HEADER MEMBRANE PROTEIN 12-JUL-19 6PS6 TITLE XFEL BETA2 AR STRUCTURE BY LIGAND EXCHANGE FROM TIMOLOL TO TIMOLOL. 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, 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 6PS6 1 REMARK REVDAT 2 25-DEC-19 6PS6 1 JRNL REVDAT 1 13-NOV-19 6PS6 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. 2.70 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) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.35 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 15665 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) : 0.218 REMARK 3 R VALUE (WORKING SET) : 0.218 REMARK 3 FREE R VALUE : 0.232 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010 REMARK 3 FREE R VALUE TEST SET COUNT : 785 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 : 8 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.89 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.36 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2777 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2400 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2636 REMARK 3 BIN R VALUE (WORKING SET) : 0.2380 REMARK 3 BIN FREE R VALUE : 0.2650 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.08 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 141 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 : 3478 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 226 REMARK 3 SOLVENT ATOMS : 10 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 87.50 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -11.98320 REMARK 3 B22 (A**2) : 5.80430 REMARK 3 B33 (A**2) : 6.17880 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) : 0.470 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 1.492 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.301 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 1.288 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.304 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 : 0.936 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3789 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 5127 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1743 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 61 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 547 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3789 ; 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 : 499 ; 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 : 4508 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 0.96 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.01 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.95 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): 8.7680 3.5750 25.8497 REMARK 3 T TENSOR REMARK 3 T11: 0.0253 T22: -0.2174 REMARK 3 T33: -0.2244 T12: -0.0065 REMARK 3 T13: -0.0077 T23: 0.0470 REMARK 3 L TENSOR REMARK 3 L11: 0.8911 L22: 0.6741 REMARK 3 L33: 2.9383 L12: -0.3177 REMARK 3 L13: -0.8803 L23: 0.5914 REMARK 3 S TENSOR REMARK 3 S11: -0.0052 S12: -0.0008 S13: 0.0308 REMARK 3 S21: 0.0728 S22: -0.0249 S23: -0.0343 REMARK 3 S31: -0.2669 S32: 0.0243 S33: 0.0301 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6PS6 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_1000242973. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-NOV-14 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 : CXI REMARK 200 X-RAY GENERATOR MODEL : SLAC LCLS BEAMLINE CXI REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.33 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : CS-PAD CXI-1 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL REMARK 200 DATA SCALING SOFTWARE : CRYSTFEL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15738 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 31.400 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 170.9 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.89 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 (%): 47.70 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35 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 TIMOLOL, 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 20.74000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.98000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.09500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.98000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.74000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.09500 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 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 60 CG CD CE NZ REMARK 470 ARG A 63 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 187 CG CD OE1 OE2 REMARK 470 GLU A 188 OE1 OE2 REMARK 470 GLN A 197 OE1 NE2 REMARK 470 LYS A 227 CD CE NZ REMARK 470 LYS A1016 CD CE NZ REMARK 470 ILE A1017 CD1 REMARK 470 LYS A1019 CG CD CE NZ REMARK 470 THR A1021 OG1 CG2 REMARK 470 GLU A1022 CG CD OE1 OE2 REMARK 470 LYS A1043 CD CE NZ REMARK 470 LYS A1048 CD CE NZ REMARK 470 LYS A1060 CG CD CE NZ REMARK 470 ASP A1061 CG OD1 OD2 REMARK 470 GLU A1064 CG CD OE1 OE2 REMARK 470 LYS A1065 CG CD CE NZ REMARK 470 GLN A1069 CD OE1 NE2 REMARK 470 GLU A1108 CD OE1 OE2 REMARK 470 LYS A 267 CG CD CE NZ REMARK 470 ASP A 300 CG OD1 OD2 REMARK 470 ASN A 301 CG OD1 ND2 REMARK 470 LEU A 302 CG CD1 CD2 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 LYS A 97 19.62 57.28 REMARK 500 LYS A 140 -53.05 62.48 REMARK 500 CYS A 191 37.49 -148.30 REMARK 500 PHE A 208 -54.84 -136.07 REMARK 500 PHE A1114 49.55 -81.12 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 OLC A 1213 REMARK 610 OLA A 1214 REMARK 610 OLA A 1215 REMARK 610 OLA A 1216 REMARK 610 OLA A 1217 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue TIM 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 OLC 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 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1216 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1217 DBREF 6PS6 A 1 230 UNP P07550 ADRB2_HUMAN 1 230 DBREF 6PS6 A 1002 1161 UNP D9IEF7 D9IEF7_BPT4 2 161 DBREF 6PS6 A 263 348 UNP P07550 ADRB2_HUMAN 263 348 SEQADV 6PS6 MET A -23 UNP P07550 INITIATING METHIONINE SEQADV 6PS6 LYS A -22 UNP P07550 EXPRESSION TAG SEQADV 6PS6 THR A -21 UNP P07550 EXPRESSION TAG SEQADV 6PS6 ILE A -20 UNP P07550 EXPRESSION TAG SEQADV 6PS6 ILE A -19 UNP P07550 EXPRESSION TAG SEQADV 6PS6 ALA A -18 UNP P07550 EXPRESSION TAG SEQADV 6PS6 LEU A -17 UNP P07550 EXPRESSION TAG SEQADV 6PS6 SER A -16 UNP P07550 EXPRESSION TAG SEQADV 6PS6 TYR A -15 UNP P07550 EXPRESSION TAG SEQADV 6PS6 ILE A -14 UNP P07550 EXPRESSION TAG SEQADV 6PS6 PHE A -13 UNP P07550 EXPRESSION TAG SEQADV 6PS6 CYS A -12 UNP P07550 EXPRESSION TAG SEQADV 6PS6 LEU A -11 UNP P07550 EXPRESSION TAG SEQADV 6PS6 VAL A -10 UNP P07550 EXPRESSION TAG SEQADV 6PS6 PHE A -9 UNP P07550 EXPRESSION TAG SEQADV 6PS6 ALA A -8 UNP P07550 EXPRESSION TAG SEQADV 6PS6 ASP A -7 UNP P07550 EXPRESSION TAG SEQADV 6PS6 TYR A -6 UNP P07550 EXPRESSION TAG SEQADV 6PS6 LYS A -5 UNP P07550 EXPRESSION TAG SEQADV 6PS6 ASP A -4 UNP P07550 EXPRESSION TAG SEQADV 6PS6 ASP A -3 UNP P07550 EXPRESSION TAG SEQADV 6PS6 ASP A -2 UNP P07550 EXPRESSION TAG SEQADV 6PS6 ASP A -1 UNP P07550 EXPRESSION TAG SEQADV 6PS6 ALA A 0 UNP P07550 EXPRESSION TAG SEQADV 6PS6 ARG A 16 UNP P07550 GLY 16 VARIANT SEQADV 6PS6 GLN A 27 UNP P07550 GLU 27 VARIANT SEQADV 6PS6 TRP A 122 UNP P07550 GLU 122 ENGINEERED MUTATION SEQADV 6PS6 GLU A 187 UNP P07550 ASN 187 ENGINEERED MUTATION SEQADV 6PS6 THR A 1054 UNP D9IEF7 CYS 54 ENGINEERED MUTATION SEQADV 6PS6 ALA A 1097 UNP D9IEF7 CYS 97 ENGINEERED MUTATION SEQADV 6PS6 HIS A 349 UNP P07550 EXPRESSION TAG SEQADV 6PS6 HIS A 350 UNP P07550 EXPRESSION TAG SEQADV 6PS6 HIS A 351 UNP P07550 EXPRESSION TAG SEQADV 6PS6 HIS A 352 UNP P07550 EXPRESSION TAG SEQADV 6PS6 HIS A 353 UNP P07550 EXPRESSION TAG SEQADV 6PS6 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 TIM A1201 21 HET SO4 A1202 5 HET SO4 A1203 5 HET SO4 A1204 5 HET SO4 A1205 5 HET CLR A1206 28 HET OLC A1207 10 HET OLC A1208 15 HET OLC A1209 16 HET OLC A1210 21 HET OLC A1211 18 HET OLC A1212 13 HET OLC A1213 13 HET OLA A1214 14 HET OLA A1215 10 HET OLA A1216 14 HET OLA A1217 13 HETNAM TIM (2S)-1-(TERT-BUTYLAMINO)-3-[(4-MORPHOLIN-4-YL-1,2,5- HETNAM 2 TIM THIADIAZOL-3-YL)OXY]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 TIM TIMOLOL MALEATE HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 TIM C13 H24 N4 O3 S FORMUL 3 SO4 4(O4 S 2-) FORMUL 7 CLR C27 H46 O FORMUL 8 OLC 7(C21 H40 O4) FORMUL 15 OLA 4(C18 H34 O2) FORMUL 19 HOH *10(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 MET A 96 1 11 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 ALA A 198 PHE A 208 1 11 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 LEU A 1091 1 8 HELIX 14 AB5 ASP A 1092 GLY A 1107 1 16 HELIX 15 AB6 GLY A 1107 ALA A 1112 1 6 HELIX 16 AB7 PHE A 1114 GLN A 1123 1 10 HELIX 17 AB8 ARG A 1125 LYS A 1135 1 11 HELIX 18 AB9 SER A 1136 THR A 1142 1 7 HELIX 19 AC1 THR A 1142 GLY A 1156 1 15 HELIX 20 AC2 TRP A 1158 LYS A 263 5 5 HELIX 21 AC3 LEU A 266 VAL A 297 1 32 HELIX 22 AC4 ARG A 304 VAL A 317 1 14 HELIX 23 AC5 ASN A 318 GLY A 320 5 3 HELIX 24 AC6 PHE A 321 TYR A 326 1 6 HELIX 25 AC7 SER A 329 CYS A 341 1 13 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 2.04 SITE 1 AC1 14 ASP A 113 VAL A 114 VAL A 117 THR A 118 SITE 2 AC1 14 TYR A 199 SER A 203 SER A 204 SER A 207 SITE 3 AC1 14 TRP A 286 PHE A 289 PHE A 290 ASN A 293 SITE 4 AC1 14 TYR A 308 ASN A 312 SITE 1 AC2 6 THR A 66 VAL A 67 THR A 68 ARG A 131 SITE 2 AC2 6 TYR A 141 SER A 143 SITE 1 AC3 3 LYS A 270 LYS A 273 ARG A 328 SITE 1 AC4 4 PHE A1114 ASN A1116 SER A1117 ASN A1132 SITE 1 AC5 3 THR A1142 ASN A1144 ARG A1145 SITE 1 AC6 5 TYR A 70 SER A 74 CYS A 77 ILE A 154 SITE 2 AC6 5 TRP A 158 SITE 1 AC7 2 TRP A 122 VAL A 160 SITE 1 AC8 4 ASP A 130 PHE A 133 LEU A 144 LEU A 145 SITE 1 AC9 3 ILE A 55 GLN A 65 THR A 73 SITE 1 AD1 6 PHE A 49 VAL A 52 GLN A 197 VAL A 297 SITE 2 AD1 6 LEU A 339 OLA A1214 SITE 1 AD2 2 ALA A 59 OLA A1214 SITE 1 AD3 3 TRP A 173 ASN A 196 LEU A 340 SITE 1 AD4 2 PHE A 223 LYS A 273 SITE 1 AD5 3 THR A 56 OLC A1210 OLC A1211 SITE 1 AD6 4 MET A 96 THR A 100 PHE A 101 PHE A 217 SITE 1 AD7 1 TRP A 313 SITE 1 AD8 1 THR A 283 CRYST1 41.480 76.190 171.960 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 0.024108 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013125 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005815 0.00000 ATOM 1 N ARG A 28 17.321 21.865 62.509 1.00144.36 N ANISOU 1 N ARG A 28 21332 18998 14522 -2000 -632 -2322 N ATOM 2 CA ARG A 28 16.095 22.544 62.094 1.00143.10 C ANISOU 2 CA ARG A 28 21455 18441 14477 -1949 -499 -2250 C ATOM 3 C ARG A 28 16.387 24.022 61.703 1.00148.86 C ANISOU 3 C ARG A 28 22394 18959 15208 -2254 -383 -2429 C ATOM 4 O ARG A 28 15.454 24.821 61.565 1.00148.63 O ANISOU 4 O ARG A 28 22638 18607 15229 -2231 -265 -2413 O ATOM 5 CB ARG A 28 15.006 22.429 63.200 1.00142.46 C ANISOU 5 CB ARG A 28 21495 18301 14333 -1735 -491 -2196 C ATOM 6 CG ARG A 28 15.041 23.460 64.345 1.00151.56 C ANISOU 6 CG ARG A 28 22801 19452 15333 -1874 -461 -2396 C ATOM 7 CD ARG A 28 16.120 23.223 65.388 1.00158.77 C ANISOU 7 CD ARG A 28 23518 20749 16058 -1966 -581 -2549 C ATOM 8 NE ARG A 28 16.282 24.387 66.260 1.00165.56 N ANISOU 8 NE ARG A 28 24537 21585 16783 -2170 -537 -2776 N ATOM 9 CZ ARG A 28 15.621 24.574 67.398 1.00177.15 C ANISOU 9 CZ ARG A 28 26123 23038 18146 -2060 -529 -2805 C ATOM 10 NH1 ARG A 28 15.830 25.667 68.120 1.00165.68 N ANISOU 10 NH1 ARG A 28 24822 21558 16571 -2267 -483 -3024 N ATOM 11 NH2 ARG A 28 14.745 23.672 67.824 1.00161.21 N ANISOU 11 NH2 ARG A 28 24080 21030 16141 -1753 -560 -2620 N ATOM 12 N ASP A 29 17.686 24.350 61.479 1.00146.68 N ANISOU 12 N ASP A 29 21990 18866 14873 -2533 -409 -2596 N ATOM 13 CA ASP A 29 18.225 25.667 61.106 1.00148.26 C ANISOU 13 CA ASP A 29 22359 18916 15057 -2876 -297 -2790 C ATOM 14 C ASP A 29 17.407 26.339 59.991 1.00150.13 C ANISOU 14 C ASP A 29 