221 50.451 1.00 77.98 C ANISOU 1392 CA SER A 203 12269 8972 8389 267 687 185 C ATOM 1393 C SER A 203 -0.167 -4.897 49.554 1.00 82.52 C ANISOU 1393 C SER A 203 12779 9575 8999 294 578 199 C ATOM 1394 O SER A 203 -0.366 -4.372 48.458 1.00 81.76 O ANISOU 1394 O SER A 203 12583 9514 8969 264 552 170 O ATOM 1395 CB SER A 203 -1.827 -3.953 51.187 1.00 82.09 C ANISOU 1395 CB SER A 203 12789 9522 8880 281 661 160 C ATOM 1396 OG SER A 203 -0.746 -3.373 51.896 1.00 93.04 O ANISOU 1396 OG SER A 203 14224 10914 10214 333 573 182 O ATOM 1397 N SER A 204 1.080 -5.163 50.021 1.00 79.45 N ANISOU 1397 N SER A 204 12441 9186 8559 354 515 240 N ATOM 1398 CA SER A 204 2.304 -4.894 49.248 1.00 78.81 C ANISOU 1398 CA SER A 204 12292 9152 8501 375 415 247 C ATOM 1399 C SER A 204 2.387 -5.796 48.016 1.00 83.18 C ANISOU 1399 C SER A 204 12799 9689 9116 358 441 256 C ATOM 1400 O SER A 204 2.759 -5.319 46.940 1.00 82.22 O ANISOU 1400 O SER A 204 12583 9604 9052 336 387 239 O ATOM 1401 CB SER A 204 3.556 -5.072 50.109 1.00 82.49 C ANISOU 1401 CB SER A 204 12812 9652 8880 451 349 281 C ATOM 1402 OG SER A 204 3.669 -4.062 51.099 1.00 88.72 O ANISOU 1402 OG SER A 204 13624 10474 9612 455 305 260 O ATOM 1403 N ILE A 205 2.022 -7.090 48.176 1.00 81.23 N ANISOU 1403 N ILE A 205 12632 9379 8852 363 534 280 N ATOM 1404 CA AILE A 205 2.104 -8.030 47.063 0.50 81.31 C ANISOU 1404 CA AILE A 205 12619 9362 8911 343 570 285 C ATOM 1405 CA BILE A 205 2.040 -8.109 47.123 0.50 80.54 C ANISOU 1405 CA BILE A 205 12532 9260 8812 342 579 286 C ATOM 1406 C ILE A 205 0.911 -7.849 46.104 1.00 84.63 C ANISOU 1406 C ILE A 205 12951 9792 9410 247 624 230 C ATOM 1407 O ILE A 205 1.151 -7.820 44.902 1.00 83.85 O ANISOU 1407 O ILE A 205 12766 9721 9372 227 592 216 O ATOM 1408 CB AILE A 205 2.329 -9.512 47.474 0.50 85.27 C ANISOU 1408 CB AILE A 205 13259 9782 9357 388 652 331 C ATOM 1409 CB BILE A 205 1.951 -9.534 47.762 0.50 83.66 C ANISOU 1409 CB BILE A 205 13079 9564 9145 372 683 326 C ATOM 1410 CG1AILE A 205 1.400 -9.958 48.611 0.50 86.20 C ANISOU 1410 CG1AILE A 205 13501 9833 9419 368 762 335 C ATOM 1411 CG1BILE A 205 3.261 -9.862 48.517 0.50 84.19 C ANISOU 1411 CG1BILE A 205 13227 9640 9123 501 623 387 C ATOM 1412 CG2AILE A 205 3.811 -9.734 47.834 0.50 86.71 C ANISOU 1412 CG2AILE A 205 13479 9996 9472 511 569 385 C ATOM 1413 CG2BILE A 205 1.616 -10.621 46.721 0.50 83.07 C ANISOU 1413 CG2BILE A 205 13013 9433 9116 318 768 316 C ATOM 1414 CD1AILE A 205 1.730 -11.321 49.154 0.50 94.86 C ANISOU 1414 CD1AILE A 205 14770 10835 10439 430 847 389 C ATOM 1415 CD1BILE A 205 3.173 -10.928 49.535 0.50 90.72 C ANISOU 1415 CD1BILE A 205 14233 10381 9857 562 716 434 C ATOM 1416 N VAL A 206 -0.319 -7.664 46.596 1.00 81.43 N ANISOU 1416 N VAL A 206 12556 9384 9000 195 699 196 N ATOM 1417 CA VAL A 206 -1.493 -7.469 45.733 1.00 80.89 C ANISOU 1417 CA VAL A 206 12385 9360 8988 116 748 135 C ATOM 1418 C VAL A 206 -1.452 -6.091 45.008 1.00 81.81 C ANISOU 1418 C VAL A 206 12383 9553 9148 134 655 110 C ATOM 1419 O VAL A 206 -1.840 -6.013 43.851 1.00 80.91 O ANISOU 1419 O VAL A 206 12172 9485 9086 102 655 76 O ATOM 1420 CB VAL A 206 -2.827 -7.681 46.516 1.00 86.27 C ANISOU 1420 CB VAL A 206 13101 10039 9639 58 859 98 C ATOM 1421 CG1 VAL A 206 -4.043 -7.498 45.617 1.00 86.40 C ANISOU 1421 CG1 VAL A 206 12990 10138 9701 -17 906 24 C ATOM 1422 CG2 VAL A 206 -2.877 -9.067 47.159 1.00 87.14 C ANISOU 1422 CG2 VAL A 206 13353 10055 9702 30 970 122 C ATOM 1423 N SER A 207 -0.970 -5.031 45.665 1.00 77.69 N ANISOU 1423 N SER A 207 11881 9042 8596 184 582 125 N ATOM 1424 CA SER A 207 -0.926 -3.680 45.094 1.00 75.63 C ANISOU 1424 CA SER A 207 11548 8829 8361 201 512 104 C ATOM 1425 C SER A 207 0.293 -3.420 44.235 1.00 76.80 C ANISOU 1425 C SER A 207 11658 8985 8539 216 426 123 C ATOM 1426 O SER A 207 0.183 -2.629 43.307 1.00 77.19 O ANISOU 1426 O SER A 207 11639 9065 8624 214 395 103 O ATOM 1427 CB SER A 207 -0.955 -2.617 46.197 1.00 78.80 C ANISOU 1427 CB SER A 207 12007 9225 8708 234 487 104 C ATOM 1428 OG SER A 207 -2.201 -2.528 46.868 1.00 84.25 O ANISOU 1428 OG SER A 207 12713 9925 9372 227 562 77 O ATOM 1429 N PHE A 208 1.457 -4.003 44.568 1.00 71.84 N ANISOU 1429 N PHE A 208 11073 8337 7885 239 388 161 N ATOM 1430 CA PHE A 208 2.692 -3.707 43.857 1.00 71.25 C ANISOU 1430 CA PHE A 208 10954 8290 7829 251 304 173 C ATOM 1431 C PHE A 208 3.400 -4.918 43.243 1.00 76.23 C ANISOU 1431 C PHE A 208 11574 8914 8476 266 306 201 C ATOM 1432 O PHE A 208 3.657 -4.895 42.040 1.00 77.40 O ANISOU 1432 O PHE A 208 11649 9082 8678 249 283 193 O ATOM 1433 CB PHE A 208 3.669 -2.978 44.796 1.00 73.36 C ANISOU 1433 CB PHE A 208 11261 8578 8035 274 234 181 C ATOM 1434 CG PHE A 208 4.995 -2.561 44.190 1.00 74.34 C ANISOU 1434 CG PHE A 208 11330 8751 8164 269 150 180 C ATOM 1435 CD1 PHE A 208 5.081 -1.439 43.365 1.00 76.11 C ANISOU 1435 CD1 PHE A 208 11506 8987 8424 228 119 152 C ATOM 1436 CD2 PHE A 208 6.168 -3.243 44.502 1.00 75.62 C ANISOU 1436 CD2 PHE A 208 11496 8955 8283 311 106 206 C ATOM 1437 CE1 PHE A 208 6.310 -1.035 42.828 1.00 76.30 C ANISOU 1437 CE1 PHE A 208 11483 9059 8448 205 52 144 C ATOM 1438 CE2 PHE A 208 7.398 -2.833 43.971 1.00 78.20 C ANISOU 1438 CE2 PHE A 208 11756 9351 8607 299 30 195 C ATOM 1439 CZ PHE A 208 7.458 -1.736 43.127 1.00 75.63 C ANISOU 1439 CZ PHE A 208 11380 9032 8324 234 7 162 C ATOM 1440 N TYR A 209 3.787 -5.921 44.049 1.00 71.68 N ANISOU 1440 N TYR A 209 11080 8308 7847 309 331 237 N ATOM 1441 CA TYR A 209 4.591 -7.052 43.592 1.00 70.72 C ANISOU 1441 CA TYR A 209 10974 8175 7721 350 333 270 C ATOM 1442 C TYR A 209 3.931 -7.941 42.520 1.00 74.73 C ANISOU 1442 C TYR A 209 11463 8641 8288 305 408 257 C ATOM 1443 O TYR A 209 4.647 -8.387 41.622 1.00 74.00 O ANISOU 1443 O TYR A 209 11335 8561 8221 323 383 269 O ATOM 1444 CB TYR A 209 5.038 -7.905 44.771 1.00 72.04 C ANISOU 1444 CB TYR A 209 11259 8313 7801 428 356 315 C ATOM 1445 CG TYR A 209 6.072 -7.233 45.644 1.00 73.40 C ANISOU 1445 CG TYR A 209 11429 8557 7902 487 264 326 C ATOM 1446 CD1 TYR A 209 7.415 -7.193 45.267 1.00 75.70 C ANISOU 1446 CD1 TYR A 209 11660 8930 8173 537 178 337 C ATOM 1447 CD2 TYR A 209 5.719 -6.660 46.864 1.00 73.70 C ANISOU 1447 CD2 TYR A 209 11522 8596 7885 490 264 319 C ATOM 1448 CE1 TYR A 209 8.380 -6.596 46.081 1.00 77.44 C ANISOU 1448 CE1 TYR A 209 11863 9244 8317 579 94 332 C ATOM 1449 CE2 TYR A 209 6.676 -6.077 47.695 1.00 74.75 C ANISOU 1449 CE2 TYR A 209 11652 8808 7943 536 180 320 C ATOM 1450 CZ TYR A 209 8.009 -6.058 47.305 1.00 83.24 C ANISOU 1450 CZ TYR A 209 12656 9976 8995 577 95 323 C ATOM 1451 OH TYR A 209 8.965 -5.492 48.113 1.00 84.07 O ANISOU 1451 OH TYR A 209 12741 10186 9016 611 12 309 O ATOM 1452 N VAL A 210 2.604 -8.183 42.592 1.00 71.48 N ANISOU 1452 N VAL A 210 11069 8195 7894 242 499 226 N ATOM 1453 CA VAL A 210 1.884 -9.000 41.607 1.00 71.11 C ANISOU 1453 CA VAL A 210 10998 8127 7895 178 577 196 C ATOM 1454 C VAL A 210 1.916 -8.306 40.237 1.00 76.40 C ANISOU 1454 C VAL A 210 11533 8861 8632 152 518 166 C ATOM 1455 O VAL A 210 2.444 -8.937 39.319 1.00 76.89 O ANISOU 1455 O VAL A 210 11576 8917 8722 154 514 173 O ATOM 1456 CB VAL A 210 0.448 -9.403 42.042 1.00 74.63 C ANISOU 1456 CB VAL A 210 11478 8547 8332 101 692 156 C ATOM 1457 CG1 VAL A 210 -0.427 -9.776 40.841 1.00 74.01 C ANISOU 1457 CG1 VAL A 210 11314 8499 8308 12 749 96 C ATOM 1458 CG2 VAL A 210 0.494 -10.545 43.046 1.00 74.85 C ANISOU 1458 CG2 VAL A 210 11666 8480 8295 115 782 190 C ATOM 1459 N PRO A 211 1.440 -7.031 40.050 1.00 74.22 N ANISOU 1459 N PRO A 211 11178 8644 8377 141 475 136 N ATOM 1460 CA PRO A 211 1.501 -6.420 38.701 1.00 73.24 C ANISOU 1460 CA PRO A 211 10947 8574 8307 131 428 113 C ATOM 1461 C PRO A 211 2.916 -6.166 38.159 1.00 77.27 C ANISOU 1461 C PRO A 211 11436 9095 8829 168 342 146 C ATOM 1462 O PRO A 211 3.061 -6.138 36.939 1.00 76.33 O ANISOU 1462 O PRO A 211 11247 9003 8753 156 324 134 O ATOM 1463 CB PRO A 211 0.750 -5.092 38.870 1.00 74.71 C ANISOU 1463 CB PRO A 211 11095 8803 8487 137 409 86 C ATOM 1464 CG PRO A 211 0.785 -4.803 40.322 1.00 79.46 C ANISOU 1464 CG PRO A 211 11781 9374 9036 158 412 104 C ATOM 1465 CD PRO A 211 0.749 -6.130 41.004 1.00 75.59 C ANISOU 1465 CD PRO A 211 11369 8832 8520 145 479 122 C ATOM 1466 N LEU A 212 3.928 -5.961 39.057 1.00 75.72 N ANISOU 1466 N LEU A 212 11291 8891 8588 211 291 180 N ATOM 1467 CA ALEU A 212 5.337 -5.709 38.715 0.50 75.72 C ANISOU 1467 CA ALEU A 212 11260 8926 8583 241 211 202 C ATOM 1468 CA BLEU A 212 5.337 -5.711 38.711 0.50 75.98 C ANISOU 1468 CA BLEU A 212 11294 8960 8617 240 211 202 C ATOM 1469 C LEU A 212 5.973 -6.949 38.070 1.00 80.78 C ANISOU 1469 C LEU A 212 11901 9558 9235 268 224 225 C ATOM 1470 O LEU A 212 6.704 -6.809 37.092 1.00 81.43 O ANISOU 1470 O LEU A 212 11918 9677 9346 269 180 225 O ATOM 1471 CB ALEU A 212 6.139 -5.268 39.976 0.50 76.16 C ANISOU 1471 CB ALEU A 212 11364 9003 8570 276 160 219 C ATOM 1472 CB BLEU A 212 6.136 -5.289 39.967 0.50 76.68 C ANISOU 1472 CB BLEU A 212 11430 9068 8636 276 161 220 C ATOM 1473 CG ALEU A 212 7.679 -5.410 39.967 0.50 80.43 C ANISOU 1473 CG ALEU A 212 11878 9605 9076 318 88 239 C ATOM 1474 CG BLEU A 212 7.623 -4.985 39.773 0.50 81.41 C ANISOU 1474 CG BLEU A 212 11983 9736 9214 297 78 228 C ATOM 1475 CD1ALEU A 212 8.333 -4.430 39.009 0.50 79.99 C ANISOU 1475 CD1ALEU A 212 11736 9602 9054 274 29 215 C ATOM 1476 CD1BLEU A 212 7.918 -3.560 40.086 0.50 81.57 C ANISOU 1476 CD1BLEU A 212 11986 9792 9216 255 26 199 C ATOM 1477 CD2ALEU A 212 8.252 -5.255 41.356 0.50 81.81 C ANISOU 1477 CD2ALEU A 212 12105 9813 9167 360 54 250 C ATOM 1478 CD2BLEU A 212 8.478 -5.887 40.630 0.50 84.25 C ANISOU 1478 CD2BLEU A 212 12390 10120 9502 376 63 263 C ATOM 1479 N VAL A 213 5.708 -8.153 38.627 1.00 77.85 N ANISOU 1479 N VAL A 213 11617 9129 8833 292 293 246 N ATOM 1480 CA VAL A 213 6.239 -9.426 38.108 1.00 78.02 C ANISOU 1480 CA VAL A 213 11675 9119 8851 330 326 271 C ATOM 1481 C VAL A 213 5.623 -9.726 36.704 1.00 81.89 C ANISOU 1481 C VAL A 213 12102 9601 9411 264 365 235 C ATOM 1482 O VAL A 213 6.365 -10.088 35.788 1.00 82.08 O ANISOU 1482 O VAL A 213 12091 9642 9456 287 341 245 O ATOM 1483 CB VAL A 213 6.054 -10.605 39.106 1.00 81.86 C ANISOU 1483 CB VAL A 213 12305 9525 9274 373 408 303 C ATOM 1484 CG1 VAL A 213 6.449 -11.937 38.475 1.00 82.02 C ANISOU 1484 CG1 VAL A 213 12387 9488 9288 410 463 325 C ATOM 1485 CG2 VAL A 213 6.874 -10.376 40.367 1.00 81.97 C ANISOU 1485 CG2 VAL A 213 12372 9568 9207 462 355 341 C ATOM 1486 N ILE A 214 4.296 -9.534 36.535 1.00 77.13 N ANISOU 1486 N ILE A 214 11477 8991 8838 188 421 190 N ATOM 1487 CA ILE A 214 3.589 -9.736 35.266 1.00 76.30 C ANISOU 1487 CA ILE A 214 11299 8906 8787 124 456 144 C ATOM 1488 C ILE A 214 4.152 -8.765 34.186 1.00 81.99 C ANISOU 1488 C ILE A 214 11909 9696 9548 137 368 140 C ATOM 1489 O ILE A 214 4.563 -9.217 33.126 1.00 82.62 O ANISOU 1489 O ILE A 214 11953 9783 9656 135 363 137 O ATOM 1490 CB ILE A 214 2.045 -9.594 35.449 1.00 78.64 C ANISOU 1490 CB ILE A 214 11574 9219 9088 49 526 88 C ATOM 1491 CG1 ILE A 214 1.481 -10.748 36.303 1.00 78.84 C ANISOU 1491 CG1 ILE A 214 11714 9167 9074 10 637 83 C ATOM 1492 CG2 ILE A 214 1.338 -9.530 34.097 1.00 78.58 C ANISOU 1492 CG2 ILE A 214 11457 9275 9124 -6 539 31 C ATOM 1493 CD1 ILE A 214 0.248 -10.441 37.025 1.00 81.22 C ANISOU 1493 CD1 ILE A 214 12013 9490 9358 -44 693 43 C ATOM 1494 N MET A 215 4.195 -7.459 34.480 1.00 78.97 N ANISOU 1494 N MET A 215 11492 9353 9162 149 308 140 N ATOM 1495 CA MET A 215 4.701 -6.388 33.618 1.00 78.10 C ANISOU 1495 CA MET A 215 11308 9291 9076 157 238 137 C ATOM 1496 C MET A 215 6.139 -6.655 33.115 1.00 84.84 C ANISOU 1496 C MET A 215 12144 10158 9934 186 186 167 C ATOM 1497 O MET A 215 6.393 -6.464 31.932 1.00 84.80 O ANISOU 1497 O MET A 215 12076 10181 9963 176 165 158 O ATOM 1498 CB MET A 215 4.650 -5.066 34.400 1.00 79.78 C ANISOU 1498 CB MET A 215 11537 9513 9262 165 200 138 C ATOM 1499 CG MET A 215 5.061 -3.844 33.621 1.00 82.08 C ANISOU 1499 CG MET A 215 11786 9834 9567 164 148 132 C ATOM 1500 SD MET A 215 5.206 -2.404 34.717 1.00 85.66 S ANISOU 1500 SD MET A 215 12298 10275 9975 165 117 132 S ATOM 1501 CE MET A 215 6.787 -2.679 35.440 1.00 81.87 C ANISOU 1501 CE MET A 215 11835 9811 9460 164 63 155 C ATOM 1502 N VAL A 216 7.068 -7.063 33.999 1.00 83.92 N ANISOU 1502 N VAL A 216 12077 10034 9774 228 164 200 N ATOM 1503 CA VAL A 216 8.471 -7.311 33.616 1.00 84.66 C ANISOU 1503 CA VAL A 216 12141 10169 9857 269 112 224 C ATOM 1504 C VAL A 216 8.584 -8.616 32.803 1.00 89.45 C ANISOU 1504 C VAL A 216 12756 10748 10483 292 156 234 C ATOM 1505 O VAL A 216 9.407 -8.688 31.892 1.00 89.42 O ANISOU 1505 O VAL A 216 12696 10783 10496 307 123 239 O ATOM 1506 CB VAL A 216 9.505 -7.257 34.788 1.00 89.28 C ANISOU 1506 CB VAL A 216 12757 10792 10374 323 65 250 C ATOM 1507 CG1 VAL A 216 9.449 -5.910 35.503 1.00 89.08 C ANISOU 1507 CG1 VAL A 216 12725 10793 10329 284 25 230 C ATOM 1508 CG2 VAL A 216 9.336 -8.406 35.781 1.00 89.64 C ANISOU 1508 CG2 VAL A 216 12903 10786 10368 386 115 280 C ATOM 1509 N PHE A 217 7.749 -9.621 33.102 1.00 86.17 N ANISOU 1509 N PHE A 217 12417 10263 10062 285 238 232 N ATOM 1510 CA PHE A 217 7.744 -10.874 32.359 1.00 86.01 C ANISOU 1510 CA PHE A 217 12430 10197 10053 292 297 233 C ATOM 1511 C PHE A 217 7.129 -10.678 30.948 1.00 84.98 C ANISOU 1511 C PHE A 217 12214 10089 9985 224 308 189 C ATOM 1512 O PHE A 217 7.699 -11.171 29.974 1.00 85.16 O ANISOU 1512 O PHE A 217 12212 10120 10025 240 304 192 O ATOM 1513 CB PHE A 217 6.994 -11.975 33.144 1.00 90.03 C ANISOU 1513 CB PHE A 217 13067 10613 10528 285 399 235 C ATOM 1514 CG PHE A 217 6.583 -13.140 32.277 1.00 94.41 C ANISOU 1514 CG PHE A 217 13664 11108 11101 245 486 212 C ATOM 1515 CD1 PHE A 217 7.495 -14.138 31.946 1.00 99.60 C ANISOU 1515 CD1 PHE A 217 14387 11725 11733 319 505 247 C ATOM 1516 CD2 PHE A 217 5.306 -13.195 31.716 1.00 98.62 C ANISOU 1516 CD2 PHE A 217 14162 11639 11672 136 548 149 C ATOM 1517 CE1 PHE A 217 7.136 -15.179 31.086 1.00101.73 C ANISOU 1517 CE1 PHE A 217 14704 11930 12016 275 590 219 C ATOM 1518 CE2 PHE A 217 4.954 -14.228 30.844 1.00102.61 C ANISOU 1518 CE2 PHE A 217 14697 12100 12191 81 628 114 C ATOM 1519 CZ PHE A 217 5.869 -15.214 30.537 1.00101.41 C ANISOU 1519 CZ PHE A 217 14628 11887 12017 146 652 150 C ATOM 1520 N VAL A 218 5.961 -9.996 30.856 1.00 77.53 N ANISOU 1520 N VAL A 218 11228 9166 9065 160 324 147 N ATOM 1521 CA VAL A 218 5.192 -9.758 29.621 1.00 75.83 C ANISOU 1521 CA VAL A 218 10927 8993 8891 107 335 99 C ATOM 1522 C VAL A 218 5.874 -8.710 28.721 1.00 76.01 C ANISOU 1522 C VAL A 218 10867 9075 8938 130 255 108 C ATOM 1523 O VAL A 218 5.788 -8.841 27.505 1.00 74.18 O ANISOU 1523 O VAL A 218 10579 8873 8734 114 256 86 O ATOM 1524 CB VAL A 218 3.699 -9.379 29.922 1.00 79.95 C ANISOU 1524 CB VAL A 218 11427 9540 9411 53 379 50 C ATOM 1525 CG1 VAL A 218 2.965 -8.896 28.684 1.00 79.23 C ANISOU 1525 CG1 VAL A 218 11231 9527 9345 26 371 1 C ATOM 1526 CG2 VAL A 218 2.941 -10.553 30.534 1.00 80.91 C ANISOU 1526 CG2 VAL A 218 11624 9606 9511 0 480 25 C ATOM 1527 N TYR A 219 6.539 -7.690 29.290 1.00 71.91 N ANISOU 1527 N TYR A 219 10347 8573 8402 157 193 135 N ATOM 1528 CA TYR A 219 7.163 -6.649 28.475 1.00 70.46 C ANISOU 1528 CA TYR A 219 10103 8433 8233 161 134 139 C ATOM 1529 C TYR A 219 8.592 -7.011 28.015 1.00 77.81 C ANISOU 1529 C TYR A 219 11014 9385 9166 187 97 165 C ATOM 1530 O TYR A 219 9.099 -6.430 27.049 1.00 78.18 O ANISOU 1530 O TYR A 219 11007 9467 9229 178 65 163 O ATOM 1531 CB TYR A 219 7.136 -5.295 29.169 1.00 68.99 C ANISOU 1531 CB TYR A 219 9934 8254 8025 158 100 142 C ATOM 1532 CG TYR A 219 7.030 -4.166 28.174 1.00 67.28 C ANISOU 1532 CG TYR A 219 9680 8062 7822 150 80 130 C ATOM 1533 CD1 TYR A 219 5.809 -3.843 27.587 1.00 69.24 C ANISOU 1533 CD1 TYR A 219 9905 8326 8076 158 108 104 C ATOM 1534 CD2 TYR A 219 8.138 -3.391 27.852 1.00 66.45 C ANISOU 1534 CD2 TYR A 219 9567 7970 7710 138 37 143 C ATOM 1535 CE1 TYR A 219 5.703 -2.800 26.669 1.00 69.10 C ANISOU 1535 CE1 TYR A 219 9873 8327 8056 174 94 100 C ATOM 1536 CE2 TYR A 219 8.036 -2.327 26.961 1.00 66.60 C ANISOU 1536 CE2 TYR A 219 9581 7994 7732 132 33 137 C ATOM 1537 CZ TYR A 219 6.824 -2.054 26.349 1.00 70.71 C ANISOU 1537 CZ TYR A 219 10092 8518 8255 161 61 120 C ATOM 1538 OH TYR A 219 6.714 -1.024 25.456 1.00 66.72 O ANISOU 1538 OH TYR A 219 9598 8013 7738 178 61 120 O ATOM 1539 N SER A 220 9.222 -7.986 28.660 1.00 76.74 N ANISOU 1539 N SER A 220 10921 9233 9004 227 105 190 N ATOM 1540 CA SER A 220 10.508 -8.477 28.177 1.00 78.18 C ANISOU 1540 CA SER A 220 11076 9451 9177 270 76 212 C ATOM 1541 C SER A 220 10.239 -9.292 26.884 1.00 83.87 C ANISOU 1541 C SER A 220 11777 10154 9935 263 115 198 C ATOM 1542 O SER A 220 11.082 -9.336 25.983 1.00 83.97 O ANISOU 1542 O SER A 220 11739 10208 9959 279 89 204 O ATOM 1543 CB SER A 220 11.202 -9.312 29.247 1.00 82.55 C ANISOU 1543 CB SER A 220 11691 9999 9675 343 77 245 C ATOM 1544 OG SER A 220 10.359 -10.368 29.683 1.00 94.12 O ANISOU 1544 OG SER A 220 13249 11380 11132 353 153 249 O ATOM 1545 N ARG A 221 9.016 -9.877 26.790 1.00 80.65 N ANISOU 1545 N ARG A 221 11406 9695 9543 227 181 171 N ATOM 1546 CA ARG A 221 8.510 -10.651 25.661 1.00 80.12 C ANISOU 1546 CA ARG A 221 11325 9614 9504 197 230 141 C ATOM 1547 C ARG A 221 8.136 -9.769 24.472 1.00 83.46 C ANISOU 1547 C ARG A 221 11656 10094 9960 163 201 112 C ATOM 1548 O ARG A 221 8.294 -10.223 23.338 1.00 83.40 O ANISOU 1548 O ARG A 221 11616 10101 9971 159 212 98 O ATOM 1549 CB ARG A 221 7.288 -11.486 26.071 1.00 80.82 C ANISOU 1549 CB ARG A 221 11476 9645 9585 148 316 107 C ATOM 1550 CG ARG A 221 7.604 -12.906 26.521 1.00 97.59 C ANISOU 1550 CG ARG A 221 13715 11685 11679 176 385 126 C ATOM 1551 CD ARG A 221 8.204 -13.800 25.427 1.00114.76 C ANISOU 1551 CD ARG A 221 15898 13843 13861 197 407 125 C ATOM 1552 NE ARG A 221 7.416 -13.852 24.188 1.00121.65 N ANISOU 1552 NE ARG A 221 16704 14745 14770 119 433 65 N ATOM 1553 CZ ARG A 221 6.521 -14.794 23.898 1.00134.57 C ANISOU 1553 CZ ARG A 221 18389 16337 16404 42 525 11 C ATOM 1554 NH1 ARG A 221 6.260 -15.764 24.769 1.00126.05 N ANISOU 1554 NH1 ARG A 221 17443 15160 15289 28 612 14 N ATOM 1555 NH2 ARG A 221 5.875 -14.769 22.739 1.00112.59 N ANISOU 1555 NH2 ARG A 221 15527 13608 13645 -25 536 -50 N ATOM 1556 N VAL A 222 7.625 -8.535 24.711 1.00 79.18 N ANISOU 1556 N VAL A 222 11085 9582 9417 149 172 104 N ATOM 1557 CA VAL A 222 7.223 -7.639 23.614 1.00 78.25 C ANISOU 1557 CA VAL A 222 10901 9515 9316 139 151 83 C ATOM 1558 C VAL A 222 8.482 -7.157 22.856 1.00 83.54 C ANISOU 1558 C VAL A 222 11540 10209 9994 158 103 110 C ATOM 1559 O VAL A 222 8.423 -6.994 21.636 1.00 82.93 O ANISOU 1559 O VAL A 222 11417 10162 9930 157 100 97 O ATOM 1560 CB VAL A 222 6.278 -6.448 23.991 1.00 80.68 C ANISOU 1560 CB VAL A 222 11205 9843 9608 139 143 69 C ATOM 1561 CG1 VAL A 222 5.143 -6.879 24.905 1.00 80.19 C ANISOU 1561 CG1 VAL A 222 11167 9769 9531 118 190 41 C ATOM 1562 CG2 VAL A 222 7.031 -5.276 24.584 1.00 80.34 C ANISOU 1562 CG2 VAL A 222 11191 9786 9547 152 98 101 C ATOM 1563 N PHE A 223 9.600 -6.930 23.586 1.00 81.29 N ANISOU 1563 N PHE A 223 11274 9921 9692 172 68 142 N ATOM 1564 CA PHE A 223 10.878 -6.493 23.028 1.00 81.49 C ANISOU 1564 CA PHE A 223 11261 9985 9716 175 28 159 C ATOM 1565 C PHE A 223 11.467 -7.618 22.167 1.00 85.95 C ANISOU 1565 C PHE A 223 11798 10564 10294 201 40 163 C ATOM 1566 O PHE A 223 11.949 -7.356 21.059 1.00 86.38 O ANISOU 1566 O PHE A 223 11806 10652 10362 195 28 161 O ATOM 1567 CB PHE A 223 11.862 -6.080 24.152 1.00 83.47 C ANISOU 1567 CB PHE A 223 11525 10258 9933 176 -10 177 C ATOM 1568 CG PHE A 223 11.690 -4.707 24.757 1.00 84.75 C ANISOU 1568 CG PHE A 223 11712 10413 10076 136 -27 170 C ATOM 1569 CD1 PHE A 223 11.139 -3.663 24.019 1.00 87.72 C ANISOU 1569 CD1 PHE A 223 12095 10774 10461 111 -18 159 C ATOM 1570 CD2 PHE A 223 12.123 -4.442 26.050 1.00 87.86 C ANISOU 1570 CD2 PHE A 223 12133 10817 10434 131 -50 175 C ATOM 1571 CE1 PHE A 223 10.988 -2.387 24.578 1.00 88.85 C ANISOU 1571 CE1 PHE A 223 12288 10893 10579 80 -21 154 C ATOM 1572 CE2 PHE A 223 11.975 -3.164 26.608 1.00 90.84 C ANISOU 1572 CE2 PHE A 223 12546 11180 10789 86 -59 162 C ATOM 1573 CZ PHE A 223 11.412 -2.145 25.866 1.00 88.47 C ANISOU 1573 CZ PHE A 223 12269 10848 10500 60 -40 153 C ATOM 1574 N GLN A 224 11.392 -8.869 22.680 1.00 82.09 N ANISOU 1574 N GLN A 224 11355 10041 9797 233 73 169 N ATOM 1575 CA GLN A 224 11.816 -10.103 22.011 1.00 81.55 C ANISOU 1575 CA GLN A 224 11293 9960 9731 269 102 173 C ATOM 1576 C GLN A 224 11.078 -10.254 20.674 1.00 83.76 C ANISOU 1576 C GLN A 224 11541 10241 10044 232 130 138 C ATOM 1577 O GLN A 224 11.715 -10.465 19.639 1.00 83.08 O ANISOU 1577 O GLN A 224 11417 10184 9968 247 123 139 O ATOM 1578 CB GLN A 224 11.541 -11.318 22.911 1.00 83.06 C ANISOU 1578 CB GLN A 224 11578 10085 9898 302 154 182 C ATOM 1579 CG GLN A 224 12.632 -11.593 23.938 1.00103.03 C ANISOU 1579 CG GLN A 224 14139 12630 12377 381 128 224 C ATOM 1580 CD GLN A 224 12.356 -12.860 24.718 1.00133.23 C ANISOU 1580 CD GLN A 224 18083 16372 16166 430 194 240 C ATOM 1581 OE1 GLN A 224 11.997 -13.906 24.156 1.00130.87 O ANISOU 1581 OE1 GLN A 224 17844 16008 15873 429 261 228 O ATOM 1582 NE2 GLN A 224 12.541 -12.799 26.035 1.00127.11 N ANISOU 1582 NE2 GLN A 224 17358 15593 15346 473 181 266 N ATOM 1583 N GLU A 225 9.733 -10.088 20.703 1.00 78.76 N ANISOU 1583 N GLU A 225 10913 9593 9420 186 160 102 N ATOM 1584 CA GLU A 225 8.856 -10.174 19.538 1.00 77.16 C ANISOU 1584 CA GLU A 225 10668 9417 9234 152 184 57 C ATOM 1585 C GLU A 225 9.213 -9.127 18.508 1.00 79.88 C ANISOU 1585 C GLU A 225 10948 9817 9586 163 139 64 C ATOM 1586 O GLU A 225 9.378 -9.474 17.348 1.00 79.73 O ANISOU 1586 O GLU A 225 10895 9822 9575 164 145 49 O ATOM 1587 CB GLU A 225 7.375 -10.035 19.935 1.00 78.12 C ANISOU 1587 CB GLU A 225 10789 9546 9349 109 217 13 C ATOM 1588 CG GLU A 225 6.773 -11.272 20.583 1.00 84.46 C ANISOU 1588 CG GLU A 225 11656 10294 10143 69 290 -15 C ATOM 1589 CD GLU A 225 7.002 -12.590 19.868 1.00 99.23 C ANISOU 1589 CD GLU A 225 13560 12127 12015 51 344 -36 C ATOM 1590 OE1 GLU A 225 6.842 -12.639 18.627 1.00 97.34 O ANISOU 1590 OE1 GLU A 225 13261 11936 11786 34 342 -70 O ATOM 1591 OE2 GLU A 225 7.335 -13.580 20.555 1.00 91.66 O ANISOU 1591 OE2 GLU A 225 12699 11088 11041 61 393 -19 O ATOM 1592 N ALA A 226 9.371 -7.863 18.928 1.00 75.41 N ANISOU 1592 N ALA A 226 10379 9263 9009 168 101 85 N ATOM 1593 CA ALA A 226 9.701 -6.756 18.039 1.00 74.58 C ANISOU 1593 CA ALA A 226 10244 9192 8901 175 72 95 C ATOM 1594 C ALA A 226 10.995 -7.024 17.238 1.00 79.59 C ANISOU 1594 C ALA A 226 10850 9846 9545 182 57 114 C ATOM 1595 O ALA A 226 10.977 -6.869 16.013 1.00 78.26 O ANISOU 1595 O ALA A 226 10650 9705 9379 187 60 105 O ATOM 1596 CB ALA A 226 9.818 -5.469 18.831 1.00 74.84 C ANISOU 1596 CB ALA A 226 10311 9211 8915 169 49 115 C ATOM 1597 N LYS A 227 12.081 -7.473 17.914 1.00 78.02 N ANISOU 1597 N LYS A 227 10657 9645 9342 191 43 137 N ATOM 1598 CA LYS A 227 13.379 -7.775 17.291 1.00 79.26 C ANISOU 1598 CA LYS A 227 10775 9841 9498 207 29 152 C ATOM 1599 C LYS A 227 13.324 -8.988 16.321 1.00 87.90 C ANISOU 1599 C LYS A 227 11859 10931 10606 234 60 139 C ATOM 1600 O LYS A 227 13.899 -8.920 15.228 1.00 88.30 O ANISOU 1600 O LYS A 227 11870 11018 10661 238 56 140 O ATOM 1601 CB LYS A 227 14.456 -8.023 18.360 1.00 81.27 C ANISOU 1601 CB LYS A 227 11030 10120 9728 231 5 174 C ATOM 1602 CG LYS A 227 15.439 -6.873 18.505 1.00 91.94 C ANISOU 1602 CG LYS A 227 12344 11528 11060 191 -30 179 C ATOM 1603 N ARG A 228 12.637 -10.080 16.714 1.00 86.58 N ANISOU 1603 N ARG A 228 11739 10717 10441 245 99 125 N ATOM 1604 CA ARG A 228 12.547 -11.307 15.917 1.00 87.25 C ANISOU 1604 CA ARG A 228 11839 10782 10532 259 142 105 C ATOM 1605 C ARG A 228 11.454 -11.250 14.816 1.00 91.59 C ANISOU 1605 C ARG A 228 12360 11346 11094 216 164 57 C ATOM 1606 O ARG A 228 11.297 -12.224 14.069 1.00 92.60 O ANISOU 1606 O ARG A 228 12498 11461 11223 210 204 28 O ATOM 1607 CB ARG A 228 12.351 -12.536 16.832 1.00 89.60 C ANISOU 1607 CB ARG A 228 12222 11008 10814 280 191 106 C ATOM 1608 CG ARG A 228 10.917 -12.839 17.258 1.00101.50 C ANISOU 1608 CG ARG A 228 13773 12470 12324 220 239 65 C ATOM 1609 CD ARG A 228 10.613 -14.303 17.034 1.00109.51 C ANISOU 1609 CD ARG A 228 14865 13416 13329 209 319 36 C ATOM 1610 NE ARG A 228 9.186 -14.577 17.174 1.00123.77 N ANISOU 1610 NE ARG A 228 16691 15202 15135 123 374 -24 N ATOM 1611 CZ ARG A 228 8.531 -15.506 16.486 1.00144.72 C ANISOU 1611 CZ ARG A 228 19370 17832 17784 62 443 -84 C ATOM 1612 NH1 ARG A 228 7.231 -15.686 16.682 1.00137.11 N ANISOU 1612 NH1 ARG A 228 18406 16875 16814 -29 493 -149 N ATOM 1613 NH2 ARG A 228 9.166 -16.261 15.599 1.00133.50 N ANISOU 1613 NH2 ARG A 228 17974 16390 16360 86 466 -86 N ATOM 1614 N GLN A 229 10.728 -10.129 14.698 1.00 87.20 N ANISOU 1614 N GLN A 229 11771 10824 10538 193 141 47 N ATOM 1615 CA GLN A 229 9.698 -9.979 13.670 1.00 86.76 C ANISOU 1615 CA GLN A 229 11675 10811 10477 174 153 1 C ATOM 1616 C GLN A 229 10.153 -8.975 12.589 1.00 90.91 C ANISOU 1616 C GLN A 229 12160 11385 10995 199 119 19 C ATOM 1617 O GLN A 229 9.398 -8.694 11.650 1.00 91.28 O ANISOU 1617 O GLN A 229 12173 11483 11026 205 121 -12 O ATOM 1618 CB GLN A 229 8.348 -9.591 14.283 1.00 87.95 C ANISOU 1618 CB GLN A 229 11824 10978 10615 151 162 -32 C ATOM 1619 CG GLN A 229 7.594 -10.780 14.887 1.00101.55 C ANISOU 1619 CG GLN A 229 13579 12669 12338 103 219 -76 C ATOM 1620 CD GLN A 229 6.250 -10.385 15.458 1.00128.30 C ANISOU 1620 CD GLN A 229 16947 16093 15708 76 231 -116 C ATOM 1621 OE1 GLN A 229 5.569 -9.485 14.956 1.00127.41 O ANISOU 1621 OE1 GLN A 229 16778 16057 15574 99 206 -133 O ATOM 1622 NE2 GLN A 229 5.816 -11.083 16.501 1.00120.23 N ANISOU 1622 NE2 GLN A 229 15975 15022 14684 34 276 -132 N ATOM 1623 N LEU A 230 11.418 -8.489 12.698 1.00 86.82 N ANISOU 1623 N LEU A 230 11647 10860 10483 212 94 65 N ATOM 1624 CA LEU A 230 12.051 -7.578 11.732 1.00 86.02 C ANISOU 1624 CA LEU A 230 11523 10789 10370 220 77 85 C ATOM 1625 C LEU A 230 12.317 -8.313 10.430 1.00 89.09 C ANISOU 1625 C LEU A 230 11880 11208 10763 234 92 68 C ATOM 1626 O LEU A 230 12.834 -9.434 10.456 1.00 88.75 O ANISOU 1626 O LEU A 230 11836 11151 10732 240 108 63 O ATOM 1627 CB LEU A 230 13.371 -6.992 12.277 1.00 85.85 C ANISOU 1627 CB LEU A 230 11506 10766 10348 206 56 122 C ATOM 1628 CG LEU A 230 13.288 -5.674 13.042 1.00 89.86 C ANISOU 1628 CG LEU A 230 12050 11253 10838 181 43 138 C ATOM 1629 CD1 LEU A 230 14.620 -5.327 13.661 1.00 90.07 C ANISOU 1629 CD1 LEU A 230 12067 11297 10858 147 26 157 C ATOM 1630 CD2 LEU A 230 12.849 -4.538 12.146 1.00 91.24 C ANISOU 1630 CD2 LEU A 230 12251 11427 10989 187 53 142 C ATOM 1631 N ASN A1002 11.937 -7.692 9.298 1.00 84.41 N ANISOU 1631 N ASN A1002 11270 10651 10150 248 91 59 N ATOM 1632 CA ASN A1002 12.112 -8.250 7.953 1.00 83.28 C ANISOU 1632 CA ASN A1002 11096 10544 10002 262 104 40 C ATOM 1633 C ASN A1002 12.884 -7.251 7.043 1.00 85.82 C ANISOU 1633 C ASN A1002 11418 10886 10305 275 97 73 C ATOM 1634 O ASN A1002 13.244 -6.165 7.509 1.00 84.59 O ANISOU 1634 O ASN A1002 11293 10708 10138 262 90 105 O ATOM 1635 CB ASN A1002 10.747 -8.631 7.350 1.00 81.90 C ANISOU 1635 CB ASN A1002 10897 10413 9806 268 116 -16 C ATOM 1636 CG ASN A1002 9.705 -7.542 7.426 1.00105.92 C ANISOU 1636 CG ASN A1002 13941 13491 12814 296 101 -20 C ATOM 1637 OD1 ASN A1002 9.890 -6.410 6.956 1.00 97.45 O ANISOU 1637 OD1 ASN A1002 12890 12426 11712 334 90 13 O ATOM 1638 ND2 ASN A1002 8.584 -7.865 8.033 1.00102.66 N ANISOU 1638 ND2 ASN A1002 13513 13098 12394 282 108 -63 N ATOM 1639 N ILE A1003 13.127 -7.631 5.753 1.00 82.10 N ANISOU 1639 N ILE A1003 10921 10450 9824 292 109 61 N ATOM 1640 CA ILE A1003 13.843 -6.820 4.751 1.00 81.59 C ANISOU 1640 CA ILE A1003 10862 10403 9735 301 115 89 C ATOM 1641 C ILE A1003 13.073 -5.506 4.458 1.00 85.71 C ANISOU 1641 C ILE A1003 11429 10925 10211 332 115 103 C ATOM 1642 O ILE A1003 13.709 -4.459 4.294 1.00 86.61 O ANISOU 1642 O ILE A1003 11590 11014 10304 320 129 139 O ATOM 1643 CB ILE A1003 14.205 -7.617 3.439 1.00 84.28 C ANISOU 1643 CB ILE A1003 11167 10783 10071 320 130 70 C ATOM 1644 CG1 ILE A1003 14.953 -6.751 2.389 1.00 84.79 C ANISOU 1644 CG1 ILE A1003 11244 10865 10107 326 144 100 C ATOM 1645 CG2 ILE A1003 13.000 -8.315 2.805 1.00 84.05 C ANISOU 1645 CG2 ILE A1003 11117 10793 10026 342 132 16 C ATOM 1646 CD1 ILE A1003 16.346 -6.207 2.800 1.00 90.78 C ANISOU 1646 CD1 ILE A1003 12005 11611 10876 279 153 136 C ATOM 1647 N PHE A1004 11.726 -5.546 4.449 1.00 81.00 N ANISOU 1647 N PHE A1004 10826 10359 9590 371 106 72 N ATOM 1648 CA PHE A1004 10.905 -4.355 4.214 1.00 80.30 C ANISOU 1648 CA PHE A1004 10784 10282 9443 432 106 85 C ATOM 1649 C PHE A1004 11.105 -3.322 5.331 1.00 81.68 C ANISOU 1649 C PHE A1004 11030 10385 9618 413 110 123 C ATOM 1650 O PHE A1004 11.307 -2.152 5.038 1.00 81.73 O ANISOU 1650 O PHE A1004 11116 10356 9582 437 130 160 O ATOM 1651 CB PHE A1004 9.425 -4.727 4.069 1.00 82.48 C ANISOU 1651 CB PHE A1004 11012 10638 9688 481 92 33 C ATOM 1652 CG PHE A1004 9.160 -5.776 3.008 1.00 84.53 C ANISOU 1652 CG PHE A1004 11201 10975 9940 482 92 -20 C ATOM 1653 CD1 PHE A1004 9.042 -5.419 1.665 1.00 87.78 C ANISOU 1653 CD1 PHE A1004 11610 11448 10294 547 93 -21 C ATOM 1654 CD2 PHE A1004 9.042 -7.123 3.350 1.00 86.53 C ANISOU 1654 CD2 PHE A1004 11405 11234 10238 418 99 -71 C ATOM 1655 CE1 PHE A1004 8.819 -6.390 0.687 1.00 88.66 C ANISOU 1655 CE1 PHE A1004 11657 11635 10395 541 94 -76 C ATOM 1656 CE2 PHE A1004 8.805 -8.093 2.371 1.00 89.12 C ANISOU 1656 CE2 PHE A1004 11683 11625 10554 406 108 -128 C ATOM 1657 CZ PHE A1004 8.704 -7.720 1.047 1.00 87.70 C ANISOU 1657 CZ PHE A1004 11487 11515 10320 464 102 -132 C ATOM 1658 N GLU A1005 11.117 -3.763 6.594 1.00 77.25 N ANISOU 1658 N GLU A1005 10455 9797 9101 366 97 114 N ATOM 1659 CA GLU A1005 11.335 -2.883 7.745 1.00 76.92 C ANISOU 1659 CA GLU A1005 10475 9692 9060 338 99 142 C ATOM 1660 C GLU A1005 12.802 -2.423 7.817 1.00 79.51 C ANISOU 1660 C GLU A1005 10830 9980 9399 271 113 172 C ATOM 1661 O GLU A1005 13.070 -1.291 8.227 1.00 79.11 O ANISOU 1661 O GLU A1005 10858 9878 9323 245 132 195 O ATOM 1662 CB GLU A1005 10.930 -3.583 9.044 1.00 78.33 C ANISOU 1662 CB GLU A1005 10625 9862 9275 311 82 121 C ATOM 1663 CG GLU A1005 9.428 -3.610 9.309 1.00 92.48 C ANISOU 1663 CG GLU A1005 12406 11690 11043 360 77 90 C ATOM 1664 CD GLU A1005 8.990 -4.231 10.629 1.00121.98 C ANISOU 1664 CD GLU A1005 16127 15409 14809 326 72 70 C ATOM 1665 OE1 GLU A1005 7.921 -3.827 11.142 1.00115.43 O ANISOU 1665 OE1 GLU A1005 15307 14598 13954 358 72 55 O ATOM 1666 OE2 GLU A1005 9.697 -5.131 11.144 1.00120.35 O ANISOU 1666 OE2 GLU A1005 15905 15178 14646 277 71 70 O ATOM 1667 N MET A1006 13.744 -3.302 7.405 1.00 74.82 N ANISOU 1667 N MET A1006 10173 9417 8836 240 110 166 N ATOM 1668 CA MET A1006 15.196 -3.053 7.361 1.00 73.26 C ANISOU 1668 CA MET A1006 9969 9223 8646 175 122 181 C ATOM 1669 C MET A1006 15.519 -1.905 6.395 1.00 77.21 C ANISOU 1669 C MET A1006 10535 9700 9100 164 162 203 C ATOM 1670 O MET A1006 16.219 -0.963 6.770 1.00 77.26 O ANISOU 1670 O MET A1006 10594 9673 9087 94 188 214 O ATOM 1671 CB MET A1006 15.927 -4.341 6.926 1.00 74.55 C ANISOU 1671 CB MET A1006 10048 9439 8840 179 113 168 C ATOM 1672 CG MET A1006 17.427 -4.253 6.997 1.00 76.89 C ANISOU 1672 CG MET A1006 10306 9772 9138 123 120 174 C ATOM 1673 SD MET A1006 18.211 -5.596 6.105 1.00 79.00 S ANISOU 1673 SD MET A1006 10491 10104 9422 159 121 164 S ATOM 1674 CE MET A1006 19.845 -5.381 6.602 1.00 76.02 C ANISOU 1674 CE MET A1006 10053 9796 9035 100 121 165 C ATOM 1675 N LEU A1007 14.988 -1.983 5.161 1.00 73.51 N ANISOU 1675 N LEU A1007 10074 9251 8606 228 173 204 N ATOM 1676 CA LEU A1007 15.200 -0.970 4.133 1.00 73.53 C ANISOU 1676 CA LEU A1007 10157 9228 8554 238 218 229 C ATOM 1677 C LEU A1007 14.463 0.332 4.446 1.00 80.85 C ANISOU 1677 C LEU A1007 11210 10083 9425 272 244 253 C ATOM 1678 O LEU A1007 14.976 1.379 4.071 1.00 82.31 O ANISOU 1678 O LEU A1007 11497 10211 9565 239 299 278 O ATOM 1679 CB LEU A1007 14.813 -1.487 2.741 1.00 72.93 C ANISOU 1679 CB LEU A1007 10050 9203 8456 312 218 223 C ATOM 1680 CG LEU A1007 15.814 -2.407 2.060 1.00 75.92 C ANISOU 1680 CG LEU A1007 10346 9632 8866 278 219 210 C ATOM 1681 CD1 LEU A1007 15.154 -3.179 0.946 1.00 75.74 C ANISOU 1681 CD1 LEU A1007 10282 9667 8830 353 206 189 C ATOM 1682 CD2 LEU A1007 17.018 -1.636 1.545 1.00 76.55 C ANISOU 1682 CD2 LEU A1007 10468 9694 8923 211 269 233 C ATOM 1683 N ARG A1008 13.297 0.294 5.143 1.00 78.82 N ANISOU 1683 N ARG A1008 10956 9826 9165 334 216 244 N ATOM 1684 CA ARG A1008 12.577 1.521 5.542 1.00 79.52 C ANISOU 1684 CA ARG A1008 11170 9850 9195 383 242 267 C ATOM 1685 C ARG A1008 13.431 2.329 6.548 1.00 80.98 C ANISOU 1685 C ARG A1008 11431 9951 9387 273 273 277 C ATOM 1686 O ARG A1008 13.379 3.559 6.538 1.00 81.85 O ANISOU 1686 O ARG A1008 11686 9976 9436 278 327 303 O ATOM 1687 CB ARG A1008 11.181 1.215 6.130 1.00 82.67 C ANISOU 1687 CB ARG A1008 11533 10289 9589 469 203 247 C ATOM 1688 CG ARG A1008 10.295 2.466 6.281 1.00100.87 C ANISOU 1688 CG ARG A1008 13967 12545 11814 566 232 273 C ATOM 1689 CD ARG A1008 8.862 2.119 6.638 1.00125.00 C ANISOU 1689 CD ARG A1008 16963 15679 14852 665 194 246 C ATOM 1690 NE ARG A1008 8.028 3.315 6.810 1.00144.72 N ANISOU 1690 NE ARG A1008 19584 18141 17263 779 222 273 N ATOM 1691 CZ ARG A1008 6.810 3.315 7.348 1.00163.33 C ANISOU 1691 CZ ARG A1008 21909 20558 19591 868 198 252 C ATOM 1692 NH1 ARG A1008 6.268 2.183 7.787 1.00151.94 N ANISOU 1692 NH1 ARG A1008 20319 19210 18202 837 152 200 N ATOM 1693 NH2 ARG A1008 6.129 4.449 7.466 1.00149.80 N ANISOU 1693 NH2 ARG A1008 20319 18811 17788 990 229 281 N ATOM 1694 N ILE A1009 14.212 1.630 7.401 1.00 74.10 N ANISOU 1694 N ILE A1009 10469 9108 8579 178 243 254 N ATOM 1695 CA ILE A1009 15.131 2.242 8.355 1.00 73.20 C ANISOU 1695 CA ILE A1009 10393 8950 8469 60 264 248 C ATOM 1696 C ILE A1009 16.276 2.905 7.571 1.00 79.16 C ANISOU 1696 C ILE A1009 11198 9686 9194 -28 324 254 C ATOM 1697 O ILE A1009 16.503 4.098 7.724 1.00 79.58 O ANISOU 1697 O ILE A1009 11383 9656 9198 -87 385 262 O ATOM 1698 CB ILE A1009 15.646 1.199 9.389 1.00 75.12 C ANISOU 1698 CB ILE A1009 10512 9257 8774 9 210 222 C ATOM 1699 CG1 ILE A1009 14.554 0.835 10.416 1.00 73.80 C ANISOU 1699 CG1 ILE A1009 10335 9080 8624 67 171 216 C ATOM 1700 CG2 ILE A1009 16.919 1.676 10.094 1.00 76.69 C ANISOU 1700 CG2 ILE A1009 10709 9461 8969 -123 227 204 C ATOM 1701 CD1 ILE A1009 14.747 -0.526 11.102 1.00 72.71 C ANISOU 1701 CD1 ILE A1009 10082 9004 8541 64 121 197 C ATOM 1702 N ASP A1010 16.945 2.145 6.687 1.00 77.09 N ANISOU 1702 N ASP A1010 10842 9495 8954 -37 316 247 N ATOM 1703 CA ASP A1010 18.105 2.596 5.915 1.00 77.29 C ANISOU 1703 CA ASP A1010 10886 9525 8955 -129 373 245 C ATOM 1704 C ASP A1010 17.798 3.668 4.852 1.00 83.24 C ANISOU 1704 C ASP A1010 11798 10194 9638 -97 449 278 C ATOM 1705 O ASP A1010 18.560 4.631 4.743 1.00 83.46 O ANISOU 1705 O ASP A1010 11923 10165 9624 -205 525 276 O ATOM 1706 CB ASP A1010 18.790 1.394 5.258 1.00 78.08 C ANISOU 1706 CB ASP A1010 10839 9731 9097 -122 341 231 C ATOM 1707 CG ASP A1010 19.538 0.492 6.228 1.00 84.08 C ANISOU 1707 CG ASP A1010 11464 10577 9905 -169 290 201 C ATOM 1708 OD1 ASP A1010 20.016 1.003 7.279 1.00 82.80 O ANISOU 1708 OD1 ASP A1010 11310 10413 9736 -258 293 182 O ATOM 1709 OD2 ASP A1010 19.728 -0.708 5.898 1.00 88.65 O ANISOU 1709 OD2 ASP A1010 11935 11230 10519 -117 253 194 O ATOM 1710 N GLU A1011 16.717 3.502 4.070 1.00 81.07 N ANISOU 1710 N GLU A1011 11550 9915 9338 49 435 304 N ATOM 1711 CA GLU A1011 16.353 4.433 2.991 1.00 82.12 C ANISOU 1711 CA GLU A1011 11835 9978 9388 118 502 342 C ATOM 1712 C GLU A1011 15.467 5.597 3.448 1.00 90.72 C ANISOU 1712 C GLU A1011 13101 10960 10410 184 541 370 C ATOM 1713 O GLU A1011 15.528 6.676 2.850 1.00 91.86 O ANISOU 1713 O GLU A1011 13422 11008 10472 198 627 402 O ATOM 1714 CB GLU A1011 15.618 3.702 1.854 1.00 82.46 C ANISOU 1714 CB GLU A1011 11816 10094 9420 258 465 351 C ATOM 1715 CG GLU A1011 16.401 2.602 1.168 1.00 83.73 C ANISOU 1715 CG GLU A1011 11833 10348 9631 218 439 329 C ATOM 1716 CD GLU A1011 17.554 3.071 0.311 1.00 96.15 C ANISOU 1716 CD GLU A1011 13456 11901 11175 132 512 339 C ATOM 1717 OE1 GLU A1011 17.764 4.300 0.203 1.00 91.70 O ANISOU 1717 OE1 GLU A1011 13055 11238 10548 92 594 364 O ATOM 1718 OE2 GLU A1011 18.260 2.202 -0.248 1.00 96.94 O ANISOU 1718 OE2 GLU A1011 13439 12081 11312 102 496 321 O ATOM 1719 N GLY A1012 14.618 5.345 4.445 1.00 88.80 N ANISOU 1719 N GLY A1012 12817 10732 10192 237 485 359 N ATOM 1720 CA GLY A1012 13.650 6.312 4.947 1.00 89.93 C ANISOU 1720 CA GLY A1012 13107 10791 10271 326 511 383 C ATOM 1721 C GLY A1012 12.401 6.298 4.091 1.00 96.44 C ANISOU 1721 C GLY A1012 13952 11659 11032 525 494 407 C ATOM 1722 O GLY A1012 12.236 5.401 3.253 1.00 95.85 O ANISOU 1722 O GLY A1012 13755 11688 10977 577 450 395 O ATOM 1723 N LEU A1013 11.505 7.291 4.293 1.00 95.26 N ANISOU 1723 N LEU A1013 13956 11440 10797 645 530 437 N ATOM 1724 CA LEU A1013 10.276 7.409 3.501 1.00 96.27 C ANISOU 1724 CA LEU A1013 14107 11630 10840 858 515 459 C ATOM 1725 C LEU A1013 9.908 8.891 3.244 1.00102.89 C ANISOU 1725 C LEU A1013 15205 12341 11549 976 607 515 C ATOM 1726 O LEU A1013 9.574 9.633 4.176 1.00103.62 O ANISOU 1726 O LEU A1013 15412 12347 11613 990 637 525 O ATOM 1727 CB LEU A1013 9.110 6.642 4.161 1.00 95.61 C ANISOU 1727 CB LEU A1013 13872 11669 10788 942 428 422 C ATOM 1728 CG LEU A1013 7.719 6.730 3.510 1.00100.93 C ANISOU 1728 CG LEU A1013 14533 12449 11365 1163 403 427 C ATOM 1729 CD1 LEU A1013 7.724 6.259 2.039 1.00101.06 C ANISOU 1729 CD1 LEU A1013 14490 12563 11347 1232 390 426 C ATOM 1730 CD2 LEU A1013 6.703 5.955 4.325 1.00103.06 C ANISOU 1730 CD2 LEU A1013 14642 12841 11675 1195 328 376 C ATOM 1731 N ARG A1014 9.988 9.305 1.971 1.00 99.92 N ANISOU 1731 N ARG A1014 14932 11947 11088 1066 659 553 N ATOM 1732 CA ARG A1014 9.652 10.660 1.540 1.00101.32 C ANISOU 1732 CA ARG A1014 15377 11996 11122 1204 758 614 C ATOM 1733 C ARG A1014 8.643 10.571 0.400 1.00105.60 C ANISOU 1733 C ARG A1014 15905 12656 11561 1450 730 639 C ATOM 1734 O ARG A1014 8.845 9.806 -0.546 1.00103.34 O ANISOU 1734 O ARG A1014 15491 12477 11297 1449 691 624 O ATOM 1735 CB ARG A1014 10.903 11.455 1.140 1.00101.80 C ANISOU 1735 CB ARG A1014 15629 11892 11159 1056 878 641 C ATOM 1736 N LEU A1015 7.527 11.316 0.520 1.00104.29 N ANISOU 1736 N LEU A1015 15860 12489 11278 1669 744 670 N ATOM 1737 CA LEU A1015 6.454 11.284 -0.474 1.00104.93 C ANISOU 1737 CA LEU A1015 15916 12714 11239 1930 710 687 C ATOM 1738 C LEU A1015 6.582 12.421 -1.506 1.00110.30 C ANISOU 1738 C LEU A1015 16876 13271 11761 2079 822 766 C ATOM 1739 O LEU A1015 5.713 12.573 -2.366 1.00110.61 O ANISOU 1739 O LEU A1015 16933 13422 11671 2326 806 790 O ATOM 1740 CB LEU A1015 5.076 11.286 0.213 1.00105.19 C ANISOU 1740 CB LEU A1015 15875 12869 11225 2106 648 667 C ATOM 1741 CG LEU A1015 4.712 10.007 1.005 1.00108.57 C ANISOU 1741 CG LEU A1015 16006 13458 11786 1996 534 584 C ATOM 1742 CD1 LEU A1015 3.281 10.034 1.434 1.00109.22 C ANISOU 1742 CD1 LEU A1015 16011 13690 11797 2189 482 560 C ATOM 1743 CD2 LEU A1015 4.948 8.735 0.194 1.00110.38 C ANISOU 1743 CD2 LEU A1015 16011 13840 12088 1919 463 533 C ATOM 1744 N LYS A1016 7.708 13.155 -1.464 1.00107.60 N ANISOU 1744 N LYS A1016 16744 12714 11426 1919 938 800 N ATOM 1745 CA LYS A1016 8.036 14.233 -2.393 1.00109.41 C ANISOU 1745 CA LYS A1016 17270 12786 11514 2009 1070 873 C ATOM 1746 C LYS A1016 9.450 14.027 -2.918 1.00114.08 C ANISOU 1746 C LYS A1016 17869 13297 12180 1766 1127 865 C ATOM 1747 O LYS A1016 10.339 13.678 -2.135 1.00113.21 O ANISOU 1747 O LYS A1016 17667 13147 12202 1508 1121 818 O ATOM 1748 CB LYS A1016 7.898 15.610 -1.719 1.00113.34 C ANISOU 1748 CB LYS A1016 18087 13066 11912 2062 1192 923 C ATOM 1749 N ILE A1017 9.653 14.243 -4.240 1.00111.61 N ANISOU 1749 N ILE A1017 17662 12974 11773 1858 1183 908 N ATOM 1750 CA ILE A1017 10.930 14.098 -4.954 1.00111.38 C ANISOU 1750 CA ILE A1017 17651 12882 11787 1660 1248 905 C ATOM 1751 C ILE A1017 12.033 14.932 -4.242 1.00115.86 C ANISOU 1751 C ILE A1017 18415 13225 12383 1408 1380 903 C ATOM 1752 O ILE A1017 11.785 16.060 -3.811 1.00116.20 O ANISOU 1752 O ILE A1017 18728 13094 12329 1463 1483 942 O ATOM 1753 CB ILE A1017 10.788 14.419 -6.480 1.00115.68 C ANISOU 1753 CB ILE A1017 18334 13430 12188 1846 1305 966 C ATOM 1754 CG1 ILE A1017 12.099 14.190 -7.261 1.00116.02 C ANISOU 1754 CG1 ILE A1017 18376 13427 12279 1639 1371 958 C ATOM 1755 CG2 ILE A1017 10.195 15.804 -6.761 1.00118.81 C ANISOU 1755 CG2 ILE A1017 19090 13665 12386 2074 1430 1051 C ATOM 1756 N TYR A1018 13.213 14.310 -4.049 1.00112.32 N ANISOU 1756 N TYR A1018 17809 12800 12068 1132 1369 847 N ATOM 1757 CA TYR A1018 14.380 14.863 -3.358 1.00112.67 C ANISOU 1757 CA TYR A1018 17958 12694 12157 850 1473 817 C ATOM 1758 C TYR A1018 15.681 14.324 -3.971 1.00116.75 C ANISOU 1758 C TYR A1018 18356 13257 12746 632 1495 780 C ATOM 1759 O TYR A1018 15.640 13.375 -4.753 1.00115.15 O ANISOU 1759 O TYR A1018 17961 13209 12583 695 1410 774 O ATOM 1760 CB TYR A1018 14.314 14.541 -1.835 1.00112.69 C ANISOU 1760 CB TYR A1018 17815 12730 12271 732 1394 760 C ATOM 1761 CG TYR A1018 14.467 13.077 -1.459 1.00112.29 C ANISOU 1761 CG TYR A1018 17402 12888 12376 655 1237 697 C ATOM 1762 CD1 TYR A1018 13.372 12.217 -1.461 1.00113.12 C ANISOU 1762 CD1 TYR A1018 17319 13153 12507 842 1102 693 C ATOM 1763 CD2 TYR A1018 15.693 12.568 -1.036 1.00112.45 C ANISOU 1763 CD2 TYR A1018 17274 12946 12507 395 1228 637 C ATOM 1764 CE1 TYR A1018 13.507 10.869 -1.119 1.00112.17 C ANISOU 1764 CE1 TYR A1018 16898 13201 12520 768 975 637 C ATOM 1765 CE2 TYR A1018 15.841 11.220 -0.692 1.00111.70 C ANISOU 1765 CE2 TYR A1018 16872 13028 12540 345 1094 587 C ATOM 1766 CZ TYR A1018 14.741 10.376 -0.720 1.00117.13 C ANISOU 1766 CZ TYR A1018 17403 13846 13253 529 973 589 C ATOM 1767 OH TYR A1018 14.869 9.054 -0.353 1.00114.33 O ANISOU 1767 OH TYR A1018 16777 13644 13018 476 856 539 O ATOM 1768 N LYS A1019 16.827 14.922 -3.605 1.00115.68 N ANISOU 1768 N LYS A1019 18330 12999 12623 372 1612 749 N ATOM 1769 CA LYS A1019 18.146 14.502 -4.075 1.00116.75 C ANISOU 1769 CA LYS A1019 18353 13187 12820 145 1646 705 C ATOM 1770 C LYS A1019 18.873 13.758 -2.974 1.00123.57 C ANISOU 1770 C LYS A1019 18958 14166 13828 -71 1561 621 C ATOM 1771 O LYS A1019 18.889 14.221 -1.832 1.00123.41 O ANISOU 1771 O LYS A1019 18991 14078 13823 -168 1577 592 O ATOM 1772 CB LYS A1019 18.975 15.706 -4.553 1.00121.28 C ANISOU 1772 CB LYS A1019 19228 13564 13289 -5 1851 720 C ATOM 1773 N ASP A1020 19.475 12.605 -3.313 1.00122.95 N ANISOU 1773 N ASP A1020 18608 14262 13845 -135 1473 582 N ATOM 1774 CA ASP A1020 20.227 11.774 -2.363 1.00123.57 C ANISOU 1774 CA ASP A1020 18427 14473 14050 -313 1387 505 C ATOM 1775 C ASP A1020 21.678 12.326 -2.213 1.00132.62 C ANISOU 1775 C ASP A1020 19616 15583 15191 -604 1506 449 C ATOM 1776 O ASP A1020 21.893 13.531 -2.397 1.00134.36 O ANISOU 1776 O ASP A1020 20106 15632 15314 -686 1660 463 O ATOM 1777 CB ASP A1020 20.194 10.276 -2.786 1.00124.01 C ANISOU 1777 CB ASP A1020 18190 14728 14199 -233 1246 490 C ATOM 1778 CG ASP A1020 20.897 9.887 -4.086 1.00135.70 C ANISOU 1778 CG ASP A1020 19621 16271 15668 -255 1281 495 C ATOM 1779 OD1 ASP A1020 21.145 10.783 -4.925 1.00138.69 O ANISOU 1779 OD1 ASP A1020 20213 16534 15950 -272 1411 529 O ATOM 1780 OD2 ASP A1020 21.170 8.676 -4.275 1.00138.10 O ANISOU 1780 OD2 ASP A1020 19684 16732 16055 -245 1183 466 O ATOM 1781 N THR A1021 22.657 11.466 -1.849 1.00130.61 N ANISOU 1781 N THR A1021 19103 15493 15031 -759 1443 380 N ATOM 1782 CA THR A1021 24.062 11.871 -1.692 1.00132.27 C ANISOU 1782 CA THR A1021 19300 15723 15234 -1039 1542 309 C ATOM 1783 C THR A1021 24.703 12.046 -3.077 1.00137.27 C ANISOU 1783 C THR A1021 20000 16344 15811 -1082 1646 325 C ATOM 1784 O THR A1021 25.454 13.006 -3.288 1.00138.83 O ANISOU 1784 O THR A1021 20368 16445 15937 -1274 1803 299 O ATOM 1785 CB THR A1021 24.839 10.863 -0.830 1.00143.27 C ANISOU 1785 CB THR A1021 20383 17321 16731 -1153 1431 233 C ATOM 1786 OG1 THR A1021 24.802 9.575 -1.452 1.00143.83 O ANISOU 1786 OG1 THR A1021 20235 17545 16867 -1021 1320 247 O ATOM 1787 CG2 THR A1021 24.315 10.785 0.611 1.00141.21 C ANISOU 1787 CG2 THR A1021 20073 17063 16515 -1137 1345 212 C ATOM 1788 N GLU A1022 24.360 11.143 -4.025 1.00132.11 N ANISOU 1788 N GLU A1022 19230 15783 15184 -906 1567 366 N ATOM 1789 CA GLU A1022 24.842 11.152 -5.408 1.00132.32 C ANISOU 1789 CA GLU A1022 19302 15814 15161 -907 1646 389 C ATOM 1790 C GLU A1022 24.201 12.290 -6.230 1.00136.86 C ANISOU 1790 C GLU A1022 20216 16180 15604 -802 1777 465 C ATOM 1791 O GLU A1022 24.507 12.438 -7.421 1.00137.75 O ANISOU 1791 O GLU A1022 20414 16269 15656 -787 1859 495 O ATOM 1792 CB GLU A1022 24.565 9.793 -6.069 1.00132.31 C ANISOU 1792 CB GLU A1022 19072 15974 15225 -737 1511 404 C ATOM 1793 N GLY A1023 23.330 13.074 -5.591 1.00132.39 N ANISOU 1793 N GLY A1023 19846 15467 14989 -721 1800 499 N ATOM 1794 CA GLY A1023 22.619 14.187 -6.211 1.00132.76 C ANISOU 1794 CA GLY A1023 20235 15309 14899 -587 1922 577 C ATOM 1795 C GLY A1023 21.565 13.744 -7.208 1.00133.76 C ANISOU 1795 C GLY A1023 20365 15474 14985 -283 1847 654 C ATOM 1796 O GLY A1023 21.068 14.560 -7.994 1.00135.13 O ANISOU 1796 O GLY A1023 20808 15507 15028 -143 1948 725 O ATOM 1797 N TYR A1024 21.225 12.440 -7.181 1.00125.28 N ANISOU 1797 N TYR A1024 18994 14594 14012 -180 1674 635 N ATOM 1798 CA TYR A1024 20.239 11.822 -8.059 1.00122.78 C ANISOU 1798 CA TYR A1024 18620 14360 13669 86 1582 684 C ATOM 1799 C TYR A1024 18.841 11.970 -7.454 1.00121.99 C ANISOU 1799 C TYR A1024 18566 14241 13544 299 1504 717 C ATOM 1800 O TYR A1024 18.695 11.932 -6.231 1.00120.05 O ANISOU 1800 O TYR A1024 18255 13995 13362 233 1454 683 O ATOM 1801 CB TYR A1024 20.586 10.343 -8.300 1.00122.36 C ANISOU 1801 CB TYR A1024 18241 14517 13733 69 1450 638 C ATOM 1802 CG TYR A1024 21.989 10.116 -8.822 1.00124.38 C ANISOU 1802 CG TYR A1024 18420 14821 14018 -133 1518 599 C ATOM 1803 N TYR A1025 17.824 12.175 -8.316 1.00116.63 N ANISOU 1803 N TYR A1025 18001 13555 12758 557 1498 780 N ATOM 1804 CA TYR A1025 16.430 12.338 -7.905 1.00114.91 C ANISOU 1804 CA TYR A1025 17822 13347 12492 790 1427 810 C ATOM 1805 C TYR A1025 15.853 11.003 -7.441 1.00112.43 C ANISOU 1805 C TYR A1025 17188 13235 12295 842 1247 759 C ATOM 1806 O TYR A1025 15.948 9.994 -8.143 1.00110.38 O ANISOU 1806 O TYR A1025 16738 13119 12081 864 1172 736 O ATOM 1807 CB TYR A1025 15.577 12.946 -9.033 1.00117.85 C ANISOU 1807 CB TYR A1025 18400 13681 12698 1060 1476 888 C ATOM 1808 CG TYR A1025 15.880 14.403 -9.327 1.00122.27 C ANISOU 1808 CG TYR A1025 19337 14004 13116 1054 1667 950 C ATOM 1809 CD1 TYR A1025 15.358 15.419 -8.531 1.00125.15 C ANISOU 1809 CD1 TYR A1025 19928 14214 13408 1113 1733 980 C ATOM 1810 CD2 TYR A1025 16.634 14.767 -10.441 1.00124.44 C ANISOU 1810 CD2 TYR A1025 19760 14204 13317 1002 1788 981 C ATOM 1811 CE1 TYR A1025 15.616 16.762 -8.810 1.00128.29 C ANISOU 1811 CE1 TYR A1025 20704 14374 13664 1110 1924 1038 C ATOM 1812 CE2 TYR A1025 16.900 16.107 -10.729 1.00127.41 C ANISOU 1812 CE2 TYR A1025 20511 14346 13553 991 1981 1038 C ATOM 1813 CZ TYR A1025 16.387 17.103 -9.911 1.00136.09 C ANISOU 1813 CZ TYR A1025 21845 15281 14581 1045 2051 1067 C ATOM 1814 OH TYR A1025 16.639 18.426 -10.190 1.00138.88 O ANISOU 1814 OH TYR A1025 22597 15384 14787 1034 2256 1123 O ATOM 1815 N THR A1026 15.288 11.011 -6.233 1.00106.43 N ANISOU 1815 N THR A1026 16383 12475 11582 847 1189 739 N ATOM 1816 CA THR A1026 14.715 9.843 -5.559 1.00103.64 C ANISOU 1816 CA THR A1026 15756 12285 11337 874 1036 687 C ATOM 1817 C THR A1026 13.303 10.198 -5.035 1.00107.18 C ANISOU 1817 C THR A1026 16258 12743 11722 1080 990 708 C ATOM 1818 O THR A1026 12.944 11.378 -5.001 1.00107.93 O ANISOU 1818 O THR A1026 16603 12701 11703 1175 1081 760 O ATOM 1819 CB THR A1026 15.678 9.398 -4.422 1.00100.39 C ANISOU 1819 CB THR A1026 15206 11876 11060 626 1013 629 C ATOM 1820 OG1 THR A1026 17.033 9.485 -4.861 1.00 96.54 O ANISOU 1820 OG1 THR A1026 14734 11354 10593 438 1093 616 O ATOM 1821 CG2 THR A1026 15.420 7.995 -3.938 1.00 94.84 C ANISOU 1821 CG2 THR A1026 14219 11339 10477 620 873 575 C ATOM 1822 N ILE A1027 12.504 9.163 -4.669 1.00101.88 N ANISOU 1822 N ILE A1027 15356 12236 11117 1150 858 665 N ATOM 1823 CA ILE A1027 11.156 9.251 -4.080 1.00101.19 C ANISOU 1823 CA ILE A1027 15250 12208 10990 1325 796 663 C ATOM 1824 C ILE A1027 10.860 7.918 -3.353 1.00102.10 C ANISOU 1824 C ILE A1027 15082 12474 11236 1257 670 592 C ATOM 1825 O ILE A1027 11.449 6.893 -3.696 1.00100.71 O ANISOU 1825 O ILE A1027 14740 12380 11146 1153 626 554 O ATOM 1826 CB ILE A1027 10.043 9.654 -5.111 1.00105.32 C ANISOU 1826 CB ILE A1027 15859 12800 11357 1607 795 704 C ATOM 1827 CG1 ILE A1027 8.775 10.209 -4.396 1.00106.26 C ANISOU 1827 CG1 ILE A1027 16037 12938 11400 1792 772 717 C ATOM 1828 CG2 ILE A1027 9.710 8.533 -6.109 1.00104.60 C ANISOU 1828 CG2 ILE A1027 15559 12908 11275 1676 706 666 C ATOM 1829 CD1 ILE A1027 8.084 11.329 -5.072 1.00115.21 C ANISOU 1829 CD1 ILE A1027 17408 14021 12347 2044 843 787 C ATOM 1830 N GLY A1028 9.991 7.967 -2.341 1.00 98.00 N ANISOU 1830 N GLY A1028 14530 11980 10725 1314 624 576 N ATOM 1831 CA GLY A1028 9.588 6.806 -1.550 1.00 96.54 C ANISOU 1831 CA GLY A1028 14112 11920 10648 1258 521 511 C ATOM 1832 C GLY A1028 10.695 6.214 -0.703 1.00 99.46 C ANISOU 1832 C GLY A1028 14390 12246 11155 1026 511 479 C ATOM 1833 O GLY A1028 11.460 6.944 -0.057 1.00 99.31 O ANISOU 1833 O GLY A1028 14492 12092 11150 909 574 497 O ATOM 1834 N ILE A1029 10.786 4.871 -0.710 1.00 94.49 N ANISOU 1834 N ILE A1029 13550 11735 10618 963 435 426 N ATOM 1835 CA ILE A1029 11.801 4.130 0.035 1.00 92.63 C ANISOU 1835 CA ILE A1029 13207 11486 10502 776 415 395 C ATOM 1836 C ILE A1029 12.930 3.789 -0.952 1.00 95.55 C ANISOU 1836 C ILE A1029 13553 11862 10891 696 445 398 C ATOM 1837 O ILE A1029 12.961 2.693 -1.530 1.00 94.84 O ANISOU 1837 O ILE A1029 13322 11872 10840 700 398 366 O ATOM 1838 CB ILE A1029 11.215 2.887 0.780 1.00 94.44 C ANISOU 1838 CB ILE A1029 13251 11819 10813 761 329 339 C ATOM 1839 CG1 ILE A1029 9.935 3.246 1.552 1.00 94.47 C ANISOU 1839 CG1 ILE A1029 13274 11841 10779 863 304 334 C ATOM 1840 CG2 ILE A1029 12.242 2.255 1.728 1.00 94.49 C ANISOU 1840 CG2 ILE A1029 13178 11799 10925 595 314 317 C ATOM 1841 CD1 ILE A1029 8.793 2.333 1.278 1.00100.52 C ANISOU 1841 CD1 ILE A1029 13897 12757 11538 952 241 284 C ATOM 1842 N GLY A1030 13.805 4.779 -1.156 1.00 91.82 N ANISOU 1842 N GLY A1030 13229 11277 10380 625 531 433 N ATOM 1843 CA GLY A1030 14.982 4.722 -2.018 1.00 91.53 C ANISOU 1843 CA GLY A1030 13198 11231 10349 532 582 439 C ATOM 1844 C GLY A1030 14.759 4.319 -3.462 1.00 96.06 C ANISOU 1844 C GLY A1030 13746 11877 10876 637 577 448 C ATOM 1845 O GLY A1030 15.507 3.482 -3.979 1.00 95.69 O ANISOU 1845 O GLY A1030 13585 11894 10880 569 562 424 O ATOM 1846 N HIS A1031 13.744 4.912 -4.133 1.00 93.20 N ANISOU 1846 N HIS A1031 13491 11515 10407 813 590 481 N ATOM 1847 CA HIS A1031 13.466 4.623 -5.542 1.00 93.04 C ANISOU 1847 CA HIS A1031 13457 11573 10322 929 585 489 C ATOM 1848 C HIS A1031 14.109 5.692 -6.424 1.00 99.72 C ANISOU 1848 C HIS A1031 14505 12308 11075 933 697 546 C ATOM 1849 O HIS A1031 13.599 6.813 -6.512 1.00100.36 O ANISOU 1849 O HIS A1031 14782 12300 11049 1042 757 595 O ATOM 1850 CB HIS A1031 11.957 4.496 -5.833 1.00 93.42 C ANISOU 1850 CB HIS A1031 13471 11729 10295 1133 524 480 C ATOM 1851 CG HIS A1031 11.660 4.038 -7.230 1.00 96.96 C ANISOU 1851 CG HIS A1031 13871 12289 10679 1244 505 473 C ATOM 1852 ND1 HIS A1031 11.542 4.936 -8.277 1.00 99.88 N ANISOU 1852 ND1 HIS A1031 14408 12623 10917 1376 568 528 N ATOM 1853 CD2 HIS A1031 11.494 2.786 -7.713 1.00 97.61 C ANISOU 1853 CD2 HIS A1031 13770 12510 10808 1235 436 414 C ATOM 1854 CE1 HIS A1031 11.310 4.206 -9.358 1.00 98.93 C ANISOU 1854 CE1 HIS A1031 14187 12635 10768 1446 528 501 C ATOM 1855 NE2 HIS A1031 11.264 2.909 -9.066 1.00 98.14 N ANISOU 1855 NE2 HIS A1031 13876 12641 10773 1359 449 429 N ATOM 1856 N LEU A1032 15.235 5.342 -7.071 1.00 97.42 N ANISOU 1856 N LEU A1032 14177 12021 10819 816 733 539 N ATOM 1857 CA LEU A1032 15.950 6.224 -7.985 1.00 99.46 C ANISOU 1857 CA LEU A1032 14614 12183 10994 794 847 585 C ATOM 1858 C LEU A1032 15.099 6.498 -9.226 1.00104.90 C ANISOU 1858 C LEU A1032 15396 12908 11556 1009 856 624 C ATOM 1859 O LEU A1032 14.689 5.559 -9.927 1.00103.49 O ANISOU 1859 O LEU A1032 15070 12870 11384 1092 780 596 O ATOM 1860 CB LEU A1032 17.307 5.610 -8.393 1.00 99.84 C ANISOU 1860 CB LEU A1032 14557 12264 11112 625 871 557 C ATOM 1861 CG LEU A1032 18.494 6.565 -8.597 1.00106.44 C ANISOU 1861 CG LEU A1032 15550 12979 11913 471 1005 578 C ATOM 1862 CD1 LEU A1032 18.440 7.280 -9.937 1.00107.50 C ANISOU 1862 CD1 LEU A1032 15872 13052 11920 569 1099 633 C ATOM 1863 CD2 LEU A1032 18.676 7.513 -7.401 1.00111.41 C ANISOU 1863 CD2 LEU A1032 16302 13484 12545 360 1061 580 C ATOM 1864 N LEU A1033 14.810 7.789 -9.469 1.00103.11 N ANISOU 1864 N LEU A1033 15420 12554 11203 1105 950 687 N ATOM 1865 CA LEU A1033 14.009 8.214 -10.607 1.00104.08 C ANISOU 1865 CA LEU A1033 15663 12703 11177 1335 969 735 C ATOM 1866 C LEU A1033 14.897 8.443 -11.833 1.00112.00 C ANISOU 1866 C LEU A1033 16770 13660 12126 1297 1062 766 C ATOM 1867 O LEU A1033 14.570 7.940 -12.912 1.00111.30 O ANISOU 1867 O LEU A1033 16618 13685 11985 1421 1024 765 O ATOM 1868 CB LEU A1033 13.187 9.467 -10.275 1.00104.62 C ANISOU 1868 CB LEU A1033 15970 12661 11121 1495 1027 793 C ATOM 1869 CG LEU A1033 12.020 9.268 -9.318 1.00107.53 C ANISOU 1869 CG LEU A1033 16240 13111 11507 1604 930 767 C ATOM 1870 CD1 LEU A1033 11.658 10.565 -8.633 1.00108.45 C ANISOU 1870 CD1 LEU A1033 16605 13066 11536 1674 1013 820 C ATOM 1871 CD2 LEU A1033 10.833 8.641 -10.011 1.00108.28 C ANISOU 1871 CD2 LEU A1033 16197 13409 11535 1825 828 746 C ATOM 1872 N THR A1034 16.014 9.195 -11.668 1.00111.88 N ANISOU 1872 N THR A1034 16909 13485 12115 1117 1188 786 N ATOM 1873 CA THR A1034 16.971 9.509 -12.738 1.00113.84 C ANISOU 1873 CA THR A1034 17271 13672 12311 1044 1299 813 C ATOM 1874 C THR A1034 18.283 10.096 -12.172 1.00120.82 C ANISOU 1874 C THR A1034 18244 14420 13244 773 1418 799 C ATOM 1875 O THR A1034 18.290 10.792 -11.148 1.00120.26 O ANISOU 1875 O THR A1034 18276 14236 13180 694 1460 799 O ATOM 1876 CB THR A1034 16.352 10.455 -13.829 1.00121.14 C ANISOU 1876 CB THR A1034 18461 14522 13046 1270 1385 894 C ATOM 1877 OG1 THR A1034 17.224 10.519 -14.959 1.00119.96 O ANISOU 1877 OG1 THR A1034 18381 14344 12853 1208 1476 913 O ATOM 1878 CG2 THR A1034 16.020 11.872 -13.316 1.00119.54 C ANISOU 1878 CG2 THR A1034 18566 14120 12735 1326 1500 954 C ATOM 1879 N LYS A1035 19.388 9.815 -12.880 1.00119.66 N ANISOU 1879 N LYS A1035 18051 14293 13119 631 1474 782 N ATOM 1880 CA LYS A1035 20.726 10.340 -12.587 1.00120.63 C ANISOU 1880 CA LYS A1035 18242 14322 13270 364 1599 758 C ATOM 1881 C LYS A1035 20.865 11.751 -13.221 1.00127.65 C ANISOU 1881 C LYS A1035 19488 15010 14004 373 1785 823 C ATOM 1882 O LYS A1035 21.720 12.537 -12.802 1.00128.33 O ANISOU 1882 O LYS A1035 19710 14970 14080 159 1916 807 O ATOM 1883 CB LYS A1035 21.840 9.375 -13.066 1.00121.97 C ANISOU 1883 CB LYS A1035 18191 14626 13526 216 1578 706 C ATOM 1884 CG LYS A1035 21.521 8.584 -14.339 1.00129.20 C ANISOU 1884 CG LYS A1035 19019 15657 14413 379 1520 722 C ATOM 1885 CD LYS A1035 21.152 7.129 -14.038 1.00130.74 C ANISOU 1885 CD LYS A1035 18914 16035 14725 436 1348 670 C ATOM 1886 CE LYS A1035 20.454 6.458 -15.198 1.00134.25 C ANISOU 1886 CE LYS A1035 19304 16585 15122 634 1282 685 C ATOM 1887 NZ LYS A1035 19.052 6.939 -15.364 1.00139.84 N ANISOU 1887 NZ LYS A1035 20137 17270 15726 868 1250 730 N ATOM 1888 N SER A1036 19.971 12.069 -14.198 1.00124.97 N ANISOU 1888 N SER A1036 19306 14643 13533 629 1798 894 N ATOM 1889 CA SER A1036 19.891 13.345 -14.913 1.00126.64 C ANISOU 1889 CA SER A1036 19882 14663 13573 708 1969 972 C ATOM 1890 C SER A1036 19.568 14.510 -13.970 1.00131.92 C ANISOU 1890 C SER A1036 20802 15137 14182 692 2060 998 C ATOM 1891 O SER A1036 18.679 14.372 -13.121 1.00130.41 O ANISOU 1891 O SER A1036 20540 14985 14023 806 1955 993 O ATOM 1892 CB SER A1036 18.837 13.276 -16.018 1.00129.76 C ANISOU 1892 CB SER A1036 20346 15116 13841 1030 1926 1037 C ATOM 1893 OG SER A1036 18.621 14.539 -16.631 1.00138.44 O ANISOU 1893 OG SER A1036 21821 16022 14756 1153 2088 1123 O ATOM 1894 N PRO A1037 20.231 15.683 -14.142 1.00130.96 N ANISOU 1894 N PRO A1037 20995 14800 13964 560 2265 1026 N ATOM 1895 CA PRO A1037 19.932 16.832 -13.269 1.00131.85 C ANISOU 1895 CA PRO A1037 21380 14708 14008 542 2369 1049 C ATOM 1896 C PRO A1037 18.843 17.714 -13.887 1.00136.96 C ANISOU 1896 C PRO A1037 22351 15224 14462 864 2437 1155 C ATOM 1897 O PRO A1037 19.114 18.816 -14.366 1.00138.93 O ANISOU 1897 O PRO A1037 22962 15256 14568 854 2634 1210 O ATOM 1898 CB PRO A1037 21.288 17.547 -13.151 1.00134.82 C ANISOU 1898 CB PRO A1037 21913 14933 14380 203 2561 1009 C ATOM 1899 CG PRO A1037 22.131 17.019 -14.323 1.00139.31 C ANISOU 1899 CG PRO A1037 22381 15595 14956 122 2592 999 C ATOM 1900 CD PRO A1037 21.307 16.018 -15.095 1.00133.59 C ANISOU 1900 CD PRO A1037 21455 15060 14242 402 2422 1032 C ATOM 1901 N SER A1038 17.602 17.202 -13.895 1.00132.07 N ANISOU 1901 N SER A1038 21601 14749 13831 1157 2276 1180 N ATOM 1902 CA SER A1038 16.436 17.877 -14.465 1.00132.75 C ANISOU 1902 CA SER A1038 21933 14777 13730 1513 2304 1273 C ATOM 1903 C SER A1038 15.172 17.419 -13.728 1.00135.01 C ANISOU 1903 C SER A1038 22035 15215 14049 1727 2126 1261 C ATOM 1904 O SER A1038 14.858 16.228 -13.744 1.00133.81 O ANISOU 1904 O SER A1038 21537 15300 14005 1758 1949 1209 O ATOM 1905 CB SER A1038 16.351 17.584 -15.960 1.00136.32 C ANISOU 1905 CB SER A1038 22395 15316 14084 1685 2304 1319 C ATOM 1906 OG SER A1038 15.343 18.345 -16.599 1.00146.99 O ANISOU 1906 OG SER A1038 24017 16605 15226 2033 2353 1414 O ATOM 1907 N LEU A1039 14.482 18.351 -13.038 1.00131.37 N ANISOU 1907 N LEU A1039 21806 14613 13495 1856 2183 1303 N ATOM 1908 CA LEU A1039 13.282 18.048 -12.252 1.00129.87 C ANISOU 1908 CA LEU A1039 21465 14554 13324 2051 2034 1291 C ATOM 1909 C LEU A1039 12.080 17.641 -13.136 1.00134.97 C ANISOU 1909 C LEU A1039 22019 15404 13858 2416 1919 1327 C ATOM 1910 O LEU A1039 11.324 16.758 -12.724 1.00133.47 O ANISOU 1910 O LEU A1039 21529 15435 13748 2496 1744 1275 O ATOM 1911 CB LEU A1039 12.904 19.221 -11.332 1.00130.70 C ANISOU 1911 CB LEU A1039 21868 14447 13345 2099 2142 1328 C ATOM 1912 CG LEU A1039 11.727 19.000 -10.377 1.00134.12 C ANISOU 1912 CG LEU A1039 22158 15000 13800 2276 2004 1311 C ATOM 1913 CD1 LEU A1039 12.121 18.125 -9.197 1.00132.01 C ANISOU 1913 CD1 LEU A1039 21572 14833 13753 2008 1886 1213 C ATOM 1914 CD2 LEU A1039 11.169 20.317 -9.899 1.00137.83 C ANISOU 1914 CD2 LEU A1039 22999 15255 14115 2437 2133 1378 C ATOM 1915 N ASN A1040 11.909 18.247 -14.339 1.00133.43 N ANISOU 1915 N ASN A1040 22073 15150 13476 2630 2016 1408 N ATOM 1916 CA ASN A1040 10.800 17.877 -15.233 1.00133.28 C ANISOU 1916 CA ASN A1040 21959 15349 13332 2980 1906 1436 C ATOM 1917 C ASN A1040 11.083 16.501 -15.898 1.00134.65 C ANISOU 1917 C ASN A1040 21768 15766 13627 2887 1767 1365 C ATOM 1918 O ASN A1040 10.134 15.814 -16.285 1.00134.07 O ANISOU 1918 O ASN A1040 21481 15941 13520 3099 1621 1341 O ATOM 1919 CB ASN A1040 10.485 18.976 -16.269 1.00136.09 C ANISOU 1919 CB ASN A1040 22707 15570 13432 3266 2053 1549 C ATOM 1920 CG ASN A1040 11.605 19.353 -17.212 1.00166.90 C ANISOU 1920 CG ASN A1040 26826 19299 17289 3120 2217 1589 C ATOM 1921 OD1 ASN A1040 12.790 19.177 -16.924 1.00161.95 O ANISOU 1921 OD1 ASN A1040 26156 18571 16806 2766 2280 1542 O ATOM 1922 ND2 ASN A1040 11.249 19.916 -18.365 1.00162.40 N ANISOU 1922 ND2 ASN A1040 26502 18699 16505 3398 2298 1677 N ATOM 1923 N ALA A1041 12.380 16.090 -15.971 1.00129.18 N ANISOU 1923 N ALA A1041 20999 15010 13073 2563 1812 1325 N ATOM 1924 CA ALA A1041 12.836 14.785 -16.480 1.00126.95 C ANISOU 1924 CA ALA A1041 20387 14925 12922 2434 1698 1254 C ATOM 1925 C ALA A1041 12.655 13.704 -15.395 1.00128.01 C ANISOU 1925 C ALA A1041 20167 15220 13253 2294 1534 1159 C ATOM 1926 O ALA A1041 12.510 12.520 -15.708 1.00126.40 O ANISOU 1926 O ALA A1041 19667 15227 13134 2284 1400 1097 O ATOM 1927 CB ALA A1041 14.292 14.861 -16.904 1.00127.69 C ANISOU 1927 CB ALA A1041 20556 14887 13073 2157 1823 1251 C ATOM 1928 N ALA A1042 12.679 14.136 -14.119 1.00123.16 N ANISOU 1928 N ALA A1042 19602 14490 12703 2183 1556 1147 N ATOM 1929 CA ALA A1042 12.471 13.320 -12.931 1.00120.33 C ANISOU 1929 CA ALA A1042 18967 14242 12511 2062 1424 1069 C ATOM 1930 C ALA A1042 10.975 13.155 -12.665 1.00123.07 C ANISOU 1930 C ALA A1042 19220 14748 12794 2332 1305 1064 C ATOM 1931 O ALA A1042 10.551 12.091 -12.215 1.00120.60 O ANISOU 1931 O ALA A1042 18608 14621 12594 2301 1161 991 O ATOM 1932 CB ALA A1042 13.150 13.972 -11.738 1.00120.91 C ANISOU 1932 CB ALA A1042 19163 14121 12657 1837 1512 1061 C ATOM 1933 N LYS A1043 10.180 14.207 -12.966 1.00121.63 N ANISOU 1933 N LYS A1043 19298 14495 12420 2602 1373 1141 N ATOM 1934 CA LYS A1043 8.722 14.256 -12.796 1.00121.98 C ANISOU 1934 CA LYS A1043 19288 14696 12362 2899 1280 1144 C ATOM 1935 C LYS A1043 8.005 13.425 -13.881 1.00126.28 C ANISOU 1935 C LYS A1043 19625 15513 12842 3093 1163 1115 C ATOM 1936 O LYS A1043 6.871 12.989 -13.660 1.00126.02 O ANISOU 1936 O LYS A1043 19408 15694 12782 3261 1042 1072 O ATOM 1937 CB LYS A1043 8.226 15.718 -12.815 1.00126.03 C ANISOU 1937 CB LYS A1043 20179 15032 12674 3136 1410 1242 C ATOM 1938 CG LYS A1043 6.960 15.965 -12.000 1.00134.23 C ANISOU 1938 CG LYS A1043 21186 16162 13652 3353 1340 1238 C ATOM 1939 N SER A1044 8.654 13.212 -15.042 1.00122.85 N ANISOU 1939 N SER A1044 19218 15081 12379 3063 1202 1131 N ATOM 1940 CA SER A1044 8.074 12.419 -16.125 1.00122.87 C ANISOU 1940 CA SER A1044 19030 15337 12317 3225 1098 1097 C ATOM 1941 C SER A1044 8.310 10.935 -15.868 1.00124.07 C ANISOU 1941 C SER A1044 18815 15661 12666 3008 966 987 C ATOM 1942 O SER A1044 7.477 10.113 -16.252 1.00123.03 O ANISOU 1942 O SER A1044 18453 15780 12512 3123 843 924 O ATOM 1943 CB SER A1044 8.629 12.845 -17.482 1.00128.57 C ANISOU 1943 CB SER A1044 19952 15985 12912 3300 1200 1164 C ATOM 1944 OG SER A1044 10.043 12.757 -17.530 1.00138.46 O ANISOU 1944 OG SER A1044 21255 17067 14288 3002 1292 1165 O ATOM 1945 N GLU A1045 9.420 10.600 -15.178 1.00119.88 N ANISOU 1945 N GLU A1045 18232 14998 12317 2696 997 960 N ATOM 1946 CA GLU A1045 9.773 9.228 -14.787 1.00117.96 C ANISOU 1946 CA GLU A1045 17675 14879 12265 2480 890 864 C ATOM 1947 C GLU A1045 8.820 8.689 -13.706 1.00120.76 C ANISOU 1947 C GLU A1045 17829 15365 12690 2498 773 798 C ATOM 1948 O GLU A1045 8.650 7.474 -13.604 1.00118.68 O ANISOU 1948 O GLU A1045 17299 15264 12531 2411 668 713 O ATOM 1949 CB GLU A1045 11.231 9.133 -14.313 1.00118.56 C ANISOU 1949 CB GLU A1045 17769 14785 12492 2172 962 859 C ATOM 1950 CG GLU A1045 12.264 9.198 -15.432 1.00131.49 C ANISOU 1950 CG GLU A1045 19500 16359 14103 2098 1050 889 C ATOM 1951 CD GLU A1045 12.163 8.175 -16.552 1.00157.84 C ANISOU 1951 CD GLU A1045 22655 19885 17433 2153 973 847 C ATOM 1952 OE1 GLU A1045 11.809 7.005 -16.276 1.00157.32 O ANISOU 1952 OE1 GLU A1045 22321 19985 17467 2107 850 765 O ATOM 1953 OE2 GLU A1045 12.464 8.543 -17.709 1.00154.10 O ANISOU 1953 OE2 GLU A1045 22319 19383 16848 2233 1045 894 O ATOM 1954 N LEU A1046 8.205 9.592 -12.914 1.00118.74 N ANISOU 1954 N LEU A1046 17715 15031 12370 2608 803 837 N ATOM 1955 CA LEU A1046 7.197 9.287 -11.895 1.00118.78 C ANISOU 1955 CA LEU A1046 17567 15154 12411 2658 708 785 C ATOM 1956 C LEU A1046 5.875 8.907 -12.565 1.00125.70 C ANISOU 1956 C LEU A1046 18299 16300 13162 