22874 18723 15446 -2866 -145 -2691 C ATOM 15 O ASP A 29 16.921 25.660 59.085 1.00147.24 O ANISOU 15 O ASP A 29 22461 18267 15217 -2676 -150 -2491 O ATOM 16 CB ASP A 29 19.695 25.524 60.672 1.00151.46 C ANISOU 16 CB ASP A 29 22514 19612 15423 -3124 -356 -2916 C ATOM 17 CG ASP A 29 20.482 26.822 60.597 1.00165.13 C ANISOU 17 CG ASP A 29 24371 21286 17085 -3531 -255 -3171 C ATOM 18 OD1 ASP A 29 20.517 27.559 61.608 1.00167.57 O ANISOU 18 OD1 ASP A 29 24797 21611 17261 -3665 -230 -3352 O ATOM 19 OD2 ASP A 29 21.137 27.057 59.563 1.00171.85 O ANISOU 19 OD2 ASP A 29 25188 22104 18003 -3728 -201 -3203 O ATOM 20 N GLU A 30 17.266 27.678 60.072 1.00147.87 N ANISOU 20 N GLU A 30 22885 18176 15122 -3069 -7 -2836 N ATOM 21 CA GLU A 30 16.488 28.522 59.154 1.00146.95 C ANISOU 21 CA GLU A 30 23089 17634 15112 -3060 156 -2766 C ATOM 22 C GLU A 30 16.808 28.274 57.674 1.00148.58 C ANISOU 22 C GLU A 30 23234 17766 15455 -3098 186 -2657 C ATOM 23 O GLU A 30 15.895 28.349 56.856 1.00146.72 O ANISOU 23 O GLU A 30 23161 17256 15332 -2921 261 -2496 O ATOM 24 CB GLU A 30 16.671 30.020 59.474 1.00151.18 C ANISOU 24 CB GLU A 30 23939 17946 15557 -3343 304 -2982 C ATOM 25 CG GLU A 30 16.296 30.429 60.895 1.00164.08 C ANISOU 25 CG GLU A 30 25684 19607 17052 -3319 298 -3104 C ATOM 26 CD GLU A 30 14.870 30.184 61.360 1.00184.81 C ANISOU 26 CD GLU A 30 28434 22082 19705 -2961 301 -2943 C ATOM 27 OE1 GLU A 30 13.932 30.344 60.545 1.00177.41 O ANISOU 27 OE1 GLU A 30 27675 20853 18880 -2779 389 -2784 O ATOM 28 OE2 GLU A 30 14.692 29.863 62.557 1.00179.82 O ANISOU 28 OE2 GLU A 30 27721 21634 18969 -2865 219 -2985 O ATOM 29 N VAL A 31 18.073 27.957 57.330 1.00144.93 N ANISOU 29 N VAL A 31 22529 17563 14974 -3312 125 -2745 N ATOM 30 CA VAL A 31 18.468 27.703 55.937 1.00143.33 C ANISOU 30 CA VAL A 31 22253 17314 14891 -3363 152 -2652 C ATOM 31 C VAL A 31 17.995 26.306 55.467 1.00142.88 C ANISOU 31 C VAL A 31 21973 17370 14943 -3035 39 -2411 C ATOM 32 O VAL A 31 17.884 26.086 54.261 1.00141.16 O ANISOU 32 O VAL A 31 21757 17031 14847 -2987 76 -2285 O ATOM 33 CB VAL A 31 19.985 27.916 55.655 1.00149.21 C ANISOU 33 CB VAL A 31 22823 18291 15579 -3721 144 -2838 C ATOM 34 CG1 VAL A 31 20.426 29.334 56.014 1.00152.11 C ANISOU 34 CG1 VAL A 31 23437 18515 15844 -4079 282 -3083 C ATOM 35 CG2 VAL A 31 20.859 26.873 56.351 1.00149.11 C ANISOU 35 CG2 VAL A 31 22417 18759 15480 -3694 -39 -2886 C ATOM 36 N TRP A 32 17.722 25.379 56.407 1.00137.49 N ANISOU 36 N TRP A 32 21115 16911 14212 -2817 -88 -2353 N ATOM 37 CA TRP A 32 17.261 24.027 56.087 1.00134.26 C ANISOU 37 CA TRP A 32 20515 16605 13892 -2517 -183 -2137 C ATOM 38 C TRP A 32 15.753 24.026 55.799 1.00133.15 C ANISOU 38 C TRP A 32 20576 16165 13850 -2256 -114 -1963 C ATOM 39 O TRP A 32 15.337 23.456 54.792 1.00130.78 O ANISOU 39 O TRP A 32 20237 15780 13674 -2114 -108 -1799 O ATOM 40 CB TRP A 32 17.610 23.040 57.221 1.00133.46 C ANISOU 40 CB TRP A 32 20167 16859 13684 -2393 -331 -2145 C ATOM 41 CG TRP A 32 17.070 21.653 57.021 1.00132.40 C ANISOU 41 CG TRP A 32 19876 16803 13626 -2084 -410 -1927 C ATOM 42 CD1 TRP A 32 17.579 20.683 56.208 1.00134.18 C ANISOU 42 CD1 TRP A 32 19890 17170 13922 -2021 -471 -1824 C ATOM 43 CD2 TRP A 32 15.906 21.087 57.642 1.00131.00 C ANISOU 43 CD2 TRP A 32 19756 16560 13457 -1806 -423 -1793 C ATOM 44 NE1 TRP A 32 16.805 19.547 56.282 1.00131.74 N ANISOU 44 NE1 TRP A 32 19516 16873 13665 -1727 -517 -1635 N ATOM 45 CE2 TRP A 32 15.771 19.767 57.156 1.00133.06 C ANISOU 45 CE2 TRP A 32 19840 16919 13796 -1599 -486 -1614 C ATOM 46 CE3 TRP A 32 14.960 21.568 58.565 1.00132.64 C ANISOU 46 CE3 TRP A 32 20149 16636 13611 -1717 -379 -1811 C ATOM 47 CZ2 TRP A 32 14.731 18.921 57.564 1.00130.90 C ANISOU 47 CZ2 TRP A 32 19575 16614 13548 -1327 -500 -1459 C ATOM 48 CZ3 TRP A 32 13.930 20.730 58.968 1.00132.60 C ANISOU 48 CZ3 TRP A 32 20136 16614 13631 -1439 -399 -1654 C ATOM 49 CH2 TRP A 32 13.823 19.424 58.470 1.00131.41 C ANISOU 49 CH2 TRP A 32 19811 16561 13559 -1257 -455 -1483 C ATOM 50 N VAL A 33 14.946 24.662 56.677 1.00128.01 N ANISOU 50 N VAL A 33 20132 15371 13136 -2195 -63 -2006 N ATOM 51 CA VAL A 33 13.484 24.736 56.566 1.00125.39 C ANISOU 51 CA VAL A 33 19985 14788 12871 -1942 3 -1865 C ATOM 52 C VAL A 33 13.066 25.579 55.329 1.00126.78 C ANISOU 52 C VAL A 33 20395 14635 13141 -1977 137 -1820 C ATOM 53 O VAL A 33 12.133 25.189 54.624 1.00124.68 O ANISOU 53 O VAL A 33 20153 14244 12975 -1756 158 -1653 O ATOM 54 CB VAL A 33 12.820 25.226 57.892 1.00130.32 C ANISOU 54 CB VAL A 33 20760 15370 13384 -1874 24 -1940 C ATOM 55 CG1 VAL A 33 13.198 26.665 58.248 1.00132.69 C ANISOU 55 CG1 VAL A 33 21309 15516 13592 -2128 126 -2144 C ATOM 56 CG2 VAL A 33 11.305 25.041 57.872 1.00128.61 C ANISOU 56 CG2 VAL A 33 20662 14975 13229 -1577 69 -1783 C ATOM 57 N VAL A 34 13.771 26.693 55.050 1.00123.41 N ANISOU 57 N VAL A 34 20134 14081 12674 -2254 231 -1971 N ATOM 58 CA VAL A 34 13.488 27.557 53.900 1.00122.68 C ANISOU 58 CA VAL A 34 20293 13672 12650 -2300 371 -1937 C ATOM 59 C VAL A 34 14.005 26.853 52.625 1.00123.52 C ANISOU 59 C VAL A 34 20212 13854 12865 -2316 334 -1831 C ATOM 60 O VAL A 34 13.280 26.788 51.630 1.00121.84 O ANISOU 60 O VAL A 34 20083 13462 12748 -2152 384 -1683 O ATOM 61 CB VAL A 34 14.073 28.987 54.100 1.00129.35 C ANISOU 61 CB VAL A 34 21408 14337 13401 -2607 502 -2140 C ATOM 62 CG1 VAL A 34 14.017 29.819 52.820 1.00129.68 C ANISOU 62 CG1 VAL A 34 21702 14068 13504 -2686 653 -2106 C ATOM 63 CG2 VAL A 34 13.357 29.715 55.236 1.00130.43 C ANISOU 63 CG2 VAL A 34 21774 14345 13439 -2546 556 -2223 C ATOM 64 N GLY A 35 15.218 26.295 52.705 1.00118.96 N ANISOU 64 N GLY A 35 19372 13564 12265 -2492 242 -1907 N ATOM 65 CA GLY A 35 15.875 25.566 51.623 1.00116.93 C ANISOU 65 CA GLY A 35 18905 13428 12094 -2524 197 -1829 C ATOM 66 C GLY A 35 15.088 24.369 51.131 1.00116.30 C ANISOU 66 C GLY A 35 18677 13391 12121 -2214 123 -1614 C ATOM 67 O GLY A 35 14.874 24.228 49.924 1.00114.37 O ANISOU 67 O GLY A 35 18452 13026 11976 -2156 162 -1501 O ATOM 68 N MET A 36 14.624 23.515 52.067 1.00111.31 N ANISOU 68 N MET A 36 17908 12923 11461 -2018 24 -1560 N ATOM 69 CA MET A 36 13.805 22.347 51.733 1.00108.44 C ANISOU 69 CA MET A 36 17417 12598 11188 -1735 -34 -1368 C ATOM 70 C MET A 36 12.382 22.773 51.372 1.00108.62 C ANISOU 70 C MET A 36 17660 12342 11266 -1541 56 -1264 C ATOM 71 O MET A 36 11.714 22.063 50.625 1.00106.28 O ANISOU 71 O MET A 36 17299 12017 11066 -1356 45 -1113 O ATOM 72 CB MET A 36 13.790 21.304 52.856 1.00110.66 C ANISOU 72 CB MET A 36 17503 13134 11410 -1598 -150 -1345 C ATOM 73 CG MET A 36 14.922 20.315 52.745 1.00114.90 C ANISOU 73 CG MET A 36 17756 13964 11936 -1647 -258 -1345 C ATOM 74 SD MET A 36 14.563 18.721 53.525 1.00118.49 S ANISOU 74 SD MET A 36 18005 14644 12372 -1374 -371 -1214 S ATOM 75 CE MET A 36 16.081 17.849 53.156 1.00115.56 C ANISOU 75 CE MET A 36 17343 14585 11978 -1458 -474 -1236 C ATOM 76 N GLY A 37 11.953 23.929 51.882 1.00104.24 N ANISOU 76 N GLY A 37 17364 11597 10646 -1585 146 -1353 N ATOM 77 CA GLY A 37 10.646 24.507 51.594 1.00102.44 C ANISOU 77 CA GLY A 37 17368 11108 10446 -1398 241 -1275 C ATOM 78 C GLY A 37 10.527 24.965 50.153 1.00102.69 C ANISOU 78 C GLY A 37 17527 10935 10556 -1404 327 -1206 C ATOM 79 O GLY A 37 9.484 24.765 49.528 1.00100.68 O ANISOU 79 O GLY A 37 17313 10577 10363 -1178 353 -1073 O ATOM 80 N ILE A 38 11.613 25.560 49.613 1.00 98.49 N ANISOU 80 N ILE A 38 17046 10361 10014 -1665 374 -1299 N ATOM 81 CA ILE A 38 11.694 26.058 48.236 1.00 97.54 C ANISOU 81 CA ILE A 38 17060 10048 9953 -1709 466 -1247 C ATOM 82 C ILE A 38 11.696 24.879 47.248 1.00 97.64 C ANISOU 82 C ILE A 38 16826 10196 10075 -1590 386 -1101 C ATOM 83 O ILE A 38 10.940 24.922 46.276 1.00 96.27 O ANISOU 83 O ILE A 38 16740 9877 9963 -1428 434 -981 O ATOM 84 CB ILE A 38 12.929 26.992 48.038 1.00102.68 C ANISOU 84 CB ILE A 38 17828 10635 10552 -2057 547 -1405 C ATOM 85 CG1 ILE A 38 12.736 28.331 48.788 1.00105.26 C ANISOU 85 CG1 ILE A 38 18480 10741 10774 -2163 667 -1540 C ATOM 86 CG2 ILE A 38 13.234 27.243 46.542 1.00103.33 C ANISOU 86 CG2 ILE A 38 17984 10577 10701 -2123 626 -1340 C ATOM 87 CD1 ILE A 38 14.040 29.085 49.145 1.00113.82 C ANISOU 87 CD1 ILE A 38 19617 11855 11775 -2550 720 -1751 C ATOM 88 N VAL A 39 12.535 23.837 47.495 1.00 92.29 N ANISOU 88 N VAL A 39 15850 9803 9413 -1660 267 -1113 N ATOM 89 CA VAL A 39 12.651 22.673 46.602 1.00 89.63 C ANISOU 89 CA VAL A 39 15282 9601 9173 -1563 195 -987 C ATOM 90 C VAL A 39 11.325 21.886 46.560 1.00 90.02 C ANISOU 90 C VAL A 39 15283 9641 9279 -1259 162 -837 C ATOM 91 O VAL A 39 10.924 21.473 45.473 1.00 88.60 O ANISOU 91 O VAL A 39 15066 9417 9182 -1147 170 -723 O ATOM 92 CB VAL A 39 13.879 21.743 46.849 1.00 93.38 C ANISOU 92 CB VAL A 39 15462 10379 9640 -1687 83 -1032 C ATOM 93 CG1 VAL A 39 15.193 22.481 46.610 1.00 94.99 C ANISOU 93 CG1 VAL A 39 15683 10612 9797 -1998 124 -1177 C ATOM 94 CG2 VAL A 39 13.864 21.092 48.226 1.00 93.18 C ANISOU 94 CG2 VAL A 39 15298 10560 9546 -1614 -13 -1064 C ATOM 95 N MET A 40 10.625 21.746 47.709 1.00 85.23 N ANISOU 95 N MET A 40 14687 9073 8623 -1136 135 -846 N ATOM 96 CA MET A 40 9.327 21.066 47.808 1.00 83.19 C ANISOU 96 CA MET A 40 14388 8816 8403 -870 118 -726 C ATOM 97 C MET A 40 8.261 21.824 47.020 1.00 84.89 C ANISOU 97 C MET A 40 14812 8800 8644 -731 215 -665 C ATOM 98 O MET A 40 7.426 21.196 46.372 1.00 83.29 O ANISOU 98 O MET A 40 14534 8608 8507 -548 205 -550 O ATOM 99 CB MET A 40 8.891 20.911 49.272 1.00 86.13 C ANISOU 99 CB MET A 40 14753 9274 8700 -797 85 -768 C ATOM 100 CG MET A 40 9.532 19.739 49.968 1.00 89.73 C ANISOU 100 CG MET A 40 14966 9987 9139 -812 -23 -765 C ATOM 101 SD MET A 40 9.114 19.693 51.724 1.00 95.36 S ANISOU 101 SD MET A 40 15700 10792 9740 -743 -51 -824 S ATOM 102 CE MET A 40 10.116 18.345 52.243 1.00 91.77 C ANISOU 102 CE MET A 40 14972 10636 9259 -767 -172 -810 C ATOM 103 N SER A 41 8.316 23.171 47.056 1.00 81.42 N ANISOU 103 N SER A 41 14637 8155 8143 -817 312 -746 N ATOM 104 CA SER A 41 7.413 24.067 46.334 1.00 80.97 C ANISOU 104 CA SER A 41 14823 7859 8082 -681 418 -697 C ATOM 105 C SER A 41 7.645 23.966 44.827 1.00 83.21 C ANISOU 105 C SER A 41 15092 8086 8438 -687 441 -616 C ATOM 106 O SER A 41 6.678 23.978 44.066 1.00 81.92 O ANISOU 106 O SER A 41 14980 7843 8302 -480 473 -516 O ATOM 107 CB SER A 41 7.606 25.507 46.801 1.00 86.04 C ANISOU 107 CB SER A 41 15774 8288 8631 -799 527 -815 C ATOM 108 OG SER A 41 7.310 25.643 48.181 1.00 92.73 O ANISOU 108 OG SER A 41 16647 9181 9403 -777 510 -891 O ATOM 109 N LEU A 42 8.926 23.853 44.401 1.00 79.67 N ANISOU 109 N LEU A 42 14561 7697 8014 -922 423 -664 N ATOM 110 CA LEU A 42 9.315 23.720 42.994 1.00 78.88 C ANISOU 110 CA LEU A 42 14432 7560 7977 -959 444 -596 C ATOM 111 C LEU A 42 8.912 22.347 42.461 1.00 80.26 C ANISOU 111 C LEU A 42 14341 7913 8241 -798 349 -477 C ATOM 112 O LEU A 42 8.446 22.249 41.325 1.00 79.31 O ANISOU 112 O LEU A 42 14237 7730 8167 -681 374 -383 O ATOM 113 CB LEU A 42 10.829 23.952 42.786 1.00 79.90 C ANISOU 113 CB LEU A 42 14525 7733 8098 -1267 453 -695 C ATOM 114 CG LEU A 42 11.375 25.391 42.905 1.00 86.97 C ANISOU 114 CG LEU A 42 15713 8418 8915 -1483 581 -817 C ATOM 115 CD1 LEU A 42 12.879 25.408 42.706 1.00 87.93 C ANISOU 115 CD1 LEU A 42 15729 8649 9032 -1798 577 -921 C ATOM 116 CD2 LEU A 42 10.726 26.342 41.894 1.00 90.13 C ANISOU 116 CD2 LEU A 42 16413 8527 9304 -1381 714 -749 C ATOM 117 N ILE A 43 9.067 21.295 43.296 1.00 75.37 N ANISOU 117 N ILE A 43 13492 7511 7636 -787 247 -482 N ATOM 118 CA ILE A 43 8.702 19.914 42.974 1.00 73.15 C ANISOU 118 CA ILE A 43 12969 7395 7429 -649 166 -381 C ATOM 119 C ILE A 43 7.181 19.864 42.703 1.00 75.62 C ANISOU 119 C ILE A 43 13338 7637 7758 -396 196 -293 C ATOM 120 O ILE A 43 6.787 19.329 41.669 1.00 74.44 O ANISOU 120 O ILE A 43 13107 7506 7670 -297 189 -206 O ATOM 121 CB ILE A 43 9.194 18.931 44.086 1.00 75.86 C ANISOU 121 CB ILE A 43 13110 7958 7757 -687 71 -412 C ATOM 122 CG1 ILE A 43 10.692 