2911 610 745 C ATOM 1957 O LEU A1046 5.281 7.875 -12.237 1.00124.33 O ANISOU 1957 O LEU A1046 17858 16320 13063 2867 499 653 O ATOM 1958 CB LEU A1046 6.965 10.520 -11.007 1.00119.67 C ANISOU 1958 CB LEU A1046 17915 15092 12462 2730 788 848 C ATOM 1959 CG LEU A1046 7.764 10.648 -9.735 1.00123.66 C ANISOU 1959 CG LEU A1046 18452 15417 13118 2475 828 840 C ATOM 1960 CD1 LEU A1046 8.481 11.964 -9.707 1.00125.33 C ANISOU 1960 CD1 LEU A1046 19001 15362 13257 2447 986 925 C ATOM 1961 CD2 LEU A1046 6.858 10.615 -8.546 1.00125.64 C ANISOU 1961 CD2 LEU A1046 18614 15728 13397 2522 763 807 C ATOM 1962 N ASP A1047 5.412 9.786 -13.501 1.00125.71 N ANISOU 1962 N ASP A1047 18492 16315 12959 3182 660 815 N ATOM 1963 CA ASP A1047 4.159 9.683 -14.252 1.00127.12 C ANISOU 1963 CA ASP A1047 18575 16756 12968 3472 582 790 C ATOM 1964 C ASP A1047 4.090 8.382 -15.055 1.00131.65 C ANISOU 1964 C ASP A1047 18874 17559 13589 3404 483 695 C ATOM 1965 O ASP A1047 3.013 7.790 -15.135 1.00131.41 O ANISOU 1965 O ASP A1047 18625 17795 13507 3516 377 613 O ATOM 1966 CB ASP A1047 3.963 10.903 -15.180 1.00130.96 C ANISOU 1966 CB ASP A1047 19360 17173 13224 3761 677 897 C ATOM 1967 CG ASP A1047 3.820 12.270 -14.506 1.00141.68 C ANISOU 1967 CG ASP A1047 21026 18319 14489 3889 784 992 C ATOM 1968 OD1 ASP A1047 3.526 12.313 -13.289 1.00141.55 O ANISOU 1968 OD1 ASP A1047 20957 18270 14556 3818 760 966 O ATOM 1969 OD2 ASP A1047 3.965 13.296 -15.208 1.00148.95 O ANISOU 1969 OD2 ASP A1047 22249 19105 15242 4071 896 1091 O ATOM 1970 N LYS A1048 5.224 7.923 -15.624 1.00128.50 N ANISOU 1970 N LYS A1048 18479 17063 13281 3214 520 698 N ATOM 1971 CA LYS A1048 5.253 6.672 -16.384 1.00128.27 C ANISOU 1971 CA LYS A1048 18210 17225 13301 3135 438 609 C ATOM 1972 C LYS A1048 5.266 5.452 -15.427 1.00132.00 C ANISOU 1972 C LYS A1048 18419 17764 13971 2895 355 504 C ATOM 1973 O LYS A1048 4.680 4.418 -15.752 1.00131.55 O ANISOU 1973 O LYS A1048 18130 17929 13923 2885 264 404 O ATOM 1974 CB LYS A1048 6.421 6.627 -17.396 1.00130.58 C ANISOU 1974 CB LYS A1048 18608 17402 13605 3044 511 652 C ATOM 1975 CG LYS A1048 7.821 6.738 -16.808 1.00142.87 C ANISOU 1975 CG LYS A1048 20262 18700 15321 2775 599 689 C ATOM 1976 N ALA A1049 5.890 5.596 -14.242 1.00128.34 N ANISOU 1976 N ALA A1049 18003 17111 13650 2709 393 524 N ATOM 1977 CA ALA A1049 5.979 4.534 -13.241 1.00126.93 C ANISOU 1977 CA ALA A1049 17615 16963 13651 2491 329 440 C ATOM 1978 C ALA A1049 4.649 4.312 -12.507 1.00133.10 C ANISOU 1978 C ALA A1049 18247 17918 14405 2582 248 374 C ATOM 1979 O ALA A1049 4.332 3.167 -12.170 1.00132.34 O ANISOU 1979 O ALA A1049 17929 17952 14402 2459 176 275 O ATOM 1980 CB ALA A1049 7.071 4.858 -12.241 1.00126.51 C ANISOU 1980 CB ALA A1049 17669 16665 13735 2287 397 487 C ATOM 1981 N ILE A1050 3.876 5.396 -12.266 1.00131.62 N ANISOU 1981 N ILE A1050 18191 17733 14084 2795 268 427 N ATOM 1982 CA ILE A1050 2.598 5.365 -11.541 1.00132.01 C ANISOU 1982 CA ILE A1050 18118 17951 14089 2906 202 372 C ATOM 1983 C ILE A1050 1.395 5.280 -12.510 1.00138.88 C ANISOU 1983 C ILE A1050 18875 19118 14775 3155 136 321 C ATOM 1984 O ILE A1050 0.451 4.531 -12.247 1.00138.89 O ANISOU 1984 O ILE A1050 18645 19351 14777 3152 53 214 O ATOM 1985 CB ILE A1050 2.516 6.596 -10.579 1.00135.24 C ANISOU 1985 CB ILE A1050 18737 18181 14465 2987 266 457 C ATOM 1986 CG1 ILE A1050 3.589 6.504 -9.465 1.00134.07 C ANISOU 1986 CG1 ILE A1050 18642 17793 14507 2714 311 476 C ATOM 1987 CG2 ILE A1050 1.109 6.843 -9.989 1.00136.30 C ANISOU 1987 CG2 ILE A1050 18787 18498 14504 3174 211 419 C ATOM 1988 CD1 ILE A1050 3.542 5.236 -8.497 1.00137.16 C ANISOU 1988 CD1 ILE A1050 18785 18255 15076 2488 237 376 C ATOM 1989 N GLY A1051 1.451 6.023 -13.606 1.00137.27 N ANISOU 1989 N GLY A1051 18833 18912 14410 3360 178 392 N ATOM 1990 CA GLY A1051 0.364 6.071 -14.577 1.00139.02 C ANISOU 1990 CA GLY A1051 18969 19421 14431 3628 119 354 C ATOM 1991 C GLY A1051 -0.662 7.105 -14.166 1.00144.71 C ANISOU 1991 C GLY A1051 19782 20211 14990 3909 123 396 C ATOM 1992 O GLY A1051 -1.868 6.833 -14.166 1.00145.81 O ANISOU 1992 O GLY A1051 19727 20645 15029 4053 40 312 O ATOM 1993 N ARG A1052 -0.163 8.299 -13.781 1.00140.73 N ANISOU 1993 N ARG A1052 19579 19434 14457 3977 227 522 N ATOM 1994 CA ARG A1052 -0.926 9.457 -13.309 1.00141.44 C ANISOU 1994 CA ARG A1052 19836 19507 14397 4241 261 589 C ATOM 1995 C ARG A1052 -0.019 10.686 -13.284 1.00145.15 C ANISOU 1995 C ARG A1052 20689 19626 14836 4269 405 732 C ATOM 1996 O ARG A1052 1.187 10.539 -13.088 1.00143.14 O ANISOU 1996 O ARG A1052 20515 19135 14738 4002 466 757 O ATOM 1997 CB ARG A1052 -1.480 9.168 -11.893 1.00139.66 C ANISOU 1997 CB ARG A1052 19461 19323 14282 4135 214 525 C ATOM 1998 CG ARG A1052 -2.685 10.006 -11.467 1.00148.76 C ANISOU 1998 CG ARG A1052 20658 20602 15261 4439 205 544 C ATOM 1999 CD ARG A1052 -2.354 11.162 -10.526 1.00154.28 C ANISOU 1999 CD ARG A1052 21651 21001 15965 4469 309 651 C ATOM 2000 NE ARG A1052 -1.265 10.881 -9.580 1.00154.29 N ANISOU 2000 NE ARG A1052 21689 20734 16199 4119 351 656 N ATOM 2001 CZ ARG A1052 -1.402 10.239 -8.423 1.00160.05 C ANISOU 2001 CZ ARG A1052 22239 21486 17086 3919 301 583 C ATOM 2002 NH1 ARG A1052 -2.586 9.767 -8.053 1.00145.03 N ANISOU 2002 NH1 ARG A1052 20099 19859 15145 4010 210 493 N ATOM 2003 NH2 ARG A1052 -0.352 10.050 -7.636 1.00142.45 N ANISOU 2003 NH2 ARG A1052 20062 19015 15047 3628 343 595 N ATOM 2004 N ASN A1053 -0.589 11.896 -13.464 1.00143.48 N ANISOU 2004 N ASN A1053 20718 19383 14416 4589 467 821 N ATOM 2005 CA ASN A1053 0.168 13.153 -13.398 1.00143.82 C ANISOU 2005 CA ASN A1053 21159 19080 14405 4627 622 955 C ATOM 2006 C ASN A1053 0.427 13.465 -11.911 1.00145.87 C ANISOU 2006 C ASN A1053 21486 19134 14805 4446 663 962 C ATOM 2007 O ASN A1053 -0.340 14.202 -11.278 1.00146.79 O ANISOU 2007 O ASN A1053 21705 19249 14820 4642 681 992 O ATOM 2008 CB ASN A1053 -0.581 14.286 -14.117 1.00147.01 C ANISOU 2008 CB ASN A1053 21811 19523 14523 5050 679 1047 C ATOM 2009 N THR A1054 1.489 12.835 -11.350 1.00139.15 N ANISOU 2009 N THR A1054 20555 18132 14183 4077 670 926 N ATOM 2010 CA THR A1054 1.904 12.889 -9.937 1.00136.91 C ANISOU 2010 CA THR A1054 20283 17673 14064 3845 694 914 C ATOM 2011 C THR A1054 2.149 14.319 -9.420 1.00140.19 C ANISOU 2011 C THR A1054 21073 17800 14393 3924 836 1017 C ATOM 2012 O THR A1054 1.728 14.634 -8.306 1.00138.65 O ANISOU 2012 O THR A1054 20894 17563 14224 3928 834 1010 O ATOM 2013 CB THR A1054 3.174 12.042 -9.715 1.00139.30 C ANISOU 2013 CB THR A1054 20473 17863 14591 3467 692 872 C ATOM 2014 OG1 THR A1054 4.249 12.586 -10.486 1.00136.90 O ANISOU 2014 OG1 THR A1054 20403 17353 14258 3404 808 944 O ATOM 2015 CG2 THR A1054 2.971 10.574 -10.058 1.00135.92 C ANISOU 2015 CG2 THR A1054 19692 17688 14264 3361 562 764 C ATOM 2016 N ASN A1055 2.836 15.161 -10.228 1.00137.49 N ANISOU 2016 N ASN A1055 21037 17255 13949 3975 967 1109 N ATOM 2017 CA ASN A1055 3.232 16.549 -9.951 1.00138.28 C ANISOU 2017 CA ASN A1055 21545 17044 13952 4026 1135 1209 C ATOM 2018 C ASN A1055 4.281 16.590 -8.811 1.00139.11 C ANISOU 2018 C ASN A1055 21692 16912 14250 3663 1193 1188 C ATOM 2019 O ASN A1055 4.341 17.553 -8.042 1.00139.15 O ANISOU 2019 O ASN A1055 21948 16706 14216 3666 1295 1233 O ATOM 2020 CB ASN A1055 2.020 17.460 -9.665 1.00142.27 C ANISOU 2020 CB ASN A1055 22209 17587 14259 4386 1153 1259 C ATOM 2021 N GLY A1056 5.120 15.553 -8.765 1.00132.90 N ANISOU 2021 N GLY A1056 20669 16170 13657 3361 1133 1120 N ATOM 2022 CA GLY A1056 6.202 15.407 -7.800 1.00130.94 C ANISOU 2022 CA GLY A1056 20407 15750 13594 3010 1170 1087 C ATOM 2023 C GLY A1056 5.814 14.846 -6.447 1.00132.58 C ANISOU 2023 C GLY A1056 20399 16037 13939 2900 1072 1017 C ATOM 2024 O GLY A1056 6.677 14.720 -5.576 1.00130.78 O ANISOU 2024 O GLY A1056 20151 15683 13856 2622 1096 987 O ATOM 2025 N VAL A1057 4.525 14.492 -6.258 1.00129.05 N ANISOU 2025 N VAL A1057 19780 15812 13441 3112 963 985 N ATOM 2026 CA VAL A1057 4.016 13.942 -4.997 1.00127.49 C ANISOU 2026 CA VAL A1057 19375 15707 13358 3029 871 917 C ATOM 2027 C VAL A1057 3.403 12.543 -5.214 1.00130.03 C ANISOU 2027 C VAL A1057 19322 16329 13755 3022 717 825 C ATOM 2028 O VAL A1057 2.769 12.279 -6.236 1.00130.00 O ANISOU 2028 O VAL A1057 19235 16516 13645 3214 669 817 O ATOM 2029 CB VAL A1057 3.037 14.888 -4.240 1.00132.52 C ANISOU 2029 CB VAL A1057 20168 16308 13875 3249 903 953 C ATOM 2030 CG1 VAL A1057 3.784 16.064 -3.616 1.00133.01 C ANISOU 2030 CG1 VAL A1057 20568 16048 13921 3152 1052 1015 C ATOM 2031 CG2 VAL A1057 1.892 15.379 -5.124 1.00134.10 C ANISOU 2031 CG2 VAL A1057 20439 16659 13852 3637 895 994 C ATOM 2032 N ILE A1058 3.618 11.651 -4.237 1.00125.71 N ANISOU 2032 N ILE A1058 18559 15819 13385 2794 647 753 N ATOM 2033 CA ILE A1058 3.157 10.259 -4.234 1.00124.68 C ANISOU 2033 CA ILE A1058 18091 15932 13349 2726 519 657 C ATOM 2034 C ILE A1058 2.394 9.985 -2.932 1.00128.28 C ANISOU 2034 C ILE A1058 18415 16461 13864 2704 461 605 C ATOM 2035 O ILE A1058 2.763 10.528 -1.897 1.00127.63 O ANISOU 2035 O ILE A1058 18457 16203 13833 2608 511 630 O ATOM 2036 CB ILE A1058 4.412 9.327 -4.421 1.00126.53 C ANISOU 2036 CB ILE A1058 18215 16112 13750 2441 510 624 C ATOM 2037 CG1 ILE A1058 4.914 9.337 -5.874 1.00127.93 C ANISOU 2037 CG1 ILE A1058 18452 16296 13858 2489 543 655 C ATOM 2038 CG2 ILE A1058 4.216 7.887 -3.939 1.00125.88 C ANISOU 2038 CG2 ILE A1058 17828 16192 13810 2288 403 526 C ATOM 2039 CD1 ILE A1058 3.848 9.041 -6.969 1.00137.99 C ANISOU 2039 CD1 ILE A1058 19617 17816 14996 2732 478 631 C ATOM 2040 N THR A1059 1.333 9.159 -2.982 1.00125.27 N ANISOU 2040 N THR A1059 17785 16342 13470 2785 362 526 N ATOM 2041 CA THR A1059 0.604 8.798 -1.764 1.00125.15 C ANISOU 2041 CA THR A1059 17627 16409 13514 2745 310 468 C ATOM 2042 C THR A1059 1.299 7.562 -1.134 1.00127.75 C ANISOU 2042 C THR A1059 17773 16721 14046 2443 266 402 C ATOM 2043 O THR A1059 1.922 6.785 -1.859 1.00126.86 O ANISOU 2043 O THR A1059 17571 16634 13995 2328 247 377 O ATOM 2044 CB THR A1059 -0.907 8.628 -2.024 1.00136.82 C ANISOU 2044 CB THR A1059 18943 18179 14863 2977 240 411 C ATOM 2045 OG1 THR A1059 -1.592 8.574 -0.770 1.00141.01 O ANISOU 2045 OG1 THR A1059 19394 18752 15430 2959 216 372 O ATOM 2046 CG2 THR A1059 -1.251 7.411 -2.880 1.00133.57 C ANISOU 2046 CG2 THR A1059 18271 18015 14466 2939 158 318 C ATOM 2047 N LYS A1060 1.192 7.389 0.198 1.00123.80 N ANISOU 2047 N LYS A1060 17226 16173 13638 2328 253 376 N ATOM 2048 CA LYS A1060 1.820 6.285 0.938 1.00122.23 C ANISOU 2048 CA LYS A1060 16880 15944 13616 2066 219 322 C ATOM 2049 C LYS A1060 1.481 4.903 0.351 1.00126.35 C ANISOU 2049 C LYS A1060 17156 16669 14182 2003 148 233 C ATOM 2050 O LYS A1060 2.356 4.037 0.324 1.00125.43 O ANISOU 2050 O LYS A1060 16971 16500 14185 1813 140 211 O ATOM 2051 CB LYS A1060 1.435 6.334 2.420 1.00124.37 C ANISOU 2051 CB LYS A1060 17131 16180 13943 2008 211 303 C ATOM 2052 N ASP A1061 0.238 4.712 -0.149 1.00123.51 N ANISOU 2052 N ASP A1061 16667 16545 13715 2166 102 178 N ATOM 2053 CA ASP A1061 -0.228 3.461 -0.765 1.00122.97 C ANISOU 2053 CA ASP A1061 16370 16690 13664 2111 42 78 C ATOM 2054 C ASP A1061 0.497 3.178 -2.109 1.00125.65 C ANISOU 2054 C ASP A1061 16725 17024 13992 2099 47 92 C ATOM 2055 O ASP A1061 0.685 2.012 -2.467 1.00124.33 O ANISOU 2055 O ASP A1061 16410 16933 13897 1962 17 22 O ATOM 2056 CB ASP A1061 -1.750 3.511 -0.978 1.00126.16 C ANISOU 2056 CB ASP A1061 16638 17366 13930 2301 -3 11 C ATOM 2057 N GLU A1062 0.894 4.247 -2.839 1.00121.91 N ANISOU 2057 N GLU A1062 16444 16454 13422 2241 95 182 N ATOM 2058 CA GLU A1062 1.603 4.176 -4.124 1.00121.06 C ANISOU 2058 CA GLU A1062 16386 16326 13287 2250 113 209 C ATOM 2059 C GLU A1062 3.100 3.890 -3.937 1.00122.13 C ANISOU 2059 C GLU A1062 16591 16248 13566 2025 154 245 C ATOM 2060 O GLU A1062 3.671 3.119 -4.710 1.00121.11 O ANISOU 2060 O GLU A1062 16388 16146 13481 1936 143 219 O ATOM 2061 CB GLU A1062 1.426 5.483 -4.913 1.00123.73 C ANISOU 2061 CB GLU A1062 16927 16631 13454 2495 161 296 C ATOM 2062 CG GLU A1062 0.145 5.550 -5.728 1.00133.86 C ANISOU 2062 CG GLU A1062 18113 18183 14566 2743 112 255 C ATOM 2063 CD GLU A1062 -0.114 6.859 -6.450 1.00147.09 C ANISOU 2063 CD GLU A1062 20006 19830 16051 3023 163 347 C ATOM 2064 OE1 GLU A1062 0.600 7.853 -6.182 1.00128.58 O ANISOU 2064 OE1 GLU A1062 17917 17236 13703 3027 250 445 O ATOM 2065 OE2 GLU A1062 -1.053 6.893 -7.278 1.00142.60 O ANISOU 2065 OE2 GLU A1062 19357 19497 15327 3243 120 316 O ATOM 2066 N ALA A1063 3.733 4.532 -2.935 1.00117.09 N ANISOU 2066 N ALA A1063 16090 15408 12990 1941 203 301 N ATOM 2067 CA ALA A1063 5.151 4.367 -2.623 1.00115.46 C ANISOU 2067 CA ALA A1063 15944 15020 12908 1732 243 329 C ATOM 2068 C ALA A1063 5.475 2.935 -2.164 1.00117.24 C ANISOU 2068 C ALA A1063 15973 15295 13277 1541 191 256 C ATOM 2069 O ALA A1063 6.563 2.438 -2.473 1.00115.97 O ANISOU 2069 O ALA A1063 15802 15069 13194 1407 206 261 O ATOM 2070 CB ALA A1063 5.568 5.360 -1.551 1.00116.19 C ANISOU 2070 CB ALA A1063 16206 14922 13018 1688 300 386 C ATOM 2071 N GLU A1064 4.538 2.274 -1.440 1.00112.94 N ANISOU 2071 N GLU A1064 15284 14868 12759 1532 138 188 N ATOM 2072 CA GLU A1064 4.745 0.908 -0.954 1.00111.72 C ANISOU 2072 CA GLU A1064 14972 14751 12728 1361 103 119 C ATOM 2073 C GLU A1064 4.669 -0.104 -2.115 1.00113.72 C ANISOU 2073 C GLU A1064 15100 15136 12971 1349 75 60 C ATOM 2074 O GLU A1064 5.381 -1.108 -2.078 1.00112.92 O ANISOU 2074 O GLU A1064 14934 15001 12968 1203 72 31 O ATOM 2075 CB GLU A1064 3.796 0.536 0.208 1.00113.41 C ANISOU 2075 CB GLU A1064 15090 15032 12968 1339 72 65 C ATOM 2076 CG GLU A1064 2.315 0.411 -0.131 1.00129.92 C ANISOU 2076 CG GLU A1064 17065 17341 14958 1472 34 -3 C ATOM 2077 CD GLU A1064 1.388 -0.052 0.982 1.00154.10 C ANISOU 2077 CD GLU A1064 20019 20484 18049 1429 11 -68 C ATOM 2078 OE1 GLU A1064 0.213 -0.359 0.674 1.00153.38 O ANISOU 2078 OE1 GLU A1064 19797 20602 17881 1504 -20 -145 O ATOM 2079 OE2 GLU A1064 1.825 -0.107 2.156 1.00143.93 O ANISOU 2079 OE2 GLU A1064 18772 19064 16852 1319 26 -47 O ATOM 2080 N LYS A1065 3.867 0.191 -3.159 1.00109.31 N ANISOU 2080 N LYS A1065 14521 14726 12288 1510 59 43 N ATOM 2081 CA LYS A1065 3.748 -0.641 -4.362 1.00108.30 C ANISOU 2081 CA LYS A1065 14285 14735 12129 1514 35 -16 C ATOM 2082 C LYS A1065 5.067 -0.627 -5.165 1.00110.12 C ANISOU 2082 C LYS A1065 14603 14843 12393 1458 72 39 C ATOM 2083 O LYS A1065 5.479 -1.663 -5.691 1.00108.96 O ANISOU 2083 O LYS A1065 14370 14731 12299 1361 62 -8 O ATOM 2084 CB LYS A1065 2.580 -0.152 -5.228 1.00111.88 C ANISOU 2084 CB LYS A1065 14704 15387 12419 1724 7 -40 C ATOM 2085 N LEU A1066 5.727 0.552 -5.236 1.00106.19 N ANISOU 2085 N LEU A1066 14286 14200 11863 1513 123 136 N ATOM 2086 CA LEU A1066 7.015 0.783 -5.912 1.00105.24 C ANISOU 2086 CA LEU A1066 14268 13955 11765 1455 174 194 C ATOM 2087 C LEU A1066 8.141 0.048 -5.214 1.00105.87 C ANISOU 2087 C LEU A1066 14308 13926 11991 1252 183 186 C ATOM 2088 O LEU A1066 9.062 -0.426 -5.880 1.00104.65 O ANISOU 2088 O LEU A1066 14141 13747 11874 1179 201 189 O ATOM 2089 CB LEU A1066 7.363 2.289 -5.940 1.00106.03 C ANISOU 2089 CB LEU A1066 14587 13913 11788 1542 243 290 C ATOM 2090 CG LEU A1066 6.613 3.188 -6.914 1.00112.05 C ANISOU 2090 CG LEU A1066 15452 14742 12382 1770 259 327 C ATOM 2091 CD1 LEU A1066 6.616 4.609 -6.416 1.00112.99 C ANISOU 2091 CD1 LEU A1066 15788 14711 12431 1854 326 409 C ATOM 2092 CD2 LEU A1066 7.233 3.136 -8.303 1.00114.57 C ANISOU 2092 CD2 LEU A1066 15813 15067 12651 1795 288 350 C ATOM 2093 N PHE A1067 8.081 0.006 -3.863 1.00100.62 N ANISOU 2093 N PHE A1067 13629 13202 11399 1174 174 180 N ATOM 2094 CA PHE A1067 9.066 -0.621 -2.988 1.00 99.02 C ANISOU 2094 CA PHE A1067 13393 12908 11324 1003 178 175 C ATOM 2095 C PHE A1067 8.995 -2.151 -3.089 1.00100.48 C ANISOU 2095 C PHE A1067 13424 13178 11576 925 141 100 C ATOM 2096 O PHE A1067 10.045 -2.792 -3.164 1.00 99.33 O ANISOU 2096 O PHE A1067 13256 12983 11501 825 153 102 O ATOM 2097 CB PHE A1067 8.881 -0.133 -1.537 1.00100.79 C ANISOU 2097 CB PHE A1067 13657 13054 11583 968 179 191 C ATOM 2098 CG PHE A1067 9.797 -0.725 -0.486 1.00101.92 C ANISOU 2098 CG PHE A1067 13764 13119 11841 812 178 185 C ATOM 2099 CD1 PHE A1067 11.179 -0.643 -0.613 1.00105.23 C ANISOU 2099 CD1 PHE A1067 14222 13457 12303 717 212 217 C ATOM 2100 CD2 PHE A1067 9.276 -1.313 0.662 1.00103.82 C ANISOU 2100 CD2 PHE A1067 13935 13376 12137 768 146 148 C ATOM 2101 CE1 PHE A1067 12.018 -1.195 0.361 1.00105.59 C ANISOU 2101 CE1 PHE A1067 14223 13458 12440 595 205 208 C ATOM 2102 CE2 PHE A1067 10.118 -1.843 1.646 1.00105.65 C ANISOU 2102 CE2 PHE A1067 14142 13541 12460 646 144 147 C ATOM 2103 CZ PHE A1067 11.480 -1.786 1.486 1.00103.65 C ANISOU 2103 CZ PHE A1067 13917 13224 12242 568 170 177 C ATOM 2104 N ASN A1068 7.774 -2.732 -3.132 1.00 96.12 N ANISOU 2104 N ASN A1068 12771 12759 10993 970 102 31 N ATOM 2105 CA ASN A1068 7.594 -4.179 -3.279 1.00 95.11 C ANISOU 2105 CA ASN A1068 12517 12706 10913 888 81 -51 C ATOM 2106 C ASN A1068 8.179 -4.650 -4.620 1.00 99.03 C ANISOU 2106 C ASN A1068 12999 13236 11392 890 91 -60 C ATOM 2107 O ASN A1068 8.737 -5.746 -4.685 1.00 98.10 O ANISOU 2107 O ASN A1068 12832 13100 11340 794 97 -94 O ATOM 2108 CB ASN A1068 6.118 -4.587 -3.149 1.00 95.37 C ANISOU 2108 CB ASN A1068 12447 12892 10898 925 48 -135 C ATOM 2109 CG ASN A1068 5.525 -4.442 -1.761 1.00128.61 C ANISOU 2109 CG ASN A1068 16648 17079 15139 898 41 -143 C ATOM 2110 OD1 ASN A1068 4.467 -3.837 -1.572 1.00126.72 O ANISOU 2110 OD1 ASN A1068 16391 16931 14826 994 23 -158 O ATOM 2111 ND2 ASN A1068 6.151 -5.038 -0.758 1.00123.57 N ANISOU 2111 ND2 ASN A1068 16018 16332 14602 777 53 -137 N ATOM 2112 N GLN A1069 8.076 -3.808 -5.677 1.00 96.26 N ANISOU 2112 N GLN A1069 12704 12926 10944 1008 99 -25 N ATOM 2113 CA GLN A1069 8.606 -4.080 -7.024 1.00 96.04 C ANISOU 2113 CA GLN A1069 12676 12931 10882 1028 112 -26 C ATOM 2114 C GLN A1069 10.148 -4.002 -7.049 1.00 97.00 C ANISOU 2114 C GLN A1069 12868 12914 11073 943 155 36 C ATOM 2115 O GLN A1069 10.789 -4.780 -7.759 1.00 95.87 O ANISOU 2115 O GLN A1069 12688 12783 10956 897 165 15 O ATOM 2116 CB GLN A1069 8.013 -3.091 -8.051 1.00 98.83 C ANISOU 2116 CB GLN A1069 13089 13364 11098 1196 112 2 C ATOM 2117 CG GLN A1069 6.547 -3.327 -8.402 1.00120.86 C ANISOU 2117 CG GLN A1069 15775 16352 13794 1296 64 -76 C ATOM 2118 N ASP A1070 10.725 -3.042 -6.293 1.00 92.77 N ANISOU 2118 N ASP A1070 12431 12257 10559 922 184 105 N ATOM 2119 CA ASP A1070 12.161 -2.791 -6.172 1.00 92.42 C ANISOU 2119 CA ASP A1070 12446 12100 10568 831 229 156 C ATOM 2120 C ASP A1070 12.887 -3.942 -5.445 1.00 98.21 C ANISOU 2120 C ASP A1070 13093 12811 11413 709 217 124 C ATOM 2121 O ASP A1070 13.954 -4.358 -5.899 1.00 98.37 O ANISOU 2121 O ASP A1070 13097 12814 11464 656 240 131 O ATOM 2122 CB ASP A1070 12.404 -1.466 -5.432 1.00 93.89 C ANISOU 2122 CB ASP A1070 12759 12178 10739 829 265 219 C ATOM 2123 CG ASP A1070 12.368 -0.201 -6.269 1.00101.80 C ANISOU 2123 CG ASP A1070 13905 13140 11633 925 316 277 C ATOM 2124 OD1 ASP A1070 11.822 -0.241 -7.387 1.00102.49 O ANISOU 2124 OD1 ASP A1070 13990 13310 11639 1035 309 270 O ATOM 2125 OD2 ASP A1070 12.863 0.837 -5.789 1.00107.91 O ANISOU 2125 OD2 ASP A1070 14805 13801 12395 891 368 328 O ATOM 2126 N VAL A1071 12.314 -4.447 -4.324 1.00 95.55 N ANISOU 2126 N VAL A1071 12704 12476 11124 675 185 90 N ATOM 2127 CA VAL A1071 12.863 -5.564 -3.542 1.00 95.62 C ANISOU 2127 CA VAL A1071 12648 12459 11223 583 176 63 C ATOM 2128 C VAL A1071 12.756 -6.875 -4.375 1.00100.32 C ANISOU 2128 C VAL A1071 13172 13121 11825 577 172 3 C ATOM 2129 O VAL A1071 13.632 -7.737 -4.277 1.00100.59 O ANISOU 2129 O VAL A1071 13181 13127 11912 524 185 -4 O ATOM 2130 CB VAL A1071 12.204 -5.678 -2.132 1.00 99.76 C ANISOU 2130 CB VAL A1071 13160 12961 11786 555 153 46 C ATOM 2131 CG1 VAL A1071 10.744 -6.094 -2.213 1.00100.03 C ANISOU 2131 CG1 VAL A1071 13141 13084 11784 597 127 -16 C ATOM 2132 CG2 VAL A1071 12.980 -6.620 -1.216 1.00 99.14 C ANISOU 2132 CG2 VAL A1071 13048 12834 11788 473 154 39 C ATOM 2133 N ASP A1072 11.720 -6.975 -5.227 1.00 96.42 N ANISOU 2133 N ASP A1072 12649 12722 11265 639 156 -42 N ATOM 2134 CA ASP A1072 11.451 -8.101 -6.121 1.00 95.82 C ANISOU 2134 CA ASP A1072 12511 12720 11175 630 155 -112 C ATOM 2135 C ASP A1072 12.526 -8.169 -7.201 1.00 94.94 C ANISOU 2135 C ASP A1072 12421 12598 11056 639 182 -84 C ATOM 2136 O ASP A1072 13.061 -9.237 -7.466 1.00 93.41 O ANISOU 2136 O ASP A1072 12199 12395 10898 595 197 -115 O ATOM 2137 CB ASP A1072 10.055 -7.925 -6.747 1.00 99.43 C ANISOU 2137 CB ASP A1072 12926 13309 11544 701 128 -168 C ATOM 2138 CG ASP A1072 9.442 -9.139 -7.419 1.00120.39 C ANISOU 2138 CG ASP A1072 15501 16063 14178 667 124 -269 C ATOM 2139 OD1 ASP A1072 10.203 -10.038 -7.842 1.00122.33 O ANISOU 2139 OD1 ASP A1072 15748 16271 14462 614 150 -285 O ATOM 2140 OD2 ASP A1072 8.199 -9.173 -7.557 1.00131.84 O ANISOU 2140 OD2 ASP A1072 16890 17638 15567 695 100 -338 O ATOM 2141 N ALA A1073 12.852 -7.020 -7.798 1.00 90.28 N ANISOU 2141 N ALA A1073 11892 11998 10413 698 196 -24 N ATOM 2142 CA ALA A1073 13.883 -6.886 -8.821 1.00 89.47 C ANISOU 2142 CA ALA A1073 11819 11882 10293 704 230 10 C ATOM 2143 C ALA A1073 15.267 -7.229 -8.233 1.00 91.46 C ANISOU 2143 C ALA A1073 12067 12058 10626 620 256 39 C ATOM 2144 O ALA A1073 16.087 -7.837 -8.931 1.00 91.30 O ANISOU 2144 O ALA A1073 12025 12049 10616 606 279 33 O ATOM 2145 CB ALA A1073 13.876 -5.470 -9.382 1.00 90.42 C ANISOU 2145 CB ALA A1073 12033 11989 10334 777 253 73 C ATOM 2146 N ALA A1074 15.491 -6.884 -6.933 1.00 85.37 N ANISOU 2146 N ALA A1074 11308 11223 9905 572 251 65 N ATOM 2147 CA ALA A1074 16.737 -7.133 -6.206 1.00 84.36 C ANISOU 2147 CA ALA A1074 11164 11049 9841 502 267 88 C ATOM 2148 C ALA A1074 16.977 -8.620 -5.997 1.00 88.98 C ANISOU 2148 C ALA A1074 11687 11646 10476 484 259 44 C ATOM 2149 O ALA A1074 18.072 -9.086 -6.303 1.00 88.58 O ANISOU 2149 O ALA A1074 11613 11602 10442 471 282 52 O ATOM 2150 CB ALA A1074 16.723 -6.421 -4.860 1.00 84.55 C ANISOU 2150 CB ALA A1074 11216 11017 9893 463 257 115 C ATOM 2151 N VAL A1075 15.957 -9.366 -5.483 1.00 86.11 N ANISOU 2151 N VAL A1075 11305 11285 10127 484 235 -4 N ATOM 2152 CA VAL A1075 16.056 -10.802 -5.198 1.00 86.01 C ANISOU 2152 CA VAL A1075 11268 11260 10152 465 243 -48 C ATOM 2153 C VAL A1075 16.160 -11.603 -6.523 1.00 89.10 C ANISOU 2153 C VAL A1075 11646 11694 10515 486 265 -88 C ATOM 2154 O VAL A1075 16.937 -12.558 -6.580 1.00 88.57 O ANISOU 2154 O VAL A1075 11576 11605 10470 485 290 -96 O ATOM 2155 CB VAL A1075 14.946 -11.331 -4.234 1.00 90.06 C ANISOU 2155 CB VAL A1075 11780 11755 10684 438 228 -92 C ATOM 2156 CG1 VAL A1075 13.545 -11.207 -4.816 1.00 90.64 C ANISOU 2156 CG1 VAL A1075 11835 11897 10707 451 213 -148 C ATOM 2157 CG2 VAL A1075 15.220 -12.760 -3.800 1.00 89.83 C ANISOU 2157 CG2 VAL A1075 11760 11681 10690 415 254 -125 C ATOM 2158 N ARG A1076 15.458 -11.163 -7.589 1.00 85.56 N ANISOU 2158 N ARG A1076 11195 11308 10006 518 257 -108 N ATOM 2159 CA ARG A1076 15.503 -11.798 -8.912 1.00 85.32 C ANISOU 2159 CA ARG A1076 11152 11328 9937 540 275 -149 C ATOM 2160 C ARG A1076 16.871 -11.592 -9.590 1.00 87.92 C ANISOU 2160 C ARG A1076 11490 11649 10266 558 305 -99 C ATOM 2161 O ARG A1076 17.328 -12.470 -10.322 1.00 88.01 O ANISOU 2161 O ARG A1076 11495 11674 10273 566 330 -127 O ATOM 2162 CB ARG A1076 14.384 -11.259 -9.810 1.00 86.78 C ANISOU 2162 CB ARG A1076 11327 11603 10044 583 253 -182 C ATOM 2163 CG ARG A1076 12.991 -11.825 -9.507 1.00 99.55 C ANISOU 2163 CG ARG A1076 12906 13274 11643 558 232 -266 C ATOM 2164 CD ARG A1076 11.882 -11.173 -10.331 1.00112.73 C ANISOU 2164 CD ARG A1076 14547 15066 13220 622 202 -298 C ATOM 2165 NE ARG A1076 12.099 -11.308 -11.774 1.00128.33 N ANISOU 2165 NE ARG A1076 16518 17107 15133 665 211 -316 N ATOM 2166 CZ ARG A1076 12.503 -10.322 -12.572 1.00141.93 C ANISOU 2166 CZ ARG A1076 18279 18845 16802 744 214 -252 C ATOM 2167 NH1 ARG A1076 12.708 -9.104 -12.084 1.00126.77 N ANISOU 2167 NH1 ARG A1076 16412 16874 14880 784 212 -171 N ATOM 2168 NH2 ARG A1076 12.697 -10.546 -13.865 1.00126.58 N ANISOU 2168 NH2 ARG A1076 16332 16961 14800 781 225 -272 N ATOM 2169 N GLY A1077 17.494 -10.441 -9.332 1.00 83.32 N ANISOU 2169 N GLY A1077 10927 11047 9685 557 308 -32 N ATOM 2170 CA GLY A1077 18.808 -10.085 -9.849 1.00 83.12 C ANISOU 2170 CA GLY A1077 10903 11023 9656 553 343 12 C ATOM 2171 C GLY A1077 19.909 -10.938 -9.259 1.00 88.12 C ANISOU 2171 C GLY A1077 11498 11642 10341 532 358 14 C ATOM 2172 O GLY A1077 20.880 -11.252 -9.950 1.00 88.04 O ANISOU 2172 O GLY A1077 11467 11661 10322 545 388 20 O ATOM 2173 N ILE A1078 19.739 -11.351 -7.983 1.00 85.82 N ANISOU 2173 N ILE A1078 11200 11313 10097 513 337 8 N ATOM 2174 CA ILE A1078 20.672 -12.191 -7.226 1.00 86.44 C ANISOU 2174 CA ILE A1078 11251 11379 10214 518 346 12 C ATOM 2175 C ILE A1078 20.728 -13.617 -7.827 1.00 93.04 C ANISOU 2175 C ILE A1078 12095 12212 11044 559 371 -31 C ATOM 2176 O ILE A1078 21.815 -14.036 -8.249 1.00 92.85 O ANISOU 2176 O ILE A1078 12048 12220 11013 593 398 -20 O ATOM 2177 CB ILE A1078 20.323 -12.214 -5.698 1.00 88.67 C ANISOU 2177 CB ILE A1078 11540 11616 10535 496 318 19 C ATOM 2178 CG1 ILE A1078 20.677 -10.874 -5.027 1.00 88.73 C ANISOU 2178 CG1 ILE A1078 11539 11627 10546 451 304 63 C ATOM 2179 CG2 ILE A1078 21.023 -13.372 -4.967 1.00 88.57 C ANISOU 2179 CG2 ILE A1078 11520 11588 10545 530 329 15 C ATOM 2180 CD1 ILE A1078 19.856 -10.543 -3.791 1.00 95.00 C ANISOU 2180 CD1 ILE A1078 12357 12375 11364 427 273 65 C ATOM 2181 N LEU A1079 19.573 -14.350 -7.870 1.00 90.58 N ANISOU 2181 N LEU A1079 11819 11869 10729 552 369 -85 N ATOM 2182 CA LEU A1079 19.529 -15.739 -8.367 1.00 91.22 C ANISOU 2182 CA LEU A1079 11933 11927 10800 574 405 -137 C ATOM 2183 C LEU A1079 19.758 -15.836 -9.894 1.00 95.54 C ANISOU 2183 C LEU A1079 12472 12525 11303 597 427 -157 C ATOM 2184 O LEU A1079 20.034 -16.927 -10.400 1.00 96.05 O ANISOU 2184 O LEU A1079 12566 12572 11355 623 465 -191 O ATOM 2185 CB LEU A1079 18.264 -16.519 -7.945 1.00 91.42 C ANISOU 2185 CB LEU A1079 12002 11904 10828 532 411 -202 C ATOM 2186 CG LEU A1079 17.005 -15.736 -7.611 1.00 96.08 C ANISOU 2186 CG LEU A1079 12574 12519 11414 485 372 -221 C ATOM 2187 CD1 LEU A1079 16.038 -15.752 -8.778 1.00 97.64 C ANISOU 2187 CD1 LEU A1079 12755 12785 11558 470 369 -286 C ATOM 2188 CD2 LEU A1079 16.338 -16.284 -6.372 1.00 95.98 C ANISOU 2188 CD2 LEU A1079 12594 12442 11430 444 377 -246 C ATOM 2189 N ARG A1080 19.731 -14.696 -10.602 1.00 91.72 N ANISOU 2189 N ARG A1080 11961 12098 10792 595 410 -130 N ATOM 2190 CA ARG A1080 20.014 -14.613 -12.040 1.00 91.80 C ANISOU 2190 CA ARG A1080 11967 12161 10754 623 430 -138 C ATOM 2191 C ARG A1080 21.540 -14.389 -12.269 1.00 94.85 C ANISOU 2191 C ARG A1080 12323 12570 11145 647 459 -86 C ATOM 2192 O ARG A1080 22.036 -14.657 -13.365 1.00 95.68 O ANISOU 2192 O ARG A1080 12426 12712 11217 677 489 -95 O ATOM 2193 CB ARG A1080 19.167 -13.490 -12.671 1.00 92.15 C ANISOU 2193 CB ARG A1080 12013 12251 10751 622 405 -133 C ATOM 2194 CG ARG A1080 19.117 -13.467 -14.196 1.00 98.69 C ANISOU 2194 CG ARG A1080 12846 13139 11513 657 421 -154 C ATOM 2195 CD ARG A1080 18.113 -12.473 -14.800 1.00106.22 C ANISOU 2195 CD ARG A1080 13812 14147 12400 684 393 -154 C ATOM 2196 NE ARG A1080 17.723 -11.332 -13.953 1.00107.09 N ANISOU 2196 NE ARG A1080 13937 14234 12517 679 368 -107 N ATOM 2197 CZ ARG A1080 18.394 -10.186 -13.853 1.00115.28 C ANISOU 2197 CZ ARG A1080 15007 15244 13550 679 386 -34 C ATOM 2198 NH1 ARG A1080 17.934 -9.207 -13.085 1.00 95.79 N ANISOU 2198 NH1 ARG A1080 12568 12746 11081 676 368 1 N ATOM 2199 NH2 ARG A1080 19.538 -10.017 -14.505 1.00103.91 N ANISOU 2199 NH2 ARG A1080 13574 13805 12101 676 430 0 N ATOM 2200 N ASN A1081 22.272 -13.916 -11.231 1.00 89.01 N ANISOU 2200 N ASN A1081 11555 11823 10441 631 451 -40 N ATOM 2201 CA ASN A1081 23.714 -13.677 -11.270 1.00 87.98 C ANISOU 2201 CA ASN A1081 11375 11743 10310 641 477 -3 C ATOM 2202 C ASN A1081 24.480 -14.929 -10.810 1.00 92.11 C ANISOU 2202 C ASN A1081 11882 12267 10849 700 494 -14 C ATOM 2203 O ASN A1081 24.202 -15.473 -9.737 1.00 92.24 O ANISOU 2203 O ASN A1081 11918 12236 10894 712 477 -19 O ATOM 2204 CB ASN A1081 24.075 -12.480 -10.393 1.00 84.38 C ANISOU 2204 CB ASN A1081 10894 11296 9872 583 462 40 C ATOM 2205 CG ASN A1081 25.430 -11.895 -10.684 1.00 88.36 C ANISOU 2205 CG ASN A1081 11340 11875 10358 559 496 67 C ATOM 2206 OD1 ASN A1081 26.476 -12.494 -10.436 1.00 77.05 O ANISOU 2206 OD1 ASN A1081 9845 10500 8929 590 510 65 O ATOM 2207 ND2 ASN A1081 25.442 -10.704 -11.225 1.00 79.61 N ANISOU 2207 ND2 ASN A1081 10256 10771 9221 504 518 90 N ATOM 2208 N ALA A1082 25.456 -15.368 -11.611 1.00 88.47 N ANISOU 2208 N ALA A1082 11392 11861 10361 748 531 -14 N ATOM 2209 CA ALA A1082 26.275 -16.548 -11.321 1.00 88.80 C ANISOU 2209 CA ALA A1082 11425 11915 10399 835 556 -20 C ATOM 2210 C ALA A1082 27.227 -16.363 -10.114 1.00 92.81 C ANISOU 2210 C ALA A1082 11864 12478 10920 855 540 13 C ATOM 2211 O ALA A1082 27.618 -17.359 -9.502 1.00 93.68 O ANISOU 2211 O ALA A1082 11989 12580 11025 943 548 12 O ATOM 2212 CB ALA A1082 27.084 -16.927 -12.547 1.00 90.23 C ANISOU 2212 CB ALA A1082 11586 12158 10541 886 600 -29 C ATOM 2213 N LYS A1083 27.609 -15.116 -9.783 1.00 87.95 N ANISOU 2213 N LYS A1083 11182 11922 10311 779 522 39 N ATOM 2214 CA LYS A1083 28.513 -14.818 -8.666 1.00 87.33 C ANISOU 2214 CA LYS A1083 11023 11922 10236 778 504 58 C ATOM 2215 C LYS A1083 27.764 -14.625 -7.330 1.00 89.55 C ANISOU 2215 C LYS A1083 11339 12134 10553 748 460 66 C ATOM 2216 O LYS A1083 28.323 -14.962 -6.283 1.00 90.69 O ANISOU 2216 O LYS A1083 11444 12319 10695 795 442 75 O ATOM 2217 CB LYS A1083 29.367 -13.570 -8.956 1.00 89.91 C ANISOU 2217 CB LYS A1083 11264 12352 10545 687 520 69 C ATOM 2218 CG LYS A1083 30.358 -13.734 -10.094 1.00102.83 C ANISOU 2218 CG LYS A1083 12842 14087 12140 715 568 60 C ATOM 2219 N LEU A1084 26.523 -14.085 -7.358 1.00 82.88 N ANISOU 2219 N LEU A1084 10563 11196 9733 680 442 63 N ATOM 2220 CA LEU A1084 25.725 -13.811 -6.151 1.00 81.04 C ANISOU 2220 CA LEU A1084 10364 10897 9531 645 403 69 C ATOM 2221 C LEU A1084 24.894 -15.034 -5.678 1.00 85.23 C ANISOU 2221 C LEU A1084 10972 11334 10076 703 401 49 C ATOM 2222 O LEU A1084 24.818 -15.277 -4.472 1.00 84.53 O ANISOU 2222 O LEU A1084 10895 11219 10003 719 381 58 O ATOM 2223 CB LEU A1084 24.783 -12.589 -6.352 1.00 79.62 C ANISOU 2223 CB LEU A1084 10221 10671 9359 555 389 76 C ATOM 2224 CG LEU A1084 25.388 -11.274 -6.884 1.00 82.59 C ANISOU 2224 CG LEU A1084 10567 11101 9713 482 410 96 C ATOM 2225 CD1 LEU A1084 24.310 -10.291 -7.231 1.00 81.62 C ANISOU 2225 CD1 LEU A1084 10516 10914 9582 436 405 104 C ATOM 2226 CD2 LEU A1084 26.330 -10.644 -5.887 1.00 83.60 C ANISOU 2226 CD2 LEU A1084 10629 11292 9843 429 404 108 C ATOM 2227 N LYS A1085 24.249 -15.772 -6.615 1.00 81.91 N ANISOU 2227 N LYS A1085 10611 10864 9646 723 427 16 N ATOM 2228 CA LYS A1085 23.397 -16.936 -6.324 1.00 81.62 C ANISOU 2228 CA LYS A1085 10663 10733 9615 749 443 -18 C ATOM 2229 C LYS A1085 24.062 -17.930 -5.335 1.00 83.96 C ANISOU 2229 C LYS A1085 10988 11006 9905 839 460 -3 C ATOM 2230 O LYS A1085 23.379 -18.268 -4.360 1.00 83.13 O ANISOU 2230 O LYS A1085 10943 10825 9817 827 455 -8 O ATOM 2231 CB LYS A1085 22.978 -17.663 -7.619 1.00 85.24 C ANISOU 2231 CB LYS A1085 11169 11169 10049 759 481 -65 C ATOM 2232 CG LYS A1085 22.010 -18.837 -7.425 1.00 97.01 C ANISOU 2232 CG LYS A1085 12763 12560 11538 753 513 -118 C ATOM 2233 CD LYS A1085 21.579 -19.397 -8.770 1.00104.36 C ANISOU 2233 CD LYS A1085 13728 13486 12437 741 548 -175 C ATOM 2234 CE LYS A1085 20.647 -20.567 -8.646 1.00108.73 C ANISOU 2234 CE LYS A1085 14387 13944 12980 709 594 -242 C ATOM 2235 NZ LYS A1085 21.409 -21.826 -8.473 1.00119.97 N ANISOU 2235 NZ LYS A1085 15902 15299 14385 796 658 -239 N ATOM 2236 N PRO A1086 25.343 -18.405 -5.532 1.00 79.57 N ANISOU 2236 N PRO A1086 10395 10520 9318 936 482 17 N ATOM 2237 CA PRO A1086 25.932 -19.364 -4.569 1.00 79.17 C ANISOU 2237 CA PRO A1086 10383 10452 9244 1051 498 35 C ATOM 2238 C PRO A1086 26.218 -18.770 -3.185 1.00 82.12 C ANISOU 2238 C PRO A1086 10704 10870 9629 1048 451 69 C ATOM 2239 O PRO A1086 26.192 -19.514 -2.201 1.00 81.64 O ANISOU 2239 O PRO A1086 10711 10756 9553 1123 460 82 O ATOM 2240 CB PRO A1086 27.245 -19.795 -5.241 1.00 81.49 C ANISOU 2240 CB PRO A1086 10624 10847 9492 1161 526 46 C ATOM 2241 CG PRO A1086 27.165 -19.327 -6.647 1.00 85.53 C ANISOU 2241 CG PRO A1086 11100 11390 10006 1096 538 24 C ATOM 2242 CD PRO A1086 26.295 -18.129 -6.631 1.00 80.74 C ANISOU 2242 CD PRO A1086 10468 10769 9440 958 497 21 C ATOM 2243 N VAL A1087 26.497 -17.448 -3.098 1.00 78.43 N ANISOU 2243 N VAL A1087 10130 10492 9179 961 408 81 N ATOM 2244 CA VAL A1087 26.761 -16.809 -1.811 1.00 78.40 C ANISOU 2244 CA VAL A1087 10073 10535 9181 941 364 104 C ATOM 2245 C VAL A1087 25.422 -16.656 -1.045 1.00 80.80 C ANISOU 2245 C VAL A1087 10462 10715 9524 872 347 99 C ATOM 2246 O VAL A1087 25.407 -16.826 0.171 1.00 78.80 O ANISOU 2246 O VAL A1087 10227 10445 9268 903 328 115 O ATOM 2247 CB VAL A1087 27.595 -15.493 -1.910 1.00 82.91 C ANISOU 2247 CB VAL A1087 10513 11241 9747 860 339 110 C ATOM 2248 CG1 VAL A1087 26.807 -14.337 -2.500 1.00 82.42 C ANISOU 2248 CG1 VAL A1087 10464 11132 9717 725 334 103 C ATOM 2249 CG2 VAL A1087 28.184 -15.100 -0.561 1.00 83.04 C ANISOU 2249 CG2 VAL A1087 10463 11340 9750 864 300 123 C ATOM 2250 N TYR A1088 24.298 -16.440 -1.784 1.00 78.06 N ANISOU 2250 N TYR A1088 10166 10290 9203 793 356 73 N ATOM 2251 CA TYR A1088 22.922 -16.293 -1.274 1.00 77.44 C ANISOU 2251 CA TYR A1088 10154 10114 9155 724 345 57 C ATOM 2252 C TYR A1088 22.415 -17.614 -0.659 1.00 81.96 C ANISOU 2252 C TYR A1088 10835 10584 9722 777 380 41 C ATOM 2253 O TYR A1088 21.809 -17.607 0.427 1.00 80.26 O ANISOU 2253 O TYR A1088 10661 10313 9521 754 369 45 O ATOM 2254 CB TYR A1088 22.009 -15.842 -2.435 1.00 78.51 C ANISOU 2254 CB TYR A1088 10299 10233 9298 653 349 26 C ATOM 2255 CG TYR A1088 20.605 -15.398 -2.068 1.00 80.82 C ANISOU 2255 CG TYR A1088 10627 10471 9612 580 330 4 C ATOM 2256 CD1 TYR A1088 20.388 -14.218 -1.356 1.00 82.54 C ANISOU 2256 CD1 TYR A1088 10814 10702 9844 530 291 29 C ATOM 2257 CD2 TYR A1088 19.489 -16.084 -2.542 1.00 81.81 C ANISOU 2257 CD2 TYR A1088 10808 10544 9732 555 354 -49 C ATOM 2258 CE1 TYR A1088 19.098 -13.766 -1.077 1.00 83.39 C ANISOU 2258 CE1 TYR A1088 10949 10773 9962 478 274 9 C ATOM 2259 CE2 TYR A1088 18.194 -15.643 -2.267 1.00 82.26 C ANISOU 2259 CE2 TYR A1088 10875 10581 9798 491 336 -77 C ATOM 2260 CZ TYR A1088 18.002 -14.478 -1.542 1.00 91.15 C ANISOU 2260 CZ TYR A1088 11971 11723 10938 463 294 -44 C ATOM 2261 OH TYR A1088 16.725 -14.054 -1.249 1.00 93.63 O ANISOU 2261 OH TYR A1088 12294 12029 11254 417 277 -71 O ATOM 2262 N ASP A1089 22.697 -18.747 -1.360 1.00 80.09 N ANISOU 2262 N ASP A1089 10656 10316 9457 846 433 23 N ATOM 2263 CA ASP A1089 22.338 -20.114 -0.981 1.00 80.37 C ANISOU 2263 CA ASP A1089 10826 10238 9473 900 492 5 C ATOM 2264 C ASP A1089 23.045 -20.576 0.299 1.00 85.03 C ANISOU 2264 C ASP A1089 11450 10820 10037 1008 493 50 C ATOM 2265 O ASP A1089 22.477 -21.405 1.012 1.00 85.72 O ANISOU 2265 O ASP A1089 11663 10794 10114 1024 536 43 O ATOM 2266 CB ASP A1089 22.651 -21.099 -2.121 1.00 82.85 C ANISOU 2266 CB ASP A1089 11198 10528 9755 955 552 -22 C ATOM 2267 CG ASP A1089 21.678 -21.096 -3.294 1.00 96.45 C ANISOU 2267 CG ASP A1089 12935 12224 11486 855 571 -84 C ATOM 2268 OD1 ASP A1089 20.539 -20.580 -3.130 1.00 98.13 O ANISOU 2268 OD1 ASP A1089 13140 12418 11726 747 548 -115 O ATOM 2269 OD2 ASP A1089 22.030 -21.664 -4.363 1.00100.13 O ANISOU 2269 OD2 ASP A1089 13424 12696 11926 891 610 -107 O ATOM 2270 N SER A1090 24.260 -20.056 0.598 1.00 80.76 N ANISOU 2270 N SER A1090 10801 10408 9477 1079 451 92 N ATOM 2271 CA SER A1090 25.031 -20.443 1.794 1.00 80.59 C ANISOU 2271 CA SER A1090 10789 10418 9414 1202 443 132 C ATOM 2272 C SER A1090 24.713 -19.564 3.038 1.00 83.92 C ANISOU 2272 C SER A1090 11167 10859 9860 1138 386 150 C ATOM 2273 O SER A1090 25.268 -19.814 4.113 1.00 84.57 O ANISOU 2273 O SER A1090 11255 10975 9904 1234 372 181 O ATOM 2274 CB SER A1090 26.530 -20.416 1.494 1.00 83.83 C ANISOU 2274 CB SER A1090 11089 10987 9775 1317 428 155 C ATOM 2275 OG SER A1090 27.026 -19.099 1.328 1.00 91.71 O ANISOU 2275 OG SER A1090 11925 12125 10794 1229 371 155 O ATOM 2276 N LEU A1091 23.800 -18.574 2.899 1.00 78.89 N ANISOU 2276 N LEU A1091 10497 10200 9278 989 356 129 N ATOM 2277 CA LEU A1091 23.427 -17.641 3.971 1.00 77.46 C ANISOU 2277 CA LEU A1091 10280 10030 9121 918 306 142 C ATOM 2278 C LEU A1091 22.054 -17.940 4.581 1.00 81.50 C ANISOU 2278 C LEU A1091 10902 10407 9659 859 327 124 C ATOM 2279 O LEU A1091 21.148 -18.425 3.902 1.00 81.06 O ANISOU 2279 O LEU A1091 10914 10267 9617 810 368 87 O ATOM 2280 CB LEU A1091 23.435 -16.176 3.464 1.00 76.31 C ANISOU 2280 CB LEU A1091 10026 9963 9006 803 263 135 C ATOM 2281 CG LEU A1091 24.776 -15.534 3.052 1.00 79.93 C ANISOU 2281 CG LEU A1091 10358 10572 9440 814 242 145 C ATOM 2282 CD1 LEU A1091 24.561 -14.141 2.460 1.00 78.06 C ANISOU 2282 CD1 LEU A1091 10065 10366 9231 685 223 136 C ATOM 2283 CD2 LEU A1091 25.771 -15.490 4.201 1.00 82.32 C ANISOU 2283 CD2 LEU A1091 10596 10978 9703 879 210 166 C ATOM 2284 N ASP A1092 21.915 -17.607 5.869 1.00 78.17 N ANISOU 2284 N ASP A1092 10485 9978 9237 855 298 145 N ATOM 2285 CA ASP A1092 20.697 -17.717 6.660 1.00 77.73 C ANISOU 2285 CA ASP A1092 10516 9816 9203 794 312 132 C ATOM 2286 C ASP A1092 19.776 -16.544 6.334 1.00 83.48 C ANISOU 2286 C ASP A1092 11188 10554 9976 663 278 108 C ATOM 2287 O ASP A1092 20.247 -15.526 5.819 1.00 84.19 O ANISOU 2287 O ASP A1092 11183 10731 10076 630 239 115 O ATOM 2288 CB ASP A1092 21.044 -17.750 8.151 1.00 79.54 C ANISOU 2288 CB ASP A1092 10765 10050 9406 854 291 168 C ATOM 2289 CG ASP A1092 21.872 -16.573 8.621 1.00 89.15 C ANISOU 2289 CG ASP A1092 11854 11400 10619 842 219 189 C ATOM 2290 OD1 ASP A1092 21.287 -15.512 8.883 1.00 90.50 O ANISOU 2290 OD1 ASP A1092 11988 11573 10825 738 186 180 O ATOM 2291 OD2 ASP A1092 23.107 -16.722 8.730 1.00 92.71 O ANISOU 2291 OD2 ASP A1092 12243 11958 11026 937 202 210 O ATOM 2292 N ALA A1093 18.476 -16.671 6.663 1.00 80.05 N ANISOU 2292 N ALA A1093 10817 10037 9561 594 299 78 N ATOM 2293 CA ALA A1093 17.403 -15.705 6.388 1.00 78.88 C ANISOU 2293 CA ALA A1093 10631 9898 9443 493 274 50 C ATOM 2294 C ALA A1093 17.785 -14.229 6.630 1.00 82.98 C ANISOU 2294 C ALA A1093 11066 10491 9972 465 213 80 C ATOM 2295 O ALA A1093 17.431 -13.387 5.803 1.00 83.11 O ANISOU 2295 O ALA A1093 11040 10541 9997 419 198 68 O ATOM 2296 CB ALA A1093 16.174 -16.049 7.215 1.00 79.34 C ANISOU 2296 CB ALA A1093 10759 9878 9508 443 300 22 C ATOM 2297 N VAL A1094 18.472 -13.916 7.760 1.00 78.97 N ANISOU 2297 N VAL A1094 10543 10007 9456 492 185 115 N ATOM 2298 CA VAL A1094 18.823 -12.540 8.129 1.00 78.03 C ANISOU 2298 CA VAL A1094 10362 9947 9340 447 139 133 C ATOM 2299 C VAL A1094 20.069 -12.085 7.328 1.00 81.62 C ANISOU 2299 C VAL A1094 10736 10496 9779 454 128 144 C ATOM 2300 O VAL A1094 20.071 -10.952 6.836 1.00 82.26 O ANISOU 2300 O VAL A1094 10785 10604 9865 390 116 144 O ATOM 2301 CB VAL A1094 18.929 -12.324 9.672 1.00 82.06 C ANISOU 2301 CB VAL A1094 10886 10451 9841 453 113 153 C ATOM 2302 CG1 VAL A1094 19.621 -13.475 10.360 1.00 83.23 C ANISOU 2302 CG1 VAL A1094 11064 10600 9958 551 126 171 C ATOM 2303 CG2 VAL A1094 19.553 -10.984 10.064 1.00 81.63 C ANISOU 2303 CG2 VAL A1094 10769 10467 9780 401 73 165 C ATOM 2304 N ARG A1095 21.070 -12.956 7.119 1.00 76.41 N ANISOU 2304 N ARG A1095 10055 9883 9096 534 140 152 N ATOM 2305 CA ARG A1095 22.236 -12.574 6.309 1.00 75.37 C ANISOU 2305 CA ARG A1095 9837 9856 8946 537 136 155 C ATOM 2306 C ARG A1095 21.833 -12.425 4.814 1.00 78.41 C ANISOU 2306 C ARG A1095 10226 10221 9345 502 161 139 C ATOM 2307 O ARG A1095 22.453 -11.635 4.090 1.00 77.16 O ANISOU 2307 O ARG A1095 10011 10129 9179 461 161 140 O ATOM 2308 CB ARG A1095 23.399 -13.548 6.498 1.00 73.21 C ANISOU 2308 CB ARG A1095 9530 9654 8631 650 142 167 C ATOM 2309 CG ARG A1095 24.011 -13.447 7.887 1.00 77.73 C ANISOU 2309 CG ARG A1095 10070 10293 9172 688 107 182 C ATOM 2310 CD ARG A1095 25.265 -14.276 7.973 1.00 80.61 C ANISOU 2310 CD ARG A1095 10382 10766 9478 819 108 193 C ATOM 2311 NE ARG A1095 26.062 -13.993 9.166 1.00 74.39 N ANISOU 2311 NE ARG A1095 9525 10097 8644 854 65 199 N ATOM 2312 CZ ARG A1095 26.091 -14.749 10.262 1.00 83.25 C ANISOU 2312 CZ ARG A1095 10700 11206 9726 966 58 221 C ATOM 2313 NH1 ARG A1095 25.350 -15.846 10.342 1.00 66.86 N ANISOU 2313 NH1 ARG A1095 8764 8986 7655 1043 101 239 N ATOM 2314 NH2 ARG A1095 26.866 -14.415 11.285 1.00 72.24 N ANISOU 2314 NH2 ARG A1095 9225 9945 8279 998 13 220 N ATOM 2315 N ARG A1096 20.746 -13.133 4.386 1.00 75.11 N ANISOU 2315 N ARG A1096 9880 9717 8943 510 187 118 N ATOM 2316 CA ARG A1096 20.156 -13.030 3.042 1.00 74.48 C ANISOU 2316 CA ARG A1096 9807 9625 8868 481 206 94 C ATOM 2317 C ARG A1096 19.558 -11.625 2.873 1.00 77.30 C ANISOU 2317 C ARG A1096 10153 9987 9232 408 185 98 C ATOM 2318 O ARG A1096 19.711 -11.030 1.804 1.00 77.14 O ANISOU 2318 O ARG A1096 10113 9999 9199 390 193 98 O ATOM 2319 CB ARG A1096 19.099 -14.118 2.789 1.00 74.16 C ANISOU 2319 CB ARG A1096 9837 9508 8832 491 239 57 C ATOM 2320 CG ARG A1096 19.678 -15.489 2.446 1.00 86.82 C ANISOU 2320 CG ARG A1096 11479 11092 10418 564 282 49 C ATOM 2321 CD ARG A1096 18.696 -16.402 1.712 1.00 98.48 C ANISOU 2321 CD ARG A1096 13022 12505 11891 543 327 -4 C ATOM 2322 NE ARG A1096 17.537 -16.774 2.530 1.00107.35 N ANISOU 2322 NE ARG A1096 14210 13553 13025 495 344 -34 N ATOM 2323 CZ ARG A1096 17.453 -17.873 3.274 1.00118.75 C ANISOU 2323 CZ ARG A1096 15748 14913 14458 523 391 -39 C ATOM 2324 NH1 ARG A1096 18.456 -18.744 3.299 1.00106.13 N ANISOU 2324 NH1 ARG A1096 14196 13294 12834 618 423 -15 N ATOM 2325 NH2 ARG A1096 16.364 -18.114 3.994 1.00103.00 N ANISOU 2325 NH2 ARG A1096 13809 12855 12470 462 412 -70 N ATOM 2326 N ALA A1097 18.934 -11.079 3.952 1.00 72.79 N ANISOU 2326 N ALA A1097 9605 9380 8671 376 163 104 N ATOM 2327 CA ALA A1097 18.384 -9.713 4.010 1.00 71.99 C ANISOU 2327 CA ALA A1097 9514 9271 8566 322 148 112 C ATOM 2328 C ALA A1097 19.502 -8.668 3.815 1.00 74.31 C ANISOU 2328 C ALA A1097 9774 9616 8844 283 148 136 C ATOM 2329 O ALA A1097 19.329 -7.751 3.020 1.00 73.79 O ANISOU 2329 O ALA A1097 9727 9549 8760 255 161 142 O ATOM 2330 CB ALA A1097 17.671 -9.480 5.338 1.00 72.54 C ANISOU 2330 CB ALA A1097 9617 9297 8648 305 128 115 C ATOM 2331 N ALA A1098 20.662 -8.851 4.493 1.00 70.38 N ANISOU 2331 N ALA A1098 9228 9173 8343 283 139 144 N ATOM 2332 CA ALA A1098 21.840 -7.980 4.406 1.00 70.02 C ANISOU 2332 CA ALA A1098 9131 9200 8275 226 145 150 C ATOM 2333 C ALA A1098 22.404 -7.906 2.962 1.00 74.30 C ANISOU 2333 C ALA A1098 9647 9784 8801 222 178 148 C ATOM 2334 O ALA A1098 22.782 -6.822 2.516 1.00 74.21 O ANISOU 2334 O ALA A1098 9642 9787 8769 150 203 152 O ATOM 2335 CB ALA A1098 22.919 -8.449 5.377 1.00 70.77 C ANISOU 2335 CB ALA A1098 9156 9378 8357 247 124 148 C ATOM 2336 N LEU A1099 22.419 -9.039 2.232 1.00 71.04 N ANISOU 2336 N LEU A1099 9221 9380 8392 296 187 141 N ATOM 2337 CA LEU A1099 22.894 -9.107 0.847 1.00 70.90 C ANISOU 2337 CA LEU A1099 9180 9401 8357 304 218 137 C ATOM 2338 C LEU A1099 21.887 -8.421 -0.130 1.00 78.18 C ANISOU 2338 C LEU A1099 10170 10265 9272 284 234 139 C ATOM 2339 O LEU A1099 22.333 -7.732 -1.050 1.00 78.79 O ANISOU 2339 O LEU A1099 10248 10366 9323 251 265 147 O ATOM 2340 CB LEU A1099 23.161 -10.572 0.431 1.00 70.26 C ANISOU 2340 CB LEU A1099 9081 9339 8278 396 227 126 C ATOM 2341 CG LEU A1099 23.792 -10.784 -0.964 1.00 73.15 C ANISOU 2341 CG LEU A1099 9416 9755 8623 416 260 121 C ATOM 2342 CD1 LEU A1099 25.247 -10.312 -0.988 1.00 73.76 C ANISOU 2342 CD1 LEU A1099 9404 9948 8674 385 272 125 C ATOM 2343 CD2 LEU A1099 23.635 -12.227 -1.434 1.00 68.79 C ANISOU 2343 CD2 LEU A1099 8885 9180 8070 506 275 105 C ATOM 2344 N ILE A1100 20.549 -8.614 0.064 1.00 76.02 N ANISOU 2344 N ILE A1100 9949 9924 9010 307 217 130 N ATOM 2345 CA ILE A1100 19.503 -7.959 -0.754 1.00 75.82 C ANISOU 2345 CA ILE A1100 9978 9869 8962 311 224 128 C ATOM 2346 C ILE A1100 19.636 -6.452 -0.552 1.00 78.02 C ANISOU 2346 C ILE A1100 10302 10126 9217 257 238 157 C ATOM 2347 O ILE A1100 19.645 -5.719 -1.537 1.00 78.48 O ANISOU 2347 O ILE A1100 10400 10183 9238 255 267 170 O ATOM 2348 CB ILE A1100 18.037 -8.453 -0.467 1.00 78.92 C ANISOU 2348 CB ILE A1100 10397 10226 9363 343 203 101 C ATOM 2349 CG1 ILE A1100 17.872 -9.969 -0.765 1.00 79.37 C ANISOU 2349 CG1 ILE A1100 10434 10289 9435 377 209 64 C ATOM 2350 CG2 ILE A1100 16.982 -7.611 -1.247 1.00 78.91 C ANISOU 2350 CG2 ILE A1100 10439 10225 9320 365 204 99 C ATOM 2351 CD1 ILE A1100 16.799 -10.692 0.091 1.00 83.86 C ANISOU 2351 CD1 ILE A1100 11023 10818 10022 375 199 31 C ATOM 2352 N ASN A1101 19.791 -6.006 0.721 1.00 73.14 N ANISOU 2352 N ASN A1101 9689 9487 8614 213 223 164 N ATOM 2353 CA ASN A1101 19.979 -4.602 1.115 1.00 73.18 C ANISOU 2353 CA ASN A1101 9751 9459 8595 146 243 184 C ATOM 2354 C ASN A1101 21.072 -3.906 0.240 1.00 77.64 C ANISOU 2354 C ASN A1101 10320 10054 9127 86 295 193 C ATOM 2355 O ASN A1101 20.875 -2.761 -0.194 1.00 79.37 O ANISOU 2355 O ASN A1101 10632 10222 9305 56 337 212 O ATOM 2356 CB ASN A1101 20.340 -4.516 2.615 1.00 71.09 C ANISOU 2356 CB ASN A1101 9463 9196 8353 98 219 179 C ATOM 2357 CG ASN A1101 20.326 -3.123 3.198 1.00 87.70 C ANISOU 2357 CG ASN A1101 11642 11249 10431 23 241 190 C ATOM 2358 OD1 ASN A1101 21.072 -2.224 2.785 1.00 84.03 O ANISOU 2358 OD1 ASN A1101 11207 10786 9933 -53 289 194 O ATOM 2359 ND2 ASN A1101 19.494 -2.921 4.197 1.00 77.26 N ANISOU 2359 ND2 ASN A1101 10359 9877 9118 35 216 192 N ATOM 2360 N MET A1102 22.197 -4.623 -0.023 1.00 71.50 N ANISOU 2360 N MET A1102 9449 9358 8358 75 299 179 N ATOM 2361 CA MET A1102 23.356 -4.201 -0.820 1.00 70.65 C ANISOU 2361 CA MET A1102 9315 9307 8222 13 350 177 C ATOM 2362 C MET A1102 23.032 -4.135 -2.321 1.00 75.59 C ANISOU 2362 C MET A1102 9989 9913 8818 56 384 190 C ATOM 2363 O MET A1102 23.454 -3.194 -3.001 1.00 75.13 O ANISOU 2363 O MET A1102 9986 9842 8718 -3 443 202 O ATOM 2364 CB MET A1102 24.532 -5.175 -0.600 1.00 72.40 C ANISOU 2364 CB MET A1102 9407 9645 8458 21 335 154 C ATOM 2365 CG MET A1102 25.264 -4.983 0.715 1.00 75.30 C ANISOU 2365 CG MET A1102 9711 10072 8826 -41 314 136 C ATOM 2366 SD MET A1102 26.777 -5.985 0.787 1.00 79.27 S ANISOU 2366 SD MET A1102 10054 10749 9318 -9 304 110 S ATOM 2367 CE MET A1102 27.930 -4.895 0.016 1.00 76.99 C ANISOU 2367 CE MET A1102 9730 10540 8982 -149 376 87 C ATOM 2368 N VAL A1103 22.344 -5.175 -2.849 1.00 72.66 N ANISOU 2368 N VAL A1103 9599 9546 8463 154 354 183 N ATOM 2369 CA VAL A1103 21.965 -5.275 -4.264 1.00 72.55 C ANISOU 2369 CA VAL A1103 9619 9530 8417 208 376 188 C ATOM 2370 C VAL A1103 20.945 -4.154 -4.590 1.00 77.69 C ANISOU 2370 C VAL A1103 10386 10109 9022 226 392 212 C ATOM 2371 O VAL A1103 21.060 -3.522 -5.639 1.00 79.00 O ANISOU 2371 O VAL A1103 10615 10266 9137 232 439 231 O ATOM 2372 CB VAL A1103 21.477 -6.704 -4.634 1.00 74.96 C ANISOU 2372 CB VAL A1103 9875 9860 8745 292 343 161 C ATOM 2373 CG1 VAL A1103 20.831 -6.749 -6.019 1.00 74.41 C ANISOU 2373 CG1 VAL A1103 9843 9794 8634 350 357 157 C ATOM 2374 CG2 VAL A1103 22.633 -7.701 -4.559 1.00 74.68 C ANISOU 2374 CG2 VAL A1103 9750 9892 8733 297 346 146 C ATOM 2375 N PHE A1104 20.013 -3.867 -3.660 1.00 72.87 N ANISOU 2375 N PHE A1104 9814 9451 8423 241 360 214 N ATOM 2376 CA PHE A1104 18.991 -2.821 -3.758 1.00 72.15 C ANISOU 2376 CA PHE A1104 9834 9299 8282 281 371 238 C ATOM 2377 C PHE A1104 19.629 -1.422 -3.837 1.00 76.99 C ANISOU 2377 C PHE A1104 10553 9852 8849 210 440 270 C ATOM 2378 O PHE A1104 19.074 -0.524 -4.474 1.00 77.04 O ANISOU 2378 O PHE A1104 10677 9806 8787 259 478 300 O ATOM 2379 CB PHE A1104 18.075 -2.917 -2.519 1.00 73.14 C ANISOU 2379 CB PHE A1104 9955 9398 8437 298 323 227 C ATOM 2380 CG PHE A1104 16.888 -1.983 -2.424 1.00 74.31 C ANISOU 2380 CG PHE A1104 10203 9499 8534 362 324 246 C ATOM 2381 CD1 PHE A1104 15.608 -2.425 -2.737 1.00 76.65 C ANISOU 2381 CD1 PHE A1104 10477 9836 8809 459 286 224 C ATOM 2382 CD2 PHE A1104 17.033 -0.692 -1.919 1.00 75.54 C ANISOU 2382 CD2 PHE A1104 10470 9576 8657 322 365 277 C ATOM 2383 CE1 PHE A1104 14.501 -1.583 -2.578 1.00 77.08 C ANISOU 2383 CE1 PHE A1104 10609 9871 8807 536 283 239 C ATOM 2384 CE2 PHE A1104 15.931 0.154 -1.789 1.00 77.88 C ANISOU 2384 CE2 PHE A1104 10867 9828 8898 403 369 298 C ATOM 2385 CZ PHE A1104 14.672 -0.297 -2.121 1.00 75.78 C ANISOU 2385 CZ PHE A1104 10566 9619 8608 519 325 280 C ATOM 2386 N GLN A1105 20.775 -1.245 -3.181 1.00 74.57 N ANISOU 2386 N GLN A1105 10210 9555 8569 95 462 261 N ATOM 2387 CA GLN A1105 21.462 0.035 -3.091 1.00 75.71 C ANISOU 2387 CA GLN A1105 10452 9645 8671 -12 538 276 C ATOM 2388 C GLN A1105 22.493 0.272 -4.217 1.00 83.03 C ANISOU 2388 C GLN A1105 11386 10600 9562 -70 610 278 C ATOM 2389 O GLN A1105 22.581 1.386 -4.718 1.00 84.36 O ANISOU 2389 O GLN A1105 11694 10693 9666 -110 691 303 O ATOM 2390 CB GLN A1105 22.148 0.152 -1.711 1.00 76.61 C ANISOU 2390 CB GLN A1105 10511 9776 8823 -123 525 250 C ATOM 2391 CG GLN A1105 22.823 1.507 -1.471 1.00 85.06 C ANISOU 2391 CG GLN A1105 11687 10787 9846 -263 611 249 C ATOM 2392 CD GLN A1105 23.859 1.517 -0.372 1.00 99.87 C ANISOU 2392 CD GLN A1105 13468 12730 11746 -397 605 206 C ATOM 2393 OE1 GLN A1105 24.073 0.535 0.354 1.00 96.14 O ANISOU 2393 OE1 GLN A1105 12856 12347 11325 -372 532 183 O ATOM 2394 NE2 GLN A1105 24.529 2.648 -0.227 1.00 85.72 N ANISOU 2394 NE2 GLN A1105 11761 10901 9909 -545 689 190 N ATOM 2395 N MET A1106 23.295 -0.727 -4.566 1.00 81.02 N ANISOU 2395 N MET A1106 10995 10448 9340 -78 591 254 N ATOM 2396 CA MET A1106 24.377 -0.553 -5.539 1.00 82.26 C ANISOU 2396 CA MET A1106 11139 10652 9466 -144 661 249 C ATOM 2397 C MET A1106 24.170 -1.328 -6.831 1.00 83.90 C ANISOU 2397 C MET A1106 11318 10897 9662 -40 652 257 C ATOM 2398 O MET A1106 25.007 -1.227 -7.736 1.00 85.11 O ANISOU 2398 O MET A1106 11464 11090 9785 -82 712 255 O ATOM 2399 CB MET A1106 25.713 -1.013 -4.929 1.00 86.03 C ANISOU 2399 CB MET A1106 11466 11245 9975 -244 657 207 C ATOM 2400 CG MET A1106 25.942 -0.577 -3.504 1.00 91.51 C ANISOU 2400 CG MET A1106 12142 11939 10687 -336 640 185 C ATOM 2401 SD MET A1106 27.260 -1.554 -2.746 1.00 97.97 S ANISOU 2401 SD MET A1106 12745 12938 11540 -378 597 133 S ATOM 2402 CE MET A1106 28.669 -0.774 -3.545 1.00 96.56 C ANISOU 2402 CE MET A1106 12545 12839 11304 -537 704 102 C ATOM 2403 N GLY A1107 23.111 -2.129 -6.898 1.00 77.15 N ANISOU 2403 N GLY A1107 10443 10042 8829 83 583 257 N ATOM 2404 CA GLY A1107 22.837 -2.942 -8.074 1.00 76.58 C ANISOU 2404 CA GLY A1107 10341 10011 8743 178 570 253 C ATOM 2405 C GLY A1107 23.516 -4.290 -8.031 1.00 79.97 C ANISOU 2405 C GLY A1107 10631 10532 9225 189 537 219 C ATOM 2406 O GLY A1107 24.533 -4.464 -7.360 1.00 80.48 O ANISOU 2406 O GLY A1107 10613 10647 9317 119 541 204 O ATOM 2407 N GLU A1108 22.963 -5.245 -8.767 1.00 76.21 N ANISOU 2407 N GLU A1108 10128 10080 8749 281 507 204 N ATOM 2408 CA GLU A1108 23.442 -6.622 -8.872 1.00 76.06 C ANISOU 2408 CA GLU A1108 10007 10126 8766 317 484 173 C ATOM 2409 C GLU A1108 24.930 -6.650 -9.306 1.00 81.98 C ANISOU 2409 C GLU A1108 10693 10950 9506 267 534 172 C ATOM 2410 O GLU A1108 25.734 -7.379 -8.734 1.00 82.55 O ANISOU 2410 O GLU A1108 10671 11084 9609 264 520 154 O ATOM 2411 CB GLU A1108 22.526 -7.370 -9.871 1.00 77.05 C ANISOU 2411 CB GLU A1108 10150 10256 8871 408 465 153 C ATOM 2412 CG GLU A1108 23.036 -8.679 -10.446 1.00 85.83 C ANISOU 2412 CG GLU A1108 11195 11421 9996 449 467 122 C ATOM 2413 CD GLU A1108 22.416 -9.108 -11.769 1.00105.97 C ANISOU 2413 CD GLU A1108 13773 13988 12503 513 472 100 C ATOM 2414 OE1 GLU A1108 23.157 -9.650 -12.620 1.00 92.85 O ANISOU 2414 OE1 GLU A1108 12081 12370 10827 531 503 91 O ATOM 2415 OE2 GLU A1108 21.192 -8.916 -11.954 1.00102.71 O ANISOU 2415 OE2 GLU A1108 13404 13557 12065 547 445 89 O ATOM 2416 N THR A1109 25.285 -5.824 -10.277 1.00 80.06 N ANISOU 2416 N THR A1109 10503 10704 9211 232 595 190 N ATOM 2417 CA THR A1109 26.628 -5.786 -10.854 1.00 80.67 C ANISOU 2417 CA THR A1109 10521 10860 9268 177 654 184 C ATOM 2418 C THR A1109 27.667 -5.165 -9.878 1.00 83.28 C ANISOU 2418 C THR A1109 10796 11238 9608 55 679 174 C ATOM 2419 O THR A1109 28.789 -5.662 -9.822 1.00 83.20 O ANISOU 2419 O THR A1109 10669 11339 9603 33 691 149 O ATOM 2420 CB THR A1109 26.568 -5.098 -12.220 1.00 90.03 C ANISOU 2420 CB THR A1109 11800 12019 10387 178 719 207 C ATOM 2421 OG1 THR A1109 27.626 -5.585 -13.033 1.00 87.96 O ANISOU 2421 OG1 THR A1109 11464 11847 10111 170 761 191 O ATOM 2422 CG2 THR A1109 26.544 -3.571 -12.139 1.00 90.32 C ANISOU 2422 CG2 THR A1109 11959 11980 10379 87 783 237 C ATOM 2423 N GLY A1110 27.265 -4.146 -9.111 1.00 78.78 N ANISOU 2423 N GLY A1110 10303 10595 9036 -15 685 187 N ATOM 2424 CA GLY A1110 28.099 -3.479 -8.114 1.00 78.56 C ANISOU 2424 CA GLY A1110 10233 10604 9010 -144 707 168 C ATOM 2425 C GLY A1110 28.525 -4.378 -6.964 1.00 81.31 C ANISOU 2425 C GLY A1110 10445 11043 9406 -121 640 139 C ATOM 2426 O GLY A1110 29.707 -4.385 -6.600 1.00 82.22 O ANISOU 2426 O GLY A1110 10448 11280 9512 -194 658 107 O ATOM 2427 N VAL A1111 27.567 -5.161 -6.402 1.00 74.98 N ANISOU 2427 N VAL A1111 9650 10192 8646 -16 566 148 N ATOM 2428 CA VAL A1111 27.785 -6.116 -5.311 1.00 74.43 C ANISOU 2428 CA VAL A1111 9484 10183 8615 34 503 130 C ATOM 2429 C VAL A1111 28.678 -7.289 -5.802 1.00 80.80 C ANISOU 2429 C VAL A1111 10179 11103 9417 112 502 112 C ATOM 2430 O VAL A1111 29.545 -7.763 -5.056 1.00 80.96 O ANISOU 2430 O VAL A1111 10091 11233 9437 124 482 92 O ATOM 2431 CB VAL A1111 26.439 -6.612 -4.724 1.00 76.54 C ANISOU 2431 CB VAL A1111 9813 10349 8919 116 444 142 C ATOM 2432 CG1 VAL A1111 26.658 -7.593 -3.574 1.00 75.64 C ANISOU 2432 CG1 VAL A1111 9624 10280 8836 171 391 129 C ATOM 2433 CG2 VAL A1111 25.596 -5.436 -4.253 1.00 75.90 C ANISOU 2433 CG2 VAL A1111 9836 10167 8833 56 447 160 C ATOM 2434 N ALA A1112 28.494 -7.709 -7.073 1.00 77.72 N ANISOU 2434 N ALA A1112 9818 10697 9014 170 527 118 N ATOM 2435 CA ALA A1112 29.269 -8.763 -7.724 1.00 77.92 C ANISOU 2435 CA ALA A1112 9763 10815 9028 250 538 104 C ATOM 2436 C ALA A1112 30.784 -8.400 -7.870 1.00 83.26 C ANISOU 2436 C ALA A1112 10323 11645 9666 179 585 82 C ATOM 2437 O ALA A1112 31.603 -9.295 -8.110 1.00 83.95 O ANISOU 2437 O ALA A1112 10316 11842 9738 257 587 66 O ATOM 2438 CB ALA A1112 28.672 -9.069 -9.080 1.00 78.40 C ANISOU 2438 CB ALA A1112 9894 10819 9075 305 560 112 C ATOM 2439 N GLY A1113 31.129 -7.116 -7.699 1.00 79.25 N ANISOU 2439 N GLY A1113 9826 11148 9138 33 626 76 N ATOM 2440 CA GLY A1113 32.506 -6.633 -7.753 1.00 80.02 C ANISOU 2440 CA GLY A1113 9811 11399 9194 -72 678 41 C ATOM 2441 C GLY A1113 33.286 -6.879 -6.468 1.00 84.16 C ANISOU 2441 C GLY A1113 10198 12063 9715 -82 637 7 C ATOM 2442 O GLY A1113 34.521 -6.793 -6.452 1.00 84.32 O ANISOU 2442 O GLY A1113 10080 12263 9694 -138 667 -35 O ATOM 2443 N PHE A1114 32.564 -7.203 -5.376 1.00 80.18 N ANISOU 2443 N PHE A1114 9725 11492 9248 -24 568 21 N ATOM 2444 CA PHE A1114 33.133 -7.477 -4.057 1.00 80.32 C ANISOU 2444 CA PHE A1114 9632 11628 9258 -10 519 -5 C ATOM 2445 C PHE A1114 33.563 -8.947 -3.948 1.00 84.79 C ANISOU 2445 C PHE A1114 10111 12290 9816 175 478 -4 C ATOM 2446 O PHE A1114 33.199 -9.618 -2.990 1.00 84.69 O ANISOU 2446 O PHE A1114 10106 12252 9819 274 421 9 O ATOM 2447 CB PHE A1114 32.103 -7.137 -2.974 1.00 81.14 C ANISOU 2447 CB PHE A1114 9829 11600 9400 -26 471 14 C ATOM 2448 CG PHE A1114 31.804 -5.675 -2.783 1.00 83.28 C ANISOU 2448 CG PHE A1114 10185 11792 9667 -198 510 8 C ATOM 2449 CD1 PHE A1114 30.961 -5.003 -3.654 1.00 86.43 C ANISOU 2449 CD1 PHE A1114 10732 12036 10074 -235 553 40 C ATOM 2450 CD2 PHE A1114 32.281 -4.993 -1.671 1.00 87.59 C ANISOU 2450 CD2 PHE A1114 10677 12410 10194 -310 503 -28 C ATOM 2451 CE1 PHE A1114 30.667 -3.651 -3.465 1.00 87.99 C ANISOU 2451 CE1 PHE A1114 11035 12143 10256 -375 599 40 C ATOM 2452 CE2 PHE A1114 31.961 -3.645 -1.465 1.00 90.85 C ANISOU 2452 CE2 PHE A1114 11194 12727 10598 -469 549 -34 C ATOM 2453 CZ PHE A1114 31.157 -2.984 -2.365 1.00 88.29 C ANISOU 2453 CZ PHE A1114 11031 12236 10278 -495 600 4 C ATOM 2454 N THR A1115 34.387 -9.420 -4.902 1.00 81.81 N ANISOU 2454 N THR A1115 9656 12023 9404 225 516 -17 N ATOM 2455 CA THR A1115 34.856 -10.801 -5.038 1.00 81.91 C ANISOU 2455 CA THR A1115 9607 12120 9396 413 496 -13 C ATOM 2456 C THR A1115 35.488 -11.394 -3.770 1.00 86.12 C ANISOU 2456 C THR A1115 10032 12795 9896 513 443 -28 C ATOM 2457 O THR A1115 35.114 -12.516 -3.412 1.00 85.50 O ANISOU 2457 O THR A1115 10006 12656 9823 682 411 -1 O ATOM 2458 CB THR A1115 35.825 -10.941 -6.218 1.00 91.46 C ANISOU 2458 CB THR A1115 10729 13459 10561 421 554 -34 C ATOM 2459 OG1 THR A1115 36.922 -10.045 -6.033 1.00 95.58 O ANISOU 2459 OG1 THR A1115 11110 14170 11037 280 586 -84 O ATOM 2460 CG2 THR A1115 35.151 -10.692 -7.567 1.00 87.49 C ANISOU 2460 CG2 THR A1115 10349 12811 10082 381 603 -12 C ATOM 2461 N ASN A1116 36.428 -10.682 -3.100 1.00 83.56 N ANISOU 2461 N ASN A1116 9564 12658 9528 414 440 -73 N ATOM 2462 CA ASN A1116 37.115 -11.219 -1.909 1.00 84.21 C ANISOU 2462 CA ASN A1116 9524 12912 9559 521 386 -92 C ATOM 2463 C ASN A1116 36.185 -11.294 -0.697 1.00 85.56 C ANISOU 2463 C ASN A1116 9795 12947 9767 549 328 -64 C ATOM 2464 O ASN A1116 36.268 -12.263 0.057 1.00 85.07 O ANISOU 2464 O ASN A1116 9724 12922 9679 724 285 -46 O ATOM 2465 CB ASN A1116 38.378 -10.434 -1.575 1.00 89.42 C ANISOU 2465 CB ASN A1116 9987 13838 10151 395 398 -164 C ATOM 2466 CG ASN A1116 39.386 -10.431 -2.701 1.00122.91 C ANISOU 2466 CG ASN A1116 14110 18243 14345 374 459 -199 C ATOM 2467 OD1 ASN A1116 39.219 -9.751 -3.723 1.00119.77 O ANISOU 2467 OD1 ASN A1116 13773 17760 13973 235 525 -201 O ATOM 2468 ND2 ASN A1116 40.441 -11.216 -2.556 1.00117.12 N ANISOU 2468 ND2 ASN A1116 13213 17751 13536 525 443 -226 N ATOM 2469 N SER A1117 35.286 -10.299 -0.530 1.00 80.58 N ANISOU 2469 N SER A1117 9270 12154 9190 389 333 -56 N ATOM 2470 CA SER A1117 34.289 -10.253 0.547 1.00 79.19 C ANISOU 2470 CA SER A1117 9199 11836 9055 397 285 -29 C ATOM 2471 C SER A1117 33.280 -11.370 0.367 1.00 81.91 C ANISOU 2471 C SER A1117 9682 12000 9440 551 271 22 C ATOM 2472 O SER A1117 32.924 -12.023 1.341 1.00 81.38 O ANISOU 2472 O SER A1117 9655 11894 9373 656 231 41 O ATOM 2473 CB SER A1117 33.556 -8.912 0.572 1.00 82.18 C ANISOU 2473 CB SER A1117 9669 12081 9474 201 306 -32 C ATOM 2474 OG SER A1117 34.424 -7.791 0.569 1.00 92.61 O ANISOU 2474 OG SER A1117 10895 13535 10756 23 342 -85 O ATOM 2475 N LEU A1118 32.822 -11.583 -0.888 1.00 78.56 N ANISOU 2475 N LEU A1118 9335 11469 9044 558 312 38 N ATOM 2476 CA LEU A1118 31.841 -12.597 -1.280 1.00 77.95 C ANISOU 2476 CA LEU A1118 9392 11225 9002 673 314 70 C ATOM 2477 C LEU A1118 32.371 -14.003 -1.029 1.00 83.77 C ANISOU 2477 C LEU A1118 10110 12023 9697 871 307 80 C ATOM 2478 O LEU A1118 31.631 -14.854 -0.519 1.00 83.80 O ANISOU 2478 O LEU A1118 10222 11902 9716 967 295 102 O ATOM 2479 CB LEU A1118 31.436 -12.435 -2.753 1.00 77.75 C ANISOU 2479 CB LEU A1118 9426 11118 8996 629 360 73 C ATOM 2480 CG LEU A1118 30.492 -11.269 -3.109 1.00 81.25 C ANISOU 2480 CG LEU A1118 9954 11438 9478 482 371 79 C ATOM 2481 CD1 LEU A1118 30.335 -11.151 -4.616 1.00 80.87 C ANISOU 2481 CD1 LEU A1118 9946 11353 9427 463 418 80 C ATOM 2482 CD2 LEU A1118 29.134 -11.384 -2.404 1.00 81.34 C ANISOU 2482 CD2 LEU A1118 10081 11290 9533 491 336 97 C ATOM 2483 N ARG A1119 33.661 -14.227 -1.339 1.00 80.90 N ANISOU 2483 N ARG A1119 9612 11854 9273 934 321 60 N ATOM 2484 CA ARG A1119 34.337 -15.492 -1.110 1.00 81.31 C ANISOU 2484 CA ARG A1119 9638 11992 9264 1146 319 70 C ATOM 2485 C ARG A1119 34.329 -15.826 0.381 1.00 86.98 C ANISOU 2485 C ARG A1119 10359 12735 9955 1235 271 83 C ATOM 2486 O ARG A1119 34.075 -16.975 0.732 1.00 87.73 O ANISOU 2486 O ARG A1119 10556 12750 10029 1405 276 113 O ATOM 2487 CB ARG A1119 35.775 -15.428 -1.647 1.00 82.38 C ANISOU 2487 CB ARG A1119 9596 12373 9330 1180 339 38 C ATOM 2488 CG ARG A1119 36.492 -16.781 -1.722 1.00 92.37 C ANISOU 2488 CG ARG A1119 10846 13728 10522 1426 351 51 C ATOM 2489 CD ARG A1119 37.930 -16.635 -2.199 1.00104.31 C ANISOU 2489 CD ARG A1119 12159 15516 11958 1458 367 13 C ATOM 2490 NE ARG A1119 38.008 -16.336 -3.634 1.00114.23 N ANISOU 2490 NE ARG A1119 13411 16752 13239 1367 422 -1 N ATOM 2491 CZ ARG A1119 38.445 -15.189 -4.146 1.00126.70 C ANISOU 2491 CZ ARG A1119 14882 18434 14825 1173 444 -40 C ATOM 2492 NH1 ARG A1119 38.472 -15.016 -5.465 1.00114.56 N ANISOU 2492 NH1 ARG A1119 13363 16861 13302 1112 500 -45 N ATOM 2493 NH2 ARG A1119 38.862 -14.212 -3.354 1.00112.04 N ANISOU 2493 NH2 ARG A1119 12907 16710 12954 1035 419 -76 N ATOM 2494 N MET A1120 34.574 -14.819 1.253 1.00 84.04 N ANISOU 2494 N MET A1120 9893 12462 9578 1115 232 61 N ATOM 2495 CA MET A1120 34.641 -14.972 2.712 1.00 84.15 C ANISOU 2495 CA MET A1120 9891 12525 9557 1184 181 67 C ATOM 2496 C MET A1120 33.281 -15.294 3.335 1.00 87.49 C ANISOU 2496 C MET A1120 10499 12707 10038 1192 172 106 C ATOM 2497 O MET A1120 33.240 -16.040 4.310 1.00 87.77 O ANISOU 2497 O MET A1120 10580 12731 10035 1333 150 130 O ATOM 2498 CB MET A1120 35.227 -13.717 3.370 1.00 87.03 C ANISOU 2498 CB MET A1120 10108 13057 9902 1022 150 21 C ATOM 2499 CG MET A1120 36.691 -13.496 3.070 1.00 92.48 C ANISOU 2499 CG MET A1120 10590 14037 10513 1023 156 -31 C ATOM 2500 SD MET A1120 37.780 -14.660 3.907 1.00 98.83 S ANISOU 2500 SD MET A1120 11277 15081 11193 1303 116 -30 S ATOM 2501 CE MET A1120 39.154 -14.694 2.766 1.00 97.08 C ANISOU 2501 CE MET A1120 10862 15120 10903 1324 155 -78 C ATOM 2502 N LEU A1121 32.186 -14.716 2.799 1.00 83.47 N ANISOU 2502 N LEU A1121 10089 12014 9609 1046 189 110 N ATOM 2503 CA LEU A1121 30.799 -14.934 3.240 1.00 82.30 C ANISOU 2503 CA LEU A1121 10104 11647 9518 1028 186 135 C ATOM 2504 C LEU A1121 30.349 -16.372 2.924 1.00 87.80 C ANISOU 2504 C LEU A1121 10933 12216 10209 1182 223 159 C ATOM 2505 O LEU A1121 29.656 -16.988 3.736 1.00 88.53 O ANISOU 2505 O LEU A1121 11141 12191 10307 1241 222 180 O ATOM 2506 CB LEU A1121 29.850 -13.931 2.556 1.00 81.01 C ANISOU 2506 CB LEU A1121 9992 11362 9425 850 199 126 C ATOM 2507 CG LEU A1121 29.989 -12.458 2.899 1.00 84.95 C ANISOU 2507 CG LEU A1121 10424 11919 9935 682 180 106 C ATOM 2508 CD1 LEU A1121 29.353 -11.608 1.822 1.00 84.27 C ANISOU 2508 CD1 LEU A1121 10389 11739 9892 553 212 102 C ATOM 2509 CD2 LEU A1121 29.367 -12.143 4.251 1.00 86.67 C ANISOU 2509 CD2 LEU A1121 10686 12076 10167 652 141 114 C ATOM 2510 N GLN A1122 30.726 -16.880 1.727 1.00 84.80 N ANISOU 2510 N GLN A1122 10549 11854 9817 1234 264 153 N ATOM 2511 CA GLN A1122 30.491 -18.241 1.229 1.00 84.88 C ANISOU 2511 CA GLN A1122 10684 11758 9810 1374 314 166 C ATOM 2512 C GLN A1122 31.111 -19.279 2.186 1.00 89.65 C ANISOU 2512 C GLN A1122 11318 12409 10336 1579 315 192 C ATOM 2513 O GLN A1122 30.455 -20.263 2.537 1.00 90.52 O ANISOU 2513 O GLN A1122 11593 12361 10440 1665 350 211 O ATOM 2514 CB GLN A1122 31.114 -18.384 -0.162 1.00 86.65 C ANISOU 2514 CB GLN A1122 10854 12050 10018 1392 350 150 C ATOM 2515 CG GLN A1122 30.153 -18.711 -1.295 1.00107.36 C ANISOU 2515 CG GLN A1122 13595 14511 12686 1337 394 138 C ATOM 2516 CD GLN A1122 30.877 -18.695 -2.626 1.00130.22 C ANISOU 2516 CD GLN A1122 16421 17497 15561 1349 425 123 C ATOM 2517 OE1 GLN A1122 31.903 -19.357 -2.820 1.00123.83 O ANISOU 2517 OE1 GLN A1122 15563 16796 14689 1491 446 127 O ATOM 2518 NE2 GLN A1122 30.370 -17.916 -3.570 1.00128.33 N ANISOU 2518 NE2 GLN A1122 16174 17222 15365 1209 431 106 N ATOM 2519 N GLN A1123 32.362 -19.019 2.643 1.00 84.62 N ANISOU 2519 N GLN A1123 10523 11997 9632 1655 279 190 N ATOM 2520 CA GLN A1123 33.138 -19.848 3.580 1.00 84.20 C ANISOU 