18.589 43.868 1.00 76.65 C ANISOU 122 CG1 ILE A 43 13066 8194 7863 -888 22 -463 C ATOM 123 CG2 ILE A 43 8.354 17.650 44.158 1.00 74.81 C ANISOU 123 CG2 ILE A 43 12808 7943 7675 -497 19 -311 C ATOM 124 CD1 ILE A 43 11.487 18.127 45.121 1.00 84.46 C ANISOU 124 CD1 ILE A 43 13920 9383 8786 -972 -56 -541 C ATOM 125 N VAL A 44 6.354 20.499 43.572 1.00 72.21 N ANISOU 125 N VAL A 44 13049 7126 7260 -297 235 -325 N ATOM 126 CA VAL A 44 4.890 20.594 43.418 1.00 71.40 C ANISOU 126 CA VAL A 44 13004 6974 7151 -52 271 -260 C ATOM 127 C VAL A 44 4.558 21.285 42.076 1.00 76.28 C ANISOU 127 C VAL A 44 13766 7439 7777 28 339 -206 C ATOM 128 O VAL A 44 3.748 20.754 41.312 1.00 75.23 O ANISOU 128 O VAL A 44 13539 7362 7683 194 327 -124 O ATOM 129 CB VAL A 44 4.202 21.313 44.622 1.00 75.65 C ANISOU 129 CB VAL A 44 13694 7447 7604 26 311 -319 C ATOM 130 CG1 VAL A 44 2.767 21.730 44.294 1.00 75.52 C ANISOU 130 CG1 VAL A 44 13779 7355 7560 281 368 -264 C ATOM 131 CG2 VAL A 44 4.227 20.446 45.876 1.00 74.66 C ANISOU 131 CG2 VAL A 44 13405 7495 7467 10 242 -344 C ATOM 132 N LEU A 45 5.211 22.436 41.785 1.00 74.26 N ANISOU 132 N LEU A 45 13739 6999 7479 -96 415 -256 N ATOM 133 CA LEU A 45 5.000 23.201 40.551 1.00 74.99 C ANISOU 133 CA LEU A 45 14013 6920 7559 -26 496 -205 C ATOM 134 C LEU A 45 5.384 22.392 39.298 1.00 77.74 C ANISOU 134 C LEU A 45 14187 7360 7989 -49 453 -130 C ATOM 135 O LEU A 45 4.598 22.354 38.351 1.00 76.98 O ANISOU 135 O LEU A 45 14104 7246 7901 135 470 -48 O ATOM 136 CB LEU A 45 5.763 24.541 40.578 1.00 77.10 C ANISOU 136 CB LEU A 45 14573 6961 7760 -199 601 -284 C ATOM 137 CG LEU A 45 5.240 25.622 41.543 1.00 83.48 C ANISOU 137 CG LEU A 45 15640 7607 8470 -141 680 -351 C ATOM 138 CD1 LEU A 45 6.284 26.705 41.771 1.00 85.04 C ANISOU 138 CD1 LEU A 45 16078 7623 8611 -402 773 -461 C ATOM 139 CD2 LEU A 45 3.931 26.236 41.055 1.00 86.97 C ANISOU 139 CD2 LEU A 45 16268 7918 8859 160 751 -274 C ATOM 140 N ALA A 46 6.557 21.715 39.312 1.00 73.80 N ANISOU 140 N ALA A 46 13517 6981 7544 -260 394 -162 N ATOM 141 CA ALA A 46 7.052 20.888 38.199 1.00 72.33 C ANISOU 141 CA ALA A 46 13156 6891 7434 -299 351 -101 C ATOM 142 C ALA A 46 6.133 19.686 37.909 1.00 73.82 C ANISOU 142 C ALA A 46 13129 7239 7681 -110 282 -18 C ATOM 143 O ALA A 46 6.017 19.271 36.752 1.00 73.15 O ANISOU 143 O ALA A 46 12972 7182 7640 -53 275 49 O ATOM 144 CB ALA A 46 8.462 20.399 38.492 1.00 72.91 C ANISOU 144 CB ALA A 46 13081 7084 7536 -542 300 -163 C ATOM 145 N ILE A 47 5.481 19.142 38.952 1.00 68.73 N ANISOU 145 N ILE A 47 12387 6697 7029 -24 239 -28 N ATOM 146 CA ILE A 47 4.558 18.017 38.828 1.00 66.84 C ANISOU 146 CA ILE A 47 11956 6606 6836 131 191 33 C ATOM 147 C ILE A 47 3.230 18.498 38.202 1.00 71.51 C ANISOU 147 C ILE A 47 12637 7140 7394 357 238 80 C ATOM 148 O ILE A 47 2.779 17.894 37.230 1.00 70.26 O ANISOU 148 O ILE A 47 12363 7057 7275 447 220 138 O ATOM 149 CB ILE A 47 4.344 17.306 40.201 1.00 69.11 C ANISOU 149 CB ILE A 47 12128 7016 7115 133 145 3 C ATOM 150 CG1 ILE A 47 5.607 16.521 40.622 1.00 68.62 C ANISOU 150 CG1 ILE A 47 11924 7064 7083 -43 82 -24 C ATOM 151 CG2 ILE A 47 3.128 16.378 40.160 1.00 68.58 C ANISOU 151 CG2 ILE A 47 11916 7068 7075 302 128 54 C ATOM 152 CD1 ILE A 47 5.686 16.117 42.076 1.00 72.99 C ANISOU 152 CD1 ILE A 47 12423 7709 7600 -66 46 -66 C ATOM 153 N VAL A 48 2.615 19.570 38.758 1.00 69.77 N ANISOU 153 N VAL A 48 12617 6800 7094 454 298 51 N ATOM 154 CA VAL A 48 1.322 20.121 38.320 1.00 70.63 C ANISOU 154 CA VAL A 48 12820 6868 7146 701 344 89 C ATOM 155 C VAL A 48 1.405 20.640 36.869 1.00 76.07 C ANISOU 155 C VAL A 48 13616 7461 7825 759 385 145 C ATOM 156 O VAL A 48 0.625 20.181 36.029 1.00 75.04 O ANISOU 156 O VAL A 48 13374 7433 7703 917 366 199 O ATOM 157 CB VAL A 48 0.783 21.208 39.298 1.00 76.04 C ANISOU 157 CB VAL A 48 13722 7432 7737 792 407 41 C ATOM 158 CG1 VAL A 48 -0.423 21.950 38.715 1.00 77.02 C ANISOU 158 CG1 VAL A 48 13980 7500 7784 1065 465 83 C ATOM 159 CG2 VAL A 48 0.425 20.599 40.654 1.00 75.25 C ANISOU 159 CG2 VAL A 48 13496 7459 7638 785 367 -1 C ATOM 160 N PHE A 49 2.343 21.581 36.587 1.00 74.46 N ANISOU 160 N PHE A 49 13627 7068 7595 625 445 126 N ATOM 161 CA PHE A 49 2.570 22.194 35.271 1.00 74.86 C ANISOU 161 CA PHE A 49 13826 6992 7624 655 503 178 C ATOM 162 C PHE A 49 2.793 21.136 34.213 1.00 74.61 C ANISOU 162 C PHE A 49 13567 7109 7671 633 439 232 C ATOM 163 O PHE A 49 2.084 21.123 33.211 1.00 74.42 O ANISOU 163 O PHE A 49 13537 7114 7625 813 446 295 O ATOM 164 CB PHE A 49 3.777 23.151 35.326 1.00 78.62 C ANISOU 164 CB PHE A 49 14530 7265 8075 430 578 128 C ATOM 165 CG PHE A 49 4.147 23.888 34.054 1.00 82.22 C ANISOU 165 CG PHE A 49 15184 7558 8500 426 661 176 C ATOM 166 CD1 PHE A 49 3.572 25.118 33.750 1.00 87.74 C ANISOU 166 CD1 PHE A 49 16200 8045 9094 590 772 204 C ATOM 167 CD2 PHE A 49 5.130 23.391 33.202 1.00 84.20 C ANISOU 167 CD2 PHE A 49 15323 7854 8815 253 640 193 C ATOM 168 CE1 PHE A 49 3.951 25.824 32.602 1.00 89.88 C ANISOU 168 CE1 PHE A 49 16682 8145 9322 583 863 254 C ATOM 169 CE2 PHE A 49 5.497 24.090 32.048 1.00 88.24 C ANISOU 169 CE2 PHE A 49 16028 8209 9290 239 727 237 C ATOM 170 CZ PHE A 49 4.910 25.305 31.762 1.00 88.35 C ANISOU 170 CZ PHE A 49 16368 8005 9198 400 841 269 C ATOM 171 N GLY A 50 3.762 20.260 34.461 1.00 68.46 N ANISOU 171 N GLY A 50 12606 6433 6974 424 378 204 N ATOM 172 CA GLY A 50 4.135 19.179 33.564 1.00 66.49 C ANISOU 172 CA GLY A 50 12141 6320 6803 375 319 245 C ATOM 173 C GLY A 50 3.001 18.243 33.209 1.00 68.87 C ANISOU 173 C GLY A 50 12249 6790 7127 559 269 288 C ATOM 174 O GLY A 50 2.874 17.848 32.048 1.00 67.94 O ANISOU 174 O GLY A 50 12055 6727 7031 614 257 336 O ATOM 175 N ASN A 51 2.160 17.889 34.195 1.00 64.77 N ANISOU 175 N ASN A 51 11650 6361 6598 647 246 264 N ATOM 176 CA ASN A 51 1.074 16.945 33.955 1.00 63.44 C ANISOU 176 CA ASN A 51 11284 6371 6450 790 207 286 C ATOM 177 C ASN A 51 -0.155 17.589 33.308 1.00 68.25 C ANISOU 177 C ASN A 51 11969 6984 6980 1038 242 315 C ATOM 178 O ASN A 51 -0.733 16.944 32.429 1.00 66.79 O ANISOU 178 O ASN A 51 11635 6934 6808 1128 216 341 O ATOM 179 CB ASN A 51 0.713 16.177 35.204 1.00 60.86 C ANISOU 179 CB ASN A 51 10823 6156 6145 766 175 249 C ATOM 180 CG ASN A 51 1.715 15.076 35.432 1.00 67.15 C ANISOU 180 CG ASN A 51 11467 7024 7023 579 125 243 C ATOM 181 OD1 ASN A 51 1.805 14.112 34.660 1.00 54.46 O ANISOU 181 OD1 ASN A 51 9707 5514 5474 556 96 271 O ATOM 182 ND2 ASN A 51 2.554 15.234 36.443 1.00 58.47 N ANISOU 182 ND2 ASN A 51 10417 5879 5921 446 117 205 N ATOM 183 N VAL A 52 -0.524 18.852 33.657 1.00 66.69 N ANISOU 183 N VAL A 52 12005 6644 6691 1155 304 308 N ATOM 184 CA VAL A 52 -1.656 19.496 32.962 1.00 67.65 C ANISOU 184 CA VAL A 52 12208 6777 6718 1425 338 343 C ATOM 185 C VAL A 52 -1.269 19.698 31.494 1.00 71.11 C ANISOU 185 C VAL A 52 12704 7167 7149 1448 351 401 C ATOM 186 O VAL A 52 -2.119 19.524 30.628 1.00 70.89 O ANISOU 186 O VAL A 52 12594 7263 7080 1636 337 433 O ATOM 187 CB VAL A 52 -2.244 20.794 33.578 1.00 73.20 C ANISOU 187 CB VAL A 52 13164 7338 7309 1593 410 331 C ATOM 188 CG1 VAL A 52 -3.039 20.503 34.841 1.00 72.94 C ANISOU 188 CG1 VAL A 52 13032 7416 7265 1650 394 280 C ATOM 189 CG2 VAL A 52 -1.181 21.852 33.823 1.00 73.93 C ANISOU 189 CG2 VAL A 52 13544 7166 7381 1449 479 320 C ATOM 190 N LEU A 53 0.028 19.980 31.226 1.00 67.18 N ANISOU 190 N LEU A 53 12321 6516 6690 1244 375 408 N ATOM 191 CA LEU A 53 0.614 20.144 29.893 1.00 67.10 C ANISOU 191 CA LEU A 53 12373 6444 6680 1216 396 460 C ATOM 192 C LEU A 53 0.352 18.890 29.043 1.00 69.73 C ANISOU 192 C LEU A 53 12427 6994 7074 1235 321 481 C ATOM 193 O LEU A 53 -0.140 19.010 27.925 1.00 69.76 O ANISOU 193 O LEU A 53 12438 7042 7027 1393 327 528 O ATOM 194 CB LEU A 53 2.129 20.408 30.037 1.00 67.28 C ANISOU 194 CB LEU A 53 12497 6314 6751 936 426 437 C ATOM 195 CG LEU A 53 2.910 20.881 28.815 1.00 73.12 C ANISOU 195 CG LEU A 53 13372 6932 7477 871 480 483 C ATOM 196 CD1 LEU A 53 2.614 22.343 28.495 1.00 75.39 C ANISOU 196 CD1 LEU A 53 14007 6994 7644 1011 592 516 C ATOM 197 CD2 LEU A 53 4.403 20.715 29.044 1.00 76.11 C ANISOU 197 CD2 LEU A 53 13731 7260 7926 562 483 440 C ATOM 198 N VAL A 54 0.616 17.695 29.609 1.00 64.98 N ANISOU 198 N VAL A 54 11591 6530 6569 1088 256 444 N ATOM 199 CA VAL A 54 0.421 16.389 28.971 1.00 63.59 C ANISOU 199 CA VAL A 54 11154 6548 6458 1071 194 449 C ATOM 200 C VAL A 54 -1.084 16.143 28.710 1.00 67.60 C ANISOU 200 C VAL A 54 11545 7230 6909 1299 177 445 C ATOM 201 O VAL A 54 -1.453 15.766 27.597 1.00 66.52 O ANISOU 201 O VAL A 54 11310 7204 6759 1382 158 466 O ATOM 202 CB VAL A 54 1.066 15.255 29.832 1.00 66.30 C ANISOU 202 CB VAL A 54 11323 6965 6902 871 147 411 C ATOM 203 CG1 VAL A 54 0.674 13.862 29.338 1.00 65.23 C ANISOU 203 CG1 VAL A 54 10938 7021 6826 866 99 407 C ATOM 204 CG2 VAL A 54 2.584 15.393 29.868 1.00 65.75 C ANISOU 204 CG2 VAL A 54 11323 6781 6879 656 153 409 C ATOM 205 N ILE A 55 -1.934 16.362 29.734 1.00 65.50 N ANISOU 205 N ILE A 55 11283 7003 6603 1397 186 411 N ATOM 206 CA ILE A 55 -3.387 16.158 29.672 1.00 66.04 C ANISOU 206 CA ILE A 55 11223 7262 6609 1605 175 389 C ATOM 207 C ILE A 55 -4.007 17.106 28.621 1.00 71.49 C ANISOU 207 C ILE A 55 12038 7944 7181 1853 201 432 C ATOM 208 O ILE A 55 -4.833 16.652 27.826 1.00 71.14 O ANISOU 208 O ILE A 55 11832 8098 7098 1984 172 426 O ATOM 209 CB ILE A 55 -4.032 16.288 31.089 1.00 69.49 C ANISOU 209 CB ILE A 55 11658 7724 7024 1643 190 342 C ATOM 210 CG1 ILE A 55 -3.589 15.104 31.993 1.00 68.01 C ANISOU 210 CG1 ILE A 55 11305 7594 6940 1425 159 305 C ATOM 211 CG2 ILE A 55 -5.571 16.362 31.020 1.00 71.71 C ANISOU 211 CG2 ILE A 55 11835 8200 7212 1887 192 316 C ATOM 212 CD1 ILE A 55 -3.502 15.402 33.486 1.00 73.31 C ANISOU 212 CD1 ILE A 55 12059 8190 7607 1374 179 273 C ATOM 213 N THR A 56 -3.560 18.385 28.581 1.00 69.51 N ANISOU 213 N THR A 56 12079 7465 6866 1909 261 473 N ATOM 214 CA THR A 56 -4.014 19.401 27.617 1.00 70.95 C ANISOU 214 CA THR A 56 12445 7592 6922 2155 304 530 C ATOM 215 C THR A 56 -3.619 18.984 26.186 1.00 74.64 C ANISOU 215 C THR A 56 12844 8112 7403 2132 280 572 C ATOM 216 O THR A 56 -4.450 19.075 25.278 1.00 75.04 O ANISOU 216 O THR A 56 12849 8302 7362 2358 267 595 O ATOM 217 CB THR A 56 -3.454 20.797 27.981 1.00 77.39 C ANISOU 217 CB THR A 56 13621 8109 7676 2167 394 560 C ATOM 218 OG1 THR A 56 -3.840 21.123 29.314 1.00 74.03 O ANISOU 218 OG1 THR A 56 13245 7647 7235 2186 412 512 O ATOM 219 CG2 THR A 56 -3.941 21.899 27.045 1.00 78.24 C ANISOU 219 CG2 THR A 56 13962 8128 7635 2444 455 628 C ATOM 220 N ALA A 57 -2.364 18.506 26.009 1.00 69.91 N ANISOU 220 N ALA A 57 12227 7423 6913 1867 271 578 N ATOM 221 CA ALA A 57 -1.802 18.063 24.733 1.00 69.32 C ANISOU 221 CA ALA A 57 12093 7381 6866 1806 253 614 C ATOM 222 C ALA A 57 -2.611 16.925 24.109 1.00 72.93 C ANISOU 222 C ALA A 57 12256 8120 7337 1875 182 586 C ATOM 223 O ALA A 57 -2.923 17.001 22.923 1.00 73.47 O ANISOU 223 O ALA A 57 12313 8266 7337 2012 175 620 O ATOM 224 CB ALA A 57 -0.355 17.633 24.917 1.00 68.85 C ANISOU 224 CB ALA A 57 12026 7209 6925 1502 252 607 C ATOM 225 N ILE A 58 -2.974 15.895 24.903 1.00 68.72 N ANISOU 225 N ILE A 58 11495 7737 6878 1780 137 521 N ATOM 226 CA ILE A 58 -3.740 14.739 24.421 1.00 68.32 C ANISOU 226 CA ILE A 58 11163 7950 6844 1802 83 475 C ATOM 227 C ILE A 58 -5.201 15.158 24.141 1.00 75.54 C ANISOU 227 C ILE A 58 12028 9050 7626 2089 78 456 C ATOM 228 O ILE A 58 -5.745 14.767 23.107 1.00 75.64 O ANISOU 228 O ILE A 58 11902 9249 7589 2188 46 445 O ATOM 229 CB ILE A 58 -3.617 13.519 25.385 1.00 69.77 C ANISOU 229 CB ILE A 58 11155 8210 7145 1596 58 413 C ATOM 230 CG1 ILE A 58 -2.161 13.001 25.409 1.00 68.78 C ANISOU 230 CG1 ILE A 58 11051 7948 7134 1347 53 434 C ATOM 231 CG2 ILE A 58 -4.571 12.375 24.997 1.00 70.28 C ANISOU 231 CG2 ILE A 58 10948 8542 7214 1614 24 349 C ATOM 232 CD1 ILE A 58 -1.729 12.360 26.717 1.00 77.02 C ANISOU 232 CD1 ILE A 58 12042 8959 8265 1173 49 400 C ATOM 233 N ALA A 