2520 CA GLN A1123 10463 12047 9483 1872 269 214 C ATOM 2521 C GLN A1123 32.726 -19.606 5.051 1.00 86.27 C ANISOU 2521 C GLN A1123 10756 12282 9741 1863 225 230 C ATOM 2522 O GLN A1123 33.358 -20.152 5.968 1.00 86.65 O ANISOU 2522 O GLN A1123 10791 12432 9701 2041 207 251 O ATOM 2523 CB GLN A1123 34.637 -19.552 3.412 1.00 86.32 C ANISOU 2523 CB GLN A1123 10516 12610 9673 1941 244 190 C ATOM 2524 CG GLN A1123 35.214 -19.914 2.050 1.00 90.93 C ANISOU 2524 CG GLN A1123 11061 13247 10240 1988 291 177 C ATOM 2525 CD GLN A1123 36.686 -19.591 1.950 1.00 99.04 C ANISOU 2525 CD GLN A1123 11859 14587 11184 2047 268 146 C ATOM 2526 OE1 GLN A1123 37.395 -19.441 2.957 1.00 92.53 O ANISOU 2526 OE1 GLN A1123 10915 13955 10287 2121 220 137 O ATOM 2527 NE2 GLN A1123 37.180 -19.495 0.722 1.00 87.30 N ANISOU 2527 NE2 GLN A1123 10301 13171 9699 2016 304 123 N ATOM 2528 N LYS A1124 31.685 -18.761 5.259 1.00 80.77 N ANISOU 2528 N LYS A1124 10099 11459 9132 1665 207 220 N ATOM 2529 CA LYS A1124 31.101 -18.362 6.545 1.00 79.91 C ANISOU 2529 CA LYS A1124 10026 11298 9037 1614 168 230 C ATOM 2530 C LYS A1124 32.157 -17.755 7.515 1.00 85.42 C ANISOU 2530 C LYS A1124 10552 12237 9665 1643 104 216 C ATOM 2531 O LYS A1124 32.130 -18.043 8.717 1.00 85.96 O ANISOU 2531 O LYS A1124 10657 12315 9688 1735 79 237 O ATOM 2532 CB LYS A1124 30.352 -19.544 7.196 1.00 82.99 C ANISOU 2532 CB LYS A1124 10621 11501 9410 1743 208 269 C ATOM 2533 CG LYS A1124 29.128 -19.999 6.400 1.00 99.91 C ANISOU 2533 CG LYS A1124 12928 13410 11625 1664 270 264 C ATOM 2534 CD LYS A1124 28.352 -21.111 7.114 1.00107.36 C ANISOU 2534 CD LYS A1124 14082 14163 12548 1756 322 291 C ATOM 2535 CE LYS A1124 27.172 -21.623 6.306 1.00110.91 C ANISOU 2535 CE LYS A1124 14683 14402 13056 1664 391 270 C ATOM 2536 NZ LYS A1124 27.588 -22.477 5.153 1.00109.05 N ANISOU 2536 NZ LYS A1124 14495 14148 12792 1753 450 262 N ATOM 2537 N ARG A1125 33.050 -16.877 6.996 1.00 82.27 N ANISOU 2537 N ARG A1125 9966 12035 9256 1548 83 174 N ATOM 2538 CA ARG A1125 34.099 -16.202 7.789 1.00 82.79 C ANISOU 2538 CA ARG A1125 9844 12361 9252 1535 28 138 C ATOM 2539 C ARG A1125 33.753 -14.719 7.911 1.00 84.84 C ANISOU 2539 C ARG A1125 10046 12614 9575 1275 7 99 C ATOM 2540 O ARG A1125 34.399 -13.872 7.294 1.00 85.33 O ANISOU 2540 O ARG A1125 9975 12810 9635 1141 13 53 O ATOM 2541 CB ARG A1125 35.506 -16.399 7.175 1.00 83.83 C ANISOU 2541 CB ARG A1125 9798 12753 9300 1629 31 108 C ATOM 2542 CG ARG A1125 35.671 -17.649 6.324 1.00 91.83 C ANISOU 2542 CG ARG A1125 10894 13711 10286 1824 82 142 C ATOM 2543 CD ARG A1125 37.025 -18.320 6.449 1.00 97.30 C ANISOU 2543 CD ARG A1125 11453 14669 10849 2049 71 134 C ATOM 2544 NE ARG A1125 38.141 -17.398 6.241 1.00100.31 N ANISOU 2544 NE ARG A1125 11580 15345 11188 1943 43 66 N ATOM 2545 CZ ARG A1125 39.218 -17.679 5.517 1.00118.23 C ANISOU 2545 CZ ARG A1125 13708 17825 13387 2037 61 40 C ATOM 2546 NH1 ARG A1125 40.193 -16.790 5.400 1.00106.45 N ANISOU 2546 NH1 ARG A1125 11982 16610 11855 1912 42 -32 N ATOM 2547 NH2 ARG A1125 39.328 -18.851 4.907 1.00112.34 N ANISOU 2547 NH2 ARG A1125 13059 17018 12606 2252 105 81 N ATOM 2548 N TRP A1126 32.716 -14.430 8.706 1.00 79.22 N ANISOU 2548 N TRP A1126 9449 11738 8912 1207 -9 118 N ATOM 2549 CA TRP A1126 32.084 -13.128 8.942 1.00 78.15 C ANISOU 2549 CA TRP A1126 9321 11532 8840 984 -21 95 C ATOM 2550 C TRP A1126 33.025 -11.963 9.338 1.00 82.80 C ANISOU 2550 C TRP A1126 9736 12338 9386 843 -50 33 C ATOM 2551 O TRP A1126 32.896 -10.885 8.756 1.00 82.24 O ANISOU 2551 O TRP A1126 9650 12238 9359 650 -25 4 O ATOM 2552 CB TRP A1126 30.995 -13.268 10.002 1.00 76.24 C ANISOU 2552 CB TRP A1126 9217 11121 8629 996 -39 126 C ATOM 2553 CG TRP A1126 30.247 -14.573 9.962 1.00 76.89 C ANISOU 2553 CG TRP A1126 9463 11030 8724 1149 -8 176 C ATOM 2554 CD1 TRP A1126 30.147 -15.488 10.970 1.00 80.30 C ANISOU 2554 CD1 TRP A1126 9974 11430 9105 1310 -16 210 C ATOM 2555 CD2 TRP A1126 29.494 -15.108 8.858 1.00 76.01 C ANISOU 2555 CD2 TRP A1126 9463 10747 8669 1148 45 192 C ATOM 2556 NE1 TRP A1126 29.357 -16.545 10.574 1.00 79.32 N ANISOU 2556 NE1 TRP A1126 10018 11113 9007 1393 39 244 N ATOM 2557 CE2 TRP A1126 28.952 -16.343 9.279 1.00 79.70 C ANISOU 2557 CE2 TRP A1126 10080 11082 9120 1293 73 229 C ATOM 2558 CE3 TRP A1126 29.205 -14.648 7.554 1.00 76.76 C ANISOU 2558 CE3 TRP A1126 9554 10790 8821 1034 76 176 C ATOM 2559 CZ2 TRP A1126 28.113 -17.112 8.460 1.00 78.45 C ANISOU 2559 CZ2 TRP A1126 10059 10744 9004 1305 132 239 C ATOM 2560 CZ3 TRP A1126 28.404 -15.428 6.729 1.00 77.56 C ANISOU 2560 CZ3 TRP A1126 9780 10730 8960 1067 123 190 C ATOM 2561 CH2 TRP A1126 27.855 -16.637 7.186 1.00 78.37 C ANISOU 2561 CH2 TRP A1126 10022 10705 9048 1191 151 216 C ATOM 2562 N ASP A1127 33.933 -12.145 10.319 1.00 80.43 N ANISOU 2562 N ASP A1127 9315 12253 8994 933 -96 9 N ATOM 2563 CA ASP A1127 34.867 -11.079 10.726 1.00 81.19 C ANISOU 2563 CA ASP A1127 9232 12580 9036 786 -120 -66 C ATOM 2564 C ASP A1127 35.857 -10.688 9.586 1.00 84.59 C ANISOU 2564 C ASP A1127 9517 13179 9446 698 -82 -117 C ATOM 2565 O ASP A1127 36.164 -9.506 9.433 1.00 83.72 O ANISOU 2565 O ASP A1127 9335 13137 9340 478 -63 -177 O ATOM 2566 CB ASP A1127 35.638 -11.488 11.983 1.00 84.73 C ANISOU 2566 CB ASP A1127 9568 13250 9375 927 -182 -85 C ATOM 2567 CG ASP A1127 34.895 -11.274 13.286 1.00101.26 C ANISOU 2567 CG ASP A1127 11755 15243 11477 914 -220 -68 C ATOM 2568 OD1 ASP A1127 33.641 -11.237 13.263 1.00102.01 O ANISOU 2568 OD1 ASP A1127 12032 15065 11663 869 -199 -20 O ATOM 2569 OD2 ASP A1127 35.561 -11.180 14.333 1.00112.35 O ANISOU 2569 OD2 ASP A1127 13046 16853 12790 957 -273 -104 O ATOM 2570 N GLU A1128 36.317 -11.674 8.781 1.00 81.21 N ANISOU 2570 N GLU A1128 9062 12803 8991 866 -62 -94 N ATOM 2571 CA GLU A1128 37.222 -11.451 7.648 1.00 81.16 C ANISOU 2571 CA GLU A1128 8926 12950 8962 807 -22 -136 C ATOM 2572 C GLU A1128 36.460 -10.844 6.449 1.00 83.09 C ANISOU 2572 C GLU A1128 9289 12976 9306 642 40 -121 C ATOM 2573 O GLU A1128 37.042 -10.052 5.704 1.00 82.78 O ANISOU 2573 O GLU A1128 9160 13032 9260 483 82 -170 O ATOM 2574 CB GLU A1128 37.949 -12.740 7.269 1.00 83.06 C ANISOU 2574 CB GLU A1128 9109 13320 9132 1064 -22 -114 C ATOM 2575 CG GLU A1128 39.080 -13.042 8.229 1.00 89.03 C ANISOU 2575 CG GLU A1128 9679 14391 9758 1201 -76 -154 C ATOM 2576 CD GLU A1128 39.596 -14.462 8.186 1.00104.33 C ANISOU 2576 CD GLU A1128 11612 16419 11612 1518 -83 -112 C ATOM 2577 OE1 GLU A1128 38.790 -15.395 8.403 1.00 96.90 O ANISOU 2577 OE1 GLU A1128 10866 15255 10696 1682 -77 -35 O ATOM 2578 OE2 GLU A1128 40.821 -14.637 7.985 1.00 98.35 O ANISOU 2578 OE2 GLU A1128 10655 15961 10752 1605 -91 -159 O ATOM 2579 N ALA A1129 35.157 -11.175 6.296 1.00 77.86 N ANISOU 2579 N ALA A1129 8827 12031 8726 674 49 -58 N ATOM 2580 CA ALA A1129 34.284 -10.574 5.286 1.00 76.19 C ANISOU 2580 CA ALA A1129 8736 11613 8598 535 98 -41 C ATOM 2581 C ALA A1129 34.108 -9.089 5.629 1.00 82.12 C ANISOU 2581 C ALA A1129 9488 12345 9369 301 108 -79 C ATOM 2582 O ALA A1129 34.220 -8.246 4.742 1.00 82.89 O ANISOU 2582 O ALA A1129 9588 12424 9483 148 161 -101 O ATOM 2583 CB ALA A1129 32.936 -11.289 5.250 1.00 75.08 C ANISOU 2583 CB ALA A1129 8786 11216 8523 627 97 21 C ATOM 2584 N ALA A1130 33.951 -8.777 6.949 1.00 79.46 N ANISOU 2584 N ALA A1130 9148 12028 9016 276 62 -91 N ATOM 2585 CA ALA A1130 33.760 -7.445 7.549 1.00 79.30 C ANISOU 2585 CA ALA A1130 9143 11983 9003 70 68 -129 C ATOM 2586 C ALA A1130 34.941 -6.493 7.358 1.00 86.04 C ANISOU 2586 C ALA A1130 9847 13047 9798 -109 102 -212 C ATOM 2587 O ALA A1130 34.699 -5.299 7.178 1.00 86.21 O ANISOU 2587 O ALA A1130 9932 12984 9839 -312 150 -237 O ATOM 2588 CB ALA A1130 33.494 -7.587 9.032 1.00 79.77 C ANISOU 2588 CB ALA A1130 9212 12054 9043 124 7 -126 C ATOM 2589 N VAL A1131 36.201 -6.995 7.442 1.00 84.02 N ANISOU 2589 N VAL A1131 9396 13066 9460 -38 83 -258 N ATOM 2590 CA VAL A1131 37.424 -6.178 7.311 1.00 85.70 C ANISOU 2590 CA VAL A1131 9434 13525 9602 -214 117 -353 C ATOM 2591 C VAL A1131 37.484 -5.581 5.886 1.00 91.29 C ANISOU 2591 C VAL A1131 10187 14155 10343 -355 207 -359 C ATOM 2592 O VAL A1131 37.697 -4.369 5.741 1.00 91.72 O ANISOU 2592 O VAL A1131 10250 14211 10388 -594 268 -415 O ATOM 2593 CB VAL A1131 38.738 -6.956 7.685 1.00 90.62 C ANISOU 2593 CB VAL A1131 9822 14490 10120 -73 71 -402 C ATOM 2594 CG1 VAL A1131 39.979 -6.084 7.503 1.00 92.23 C ANISOU 2594 CG1 VAL A1131 9828 14968 10246 -280 113 -516 C ATOM 2595 CG2 VAL A1131 38.687 -7.485 9.111 1.00 90.29 C ANISOU 2595 CG2 VAL A1131 9748 14527 10031 74 -14 -394 C ATOM 2596 N ASN A1132 37.254 -6.437 4.859 1.00 87.96 N ANISOU 2596 N ASN A1132 9813 13653 9956 -206 220 -301 N ATOM 2597 CA ASN A1132 37.263 -6.106 3.430 1.00 87.88 C ANISOU 2597 CA ASN A1132 9852 13566 9972 -289 300 -293 C ATOM 2598 C ASN A1132 36.086 -5.200 3.040 1.00 91.52 C ANISOU 2598 C ASN A1132 10529 13741 10505 -417 345 -254 C ATOM 2599 O ASN A1132 36.291 -4.290 2.224 1.00 92.09 O ANISOU 2599 O ASN A1132 10635 13783 10570 -587 426 -278 O ATOM 2600 CB ASN A1132 37.255 -7.376 2.569 1.00 86.83 C ANISOU 2600 CB ASN A1132 9721 13420 9851 -72 292 -241 C ATOM 2601 CG ASN A1132 38.560 -8.132 2.573 1.00111.23 C ANISOU 2601 CG ASN A1132 12600 16804 12857 48 275 -282 C ATOM 2602 OD1 ASN A1132 38.633 -9.274 3.030 1.00108.46 O ANISOU 2602 OD1 ASN A1132 12223 16506 12482 275 220 -251 O ATOM 2603 ND2 ASN A1132 39.618 -7.528 2.047 1.00106.24 N ANISOU 2603 ND2 ASN A1132 11822 16374 12171 -94 328 -354 N ATOM 2604 N LEU A1133 34.864 -5.453 3.599 1.00 86.20 N ANISOU 2604 N LEU A1133 10001 12863 9888 -330 299 -194 N ATOM 2605 CA LEU A1133 33.665 -4.644 3.334 1.00 84.93 C ANISOU 2605 CA LEU A1133 10038 12447 9784 -418 332 -155 C ATOM 2606 C LEU A1133 33.848 -3.222 3.869 1.00 91.49 C ANISOU 2606 C LEU A1133 10898 13277 10589 -643 375 -206 C ATOM 2607 O LEU A1133 33.400 -2.273 3.229 1.00 91.16 O ANISOU 2607 O LEU A1133 10991 13086 10560 -765 445 -196 O ATOM 2608 CB LEU A1133 32.385 -5.273 3.930 1.00 83.24 C ANISOU 2608 CB LEU A1133 9945 12056 9626 -277 272 -93 C ATOM 2609 CG LEU A1133 31.782 -6.514 3.241 1.00 86.46 C ANISOU 2609 CG LEU A1133 10403 12375 10071 -88 254 -37 C ATOM 2610 CD1 LEU A1133 30.708 -7.117 4.101 1.00 85.16 C ANISOU 2610 CD1 LEU A1133 10330 12080 9946 20 200 2 C ATOM 2611 CD2 LEU A1133 31.206 -6.197 1.844 1.00 87.32 C ANISOU 2611 CD2 LEU A1133 10619 12349 10210 -121 310 -11 C ATOM 2612 N ALA A1134 34.525 -3.081 5.025 1.00 90.56 N ANISOU 2612 N ALA A1134 10658 13326 10424 -695 338 -264 N ATOM 2613 CA ALA A1134 34.816 -1.799 5.666 1.00 92.11 C ANISOU 2613 CA ALA A1134 10867 13547 10584 -920 379 -330 C ATOM 2614 C ALA A1134 35.901 -1.026 4.910 1.00100.15 C ANISOU 2614 C ALA A1134 11806 14699 11546 -1120 473 -404 C ATOM 2615 O ALA A1134 35.976 0.197 5.047 1.00100.72 O ANISOU 2615 O ALA A1134 11957 14719 11593 -1339 546 -452 O ATOM 2616 CB ALA A1134 35.249 -2.029 7.104 1.00 93.36 C ANISOU 2616 CB ALA A1134 10899 13873 10700 -898 304 -376 C ATOM 2617 N LYS A1135 36.729 -1.732 4.112 1.00 99.26 N ANISOU 2617 N LYS A1135 11552 14753 11410 -1049 480 -417 N ATOM 2618 CA LYS A1135 37.809 -1.147 3.300 1.00101.39 C ANISOU 2618 CA LYS A1135 11729 15173 11623 -1225 573 -489 C ATOM 2619 C LYS A1135 37.336 -0.918 1.844 1.00107.66 C ANISOU 2619 C LYS A1135 12677 15775 12453 -1235 654 -431 C ATOM 2620 O LYS A1135 38.048 -1.283 0.904 1.00109.15 O ANISOU 2620 O LYS A1135 12769 16083 12618 -1218 691 -446 O ATOM 2621 CB LYS A1135 39.068 -2.039 3.343 1.00104.25 C ANISOU 2621 CB LYS A1135 11824 15864 11922 -1134 532 -544 C ATOM 2622 CG LYS A1135 39.914 -1.808 4.583 1.00116.13 C ANISOU 2622 CG LYS A1135 13147 17628 13350 -1220 491 -641 C ATOM 2623 CD LYS A1135 41.254 -2.513 4.509 1.00124.10 C ANISOU 2623 CD LYS A1135 13881 18997 14276 -1148 466 -709 C ATOM 2624 CE LYS A1135 42.102 -2.149 5.702 1.00133.93 C ANISOU 2624 CE LYS A1135 14935 20523 15430 -1257 431 -821 C ATOM 2625 NZ LYS A1135 43.372 -2.918 5.746 1.00144.29 N ANISOU 2625 NZ LYS A1135 15961 22218 16645 -1144 391 -886 N ATOM 2626 N SER A1136 36.134 -0.306 1.670 1.00103.21 N ANISOU 2626 N SER A1136 12349 14926 11939 -1253 681 -368 N ATOM 2627 CA SER A1136 35.510 -0.035 0.364 1.00102.25 C ANISOU 2627 CA SER A1136 12397 14608 11843 -1240 751 -306 C ATOM 2628 C SER A1136 34.982 1.407 0.255 1.00107.08 C ANISOU 2628 C SER A1136 13229 15017 12441 -1422 849 -304 C ATOM 2629 O SER A1136 34.863 2.085 1.285 1.00108.01 O ANISOU 2629 O SER A1136 13386 15107 12545 -1531 848 -338 O ATOM 2630 CB SER A1136 34.357 -1.006 0.140 1.00103.52 C ANISOU 2630 CB SER A1136 12639 14620 12072 -1000 673 -214 C ATOM 2631 OG SER A1136 33.278 -0.732 1.018 1.00110.29 O ANISOU 2631 OG SER A1136 13624 15317 12966 -971 629 -180 O ATOM 2632 N ARG A1137 34.634 1.862 -0.987 1.00102.37 N ANISOU 2632 N ARG A1137 12787 14270 11840 -1440 935 -260 N ATOM 2633 CA ARG A1137 34.060 3.199 -1.224 1.00101.76 C ANISOU 2633 CA ARG A1137 12954 13974 11736 -1574 1039 -242 C ATOM 2634 C ARG A1137 32.631 3.276 -0.659 1.00101.15 C ANISOU 2634 C ARG A1137 13037 13691 11703 -1444 977 -172 C ATOM 2635 O ARG A1137 32.247 4.328 -0.146 1.00100.89 O ANISOU 2635 O ARG A1137 13163 13525 11647 -1554 1031 -178 O ATOM 2636 CB ARG A1137 34.083 3.593 -2.711 1.00103.73 C ANISOU 2636 CB ARG A1137 13329 14130 11956 -1598 1146 -208 C ATOM 2637 CG ARG A1137 35.487 3.886 -3.234 1.00122.12 C ANISOU 2637 CG ARG A1137 15542 16634 14225 -1789 1245 -289 C ATOM 2638 CD ARG A1137 35.489 4.552 -4.605 1.00141.47 C ANISOU 2638 CD ARG A1137 18163 18957 16631 -1853 1379 -258 C ATOM 2639 NE ARG A1137 36.794 4.455 -5.273 1.00156.10 N ANISOU 2639 NE ARG A1137 19864 21008 18438 -1981 1453 -326 N ATOM 2640 CZ ARG A1137 37.811 5.295 -5.087 1.00173.68 C ANISOU 2640 CZ ARG A1137 22057 23336 20599 -2250 1567 -423 C ATOM 2641 NH1 ARG A1137 38.952 5.119 -5.740 1.00162.17 N ANISOU 2641 NH1 ARG A1137 20444 22075 19099 -2352 1631 -485 N ATOM 2642 NH2 ARG A1137 37.698 6.311 -4.239 1.00162.48 N ANISOU 2642 NH2 ARG A1137 20757 21827 19152 -2427 1621 -464 N ATOM 2643 N TRP A1138 31.872 2.143 -0.707 1.00 94.02 N ANISOU 2643 N TRP A1138 12090 12773 10860 -1215 869 -113 N ATOM 2644 CA TRP A1138 30.517 1.977 -0.157 1.00 91.09 C ANISOU 2644 CA TRP A1138 11828 12248 10534 -1075 798 -54 C ATOM 2645 C TRP A1138 30.502 2.415 1.313 1.00 97.84 C ANISOU 2645 C TRP A1138 12674 13113 11388 -1159 767 -92 C ATOM 2646 O TRP A1138 29.643 3.209 1.710 1.00 97.18 O ANISOU 2646 O TRP A1138 12760 12862 11300 -1177 788 -66 O ATOM 2647 CB TRP A1138 30.053 0.505 -0.298 1.00 87.06 C ANISOU 2647 CB TRP A1138 11215 11783 10081 -857 692 -15 C ATOM 2648 CG TRP A1138 28.840 0.126 0.514 1.00 85.65 C ANISOU 2648 CG TRP A1138 11092 11503 9949 -731 610 23 C ATOM 2649 CD1 TRP A1138 27.602 0.699 0.461 1.00 87.75 C ANISOU 2649 CD1 TRP A1138 11532 11590 10220 -686 618 69 C ATOM 2650 CD2 TRP A1138 28.739 -0.957 1.453 1.00 84.37 C ANISOU 2650 CD2 TRP A1138 10813 11417 9826 -622 511 20 C ATOM 2651 NE1 TRP A1138 26.746 0.068 1.337 1.00 85.75 N ANISOU 2651 NE1 TRP A1138 11264 11307 10011 -575 532 87 N ATOM 2652 CE2 TRP A1138 27.415 -0.957 1.954 1.00 86.78 C ANISOU 2652 CE2 TRP A1138 11227 11580 10164 -538 469 59 C ATOM 2653 CE3 TRP A1138 29.641 -1.931 1.922 1.00 85.18 C ANISOU 2653 CE3 TRP A1138 10735 11698 9931 -578 459 -12 C ATOM 2654 CZ2 TRP A1138 26.968 -1.896 2.892 1.00 84.76 C ANISOU 2654 CZ2 TRP A1138 10915 11344 9947 -430 385 67 C ATOM 2655 CZ3 TRP A1138 29.205 -2.843 2.868 1.00 85.55 C ANISOU 2655 CZ3 TRP A1138 10739 11756 10010 -455 375 1 C ATOM 2656 CH2 TRP A1138 27.884 -2.819 3.346 1.00 84.95 C ANISOU 2656 CH2 TRP A1138 10782 11524 9971 -392 343 40 C ATOM 2657 N TYR A1139 31.498 1.933 2.095 1.00 97.03 N ANISOU 2657 N TYR A1139 12373 13216 11278 -1207 722 -155 N ATOM 2658 CA TYR A1139 31.662 2.262 3.505 1.00 97.97 C ANISOU 2658 CA TYR A1139 12452 13388 11386 -1289 687 -204 C ATOM 2659 C TYR A1139 31.960 3.747 3.696 1.00102.68 C ANISOU 2659 C TYR A1139 13173 13916 11925 -1528 797 -255 C ATOM 2660 O TYR A1139 31.334 4.358 4.547 1.00101.66 O ANISOU 2660 O TYR A1139 13159 13671 11795 -1563 794 -252 O ATOM 2661 CB TYR A1139 32.762 1.406 4.166 1.00100.73 C ANISOU 2661 CB TYR A1139 12550 14005 11719 -1274 618 -264 C ATOM 2662 CG TYR A1139 32.801 1.576 5.670 1.00104.51 C ANISOU 2662 CG TYR A1139 12981 14543 12184 -1317 562 -306 C ATOM 2663 CD1 TYR A1139 31.910 0.892 6.492 1.00105.69 C ANISOU 2663 CD1 TYR A1139 13153 14625 12380 -1150 468 -256 C ATOM 2664 CD2 TYR A1139 33.687 2.470 6.269 1.00107.38 C ANISOU 2664 CD2 TYR A1139 13291 15026 12484 -1539 613 -401 C ATOM 2665 CE1 TYR A1139 31.889 1.097 7.872 1.00106.97 C ANISOU 2665 CE1 TYR A1139 13289 14829 12526 -1188 420 -290 C ATOM 2666 CE2 TYR A1139 33.690 2.669 7.651 1.00108.91 C ANISOU 2666 CE2 TYR A1139 13448 15274 12659 -1582 562 -443 C ATOM 2667 CZ TYR A1139 32.791 1.975 8.449 1.00115.89 C ANISOU 2667 CZ TYR A1139 14359 16084 13591 -1398 463 -383 C ATOM 2668 OH TYR A1139 32.791 2.146 9.812 1.00119.79 O ANISOU 2668 OH TYR A1139 14820 16633 14062 -1431 412 -422 O ATOM 2669 N ASN A1140 32.891 4.327 2.908 1.00101.20 N ANISOU 2669 N ASN A1140 12976 13791 11685 -1696 904 -304 N ATOM 2670 CA ASN A1140 33.286 5.744 3.008 1.00102.71 C ANISOU 2670 CA ASN A1140 13301 13914 11811 -1952 1034 -365 C ATOM 2671 C ASN A1140 32.145 6.719 2.628 1.00106.17 C ANISOU 2671 C ASN A1140 14047 14051 12242 -1940 1113 -294 C ATOM 2672 O ASN A1140 32.009 7.762 3.276 1.00106.40 O ANISOU 2672 O ASN A1140 14222 13973 12232 -2086 1179 -326 O ATOM 2673 CB ASN A1140 34.529 6.027 2.158 1.00104.43 C ANISOU 2673 CB ASN A1140 13434 14272 11972 -2129 1138 -433 C ATOM 2674 CG ASN A1140 35.708 5.120 2.452 1.00131.75 C ANISOU 2674 CG ASN A1140 16585 18054 15422 -2131 1069 -507 C ATOM 2675 OD1 ASN A1140 35.923 4.657 3.589 1.00126.16 O ANISOU 2675 OD1 ASN A1140 15723 17494 14717 -2095 972 -546 O ATOM 2676 ND2 ASN A1140 36.507 4.849 1.426 1.00125.14 N ANISOU 2676 ND2 ASN A1140 15649 17339 14561 -2160 1120 -528 N ATOM 2677 N GLN A1141 31.321 6.367 1.614 1.00101.12 N ANISOU 2677 N GLN A1141 13506 13285 11632 -1758 1104 -202 N ATOM 2678 CA GLN A1141 30.199 7.196 1.160 1.00100.35 C ANISOU 2678 CA GLN A1141 13687 12927 11514 -1700 1168 -128 C ATOM 2679 C GLN A1141 29.045 7.182 2.175 1.00101.80 C ANISOU 2679 C GLN A1141 13944 13004 11733 -1577 1086 -89 C ATOM 2680 O GLN A1141 28.677 8.247 2.677 1.00102.20 O ANISOU 2680 O GLN A1141 14181 12906 11742 -1664 1154 -93 O ATOM 2681 CB GLN A1141 29.727 6.760 -0.230 1.00101.39 C ANISOU 2681 CB GLN A1141 13870 13000 11654 -1537 1174 -53 C ATOM 2682 CG GLN A1141 30.561 7.394 -1.347 1.00128.03 C ANISOU 2682 CG GLN A1141 17316 16367 14963 -1684 1315 -73 C ATOM 2683 CD GLN A1141 30.274 6.858 -2.732 1.00155.53 C ANISOU 2683 CD GLN A1141 20815 19830 18450 -1530 1316 -9 C ATOM 2684 OE1 GLN A1141 29.184 6.353 -3.030 1.00155.25 O ANISOU 2684 OE1 GLN A1141 20822 19719 18446 -1315 1240 63 O ATOM 2685 NE2 GLN A1141 31.246 6.990 -3.627 1.00146.02 N ANISOU 2685 NE2 GLN A1141 19577 18699 17205 -1646 1408 -40 N ATOM 2686 N THR A1142 28.512 5.989 2.511 1.00 95.77 N ANISOU 2686 N THR A1142 13038 12312 11039 -1386 949 -56 N ATOM 2687 CA THR A1142 27.426 5.837 3.490 1.00 93.84 C ANISOU 2687 CA THR A1142 12837 11987 10830 -1267 867 -23 C ATOM 2688 C THR A1142 27.886 4.929 4.662 1.00 97.08 C ANISOU 2688 C THR A1142 13032 12573 11283 -1257 758 -68 C ATOM 2689 O THR A1142 27.511 3.753 4.696 1.00 96.38 O ANISOU 2689 O THR A1142 12829 12543 11247 -1090 660 -37 O ATOM 2690 CB THR A1142 26.173 5.296 2.812 1.00 96.99 C ANISOU 2690 CB THR A1142 13301 12290 11262 -1043 817 59 C ATOM 2691 OG1 THR A1142 26.496 4.058 2.186 1.00 94.18 O ANISOU 2691 OG1 THR A1142 12772 12064 10947 -945 754 65 O ATOM 2692 CG2 THR A1142 25.578 6.266 1.810 1.00 95.02 C ANISOU 2692 CG2 THR A1142 13282 11867 10955 -1021 916 109 C ATOM 2693 N PRO A1143 28.664 5.452 5.643 1.00 93.86 N ANISOU 2693 N PRO A1143 12574 12246 10842 -1431 776 -144 N ATOM 2694 CA PRO A1143 29.171 4.585 6.725 1.00 93.20 C ANISOU 2694 CA PRO A1143 12282 12349 10781 -1405 673 -186 C ATOM 2695 C PRO A1143 28.172 4.130 7.790 1.00 95.10 C ANISOU 2695 C PRO A1143 12538 12531 11065 -1267 578 -150 C ATOM 2696 O PRO A1143 28.384 3.049 8.332 1.00 94.17 O ANISOU 2696 O PRO A1143 12258 12546 10975 -1165 484 -153 O ATOM 2697 CB PRO A1143 30.256 5.440 7.377 1.00 96.62 C ANISOU 2697 CB PRO A1143 12672 12889 11151 -1648 733 -286 C ATOM 2698 CG PRO A1143 29.842 6.838 7.107 1.00101.95 C ANISOU 2698 CG PRO A1143 13599 13353 11783 -1780 857 -282 C ATOM 2699 CD PRO A1143 29.231 6.812 5.744 1.00 97.03 C ANISOU 2699 CD PRO A1143 13102 12593 11174 -1666 901 -202 C ATOM 2700 N ASN A1144 27.143 4.933 8.136 1.00 91.36 N ANISOU 2700 N ASN A1144 12258 11867 10588 -1261 606 -117 N ATOM 2701 CA ASN A1144 26.186 4.567 9.195 1.00 90.58 C ANISOU 2701 CA ASN A1144 12175 11717 10525 -1143 523 -88 C ATOM 2702 C ASN A1144 25.268 3.408 8.751 1.00 91.56 C ANISOU 2702 C ASN A1144 12263 11816 10709 -924 449 -20 C ATOM 2703 O ASN A1144 24.819 2.622 9.594 1.00 91.17 O ANISOU 2703 O ASN A1144 12149 11796 10695 -822 366 -8 O ATOM 2704 CB ASN A1144 25.365 5.782 9.673 1.00 94.35 C ANISOU 2704 CB ASN A1144 12868 12008 10973 -1194 581 -77 C ATOM 2705 N ARG A1145 25.027 3.293 7.433 1.00 85.74 N ANISOU 2705 N ARG A1145 11569 11029 9977 -862 483 19 N ATOM 2706 CA ARG A1145 24.242 2.218 6.816 1.00 82.99 C ANISOU 2706 CA ARG A1145 11186 10670 9676 -680 427 70 C ATOM 2707 C ARG A1145 25.151 1.010 6.542 1.00 83.06 C ANISOU 2707 C ARG A1145 11008 10844 9708 -641 381 51 C ATOM 2708 O ARG A1145 24.702 -0.127 6.668 1.00 82.45 O ANISOU 2708 O ARG A1145 10865 10791 9671 -506 315 73 O ATOM 2709 CB ARG A1145 23.602 2.715 5.509 1.00 83.04 C ANISOU 2709 CB ARG A1145 11327 10561 9662 -631 487 113 C ATOM 2710 CG ARG A1145 22.561 1.768 4.943 1.00 85.71 C ANISOU 2710 CG ARG A1145 11649 10879 10039 -453 432 156 C ATOM 2711 CD ARG A1145 22.405 1.983 3.456 1.00 87.25 C ANISOU 2711 CD ARG A1145 11912 11034 10206 -412 484 185 C ATOM 2712 NE ARG A1145 21.620 0.920 2.827 1.00 86.46 N ANISOU 2712 NE ARG A1145 11760 10954 10138 -262 429 207 N ATOM 2713 CZ ARG A1145 20.725 1.128 1.871 1.00 99.47 C ANISOU 2713 CZ ARG A1145 13496 12541 11759 -167 447 240 C ATOM 2714 NH1 ARG A1145 20.489 2.356 1.429 1.00 86.70 N ANISOU 2714 NH1 ARG A1145 12038 10826 10079 -186 519 264 N ATOM 2715 NH2 ARG A1145 20.059 0.112 1.346 1.00 92.99 N ANISOU 2715 NH2 ARG A1145 12612 11757 10963 -51 398 245 N ATOM 2716 N ALA A1146 26.410 1.258 6.116 1.00 76.58 N ANISOU 2716 N ALA A1146 10110 10132 8852 -757 427 9 N ATOM 2717 CA ALA A1146 27.357 0.188 5.838 1.00 74.67 C ANISOU 2717 CA ALA A1146 9691 10062 8618 -712 391 -11 C ATOM 2718 C ALA A1146 27.739 -0.580 7.114 1.00 77.74 C ANISOU 2718 C ALA A1146 9949 10577 9013 -667 311 -37 C ATOM 2719 O ALA A1146 27.799 -1.806 7.048 1.00 77.84 O ANISOU 2719 O ALA A1146 9871 10657 9049 -529 257 -19 O ATOM 2720 CB ALA A1146 28.592 0.724 5.142 1.00 76.11 C ANISOU 2720 CB ALA A1146 9817 10348 8754 -856 465 -58 C ATOM 2721 N ALYS A1147 27.951 0.103 8.264 0.50 74.36 N ANISOU 2721 N ALYS A1147 9523 10172 8557 -772 306 -76 N ATOM 2722 N BLYS A1147 27.930 0.115 8.260 0.50 74.25 N ANISOU 2722 N BLYS A1147 9513 10155 8545 -771 307 -75 N ATOM 2723 CA ALYS A1147 28.311 -0.607 9.495 0.50 74.15 C ANISOU 2723 CA ALYS A1147 9377 10273 8525 -716 228 -98 C ATOM 2724 CA BLYS A1147 28.282 -0.527 9.529 0.50 74.03 C ANISOU 2724 CA BLYS A1147 9370 10251 8508 -724 231 -99 C ATOM 2725 C ALYS A1147 27.111 -1.405 10.051 0.50 76.33 C ANISOU 2725 C ALYS A1147 9714 10438 8849 -553 167 -42 C ATOM 2726 C BLYS A1147 27.114 -1.383 10.054 0.50 76.28 C ANISOU 2726 C BLYS A1147 9708 10431 8843 -555 168 -42 C ATOM 2727 O ALYS A1147 27.338 -2.416 10.707 0.50 76.27 O ANISOU 2727 O ALYS A1147 9615 10522 8841 -444 106 -39 O ATOM 2728 O BLYS A1147 27.363 -2.394 10.704 0.50 76.24 O ANISOU 2728 O BLYS A1147 9610 10520 8836 -448 106 -40 O ATOM 2729 CB ALYS A1147 28.961 0.300 10.568 0.50 77.75 C ANISOU 2729 CB ALYS A1147 9802 10814 8928 -879 238 -168 C ATOM 2730 CB BLYS A1147 28.767 0.490 10.595 0.50 77.41 C ANISOU 2730 CB BLYS A1147 9794 10731 8888 -891 246 -164 C ATOM 2731 CG ALYS A1147 28.070 1.346 11.219 0.50 94.50 C ANISOU 2731 CG ALYS A1147 12091 12764 11052 -957 265 -162 C ATOM 2732 CG BLYS A1147 27.697 1.412 11.175 0.50 93.82 C ANISOU 2732 CG BLYS A1147 12052 12619 10977 -937 267 -144 C ATOM 2733 CD ALYS A1147 28.754 1.979 12.435 0.50107.49 C ANISOU 2733 CD ALYS A1147 13682 14518 12641 -1099 258 -238 C ATOM 2734 CD BLYS A1147 28.159 2.089 12.462 0.50104.73 C ANISOU 2734 CD BLYS A1147 13410 14071 12311 -1068 260 -210 C ATOM 2735 CE ALYS A1147 29.603 3.186 12.093 0.50119.59 C ANISOU 2735 CE ALYS A1147 15236 16087 14116 -1334 354 -312 C ATOM 2736 CE BLYS A1147 27.004 2.587 13.309 0.50109.20 C ANISOU 2736 CE BLYS A1147 14128 14468 12894 -1048 251 -181 C ATOM 2737 NZ ALYS A1147 30.227 3.781 13.305 0.50127.88 N ANISOU 2737 NZ ALYS A1147 16230 17252 15106 -1484 348 -398 N ATOM 2738 NZ BLYS A1147 26.346 3.786 12.722 0.50113.55 N ANISOU 2738 NZ BLYS A1147 14883 14823 13440 -1130 342 -163 N ATOM 2739 N ARG A1148 25.860 -0.994 9.743 1.00 71.47 N ANISOU 2739 N ARG A1148 9251 9636 8267 -528 188 2 N ATOM 2740 CA ARG A1148 24.640 -1.708 10.152 1.00 70.55 C ANISOU 2740 CA ARG A1148 9191 9419 8194 -392 142 46 C ATOM 2741 C ARG A1148 24.509 -3.021 9.387 1.00 76.02 C ANISOU 2741 C ARG A1148 9833 10133 8917 -255 120 74 C ATOM 2742 O ARG A1148 24.229 -4.046 10.018 1.00 76.27 O ANISOU 2742 O ARG A1148 9836 10176 8966 -149 74 88 O ATOM 2743 CB ARG A1148 23.383 -0.862 9.931 1.00 70.82 C ANISOU 2743 CB ARG A1148 9385 9281 8241 -400 175 76 C ATOM 2744 CG ARG A1148 23.054 0.077 11.081 1.00 76.08 C ANISOU 2744 CG ARG A1148 10130 9889 8888 -476 178 61 C ATOM 2745 CD ARG A1148 21.573 0.426 11.103 1.00 79.21 C ANISOU 2745 CD ARG A1148 10661 10133 9302 -408 185 99 C ATOM 2746 NE ARG A1148 21.164 1.229 9.947 1.00 82.44 N ANISOU 2746 NE ARG A1148 11180 10450 9692 -418 247 120 N ATOM 2747 CZ ARG A1148 21.243 2.550 9.885 1.00 99.88 C ANISOU 2747 CZ ARG A1148 13513 12582 11857 -516 314 113 C ATOM 2748 NH1 ARG A1148 20.860 3.191 8.790 1.00 92.93 N ANISOU 2748 NH1 ARG A1148 12744 11615 10949 -499 375 141 N ATOM 2749 NH2 ARG A1148 21.722 3.244 10.911 1.00 94.50 N ANISOU 2749 NH2 ARG A1148 12853 11905 11148 -632 328 76 N ATOM 2750 N VAL A1149 24.724 -2.989 8.029 1.00 72.20 N ANISOU 2750 N VAL A1149 9350 9648 8434 -259 161 81 N ATOM 2751 CA VAL A1149 24.695 -4.159 7.130 1.00 71.01 C ANISOU 2751 CA VAL A1149 9157 9518 8305 -145 152 100 C ATOM 2752 C VAL A1149 25.912 -5.077 7.500 1.00 74.69 C ANISOU 2752 C VAL A1149 9483 10148 8749 -97 123 79 C ATOM 2753 O VAL A1149 25.735 -6.301 7.619 1.00 73.51 O ANISOU 2753 O VAL A1149 9314 10004 8614 31 94 97 O ATOM 2754 CB VAL A1149 24.657 -3.771 5.603 1.00 74.37 C ANISOU 2754 CB VAL A1149 9623 9909 8727 -168 206 110 C ATOM 2755 CG1 VAL A1149 24.681 -5.005 4.699 1.00 73.64 C ANISOU 2755 CG1 VAL A1149 9484 9844 8651 -56 197 122 C ATOM 2756 CG2 VAL A1149 23.450 -2.900 5.262 1.00 73.37 C ANISOU 2756 CG2 VAL A1149 9637 9638 8604 -181 232 134 C ATOM 2757 N ILE A1150 27.116 -4.480 7.735 1.00 71.19 N ANISOU 2757 N ILE A1150 8947 9841 8261 -197 134 38 N ATOM 2758 CA ILE A1150 28.319 -5.248 8.128 1.00 71.87 C ANISOU 2758 CA ILE A1150 8882 10117 8307 -142 103 11 C ATOM 2759 C ILE A1150 28.097 -5.925 9.522 1.00 79.14 C ANISOU 2759 C ILE A1150 9792 11056 9220 -44 42 20 C ATOM 2760 O ILE A1150 28.439 -7.106 9.659 1.00 80.30 O ANISOU 2760 O ILE A1150 9886 11273 9353 101 14 35 O ATOM 2761 CB ILE A1150 29.635 -4.403 8.068 1.00 75.01 C ANISOU 2761 CB ILE A1150 9167 10684 8648 -288 133 -51 C ATOM 2762 CG1 ILE A1150 30.025 -4.093 6.609 1.00 74.18 C ANISOU 2762 CG1 ILE A1150 9059 10584 8542 -348 197 -56 C ATOM 2763 CG2 ILE A1150 30.805 -5.083 8.798 1.00 76.04 C ANISOU 2763 CG2 ILE A1150 9127 11045 8721 -223 86 -87 C ATOM 2764 CD1 ILE A1150 30.861 -2.862 6.439 1.00 75.97 C ANISOU 2764 CD1 ILE A1150 9252 10889 8723 -550 258 -114 C ATOM 2765 N THR A1151 27.481 -5.216 10.521 1.00 75.85 N ANISOU 2765 N THR A1151 9444 10565 8810 -111 27 17 N ATOM 2766 CA THR A1151 27.204 -5.803 11.850 1.00 75.21 C ANISOU 2766 CA THR A1151 9367 10490 8719 -22 -25 28 C ATOM 2767 C THR A1151 26.223 -6.985 11.704 1.00 78.72 C ANISOU 2767 C THR A1151 9896 10808 9206 127 -33 80 C ATOM 2768 O THR A1151 26.416 -7.995 12.377 1.00 79.89 O ANISOU 2768 O THR A1151 10023 11000 9331 253 -62 94 O ATOM 2769 CB THR A1151 26.722 -4.745 12.856 1.00 81.32 C ANISOU 2769 CB THR A1151 10204 11203 9490 -133 -31 12 C ATOM 2770 OG1 THR A1151 27.758 -3.782 13.012 1.00 81.28 O ANISOU 2770 OG1 THR A1151 10116 11331 9434 -279 -17 -49 O ATOM 2771 CG2 THR A1151 26.389 -5.330 14.228 1.00 78.45 C ANISOU 2771 CG2 THR A1151 9853 10840 9113 -41 -82 25 C ATOM 2772 N THR A1152 25.218 -6.879 10.799 1.00 73.11 N ANISOU 2772 N THR A1152 9280 9951 8546 114 0 103 N ATOM 2773 CA THR A1152 24.250 -7.948 10.507 1.00 71.68 C ANISOU 2773 CA THR A1152 9175 9657 8402 223 5 135 C ATOM 2774 C THR A1152 24.985 -9.181 9.933 1.00 75.98 C ANISOU 2774 C THR A1152 9666 10276 8928 341 10 141 C ATOM 2775 O THR A1152 24.568 -10.313 10.180 1.00 75.61 O ANISOU 2775 O THR A1152 9671 10172 8885 451 11 162 O ATOM 2776 CB THR A1152 23.164 -7.429 9.542 1.00 75.25 C ANISOU 2776 CB THR A1152 9713 9985 8896 174 36 143 C ATOM 2777 OG1 THR A1152 22.642 -6.207 10.047 1.00 79.87 O ANISOU 2777 OG1 THR A1152 10350 10514 9483 79 38 138 O ATOM 2778 CG2 THR A1152 22.023 -8.420 9.316 1.00 66.21 C ANISOU 2778 CG2 THR A1152 8639 8733 7782 255 44 158 C ATOM 2779 N PHE A1153 26.067 -8.962 9.167 1.00 72.98 N ANISOU 2779 N PHE A1153 9190 10016 8521 316 22 123 N ATOM 2780 CA PHE A1153 26.835 -10.071 8.597 1.00 73.02 C ANISOU 2780 CA PHE A1153 9141 10104 8501 436 30 128 C ATOM 2781 C PHE A1153 27.689 -10.749 9.678 1.00 79.78 C ANISOU 2781 C PHE A1153 9928 11088 9295 548 -6 128 C ATOM 2782 O PHE A1153 27.896 -11.958 9.618 1.00 80.72 O ANISOU 2782 O PHE A1153 10065 11214 9391 699 1 149 O ATOM 2783 CB PHE A1153 27.731 -9.612 7.424 1.00 74.32 C ANISOU 2783 CB PHE A1153 9217 10370 8650 377 58 105 C ATOM 2784 CG PHE A1153 27.090 -9.424 6.063 1.00 74.27 C ANISOU 2784 CG PHE A1153 9276 10258 8684 336 99 114 C ATOM 2785 CD1 PHE A1153 26.334 -10.441 5.480 1.00 75.87 C ANISOU 2785 CD1 PHE A1153 9557 10356 8913 430 114 134 C ATOM 2786 CD2 PHE A1153 27.341 -8.277 5.310 1.00 74.84 C ANISOU 2786 CD2 PHE A1153 9333 10348 8755 206 131 97 C ATOM 2787 CE1 PHE A1153 25.785 -10.282 4.200 1.00 75.13 C ANISOU 2787 CE1 PHE A1153 9510 10191 8845 398 147 135 C ATOM 2788 CE2 PHE A1153 26.786 -8.117 4.038 1.00 75.75 C ANISOU 2788 CE2 PHE A1153 9511 10378 8895 188 168 108 C ATOM 2789 CZ PHE A1153 26.006 -9.115 3.496 1.00 73.30 C ANISOU 2789 CZ PHE A1153 9261 9980 8609 287 170 126 C ATOM 2790 N ARG A1154 28.182 -9.977 10.645 1.00 77.34 N ANISOU 2790 N ARG A1154 9551 10883 8953 480 -39 102 N ATOM 2791 CA ARG A1154 29.052 -10.475 11.713 1.00 78.67 C ANISOU 2791 CA ARG A1154 9636 11208 9046 586 -80 95 C ATOM 2792 C ARG A1154 28.304 -11.311 12.746 1.00 86.82 C ANISOU 2792 C ARG A1154 10779 12133 10076 707 -96 135 C ATOM 2793 O ARG A1154 28.880 -12.262 13.286 1.00 88.79 O ANISOU 2793 O ARG A1154 11009 12467 10261 871 -112 151 O ATOM 2794 CB ARG A1154 29.754 -9.307 12.428 1.00 75.92 C ANISOU 2794 CB ARG A1154 9179 11010 8657 451 -108 43 C ATOM 2795 CG ARG A1154 30.829 -8.607 11.591 1.00 80.25 C ANISOU 2795 CG ARG A1154 9592 11721 9179 339 -87 -9 C ATOM 2796 CD ARG A1154 32.093 -8.352 12.393 1.00 88.54 C ANISOU 2796 CD ARG A1154 10470 13035 10136 325 -124 -67 C ATOM 2797 NE ARG A1154 31.927 -7.262 13.356 1.00 96.77 N ANISOU 2797 NE ARG A1154 11518 14082 11170 171 -141 -107 N ATOM 2798 CZ ARG A1154 32.024 -7.392 14.675 1.00107.76 C ANISOU 2798 CZ ARG A1154 12884 15550 12511 225 -193 -116 C ATOM 2799 NH1 ARG A1154 32.314 -8.571 15.215 1.00 93.50 N ANISOU 2799 NH1 ARG A1154 11049 13827 10652 442 -233 -85 N ATOM 2800 NH2 ARG A1154 31.845 -6.344 15.464 1.00 95.33 N ANISOU 2800 NH2 ARG A1154 11323 13968 10931 70 -201 -156 N ATOM 2801 N THR A1155 27.040 -10.950 13.036 1.00 83.36 N ANISOU 2801 N THR A1155 10460 