59 -5.800 15.995 25.012 1.00 74.65 N ANISOU 233 N ALA A 59 12031 8891 7442 2233 109 452 N ATOM 234 CA ALA A 59 -7.181 16.473 24.859 1.00 76.55 C ANISOU 234 CA ALA A 59 12228 9316 7541 2531 108 433 C ATOM 235 C ALA A 59 -7.372 17.437 23.672 1.00 83.54 C ANISOU 235 C ALA A 59 13281 10174 8288 2786 125 503 C ATOM 236 O ALA A 59 -8.458 17.445 23.084 1.00 84.54 O ANISOU 236 O ALA A 59 13282 10541 8299 3022 98 482 O ATOM 237 CB ALA A 59 -7.645 17.154 26.134 1.00 77.85 C ANISOU 237 CB ALA A 59 12501 9411 7667 2617 145 415 C ATOM 238 N LYS A 60 -6.346 18.249 23.327 1.00 81.10 N ANISOU 238 N LYS A 60 13251 9584 7978 2744 175 583 N ATOM 239 CA LYS A 60 -6.469 19.248 22.257 1.00 82.88 C ANISOU 239 CA LYS A 60 13688 9740 8061 2990 212 663 C ATOM 240 C LYS A 60 -5.935 18.798 20.888 1.00 86.66 C ANISOU 240 C LYS A 60 14112 10262 8553 2933 187 698 C ATOM 241 O LYS A 60 -6.465 19.261 19.877 1.00 88.39 O ANISOU 241 O LYS A 60 14386 10566 8634 3186 189 743 O ATOM 242 CB LYS A 60 -5.785 20.568 22.650 1.00 86.28 C ANISOU 242 CB LYS A 60 14506 9823 8454 3004 308 729 C ATOM 243 N PHE A 61 -4.897 17.941 20.832 1.00 81.01 N ANISOU 243 N PHE A 61 13300 9493 7988 2626 167 683 N ATOM 244 CA PHE A 61 -4.327 17.538 19.539 1.00 80.50 C ANISOU 244 CA PHE A 61 13195 9456 7934 2567 150 717 C ATOM 245 C PHE A 61 -4.698 16.094 19.164 1.00 83.59 C ANISOU 245 C PHE A 61 13239 10129 8394 2470 70 640 C ATOM 246 O PHE A 61 -4.312 15.147 19.852 1.00 81.80 O ANISOU 246 O PHE A 61 12858 9920 8303 2232 46 585 O ATOM 247 CB PHE A 61 -2.800 17.763 19.508 1.00 81.47 C ANISOU 247 CB PHE A 61 13500 9304 8152 2316 201 763 C ATOM 248 CG PHE A 61 -2.381 19.184 19.835 1.00 84.54 C ANISOU 248 CG PHE A 61 14248 9400 8471 2373 298 826 C ATOM 249 CD1 PHE A 61 -2.851 20.259 19.087 1.00 90.05 C ANISOU 249 CD1 PHE A 61 15179 10031 9006 2652 354 899 C ATOM 250 CD2 PHE A 61 -1.528 19.448 20.898 1.00 86.29 C ANISOU 250 CD2 PHE A 61 14588 9418 8781 2153 338 807 C ATOM 251 CE1 PHE A 61 -2.483 21.573 19.405 1.00 92.37 C ANISOU 251 CE1 PHE A 61 15836 10030 9229 2699 461 954 C ATOM 252 CE2 PHE A 61 -1.150 20.762 21.207 1.00 90.63 C ANISOU 252 CE2 PHE A 61 15479 9693 9263 2183 439 849 C ATOM 253 CZ PHE A 61 -1.628 21.815 20.456 1.00 90.66 C ANISOU 253 CZ PHE A 61 15731 9606 9109 2450 506 923 C ATOM 254 N GLU A 62 -5.456 15.957 18.047 1.00 81.20 N ANISOU 254 N GLU A 62 12825 10046 7981 2666 34 636 N ATOM 255 CA GLU A 62 -5.996 14.718 17.468 1.00 80.25 C ANISOU 255 CA GLU A 62 12388 10221 7883 2618 -35 554 C ATOM 256 C GLU A 62 -4.919 13.653 17.179 1.00 81.38 C ANISOU 256 C GLU A 62 12435 10309 8179 2315 -48 538 C ATOM 257 O GLU A 62 -5.203 12.466 17.321 1.00 79.77 O ANISOU 257 O GLU A 62 11984 10277 8048 2177 -86 452 O ATOM 258 CB GLU A 62 -6.822 15.009 16.189 1.00 83.35 C ANISOU 258 CB GLU A 62 12735 10829 8104 2899 -64 565 C ATOM 259 CG GLU A 62 -6.042 15.451 14.956 1.00 95.22 C ANISOU 259 CG GLU A 62 14414 12207 9558 2938 -41 656 C ATOM 260 CD GLU A 62 -5.479 16.859 14.988 1.00110.90 C ANISOU 260 CD GLU A 62 16774 13887 11476 3053 42 773 C ATOM 261 OE1 GLU A 62 -6.230 17.805 14.662 1.00109.40 O ANISOU 261 OE1 GLU A 62 16722 13732 11112 3372 61 821 O ATOM 262 OE2 GLU A 62 -4.289 17.015 15.353 1.00 92.78 O ANISOU 262 OE2 GLU A 62 14639 11321 9294 2824 92 813 O ATOM 263 N ARG A 63 -3.696 14.071 16.790 1.00 77.54 N ANISOU 263 N ARG A 63 12145 9584 7732 2211 -9 617 N ATOM 264 CA ARG A 63 -2.570 13.178 16.494 1.00 75.74 C ANISOU 264 CA ARG A 63 11849 9294 7637 1945 -16 612 C ATOM 265 C ARG A 63 -2.125 12.408 17.746 1.00 78.37 C ANISOU 265 C ARG A 63 12089 9572 8117 1708 -20 561 C ATOM 266 O ARG A 63 -1.575 11.308 17.638 1.00 77.29 O ANISOU 266 O ARG A 63 11809 9473 8084 1516 -41 526 O ATOM 267 CB ARG A 63 -1.390 13.982 15.930 1.00 75.65 C ANISOU 267 CB ARG A 63 12086 9040 7620 1897 41 705 C ATOM 268 N LEU A 64 -2.379 12.996 18.926 1.00 74.59 N ANISOU 268 N LEU A 64 11702 9004 7636 1738 2 559 N ATOM 269 CA LEU A 64 -2.041 12.459 20.243 1.00 73.13 C ANISOU 269 CA LEU A 64 11461 8761 7563 1552 2 519 C ATOM 270 C LEU A 64 -3.223 11.696 20.868 1.00 76.14 C ANISOU 270 C LEU A 64 11629 9356 7944 1588 -27 435 C ATOM 271 O LEU A 64 -3.127 11.272 22.019 1.00 74.83 O ANISOU 271 O LEU A 64 11423 9157 7854 1464 -21 402 O ATOM 272 CB LEU A 64 -1.619 13.623 21.162 1.00 73.70 C ANISOU 272 CB LEU A 64 11775 8608 7619 1561 50 560 C ATOM 273 CG LEU A 64 -0.133 13.984 21.220 1.00 78.27 C ANISOU 273 CG LEU A 64 12516 8961 8262 1374 86 605 C ATOM 274 CD1 LEU A 64 0.339 14.664 19.946 1.00 79.43 C ANISOU 274 CD1 LEU A 64 12815 9021 8344 1436 120 671 C ATOM 275 CD2 LEU A 64 0.123 14.927 22.359 1.00 81.91 C ANISOU 275 CD2 LEU A 64 13168 9240 8713 1352 129 611 C ATOM 276 N GLN A 65 -4.332 11.521 20.118 1.00 72.97 N ANISOU 276 N GLN A 65 11089 9185 7451 1752 -53 395 N ATOM 277 CA GLN A 65 -5.521 10.815 20.604 1.00 72.41 C ANISOU 277 CA GLN A 65 10798 9348 7365 1777 -71 300 C ATOM 278 C GLN A 65 -5.431 9.329 20.236 1.00 74.11 C ANISOU 278 C GLN A 65 10798 9695 7667 1583 -89 229 C ATOM 279 O GLN A 65 -6.095 8.872 19.306 1.00 74.38 O ANISOU 279 O GLN A 65 10675 9943 7643 1641 -114 175 O ATOM 280 CB GLN A 65 -6.820 11.452 20.066 1.00 75.47 C ANISOU 280 CB GLN A 65 11136 9948 7591 2063 -88 278 C ATOM 281 CG GLN A 65 -6.999 12.922 20.443 1.00 91.93 C ANISOU 281 CG GLN A 65 13456 11897 9575 2284 -59 348 C ATOM 282 CD GLN A 65 -7.990 13.164 21.550 1.00113.94 C ANISOU 282 CD GLN A 65 16193 14779 12320 2386 -48 298 C ATOM 283 OE1 GLN A 65 -8.213 12.324 22.434 1.00110.90 O ANISOU 283 OE1 GLN A 65 15657 14463 12018 2226 -47 228 O ATOM 284 NE2 GLN A 65 -8.559 14.361 21.564 1.00105.91 N ANISOU 284 NE2 GLN A 65 15328 13746 11168 2659 -30 339 N ATOM 285 N THR A 66 -4.566 8.589 20.947 1.00 68.56 N ANISOU 285 N THR A 66 10099 8858 7094 1357 -72 230 N ATOM 286 CA THR A 66 -4.371 7.149 20.751 1.00 67.26 C ANISOU 286 CA THR A 66 9771 8769 7016 1164 -72 170 C ATOM 287 C THR A 66 -4.705 6.421 22.050 1.00 71.49 C ANISOU 287 C THR A 66 10232 9317 7615 1042 -42 116 C ATOM 288 O THR A 66 -4.764 7.057 23.106 1.00 71.91 O ANISOU 288 O THR A 66 10380 9282 7663 1081 -29 141 O ATOM 289 CB THR A 66 -2.943 6.830 20.275 1.00 69.31 C ANISOU 289 CB THR A 66 10113 8861 7362 1023 -71 228 C ATOM 290 OG1 THR A 66 -2.000 7.239 21.262 1.00 63.74 O ANISOU 290 OG1 THR A 66 9555 7946 6718 944 -55 285 O ATOM 291 CG2 THR A 66 -2.612 7.447 18.924 1.00 68.92 C ANISOU 291 CG2 THR A 66 10133 8805 7249 1127 -90 279 C ATOM 292 N VAL A 67 -4.906 5.092 21.982 1.00 67.21 N ANISOU 292 N VAL A 67 9536 8874 7126 890 -23 43 N ATOM 293 CA VAL A 67 -5.226 4.280 23.159 1.00 66.60 C ANISOU 293 CA VAL A 67 9399 8803 7103 761 21 -8 C ATOM 294 C VAL A 67 -4.020 4.244 24.126 1.00 69.14 C ANISOU 294 C VAL A 67 9868 8888 7512 656 34 66 C ATOM 295 O VAL A 67 -4.237 4.218 25.338 1.00 68.54 O ANISOU 295 O VAL A 67 9816 8776 7450 627 60 60 O ATOM 296 CB VAL A 67 -5.758 2.861 22.822 1.00 70.70 C ANISOU 296 CB VAL A 67 9744 9470 7648 614 58 -110 C ATOM 297 CG1 VAL A 67 -7.124 2.932 22.143 1.00 71.95 C ANISOU 297 CG1 VAL A 67 9727 9908 7703 712 48 -209 C ATOM 298 CG2 VAL A 67 -4.780 2.074 21.969 1.00 69.74 C ANISOU 298 CG2 VAL A 67 9637 9268 7593 497 57 -91 C ATOM 299 N THR A 68 -2.770 4.319 23.597 1.00 64.76 N ANISOU 299 N THR A 68 9408 8193 7005 610 13 134 N ATOM 300 CA THR A 68 -1.537 4.351 24.397 1.00 63.74 C ANISOU 300 CA THR A 68 9401 7873 6944 520 16 197 C ATOM 301 C THR A 68 -1.488 5.660 25.177 1.00 68.48 C ANISOU 301 C THR A 68 10136 8379 7503 614 5 240 C ATOM 302 O THR A 68 -1.128 5.662 26.358 1.00 68.06 O ANISOU 302 O THR A 68 10143 8239 7480 558 17 253 O ATOM 303 CB THR A 68 -0.297 4.169 23.501 1.00 71.03 C ANISOU 303 CB THR A 68 10367 8711 7911 458 -2 245 C ATOM 304 OG1 THR A 68 -0.422 2.948 22.769 1.00 75.09 O ANISOU 304 OG1 THR A 68 10764 9311 8456 379 14 198 O ATOM 305 CG2 THR A 68 1.010 4.148 24.287 1.00 65.57 C ANISOU 305 CG2 THR A 68 9771 7863 7278 365 -3 298 C ATOM 306 N ASN A 69 -1.890 6.768 24.523 1.00 65.59 N ANISOU 306 N ASN A 69 9829 8034 7060 765 -12 259 N ATOM 307 CA ASN A 69 -1.920 8.086 25.139 1.00 65.48 C ANISOU 307 CA ASN A 69 9969 7918 6991 870 -9 295 C ATOM 308 C ASN A 69 -3.105 8.216 26.088 1.00 71.04 C ANISOU 308 C ASN A 69 10626 8717 7650 952 7 247 C ATOM 309 O ASN A 69 -3.066 9.061 26.985 1.00 71.72 O ANISOU 309 O ASN A 69 10837 8704 7711 1000 18 267 O ATOM 310 CB ASN A 69 -1.931 9.174 24.087 1.00 63.91 C ANISOU 310 CB ASN A 69 9876 7692 6716 1015 -18 339 C ATOM 311 CG ASN A 69 -0.626 9.306 23.341 1.00 76.45 C ANISOU 311 CG ASN A 69 11554 9150 8343 925 -21 394 C ATOM 312 OD1 ASN A 69 0.465 9.064 23.872 1.00 64.37 O ANISOU 312 OD1 ASN A 69 10066 7505 6885 775 -18 412 O ATOM 313 ND2 ASN A 69 -0.709 9.707 22.087 1.00 71.51 N ANISOU 313 ND2 ASN A 69 10955 8555 7660 1023 -26 420 N ATOM 314 N TYR A 70 -4.134 7.355 25.930 1.00 68.21 N ANISOU 314 N TYR A 70 10085 8552 7280 953 16 176 N ATOM 315 CA TYR A 70 -5.284 7.318 26.833 1.00 69.20 C ANISOU 315 CA TYR A 70 10134 8795 7363 1007 40 118 C ATOM 316 C TYR A 70 -4.844 6.734 28.175 1.00 71.37 C ANISOU 316 C TYR A 70 10438 8971 7709 861 70 118 C ATOM 317 O TYR A 70 -5.340 7.155 29.214 1.00 71.20 O ANISOU 317 O TYR A 70 10451 8948 7655 910 89 106 O ATOM 318 CB TYR A 70 -6.464 6.530 26.234 1.00 72.14 C ANISOU 318 CB TYR A 70 10292 9421 7698 1020 50 26 C ATOM 319 CG TYR A 70 -7.357 7.299 25.273 1.00 76.87 C ANISOU 319 CG TYR A 70 10840 10188 8180 1232 21 7 C ATOM 320 CD1 TYR A 70 -7.019 8.587 24.851 1.00 79.46 C ANISOU 320 CD1 TYR A 70 11338 10407 8446 1403 -4 84 C ATOM 321 CD2 TYR A 70 -8.529 6.740 24.779 1.00 79.32 C ANISOU 321 CD2 TYR A 70 10937 10771 8430 1264 23 -92 C ATOM 322 CE1 TYR A 70 -7.829 9.291 23.961 1.00 82.27 C ANISOU 322 CE1 TYR A 70 11665 10916 8678 1628 -27 77 C ATOM 323 CE2 TYR A 70 -9.350 7.438 23.894 1.00 82.00 C ANISOU 323 CE2 TYR A 70 11217 11294 8644 1483 -10 -112 C ATOM 324 CZ TYR A 70 -8.993 8.712 23.483 1.00 91.51 C ANISOU 324 CZ TYR A 70 12605 12380 9784 1679 -37 -20 C ATOM 325 OH TYR A 70 -9.796 9.395 22.599 1.00 95.77 O ANISOU 325 OH TYR A 70 13103 13101 10184 1923 -67 -30 O ATOM 326 N PHE A 71 -3.890 5.786 28.153 1.00 66.95 N ANISOU 326 N PHE A 71 9873 8330 7235 696 74 136 N ATOM 327 CA PHE A 71 -3.327 5.195 29.368 1.00 66.11 C ANISOU 327 CA PHE A 71 9809 8126 7185 575 100 149 C ATOM 328 C PHE A 71 -2.315 6.156 29.994 1.00 70.63 C ANISOU 328 C PHE A 71 10549 8526 7760 587 74 212 C ATOM 329 O PHE A 71 -2.135 6.147 31.214 1.00 70.47 O ANISOU 329 O PHE A 71 10582 8448 7746 550 88 216 O ATOM 330 CB PHE A 71 -2.668 3.839 29.080 1.00 66.98 C ANISOU 330 CB PHE A 71 9865 8216 7371 423 117 149 C ATOM 331 CG PHE A 71 -3.538 2.781 28.447 1.00 68.74 C ANISOU 331 CG PHE A 71 9936 8588 7595 369 156 75 C ATOM 332 CD1 PHE A 71 -4.770 2.447 28.998 1.00 72.74 C ANISOU 332 CD1 PHE A 71 10348 9225 8066 365 205 3 C ATOM 333 CD2 PHE A 71 -3.093 2.064 27.343 1.00 70.33 C ANISOU 333 CD2 PHE A 71 10088 8800 7832 304 151 70 C ATOM 334 CE1 PHE A 71 -5.577 1.468 28.409 1.00 74.22 C ANISOU 334 CE1 PHE A 71 10389 9561 8249 287 250 -83 C ATOM 335 CE2 PHE A 71 -3.897 1.082 26.757 1.00 73.61 C ANISOU 335 CE2 PHE A 71 10369 9354 8244 236 193 -13 C ATOM 336 CZ PHE A 71 -5.132 0.785 27.297 1.00 72.60 C ANISOU 336 CZ PHE A 71 10145 9362 8079 219 244 -93 C ATOM 337 N ILE A 72 -1.657 6.983 29.149 1.00 67.46 N ANISOU 337 N ILE A 72 10234 8050 7348 631 42 254 N ATOM 338 CA ILE A 72 -0.680 8.001 29.542 1.00 67.00 C ANISOU 338 CA ILE A 72 10341 7833 7283 624 27 299 C ATOM 339 C ILE A 72 -1.419 9.157 30.261 1.00 70.82 C ANISOU 339 C ILE A 72 10926 8292 7692 751 41 290 C ATOM 340 O ILE A 72 -0.897 9.659 31.259 1.00 69.58 O ANISOU 340 O ILE A 72 10878 8028 7532 713 45 298 O ATOM 341 CB ILE A 72 0.164 8.458 28.310 1.00 69.95 C ANISOU 341 CB ILE A 72 10774 8140 7662 618 8 341 C ATOM 342 CG1 ILE A 72 1.338 7.484 28.075 1.00 69.48 C ANISOU 342 CG1 ILE A 72 10663 8055 7681 468 -6 357 C ATOM 343 CG2 ILE A 72 0.671 9.908 28.429 1.00 71.18 C ANISOU 343 CG2 ILE A 72 11123 8150 7771 660 14 373 C ATOM 344 CD1 ILE A 72 1.762 