11514 9698 632 -87 150 N ATOM 2802 CA THR A1155 26.246 -11.582 14.091 1.00 82.85 C ANISOU 2802 CA THR A1155 10505 11341 9632 712 -94 181 C ATOM 2803 C THR A1155 25.087 -12.449 13.598 1.00 86.45 C ANISOU 2803 C THR A1155 11103 11605 10140 756 -47 210 C ATOM 2804 O THR A1155 24.681 -13.364 14.311 1.00 86.61 O ANISOU 2804 O THR A1155 11217 11550 10141 858 -35 236 O ATOM 2805 CB THR A1155 25.688 -10.506 15.030 1.00 89.82 C ANISOU 2805 CB THR A1155 11409 12188 10532 591 -118 166 C ATOM 2806 OG1 THR A1155 24.681 -9.749 14.346 1.00 92.77 O ANISOU 2806 OG1 THR A1155 11846 12425 10976 466 -91 162 O ATOM 2807 CG2 THR A1155 26.779 -9.585 15.585 1.00 86.60 C ANISOU 2807 CG2 THR A1155 10868 11968 10068 516 -158 123 C ATOM 2808 N GLY A1156 24.527 -12.129 12.442 1.00 83.56 N ANISOU 2808 N GLY A1156 10756 11161 9830 673 -18 200 N ATOM 2809 CA GLY A1156 23.373 -12.852 11.915 1.00 83.76 C ANISOU 2809 CA GLY A1156 10899 11026 9900 689 26 210 C ATOM 2810 C GLY A1156 22.135 -12.611 12.765 1.00 90.00 C ANISOU 2810 C GLY A1156 11779 11698 10720 636 26 213 C ATOM 2811 O GLY A1156 21.322 -13.522 12.962 1.00 90.28 O ANISOU 2811 O GLY A1156 11917 11621 10764 679 62 221 O ATOM 2812 N THR A1157 22.035 -11.391 13.344 1.00 86.92 N ANISOU 2812 N THR A1157 11354 11336 10338 540 -7 203 N ATOM 2813 CA THR A1157 20.944 -10.950 14.222 1.00 86.27 C ANISOU 2813 CA THR A1157 11341 11161 10278 486 -11 204 C ATOM 2814 C THR A1157 20.420 -9.605 13.740 1.00 90.74 C ANISOU 2814 C THR A1157 11896 11705 10876 365 -15 187 C ATOM 2815 O THR A1157 21.016 -9.012 12.844 1.00 91.15 O ANISOU 2815 O THR A1157 11892 11814 10928 320 -13 177 O ATOM 2816 CB THR A1157 21.410 -10.853 15.693 1.00 92.01 C ANISOU 2816 CB THR A1157 12057 11944 10959 519 -47 213 C ATOM 2817 OG1 THR A1157 22.439 -9.873 15.809 1.00 89.68 O ANISOU 2817 OG1 THR A1157 11657 11781 10635 460 -83 193 O ATOM 2818 CG2 THR A1157 21.863 -12.193 16.278 1.00 90.27 C ANISOU 2818 CG2 THR A1157 11873 11737 10690 667 -38 238 C ATOM 2819 N TRP A1158 19.310 -9.128 14.325 1.00 86.36 N ANISOU 2819 N TRP A1158 11405 11067 10342 320 -14 185 N ATOM 2820 CA TRP A1158 18.720 -7.832 13.995 1.00 84.88 C ANISOU 2820 CA TRP A1158 11232 10848 10172 231 -12 175 C ATOM 2821 C TRP A1158 19.144 -6.762 15.021 1.00 86.93 C ANISOU 2821 C TRP A1158 11483 11141 10407 168 -38 169 C ATOM 2822 O TRP A1158 18.521 -5.708 15.083 1.00 86.32 O ANISOU 2822 O TRP A1158 11449 11013 10334 105 -30 164 O ATOM 2823 CB TRP A1158 17.189 -7.950 13.942 1.00 82.90 C ANISOU 2823 CB TRP A1158 11050 10499 9948 230 8 170 C ATOM 2824 CG TRP A1158 16.655 -8.735 12.783 1.00 83.35 C ANISOU 2824 CG TRP A1158 11113 10531 10024 259 37 159 C ATOM 2825 CD1 TRP A1158 15.970 -9.913 12.838 1.00 86.20 C ANISOU 2825 CD1 TRP A1158 11512 10844 10395 295 65 148 C ATOM 2826 CD2 TRP A1158 16.698 -8.360 11.399 1.00 83.11 C ANISOU 2826 CD2 TRP A1158 11058 10521 9999 243 49 152 C ATOM 2827 NE1 TRP A1158 15.605 -10.310 11.573 1.00 85.48 N ANISOU 2827 NE1 TRP A1158 11414 10752 10315 296 89 127 N ATOM 2828 CE2 TRP A1158 16.042 -9.377 10.669 1.00 86.85 C ANISOU 2828 CE2 TRP A1158 11546 10970 10485 273 76 132 C ATOM 2829 CE3 TRP A1158 17.260 -7.278 10.696 1.00 84.26 C ANISOU 2829 CE3 TRP A1158 11180 10701 10133 201 47 157 C ATOM 2830 CZ2 TRP A1158 15.928 -9.343 9.274 1.00 86.08 C ANISOU 2830 CZ2 TRP A1158 11427 10891 10387 274 90 119 C ATOM 2831 CZ3 TRP A1158 17.124 -7.232 9.319 1.00 85.69 C ANISOU 2831 CZ3 TRP A1158 11352 10891 10314 207 66 151 C ATOM 2832 CH2 TRP A1158 16.476 -8.261 8.620 1.00 86.25 C ANISOU 2832 CH2 TRP A1158 11426 10949 10398 248 82 133 C ATOM 2833 N ASP A1159 20.218 -7.024 15.802 1.00 83.69 N ANISOU 2833 N ASP A1159 11015 10824 9958 191 -65 167 N ATOM 2834 CA ASP A1159 20.728 -6.150 16.865 1.00 84.32 C ANISOU 2834 CA ASP A1159 11075 10960 10004 128 -92 150 C ATOM 2835 C ASP A1159 21.137 -4.758 16.392 1.00 87.69 C ANISOU 2835 C ASP A1159 11488 11409 10421 3 -77 124 C ATOM 2836 O ASP A1159 21.050 -3.824 17.189 1.00 87.91 O ANISOU 2836 O ASP A1159 11547 11424 10430 -72 -82 107 O ATOM 2837 CB ASP A1159 21.920 -6.789 17.613 1.00 87.85 C ANISOU 2837 CB ASP A1159 11439 11542 10396 191 -127 144 C ATOM 2838 CG ASP A1159 21.586 -7.976 18.515 1.00105.58 C ANISOU 2838 CG ASP A1159 13731 13758 12627 315 -137 173 C ATOM 2839 OD1 ASP A1159 20.373 -8.233 18.748 1.00106.04 O ANISOU 2839 OD1 ASP A1159 13885 13687 12720 326 -115 190 O ATOM 2840 OD2 ASP A1159 22.541 -8.643 19.003 1.00114.09 O ANISOU 2840 OD2 ASP A1159 14752 14949 13649 405 -162 176 O ATOM 2841 N ALA A1160 21.604 -4.602 15.140 1.00 83.54 N ANISOU 2841 N ALA A1160 10928 10912 9903 -25 -52 119 N ATOM 2842 CA ALA A1160 22.013 -3.280 14.646 1.00 83.15 C ANISOU 2842 CA ALA A1160 10888 10869 9837 -151 -21 94 C ATOM 2843 C ALA A1160 20.803 -2.423 14.269 1.00 86.80 C ANISOU 2843 C ALA A1160 11473 11187 10321 -179 13 111 C ATOM 2844 O ALA A1160 20.918 -1.196 14.282 1.00 86.93 O ANISOU 2844 O ALA A1160 11545 11171 10312 -280 45 95 O ATOM 2845 CB ALA A1160 22.956 -3.419 13.463 1.00 84.06 C ANISOU 2845 CB ALA A1160 10928 11066 9944 -169 1 84 C ATOM 2846 N TYR A1161 19.639 -3.067 13.987 1.00 83.19 N ANISOU 2846 N TYR A1161 11060 10650 9898 -89 11 138 N ATOM 2847 CA TYR A1161 18.377 -2.429 13.570 1.00 82.92 C ANISOU 2847 CA TYR A1161 11124 10508 9875 -79 37 152 C ATOM 2848 C TYR A1161 17.392 -2.248 14.746 1.00 87.16 C ANISOU 2848 C TYR A1161 11722 10983 10414 -61 22 156 C ATOM 2849 O TYR A1161 16.251 -1.822 14.563 1.00 86.23 O ANISOU 2849 O TYR A1161 11673 10793 10297 -32 38 165 O ATOM 2850 CB TYR A1161 17.755 -3.232 12.413 1.00 83.55 C ANISOU 2850 CB TYR A1161 11193 10572 9980 -3 45 165 C ATOM 2851 CG TYR A1161 18.550 -3.040 11.139 1.00 85.54 C ANISOU 2851 CG TYR A1161 11415 10864 10222 -28 71 164 C ATOM 2852 CD1 TYR A1161 19.676 -3.816 10.871 1.00 87.64 C ANISOU 2852 CD1 TYR A1161 11589 11220 10489 -22 61 156 C ATOM 2853 CD2 TYR A1161 18.248 -2.007 10.257 1.00 86.64 C ANISOU 2853 CD2 TYR A1161 11626 10954 10340 -55 110 172 C ATOM 2854 CE1 TYR A1161 20.473 -3.575 9.751 1.00 88.28 C ANISOU 2854 CE1 TYR A1161 11639 11347 10558 -55 89 152 C ATOM 2855 CE2 TYR A1161 19.022 -1.775 9.119 1.00 87.86 C ANISOU 2855 CE2 TYR A1161 11763 11140 10479 -87 142 172 C ATOM 2856 CZ TYR A1161 20.135 -2.560 8.871 1.00 92.10 C ANISOU 2856 CZ TYR A1161 12197 11772 11024 -94 131 160 C ATOM 2857 OH TYR A1161 20.900 -2.314 7.758 1.00 89.80 O ANISOU 2857 OH TYR A1161 11885 11518 10715 -130 167 157 O ATOM 2858 N LYS A 263 17.898 -2.491 15.955 1.00 84.88 N ANISOU 2858 N LYS A 263 11402 10736 10115 -76 -7 146 N ATOM 2859 CA LYS A 263 17.251 -2.383 17.260 1.00 84.69 C ANISOU 2859 CA LYS A 263 11423 10672 10085 -67 -23 146 C ATOM 2860 C LYS A 263 16.903 -0.915 17.580 1.00 88.25 C ANISOU 2860 C LYS A 263 11965 11058 10510 -137 2 138 C ATOM 2861 O LYS A 263 17.788 -0.044 17.574 1.00 88.29 O ANISOU 2861 O LYS A 263 11977 11087 10484 -231 18 117 O ATOM 2862 CB LYS A 263 18.244 -2.925 18.308 1.00 88.46 C ANISOU 2862 CB LYS A 263 11833 11238 10539 -67 -60 134 C ATOM 2863 CG LYS A 263 17.674 -3.573 19.550 1.00103.17 C ANISOU 2863 CG LYS A 263 13720 13078 12400 -9 -82 144 C ATOM 2864 CD LYS A 263 18.808 -3.852 20.546 1.00109.62 C ANISOU 2864 CD LYS A 263 14474 14003 13173 -7 -120 131 C ATOM 2865 CE LYS A 263 19.155 -5.319 20.635 1.00122.01 C ANISOU 2865 CE LYS A 263 16002 15620 14738 105 -136 152 C ATOM 2866 NZ LYS A 263 20.132 -5.585 21.725 1.00132.25 N ANISOU 2866 NZ LYS A 263 17244 17031 15975 137 -176 142 N ATOM 2867 N PHE A 264 15.598 -0.664 17.854 1.00 83.18 N ANISOU 2867 N PHE A 264 11397 10334 9873 -92 12 150 N ATOM 2868 CA PHE A 264 14.973 0.608 18.265 1.00 81.48 C ANISOU 2868 CA PHE A 264 11291 10041 9628 -120 40 149 C ATOM 2869 C PHE A 264 15.227 1.731 17.256 1.00 88.56 C ANISOU 2869 C PHE A 264 12260 10894 10496 -165 89 151 C ATOM 2870 O PHE A 264 15.430 2.898 17.636 1.00 89.25 O ANISOU 2870 O PHE A 264 12441 10927 10543 -236 123 140 O ATOM 2871 CB PHE A 264 15.414 1.016 19.690 1.00 81.71 C ANISOU 2871 CB PHE A 264 11338 10076 9631 -183 24 129 C ATOM 2872 CG PHE A 264 15.192 -0.066 20.723 1.00 80.72 C ANISOU 2872 CG PHE A 264 11160 9988 9523 -130 -17 132 C ATOM 2873 CD1 PHE A 264 13.922 -0.600 20.938 1.00 81.47 C ANISOU 2873 CD1 PHE A 264 11278 10039 9640 -51 -16 147 C ATOM 2874 CD2 PHE A 264 16.249 -0.549 21.482 1.00 81.19 C ANISOU 2874 CD2 PHE A 264 11150 10133 9567 -156 -52 117 C ATOM 2875 CE1 PHE A 264 13.721 -1.614 21.867 1.00 81.32 C ANISOU 2875 CE1 PHE A 264 11230 10038 9631 -10 -39 151 C ATOM 2876 CE2 PHE A 264 16.046 -1.557 22.422 1.00 83.18 C ANISOU 2876 CE2 PHE A 264 11375 10406 9822 -91 -82 127 C ATOM 2877 CZ PHE A 264 14.785 -2.089 22.602 1.00 80.50 C ANISOU 2877 CZ PHE A 264 11077 10000 9508 -23 -71 145 C ATOM 2878 N CYS A 265 15.156 1.369 15.959 1.00 85.49 N ANISOU 2878 N CYS A 265 11841 10520 10120 -122 100 165 N ATOM 2879 CA CYS A 265 15.353 2.297 14.852 1.00 85.74 C ANISOU 2879 CA CYS A 265 11947 10509 10119 -146 152 175 C ATOM 2880 C CYS A 265 14.009 2.716 14.273 1.00 86.35 C ANISOU 2880 C CYS A 265 12108 10526 10175 -40 173 199 C ATOM 2881 O CYS A 265 13.822 3.894 13.985 1.00 86.50 O ANISOU 2881 O CYS A 265 12256 10467 10143 -42 225 212 O ATOM 2882 CB CYS A 265 16.267 1.692 13.790 1.00 86.73 C ANISOU 2882 CB CYS A 265 11987 10705 10263 -165 151 172 C ATOM 2883 SG CYS A 265 18.024 1.700 14.242 1.00 91.84 S ANISOU 2883 SG CYS A 265 12551 11441 10901 -301 147 136 S ATOM 2884 N LEU A 266 13.068 1.764 14.128 1.00 80.79 N ANISOU 2884 N LEU A 266 11335 9861 9499 55 139 202 N ATOM 2885 CA LEU A 266 11.717 1.999 13.598 1.00 79.81 C ANISOU 2885 CA LEU A 266 11253 9725 9348 167 149 213 C ATOM 2886 C LEU A 266 10.934 2.902 14.551 1.00 82.59 C ANISOU 2886 C LEU A 266 11704 10015 9662 196 165 218 C ATOM 2887 O LEU A 266 11.137 2.809 15.763 1.00 82.55 O ANISOU 2887 O LEU A 266 11693 9998 9675 142 148 205 O ATOM 2888 CB LEU A 266 11.002 0.643 13.411 1.00 78.98 C ANISOU 2888 CB LEU A 266 11032 9694 9281 223 111 194 C ATOM 2889 CG LEU A 266 10.040 0.509 12.236 1.00 82.39 C ANISOU 2889 CG LEU A 266 11445 10172 9687 320 116 191 C ATOM 2890 CD1 LEU A 266 10.780 0.505 10.892 1.00 82.10 C ANISOU 2890 CD1 LEU A 266 11401 10150 9643 314 131 203 C ATOM 2891 CD2 LEU A 266 9.188 -0.735 12.381 1.00 81.94 C ANISOU 2891 CD2 LEU A 266 11287 10185 9661 347 89 156 C ATOM 2892 N LYS A 267 10.063 3.780 14.018 1.00 78.23 N ANISOU 2892 N LYS A 267 11247 9427 9049 291 198 236 N ATOM 2893 CA LYS A 267 9.281 4.716 14.844 1.00 77.78 C ANISOU 2893 CA LYS A 267 11300 9308 8943 341 221 244 C ATOM 2894 C LYS A 267 8.456 3.982 15.927 1.00 80.42 C ANISOU 2894 C LYS A 267 11553 9692 9310 364 179 221 C ATOM 2895 O LYS A 267 8.443 4.408 17.085 1.00 80.18 O ANISOU 2895 O LYS A 267 11578 9613 9273 329 184 217 O ATOM 2896 CB LYS A 267 8.368 5.602 13.975 1.00 80.12 C ANISOU 2896 CB LYS A 267 11700 9583 9157 481 259 270 C ATOM 2897 N GLU A 268 7.845 2.855 15.552 1.00 76.72 N ANISOU 2897 N GLU A 268 10959 9318 8874 407 145 201 N ATOM 2898 CA GLU A 268 7.006 1.988 16.387 1.00 76.89 C ANISOU 2898 CA GLU A 268 10896 9395 8923 419 118 172 C ATOM 2899 C GLU A 268 7.816 1.287 17.489 1.00 82.30 C ANISOU 2899 C GLU A 268 11546 10060 9665 316 97 164 C ATOM 2900 O GLU A 268 7.261 0.975 18.545 1.00 82.63 O ANISOU 2900 O GLU A 268 11576 10106 9716 314 89 151 O ATOM 2901 CB GLU A 268 6.297 0.943 15.511 1.00 77.91 C ANISOU 2901 CB GLU A 268 10909 9628 9067 464 102 143 C ATOM 2902 CG GLU A 268 5.346 1.547 14.483 1.00 89.60 C ANISOU 2902 CG GLU A 268 12402 11166 10477 588 114 142 C ATOM 2903 CD GLU A 268 5.912 2.094 13.180 1.00113.55 C ANISOU 2903 CD GLU A 268 15485 14182 13477 621 130 171 C ATOM 2904 OE1 GLU A 268 5.111 2.579 12.349 1.00109.58 O ANISOU 2904 OE1 GLU A 268 14999 13733 12904 743 139 174 O ATOM 2905 OE2 GLU A 268 7.148 2.054 12.986 1.00109.88 O ANISOU 2905 OE2 GLU A 268 15043 13658 13048 533 136 190 O ATOM 2906 N HIS A 269 9.124 1.050 17.242 1.00 78.47 N ANISOU 2906 N HIS A 269 11043 9563 9208 238 89 172 N ATOM 2907 CA HIS A 269 10.048 0.408 18.177 1.00 76.84 C ANISOU 2907 CA HIS A 269 10799 9359 9038 160 66 167 C ATOM 2908 C HIS A 269 10.557 1.428 19.173 1.00 80.35 C ANISOU 2908 C HIS A 269 11328 9748 9455 103 74 170 C ATOM 2909 O HIS A 269 10.757 1.089 20.343 1.00 80.26 O ANISOU 2909 O HIS A 269 11303 9740 9453 71 54 162 O ATOM 2910 CB HIS A 269 11.189 -0.279 17.424 1.00 76.88 C ANISOU 2910 CB HIS A 269 10736 9403 9071 119 54 168 C ATOM 2911 CG HIS A 269 10.756 -1.509 16.682 1.00 80.12 C ANISOU 2911 CG HIS A 269 11066 9863 9512 162 46 157 C ATOM 2912 ND1 HIS A 269 11.546 -2.646 16.645 1.00 82.03 N ANISOU 2912 ND1 HIS A 269 11242 10137 9786 141 31 154 N ATOM 2913 CD2 HIS A 269 9.617 -1.750 15.986 1.00 81.97 C ANISOU 2913 CD2 HIS A 269 11280 10125 9739 222 56 143 C ATOM 2914 CE1 HIS A 269 10.882 -3.521 15.904 1.00 81.23 C ANISOU 2914 CE1 HIS A 269 11099 10064 9701 177 39 138 C ATOM 2915 NE2 HIS A 269 9.707 -3.031 15.502 1.00 81.49 N ANISOU 2915 NE2 HIS A 269 11147 10104 9711 220 51 126 N ATOM 2916 N LYS A 270 10.739 2.687 18.722 1.00 76.50 N ANISOU 2916 N LYS A 270 10939 9204 8924 91 111 181 N ATOM 2917 CA LYS A 270 11.140 3.813 19.584 1.00 75.76 C ANISOU 2917 CA LYS A 270 10952 9042 8791 25 136 176 C ATOM 2918 C LYS A 270 10.028 4.075 20.619 1.00 78.05 C ANISOU 2918 C LYS A 270 11294 9300 9062 83 137 175 C ATOM 2919 O LYS A 270 10.325 4.363 21.777 1.00 77.07 O ANISOU 2919 O LYS A 270 11204 9152 8928 26 132 161 O ATOM 2920 CB LYS A 270 11.426 5.064 18.755 1.00 77.59 C ANISOU 2920 CB LYS A 270 11308 9200 8971 6 195 187 C ATOM 2921 CG LYS A 270 12.610 4.901 17.809 1.00 89.89 C ANISOU 2921 CG LYS A 270 12821 10791 10543 -71 203 184 C ATOM 2922 CD LYS A 270 13.717 5.878 18.119 1.00 99.92 C ANISOU 2922 CD LYS A 270 14172 12015 11777 -210 246 161 C ATOM 2923 CE LYS A 270 14.677 6.031 16.972 1.00110.80 C ANISOU 2923 CE LYS A 270 15541 13409 13149 -277 279 159 C ATOM 2924 NZ LYS A 270 16.091 6.008 17.438 1.00127.40 N ANISOU 2924 NZ LYS A 270 17579 15576 15253 -432 274 115 N ATOM 2925 N ALA A 271 8.746 3.902 20.190 1.00 73.76 N ANISOU 2925 N ALA A 271 10739 8777 8510 198 140 183 N ATOM 2926 CA ALA A 271 7.529 4.038 20.985 1.00 72.93 C ANISOU 2926 CA ALA A 271 10658 8669 8384 272 143 178 C ATOM 2927 C ALA A 271 7.469 2.984 22.088 1.00 78.88 C ANISOU 2927 C ALA A 271 11328 9463 9181 235 109 160 C ATOM 2928 O ALA A 271 7.088 3.317 23.217 1.00 80.31 O ANISOU 2928 O ALA A 271 11557 9615 9343 235 114 155 O ATOM 2929 CB ALA A 271 6.309 3.936 20.096 1.00 73.34 C ANISOU 2929 CB ALA A 271 10678 8777 8412 396 151 179 C ATOM 2930 N LEU A 272 7.879 1.726 21.781 1.00 74.75 N ANISOU 2930 N LEU A 272 10697 8998 8709 206 81 153 N ATOM 2931 CA LEU A 272 7.935 0.616 22.742 1.00 73.43 C ANISOU 2931 CA LEU A 272 10470 8856 8574 178 59 142 C ATOM 2932 C LEU A 272 9.078 0.801 23.755 1.00 79.36 C ANISOU 2932 C LEU A 272 11247 9585 9320 104 40 145 C ATOM 2933 O LEU A 272 9.005 0.263 24.865 1.00 79.97 O ANISOU 2933 O LEU A 272 11317 9668 9401 96 28 141 O ATOM 2934 CB LEU A 272 8.095 -0.732 22.037 1.00 72.62 C ANISOU 2934 CB LEU A 272 10272 8806 8513 178 48 136 C ATOM 2935 CG LEU A 272 6.928 -1.248 21.202 1.00 76.22 C ANISOU 2935 CG LEU A 272 10676 9310 8974 232 65 116 C ATOM 2936 CD1 LEU A 272 7.286 -2.584 20.569 1.00 75.23 C ANISOU 2936 CD1 LEU A 272 10477 9220 8887 212 61 105 C ATOM 2937 CD2 LEU A 272 5.669 -1.397 22.040 1.00 78.48 C ANISOU 2937 CD2 LEU A 272 10962 9611 9246 259 82 93 C ATOM 2938 N LYS A 273 10.131 1.547 23.376 1.00 76.41 N ANISOU 2938 N LYS A 273 10903 9198 8931 46 41 147 N ATOM 2939 CA LYS A 273 11.259 1.831 24.262 1.00 76.20 C ANISOU 2939 CA LYS A 273 10886 9178 8886 -37 23 135 C ATOM 2940 C LYS A 273 10.844 2.895 25.280 1.00 80.61 C ANISOU 2940 C LYS A 273 11550 9675 9402 -55 43 125 C ATOM 2941 O LYS A 273 11.198 2.778 26.448 1.00 81.66 O ANISOU 2941 O LYS A 273 11682 9824 9520 -91 21 112 O ATOM 2942 CB LYS A 273 12.491 2.276 23.465 1.00 78.19 C ANISOU 2942 CB LYS A 273 11126 9452 9131 -112 28 126 C ATOM 2943 CG LYS A 273 13.774 2.218 24.263 1.00 80.71 C ANISOU 2943 CG LYS A 273 11403 9834 9431 -198 0 101 C ATOM 2944 CD LYS A 273 14.881 2.925 23.538 1.00 88.59 C ANISOU 2944 CD LYS A 273 12399 10852 10407 -295 20 80 C ATOM 2945 CE LYS A 273 16.184 2.820 24.281 1.00101.53 C ANISOU 2945 CE LYS A 273 13967 12593 12018 -382 -12 42 C ATOM 2946 NZ LYS A 273 17.292 3.453 23.520 1.00115.33 N ANISOU 2946 NZ LYS A 273 15697 14381 13743 -493 15 10 N ATOM 2947 N THR A 274 10.067 3.911 24.841 1.00 76.47 N ANISOU 2947 N THR A 274 11123 9083 8850 -17 85 132 N ATOM 2948 CA THR A 274 9.564 4.998 25.701 1.00 76.18 C ANISOU 2948 CA THR A 274 11210 8973 8764 -16 115 125 C ATOM 2949 C THR A 274 8.700 4.400 26.839 1.00 77.42 C ANISOU 2949 C THR A 274 11341 9148 8929 34 96 124 C ATOM 2950 O THR A 274 8.943 4.698 27.998 1.00 77.81 O ANISOU 2950 O THR A 274 11432 9180 8953 -11 90 109 O ATOM 2951 CB THR A 274 8.804 6.058 24.875 1.00 82.80 C ANISOU 2951 CB THR A 274 12161 9740 9561 55 169 142 C ATOM 2952 OG1 THR A 274 9.617 6.468 23.769 1.00 81.27 O ANISOU 2952 OG1 THR A 274 11992 9527 9360 7 193 147 O ATOM 2953 CG2 THR A 274 8.417 7.282 25.707 1.00 82.85 C ANISOU 2953 CG2 THR A 274 12322 9653 9505 57 213 136 C ATOM 2954 N LEU A 275 7.745 3.530 26.493 1.00 71.67 N ANISOU 2954 N LEU A 275 10540 8462 8229 115 90 133 N ATOM 2955 CA LEU A 275 6.854 2.821 27.400 1.00 70.81 C ANISOU 2955 CA LEU A 275 10398 8377 8129 155 85 127 C ATOM 2956 C LEU A 275 7.658 2.017 28.423 1.00 74.33 C ANISOU 2956 C LEU A 275 10807 8846 8590 97 52 124 C ATOM 2957 O LEU A 275 7.317 2.030 29.611 1.00 73.57 O ANISOU 2957 O LEU A 275 10744 8735 8473 99 53 118 O ATOM 2958 CB LEU A 275 5.949 1.892 26.577 1.00 70.40 C ANISOU 2958 CB LEU A 275 10258 8384 8108 217 90 125 C ATOM 2959 CG LEU A 275 4.532 2.334 26.232 1.00 74.35 C ANISOU 2959 CG LEU A 275 10767 8905 8577 310 119 116 C ATOM 2960 CD1 LEU A 275 4.430 3.806 25.962 1.00 74.24 C ANISOU 2960 CD1 LEU A 275 10867 8834 8508 356 144 129 C ATOM 2961 CD2 LEU A 275 3.999 1.526 25.064 1.00 75.62 C ANISOU 2961 CD2 LEU A 275 10829 9143 8761 346 119 103 C ATOM 2962 N GLY A 276 8.741 1.381 27.951 1.00 70.75 N ANISOU 2962 N GLY A 276 10288 8432 8161 57 25 127 N ATOM 2963 CA GLY A 276 9.671 0.599 28.763 1.00 70.12 C ANISOU 2963 CA GLY A 276 10167 8393 8080 26 -9 127 C ATOM 2964 C GLY A 276 10.423 1.441 29.775 1.00 75.23 C ANISOU 2964 C GLY A 276 10866 9038 8682 -37 -25 109 C ATOM 2965 O GLY A 276 10.660 0.979 30.891 1.00 75.34 O ANISOU 2965 O GLY A 276 10873 9078 8674 -35 -47 107 O ATOM 2966 N ILE A 277 10.783 2.700 29.397 1.00 72.87 N ANISOU 2966 N ILE A 277 10626 8705 8358 -96 -7 93 N ATOM 2967 CA ILE A 277 11.454 3.694 30.258 1.00 72.99 C ANISOU 2967 CA ILE A 277 10705 8708 8320 -182 -7 61 C ATOM 2968 C ILE A 277 10.473 4.150 31.374 1.00 78.44 C ANISOU 2968 C ILE A 277 11485 9339 8981 -149 11 59 C ATOM 2969 O ILE A 277 10.874 4.186 32.543 1.00 79.68 O ANISOU 2969 O ILE A 277 11652 9521 9102 -186 -11 39 O ATOM 2970 CB ILE A 277 12.040 4.896 29.451 1.00 75.76 C ANISOU 2970 CB ILE A 277 11120 9017 8647 -266 29 40 C ATOM 2971 CG1 ILE A 277 13.151 4.409 28.492 1.00 75.55 C ANISOU 2971 CG1 ILE A 277 10993 9070 8643 -311 9 35 C ATOM 2972 CG2 ILE A 277 12.610 5.963 30.410 1.00 77.30 C ANISOU 2972 CG2 ILE A 277 11400 9190 8779 -374 44 -6 C ATOM 2973 CD1 ILE A 277 13.415 5.264 27.295 1.00 82.50 C ANISOU 2973 CD1 ILE A 277 11927 9900 9517 -360 57 32 C ATOM 2974 N ILE A 278 9.197 4.475 31.015 1.00 73.65 N ANISOU 2974 N ILE A 278 10935 8669 8382 -72 50 77 N ATOM 2975 CA ILE A 278 8.140 4.868 31.969 1.00 73.20 C ANISOU 2975 CA ILE A 278 10953 8565 8296 -22 73 76 C ATOM 2976 C ILE A 278 8.014 3.785 33.027 1.00 76.47 C ANISOU 2976 C ILE A 278 11308 9027 8719 -4 43 80 C ATOM 2977 O ILE A 278 8.021 4.087 34.222 1.00 76.86 O ANISOU 2977 O ILE A 278 11409 9063 8730 -23 40 66 O ATOM 2978 CB ILE A 278 6.769 5.114 31.255 1.00 76.01 C ANISOU 2978 CB ILE A 278 11335 8890 8657 82 113 94 C ATOM 2979 CG1 ILE A 278 6.825 6.294 30.271 1.00 76.46 C ANISOU 2979 CG1 ILE A 278 11484 8883 8683 89 153 98 C ATOM 2980 CG2 ILE A 278 5.594 5.256 32.255 1.00 76.15 C ANISOU 2980 CG2 ILE A 278 11396 8889 8646 147 135 91 C ATOM 2981 CD1 ILE A 278 6.833 7.636 30.908 1.00 90.22 C ANISOU 2981 CD1 ILE A 278 13384 10534 10362 64 194 84 C ATOM 2982 N MET A 279 7.932 2.513 32.564 1.00 71.86 N ANISOU 2982 N MET A 279 10628 8493 8181 32 28 98 N ATOM 2983 CA MET A 279 7.821 1.312 33.391 1.00 69.90 C ANISOU 2983 CA MET A 279 10340 8279 7940 58 14 108 C ATOM 2984 C MET A 279 9.037 1.125 34.299 1.00 77.22 C ANISOU 2984 C MET A 279 11258 9249 8831 16 -29 102 C ATOM 2985 O MET A 279 8.855 0.857 35.479 1.00 79.06 O ANISOU 2985 O MET A 279 11522 9484 9033 33 -33 103 O ATOM 2986 CB MET A 279 7.652 0.063 32.513 1.00 70.27 C ANISOU 2986 CB MET A 279 10307 8356 8036 91 19 124 C ATOM 2987 CG MET A 279 6.296 -0.071 31.901 1.00 71.67 C ANISOU 2987 CG MET A 279 10472 8523 8237 135 60 120 C ATOM 2988 SD MET A 279 6.262 -1.420 30.700 1.00 72.91 S ANISOU 2988 SD MET A 279 10541 8717 8446 147 68 125 S ATOM 2989 CE MET A 279 4.732 -1.101 29.959 1.00 69.41 C ANISOU 2989 CE MET A 279 10076 8291 8008 188 108 102 C ATOM 2990 N GLY A 280 10.245 1.252 33.742 1.00 73.94 N ANISOU 2990 N GLY A 280 10797 8884 8415 -32 -60 91 N ATOM 2991 CA GLY A 280 11.507 1.038 34.449 1.00 74.09 C ANISOU 2991 CA GLY A 280 10775 8985 8389 -66 -107 76 C ATOM 2992 C GLY A 280 11.846 2.030 35.536 1.00 79.91 C ANISOU 2992 C GLY A 280 11571 9728 9064 -130 -118 39 C ATOM 2993 O GLY A 280 12.363 1.637 36.591 1.00 79.61 O ANISOU 2993 O GLY A 280 11516 9756 8977 -119 -153 31 O ATOM 2994 N THR A 281 11.585 3.329 35.277 1.00 78.31 N ANISOU 2994 N THR A 281 11445 9456 8851 -193 -84 14 N ATOM 2995 CA THR A 281 11.879 4.417 36.220 1.00 79.02 C ANISOU 2995 CA THR A 281 11614 9534 8878 -273 -79 -31 C ATOM 2996 C THR A 281 10.915 4.357 37.395 1.00 82.36 C ANISOU 2996 C THR A 281 12104 9910 9278 -215 -68 -20 C ATOM 2997 O THR A 281 11.343 4.606 38.529 1.00 83.45 O ANISOU 2997 O THR A 281 12265 10087 9357 -252 -90 -50 O ATOM 2998 CB THR A 281 11.879 5.787 35.535 1.00 91.84 C ANISOU 2998 CB THR A 281 13330 11075 10491 -353 -29 -58 C ATOM 2999 OG1 THR A 281 10.593 6.031 34.968 1.00 98.12 O ANISOU 2999 OG1 THR A 281 14195 11769 11319 -270 19 -22 O ATOM 3000 CG2 THR A 281 12.967 5.913 34.469 1.00 88.06 C ANISOU 3000 CG2 THR A 281 12789 10647 10023 -434 -34 -77 C ATOM 3001 N PHE A 282 9.638 3.991 37.146 1.00 76.56 N ANISOU 3001 N PHE A 282 11391 9112 8584 -126 -34 18 N ATOM 3002 CA PHE A 282 8.660 3.828 38.225 1.00 75.57 C ANISOU 3002 CA PHE A 282 11319 8953 8440 -69 -16 29 C ATOM 3003 C PHE A 282 9.153 2.740 39.212 1.00 80.39 C ANISOU 3003 C PHE A 282 11883 9637 9026 -43 -56 39 C ATOM 3004 O PHE A 282 9.109 2.957 40.417 1.00 80.82 O ANISOU 3004 O PHE A 282 11987 9694 9027 -46 -62 25 O ATOM 3005 CB PHE A 282 7.253 3.487 37.663 1.00 75.88 C ANISOU 3005 CB PHE A 282 11360 8946 8525 14 29 57 C ATOM 3006 CG PHE A 282 6.180 3.149 38.692 1.00 76.00 C ANISOU 3006 CG PHE A 282 11411 8942 8524 69 56 66 C ATOM 3007 CD1 PHE A 282 6.098 1.871 39.249 1.00 76.97 C ANISOU 3007 CD1 PHE A 282 11493 9099 8654 100 50 86 C ATOM 3008 CD2 PHE A 282 5.231 4.096 39.070 1.00 76.41 C ANISOU 3008 CD2 PHE A 282 11547 8939 8547 96 97 54 C ATOM 3009 CE1 PHE A 282 5.116 1.566 40.194 1.00 77.12 C ANISOU 3009 CE1 PHE A 282 11551 9099 8653 139 86 91 C ATOM 3010 CE2 PHE A 282 4.236 3.780 39.998 1.00 78.26 C ANISOU 3010 CE2 PHE A 282 11805 9167 8764 144 126 58 C ATOM 3011 CZ PHE A 282 4.186 2.519 40.553 1.00 76.38 C ANISOU 3011 CZ PHE A 282 11522 8964 8536 157 121 75 C ATOM 3012 N THR A 283 9.642 1.589 38.691 1.00 77.60 N ANISOU 3012 N THR A 283 11443 9340 8701 -8 -80 65 N ATOM 3013 CA THR A 283 10.086 0.444 39.500 1.00 77.73 C ANISOU 3013 CA THR A 283 11432 9417 8686 46 -108 86 C ATOM 3014 C THR A 283 11.364 0.760 40.262 1.00 83.24 C ANISOU 3014 C THR A 283 12104 10215 9310 8 -166 53 C ATOM 3015 O THR A 283 11.509 0.297 41.382 1.00 83.82 O ANISOU 3015 O THR A 283 12196 10327 9325 54 -185 60 O ATOM 3016 CB THR A 283 10.210 -0.846 38.673 1.00 85.83 C ANISOU 3016 CB THR A 283 12395 10460 9756 104 -105 122 C ATOM 3017 OG1 THR A 283 11.453 -0.889 37.984 1.00 95.53 O ANISOU 3017 OG1 THR A 283 13544 11771 10982 80 -149 111 O ATOM 3018 CG2 THR A 283 9.064 -1.035 37.709 1.00 76.35 C ANISOU 3018 CG2 THR A 283 11197 9187 8625 116 -51 135 C ATOM 3019 N LEU A 284 12.258 1.565 39.689 1.00 81.28 N ANISOU 3019 N LEU A 284 11815 10015 9054 -79 -189 12 N ATOM 3020 CA LEU A 284 13.498 2.024 40.334 1.00 82.46 C ANISOU 3020 CA LEU A 284 11923 10283 9124 -146 -241 -41 C ATOM 3021 C LEU A 284 13.177 2.996 41.494 1.00 85.62 C ANISOU 3021 C LEU A 284 12415 10650 9466 -200 -231 -80 C ATOM 3022 O LEU A 284 13.870 3.009 42.520 1.00 87.09 O ANISOU 3022 O LEU A 284 12581 10938 9570 -212 -275 -114 O ATOM 3023 CB LEU A 284 14.346 2.728 39.262 1.00 83.38 C ANISOU 3023 CB LEU A 284 11986 10439 9257 -251 -244 -82 C ATOM 3024 CG LEU A 284 15.751 3.169 39.624 1.00 89.89 C ANISOU 3024 CG LEU A 284 12733 11416 10003 -347 -292 -152 C ATOM 3025 CD1 LEU A 284 16.713 2.815 38.505 1.00 90.46 C ANISOU 3025 CD1 LEU A 284 12689 11584 10097 -368 -312 -159 C ATOM 3026 CD2 LEU A 284 15.796 4.674 39.915 1.00 92.74 C ANISOU 3026 CD2 LEU A 284 13181 11730 10327 -497 -259 -221 C ATOM 3027 N CYS A 285 12.133 3.819 41.311 1.00 79.07 N ANISOU 3027 N CYS A 285 11687 9686 8669 -223 -173 -78 N ATOM 3028 CA CYS A 285 11.706 4.809 42.285 1.00 78.12 C ANISOU 3028 CA CYS A 285 11674 9509 8498 -268 -150 -113 C ATOM 3029 C CYS A 285 10.991 4.169 43.477 1.00 82.37 C ANISOU 3029 C CYS A 285 12250 10038 9009 -176 -151 -83 C ATOM 3030 O CYS A 285 11.250 4.570 44.615 1.00 83.65 O ANISOU 3030 O CYS A 285 12452 10235 9096 -206 -169 -119 O ATOM 3031 CB CYS A 285 10.821 5.862 41.621 1.00 77.41 C ANISOU 3031 CB CYS A 285 11688 9281 8443 -295 -82 -115 C ATOM 3032 SG CYS A 285 11.721 7.106 40.652 1.00 81.43 S ANISOU 3032 SG CYS A 285 12225 9774 8942 -441 -59 -171 S ATOM 3033 N TRP A 286 10.084 3.207 43.232 1.00 77.52 N ANISOU 3033 N TRP A 286 11629 9377 8448 -76 -125 -24 N ATOM 3034 CA TRP A 286 9.250 2.630 44.287 1.00 77.64 C ANISOU 3034 CA TRP A 286 11696 9362 8440 1 -104 5 C ATOM 3035 C TRP A 286 9.763 1.337 44.959 1.00 83.75 C ANISOU 3035 C TRP A 286 12432 10215 9174 79 -138 37 C ATOM 3036 O TRP A 286 9.373 1.083 46.100 1.00 84.85 O ANISOU 3036 O TRP A 286 12630 10346 9263 123 -128 48 O ATOM 3037 CB TRP A 286 7.845 2.380 43.749 1.00 75.63 C ANISOU 3037 CB TRP A 286 11470 9013 8252 52 -40 40 C ATOM 3038 CG TRP A 286 7.012 3.624 43.678 1.00 76.57 C ANISOU 3038 CG TRP A 286 11668 9052 8374 26 4 16 C ATOM 3039 CD1 TRP A 286 6.638 4.303 42.555 1.00 78.88 C ANISOU 3039 CD1 TRP A 286 11967 9295 8710 13 33 12 C ATOM 3040 CD2 TRP A 286 6.460 4.349 44.788 1.00 77.21 C ANISOU 3040 CD2 TRP A 286 11845 9092 8401 26 28 -4 C ATOM 3041 NE1 TRP A 286 5.853 5.380 42.891 1.00 78.46 N ANISOU 3041 NE1 TRP A 286 12013 9170 8628 19 76 -6 N ATOM 3042 CE2 TRP A 286 5.736 5.439 44.259 1.00 80.76 C ANISOU 3042 CE2 TRP A 286 12360 9463 8862 22 74 -18 C ATOM 3043 CE3 TRP A 286 6.500 4.175 46.189 1.00 79.20 C ANISOU 3043 CE3 TRP A 286 12141 9366 8587 40 17 -10 C ATOM 3044 CZ2 TRP A 286 5.081 6.372 45.077 1.00 80.38 C ANISOU 3044 CZ2 TRP A 286 12422 9356 8764 30 112 -39 C ATOM 3045 CZ3 TRP A 286 5.850 5.099 46.993 1.00 80.82 C ANISOU 3045 CZ3 TRP A 286 12447 9514 8747 36 51 -34 C ATOM 3046 CH2 TRP A 286 5.150 6.180 46.436 1.00 81.45 C ANISOU 3046 CH2 TRP A 286 12592 9514 8842 31 99 -49 C ATOM 3047 N LEU A 287 10.609 0.531 44.288 1.00 80.57 N ANISOU 3047 N LEU A 287 11943 9884 8785 106 -172 55 N ATOM 3048 CA LEU A 287 11.128 -0.735 44.821 1.00 80.58 C ANISOU 3048 CA LEU A 287 11925 9955 8739 206 -197 93 C ATOM 3049 C LEU A 287 11.934 -0.563 46.124 1.00 84.86 C ANISOU 3049 C LEU A 287 12472 10606 9167 222 -252 66 C ATOM 3050 O LEU A 287 11.675 -1.372 47.015 1.00 85.56 O ANISOU 3050 O LEU A 287 12615 10687 9205 317 -240 104 O ATOM 3051 CB LEU A 287 11.952 -1.503 43.772 1.00 80.80 C ANISOU 3051 CB LEU A 287 11861 10044 8795 237 -223 111 C ATOM 3052 CG LEU A 287 12.310 -2.971 44.048 1.00 86.24 C ANISOU 3052 CG LEU A 287 12553 10771 9445 368 -225 165 C ATOM 3053 CD1 LEU A 287 11.076 -3.823 44.438 1.00 85.84 C ANISOU 3053 CD1 LEU A 287 12608 10592 9414 427 -146 214 C ATOM 3054 CD2 LEU A 287 13.038 -3.576 42.860 1.00 89.09 C ANISOU 3054 CD2 LEU A 287 12829 11180 9842 392 -242 178 C ATOM 3055 N PRO A 288 12.843 0.442 46.341 1.00 81.93 N ANISOU 3055 N PRO A 288 12054 10333 8743 132 -305 -2 N ATOM 3056 CA PRO A 288 13.522 0.536 47.659 1.00 82.46 C ANISOU 3056 CA PRO A 288 12121 10521 8690 152 -357 -34 C ATOM 3057 C PRO A 288 12.530 0.691 48.828 1.00 86.13 C ANISOU 3057 C PRO A 288 12706 10898 9123 181 -319 -21 C ATOM 3058 O PRO A 288 12.697 0.032 49.855 1.00 87.28 O ANISOU 3058 O PRO A 288 12878 11100 9184 277 -339 2 O ATOM 3059 CB PRO A 288 14.416 1.773 47.520 1.00 84.70 C ANISOU 3059 CB PRO A 288 12346 10898 8940 5 -396 -126 C ATOM 3060 CG PRO A 288 14.574 1.986 46.067 1.00 88.83 C ANISOU 3060 CG PRO A 288 12814 11386 9552 -60 -378 -128 C ATOM 3061 CD PRO A 288 13.300 1.523 45.440 1.00 83.52 C ANISOU 3061 CD PRO A 288 12209 10545 8980 0 -312 -59 C ATOM 3062 N PHE A 289 11.463 1.503 48.643 1.00 80.89 N ANISOU 3062 N PHE A 289 12119 10094 8520 114 -260 -30 N ATOM 3063 CA PHE A 289 10.412 1.726 49.633 1.00 79.94 C ANISOU 3063 CA PHE A 289 12110 9886 8379 137 -213 -19 C ATOM 3064 C PHE A 289 9.654 0.417 49.923 1.00 84.13 C ANISOU 3064 C PHE A 289 12683 10360 8922 256 -169 55 C ATOM 3065 O PHE A 289 9.459 0.072 51.094 1.00 84.70 O ANISOU 3065 O PHE A 289 12821 10441 8922 317 -162 71 O ATOM 3066 CB PHE A 289 9.431 2.834 49.170 1.00 80.44 C ANISOU 3066 CB PHE A 289 12236 9821 8505 61 -155 -42 C ATOM 3067 CG PHE A 289 8.218 3.009 50.063 1.00 80.85 C ANISOU 3067 CG PHE A 289 12394 9783 8543 97 -98 -28 C ATOM 3068 CD1 PHE A 289 8.310 3.708 51.260 1.00 83.74 C ANISOU 3068 CD1 PHE A 289 12829 10166 8824 70 -109 -68 C ATOM 3069 CD2 PHE A 289 6.989 2.456 49.714 1.00 81.65 C ANISOU 3069 CD2 PHE A 289 12519 9795 8710 153 -31 19 C ATOM 3070 CE1 PHE A 289 7.202 3.841 52.100 1.00 84.47 C ANISOU 3070 CE1 PHE A 289 13017 10181 8899 109 -54 -55 C ATOM 3071 CE2 PHE A 289 5.878 2.595 50.549 1.00 84.36 C ANISOU 3071 CE2 PHE A 289 12946 10072 9033 184 25 26 C ATOM 3072 CZ PHE A 289 5.993 3.285 51.740 1.00 83.13 C ANISOU 3072 CZ PHE A 289 12862 9928 8795 167 13 -7 C ATOM 3073 N PHE A 290 9.219 -0.296 48.858 1.00 79.16 N ANISOU 3073 N PHE A 290 12026 9671 8380 282 -130 97 N ATOM 3074 CA PHE A 290 8.457 -1.537 48.997 1.00 77.68 C ANISOU 3074 CA PHE A 290 11889 9418 8209 367 -68 157 C ATOM 3075 C PHE A 290 9.329 -2.697 49.523 1.00 84.18 C ANISOU 3075 C PHE A 290 12717 10315 8953 476 -98 197 C ATOM 3076 O PHE A 290 8.774 -3.581 50.180 1.00 83.19 O ANISOU 3076 O PHE A 290 12680 10132 8795 549 -43 242 O ATOM 3077 CB PHE A 290 7.718 -1.908 47.704 1.00 77.14 C ANISOU 3077 CB PHE A 290 11789 9271 8248 347 -14 175 C ATOM 3078 CG PHE A 290 6.404 -1.174 47.557 1.00 76.83 C ANISOU 3078 CG PHE A 290 11783 9148 8260 297 45 156 C ATOM 3079 CD1 PHE A 290 5.278 -1.573 48.270 1.00 78.15 C ANISOU 3079 CD1 PHE A 290 12022 9254 8417 324 117 172 C ATOM 3080 CD2 PHE A 290 6.289 -0.082 46.699 1.00 78.82 C ANISOU 3080 CD2 PHE A 290 11998 9388 8563 232 35 121 C ATOM 3081 CE1 PHE A 290 4.067 -0.887 48.141 1.00 78.63 C ANISOU 3081 CE1 PHE A 290 12098 9264 8514 292 170 149 C ATOM 3082 CE2 PHE A 290 5.067 0.600 46.556 1.00 80.59 C ANISOU 3082 CE2 PHE A 290 12255 9548 8819 216 90 106 C ATOM 3083 CZ PHE A 290 3.965 0.189 47.276 1.00 78.05 C ANISOU 3083 CZ PHE A 290 11985 9186 8484 249 154 118 C ATOM 3084 N ILE A 291 10.674 -2.668 49.303 1.00 83.56 N ANISOU 3084 N ILE A 291 12551 10368 8830 491 -180 179 N ATOM 3085 CA ILE A 291 11.594 -3.695 49.843 1.00 84.90 C ANISOU 3085 CA ILE A 291 12720 10637 8902 622 -217 215 C ATOM 3086 C ILE A 291 11.734 -3.506 51.363 1.00 90.69 C ANISOU 3086 C ILE A 291 13516 11429 9514 671 -242 206 C ATOM 3087 O ILE A 291 11.570 -4.480 52.095 1.00 91.00 O ANISOU 3087 O ILE A 291 13646 11443 9486 792 -209 262 O ATOM 3088 CB ILE A 291 