7.295 26.611 1.00 78.74 C ANISOU 344 CD1 ILE A 72 11802 9247 8868 459 -17 377 C ATOM 345 N THR A 73 -2.636 9.545 29.785 1.00 68.51 N ANISOU 345 N THR A 73 10590 8109 7330 908 50 266 N ATOM 346 CA THR A 73 -3.423 10.602 30.444 1.00 69.67 C ANISOU 346 CA THR A 73 10830 8247 7395 1057 69 256 C ATOM 347 C THR A 73 -3.941 10.067 31.795 1.00 73.22 C ANISOU 347 C THR A 73 11214 8750 7855 1012 91 214 C ATOM 348 O THR A 73 -4.026 10.836 32.750 1.00 73.45 O ANISOU 348 O THR A 73 11358 8704 7844 1060 107 213 O ATOM 349 CB THR A 73 -4.523 11.242 29.544 1.00 79.79 C ANISOU 349 CB THR A 73 12090 9645 8581 1269 70 247 C ATOM 350 OG1 THR A 73 -5.196 12.258 30.289 1.00 82.99 O ANISOU 350 OG1 THR A 73 12603 10026 8904 1422 94 240 O ATOM 351 CG2 THR A 73 -5.551 10.263 29.032 1.00 77.42 C ANISOU 351 CG2 THR A 73 11561 9583 8273 1290 65 188 C ATOM 352 N SER A 74 -4.207 8.749 31.888 1.00 69.13 N ANISOU 352 N SER A 74 10533 8345 7388 908 102 180 N ATOM 353 CA SER A 74 -4.614 8.082 33.131 1.00 69.05 C ANISOU 353 CA SER A 74 10469 8377 7389 842 136 146 C ATOM 354 C SER A 74 -3.465 8.158 34.150 1.00 72.14 C ANISOU 354 C SER A 74 10986 8608 7817 740 128 183 C ATOM 355 O SER A 74 -3.690 8.460 35.323 1.00 71.62 O ANISOU 355 O SER A 74 10976 8518 7721 757 147 171 O ATOM 356 CB SER A 74 -4.997 6.630 32.852 1.00 71.93 C ANISOU 356 CB SER A 74 10666 8866 7800 732 164 106 C ATOM 357 OG SER A 74 -5.450 5.974 34.024 1.00 80.48 O ANISOU 357 OG SER A 74 11712 9984 8885 667 214 76 O ATOM 358 N LEU A 75 -2.232 7.926 33.664 1.00 68.20 N ANISOU 358 N LEU A 75 10523 8016 7372 643 98 223 N ATOM 359 CA LEU A 75 -0.974 7.974 34.402 1.00 67.42 C ANISOU 359 CA LEU A 75 10519 7797 7302 544 78 252 C ATOM 360 C LEU A 75 -0.653 9.422 34.817 1.00 70.12 C ANISOU 360 C LEU A 75 11026 8026 7593 596 68 258 C ATOM 361 O LEU A 75 -0.195 9.642 35.936 1.00 70.19 O ANISOU 361 O LEU A 75 11106 7976 7587 550 66 251 O ATOM 362 CB LEU A 75 0.138 7.389 33.506 1.00 67.10 C ANISOU 362 CB LEU A 75 10448 7725 7322 448 51 284 C ATOM 363 CG LEU A 75 1.508 7.123 34.124 1.00 71.85 C ANISOU 363 CG LEU A 75 11093 8253 7952 339 26 308 C ATOM 364 CD1 LEU A 75 1.500 5.853 34.933 1.00 71.98 C ANISOU 364 CD1 LEU A 75 11043 8315 7990 286 47 308 C ATOM 365 CD2 LEU A 75 2.556 6.984 33.044 1.00 74.13 C ANISOU 365 CD2 LEU A 75 11370 8515 8282 278 -1 335 C ATOM 366 N ALA A 76 -0.918 10.399 33.931 1.00 65.88 N ANISOU 366 N ALA A 76 10559 7456 7017 695 69 267 N ATOM 367 CA ALA A 76 -0.690 11.824 34.188 1.00 66.15 C ANISOU 367 CA ALA A 76 10782 7359 6994 751 80 271 C ATOM 368 C ALA A 76 -1.726 12.393 35.165 1.00 69.43 C ANISOU 368 C ALA A 76 11247 7793 7341 870 109 239 C ATOM 369 O ALA A 76 -1.418 13.346 35.887 1.00 69.33 O ANISOU 369 O ALA A 76 11394 7663 7286 874 124 229 O ATOM 370 CB ALA A 76 -0.721 12.607 32.883 1.00 67.48 C ANISOU 370 CB ALA A 76 11027 7480 7131 839 86 299 C ATOM 371 N CYS A 77 -2.952 11.820 35.180 1.00 65.24 N ANISOU 371 N CYS A 77 10578 7417 6793 959 124 215 N ATOM 372 CA CYS A 77 -4.022 12.236 36.088 1.00 65.64 C ANISOU 372 CA CYS A 77 10642 7521 6776 1078 156 179 C ATOM 373 C CYS A 77 -3.637 11.894 37.517 1.00 67.95 C ANISOU 373 C CYS A 77 10957 7777 7084 972 163 163 C ATOM 374 O CYS A 77 -3.692 12.779 38.369 1.00 69.04 O ANISOU 374 O CYS A 77 11228 7836 7167 1021 179 148 O ATOM 375 CB CYS A 77 -5.359 11.610 35.705 1.00 66.60 C ANISOU 375 CB CYS A 77 10582 7849 6876 1172 172 145 C ATOM 376 SG CYS A 77 -6.256 12.506 34.410 1.00 71.88 S ANISOU 376 SG CYS A 77 11257 8595 7458 1402 170 149 S ATOM 377 N ALA A 78 -3.184 10.637 37.765 1.00 61.76 N ANISOU 377 N ALA A 78 10060 7039 6366 831 153 169 N ATOM 378 CA ALA A 78 -2.722 10.150 39.072 1.00 60.67 C ANISOU 378 CA ALA A 78 9939 6878 6236 735 157 163 C ATOM 379 C ALA A 78 -1.563 11.007 39.579 1.00 64.19 C ANISOU 379 C ALA A 78 10542 7181 6666 678 129 170 C ATOM 380 O ALA A 78 -1.483 11.303 40.772 1.00 63.58 O ANISOU 380 O ALA A 78 10535 7074 6547 668 136 148 O ATOM 381 CB ALA A 78 -2.292 8.695 38.963 1.00 60.42 C ANISOU 381 CB ALA A 78 9788 6898 6270 615 155 182 C ATOM 382 N ASP A 79 -0.699 11.441 38.645 1.00 61.36 N ANISOU 382 N ASP A 79 10237 6744 6334 635 102 191 N ATOM 383 CA ASP A 79 0.446 12.311 38.883 1.00 61.67 C ANISOU 383 CA ASP A 79 10418 6656 6357 555 83 185 C ATOM 384 C ASP A 79 -0.003 13.732 39.259 1.00 66.92 C ANISOU 384 C ASP A 79 11261 7219 6945 648 118 157 C ATOM 385 O ASP A 79 0.602 14.345 40.134 1.00 66.62 O ANISOU 385 O ASP A 79 11338 7101 6872 582 118 124 O ATOM 386 CB ASP A 79 1.346 12.342 37.640 1.00 63.06 C ANISOU 386 CB ASP A 79 10592 6788 6579 485 61 213 C ATOM 387 CG ASP A 79 2.209 11.112 37.441 1.00 73.51 C ANISOU 387 CG ASP A 79 11783 8179 7969 370 26 235 C ATOM 388 OD1 ASP A 79 2.339 10.318 38.392 1.00 74.37 O ANISOU 388 OD1 ASP A 79 11831 8344 8082 331 16 230 O ATOM 389 OD2 ASP A 79 2.781 10.961 36.343 1.00 80.50 O ANISOU 389 OD2 ASP A 79 12638 9055 8894 328 12 259 O ATOM 390 N LEU A 80 -1.064 14.245 38.608 1.00 64.75 N ANISOU 390 N LEU A 80 11011 6957 6635 809 148 164 N ATOM 391 CA LEU A 80 -1.632 15.564 38.888 1.00 65.90 C ANISOU 391 CA LEU A 80 11338 7007 6695 941 191 145 C ATOM 392 C LEU A 80 -2.337 15.558 40.256 1.00 69.79 C ANISOU 392 C LEU A 80 11829 7548 7141 992 211 105 C ATOM 393 O LEU A 80 -2.267 16.550 40.986 1.00 70.14 O ANISOU 393 O LEU A 80 12046 7482 7123 1017 239 74 O ATOM 394 CB LEU A 80 -2.597 15.970 37.762 1.00 66.71 C ANISOU 394 CB LEU A 80 11442 7145 6760 1129 213 170 C ATOM 395 CG LEU A 80 -3.245 17.354 37.851 1.00 73.59 C ANISOU 395 CG LEU A 80 12519 7914 7529 1312 266 163 C ATOM 396 CD1 LEU A 80 -2.200 18.474 37.796 1.00 74.92 C ANISOU 396 CD1 LEU A 80 12939 7853 7674 1229 297 163 C ATOM 397 CD2 LEU A 80 -4.288 17.526 36.768 1.00 76.75 C ANISOU 397 CD2 LEU A 80 12874 8408 7881 1527 277 190 C ATOM 398 N VAL A 81 -2.982 14.425 40.608 1.00 65.58 N ANISOU 398 N VAL A 81 11110 7174 6635 995 204 103 N ATOM 399 CA VAL A 81 -3.657 14.227 41.895 1.00 65.83 C ANISOU 399 CA VAL A 81 11116 7270 6625 1029 229 69 C ATOM 400 C VAL A 81 -2.572 14.154 42.995 1.00 71.95 C ANISOU 400 C VAL A 81 11960 7974 7403 881 207 53 C ATOM 401 O VAL A 81 -2.779 14.677 44.090 1.00 72.50 O ANISOU 401 O VAL A 81 12121 8013 7411 910 228 17 O ATOM 402 CB VAL A 81 -4.601 12.987 41.885 1.00 68.54 C ANISOU 402 CB VAL A 81 11248 7798 6995 1047 244 67 C ATOM 403 CG1 VAL A 81 -5.255 12.767 43.245 1.00 68.54 C ANISOU 403 CG1 VAL A 81 11231 7862 6948 1067 281 34 C ATOM 404 CG2 VAL A 81 -5.677 13.125 40.811 1.00 68.65 C ANISOU 404 CG2 VAL A 81 11178 7917 6989 1195 260 65 C ATOM 405 N MET A 82 -1.402 13.560 42.671 1.00 69.30 N ANISOU 405 N MET A 82 11580 7621 7129 732 163 76 N ATOM 406 CA MET A 82 -0.249 13.450 43.566 1.00 69.88 C ANISOU 406 CA MET A 82 11694 7660 7197 596 131 59 C ATOM 407 C MET A 82 0.257 14.842 43.964 1.00 73.59 C ANISOU 407 C MET A 82 12361 7994 7607 572 140 11 C ATOM 408 O MET A 82 0.288 15.163 45.153 1.00 73.74 O ANISOU 408 O MET A 82 12450 8002 7567 560 147 -32 O ATOM 409 CB MET A 82 0.876 12.644 42.889 1.00 72.10 C ANISOU 409 CB MET A 82 11883 7964 7548 470 84 92 C ATOM 410 CG MET A 82 1.757 11.899 43.855 1.00 76.53 C ANISOU 410 CG MET A 82 12397 8579 8103 371 48 88 C ATOM 411 SD MET A 82 0.877 10.456 44.480 1.00 81.42 S ANISOU 411 SD MET A 82 12886 9318 8730 422 76 121 S ATOM 412 CE MET A 82 2.197 9.567 45.232 1.00 78.01 C ANISOU 412 CE MET A 82 12415 8935 8288 324 28 138 C ATOM 413 N GLY A 83 0.577 15.661 42.957 1.00 69.40 N ANISOU 413 N GLY A 83 11930 7357 7083 569 151 17 N ATOM 414 CA GLY A 83 1.084 17.018 43.118 1.00 69.60 C ANISOU 414 CA GLY A 83 12169 7223 7052 528 181 -30 C ATOM 415 C GLY A 83 0.122 18.027 43.707 1.00 73.63 C ANISOU 415 C GLY A 83 12841 7656 7479 672 239 -62 C ATOM 416 O GLY A 83 0.568 19.053 44.219 1.00 75.08 O ANISOU 416 O GLY A 83 13212 7708 7604 617 270 -116 O ATOM 417 N LEU A 84 -1.195 17.774 43.630 1.00 68.84 N ANISOU 417 N LEU A 84 12163 7133 6858 853 261 -37 N ATOM 418 CA LEU A 84 -2.184 18.707 44.175 1.00 69.37 C ANISOU 418 CA LEU A 84 12371 7149 6837 1021 319 -66 C ATOM 419 C LEU A 84 -2.729 18.266 45.529 1.00 73.40 C ANISOU 419 C LEU A 84 12814 7761 7314 1044 320 -99 C ATOM 420 O LEU A 84 -2.901 19.117 46.400 1.00 74.37 O ANISOU 420 O LEU A 84 13094 7804 7360 1085 357 -149 O ATOM 421 CB LEU A 84 -3.366 18.912 43.210 1.00 69.52 C ANISOU 421 CB LEU A 84 12368 7213 6836 1239 349 -27 C ATOM 422 CG LEU A 84 -3.136 19.792 41.982 1.00 74.68 C ANISOU 422 CG LEU A 84 13174 7728 7473 1297 376 5 C ATOM 423 CD1 LEU A 84 -4.167 19.496 40.927 1.00 74.94 C ANISOU 423 CD1 LEU A 84 13087 7885 7502 1486 376 50 C ATOM 424 CD2 LEU A 84 -3.183 21.275 42.332 1.00 78.28 C ANISOU 424 CD2 LEU A 84 13927 7983 7833 1379 448 -27 C ATOM 425 N ALA A 85 -3.038 16.959 45.699 1.00 68.81 N ANISOU 425 N ALA A 85 12016 7348 6782 1021 292 -74 N ATOM 426 CA ALA A 85 -3.667 16.449 46.913 1.00 68.64 C ANISOU 426 CA ALA A 85 11926 7430 6724 1050 307 -96 C ATOM 427 C ALA A 85 -2.738 15.683 47.869 1.00 72.33 C ANISOU 427 C ALA A 85 12345 7933 7206 888 267 -104 C ATOM 428 O ALA A 85 -3.124 15.528 49.034 1.00 72.66 O ANISOU 428 O ALA A 85 12388 8025 7193 911 287 -130 O ATOM 429 CB ALA A 85 -4.845 15.561 46.547 1.00 68.89 C ANISOU 429 CB ALA A 85 11769 7627 6778 1149 328 -71 C ATOM 430 N VAL A 86 -1.553 15.188 47.426 1.00 67.48 N ANISOU 430 N VAL A 86 11683 7306 6650 742 214 -82 N ATOM 431 CA VAL A 86 -0.739 14.411 48.374 1.00 66.65 C ANISOU 431 CA VAL A 86 11523 7264 6539 627 175 -86 C ATOM 432 C VAL A 86 0.606 15.117 48.704 1.00 71.59 C ANISOU 432 C VAL A 86 12258 7810 7133 493 134 -136 C ATOM 433 O VAL A 86 0.915 15.271 49.889 1.00 72.56 O ANISOU 433 O VAL A 86 12431 7953 7187 456 124 -182 O ATOM 434 CB VAL A 86 -0.531 12.900 47.995 1.00 68.96 C ANISOU 434 CB VAL A 86 11636 7663 6901 578 151 -24 C ATOM 435 CG1 VAL A 86 -1.589 12.395 47.014 1.00 68.14 C ANISOU 435 CG1 VAL A 86 11426 7614 6852 663 187 13 C ATOM 436 CG2 VAL A 86 0.879 12.575 47.502 1.00 68.24 C ANISOU 436 CG2 VAL A 86 11512 7562 6853 449 90 -9 C ATOM 437 N VAL A 87 1.387 15.532 47.689 1.00 67.43 N ANISOU 437 N VAL A 87 11763 7209 6648 414 115 -134 N ATOM 438 CA VAL A 87 2.710 16.134 47.878 1.00 67.78 C ANISOU 438 CA VAL A 87 11886 7202 6667 256 83 -192 C ATOM 439 C VAL A 87 2.631 17.453 48.714 1.00 74.53 C ANISOU 439 C VAL A 87 12944 7946 7430 248 123 -279 C ATOM 440 O VAL A 87 3.441 17.563 49.639 1.00 75.01 O ANISOU 440 O VAL A 87 13022 8044 7434 136 91 -343 O ATOM 441 CB VAL A 87 3.485 16.319 46.545 1.00 70.93 C ANISOU 441 CB VAL A 87 12280 7543 7128 169 71 -174 C ATOM 442 CG1 VAL A 87 4.889 16.856 46.789 1.00 71.24 C ANISOU 442 CG1 VAL A 87 12372 7560 7135 -20 43 -247 C ATOM 443 CG2 VAL A 87 3.564 15.003 45.774 1.00 69.59 C ANISOU 443 CG2 VAL A 87 11918 7481 7042 179 35 -96 C ATOM 444 N PRO A 88 1.678 18.412 48.498 1.00 72.37 N ANISOU 444 N PRO A 88 12821 7550 7125 372 192 -287 N ATOM 445 CA PRO A 88 1.667 19.631 49.337 1.00 73.63 C ANISOU 445 CA PRO A 88 13193 7591 7192 359 237 -374 C ATOM 446 C PRO A 88 1.394 19.363 50.820 1.00 77.80 C ANISOU 446 C PRO A 88 13699 8211 7650 382 225 -415 C ATOM 447 O PRO A 88 2.067 19.954 51.667 1.00 77.82 O ANISOU 447 O PRO A 88 13804 8181 7582 270 220 -502 O ATOM 448 CB PRO A 88 0.545 20.478 48.721 1.00 75.93 C ANISOU 448 CB PRO A 88 13628 7758 7465 542 314 -351 C ATOM 449 CG PRO A 88 0.385 19.957 47.345 1.00 79.34 C ANISOU 449 CG PRO A 88 13949 8218 7980 589 302 -268 C ATOM 450 CD PRO A 88 0.625 18.489 47.464 1.00 73.53 C ANISOU 450 CD PRO A 88 12965 7664 7308 534 232 -225 C ATOM 451 N PHE A 89 0.442 18.456 51.134 1.00 74.35 N ANISOU 451 N PHE A 89 13127 7895 7226 512 225 -358 N ATOM 452 CA PHE A 89 0.092 18.107 52.513 1.00 74.60 C ANISOU 452 CA PHE A 89 13136 8019 7190 546 223 -384 C ATOM 453 C PHE A 89 1.199 17.275 53.171 1.00 78.24 C ANISOU 453 C PHE A 89 13489 8599 7640 410 150 -393 C ATOM 454 O PHE A 89 1.340 17.304 54.394 1.00 78.42 O ANISOU 454 O PHE A 89 13542 8675 7579 393 140 -441 O ATOM 455 CB PHE A 89 -1.261 17.386 52.577 1.00 75.95 C ANISOU 455 CB PHE A 89 13198 8285 7376 710 261 -324 C ATOM 456 CG PHE A 89 -2.421 18.250 52.138 1.00 78.53 C ANISOU 456 CG PHE A 89 13623 8534 7681 877 330 -329 C ATOM 457 CD1 PHE A 89 -2.993 19.172 53.007 1.00 82.91 C ANISOU 457 CD1 PHE A 89 14331 9029 8141 967 382 -389 C ATOM 458 CD2 PHE A 89 -2.935 18.152 50.850 1.00 80.63 C ANISOU 458 CD2 PHE A 89 13829 8797 8011 960 343 -274 C ATOM 459 CE1 PHE A 89 -4.060 19.980 52.596 1.00 84.60 C ANISOU 459 CE1 PHE A 89 14640 9181 8322 1152 447 -390 C ATOM 460 CE2 PHE A 89 -4.008 18.953 50.442 1.00 84.15 C ANISOU 460 CE2 PHE A 89 14360 9195 8419 1144 403 -277 C ATOM 461 CZ PHE A 89 -4.563 19.862 51.318 1.00 83.34 C ANISOU 461 CZ PHE A 89 14412 9032 8219 1246 456 -333 C ATOM 462 N GLY A 90 1.986 16.583 52.352 1.00 74.29 N ANISOU 462 N GLY A 90 12869 8145 7213 325 101 -348 N ATOM 463 CA GLY A 90 3.134 15.810 52.805 1.00 74.21 C ANISOU 463 CA GLY A 90 12751 8256 7188 215 28 -351 C ATOM 464 C GLY A 90 4.273 16.733 53.188 1.00 79.99 C ANISOU 464 C GLY A 90 13577 8960 7855 61 -3 -457 C ATOM 465 O GLY A 90 4.944 16.506 54.198 1.00 80.56 O ANISOU 465 O GLY A 90 13616 9143 7849 3 -50 -505 O ATOM 466 N ALA A 91 4.465 17.804 52.390 1.00 77.32 N ANISOU 466 N ALA A 91 13364 8475 7540 -5 33 -500 N ATOM 467 CA ALA A 91 5.473 18.854 52.578 1.00 78.64 C ANISOU 467 CA ALA A 91 13651 8579 7649 -180 32 -615 C ATOM 468 C ALA A 91 5.189 19.653 53.847 1.00 83.97 C ANISOU 468 C ALA A 91 14474 9217 8212 -177 62 -711 C ATOM 469 O ALA A 91 6.120 20.010 54.569 1.00 84.18 O ANISOU 469 O ALA A 91 14522 9302 8162 -325 29 -816 O ATOM 470 CB ALA A 91 5.486 19.781 51.368 1.00 79.75 C ANISOU 470 CB ALA A 91 13925 8536 7839 -222 92 -619 C ATOM 471 N ALA A 92 3.892 19.913 54.120 1.00 81.38 N ANISOU 471 N ALA A 92 14238 8813 7871 -5 124 -681 N ATOM 472 CA ALA A 92 3.414 20.620 55.306 1.00 82.81 C ANISOU 472 CA ALA A 92 14563 8955 7947 37 162 -759 C ATOM 473 C ALA A 92 3.670 19.795 56.556 1.00 88.26 C ANISOU 473 C ALA A 92 15132 9834 8568 33 100 -772 C ATOM 474 O ALA A 92 3.930 20.369 57.609 1.00 89.48 O ANISOU 474 O ALA A 92 15382 10000 8618 -24 100 -873 O ATOM 475 CB ALA A 92 1.931 20.922 55.175 1.00 83.45 C ANISOU 475 CB ALA A 92 14731 8943 8034 247 240 -709 C ATOM 476 N HIS A 93 3.622 18.453 56.438 1.00 84.73 N ANISOU 476 N HIS A 93 14490 9533 8172 93 52 -671 N ATOM 477 CA HIS A 93 3.864 17.536 57.552 1.00 85.32 C ANISOU 477 CA HIS A 93 14457 9786 8177 114 0 -660 C ATOM 478 C HIS A 93 5.350 17.499 57.936 1.00 89.51 C ANISOU 478 C HIS A 93 14927 10437 8644 -49 -84 -737 C ATOM 479 O HIS A 93 5.664 17.286 59.107 1.00 89.96 O ANISOU 479 O HIS A 93 14966 10622 8593 -51 -123 -782 O ATOM 480 CB HIS A 93 3.363 16.121 57.219 1.00 85.25 C ANISOU 480 CB HIS A 93 14286 9867 8238 224 -6 -527 C ATOM 481 CG HIS A 93 3.310 15.218 58.411 1.00 89.40 C ANISOU 481 CG HIS A 93 14749 10539 8681 286 -27 -499 C ATOM 482 ND1 HIS A 93 4.403 14.461 58.790 1.00 91.67 N ANISOU 482 ND1 HIS A 93 14934 10975 8922 233 -105 -492 N ATOM 483 CD2 HIS A 93 2.309 15.013 59.297 1.00 91.89 C ANISOU 483 CD2 HIS A 93 15100 10872 8941 401 26 -480 C ATOM 484 CE1 HIS A 93 4.028 13.809 59.879 1.00 91.67 C ANISOU 484 CE1 HIS A 93 14924 11066 8839 326 -96 -460 C ATOM 485 NE2 HIS A 93 2.775 14.108 60.221 1.00 92.09 N ANISOU 485 NE2 HIS A 93 15059 11044 8886 418 -15 -453 N ATOM 486 N ILE A 94 6.255 17.706 56.961 1.00 85.50 N ANISOU 486 N ILE A 94 14382 9909 8196 -180 -112 -757 N ATOM 487 CA ILE A 94 7.702 17.677 57.191 1.00 86.07 C ANISOU 487 CA ILE A 94 14369 10123 8209 -343 -191 -840 C ATOM 488 C ILE A 94 8.168 18.987 57.849 1.00 92.28 C ANISOU 488 C ILE A 94 15306 10861 8895 -496 -173 -1006 C ATOM 489 O ILE A 94 8.829 18.936 58.891 1.00 93.11 O ANISOU 489 O ILE A 94 15367 11127 8882 -556 -231 -1091 O ATOM 490 CB ILE A 94 8.464 17.366 55.871 1.00 88.22 C ANISOU 490 CB ILE A 94 14535 10402 8582 -430 -217 -800 C ATOM 491 CG1 ILE A 94 8.170 15.921 55.422 1.00 86.98 C ANISOU 491 CG1 ILE A 94 14218 10329 8501 -290 -244 -651 C ATOM 492 CG2 ILE A 94 9.983 17.601 56.013 1.00 90.03 C ANISOU 492 CG2 ILE A 94 14685 10778 8746 -625 -286 -915 C ATOM 493 CD1 ILE A 94 8.206 15.683 53.968 1.00 93.88 C ANISOU 493 CD1 ILE A 94 15041 11129 9501 -302 -229 -579 C ATOM 494 N LEU A 95 7.824 20.143 57.244 1.00 89.39 N ANISOU 494 N LEU A 95 15126 10275 8564 -554 -89 -1053 N ATOM 495 CA LEU A 95 8.214 21.475 57.716 1.00 91.16 C ANISOU 495 CA LEU A 95 15535 10401 8700 -715 -45 -1214 C ATOM 496 C LEU A 95 7.642 21.798 59.112 1.00 95.54 C ANISOU 496 C LEU A 95 16191 10973 9137 -643 -30 -1278 C ATOM 497 O LEU A 95 8.383 22.300 59.962 1.00 96.75 O ANISOU 497 O LEU A 95 16376 11206 9176 -790 -56 -1422 O ATOM 498 CB LEU A 95 7.797 22.568 56.705 1.00 91.66 C ANISOU 498 CB LEU A 95 15811 10190 8826 -746 62 -1222 C ATOM 499 CG LEU A 95 8.369 22.481 55.274 1.00 95.71 C ANISOU 499 CG LEU A 95 16269 10653 9444 -835 66 -1173 C ATOM 500 CD1 LEU A 95 7.676 23.465 54.356 1.00 96.00 C ANISOU 500 CD1 LEU A 95 16535 10411 9529 -792 181 -1149 C ATOM 501 CD2 LEU A 95 9.875 22.718 55.242 1.00 99.73 C ANISOU 501 CD2 LEU A 95 16709 11272 9912 -1103 25 -1298 C ATOM 502 N MET A 96 6.347 21.492 59.352 1.00 91.06 N ANISOU 502 N MET A 96 15660 10349 8590 -425 11 -1181 N ATOM 503 CA MET A 96 5.669 21.745 60.635 1.00 91.65 C ANISOU 503 CA MET A 96 15829 10438 8558 -332 36 -1227 C ATOM 504 C MET A 96 5.937 20.645 61.669 1.00 95.11 C ANISOU 504 C MET A 96 16094 11122 8920 -277 -50 -1199 C ATOM 505 O MET A 96 5.612 20.832 62.845 1.00 95.51 O ANISOU 505 O MET A 96 16210 11220 8860 -229 -42 -1253 O ATOM 506 CB MET A 96 4.154 21.906 60.438 1.00 93.34 C ANISOU 506 CB MET A 96 16146 10504 8816 -120 125 -1141 C ATOM 507 CG MET A 96 3.770 23.233 59.841 1.00 97.68 C ANISOU 507 CG MET A 96 16933 10802 9378 -133 223 -1194 C ATOM 508 SD MET A 96 2.121 23.235 59.112 1.00100.68 S ANISOU 508 SD MET A 96 17366 11052 9836 135 309 -1066 S ATOM 509 CE MET A 96 2.419 24.322 57.721 1.00 98.00 C ANISOU 509 CE MET A 96 17209 10470 9557 57 378 -1084 C ATOM 510 N LYS A 97 6.502 19.494 61.226 1.00 90.43 N ANISOU 510 N LYS A 97 15297 10682 8382 -269 -124 -1108 N ATOM 511 CA LYS A 97 6.856 18.312 62.034 1.00 89.96 C ANISOU 511 CA LYS A 97 15076 10854 8253 -198 -202 -1056 C ATOM 512 C LYS A 97 5.631 17.734 62.797 1.00 93.09 C ANISOU 512 C LYS A 97 15496 11253 8621 1 -156 -967 C ATOM 513 O LYS A 97 5.793 16.952 63.736 1.00 92.64 O ANISOU 513 O LYS A 97 15365 11361 8471 70 -199 -940 O ATOM 514 CB LYS A 97 8.033 18.616 62.980 1.00 94.17 C ANISOU 514 CB LYS A 97 15576 11565 8638 -336 -280 -1200 C ATOM 515 CG LYS A 97 9.335 18.821 62.217 1.00110.38 C ANISOU 515 CG LYS A 97 17538 13686 10717 -528 -336 -1271 C ATOM 516 CD LYS A 97 10.479 19.267 63.094 1.00125.13 C ANISOU 516 CD LYS A 97 19369 15744 12432 -690 -406 -1441 C ATOM 517 CE LYS A 97 11.708 19.512 62.256 1.00138.93 C ANISOU 517 CE LYS A 97 21017 17559 14210 -895 -446 -1519 C ATOM 518 NZ LYS A 97 12.917 19.696 63.097 1.00150.33 N ANISOU 518 NZ LYS A 97 22359 19265 15495 -1043 -533 -1682 N ATOM 519 N MET A 98 4.412 18.082 62.331 1.00 89.35 N ANISOU 519 N MET A 98 15119 10606 8225 99 -65 -917 N ATOM 520 CA MET A 98 3.116 17.649 62.863 1.00 88.90 C ANISOU 520 CA MET A 98 15082 10538 8157 275 0 -841 C ATOM 521 C MET A 98 2.011 17.806 61.794 1.00 90.02 C ANISOU 521 C MET A 98 15252 10528 8423 367 80 -768 C ATOM 522 O MET A 98 2.190 18.543 60.819 1.00 89.48 O ANISOU 522 O MET A 98 15245 10331 8423 304 94 -795 O ATOM 523 CB MET A 98 2.755 18.423 64.151 1.00 93.18 C ANISOU 523 CB MET A 98 15766 11075 8564 299 32 -942 C ATOM 524 CG MET A 98 2.439 19.900 63.932 1.00 98.64 C ANISOU 524 CG MET A 98 16654 11574 9250 256 97 -1047 C ATOM 525 SD MET A 98 2.498 20.883 65.452 1.00106.10 S ANISOU 525 SD MET A 98 17770 12526 10017 221 113 -1206 S ATOM 526 CE MET A 98 0.982 20.364 66.249 1.00102.65 C ANISOU 526 CE MET A 98 17338 12120 9543 451 187 -1120 C ATOM 527 N TRP A 99 0.873 17.119 61.997 1.00 84.56 N ANISOU 527 N TRP A 99 14516 9864 7748 515 135 -680 N ATOM 528 CA TRP A 99 -0.291 17.142 61.107 1.00 82.82 C ANISOU 528 CA TRP A 99 14290 9554 7624 623 209 -616 C ATOM 529 C TRP A 99 -1.334 18.123 61.650 1.00 86.97 C ANISOU 529 C TRP A 99 14962 9996 8085 728 289 -675 C ATOM 530 O TRP A 99 -1.803 17.966 62.779 1.00 87.10 O ANISOU 530 O TRP A 99 15001 10083 8010 792 316 -690 O ATOM 531 CB TRP A 99 -0.872 15.729 60.956 1.00 79.97 C ANISOU 531 CB TRP A 99 13773 9295 7316 699 228 -497 C ATOM 532 CG TRP A 99 -1.948 15.608 59.922 1.00 79.79 C ANISOU 532 CG TRP A 99 13700 9222 7393 786 290 -438 C ATOM 533 CD1 TRP A 99 -3.294 15.581 60.140 1.00 82.78 C ANISOU 533 CD1 TRP A 99 14074 9618 7760 913 374 -423 C ATOM 534 CD2 TRP A 99 -1.766 15.452 58.509 1.00 78.46 C ANISOU 534 CD2 TRP A 99 13463 9006 7344 755 272 -393 C ATOM 535 NE1 TRP A 99 -3.963 15.428 58.948 1.00 81.36 N ANISOU 535 NE1 TRP A 99 13817 9416 7678 963 404 -376 N ATOM 536 CE2 TRP A 99 -3.049 15.343 57.930 1.00 81.93 C ANISOU 536 CE2 TRP A 99 13855 9441 7832 870 343 -354 C ATOM 537 CE3 TRP A 99 -0.639 15.395 57.670 1.00 79.08 C ANISOU 537 CE3 TRP A 99 13505 9057 7484 641 204 -386 C ATOM 538 CZ2 TRP A 99 -3.237 15.192 56.551 1.00 80.37 C ANISOU 538 CZ2 TRP A 99 13583 9213 7739 879 343 -309 C ATOM 539 CZ3 TRP A 99 -0.826 15.247 56.305 1.00 79.55 C ANISOU 539 CZ3 TRP A 99 13501 9070 7652 648 210 -335 C ATOM 540 CH2 TRP A 99 -2.112 15.147 55.758 1.00 79.90 C ANISOU 540 CH2 TRP A 99 13506 9110 7740 768 277 -297 C ATOM 541 N THR A 100 -1.675 19.144 60.850 1.00 83.12 N ANISOU 541 N THR A 100 14586 9359 7637 756 331 -706 N ATOM 542 CA THR A 100 -2.608 20.202 61.244 1.00 83.88 C ANISOU 542 CA THR A 100 14846 9356 7667 874 411 -766 C ATOM 543 C THR A 100 -3.873 20.197 60.367 1.00 87.27 C ANISOU 543 C THR A 100 15238 9758 8162 1044 478 -699 C ATOM 544 O THR A 100 -4.445 21.264 60.109 1.00 87.57 O ANISOU 544 O THR A 100 15428 9673 8173 1145 538 -738 O ATOM 545 CB THR A 100 -1.885 21.556 61.165 1.00 92.27 C ANISOU 545 CB THR A 100 16118 10253 8687 774 416 -875 C ATOM 546 OG1 THR A 100 -1.312 21.697 59.864 1.00 91.81 O ANISOU 546 OG1 THR A 100 16049 10109 8726 695 395 -847 O ATOM 547 CG2 THR A 100 -0.804 21.712 62.229 1.00 91.46 C ANISOU 547 CG2 THR A 100 16058 10205 8488 617 361 -974 C ATOM 548 N PHE A 101 -4.326 18.997 59.934 1.00 82.78 N ANISOU 548 N PHE A 101 14472 9314 7668 1080 472 -603 N ATOM 549 CA PHE A 101 -5.493 18.857 59.056 1.00 82.23 C ANISOU 549 CA PHE A 101 14324 9264 7656 1224 526 -549 C ATOM 550 C PHE A 101 -6.542 17.849 59.588 1.00 87.36 C ANISOU 550 C PHE A 101 14821 10077 8293 1307 575 -504 C ATOM 551 O PHE A 101 -7.464 17.481 58.852 1.00 86.39 O ANISOU 551 O PHE A 101 14583 10020 8222 1397 614 -462 O ATOM 552 CB PHE A 101 -5.047 18.463 57.632 1.00 82.56 C ANISOU 552 CB PHE A 101 14271 9282 7816 1165 484 -487 C ATOM 553 CG PHE A 101 -3.992 19.358 57.020 1.00 84.12 C ANISOU 553 CG PHE A 101 14605 9324 8031 1062 447 -526 C ATOM 554 CD1 PHE A 101 -4.336 20.575 56.440 1.00 87.80 C ANISOU 554 CD1 PHE A 101 15241 9641 8480 1151 495 -558 C ATOM 555 CD2 PHE A 101 -2.651 18.988 57.030 1.00 85.41 C ANISOU 555 CD2 PHE A 101 14735 9496 8220 880 373 -532 C ATOM 556 CE1 PHE A 101 -3.356 21.411 55.892 1.00 88.84 C ANISOU 556 CE1 PHE A 101 15520 9614 8621 1036 480 -597 C ATOM 557 CE2 PHE A 101 -1.673 19.822 56.476 1.00 88.42 C ANISOU 557 CE2 PHE A 101 15236 9747 8612 763 350 -580 C ATOM 558 CZ PHE A 101 -2.032 21.029 55.915 1.00 87.30 C ANISOU 558 CZ PHE A 101 15276 9439 8457 830 409 -613 C ATOM 559 N GLY A 102 -6.418 17.449 60.857 1.00 85.55 N ANISOU 559 N GLY A 102 14598 9919 7985 1275 579 -520 N ATOM 560 CA GLY A 102 -7.349 16.524 61.498 1.00 85.82 C ANISOU 560 CA GLY A 102 14518 10097 7993 1333 641 -484 C ATOM 561 C GLY A 102 -7.165 15.064 61.132 1.00 89.90 C ANISOU 561 C GLY A 102 14868 10706 8584 1250 630 -397 C ATOM 562 O GLY A 102 -6.411 14.732 60.212 1.00 88.13 O ANISOU 562 O GLY A 102 14593 10446 8448 1167 570 -359 O ATOM 563 N ASN A 103 -7.866 14.177 61.856 1.00 88.24 N ANISOU 563 N ASN A 103 14582 10611 8336 1271 698 -367 N ATOM 564 CA ASN A 103 -7.782 12.732 61.648 1.00 87.78 C ANISOU 