12.982 -3.741 49.133 1.00 88.03 C ANISOU 3088 CB ILE A 291 12986 11186 9277 635 -296 193 C ATOM 3089 CG1 ILE A 291 12.874 -4.498 47.801 1.00 87.28 C ANISOU 3089 CG1 ILE A 291 12861 11026 9274 652 -260 230 C ATOM 3090 CG2 ILE A 291 14.059 -4.400 50.026 1.00 90.03 C ANISOU 3090 CG2 ILE A 291 13224 11597 9387 776 -358 207 C ATOM 3091 CD1 ILE A 291 14.076 -4.363 46.895 1.00 96.06 C ANISOU 3091 CD1 ILE A 291 13837 12272 10390 636 -326 201 C ATOM 3092 N VAL A 292 12.009 -2.257 51.828 1.00 88.78 N ANISOU 3092 N VAL A 292 13239 11254 9239 574 -291 135 N ATOM 3093 CA VAL A 292 12.169 -1.906 53.249 1.00 90.41 C ANISOU 3093 CA VAL A 292 13495 11528 9328 599 -321 110 C ATOM 3094 C VAL A 292 10.809 -2.064 54.009 1.00 96.09 C ANISOU 3094 C VAL A 292 14357 12094 10059 620 -234 148 C ATOM 3095 O VAL A 292 10.800 -2.172 55.231 1.00 96.55 O ANISOU 3095 O VAL A 292 14485 12185 10015 683 -240 155 O ATOM 3096 CB VAL A 292 12.816 -0.490 53.431 1.00 95.26 C ANISOU 3096 CB VAL A 292 14040 12247 9908 463 -385 11 C ATOM 3097 CG1 VAL A 292 11.812 0.650 53.272 1.00 94.48 C ANISOU 3097 CG1 VAL A 292 14005 12006 9887 333 -329 -24 C ATOM 3098 CG2 VAL A 292 13.533 -0.373 54.769 1.00 96.73 C ANISOU 3098 CG2 VAL A 292 14225 12587 9940 510 -449 -25 C ATOM 3099 N ASN A 293 9.688 -2.104 53.271 1.00 93.82 N ANISOU 3099 N ASN A 293 14104 11657 9888 571 -154 171 N ATOM 3100 CA ASN A 293 8.321 -2.250 53.773 1.00 94.23 C ANISOU 3100 CA ASN A 293 14265 11575 9965 574 -61 197 C ATOM 3101 C ASN A 293 8.085 -3.662 54.308 1.00100.79 C ANISOU 3101 C ASN A 293 15189 12362 10745 695 -4 270 C ATOM 3102 O ASN A 293 7.400 -3.816 55.315 1.00101.27 O ANISOU 3102 O ASN A 293 15353 12369 10756 725 49 287 O ATOM 3103 CB ASN A 293 7.324 -1.932 52.640 1.00 96.63 C ANISOU 3103 CB ASN A 293 14544 11772 10400 491 -1 190 C ATOM 3104 CG ASN A 293 5.981 -1.380 53.043 1.00120.10 C ANISOU 3104 CG ASN A 293 17584 14649 13400 450 72 177 C ATOM 3105 OD1 ASN A 293 5.861 -0.580 53.967 1.00120.54 O ANISOU 3105 OD1 ASN A 293 17687 14714 13398 432 61 147 O ATOM 3106 ND2 ASN A 293 4.946 -1.735 52.292 1.00108.51 N ANISOU 3106 ND2 ASN A 293 16112 13099 12017 430 147 193 N ATOM 3107 N ILE A 294 8.639 -4.692 53.639 1.00 99.23 N ANISOU 3107 N ILE A 294 14968 12178 10555 766 -5 312 N ATOM 3108 CA ILE A 294 8.479 -6.091 54.063 1.00100.36 C ANISOU 3108 CA ILE A 294 15228 12262 10642 887 64 384 C ATOM 3109 C ILE A 294 9.654 -6.506 54.994 1.00107.33 C ANISOU 3109 C ILE A 294 16133 13274 11372 1033 -7 408 C ATOM 3110 O ILE A 294 9.502 -7.449 55.770 1.00107.99 O ANISOU 3110 O ILE A 294 16350 13310 11370 1150 50 467 O ATOM 3111 CB ILE A 294 8.283 -7.093 52.872 1.00102.75 C ANISOU 3111 CB ILE A 294 15530 12484 11027 894 125 421 C ATOM 3112 CG1 ILE A 294 9.494 -7.138 51.928 1.00103.31 C ANISOU 3112 CG1 ILE A 294 15481 12664 11111 923 40 413 C ATOM 3113 CG2 ILE A 294 6.985 -6.834 52.099 1.00101.53 C ANISOU 3113 CG2 ILE A 294 15363 12215 10999 767 205 397 C ATOM 3114 CD1 ILE A 294 10.384 -8.343 52.149 1.00115.13 C ANISOU 3114 CD1 ILE A 294 17033 14204 12507 1091 34 472 C ATOM 3115 N VAL A 295 10.811 -5.805 54.902 1.00104.89 N ANISOU 3115 N VAL A 295 15696 13134 11023 1026 -123 358 N ATOM 3116 CA VAL A 295 12.011 -6.035 55.724 1.00106.18 C ANISOU 3116 CA VAL A 295 15838 13473 11032 1158 -209 360 C ATOM 3117 C VAL A 295 11.720 -5.576 57.159 1.00111.83 C ANISOU 3117 C VAL A 295 16633 14209 11648 1172 -214 345 C ATOM 3118 O VAL A 295 12.190 -6.203 58.106 1.00111.51 O ANISOU 3118 O VAL A 295 16660 14243 11467 1326 -231 382 O ATOM 3119 CB VAL A 295 13.260 -5.343 55.111 1.00109.88 C ANISOU 3119 CB VAL A 295 16124 14132 11494 1110 -324 292 C ATOM 3120 CG1 VAL A 295 14.382 -5.153 56.134 1.00111.02 C ANISOU 3120 CG1 VAL A 295 16214 14498 11470 1199 -424 257 C ATOM 3121 CG2 VAL A 295 13.769 -6.121 53.901 1.00109.32 C ANISOU 3121 CG2 VAL A 295 15990 14069 11475 1161 -323 326 C ATOM 3122 N HIS A 296 10.915 -4.503 57.305 1.00110.23 N ANISOU 3122 N HIS A 296 16434 13937 11512 1025 -193 293 N ATOM 3123 CA HIS A 296 10.489 -3.953 58.594 1.00111.56 C ANISOU 3123 CA HIS A 296 16682 14104 11603 1016 -187 272 C ATOM 3124 C HIS A 296 9.522 -4.936 59.295 1.00116.99 C ANISOU 3124 C HIS A 296 17542 14649 12260 1108 -76 350 C ATOM 3125 O HIS A 296 9.455 -4.954 60.524 1.00117.74 O ANISOU 3125 O HIS A 296 17726 14769 12242 1175 -73 359 O ATOM 3126 CB HIS A 296 9.853 -2.563 58.409 1.00111.92 C ANISOU 3126 CB HIS A 296 16694 14096 11733 842 -182 199 C ATOM 3127 CG HIS A 296 9.394 -1.918 59.683 1.00116.45 C ANISOU 3127 CG HIS A 296 17352 14663 12231 825 -172 171 C ATOM 3128 ND1 HIS A 296 10.257 -1.724 60.756 1.00119.63 N ANISOU 3128 ND1 HIS A 296 17749 15219 12484 882 -250 139 N ATOM 3129 CD2 HIS A 296 8.172 -1.446 60.018 1.00117.95 C ANISOU 3129 CD2 HIS A 296 17626 14721 12468 763 -93 166 C ATOM 3130 CE1 HIS A 296 9.529 -1.162 61.706 1.00119.25 C ANISOU 3130 CE1 HIS A 296 17793 15114 12402 850 -214 120 C ATOM 3131 NE2 HIS A 296 8.269 -0.969 61.308 1.00118.60 N ANISOU 3131 NE2 HIS A 296 17768 14860 12436 781 -119 137 N ATOM 3132 N VAL A 297 8.808 -5.772 58.513 1.00113.96 N ANISOU 3132 N VAL A 297 17209 14122 11969 1106 20 402 N ATOM 3133 CA VAL A 297 7.900 -6.810 59.017 1.00114.47 C ANISOU 3133 CA VAL A 297 17442 14042 12010 1170 145 470 C ATOM 3134 C VAL A 297 8.757 -7.972 59.594 1.00120.68 C ANISOU 3134 C VAL A 297 18322 14878 12651 1369 139 541 C ATOM 3135 O VAL A 297 8.384 -8.546 60.618 1.00121.39 O ANISOU 3135 O VAL A 297 18569 14909 12645 1457 207 588 O ATOM 3136 CB VAL A 297 6.897 -7.276 57.922 1.00117.38 C ANISOU 3136 CB VAL A 297 17820 14259 12520 1079 251 484 C ATOM 3137 CG1 VAL A 297 6.086 -8.488 58.374 1.00118.05 C ANISOU 3137 CG1 VAL A 297 18084 14199 12570 1131 393 548 C ATOM 3138 CG2 VAL A 297 5.967 -6.141 57.508 1.00115.91 C ANISOU 3138 CG2 VAL A 297 17557 14034 12448 918 263 420 C ATOM 3139 N ILE A 298 9.922 -8.270 58.969 1.00117.85 N ANISOU 3139 N ILE A 298 17870 14639 12268 1448 57 546 N ATOM 3140 CA ILE A 298 10.870 -9.302 59.413 1.00119.36 C ANISOU 3140 CA ILE A 298 18132 14910 12310 1664 36 609 C ATOM 3141 C ILE A 298 11.553 -8.840 60.730 1.00126.39 C ANISOU 3141 C ILE A 298 19016 15971 13035 1761 -55 588 C ATOM 3142 O ILE A 298 11.439 -9.524 61.747 1.00127.49 O ANISOU 3142 O ILE A 298 19316 16079 13046 1905 -6 648 O ATOM 3143 CB ILE A 298 11.918 -9.645 58.302 1.00122.19 C ANISOU 3143 CB ILE A 298 18365 15369 12690 1718 -32 610 C ATOM 3144 CG1 ILE A 298 11.272 -9.906 56.904 1.00120.90 C ANISOU 3144 CG1 ILE A 298 18180 15057 12700 1597 43 613 C ATOM 3145 CG2 ILE A 298 12.842 -10.791 58.717 1.00124.58 C ANISOU 3145 CG2 ILE A 298 18754 15749 12830 1970 -42 683 C ATOM 3146 CD1 ILE A 298 10.348 -11.147 56.714 1.00127.13 C ANISOU 3146 CD1 ILE A 298 19159 15627 13517 1626 202 686 C ATOM 3147 N GLN A 299 12.250 -7.687 60.699 1.00124.02 N ANISOU 3147 N GLN A 299 18538 15850 12732 1675 -180 499 N ATOM 3148 CA GLN A 299 12.945 -7.088 61.841 1.00125.52 C ANISOU 3148 CA GLN A 299 18689 16231 12772 1729 -278 452 C ATOM 3149 C GLN A 299 12.590 -5.611 61.916 1.00130.26 C ANISOU 3149 C GLN A 299 19200 16846 13447 1517 -315 353 C ATOM 3150 O GLN A 299 12.826 -4.877 60.952 1.00129.41 O ANISOU 3150 O GLN A 299 18955 16769 13446 1374 -357 291 O ATOM 3151 CB GLN A 299 14.465 -7.284 61.722 1.00127.98 C ANISOU 3151 CB GLN A 299 18864 16800 12965 1859 -401 432 C ATOM 3152 N ASP A 300 12.021 -5.179 63.056 1.00128.06 N ANISOU 3152 N ASP A 300 19015 16536 13105 1501 -293 340 N ATOM 3153 CA ASP A 300 11.531 -3.814 63.287 1.00127.95 C ANISOU 3153 CA ASP A 300 18964 16504 13147 1317 -306 253 C ATOM 3154 C ASP A 300 12.650 -2.752 63.370 1.00132.92 C ANISOU 3154 C ASP A 300 19433 17356 13716 1236 -435 143 C ATOM 3155 O ASP A 300 12.531 -1.695 62.743 1.00131.42 O ANISOU 3155 O ASP A 300 19165 17142 13627 1054 -447 69 O ATOM 3156 CB ASP A 300 10.679 -3.750 64.579 1.00130.67 C ANISOU 3156 CB ASP A 300 19463 16766 13420 1347 -243 273 C ATOM 3157 CG ASP A 300 9.706 -4.902 64.851 1.00141.37 C ANISOU 3157 CG ASP A 300 20998 17935 14780 1445 -111 377 C ATOM 3158 OD1 ASP A 300 9.509 -5.752 63.947 1.00141.27 O ANISOU 3158 OD1 ASP A 300 21003 17824 14849 1470 -50 433 O ATOM 3159 OD2 ASP A 300 9.141 -4.949 65.966 1.00147.13 O ANISOU 3159 OD2 ASP A 300 21857 18617 15430 1487 -61 397 O ATOM 3160 N ASN A 301 13.720 -3.035 64.149 1.00131.84 N ANISOU 3160 N ASN A 301 19253 17438 13403 1369 -525 129 N ATOM 3161 CA ASN A 301 14.860 -2.145 64.431 1.00132.92 C ANISOU 3161 CA ASN A 301 19234 17829 13441 1302 -649 14 C ATOM 3162 C ASN A 301 15.899 -2.035 63.289 1.00136.63 C ANISOU 3162 C ASN A 301 19516 18445 13952 1249 -721 -35 C ATOM 3163 O ASN A 301 16.834 -1.235 63.407 1.00137.13 O ANISOU 3163 O ASN A 301 19437 18723 13944 1156 -813 -146 O ATOM 3164 CB ASN A 301 15.576 -2.615 65.700 1.00136.08 C ANISOU 3164 CB ASN A 301 19651 18432 13620 1490 -716 20 C ATOM 3165 N LEU A 302 15.734 -2.813 62.199 1.00131.82 N ANISOU 3165 N LEU A 302 18906 17726 13452 1295 -673 39 N ATOM 3166 CA LEU A 302 16.650 -2.842 61.051 1.00131.14 C ANISOU 3166 CA LEU A 302 18655 17760 13411 1262 -729 7 C ATOM 3167 C LEU A 302 16.773 -1.481 60.322 1.00132.99 C ANISOU 3167 C LEU A 302 18776 18003 13750 1005 -751 -104 C ATOM 3168 O LEU A 302 17.874 -1.138 59.881 1.00133.53 O ANISOU 3168 O LEU A 302 18678 18276 13780 950 -830 -181 O ATOM 3169 CB LEU A 302 16.220 -3.924 60.054 1.00130.18 C ANISOU 3169 CB LEU A 302 18592 17472 13399 1350 -653 113 C ATOM 3170 N ILE A 303 15.674 -0.715 60.203 1.00126.70 N ANISOU 3170 N ILE A 303 18073 16995 13072 854 -676 -115 N ATOM 3171 CA ILE A 303 15.689 0.578 59.516 1.00124.90 C ANISOU 3171 CA ILE A 303 17781 16740 12937 625 -676 -209 C ATOM 3172 C ILE A 303 15.043 1.665 60.375 1.00126.69 C ANISOU 3172 C ILE A 303 18102 16890 13144 506 -648 -270 C ATOM 3173 O ILE A 303 14.024 1.412 61.022 1.00126.07 O ANISOU 3173 O ILE A 303 18163 16664 13072 571 -584 -210 O ATOM 3174 CB ILE A 303 14.976 0.456 58.151 1.00126.35 C ANISOU 3174 CB ILE A 303 17980 16725 13302 569 -602 -158 C ATOM 3175 N ARG A 304 15.628 2.879 60.361 1.00122.22 N ANISOU 3175 N ARG A 304 17468 16419 12550 324 -687 -392 N ATOM 3176 CA ARG A 304 15.135 4.052 61.097 1.00121.67 C ANISOU 3176 CA ARG A 304 17493 16280 12456 189 -658 -466 C ATOM 3177 C ARG A 304 14.001 4.745 60.317 1.00122.32 C ANISOU 3177 C ARG A 304 17677 16103 12697 80 -559 -447 C ATOM 3178 O ARG A 304 13.951 4.630 59.091 1.00121.45 O ANISOU 3178 O ARG A 304 17521 15923 12703 49 -536 -418 O ATOM 3179 CB ARG A 304 16.284 5.041 61.361 1.00123.45 C ANISOU 3179 CB ARG A 304 17612 16716 12577 27 -729 -614 C ATOM 3180 CG ARG A 304 16.099 5.885 62.622 1.00134.00 C ANISOU 3180 CG ARG A 304 19037 18071 13806 -46 -729 -693 C ATOM 3181 N LYS A 305 13.106 5.475 61.023 1.00116.86 N ANISOU 3181 N LYS A 305 17123 15279 12001 33 -503 -464 N ATOM 3182 CA LYS A 305 11.968 6.197 60.425 1.00114.77 C ANISOU 3182 CA LYS A 305 16964 14783 11860 -44 -408 -449 C ATOM 3183 C LYS A 305 12.406 7.201 59.329 1.00117.01 C ANISOU 3183 C LYS A 305 17207 15042 12209 -218 -398 -521 C ATOM 3184 O LYS A 305 11.673 7.403 58.358 1.00115.47 O ANISOU 3184 O LYS A 305 17053 14685 12136 -235 -333 -481 O ATOM 3185 CB LYS A 305 11.152 6.929 61.505 1.00117.04 C ANISOU 3185 CB LYS A 305 17397 14975 12097 -66 -359 -475 C ATOM 3186 N GLU A 306 13.606 7.798 59.486 1.00113.17 N ANISOU 3186 N GLU A 306 16640 14726 11633 -344 -459 -631 N ATOM 3187 CA GLU A 306 14.185 8.783 58.568 1.00112.09 C ANISOU 3187 CA GLU A 306 16472 14585 11532 -533 -445 -716 C ATOM 3188 C GLU A 306 14.452 8.191 57.192 1.00111.43 C ANISOU 3188 C GLU A 306 16284 14499 11554 -506 -450 -662 C ATOM 3189 O GLU A 306 14.162 8.868 56.206 1.00110.25 O ANISOU 3189 O GLU A 306 16181 14216 11495 -603 -390 -670 O ATOM 3190 CB GLU A 306 15.481 9.399 59.131 1.00115.32 C ANISOU 3190 CB GLU A 306 16797 15215 11804 -681 -510 -857 C ATOM 3191 CG GLU A 306 15.285 10.237 60.380 1.00126.94 C ANISOU 3191 CG GLU A 306 18382 16680 13168 -755 -495 -937 C ATOM 3192 CD GLU A 306 15.329 9.426 61.658 1.00149.57 C ANISOU 3192 CD GLU A 306 21225 19683 15923 -598 -560 -907 C ATOM 3193 OE1 GLU A 306 14.258 8.945 62.094 1.00142.70 O ANISOU 3193 OE1 GLU A 306 20460 18671 15088 -453 -519 -809 O ATOM 3194 OE2 GLU A 306 16.438 9.248 62.211 1.00145.97 O ANISOU 3194 OE2 GLU A 306 20641 19485 15336 -615 -648 -984 O ATOM 3195 N VAL A 307 14.985 6.946 57.108 1.00105.75 N ANISOU 3195 N VAL A 307 15440 13923 10819 -368 -515 -605 N ATOM 3196 CA VAL A 307 15.251 6.329 55.798 1.00104.11 C ANISOU 3196 CA VAL A 307 15135 13714 10708 -336 -519 -553 C ATOM 3197 C VAL A 307 13.933 5.929 55.133 1.00104.78 C ANISOU 3197 C VAL A 307 15313 13571 10928 -249 -441 -445 C ATOM 3198 O VAL A 307 13.816 6.041 53.915 1.00102.98 O ANISOU 3198 O VAL A 307 15062 13263 10802 -291 -409 -427 O ATOM 3199 CB VAL A 307 16.275 5.155 55.770 1.00108.61 C ANISOU 3199 CB VAL A 307 15548 14502 11217 -212 -605 -529 C ATOM 3200 CG1 VAL A 307 17.693 5.652 56.017 1.00110.12 C ANISOU 3200 CG1 VAL A 307 15601 14952 11289 -328 -682 -653 C ATOM 3201 CG2 VAL A 307 15.912 4.026 56.730 1.00108.50 C ANISOU 3201 CG2 VAL A 307 15574 14510 11141 -5 -623 -443 C ATOM 3202 N TYR A 308 12.937 5.508 55.939 1.00100.88 N ANISOU 3202 N TYR A 308 14920 12980 10427 -137 -406 -383 N ATOM 3203 CA TYR A 308 11.620 5.078 55.465 1.00 98.91 C ANISOU 3203 CA TYR A 308 14750 12543 10290 -56 -328 -292 C ATOM 3204 C TYR A 308 10.882 6.231 54.752 1.00100.09 C ANISOU 3204 C TYR A 308 14978 12530 10521 -163 -258 -318 C ATOM 3205 O TYR A 308 10.321 6.009 53.679 1.00 98.84 O ANISOU 3205 O TYR A 308 14810 12275 10468 -141 -217 -268 O ATOM 3206 CB TYR A 308 10.777 4.503 56.627 1.00100.26 C ANISOU 3206 CB TYR A 308 15015 12666 10414 63 -300 -238 C ATOM 3207 CG TYR A 308 9.509 3.809 56.177 1.00101.58 C ANISOU 3207 CG TYR A 308 15235 12678 10681 148 -222 -150 C ATOM 3208 CD1 TYR A 308 9.549 2.537 55.608 1.00103.69 C ANISOU 3208 CD1 TYR A 308 15450 12955 10993 245 -220 -77 C ATOM 3209 CD2 TYR A 308 8.270 4.434 56.292 1.00101.92 C ANISOU 3209 CD2 TYR A 308 15380 12577 10770 128 -144 -146 C ATOM 3210 CE1 TYR A 308 8.389 1.910 55.155 1.00104.06 C ANISOU 3210 CE1 TYR A 308 15541 12871 11128 298 -141 -11 C ATOM 3211 CE2 TYR A 308 7.103 3.817 55.843 1.00102.14 C ANISOU 3211 CE2 TYR A 308 15433 12493 10882 193 -72 -79 C ATOM 3212 CZ TYR A 308 7.167 2.549 55.287 1.00110.48 C ANISOU 3212 CZ TYR A 308 16433 13563 11982 267 -69 -16 C ATOM 3213 OH TYR A 308 6.017 1.940 54.855 1.00111.66 O ANISOU 3213 OH TYR A 308 16605 13613 12207 309 9 35 O ATOM 3214 N ILE A 309 10.930 7.453 55.321 1.00 95.46 N ANISOU 3214 N ILE A 309 14474 11920 9876 -275 -242 -398 N ATOM 3215 CA ILE A 309 10.287 8.641 54.763 1.00 94.79 C ANISOU 3215 CA ILE A 309 14496 11677 9842 -363 -168 -425 C ATOM 3216 C ILE A 309 11.071 9.147 53.513 1.00 98.46 C ANISOU 3216 C ILE A 309 14903 12156 10351 -481 -171 -466 C ATOM 3217 O ILE A 309 10.433 9.533 52.525 1.00 97.37 O ANISOU 3217 O ILE A 309 14815 11884 10296 -484 -111 -437 O ATOM 3218 CB ILE A 309 10.091 9.728 55.856 1.00 98.69 C ANISOU 3218 CB ILE A 309 15122 12130 10246 -436 -140 -497 C ATOM 3219 CG1 ILE A 309 9.065 9.239 56.898 1.00 99.01 C ANISOU 3219 CG1 ILE A 309 15233 12122 10263 -307 -116 -442 C ATOM 3220 CG2 ILE A 309 9.637 11.078 55.269 1.00 99.50 C ANISOU 3220 CG2 ILE A 309 15358 12072 10378 -533 -58 -537 C ATOM 3221 CD1 ILE A 309 9.285 9.767 58.307 1.00111.26 C ANISOU 3221 CD1 ILE A 309 16858 13725 11691 -347 -131 -508 C ATOM 3222 N LEU A 310 12.427 9.104 53.540 1.00 94.80 N ANISOU 3222 N LEU A 310 14329 11865 9826 -569 -239 -532 N ATOM 3223 CA LEU A 310 13.269 9.528 52.411 1.00 94.13 C ANISOU 3223 CA LEU A 310 14177 11816 9773 -693 -241 -578 C ATOM 3224 C LEU A 310 13.020 8.631 51.171 1.00 95.11 C ANISOU 3224 C LEU A 310 14220 11906 10010 -595 -240 -488 C ATOM 3225 O LEU A 310 12.868 9.152 50.058 1.00 93.06 O ANISOU 3225 O LEU A 310 13989 11548 9820 -653 -191 -485 O ATOM 3226 CB LEU A 310 14.761 9.526 52.801 1.00 95.51 C ANISOU 3226 CB LEU A 310 14222 12223 9846 -796 -319 -672 C ATOM 3227 CG LEU A 310 15.767 9.835 51.683 1.00100.85 C ANISOU 3227 CG LEU A 310 14801 12974 10544 -929 -325 -727 C ATOM 3228 CD1 LEU A 310 15.896 11.336 51.447 1.00101.83 C ANISOU 3228 CD1 LEU A 310 15048 12996 10645 -1138 -249 -823 C ATOM 3229 CD2 LEU A 310 17.116 9.204 51.969 1.00104.57 C ANISOU 3229 CD2 LEU A 310 15080 13723 10928 -939 -423 -780 C ATOM 3230 N LEU A 311 12.944 7.294 51.382 1.00 90.60 N ANISOU 3230 N LEU A 311 13566 11407 9451 -445 -285 -414 N ATOM 3231 CA LEU A 311 12.679 6.305 50.332 1.00 88.37 C ANISOU 3231 CA LEU A 311 13215 11097 9266 -346 -281 -331 C ATOM 3232 C LEU A 311 11.242 6.430 49.796 1.00 90.10 C ANISOU 3232 C LEU A 311 13532 11123 9579 -292 -201 -270 C ATOM 3233 O LEU A 311 11.005 6.079 48.642 1.00 89.67 O ANISOU 3233 O LEU A 311 13436 11022 9611 -265 -181 -227 O ATOM 3234 CB LEU A 311 12.957 4.878 50.823 1.00 88.07 C ANISOU 3234 CB LEU A 311 13097 11169 9196 -201 -334 -274 C ATOM 3235 CG LEU A 311 14.434 4.501 51.011 1.00 92.80 C ANISOU 3235 CG LEU A 311 13560 11991 9708 -210 -421 -319 C ATOM 3236 CD1 LEU A 311 14.562 3.070 51.470 1.00 92.41 C ANISOU 3236 CD1 LEU A 311 13469 12021 9621 -31 -457 -246 C ATOM 3237 CD2 LEU A 311 15.232 4.684 49.723 1.00 94.46 C ANISOU 3237 CD2 LEU A 311 13667 12255 9968 -295 -433 -348 C ATOM 3238 N ASN A 312 10.302 6.966 50.609 1.00 84.68 N ANISOU 3238 N ASN A 312 12967 10338 8869 -275 -155 -272 N ATOM 3239 CA ASN A 312 8.921 7.230 50.194 1.00 82.49 C ANISOU 3239 CA ASN A 312 12778 9905 8661 -221 -78 -228 C ATOM 3240 C ASN A 312 8.888 8.449 49.253 1.00 85.91 C ANISOU 3240 C ASN A 312 13275 10245 9122 -312 -31 -264 C ATOM 3241 O ASN A 312 8.133 8.451 48.280 1.00 84.39 O ANISOU 3241 O ASN A 312 13092 9968 9004 -263 12 -222 O ATOM 3242 CB ASN A 312 8.019 7.465 51.413 1.00 79.56 C ANISOU 3242 CB ASN A 312 12512 9477 8239 -173 -43 -225 C ATOM 3243 CG ASN A 312 6.543 7.334 51.132 1.00 84.97 C ANISOU 3243 CG ASN A 312 13248 10050 8987 -81 28 -172 C ATOM 3244 OD1 ASN A 312 5.732 6.944 51.979 1.00 85.60 O ANISOU 3244 OD1 ASN A 312 13324 10065 9134 -70 64 -154 O ATOM 3245 ND2 ASN A 312 6.155 7.641 49.928 1.00 67.99 N ANISOU 3245 ND2 ASN A 312 11139 7888 6806 -10 49 -148 N ATOM 3246 N TRP A 313 9.715 9.481 49.557 1.00 83.77 N ANISOU 3246 N TRP A 313 13054 9993 8783 -447 -36 -346 N ATOM 3247 CA TRP A 313 9.844 10.726 48.787 1.00 84.08 C ANISOU 3247 CA TRP A 313 13188 9934 8826 -554 21 -390 C ATOM 3248 C TRP A 313 10.499 10.496 47.410 1.00 85.86 C ANISOU 3248 C TRP A 313 13319 10192 9114 -595 9 -380 C ATOM 3249 O TRP A 313 10.208 11.249 46.476 1.00 84.87 O ANISOU 3249 O TRP A 313 13274 9953 9019 -623 70 -378 O ATOM 3250 CB TRP A 313 10.602 11.805 49.582 1.00 84.66 C ANISOU 3250 CB TRP A 313 13346 10023 8798 -710 29 -492 C ATOM 3251 CG TRP A 313 9.656 12.712 50.317 1.00 86.46 C ANISOU 3251 CG TRP A 313 13756 10111 8982 -690 99 -504 C ATOM 3252 CD1 TRP A 313 9.125 12.507 51.559 1.00 89.58 C ANISOU 3252 CD1 TRP A 313 14188 10519 9330 -623 88 -499 C ATOM 3253 CD2 TRP A 313 8.992 13.872 49.784 1.00 86.72 C ANISOU 3253 CD2 TRP A 313 13966 9966 9018 -703 195 -509 C ATOM 3254 NE1 TRP A 313 8.199 13.483 51.846 1.00 89.30 N ANISOU 3254 NE1 TRP A 313 14331 10329 9268 -600 170 -505 N ATOM 3255 CE2 TRP A 313 8.109 14.344 50.780 1.00 90.83 C ANISOU 3255 CE2 TRP A 313 14619 10404 9489 -643 238 -511 C ATOM 3256 CE3 TRP A 313 9.067 14.564 48.561 1.00 88.21 C ANISOU 3256 CE3 TRP A 313 14223 10054 9238 -749 255 -509 C ATOM 3257 CZ2 TRP A 313 7.313 15.483 50.597 1.00 90.62 C ANISOU 3257 CZ2 TRP A 313 14790 10201 9438 -618 337 -514 C ATOM 3258 CZ3 TRP A 313 8.289 15.702 48.390 1.00 90.22 C ANISOU 3258 CZ3 TRP A 313 14685 10129 9465 -725 355 -510 C ATOM 3259 CH2 TRP A 313 7.425 16.149 49.399 1.00 91.14 C ANISOU 3259 CH2 TRP A 313 14930 10170 9528 -655 395 -512 C ATOM 3260 N ILE A 314 11.349 9.450 47.272 1.00 80.83 N ANISOU 3260 N ILE A 314 12519 9705 8487 -583 -66 -370 N ATOM 3261 CA ILE A 314 11.958 9.086 45.991 1.00 79.59 C ANISOU 3261 CA ILE A 314 12260 9591 8390 -606 -82 -355 C ATOM 3262 C ILE A 314 10.823 8.590 45.073 1.00 83.09 C ANISOU 3262 C ILE A 314 12711 9930 8929 -479 -44 -269 C ATOM 3263 O ILE A 314 10.841 8.856 43.876 1.00 82.18 O ANISOU 3263 O ILE A 314 12594 9766 8864 -500 -15 -258 O ATOM 3264 CB ILE A 314 13.106 8.054 46.175 1.00 82.28 C ANISOU 3264 CB ILE A 314 12430 10128 8705 -599 -169 -364 C ATOM 3265 CG1 ILE A 314 14.320 8.730 46.843 1.00 83.47 C ANISOU 3265 CG1 ILE A 314 12553 10409 8752 -751 -203 -470 C ATOM 3266 CG2 ILE A 314 13.504 7.387 44.830 1.00 81.78 C ANISOU 3266 CG2 ILE A 314 12256 10102 8717 -574 -184 -326 C ATOM 3267 CD1 ILE A 314 15.242 7.815 47.568 1.00 91.28 C ANISOU 3267 CD1 ILE A 314 13399 11609 9674 -707 -293 -486 C ATOM 3268 N GLY A 315 9.829 7.927 45.670 1.00 79.97 N ANISOU 3268 N GLY A 315 12328 9507 8549 -357 -39 -217 N ATOM 3269 CA GLY A 315 8.637 7.460 44.977 1.00 78.90 C ANISOU 3269 CA GLY A 315 12195 9294 8489 -245 0 -151 C ATOM 3270 C GLY A 315 7.767 8.630 44.560 1.00 83.41 C ANISOU 3270 C GLY A 315 12895 9734 9064 -242 73 -157 C ATOM 3271 O GLY A 315 7.258 8.655 43.435 1.00 82.53 O ANISOU 3271 O GLY A 315 12775 9575 9007 -196 103 -125 O ATOM 3272 N TYR A 316 7.636 9.634 45.460 1.00 80.68 N ANISOU 3272 N TYR A 316 12677 9331 8648 -285 104 -200 N ATOM 3273 CA TYR A 316 6.862 10.862 45.265 1.00 80.25 C ANISOU 3273 CA TYR A 316 12780 9141 8570 -271 182 -209 C ATOM 3274 C TYR A 316 7.395 11.715 44.121 1.00 85.47 C ANISOU 3274 C TYR A 316 13498 9740 9237 -348 217 -229 C ATOM 3275 O TYR A 316 6.587 12.281 43.383 1.00 85.86 O ANISOU 3275 O TYR A 316 13634 9691 9299 -274 278 -201 O ATOM 3276 CB TYR A 316 6.855 11.703 46.544 1.00 82.17 C ANISOU 3276 CB TYR A 316 13152 9342 8726 -321 204 -260 C ATOM 3277 CG TYR A 316 5.921 11.256 47.650 1.00 84.39 C ANISOU 3277 CG TYR A 316 13444 9632 8989 -221 205 -236 C ATOM 3278 CD1 TYR A 316 4.924 10.312 47.419 1.00 85.79 C ANISOU 3278 CD1 TYR A 316 13542 9830 9225 -92 208 -174 C ATOM 3279 CD2 TYR A 316 5.996 11.826 48.919 1.00 85.87 C ANISOU 3279 CD2 TYR A 316 13728 9803 9095 -263 214 -282 C ATOM 3280 CE1 TYR A 316 4.054 9.913 48.435 1.00 85.97 C ANISOU 3280 CE1 TYR A 316 13578 9861 9227 -14 221 -157 C ATOM 3281 CE2 TYR A 316 5.131 11.437 49.940 1.00 86.31 C ANISOU 3281 CE2 TYR A 316 13799 9864 9130 -172 221 -260 C ATOM 3282 CZ TYR A 316 4.152 10.495 49.690 1.00 90.53 C ANISOU 3282 CZ TYR A 316 14255 10419 9725 -48 228 -196 C ATOM 3283 OH TYR A 316 3.296 10.150 50.701 1.00 88.10 O ANISOU 3283 OH TYR A 316 13967 10115 9390 27 247 -180 O ATOM 3284 N VAL A 317 8.741 11.814 43.957 1.00 82.70 N ANISOU 3284 N VAL A 317 13100 9455 8869 -492 185 -279 N ATOM 3285 CA VAL A 317 9.346 12.640 42.890 1.00 82.71 C ANISOU 3285 CA VAL A 317 13161 9395 8868 -590 230 -306 C ATOM 3286 C VAL A 317 9.072 12.037 41.490 1.00 87.60 C ANISOU 3286 C VAL A 317 13694 10020 9570 -506 225 -244 C ATOM 3287 O VAL A 317 8.963 12.811 40.539 1.00 88.96 O ANISOU 3287 O VAL A 317 13964 10095 9741 -516 287 -238 O ATOM 3288 CB VAL A 317 10.851 13.001 43.069 1.00 85.93 C ANISOU 3288 CB VAL A 317 13539 9884 9225 -788 208 -392 C ATOM 3289 CG1 VAL A 317 11.095 13.728 44.387 1.00 86.08 C ANISOU 3289 CG1 VAL A 317 13659 9896 9153 -885 221 -466 C ATOM 3290 CG2 VAL A 317 11.768 11.789 42.922 1.00 85.10 C ANISOU 3290 CG2 VAL A 317 13217 9962 9155 -800 115 -388 C ATOM 3291 N ASN A 318 8.917 10.687 41.375 1.00 83.15 N ANISOU 3291 N ASN A 318 12965 9559 9068 -420 162 -197 N ATOM 3292 CA ASN A 318 8.597 9.962 40.124 1.00 81.73 C ANISOU 3292 CA ASN A 318 12691 9396 8965 -338 154 -142 C ATOM 3293 C ASN A 318 7.346 10.518 39.426 1.00 86.33 C ANISOU 3293 C ASN A 318 13370 9871 9559 -225 219 -104 C ATOM 3294 O ASN A 318 7.275 10.519 38.193 1.00 86.63 O ANISOU 3294 O ASN A 318 13389 9894 9634 -194 235 -78 O ATOM 3295 CB ASN A 318 8.381 8.471 40.392 1.00 77.22 C ANISOU 3295 CB ASN A 318 11972 8927 8443 -256 95 -102 C ATOM 3296 CG ASN A 318 8.020 7.676 39.159 1.00 87.99 C ANISOU 3296 CG ASN A 318 13242 10309 9880 -182 91 -55 C ATOM 3297 OD1 ASN A 318 6.850 7.344 38.919 1.00 76.30 O ANISOU 3297 OD1 ASN A 318 11757 8804 8430 -77 116 -20 O ATOM 3298 ND2 ASN A 318 9.010 7.437 38.306 1.00 79.54 N ANISOU 3298 ND2 ASN A 318 12097 9290 8836 -243 65 -62 N ATOM 3299 N SER A 319 6.383 11.002 40.223 1.00 82.59 N ANISOU 3299 N SER A 319 12998 9337 9046 -155 256 -102 N ATOM 3300 CA SER A 319 5.113 11.570 39.806 1.00 82.23 C ANISOU 3300 CA SER A 319 13044 9211 8988 -22 318 -71 C ATOM 3301 C SER A 319 5.308 12.879 38.942 1.00 88.38 C ANISOU 3301 C SER A 319 13988 9869 9723 -43 389 -79 C ATOM 3302 O SER A 319 4.349 13.353 38.317 1.00 87.69 O ANISOU 3302 O SER A 319 13975 9724 9618 88 439 -47 O ATOM 3303 CB SER A 319 4.277 11.822 41.055 1.00 85.64 C ANISOU 3303 CB SER A 319 13549 9617 9372 37 339 -79 C ATOM 3304 OG SER A 319 3.033 12.429 40.770 1.00100.50 O ANISOU 3304 OG SER A 319 15520 11440 11227 179 400 -55 O ATOM 3305 N GLY A 320 6.547 13.390 38.884 1.00 86.47 N ANISOU 3305 N GLY A 320 13796 9601 9459 -205 395 -124 N ATOM 3306 CA GLY A 320 6.931 14.566 38.111 1.00 87.93 C ANISOU 3306 CA GLY A 320 14148 9664 9597 -263 473 -140 C ATOM 3307 C GLY A 320 7.877 14.307 36.948 1.00 95.03 C ANISOU 3307 C GLY A 320 14968 10602 10538 -349 459 -140 C ATOM 3308 O GLY A 320 8.176 15.233 36.187 1.00 95.84 O ANISOU 3308 O GLY A 320 15213 10599 10602 -396 532 -148 O ATOM 3309 N PHE A 321 8.348 13.049 36.786 1.00 92.21 N ANISOU 3309 N PHE A 321 14396 10389 10251 -365 372 -130 N ATOM 3310 CA PHE A 321 9.283 12.635 35.733 1.00 92.06 C ANISOU 3310 CA PHE A 321 14273 10430 10274 -440 349 -131 C ATOM 3311 C PHE A 321 8.619 12.205 34.432 1.00 95.95 C ANISOU 3311 C PHE A 321 14715 10923 10818 -308 352 -69 C ATOM 3312 O PHE A 321 9.220 12.411 33.381 1.00 95.50 O ANISOU 3312 O PHE A 321 14663 10852 10769 -360 374 -68 O ATOM 3313 CB PHE A 321 10.166 11.465 36.209 1.00 93.38 C ANISOU 3313 CB PHE A 321 14241 10758 10480 -506 256 -150 C ATOM 3314 CG PHE A 321 11.200 11.790 37.257 1.00 95.86 C ANISOU 3314 CG PHE A 321 14559 11124 10738 -662 238 -224 C ATOM 3315 CD1 PHE A 321 11.841 13.026 37.267 1.00100.57 C ANISOU 3315 CD1 PHE A 321 15299 11645 11269 -814 305 -287 C ATOM 3316 CD2 PHE A 321 11.575 10.844 38.200 1.00 97.66 C ANISOU 3316 CD2 PHE A 321 14651 11485 10971 -661 158 -235 C ATOM 3317 CE1 PHE A 321 12.795 13.328 38.241 1.00102.61 C ANISOU 3317 CE1 PHE A 321 15547 11973 11466 -973 288 -370 C ATOM 3318 CE2 PHE A 321 12.532 11.143 39.168 1.00101.60 C ANISOU 3318 CE2 PHE A 321 15140 12059 11405 -796 134 -310 C ATOM 3319 CZ PHE A 321 13.133 12.384 39.183 1.00101.32 C ANISOU 3319 CZ PHE A 321 15229 11962 11304 -957 197 -381 C ATOM 3320 N ASN A 322 7.440 11.543 34.490 1.00 93.16 N ANISOU 3320 N ASN A 322 14297 10604 10496 -151 330 -26 N ATOM 3321 CA ASN A 322 6.754 11.010 33.297 1.00 92.85 C ANISOU 3321 CA ASN A 322 14182 10597 10502 -28 325 22 C ATOM 3322 C ASN A 322 6.519 12.039 32.173 1.00 96.94 C ANISOU 3322 C ASN A 322 14843 11014 10978 25 397 42 C ATOM 3323 O ASN A 322 6.813 11.667 31.033 1.00 96.22 O ANISOU 3323 O ASN A 322 14680 10957 10921 31 386 61 O ATOM 3324 CB ASN A 322 5.447 10.321 33.636 1.00 93.51 C ANISOU 3324 CB ASN A 322 14191 10734 10604 115 306 48 C ATOM 3325 CG ASN A 322 5.622 8.904 34.097 1.00111.28 C ANISOU 3325 CG ASN A 322 16268 13096 12916 91 238 47 C ATOM 3326 OD1 ASN A 322 6.703 8.481 34.518 1.00103.46 O ANISOU 3326 OD1 ASN A 322 15222 12147 11941 -17 197 27 O ATOM 3327 ND2 ASN A 322 4.531 8.163 34.090 1.00104.28 N ANISOU 3327 ND2 ASN A 322 15300 12265 12054 196 231 66 N ATOM 3328 N PRO A 323 6.045 13.301 32.412 1.00 93.84 N ANISOU 3328 N PRO A 323 14659 10493 10505 70 476 41 N ATOM 3329 CA PRO A 323 5.890 14.247 31.285 1.00 93.80 C ANISOU 3329 CA PRO A 323 14809 10384 10448 133 553 67 C ATOM 3330 C PRO A 323 7.199 14.448 30.505 1.00 95.88 C ANISOU 3330 C PRO A 323 15089 10620 10721 -26 572 47 C ATOM 3331 O PRO A 323 7.174 14.488 29.276 1.00 94.90 O ANISOU 3331 O PRO A 323 14972 10486 10600 29 592 79 O ATOM 3332 CB PRO A 323 5.436 15.541 31.971 1.00 96.76 C ANISOU 3332 CB PRO A 323 15425 10613 10725 170 639 58 C ATOM 3333 CG PRO A 323 4.812 15.091 33.236 1.00101.17 C ANISOU 3333 CG PRO A 323 15912 11233 11296 208 595 45 C ATOM 3334 CD PRO A 323 5.633 13.933 33.684 1.00 95.93 C ANISOU 3334 CD PRO A 323 15043 10694 10713 75 505 18 C ATOM 3335 N LEU A 324 8.344 14.475 31.215 1.00 91.68 N ANISOU 3335 N LEU A 324 14539 10101 10194 -223 558 -9 N ATOM 3336 CA LEU A 324 9.679 14.636 30.644 1.00 91.39 C ANISOU 3336 CA LEU A 324 14494 10068 10162 -401 574 -45 C ATOM 3337 C LEU A 324 10.083 13.446 29.753 1.00 92.14 C ANISOU 3337 C LEU A 324 14371 10299 10339 -391 500 -22 C ATOM 3338 O LEU A 324 10.787 13.662 28.770 1.00 91.70 O ANISOU 3338 O LEU A 324 14331 10228 10283 -462 533 -25 O ATOM 3339 CB LEU A 324 10.731 14.869 31.748 1.00 92.37 C ANISOU 3339 CB LEU A 324 14617 10218 10261 -606 566 -123 C ATOM 3340 CG LEU A 324 10.398 15.958 32.790 1.00 99.35 C ANISOU 3340 CG LEU A 324 15709 10976 11063 -637 635 -157 C ATOM 3341 CD1 LEU A 324 11.448 16.015 33.871 1.00100.94 C ANISOU 3341 CD1 LEU A 324 15868 11245 11241 -840 610 -243 C ATOM 3342 CD2 LEU A 324 10.249 17.351 32.161 1.00103.88 C ANISOU 3342 CD2 LEU A 324 16563 11353 11554 -643 769 -153 C ATOM 3343 N ILE A 325 9.613 12.216 30.065 1.00 86.86 N ANISOU 3343 N ILE A 325 13516 9752 9736 -302 412 -1 N ATOM 3344 CA ILE A 325 9.890 11.013 29.264 1.00 85.06 C ANISOU 3344 CA ILE A 325 13094 9643 9581 -278 348 21 C ATOM 3345 C ILE A 325 9.037 11.070 27.961 1.00 90.03 C ANISOU 3345 C ILE A 325 13750 10241 10215 -132 376 73 C ATOM 3346 O ILE A 325 9.481 10.558 26.929 1.00 90.40 O ANISOU 3346 O ILE A 325 13708 10340 10300 -142 359 86 O ATOM 3347 CB ILE A 325 9.681 9.679 30.069 1.00 86.70 C ANISOU 3347 CB ILE A 325 13125 9973 9846 -239 261 24 C ATOM 3348 CG1 ILE A 325 10.476 9.673 31.403 1.00 86.78 C ANISOU 3348 CG1 ILE A 325 13117 10023 9832 -359 231 -24 C ATOM 3349 CG2 ILE A 325 10.023 8.428 29.221 1.00 86.10 C ANISOU 3349 CG2 ILE A 325 12872 10005 9839 -218 206 44 C ATOM 3350 CD1 ILE A 325 10.078 8.613 32.393 1.00 87.68 C ANISOU 3350 CD1 ILE A 325 13122 10218 9975 -299 168 -15 C ATOM 3351 N TYR A 326 7.853 11.737 27.990 1.00 86.53 N ANISOU 3351 N TYR A 326 13432 9723 9723 8 422 99 N ATOM 3352 CA TYR A 326 6.977 11.863 26.815 1.00 86.31 C ANISOU 3352 CA TYR A 326 13429 9686 9677 169 448 144 C ATOM 3353 C TYR A 326 7.563 12.794 25.749 1.00 91.44 C ANISOU 3353 C TYR A 326 14229 10235 10279 134 522 156 C ATOM 3354 O TYR A 326 7.079 12.809 24.620 1.00 89.79 O ANISOU 3354 O TYR A 326 14027 10033 10055 255 537 193 O ATOM 3355 CB TYR A 326 5.564 12.331 27.205 1.00 87.95 C ANISOU 3355 CB TYR A 326 13721 9866 9830 344 475 165 C ATOM 3356 CG TYR A 326 4.882 11.444 28.221 1.00 89.62 C ANISOU 3356 CG TYR A 326 13795 10175 10082 379 415 152 C ATOM 3357 CD1 TYR A 326 5.036 10.058 28.178 1.00 91.31 C ANISOU 3357 CD1 TYR A 326 13801 10514 10379 343 342 145 C ATOM 3358 CD2 TYR A 326 4.055 11.975 29.198 1.00 91.07 C ANISOU 3358 CD2 TYR A 326 14067 10319 10215 452 441 148 C ATOM 3359 CE1 TYR A 326 4.414 9.235 29.115 1.00 92.16 C ANISOU 3359 CE1 TYR A 326 13804 10696 10517 366 302 134 C ATOM 3360 CE2 TYR A 326 3.450 11.165 30.158 1.00 91.67 C ANISOU 3360 CE2 TYR A 326 14024 10482 10325 473 396 135 C ATOM 3361 CZ TYR A 326 3.637 9.794 30.113 1.00 98.45 C ANISOU 3361 CZ TYR A 326 14686 11455 11264 425 329 128 C ATOM 3362 OH TYR A 326 3.048 8.978 31.036 1.00 98.79 O ANISOU 3362 OH TYR A 326 14632 11570 11334 439 298 115 O ATOM 3363 N CYS A 327 8.618 13.543 26.094 1.00 90.99 N ANISOU 3363 N CYS A 327 14289 10092 10192 -37 572 119 N ATOM 3364 CA CYS A 327 9.295 14.439 25.165 1.00 92.70 C ANISOU 3364 CA CYS A 327 14662 10202 10358 -108 659 121 C ATOM 3365 C CYS A 327 10.115 13.648 24.144 1.00 96.43 C ANISOU 3365 C CYS A 327 14977 10770 10892 -174 619 123 C ATOM 3366 O CYS A 327 10.542 14.230 23.146 1.00 98.04 O ANISOU 3366 O CYS A 327 15289 10903 11061 -204 688 135 O ATOM 3367 CB CYS A 327 10.155 15.445 25.918 1.00 95.04 C ANISOU 3367 CB CYS A 327 15124 10387 10599 -297 732 66 C ATOM 3368 SG CYS A 327 9.218 16.823 26.636 1.00100.65 S ANISOU 3368 SG CYS A 327 16130 10912 11200 -201 833 75 S ATOM 3369 N ARG A 328 10.297 12.321 24.361 1.00 91.01 N ANISOU 3369 N ARG A 328 14050 10237 10291 -186 516 114 N ATOM 3370 CA ARG A 328 10.987 11.407 23.441 1.00 89.59 C ANISOU 3370 CA ARG A 328 13705 10161 10172 -224 471 118 C ATOM 3371 C ARG A 328 10.176 11.205 22.155 1.00 93.90 C ANISOU 3371 C ARG A 328 14244 10716 10719 -60 476 170 C ATOM 3372 O ARG A 328 10.750 10.897 21.109 1.00 94.95 O ANISOU 3372 O ARG A 328 14321 10883 10873 -88 476 178 O ATOM 3373 CB ARG A 328 11.217 10.047 24.099 1.00 86.65 C ANISOU 3373 CB ARG A 328 13112 9934 9877 -245 370 101 C ATOM 3374 CG ARG A 328 12.340 9.997 25.120 1.00 93.60 C ANISOU 3374 CG ARG A 328 13945 10860 10758 -413 347 46 C ATOM 3375 CD ARG A 328 12.432 8.620 25.763 1.00 98.75 C ANISOU 3375 CD ARG A 328 14402 11647 11472 -389 253 43 C ATOM 3376 NE ARG A 328 12.259 7.543 24.782 1.00106.76 N ANISOU 3376 NE ARG A 328 15285 12735 12544 -305 214 76 N ATOM 3377 CZ ARG A 328 13.238 7.029 24.044 1.00118.95 C ANISOU 3377 CZ ARG A 328 16729 14352 14115 -364 196 68 C ATOM 3378 NH1 ARG A 328 14.488 7.456 24.188 1.00111.43 N ANISOU 3378 NH1 ARG A 328 15773 13430 13137 -512 209 24 N ATOM 3379 NH2 ARG A 328 12.974 6.076 23.158 1.00 94.43 N ANISOU 3379 NH2 ARG A 328 13522 11300 11057 -280 167 97 N ATOM 3380 N SER A 329 8.846 11.351 22.242 1.00 89.38 N ANISOU 3380 N SER A 329 13716 10128 10117 115 479 200 N ATOM 3381 CA SER A 329 7.936 11.221 21.111 1.00 89.24 C ANISOU 3381 CA SER A 329 13687 10141 10079 290 481 241 C ATOM 3382 C SER A 329 7.809 12.556 20.367 1.00 95.32 C ANISOU 3382 C SER A 329 14694 10774 10750 356 582 272 C ATOM 3383 O SER A 329 7.503 13.567 21.004 1.00 96.45 O ANISOU 3383 O SER A 329 15021 10802 10823 380 644 274 O ATOM 3384 CB SER A 329 6.564 10.743 21.581 1.00 92.74 C ANISOU 3384 CB SER A 329 14050 10662 10524 445 438 248 C ATOM 3385 OG SER A 329 5.614 10.732 20.526 1.00103.10 O ANISOU 3385 OG SER A 329 15351 12025 11798 622 442 277 O ATOM 3386 N PRO A 330 8.001 12.596 19.024 1.00 92.69 N ANISOU 3386 N PRO A 330 14377 10443 10400 399 606 300 N ATOM 3387 CA PRO A 330 7.832 13.870 18.290 1.00 93.43 C ANISOU 3387 CA PRO A 330 14721 10395 10384 484 712 338 C ATOM 3388 C PRO A 330 6.401 14.416 18.383 1.00 97.37 C ANISOU 3388 C PRO A 330 15322 10877 10796 724 733 373 C ATOM 3389 O PRO A 330 6.230 15.625 18.481 1.00 97.71 O ANISOU 3389 O PRO A 330 15616 10768 10739 779 829 395 O ATOM 3390 CB PRO A 330 8.196 13.503 16.844 1.00 94.92 C ANISOU 3390 CB PRO A 330 14854 10631 10582 504 711 361 C ATOM 3391 CG PRO A 330 8.946 12.215 16.938 1.00 98.07 C ANISOU 3391 CG PRO A 330 15003 11163 11097 366 621 324 C ATOM 3392 CD PRO A 330 8.359 11.495 18.103 1.00 93.06 C ANISOU 3392 CD PRO A 330 14230 10613 10516 382 544 300 C ATOM 3393 N ASP A 331 5.385 13.525 18.411 1.00 93.90 N ANISOU 3393 N ASP A 331 14692 10596 10388 860 648 372 N ATOM 3394 CA ASP A 331 3.964 13.874 18.532 1.00 94.46 C ANISOU 3394 CA ASP A 331 14803 10707 10379 1093 653 394 C ATOM 3395 C ASP A 331 3.680 14.699 19.798 1.00 96.88 C ANISOU 3395 C ASP A 331 15265 10905 10639 1095 699 386 C ATOM 3396 O ASP A 331 2.947 15.687 19.723 1.00 98.39 O ANISOU 3396 O ASP A 331 15646 11021 10717 1272 767 419 O ATOM 3397 CB ASP A 331 3.089 12.609 18.531 1.00 95.86 C ANISOU 3397 CB ASP A 331 14710 11095 10616 1168 552 369 C ATOM 3398 CG ASP A 331 2.966 11.937 17.177 1.00109.43 C ANISOU 3398 CG ASP A 331 16300 12936 12344 1235 515 377 C ATOM 3399 OD1 ASP A 331 2.933 12.660 16.154 1.00112.01 O ANISOU 3399 OD1 ASP A 331 16764 13212 12584 1348 569 417 O ATOM 3400 OD2 ASP A 331 2.832 10.696 17.143 1.00115.07 O ANISOU 3400 OD2 ASP A 331 16786 13793 13141 1185 438 342 O ATOM 3401 N PHE A 332 4.283 14.312 20.943 1.00 89.96 N ANISOU 3401 N PHE A 332 14319 10020 9843 910 667 344 N ATOM 3402 CA PHE A 332 4.139 15.029 22.214 1.00 88.55 C ANISOU 3402 CA PHE A 332 14278 9739 9626 881 707 329 C ATOM 3403 C PHE A 332 4.923 16.335 22.194 1.00 92.59 C ANISOU 3403 C PHE A 332 15074 10042 10063 791 822 335 C ATOM 3404 O PHE A 332 4.390 17.338 22.672 1.00 93.73 O ANISOU 3404 O PHE A 332 15429 10070 10115 886 895 348 O ATOM 3405 CB PHE A 332 4.568 14.171 23.407 1.00 88.51 C ANISOU 3405 CB PHE A 332 14107 9802 9720 716 634 281 C ATOM 3406 CG PHE A 332 3.489 13.266 23.951 1.00 88.47 C ANISOU 3406 CG PHE A 332 13916 9947 9752 820 560 271 C ATOM 3407 CD1 PHE A 332 3.328 11.975 23.461 1.00 89.71 C ANISOU 3407 CD1 PHE A 332 13838 10261 9986 822 482 262 C ATOM 3408 CD2 PHE A 332 2.649 13.693 24.972 1.00 90.33 C ANISOU 3408 CD2 PHE A 332 14218 10163 9941 905 578 266 C ATOM 3409 CE1 PHE A 332 2.332 11.134 23.968 1.00 89.33 C ANISOU 3409 CE1 PHE A 332 13629 10346 9966 895 429 244 C ATOM 3410 CE2 PHE A 332 1.647 12.853 25.472 1.00 91.91 C ANISOU 3410 CE2 PHE A 332 14243 10507 10170 988 519 250 C ATOM 3411 CZ PHE A 332 1.497 11.581 24.966 1.00 88.58 C ANISOU 3411 CZ PHE A 332 13594 10238 9824 974 449 237 C ATOM 3412 N ARG A 333 6.161 16.340 21.619 1.00 87.91 N ANISOU 3412 N ARG A 333 14496 9402 9502 610 846 321 N ATOM 3413 CA ARG A 333 7.015 17.537 21.494 1.00 88.71 C ANISOU 3413 CA ARG A 333 14865 9309 9532 484 969 315 C ATOM 3414 C ARG A 333 6.309 18.657 20.750 1.00 93.59 C ANISOU 3414 C ARG A 333 15754 9789 10016 687 1077 373 C ATOM 3415 O ARG A 333 6.415 19.815 21.160 1.00 95.73 O ANISOU 3415 O ARG A 333 16303 9875 10197 661 1191 371 O ATOM 3416 CB ARG A 333 8.315 17.209 20.761 1.00 89.29 C ANISOU 3416 CB ARG A 333 14868 9399 9658 286 971 293 C ATOM 3417 CG ARG A 333 9.550 17.097 21.645 1.00100.59 C ANISOU 3417 CG ARG A 333 16244 10834 11143 8 962 220 C ATOM 3418 CD ARG A 333 10.790 16.763 20.820 1.00112.81 C ANISOU 3418 CD ARG A 333 17706 12423 12733 -166 966 197 C ATOM 3419 NE ARG A 333 10.709 15.437 20.197 1.00122.56 N ANISOU 3419 NE ARG A 333 18670 13837 14058 -100 854 216 N ATOM 3420 CZ ARG A 333 11.592 14.958 19.327 1.00142.61 C ANISOU 3420 CZ ARG A 333 21106 16441 16640 -195 842 208 C ATOM 3421 NH1 ARG A 333 12.640 15.685 18.962 1.00138.08 N ANISOU 3421 NH1 ARG A 333 20659 15778 16025 -371 935 179 N ATOM 3422 NH2 ARG A 333 11.435 13.743 18.817 1.00128.89 N ANISOU 3422 NH2 ARG A 333 19137 14855 14979 -124 744 223 N ATOM 3423 N ILE A 334 5.585 18.306 19.660 1.00 88.84 N ANISOU 3423 N ILE A 334 15081 9281 9393 895 1046 423 N ATOM 3424 CA ILE A 334 4.837 19.231 18.801 1.00 89.76 C ANISOU 3424 CA ILE A 334 15428 9306 9372 1138 1135 487 C ATOM 3425 C ILE A 334 3.655 19.832 19.587 1.00 93.58 C ANISOU 3425 C ILE A 334 16029 9761 9768 1345 1159 505 C ATOM 3426 O ILE A 334 3.448 21.048 19.516 1.00 95.30 O ANISOU 3426 O ILE A 334 16559 9796 9855 1450 1282 539 O ATOM 3427 CB ILE A 334 4.416 18.536 17.455 1.00 92.33 C ANISOU 3427 CB ILE A 334 15594 9785 9701 1296 1075 524 C ATOM 3428 CG1 ILE A 334 5.516 18.711 16.381 1.00 92.83 C ANISOU 3428 CG1 ILE A 334 15739 9766 9765 1164 1134 536 C ATOM 3429 CG2 ILE A 334 3.075 19.055 16.889 1.00 93.55 C ANISOU 3429 CG2 ILE A 334 15853 9971 9721 1638 1100 582 C ATOM 3430 CD1 ILE A 334 6.657 17.730 16.372 1.00 96.54 C ANISOU 3430 CD1 ILE A 334 15983 10324 10374 905 1064 485 C ATOM 3431 N ALA A 335 2.906 18.993 20.344 1.00 87.87 N ANISOU 3431 N ALA A 335 15069 9210 9109 1399 1051 479 N ATOM 3432 CA ALA A 335 1.775 19.450 21.158 1.00 87.42 C ANISOU 3432 CA ALA A 335 15084 9155 8977 1588 1064 488 C ATOM 3433 C ALA A 335 2.254 20.363 22.300 1.00 91.52 C ANISOU 3433 C ALA A 335 15835 9475 9465 1451 1151 463 C ATOM 3434 O ALA A 335 1.623 21.386 22.542 1.00 92.24 O ANISOU 3434 O ALA A 335 16171 9445 9432 1617 1240 492 O ATOM 3435 CB ALA A 335 1.001 18.264 21.715 1.00 86.45 C ANISOU 3435 CB ALA A 335 14644 9264 8940 1628 936 456 C ATOM 3436 N PHE A 336 3.392 20.017 22.955 1.00 87.20 N ANISOU 3436 N PHE A 336 15218 8897 9018 1153 1128 407 N ATOM 3437 CA PHE A 336 3.975 20.769 24.071 1.00 87.24 C ANISOU 3437 CA PHE A 336 15406 8740 9001 979 1199 365 C ATOM 3438 C PHE A 336 4.477 22.147 23.626 1.00 94.62 C ANISOU 3438 C PHE A 336 16711 9424 9816 947 1363 382 C ATOM 3439 O PHE A 336 4.190 23.143 24.309 1.00 95.20 O ANISOU 3439 O PHE A 336 17041 9337 9795 987 1459 380 O ATOM 3440 CB PHE A 336 5.120 19.985 24.760 1.00 87.53 C ANISOU 3440 CB PHE A 336 15247 8845 9164 678 1127 295 C ATOM 3441 CG PHE A 336 4.751 18.742 25.551 1.00 87.51 C ANISOU 3441 CG PHE A 336 14939 9041 9268 671 990 270 C ATOM 3442 CD1 PHE A 336 3.446 18.531 25.990 1.00 89.85 C ANISOU 3442 CD1 PHE A 336 15173 9423 9543 882 951 291 C ATOM 3443 CD2 PHE A 336 5.714 17.785 25.864 1.00 88.73 C ANISOU 3443 CD2 PHE A 336 14878 9301 9535 457 907 224 C ATOM 3444 CE1 PHE A 336 3.107 17.380 26.711 1.00 89.22 C ANISOU 3444 CE1 PHE A 336 14829 9514 9556 862 840 265 C ATOM 3445 CE2 PHE A 336 5.373 16.631 26.587 1.00 89.98 C ANISOU 3445 CE2 PHE A 336 14784 9623 9780 459 794 206 C ATOM 3446 CZ PHE A 336 4.071 16.439 27.005 1.00 87.61 C ANISOU 3446 CZ PHE A 336 14437 9390 9461 652 766 226 C ATOM 3447 N GLN A 337 5.211 22.220 22.488 1.00 92.61 N ANISOU 3447 N GLN A 337 16502 9126 9558 874 1405 398 N ATOM 3448 CA GLN A 337 5.714 23.510 21.992 1.00 94.68 C ANISOU 3448 CA GLN A 337 17134 9139 9701 830 1578 414 C ATOM 3449 C GLN A 337 4.554 24.427 21.542 1.00 99.20 C ANISOU 3449 C GLN A 337 17973 9602 10116 1166 1669 493 C ATOM 3450 O GLN A 337 4.696 25.646 21.603 1.00101.29 O ANISOU 3450 O GLN A 337 18602 9626 10258 1166 1827 504 O ATOM 3451 CB GLN A 337 6.765 23.339 20.885 1.00 96.43 C ANISOU 3451 CB GLN A 337 17334 9350 9955 670 1605 412 C ATOM 3452 CG GLN A 337 6.278 22.718 19.587 1.00117.61 C ANISOU 3452 CG GLN A 337 19875 12166 12645 873 1543 475 C ATOM 3453 CD GLN A 337 7.428 22.297 18.714 1.00143.59 C ANISOU 3453 CD GLN A 337 23072 15485 16001 671 1541 456 C ATOM 3454 OE1 GLN A 337 8.453 21.784 19.188 1.00137.86 O ANISOU 3454 OE1 GLN A 337 22187 14819 15376 397 1497 387 O ATOM 3455 NE2 GLN A 337 7.261 22.475 17.411 1.00141.34 N ANISOU 3455 NE2 GLN A 337 22872 15177 15652 817 1585 517 N ATOM 3456 N GLU A 338 3.405 23.837 21.154 1.00 94.28 N ANISOU 3456 N GLU A 338 17172 9163 9489 1450 1574 541 N ATOM 3457 CA GLU A 338 2.181 24.543 20.781 1.00 95.31 C ANISOU 3457 CA GLU A 338 17489 9257 9466 1809 1632 612 C ATOM 3458 C GLU A 338 1.488 25.067 22.036 1.00 98.75 C ANISOU 3458 C GLU A 338 18036 9635 9848 1894 1659 597 C ATOM 3459 O GLU A 338 1.136 26.243 22.080 1.00101.07 O ANISOU 3459 O GLU A 338 18678 9733 9992 2046 1796 635 O ATOM 3460 CB GLU A 338 1.241 23.620 19.978 1.00 96.16 C ANISOU 3460 CB GLU A 338 17313 9630 9593 2052 1507 646 C ATOM 3461 CG GLU A 338 0.024 24.328 19.391 1.00109.83 C ANISOU 3461 CG GLU A 338 19218 11364 11149 2446 1562 719 C ATOM 3462 CD GLU A 338 0.333 25.390 18.352 1.00135.43 C ANISOU 3462 CD GLU A 338 22818 14393 14246 2549 1713 784 C ATOM 3463 OE1 GLU A 338 1.150 25.119 17.440 1.00133.23 O ANISOU 3463 OE1 GLU A 338 22509 14101 14013 2412 1718 789 O ATOM 3464 OE2 GLU A 338 -0.246 26.495 18.450 1.00131.07 O ANISOU 3464 OE2 GLU A 338 22587 13684 13528 2773 1832 832 O ATOM 3465 N LEU A 339 1.303 24.198 23.060 1.00 93.21 N ANISOU 3465 N LEU A 339 17055 9097 9263 1800 1537 544 N ATOM 3466 CA LEU A 339 0.668 24.545 24.343 1.00 92.79 C ANISOU 3466 CA LEU A 339 17063 9016 9176 1859 1547 522 C ATOM 3467 C LEU A 339 1.498 25.528 25.176 1.00 97.05 C ANISOU 3467 C LEU A 339 17900 9298 9677 1640 1672 481 C ATOM 3468 O LEU A 339 0.917 26.244 25.992 1.00 97.66 O ANISOU 3468 O LEU A 339 18164 9276 9668 1747 1736 482 O ATOM 3469 CB LEU A 339 0.379 23.308 25.186 1.00 90.69 C ANISOU 3469 CB LEU A 339 16426 8983 9049 1784 1392 474 C ATOM 3470 CG LEU A 339 -0.676 22.343 24.677 1.00 94.40 C ANISOU 3470 CG LEU A 339 16600 9720 9546 2000 1275 495 C ATOM 3471 CD1 LEU A 339 -0.683 21.090 25.529 1.00 92.53 C ANISOU 3471 CD1 LEU A 339 16028 9672 9456 1851 1143 439 C ATOM 3472 CD2 LEU A 339 -2.056 22.993 24.616 1.00 97.62 C ANISOU 3472 CD2 LEU A 339 17126 10160 9805 2358 1317 541 C ATOM 3473 N LEU A 340 2.835 25.553 24.990 1.00 92.94 N ANISOU 3473 N LEU A 340 17415 8682 9214 1332 1708 439 N ATOM 3474 CA LEU A 340 3.720 26.481 25.694 1.00 93.71 C ANISOU 3474 CA LEU A 340 17786 8549 9269 1086 1834 383 C ATOM 3475 C LEU A 340 4.044 27.701 24.809 1.00100.09 C ANISOU 3475 C LEU A 340 18998 9096 9935 1115 2021 421 C ATOM 3476 O LEU A 340 4.842 28.551 25.214 1.00101.78 O ANISOU 3476 O LEU A 340 19476 9097 10099 890 2153 370 O ATOM 3477 CB LEU A 340 4.998 25.790 26.203 1.00 92.54 C ANISOU 3477 CB LEU A 340 17424 8479 9259 712 1763 294 C ATOM 3478 CG LEU A 340 4.814 24.753 27.338 1.00 95.16 C ANISOU 3478 CG LEU A 340 17431 9016 9710 650 1608 248 C ATOM 3479 CD1 LEU A 340 6.097 23.987 27.581 1.00 93.90 C ANISOU 3479 CD1 LEU A 340 17046 8960 9672 328 1532 174 C ATOM 3480 CD2 LEU A 340 4.323 25.402 28.635 1.00 96.87 C ANISOU 3480 CD2 LEU A 340 17808 9135 9861 678 1655 220 C ATOM 3481 N CYS A 341 3.378 27.788 23.622 1.00 96.54 N ANISOU 3481 N CYS A 341 18602 8667 9411 1399 2038 508 N ATOM 3482 CA ACYS A 341 3.496 28.881 22.650 0.50 98.71 C ANISOU 3482 CA ACYS A 341 19264 8707 9534 1499 2214 566 C ATOM 3483 CA BCYS A 341 3.497 28.873 22.642 0.50 98.06 C ANISOU 3483 CA BCYS A 341 19179 8626 9452 1499 2213 566 C ATOM 3484 C CYS A 341 4.979 29.231 22.391 1.00103.83 C ANISOU 3484 C CYS A 341 20050 9193 10208 1127 2318 508 C ATOM 3485 O CYS A 341 5.402 30.385 22.580 1.00105.71 O ANISOU 3485 O CYS A 341 20676 9156 10334 1020 2502 490 O ATOM 3486 CB ACYS A 341 2.698 30.104 23.103 0.50101.09 C ANISOU 3486 CB ACYS A 341 19954 8797 9660 1728 2358 605 C ATOM 3487 CB BCYS A 341 2.685 30.090 23.083 0.50 99.90 C ANISOU 3487 CB BCYS A 341 19798 8649 9509 1733 2356 606 C ATOM 3488 SG ACYS A 341 1.137 29.717 23.945 0.50104.41 S ANISOU 3488 SG ACYS A 341 20184 9418 10066 2063 2237 630 S ATOM 3489 SG BCYS A 341 2.114 31.141 21.722 0.50105.76 S ANISOU 3489 SG BCYS A 341 20944 9206 10037 2086 2521 723 S ATOM 3490 N LEU A 342 5.766 28.216 21.959 1.00 98.80 N ANISOU 3490 N LEU A 342 19091 8733 9713 927 2205 473 N ATOM 3491 CA LEU A 342 7.195 28.317 21.651 1.00122.82 C ANISOU 3491 CA LEU A 342 22171 11696 12798 570 2272 410 C ATOM 3492 C LEU A 342 7.456 28.357 20.132 1.00154.58 C ANISOU 3492 C LEU A 342 26262 15690 16783 637 2326 470 C ATOM 3493 O LEU A 342 6.653 27.880 19.326 1.00115.05 O ANISOU 3493 O LEU A 342 21131 10813 11769 921 2248 548 O ATOM 3494 CB LEU A 342 7.964 27.140 22.283 1.00120.76 C ANISOU 3494 CB LEU A 342 21501 11667 12717 301 2109 325 C ATOM 3495 CG LEU A 342 7.955 27.045 23.815 1.00125.11 C ANISOU 3495 CG LEU A 342 21970 12255 13312 176 2056 251 C ATOM 3496 CD1 LEU A 342 8.378 25.666 24.282 1.00122.87 C ANISOU 3496 CD1 LEU A 342 21244 12244 13195 35 1866 201 C ATOM 3497 CD2 LEU A 342 8.841 28.110 24.447 1.00129.60 C ANISOU 3497 CD2 LEU A 342 22834 12600 13806 -111 2216 168 C TER 3498 LEU A 342 HETATM 3499 O1 CVD A1201 3.529 6.483 49.808 1.00 83.08 O HETATM 3500 C1 CVD A1201 3.115 5.368 50.546 1.00 84.01 C HETATM 3501 C2 CVD A1201 2.341 4.420 49.636 1.00 82.48 C HETATM 3502 O2 CVD A1201 2.523 3.105 50.098 1.00 82.19 O HETATM 3503 C3 CVD A1201 1.691 2.089 49.584 1.00 81.65 C HETATM 3504 C14 CVD A1201 1.200 2.118 48.344 1.00 81.37 C HETATM 3505 C13 CVD A1201 0.333 0.957 47.819 1.00 81.50 C HETATM 3506 C12 CVD A1201 0.072 -0.089 48.596 1.00 80.70 C HETATM 3507 C6 CVD A1201 0.650 -0.141 50.008 1.00 78.87 C HETATM 3508 C4 CVD A1201 1.411 0.863 50.460 1.00 80.24 C HETATM 3509 C5 CVD A1201 1.816 0.479 51.947 1.00 79.81 C HETATM 3510 C8 CVD A1201 2.651 1.180 53.022 1.00 79.06 C HETATM 3511 C11 CVD A1201 2.785 0.611 54.216 1.00 76.87 C HETATM 3512 C10 CVD A1201 2.154 -0.764 54.493 1.00 75.51 C HETATM 3513 C9 CVD A1201 1.407 -1.356 53.573 1.00 76.24 C HETATM 3514 C7 CVD A1201 1.248 -0.711 52.198 1.00 78.11 C HETATM 3515 N1 CVD A1201 0.554 -1.071 51.041 1.00 78.00 N HETATM 3516 C15 CVD A1201 2.218 5.784 51.720 1.00 85.80 C HETATM 3517 N2 CVD A1201 2.876 6.810 52.501 1.00 87.07 N HETATM 3518 C16 CVD A1201 2.115 7.146 53.687 1.00 90.30 C HETATM 3519 C17 CVD A1201 2.541 8.535 54.180 1.00 93.98 C HETATM 3520 O3 CVD A1201 3.943 8.614 54.221 1.00 98.05 O HETATM 3521 C18 CVD A1201 4.518 9.827 54.642 1.00103.71 C HETATM 3522 C23 CVD A1201 5.062 10.637 53.735 1.00104.57 C HETATM 3523 C22 CVD A1201 5.724 11.954 54.165 1.00105.56 C HETATM 3524 C21 CVD A1201 5.774 12.271 55.451 1.00106.46 C HETATM 3525 C20 CVD A1201 5.162 11.335 56.506 1.00107.45 C HETATM 3526 C19 CVD A1201 4.605 10.180 56.149 1.00107.70 C HETATM 3527 O4 CVD A1201 4.024 9.352 57.142 1.00109.41 O HETATM 3528 C24 CVD A1201 4.687 8.153 57.470 1.00109.59 C HETATM 3529 S SO4 A1202 -2.848 2.253 19.567 1.00 96.86 S HETATM 3530 O1 SO4 A1202 -1.830 2.803 18.669 1.00 95.96 O HETATM 3531 O2 SO4 A1202 -4.212 2.482 19.053 1.00 94.92 O HETATM 3532 O3 SO4 A1202 -2.619 0.828 19.712 1.00 98.88 O HETATM 3533 O4 SO4 A1202 -2.722 2.860 20.888 1.00 98.52 O HETATM 3534 S SO4 A1203 16.187 5.839 21.150 1.00155.28 S HETATM 3535 O1 SO4 A1203 16.148 6.983 20.240 1.00155.21 O HETATM 3536 O2 SO4 A1203 17.096 4.822 20.628 1.00155.38 O HETATM 3537 O3 SO4 A1203 14.850 5.268 21.249 1.00155.45 O HETATM 3538 O4 SO4 A1203 16.647 6.283 22.468 1.00154.97 O HETATM 3539 S SO4 A1204 36.717 -6.917 -2.148 1.00145.03 S HETATM 3540 O1 SO4 A1204 36.123 -5.581 -2.193 1.00146.03 O HETATM 3541 O2 SO4 A1204 37.304 -7.262 -3.448 1.00144.73 O HETATM 3542 O3 SO4 A1204 35.680 -7.876 -1.832 1.00144.15 O HETATM 3543 O4 SO4 A1204 37.751 -6.939 -1.109 1.00145.39 O HETATM 3544 S SO4 A1205 24.666 7.627 6.310 1.00174.53 S HETATM 3545 O1 SO4 A1205 26.045 7.871 5.899 1.00174.41 O HETATM 3546 O2 SO4 A1205 23.764 8.172 5.299 1.00174.80 O HETATM 3547 O3 SO4 A1205 24.434 6.192 6.435 1.00174.51 O HETATM 3548 O4 SO4 A1205 24.418 8.279 7.595 1.00174.62 O HETATM 3549 C1 CLR A1206 -12.297 9.295 30.744 1.00107.45 C HETATM 3550 C2 CLR A1206 -12.324 9.127 29.217 1.00106.40 C HETATM 3551 C3 CLR A1206 -10.937 9.291 28.595 1.00106.53 C HETATM 3552 C4 CLR A1206 -9.938 8.297 29.201 1.00106.99 C HETATM 3553 C5 CLR A1206 -9.991 8.254 30.727 1.00107.49 C HETATM 3554 C6 CLR A1206 -8.808 8.064 31.360 1.00107.60 C HETATM 3555 C7 CLR A1206 -8.550 8.519 32.786 1.00107.51 C HETATM 3556 C8 CLR A1206 -9.818 8.380 33.644 1.00107.25 C HETATM 3557 C9 CLR A1206 -11.000 9.051 32.894 1.00107.51 C HETATM 3558 C10 CLR A1206 -11.309 8.389 31.517 1.00107.76 C HETATM 3559 C11 CLR A1206 -12.252 9.188 33.806 1.00107.00 C HETATM 3560 C12 CLR A1206 -11.989 9.672 35.251 1.00105.76 C HETATM 3561 C13 CLR A1206 -10.893 8.883 35.989 1.00105.42 C HETATM 3562 C14 CLR A1206 -9.668 8.964 35.064 1.00105.94 C HETATM 3563 C15 CLR A1206 -8.513 8.482 35.931 1.00105.64 C HETATM 3564 C16 CLR A1206 -8.863 9.088 37.292 1.00105.77 C HETATM 3565 C17 CLR A1206 -10.312 9.611 37.236 1.00105.36 C HETATM 3566 C18 CLR A1206 -11.357 7.431 36.276 1.00104.81 C HETATM 3567 C19 CLR A1206 -11.921 6.980 31.659 1.00108.21 C HETATM 3568 C20 CLR A1206 -11.003 9.549 38.631 1.00104.13 C HETATM 3569 C21 CLR A1206 -12.518 9.765 38.654 1.00103.33 C HETATM 3570 C22 CLR A1206 -10.400 10.601 39.573 1.00103.76 C HETATM 3571 C23 CLR A1206 -9.866 10.027 40.889 1.00102.96 C HETATM 3572 C24 CLR A1206 -10.016 11.030 42.032 1.00101.56 C HETATM 3573 C25 CLR A1206 -10.205 10.338 43.380 1.00101.05 C HETATM 3574 C26 CLR A1206 -9.283 10.942 44.430 1.00100.92 C HETATM 3575 C27 CLR A1206 -11.650 10.410 43.855 1.00101.00 C HETATM 3576 O1 CLR A1206 -11.042 9.075 27.184 1.00106.57 O HETATM 3577 C9 OLC A1207 -8.346 16.137 39.706 1.00112.53 C HETATM 3578 C8 OLC A1207 -8.549 14.932 38.816 1.00112.87 C HETATM 3579 C24 OLC A1207 -10.238 12.583 26.690 1.00126.55 C HETATM 3580 C7 OLC A1207 -9.471 15.292 37.658 1.00113.39 C HETATM 3581 C6 OLC A1207 -9.738 14.079 36.776 1.00114.46 C HETATM 3582 C5 OLC A1207 -10.643 14.440 35.602 1.00116.19 C HETATM 3583 C4 OLC A1207 -9.875 14.431 34.286 1.00117.51 C HETATM 3584 C3 OLC A1207 -10.452 13.384 33.340 1.00119.76 C HETATM 3585 C2 OLC A1207 -10.959 14.022 32.047 1.00122.63 C HETATM 3586 C21 OLC A1207 -9.943 14.299 28.531 1.00127.99 C HETATM 3587 C1 OLC A1207 -9.940 13.915 30.929 1.00125.32 C HETATM 3588 C22 OLC A1207 -10.706 13.918 27.257 1.00127.32 C HETATM 3589 O19 OLC A1207 -8.764 14.179 31.145 1.00125.73 O HETATM 3590 O25 OLC A1207 -10.694 12.464 25.336 1.00126.24 O HETATM 3591 O23 OLC A1207 -12.127 13.919 27.447 1.00127.16 O HETATM 3592 O20 OLC A1207 -10.319 13.542 29.695 1.00127.40 O HETATM 3593 C10 OLC A1208 8.347 29.259 48.815 1.00109.55 C HETATM 3594 C9 OLC A1208 8.172 28.441 49.853 1.00111.32 C HETATM 3595 C11 OLC A1208 7.179 29.618 47.934 1.00108.26 C HETATM 3596 C8 OLC A1208 9.342 28.077 50.743 1.00111.99 C HETATM 3597 C24 OLC A1208 7.493 26.698 63.094 1.00134.73 C HETATM 3598 C7 OLC A1208 8.947 28.231 52.206 1.00113.46 C HETATM 3599 C6 OLC A1208 10.089 27.837 53.136 1.00115.83 C HETATM 3600 C5 OLC A1208 9.800 28.262 54.573 1.00118.10 C HETATM 3601 C4 OLC A1208 9.346 27.085 55.431 1.00119.83 C HETATM 3602 C3 OLC A1208 8.391 27.542 56.531 1.00121.76 C HETATM 3603 C2 OLC A1208 8.724 26.852 57.854 1.00123.72 C HETATM 3604 C21 OLC A1208 7.250 25.480 60.876 1.00131.38 C HETATM 3605 C1 OLC A1208 7.534 26.716 58.784 1.00126.12 C HETATM 3606 C22 OLC A1208 7.823 25.432 62.301 1.00133.48 C HETATM 3607 O19 OLC A1208 6.385 26.738 58.353 1.00125.83 O HETATM 3608 O25 OLC A1208 8.282 26.763 64.292 1.00135.15 O HETATM 3609 O23 OLC A1208 7.283 24.299 63.000 1.00133.63 O HETATM 3610 O20 OLC A1208 7.759 26.579 60.100 1.00128.91 O HETATM 3611 C24 OLC A1209 -5.314 25.807 24.866 1.00127.55 C HETATM 3612 C5 OLC A1209 0.689 25.606 32.386 1.00121.27 C HETATM 3613 C4 OLC A1209 -0.644 25.069 31.874 1.00122.01 C HETATM 3614 C3 OLC A1209 -0.601 24.894 30.359 1.00123.92 C HETATM 3615 C2 OLC A1209 -1.999 24.750 29.748 1.00125.84 C HETATM 3616 C21 OLC A1209 -4.044 25.231 26.961 1.00127.32 C HETATM 3617 C1 OLC A1209 -2.250 25.665 28.555 1.00126.59 C HETATM 3618 C22 OLC A1209 -5.176 26.075 26.364 1.00127.82 C HETATM 3619 O19 OLC A1209 -1.340 26.252 27.982 1.00126.55 O HETATM 3620 O25 OLC A1209 -4.306 26.520 24.129 1.00126.83 O HETATM 3621 O23 OLC A1209 -6.420 25.755 27.005 1.00128.07 O HETATM 3622 O20 OLC A1209 -3.504 25.865 28.127 1.00126.98 O HETATM 3623 C24 OLC A1210 6.228 30.628 27.380 1.00119.86 C HETATM 3624 C6 OLC A1210 6.627 31.228 37.701 1.00 99.98 C HETATM 3625 C5 OLC A1210 6.264 32.478 36.910 1.00101.19 C HETATM 3626 C4 OLC A1210 5.333 32.156 35.750 1.00103.63 C HETATM 3627 C3 OLC A1210 6.035 32.350 34.410 1.00106.49 C HETATM 3628 C2 OLC A1210 5.393 31.469 33.337 1.00110.50 C HETATM 3629 C21 OLC A1210 6.262 31.663 29.645 1.00117.57 C HETATM 3630 C1 OLC A1210 6.228 31.368 32.075 1.00115.32 C HETATM 3631 C22 OLC A1210 6.546 30.387 28.856 1.00118.41 C HETATM 3632 O19 OLC A1210 7.452 31.272 32.144 1.00117.18 O HETATM 3633 O25 OLC A1210 7.380 30.438 26.547 1.00121.17 O HETATM 3634 O23 OLC A1210 7.906 29.965 29.051 1.00117.69 O HETATM 3635 O20 OLC A1210 5.606 31.350 30.883 1.00117.10 O HETATM 3636 C24 OLC A1211 -8.017 -8.437 25.074 1.00111.74 C HETATM 3637 C3 OLC A1211 -5.627 -6.765 30.747 1.00106.61 C HETATM 3638 C2 OLC A1211 -6.573 -6.605 29.560 1.00108.60 C HETATM 3639 C21 OLC A1211 -6.626 -6.624 26.066 1.00111.26 C HETATM 3640 C1 OLC A1211 -5.855 -6.119 28.311 1.00110.99 C HETATM 3641 C22 OLC A1211 -6.624 -7.818 25.121 1.00110.72 C HETATM 3642 O19 OLC A1211 -5.318 -5.016 28.290 1.00111.33 O HETATM 3643 O25 OLC A1211 -8.572 -8.362 23.753 1.00113.25 O HETATM 3644 O23 OLC A1211 -6.202 -7.388 23.820 1.00110.87 O HETATM 3645 O20 OLC A1211 -5.807 -6.888 27.211 1.00112.12 O HETATM 3646 C10 OLC A1212 -6.706 -3.952 39.961 1.00104.57 C HETATM 3647 C9 OLC A1212 -7.337 -4.822 39.165 1.00105.37 C HETATM 3648 C11 OLC A1212 -6.350 -4.330 41.381 1.00102.59 C HETATM 3649 C8 OLC A1212 -7.706 -4.456 37.742 1.00103.75 C HETATM 3650 C7 OLC A1212 -7.787 -5.711 36.883 1.00103.02 C HETATM 3651 C1 OLA A1213 -6.603 24.615 30.588 1.00116.93 C HETATM 3652 O1 OLA A1213 -7.384 24.529 29.615 1.00116.58 O HETATM 3653 O2 OLA A1213 -5.406 24.286 30.416 1.00118.28 O HETATM 3654 C2 OLA A1213 -7.093 25.130 31.927 1.00115.02 C HETATM 3655 C3 OLA A1213 -6.878 24.109 33.039 1.00113.46 C HETATM 3656 C4 OLA A1213 -5.793 24.577 34.001 1.00113.23 C HETATM 3657 C5 OLA A1213 -6.306 24.628 35.438 1.00113.53 C HETATM 3658 C6 OLA A1213 -5.588 23.608 36.321 1.00113.20 C HETATM 3659 C7 OLA A1213 -4.637 24.255 37.327 1.00112.74 C HETATM 3660 C8 OLA A1213 -5.141 24.067 38.757 1.00113.40 C HETATM 3661 C9 OLA A1213 -3.977 24.011 39.730 1.00114.19 C HETATM 3662 C10 OLA A1213 -4.008 24.387 41.022 1.00114.04 C HETATM 3663 C11 OLA A1213 -5.215 24.952 41.750 1.00113.67 C HETATM 3664 C12 OLA A1213 -4.755 25.862 42.886 1.00113.22 C HETATM 3665 C1 OLA A1214 2.646 -14.235 27.895 1.00 97.98 C HETATM 3666 O1 OLA A1214 3.104 -15.311 27.450 1.00 98.39 O HETATM 3667 O2 OLA A1214 3.471 -13.360 28.234 1.00 99.11 O HETATM 3668 C2 OLA A1214 1.146 -14.011 27.985 1.00 96.66 C HETATM 3669 C3 OLA A1214 0.714 -13.299 29.272 1.00 98.42 C HETATM 3670 C4 OLA A1214 0.545 -14.269 30.444 1.00100.34 C HETATM 3671 C5 OLA A1214 0.890 -13.630 31.792 1.00101.65 C HETATM 3672 C6 OLA A1214 1.766 -14.529 32.677 1.00100.80 C HETATM 3673 C7 OLA A1214 0.968 -15.264 33.759 1.00 98.41 C HETATM 3674 C8 OLA A1214 1.885 -15.814 34.847 1.00 96.43 C HETATM 3675 C1 OLA A1215 13.517 -6.160 30.210 1.00124.24 C HETATM 3676 O1 OLA A1215 14.308 -6.068 29.242 1.00123.69 O HETATM 3677 O2 OLA A1215 13.868 -6.839 31.198 1.00125.80 O HETATM 3678 C2 OLA A1215 12.162 -5.477 30.193 1.00122.48 C HETATM 3679 C3 OLA A1215 12.239 -4.126 30.903 1.00120.11 C HETATM 3680 C4 OLA A1215 10.945 -3.763 31.625 1.00116.61 C HETATM 3681 C5 OLA A1215 11.168 -2.579 32.555 1.00113.48 C HETATM 3682 C6 OLA A1215 11.084 -3.014 34.013 1.00112.06 C HETATM 3683 C7 OLA A1215 12.410 -2.835 34.745 1.00112.03 C HETATM 3684 C8 OLA A1215 13.035 -4.188 35.072 1.00113.49 C HETATM 3685 C9 OLA A1215 13.521 -4.218 36.512 1.00115.00 C HETATM 3686 C10 OLA A1215 14.521 -4.984 36.984 1.00115.57 C HETATM 3687 C11 OLA A1215 15.351 -5.956 36.164 1.00114.99 C HETATM 3688 C1 OLA A1216 13.381 13.023 57.271 1.00124.84 C HETATM 3689 O1 OLA A1216 14.352 13.680 57.717 1.00125.65 O HETATM 3690 O2 OLA A1216 12.439 12.745 58.052 1.00125.39 O HETATM 3691 C2 OLA A1216 13.352 12.566 55.826 1.00122.46 C HETATM 3692 C3 OLA A1216 13.254 13.767 54.887 1.00120.08 C HETATM 3693 C4 OLA A1216 12.555 13.409 53.583 1.00118.72 C HETATM 3694 C5 OLA A1216 12.390 14.649 52.715 1.00118.08 C HETATM 3695 C6 OLA A1216 12.940 14.410 51.317 1.00118.12 C HETATM 3696 C7 OLA A1216 12.576 15.547 50.366 1.00118.85 C HETATM 3697 C8 OLA A1216 13.569 15.634 49.207 1.00120.65 C HETATM 3698 C9 OLA A1216 13.055 14.870 47.999 1.00122.38 C HETATM 3699 C10 OLA A1216 13.809 14.126 47.176 1.00123.66 C HETATM 3700 C11 OLA A1216 15.308 13.936 47.310 1.00124.33 C HETATM 3701 C12 OLA A1216 15.738 12.654 46.601 1.00124.21 C HETATM 3702 O HOH A1301 1.034 9.885 32.319 1.00105.53 O HETATM 3703 O HOH A1302 22.071 -6.601 12.827 1.00 72.55 O HETATM 3704 O HOH A1303 4.720 10.055 36.523 1.00 83.78 O HETATM 3705 O HOH A1304 -5.795 -0.341 51.933 1.00 73.78 O HETATM 3706 O HOH A1305 7.979 6.494 35.755 1.00 98.09 O HETATM 3707 O HOH A1306 -4.016 9.324 63.914 1.00 94.83 O HETATM 3708 O HOH A1307 12.281 4.312 47.093 1.00 76.76 O HETATM 3709 O HOH A1308 2.385 11.241 34.260 1.00 73.22 O HETATM 3710 O HOH A1309 -4.722 -0.974 47.035 1.00 83.94 O HETATM 3711 O HOH A1310 23.764 -1.598 2.020 1.00 67.12 O HETATM 3712 O HOH A1311 -0.814 0.470 24.979 1.00 72.53 O HETATM 3713 O HOH A1312 -4.137 -5.249 22.364 1.00 66.75 O HETATM 3714 O HOH A1313 11.423 1.636 -3.563 1.00 66.66 O CONECT 600 1301 CONECT 1247 1295 CONECT 1295 1247 CONECT 1301 600 CONECT 3499 3500 CONECT 3500 3499 3501 3516 CONECT 3501 3500 3502 CONECT 3502 3501 3503 CONECT 3503 3502 3504 3508 CONECT 3504 3503 3505 CONECT 3505 3504 3506 CONECT 3506 3505 3507 CONECT 3507 3506 3508 3515 CONECT 3508 3503 3507 3509 CONECT 3509 3508 3510 3514 CONECT 3510 3509 3511 CONECT 3511 3510 3512 CONECT 3512 3511 3513 CONECT 3513 3512 3514 CONECT 3514 3509 3513 3515 CONECT 3515 3507 3514 CONECT 3516 3500 3517 CONECT 3517 3516 3518 CONECT 3518 3517 3519 CONECT 3519 3518 3520 CONECT 3520 3519 3521 CONECT 3521 3520 3522 3526 CONECT 3522 3521 3523 CONECT 3523 3522 3524 CONECT 3524 3523 3525 CONECT 3525 3524 3526 CONECT 3526 3521 3525 3527 CONECT 3527 3526 3528 CONECT 3528 3527 CONECT 3529 3530 3531 3532 3533 CONECT 3530 3529 CONECT 3531 3529 CONECT 3532 3529 CONECT 3533 3529 CONECT 3534 3535 3536 3537 3538 CONECT 3535 3534 CONECT 3536 3534 CONECT 3537 3534 CONECT 3538 3534 CONECT 3539 3540 3541 3542 3543 CONECT 3540 3539 CONECT 3541 3539 CONECT 3542 3539 CONECT 3543 3539 CONECT 3544 3545 3546 3547 3548 CONECT 3545 3544 CONECT 3546 3544 CONECT 3547 3544 CONECT 3548 3544 CONECT 3549 3550 3558 CONECT 3550 3549 3551 CONECT 3551 3550 3552 3576 CONECT 3552 3551 3553 CONECT 3553 3552 3554 3558 CONECT 3554 3553 3555 CONECT 3555 3554 3556 CONECT 3556 3555 3557 3562 CONECT 3557 3556 3558 3559 CONECT 3558 3549 3553 3557 3567 CONECT 3559 3557 3560 CONECT 3560 3559 3561 CONECT 3561 3560 3562 3565 3566 CONECT 3562 3556 3561 3563 CONECT 3563 3562 3564 CONECT 3564 3563 3565 CONECT 3565 3561 3564 3568 CONECT 3566 3561 CONECT 3567 3558 CONECT 3568 3565 3569 3570 CONECT 3569 3568 CONECT 3570 3568 3571 CONECT 3571 3570 3572 CONECT 3572 3571 3573 CONECT 3573 3572 3574 3575 CONECT 3574 3573 CONECT 3575 3573 CONECT 3576 3551 CONECT 3577 3578 CONECT 3578 3577 3580 CONECT 3579 3588 3590 CONECT 3580 3578 3581 CONECT 3581 3580 3582 CONECT 3582 3581 3583 CONECT 3583 3582 3584 CONECT 3584 3583 3585 CONECT 3585 3584 3587 CONECT 3586 3588 3592 CONECT 3587 3585 3589 3592 CONECT 3588 3579 3586 3591 CONECT 3589 3587 CONECT 3590 3579 CONECT 3591 3588 CONECT 3592 3586 3587 CONECT 3593 3594 3595 CONECT 3594 3593 3596 CONECT 3595 3593 CONECT 3596 3594 3598 CONECT 3597 3606 3608 CONECT 3598 3596 3599 CONECT 3599 3598 3600 CONECT 3600 3599 3601 CONECT 3601 3600 3602 CONECT 3602 3601 3603 CONECT 3603 3602 3605 CONECT 3604 3606 3610 CONECT 3605 3603 3607 3610 CONECT 3606 3597 3604 3609 CONECT 3607 3605 CONECT 3608 3597 CONECT 3609 3606 CONECT 3610 3604 3605 CONECT 3611 3618 3620 CONECT 3612 3613 CONECT 3613 3612 3614 CONECT 3614 3613 3615 CONECT 3615 3614 3617 CONECT 3616 3618 3622 CONECT 3617 3615 3619 3622 CONECT 3618 3611 3616 3621 CONECT 3619 3617 CONECT 3620 3611 CONECT 3621 3618 CONECT 3622 3616 3617 CONECT 3623 3631 3633 CONECT 3624 3625 CONECT 3625 3624 3626 CONECT 3626 3625 3627 CONECT 3627 3626 3628 CONECT 3628 3627 3630 CONECT 3629 3631 3635 CONECT 3630 3628 3632 3635 CONECT 3631 3623 3629 3634 CONECT 3632 3630 CONECT 3633 3623 CONECT 3634 3631 CONECT 3635 3629 3630 CONECT 3636 3641 3643 CONECT 3637 3638 CONECT 3638 3637 3640 CONECT 3639 3641 3645 CONECT 3640 3638 3642 3645 CONECT 3641 3636 3639 3644 CONECT 3642 3640 CONECT 3643 3636 CONECT 3644 3641 CONECT 3645 3639 3640 CONECT 3646 3647 3648 CONECT 3647 3646 3649 CONECT 3648 3646 CONECT 3649 3647 3650 CONECT 3650 3649 CONECT 3651 3652 3653 3654 CONECT 3652 3651 CONECT 3653 3651 CONECT 3654 3651 3655 CONECT 3655 3654 3656 CONECT 3656 3655 3657 CONECT 3657 3656 3658 CONECT 3658 3657 3659 CONECT 3659 3658 3660 CONECT 3660 3659 3661 CONECT 3661 3660 3662 CONECT 3662 3661 3663 CONECT 3663 3662 3664 CONECT 3664 3663 CONECT 3665 3666 3667 3668 CONECT 3666 3665 CONECT 3667 3665 CONECT 3668 3665 3669 CONECT 3669 3668 3670 CONECT 3670 3669 3671 CONECT 3671 3670 3672 CONECT 3672 3671 3673 CONECT 3673 3672 3674 CONECT 3674 3673 CONECT 3675 3676 3677 3678 CONECT 3676 3675 CONECT 3677 3675 CONECT 3678 3675 3679 CONECT 3679 3678 3680 CONECT 3680 3679 3681 CONECT 3681 3680 3682 CONECT 3682 3681 3683 CONECT 3683 3682 3684 CONECT 3684 3683 3685 CONECT 3685 3684 3686 CONECT 3686 3685 3687 CONECT 3687 3686 CONECT 3688 3689 3690 3691 CONECT 3689 3688 CONECT 3690 3688 CONECT 3691 3688 3692 CONECT 3692 3691 3693 CONECT 3693 3692 3694 CONECT 3694 3693 3695 CONECT 3695 3694 3696 CONECT 3696 3695 3697 CONECT 3697 3696 3698 CONECT 3698 3697 3699 CONECT 3699 3698 3700 CONECT 3700 3699 3701 CONECT 3701 3700 MASTER 433 0 16 23 3 0 19 6 3675 1 207 39 END