564 CA ASN A 103 14395 10626 8331 1194 714 -286 C ATOM 565 C ASN A 103 -8.551 12.265 60.406 1.00 92.33 C ANISOU 565 C ASN A 103 14826 11243 9011 1205 752 -256 C ATOM 566 O ASN A 103 -8.169 11.247 59.823 1.00 91.14 O ANISOU 566 O ASN A 103 14589 11105 8933 1119 741 -195 O ATOM 567 CB ASN A 103 -8.260 11.971 62.886 1.00 89.11 C ANISOU 567 CB ASN A 103 14562 10885 8410 1202 792 -267 C ATOM 568 CG ASN A 103 -7.223 11.862 63.988 1.00112.27 C ANISOU 568 CG ASN A 103 17600 13809 11251 1161 739 -263 C ATOM 569 OD1 ASN A 103 -6.006 11.897 63.758 1.00103.04 O ANISOU 569 OD1 ASN A 103 16458 12594 10100 1094 642 -255 O ATOM 570 ND2 ASN A 103 -7.687 11.692 65.218 1.00106.31 N ANISOU 570 ND2 ASN A 103 16894 13116 10386 1203 804 -271 N ATOM 571 N PHE A 104 -9.612 12.997 59.993 1.00 90.03 N ANISOU 571 N PHE A 104 14508 10981 8717 1319 798 -302 N ATOM 572 CA PHE A 104 -10.402 12.629 58.815 1.00 89.50 C ANISOU 572 CA PHE A 104 14290 10987 8731 1342 829 -288 C ATOM 573 C PHE A 104 -9.606 12.840 57.521 1.00 91.10 C ANISOU 573 C PHE A 104 14487 11097 9028 1302 744 -263 C ATOM 574 O PHE A 104 -9.587 11.938 56.682 1.00 90.00 O ANISOU 574 O PHE A 104 14225 10999 8971 1231 744 -221 O ATOM 575 CB PHE A 104 -11.744 13.387 58.755 1.00 92.73 C ANISOU 575 CB PHE A 104 14663 11483 9089 1503 895 -347 C ATOM 576 CG PHE A 104 -12.502 13.157 57.464 1.00 94.50 C ANISOU 576 CG PHE A 104 14724 11801 9380 1544 912 -346 C ATOM 577 CD1 PHE A 104 -13.230 11.988 57.263 1.00 97.71 C ANISOU 577 CD1 PHE A 104 14950 12358 9818 1474 982 -335 C ATOM 578 CD2 PHE A 104 -12.454 14.092 56.434 1.00 96.82 C ANISOU 578 CD2 PHE A 104 15053 12034 9699 1645 861 -358 C ATOM 579 CE1 PHE A 104 -13.904 11.765 56.059 1.00 98.55 C ANISOU 579 CE1 PHE A 104 14893 12572 9977 1500 992 -348 C ATOM 580 CE2 PHE A 104 -13.123 13.864 55.230 1.00 99.42 C ANISOU 580 CE2 PHE A 104 15228 12469 10079 1692 868 -357 C ATOM 581 CZ PHE A 104 -13.848 12.705 55.052 1.00 97.43 C ANISOU 581 CZ PHE A 104 14777 12387 9855 1618 929 -358 C ATOM 582 N TRP A 105 -8.978 14.025 57.345 1.00 86.72 N ANISOU 582 N TRP A 105 14074 10416 8459 1339 684 -294 N ATOM 583 CA TRP A 105 -8.189 14.311 56.148 1.00 85.16 C ANISOU 583 CA TRP A 105 13891 10123 8342 1295 612 -273 C ATOM 584 C TRP A 105 -6.898 13.478 56.136 1.00 86.04 C ANISOU 584 C TRP A 105 13986 10202 8504 1136 547 -226 C ATOM 585 O TRP A 105 -6.404 13.175 55.055 1.00 84.51 O ANISOU 585 O TRP A 105 13733 9981 8396 1079 505 -190 O ATOM 586 CB TRP A 105 -7.886 15.814 55.990 1.00 84.78 C ANISOU 586 CB TRP A 105 14022 9934 8255 1365 587 -322 C ATOM 587 CG TRP A 105 -7.060 16.142 54.771 1.00 85.22 C ANISOU 587 CG TRP A 105 14107 9884 8387 1310 527 -301 C ATOM 588 CD1 TRP A 105 -5.769 16.580 54.754 1.00 87.95 C ANISOU 588 CD1 TRP A 105 14567 10108 8741 1193 467 -314 C ATOM 589 CD2 TRP A 105 -7.428 15.931 53.399 1.00 84.39 C ANISOU 589 CD2 TRP A 105 13899 9807 8357 1351 524 -263 C ATOM 590 NE1 TRP A 105 -5.327 16.710 53.458 1.00 86.60 N ANISOU 590 NE1 TRP A 105 14382 9874 8647 1162 433 -285 N ATOM 591 CE2 TRP A 105 -6.324 16.317 52.605 1.00 87.72 C ANISOU 591 CE2 TRP A 105 14397 10103 8830 1264 464 -250 C ATOM 592 CE3 TRP A 105 -8.596 15.480 52.760 1.00 85.60 C ANISOU 592 CE3 TRP A 105 13898 10095 8531 1451 566 -249 C ATOM 593 CZ2 TRP A 105 -6.352 16.264 51.208 1.00 86.55 C ANISOU 593 CZ2 TRP A 105 14188 9945 8752 1284 447 -213 C ATOM 594 CZ3 TRP A 105 -8.622 15.433 51.375 1.00 86.61 C ANISOU 594 CZ3 TRP A 105 13958 10225 8724 1472 542 -220 C ATOM 595 CH2 TRP A 105 -7.510 15.818 50.614 1.00 86.72 C ANISOU 595 CH2 TRP A 105 14062 10099 8788 1394 484 -197 C ATOM 596 N CYS A 106 -6.389 13.072 57.320 1.00 81.47 N ANISOU 596 N CYS A 106 13451 9641 7864 1078 542 -224 N ATOM 597 CA CYS A 106 -5.191 12.238 57.458 1.00 79.68 C ANISOU 597 CA CYS A 106 13206 9411 7658 960 482 -178 C ATOM 598 C CYS A 106 -5.376 10.907 56.720 1.00 82.14 C ANISOU 598 C CYS A 106 13375 9781 8054 913 508 -107 C ATOM 599 O CYS A 106 -4.587 10.594 55.825 1.00 80.80 O ANISOU 599 O CYS A 106 13166 9577 7959 847 452 -74 O ATOM 600 CB CYS A 106 -4.855 12.019 58.930 1.00 80.08 C ANISOU 600 CB CYS A 106 13326 9500 7602 948 485 -188 C ATOM 601 SG CYS A 106 -3.596 10.752 59.228 1.00 83.02 S ANISOU 601 SG CYS A 106 13660 9913 7971 852 430 -118 S ATOM 602 N GLU A 107 -6.439 10.155 57.074 1.00 78.83 N ANISOU 602 N GLU A 107 12884 9449 7618 941 601 -91 N ATOM 603 CA GLU A 107 -6.779 8.856 56.486 1.00 77.97 C ANISOU 603 CA GLU A 107 12654 9394 7576 883 653 -38 C ATOM 604 C GLU A 107 -7.103 9.008 54.994 1.00 81.48 C ANISOU 604 C GLU A 107 13000 9841 8117 887 637 -45 C ATOM 605 O GLU A 107 -6.628 8.209 54.182 1.00 79.98 O ANISOU 605 O GLU A 107 12747 9638 8003 812 618 -1 O ATOM 606 CB GLU A 107 -7.950 8.189 57.243 1.00 79.97 C ANISOU 606 CB GLU A 107 12863 9744 7778 896 775 -42 C ATOM 607 CG GLU A 107 -7.709 8.059 58.742 1.00 90.74 C ANISOU 607 CG GLU A 107 14334 11111 9033 907 799 -33 C ATOM 608 CD GLU A 107 -8.404 6.924 59.469 1.00106.59 C ANISOU 608 CD GLU A 107 16319 13184 10995 872 922 0 C ATOM 609 OE1 GLU A 107 -7.743 5.885 59.697 1.00106.03 O ANISOU 609 OE1 GLU A 107 16284 13084 10921 811 934 69 O ATOM 610 OE2 GLU A 107 -9.569 7.103 59.894 1.00 90.51 O ANISOU 610 OE2 GLU A 107 14247 11228 8915 911 1013 -44 O ATOM 611 N PHE A 108 -7.852 10.069 54.637 1.00 78.81 N ANISOU 611 N PHE A 108 12662 9515 7766 987 642 -98 N ATOM 612 CA PHE A 108 -8.259 10.380 53.266 1.00 78.49 C ANISOU 612 CA PHE A 108 12540 9490 7792 1028 627 -108 C ATOM 613 C PHE A 108 -7.054 10.717 52.360 1.00 80.51 C ANISOU 613 C PHE A 108 12845 9632 8112 979 533 -81 C ATOM 614 O PHE A 108 -7.038 10.300 51.200 1.00 79.42 O ANISOU 614 O PHE A 108 12615 9511 8050 950 518 -59 O ATOM 615 CB PHE A 108 -9.277 11.534 53.258 1.00 81.63 C ANISOU 615 CB PHE A 108 12958 9924 8132 1184 655 -167 C ATOM 616 CG PHE A 108 -10.250 11.485 52.104 1.00 84.00 C ANISOU 616 CG PHE A 108 13116 10333 8466 1254 680 -184 C ATOM 617 CD1 PHE A 108 -11.337 10.617 52.123 1.00 88.33 C ANISOU 617 CD1 PHE A 108 13501 11050 9011 1239 761 -205 C ATOM 618 CD2 PHE A 108 -10.083 12.307 50.997 1.00 86.40 C ANISOU 618 CD2 PHE A 108 13450 10581 8796 1332 627 -184 C ATOM 619 CE1 PHE A 108 -12.236 10.569 51.051 1.00 89.65 C ANISOU 619 CE1 PHE A 108 13515 11351 9197 1300 779 -235 C ATOM 620 CE2 PHE A 108 -10.983 12.261 49.927 1.00 89.74 C ANISOU 620 CE2 PHE A 108 13734 11127 9234 1414 644 -201 C ATOM 621 CZ PHE A 108 -12.050 11.388 49.959 1.00 88.43 C ANISOU 621 CZ PHE A 108 13386 11151 9062 1398 714 -231 C ATOM 622 N TRP A 109 -6.061 11.460 52.892 1.00 76.29 N ANISOU 622 N TRP A 109 12450 8994 7542 959 474 -92 N ATOM 623 CA TRP A 109 -4.833 11.868 52.201 1.00 75.03 C ANISOU 623 CA TRP A 109 12347 8733 7428 892 393 -81 C ATOM 624 C TRP A 109 -4.003 10.631 51.883 1.00 77.60 C ANISOU 624 C TRP A 109 12589 9082 7816 781 362 -23 C ATOM 625 O TRP A 109 -3.527 10.484 50.757 1.00 77.00 O ANISOU 625 O TRP A 109 12466 8977 7813 740 325 2 O ATOM 626 CB TRP A 109 -4.051 12.866 53.075 1.00 74.31 C ANISOU 626 CB TRP A 109 12415 8556 7265 875 355 -126 C ATOM 627 CG TRP A 109 -2.634 13.133 52.668 1.00 74.75 C ANISOU 627 CG TRP A 109 12519 8535 7349 766 277 -127 C ATOM 628 CD1 TRP A 109 -2.207 14.017 51.725 1.00 77.54 C ANISOU 628 CD1 TRP A 109 12937 8788 7735 750 251 -144 C ATOM 629 CD2 TRP A 109 -1.453 12.601 53.285 1.00 74.63 C ANISOU 629 CD2 TRP A 109 12499 8546 7313 663 222 -119 C ATOM 630 NE1 TRP A 109 -0.833 14.046 51.692 1.00 76.65 N ANISOU 630 NE1 TRP A 109 12848 8643 7631 622 186 -154 N ATOM 631 CE2 TRP A 109 -0.343 13.179 52.631 1.00 78.18 C ANISOU 631 CE2 TRP A 109 12989 8925 7790 574 161 -140 C ATOM 632 CE3 TRP A 109 -1.223 11.668 54.313 1.00 76.10 C ANISOU 632 CE3 TRP A 109 12650 8815 7449 646 221 -93 C ATOM 633 CZ2 TRP A 109 0.978 12.851 52.963 1.00 77.61 C ANISOU 633 CZ2 TRP A 109 12899 8891 7700 468 94 -146 C ATOM 634 CZ3 TRP A 109 0.086 11.346 54.644 1.00 77.51 C ANISOU 634 CZ3 TRP A 109 12825 9023 7603 563 150 -90 C ATOM 635 CH2 TRP A 109 1.169 11.931 53.972 1.00 78.03 C ANISOU 635 CH2 TRP A 109 12906 9043 7697 475 84 -120 C ATOM 636 N THR A 110 -3.872 9.730 52.869 1.00 73.37 N ANISOU 636 N THR A 110 12042 8595 7241 746 386 2 N ATOM 637 CA THR A 110 -3.150 8.465 52.759 1.00 72.17 C ANISOU 637 CA THR A 110 11834 8463 7124 668 374 64 C ATOM 638 C THR A 110 -3.844 7.556 51.730 1.00 74.21 C ANISOU 638 C THR A 110 11972 8761 7465 650 427 93 C ATOM 639 O THR A 110 -3.153 6.912 50.944 1.00 73.22 O ANISOU 639 O THR A 110 11802 8617 7403 592 395 133 O ATOM 640 CB THR A 110 -3.048 7.802 54.153 1.00 79.17 C ANISOU 640 CB THR A 110 12766 9389 7924 669 407 85 C ATOM 641 OG1 THR A 110 -2.260 8.628 55.017 1.00 78.83 O ANISOU 641 OG1 THR A 110 12823 9326 7803 674 343 48 O ATOM 642 CG2 THR A 110 -2.448 6.414 54.102 1.00 74.80 C ANISOU 642 CG2 THR A 110 12178 8851 7391 620 416 158 C ATOM 643 N SER A 111 -5.200 7.502 51.745 1.00 70.08 N ANISOU 643 N SER A 111 11390 8305 6932 695 508 66 N ATOM 644 CA SER A 111 -6.007 6.688 50.826 1.00 68.65 C ANISOU 644 CA SER A 111 11081 8190 6813 666 568 69 C ATOM 645 C SER A 111 -5.791 7.108 49.369 1.00 70.42 C ANISOU 645 C SER A 111 11251 8393 7112 673 509 65 C ATOM 646 O SER A 111 -5.658 6.238 48.505 1.00 69.78 O ANISOU 646 O SER A 111 11091 8326 7098 608 517 90 O ATOM 647 CB SER A 111 -7.487 6.785 51.174 1.00 72.12 C ANISOU 647 CB SER A 111 11456 8736 7209 719 659 19 C ATOM 648 OG SER A 111 -7.745 6.401 52.512 1.00 78.99 O ANISOU 648 OG SER A 111 12380 9628 8006 711 724 23 O ATOM 649 N ILE A 112 -5.744 8.436 49.107 1.00 65.49 N ANISOU 649 N ILE A 112 10687 7727 6470 754 458 34 N ATOM 650 CA ILE A 112 -5.516 9.019 47.779 1.00 64.19 C ANISOU 650 CA ILE A 112 10505 7526 6357 779 407 34 C ATOM 651 C ILE A 112 -4.092 8.665 47.318 1.00 66.04 C ANISOU 651 C ILE A 112 10764 7680 6647 680 339 78 C ATOM 652 O ILE A 112 -3.913 8.254 46.172 1.00 65.33 O ANISOU 652 O ILE A 112 10602 7597 6625 647 323 99 O ATOM 653 CB ILE A 112 -5.781 10.557 47.781 1.00 67.76 C ANISOU 653 CB ILE A 112 11063 7926 6757 897 388 -4 C ATOM 654 CG1 ILE A 112 -7.287 10.861 47.847 1.00 69.19 C ANISOU 654 CG1 ILE A 112 11181 8221 6888 1025 452 -47 C ATOM 655 CG2 ILE A 112 -5.151 11.253 46.570 1.00 67.69 C ANISOU 655 CG2 ILE A 112 11097 7832 6789 905 332 9 C ATOM 656 CD1 ILE A 112 -7.632 12.270 48.375 1.00 79.32 C ANISOU 656 CD1 ILE A 112 12601 9448 8087 1161 458 -86 C ATOM 657 N ASP A 113 -3.102 8.805 48.224 1.00 61.73 N ANISOU 657 N ASP A 113 10312 7078 6065 636 301 87 N ATOM 658 CA ASP A 113 -1.684 8.519 47.992 1.00 60.79 C ANISOU 658 CA ASP A 113 10209 6912 5976 551 235 118 C ATOM 659 C ASP A 113 -1.493 7.096 47.473 1.00 65.50 C ANISOU 659 C ASP A 113 10708 7546 6631 495 253 170 C ATOM 660 O ASP A 113 -0.841 6.901 46.444 1.00 64.68 O ANISOU 660 O ASP A 113 10565 7421 6590 454 214 191 O ATOM 661 CB ASP A 113 -0.894 8.722 49.296 1.00 62.65 C ANISOU 661 CB ASP A 113 10533 7136 6136 528 204 107 C ATOM 662 CG ASP A 113 0.608 8.833 49.150 1.00 68.75 C ANISOU 662 CG ASP A 113 11325 7882 6913 451 124 112 C ATOM 663 OD1 ASP A 113 1.186 8.091 48.328 1.00 67.23 O ANISOU 663 OD1 ASP A 113 11061 7701 6782 408 102 153 O ATOM 664 OD2 ASP A 113 1.213 9.612 49.902 1.00 74.92 O ANISOU 664 OD2 ASP A 113 12190 8646 7630 430 86 68 O ATOM 665 N VAL A 114 -2.099 6.118 48.166 1.00 63.07 N ANISOU 665 N VAL A 114 10375 7289 6301 494 323 187 N ATOM 666 CA VAL A 114 -2.050 4.699 47.827 1.00 63.06 C ANISOU 666 CA VAL A 114 10312 7305 6341 440 368 233 C ATOM 667 C VAL A 114 -2.757 4.477 46.480 1.00 66.80 C ANISOU 667 C VAL A 114 10683 7809 6890 424 394 216 C ATOM 668 O VAL A 114 -2.209 3.771 45.635 1.00 66.47 O ANISOU 668 O VAL A 114 10600 7750 6906 374 381 246 O ATOM 669 CB VAL A 114 -2.635 3.817 48.970 1.00 68.26 C ANISOU 669 CB VAL A 114 10999 7994 6942 438 459 249 C ATOM 670 CG1 VAL A 114 -2.699 2.341 48.572 1.00 68.13 C ANISOU 670 CG1 VAL A 114 10949 7973 6965 375 532 291 C ATOM 671 CG2 VAL A 114 -1.829 3.983 50.261 1.00 68.51 C ANISOU 671 CG2 VAL A 114 11133 8009 6888 465 423 269 C ATOM 672 N LEU A 115 -3.928 5.126 46.263 1.00 63.20 N ANISOU 672 N LEU A 115 10182 7409 6422 477 425 165 N ATOM 673 CA LEU A 115 -4.725 5.031 45.031 1.00 62.66 C ANISOU 673 CA LEU A 115 10001 7407 6402 482 446 136 C ATOM 674 C LEU A 115 -3.926 5.461 43.800 1.00 65.45 C ANISOU 674 C LEU A 115 10349 7710 6811 481 367 154 C ATOM 675 O LEU A 115 -4.045 4.820 42.759 1.00 64.33 O ANISOU 675 O LEU A 115 10119 7600 6722 441 377 155 O ATOM 676 CB LEU A 115 -6.018 5.878 45.159 1.00 63.51 C ANISOU 676 CB LEU A 115 10069 7601 6459 579 477 77 C ATOM 677 CG LEU A 115 -6.779 6.287 43.878 1.00 68.05 C ANISOU 677 CG LEU A 115 10541 8261 7054 641 468 39 C ATOM 678 CD1 LEU A 115 -7.488 5.103 43.237 1.00 68.01 C ANISOU 678 CD1 LEU A 115 10389 8368 7084 560 532 12 C ATOM 679 CD2 LEU A 115 -7.767 7.397 44.166 1.00 70.85 C ANISOU 679 CD2 LEU A 115 10901 8682 7337 783 480 -8 C ATOM 680 N CYS A 116 -3.127 6.535 43.924 1.00 62.63 N ANISOU 680 N CYS A 116 10088 7273 6435 515 298 160 N ATOM 681 CA CYS A 116 -2.325 7.108 42.845 1.00 62.09 C ANISOU 681 CA CYS A 116 10038 7145 6407 508 233 174 C ATOM 682 C CYS A 116 -1.176 6.201 42.443 1.00 65.82 C ANISOU 682 C CYS A 116 10486 7589 6933 416 202 218 C ATOM 683 O CYS A 116 -0.910 6.078 41.252 1.00 65.26 O ANISOU 683 O CYS A 116 10367 7515 6914 397 181 230 O ATOM 684 CB CYS A 116 -1.814 8.490 43.232 1.00 62.77 C ANISOU 684 CB CYS A 116 10253 7148 6449 545 189 158 C ATOM 685 SG CYS A 116 -3.091 9.771 43.268 1.00 67.54 S ANISOU 685 SG CYS A 116 10909 7763 6990 691 222 112 S ATOM 686 N VAL A 117 -0.484 5.589 43.420 1.00 62.65 N ANISOU 686 N VAL A 117 10121 7175 6508 375 200 243 N ATOM 687 CA VAL A 117 0.650 4.699 43.157 1.00 62.07 C ANISOU 687 CA VAL A 117 10029 7086 6467 315 172 288 C ATOM 688 C VAL A 117 0.134 3.392 42.557 1.00 65.44 C ANISOU 688 C VAL A 117 10380 7543 6942 285 236 307 C ATOM 689 O VAL A 117 0.737 2.910 41.599 1.00 65.54 O ANISOU 689 O VAL A 117 10353 7544 7007 250 216 328 O ATOM 690 CB VAL A 117 1.543 4.458 44.406 1.00 66.49 C ANISOU 690 CB VAL A 117 10653 7643 6967 309 149 309 C ATOM 691 CG1 VAL A 117 2.771 3.614 44.065 1.00 66.01 C ANISOU 691 CG1 VAL A 117 10568 7586 6928 276 113 354 C ATOM 692 CG2 VAL A 117 1.972 5.778 45.035 1.00 66.59 C ANISOU 692 CG2 VAL A 117 10741 7635 6926 318 94 270 C ATOM 693 N THR A 118 -0.996 2.853 43.075 1.00 61.28 N ANISOU 693 N THR A 118 9835 7056 6394 288 320 289 N ATOM 694 CA THR A 118 -1.618 1.617 42.578 1.00 60.89 C ANISOU 694 CA THR A 118 9722 7034 6381 233 403 289 C ATOM 695 C THR A 118 -2.097 1.803 41.126 1.00 64.77 C ANISOU 695 C THR A 118 10114 7570 6928 223 391 253 C ATOM 696 O THR A 118 -1.815 0.950 40.280 1.00 64.19 O ANISOU 696 O THR A 118 9999 7487 6902 169 406 265 O ATOM 697 CB THR A 118 -2.776 1.174 43.490 1.00 68.24 C ANISOU 697 CB THR A 118 10653 8009 7267 222 504 262 C ATOM 698 OG1 THR A 118 -2.352 1.199 44.854 1.00 68.67 O ANISOU 698 OG1 THR A 118 10808 8029 7256 251 506 295 O ATOM 699 CG2 THR A 118 -3.302 -0.217 43.142 1.00 66.35 C ANISOU 699 CG2 THR A 118 10375 7781 7054 133 610 256 C ATOM 700 N ALA A 119 -2.794 2.927 40.841 1.00 61.01 N ANISOU 700 N ALA A 119 9606 7140 6433 289 364 212 N ATOM 701 CA ALA A 119 -3.314 3.243 39.512 1.00 60.45 C ANISOU 701 CA ALA A 119 9446 7131 6392 312 348 179 C ATOM 702 C ALA A 119 -2.187 3.439 38.497 1.00 63.86 C ANISOU 702 C ALA A 119 9894 7499 6870 299 276 215 C ATOM 703 O ALA A 119 -2.346 3.049 37.338 1.00 63.60 O ANISOU 703 O ALA A 119 9784 7506 6875 277 278 203 O ATOM 704 CB ALA A 119 -4.186 4.487 39.569 1.00 61.67 C ANISOU 704 CB ALA A 119 9596 7340 6495 421 334 139 C ATOM 705 N SER A 120 -1.046 4.016 38.934 1.00 59.76 N ANISOU 705 N SER A 120 9470 6894 6344 303 218 252 N ATOM 706 CA SER A 120 0.112 4.275 38.081 1.00 58.86 C ANISOU 706 CA SER A 120 9372 6726 6265 278 155 281 C ATOM 707 C SER A 120 0.754 2.974 37.607 1.00 62.30 C ANISOU 707 C SER A 120 9762 7159 6750 210 168 312 C ATOM 708 O SER A 120 0.865 2.772 36.403 1.00 62.09 O ANISOU 708 O SER A 120 9681 7145 6765 193 158 312 O ATOM 709 CB SER A 120 1.139 5.142 38.803 1.00 62.38 C ANISOU 709 CB SER A 120 9917 7106 6679 276 101 294 C ATOM 710 OG SER A 120 0.706 6.487 38.931 1.00 70.40 O ANISOU 710 OG SER A 120 11000 8094 7655 337 90 266 O ATOM 711 N ILE A 121 1.122 2.077 38.539 1.00 58.66 N ANISOU 711 N ILE A 121 9333 6682 6274 183 198 338 N ATOM 712 CA ILE A 121 1.758 0.794 38.227 1.00 58.11 C ANISOU 712 CA ILE A 121 9250 6593 6235 140 223 373 C ATOM 713 C ILE A 121 0.777 -0.140 37.463 1.00 61.92 C ANISOU 713 C ILE A 121 9666 7108 6754 96 301 343 C ATOM 714 O ILE A 121 1.231 -0.899 36.607 1.00 61.30 O ANISOU 714 O ILE A 121 9562 7014 6716 61 310 357 O ATOM 715 CB ILE A 121 2.365 0.132 39.510 1.00 61.47 C ANISOU 715 CB ILE A 121 9751 6992 6614 153 241 415 C ATOM 716 CG1 ILE A 121 3.220 -1.128 39.200 1.00 61.84 C ANISOU 716 CG1 ILE A 121 9809 7009 6678 141 262 462 C ATOM 717 CG2 ILE A 121 1.311 -0.171 40.571 1.00 62.53 C ANISOU 717 CG2 ILE A 121 9920 7136 6705 157 320 400 C ATOM 718 CD1 ILE A 121 4.646 -0.883 38.735 1.00 69.19 C ANISOU 718 CD1 ILE A 121 10726 7946 7618 156 177 489 C ATOM 719 N TRP A 122 -0.543 -0.063 37.739 1.00 59.01 N ANISOU 719 N TRP A 122 9260 6795 6364 93 359 295 N ATOM 720 CA TRP A 122 -1.507 -0.912 37.041 1.00 59.29 C ANISOU 720 CA TRP A 122 9216 6888 6424 30 436 245 C ATOM 721 C TRP A 122 -1.757 -0.406 35.618 1.00 63.61 C ANISOU 721 C TRP A 122 9669 7499 7000 45 390 210 C ATOM 722 O TRP A 122 -1.963 -1.233 34.727 1.00 62.77 O ANISOU 722 O TRP A 122 9503 7420 6925 -18 428 182 O ATOM 723 CB TRP A 122 -2.817 -1.085 37.819 1.00 58.80 C ANISOU 723 CB TRP A 122 9128 6892 6321 8 522 194 C ATOM 724 CG TRP A 122 -2.757 -2.225 38.794 1.00 60.46 C ANISOU 724 CG TRP A 122 9422 7039 6513 -52 618 220 C ATOM 725 CD1 TRP A 122 -2.617 -2.138 40.149 1.00 63.69 C ANISOU 725 CD1 TRP A 122 9922 7406 6870 -18 636 256 C ATOM 726 CD2 TRP A 122 -2.724 -3.625 38.477 1.00 60.75 C ANISOU 726 CD2 TRP A 122 9482 7028 6573 -147 712 220 C ATOM 727 NE1 TRP A 122 -2.533 -3.397 40.700 1.00 63.48 N ANISOU 727 NE1 TRP A 122 9978 7311 6829 -77 738 285 N ATOM 728 CE2 TRP A 122 -2.607 -4.329 39.698 1.00 65.11 C ANISOU 728 CE2 TRP A 122 10153 7504 7081 -159 793 263 C ATOM 729 CE3 TRP A 122 -2.806 -4.357 37.277 1.00 61.94 C ANISOU 729 CE3 TRP A 122 9577 7189 6770 -222 744 185 C ATOM 730 CZ2 TRP A 122 -2.564 -5.727 39.754 1.00 65.04 C ANISOU 730 CZ2 TRP A 122 10228 7412 7073 -239 912 277 C ATOM 731 CZ3 TRP A 122 -2.756 -5.741 37.334 1.00 63.93 C ANISOU 731 CZ3 TRP A 122 9903 7360 7026 -313 860 190 C ATOM 732 CH2 TRP A 122 -2.635 -6.412 38.560 1.00 65.19 C ANISOU 732 CH2 TRP A 122 10199 7429 7142 -319 947 239 C ATOM 733 N THR A 123 -1.684 0.926 35.382 1.00 61.15 N ANISOU 733 N THR A 123 9361 7202 6671 128 313 213 N ATOM 734 CA THR A 123 -1.829 1.458 34.017 1.00 61.47 C ANISOU 734 CA THR A 123 9336 7293 6726 163 269 193 C ATOM 735 C THR A 123 -0.579 1.115 33.208 1.00 64.05 C ANISOU 735 C THR A 123 9684 7551 7101 127 230 238 C ATOM 736 O THR A 123 -0.701 0.801 32.025 1.00 63.68 O ANISOU 736 O THR A 123 9570 7549 7078 109 228 217 O ATOM 737 CB THR A 123 -2.123 2.957 33.979 1.00 73.42 C ANISOU 737 CB THR A 123 10879 8821 8196 274 217 189 C ATOM 738 OG1 THR A 123 -1.219 3.647 34.837 1.00 78.18 O ANISOU 738 OG1 THR A 123 11599 9320 8787 290 178 233 O ATOM 739 CG2 THR A 123 -3.564 3.279 34.328 1.00 72.19 C ANISOU 739 CG2 THR A 123 10661 8781 7987 337 255 130 C ATOM 740 N LEU A 124 0.607 1.116 33.864 1.00 59.34 N ANISOU 740 N LEU A 124 9172 6865 6511 115 200 292 N ATOM 741 CA LEU A 124 1.888 0.744 33.251 1.00 58.23 C ANISOU 741 CA LEU A 124 9044 6675 6406 85 165 333 C ATOM 742 C LEU A 124 1.884 -0.735 32.860 1.00 60.97 C ANISOU 742 C LEU A 124 9359 7021 6785 26 227 330 C ATOM 743 O LEU A 124 2.406 -1.092 31.803 1.00 59.38 O ANISOU 743 O LEU A 124 9126 6817 6618 5 214 337 O ATOM 744 CB LEU A 124 3.066 1.049 34.190 1.00 58.13 C ANISOU 744 CB LEU A 124 9107 6606 6374 92 122 377 C ATOM 745 CG LEU A 124 3.425 2.525 34.370 1.00 62.95 C ANISOU 745 CG LEU A 124 9767 7195 6957 121 62 375 C ATOM 746 CD1 LEU A 124 4.328 2.719 35.567 1.00 63.46 C ANISOU 746 CD1 LEU A 124 9892 7234 6985 114 32 394 C ATOM 747 CD2 LEU A 124 4.053 3.105 33.119 1.00 65.32 C ANISOU 747 CD2 LEU A 124 10054 7483 7282 110 21 382 C ATOM 748 N CYS A 125 1.252 -1.577 33.702 1.00 58.39 N ANISOU 748 N CYS A 125 9053 6691 6444 -5 305 317 N ATOM 749 CA CYS A 125 1.081 -3.015 33.478 1.00 58.92 C ANISOU 749 CA CYS A 125 9122 6735 6530 -73 393 307 C ATOM 750 C CYS A 125 0.150 -3.238 32.284 1.00 61.79 C ANISOU 750 C CYS A 125 9384 7177 6915 -125 423 235 C ATOM 751 O CYS A 125 0.448 -4.078 31.438 1.00 61.66 O ANISOU 751 O CYS A 125 9356 7142 6930 -173 451 227 O ATOM 752 CB CYS A 125 0.549 -3.698 34.738 1.00 60.35 C ANISOU 752 CB CYS A 125 9369 6884 6676 -99 481 308 C ATOM 753 SG CYS A 125 0.514 -5.508 34.654 1.00 64.98 S ANISOU 753 SG CYS A 125 10022 7393 7274 -185 614 308 S ATOM 754 N VAL A 126 -0.955 -2.461 32.208 1.00 57.93 N ANISOU 754 N VAL A 126 8819 6789 6401 -103 413 179 N ATOM 755 CA VAL A 126 -1.953 -2.504 31.131 1.00 58.15 C ANISOU 755 CA VAL A 126 8727 6939 6427 -130 429 99 C ATOM 756 C VAL A 126 -1.282 -2.099 29.802 1.00 62.09 C ANISOU 756 C VAL A 126 9196 7445 6950 -93 355 117 C ATOM 757 O VAL A 126 -1.497 -2.781 28.797 1.00 61.61 O ANISOU 757 O VAL A 126 9071 7432 6905 -150 381 72 O ATOM 758 CB VAL A 126 -3.201 -1.636 31.471 1.00 62.45 C ANISOU 758 CB VAL A 126 9200 7608 6921 -75 426 45 C ATOM 759 CG1 VAL A 126 -3.964 -1.201 30.218 1.00 62.43 C ANISOU 759 CG1 VAL A 126 9070 7755 6897 -37 393 -20 C ATOM 760 CG2 VAL A 126 -4.128 -2.371 32.435 1.00 62.92 C ANISOU 760 CG2 VAL A 126 9247 7703 6958 -154 530 -5 C ATOM 761 N ILE A 127 -0.443 -1.027 29.815 1.00 58.63 N ANISOU 761 N ILE A 127 8813 6955 6510 -11 271 179 N ATOM 762 CA ILE A 127 0.315 -0.563 28.641 1.00 58.11 C ANISOU 762 CA ILE A 127 8740 6879 6461 19 208 206 C ATOM 763 C ILE A 127 1.203 -1.717 28.147 1.00 61.77 C ANISOU 763 C ILE A 127 9215 7286 6970 -50 233 225 C ATOM 764 O ILE A 127 1.131 -2.067 26.971 1.00 61.33 O ANISOU 764 O ILE A 127 9101 7275 6928 -72 235 196 O ATOM 765 CB ILE A 127 1.149 0.732 28.923 1.00 60.90 C ANISOU 765 CB ILE A 127 9173 7164 6800 88 136 264 C ATOM 766 CG1 ILE A 127 0.245 1.943 29.222 1.00 61.61 C ANISOU 766 CG1 ILE A 127 9273 7300 6838 177 118 245 C ATOM 767 CG2 ILE A 127 2.079 1.056 27.742 1.00 61.22 C ANISOU 767 CG2 ILE A 127 9219 7182 6861 93 90 295 C ATOM 768 CD1 ILE A 127 0.931 3.143 29.964 1.00 65.15 C ANISOU 768 CD1 ILE A 127 9834 7657 7265 220 75 289 C ATOM 769 N ALA A 128 1.994 -2.325 29.062 1.00 58.47 N ANISOU 769 N ALA A 128 8874 6778 6565 -72 255 271 N ATOM 770 CA ALA A 128 2.894 -3.448 28.786 1.00 58.28 C ANISOU 770 CA ALA A 128 8883 6692 6570 -109 286 298 C ATOM 771 C ALA A 128 2.159 -4.608 28.107 1.00 63.32 C ANISOU 771 C ALA A 128 9482 7352 7223 -187 370 236 C ATOM 772 O ALA A 128 2.630 -5.087 27.069 1.00 63.43 O ANISOU 772 O ALA A 128 9477 7362 7261 -206 370 231 O ATOM 773 CB ALA A 128 3.561 -3.924 30.071 1.00 58.96 C ANISOU 773 CB ALA A 128 9060 6700 6641 -92 307 352 C ATOM 774 N VAL A 129 0.983 -5.015 28.657 1.00 59.81 N ANISOU 774 N VAL A 129 9023 6942 6760 -241 445 179 N ATOM 775 CA VAL A 129 0.143 -6.098 28.118 1.00 59.84 C ANISOU 775 CA VAL A 129 8988 6979 6769 -348 542 97 C ATOM 776 C VAL A 129 -0.386 -5.702 26.722 1.00 62.80 C ANISOU 776 C VAL A 129 9237 7483 7142 -355 500 30 C ATOM 777 O VAL A 129 -0.241 -6.487 25.781 1.00 62.38 O ANISOU 777 O VAL A 129 9167 7428 7106 -415 533 -7 O ATOM 778 CB VAL A 129 -1.001 -6.489 29.096 1.00 64.29 C ANISOU 778 CB VAL A 129 9556 7568 7304 -418 636 44 C ATOM 779 CG1 VAL A 129 -2.013 -7.426 28.439 1.00 65.02 C ANISOU 779 CG1 VAL A 129 9581 7731 7393 -554 736 -69 C ATOM 780 CG2 VAL A 129 -0.440 -7.123 30.364 1.00 64.19 C ANISOU 780 CG2 VAL A 129 9688 7417 7283 -414 696 113 C ATOM 781 N ASP A 130 -0.946 -4.473 26.593 1.00 58.53 N ANISOU 781 N ASP A 130 8621 7047 6571 -277 427 17 N ATOM 782 CA ASP A 130 -1.483 -3.915 25.344 1.00 58.11 C ANISOU 782 CA ASP A 130 8455 7131 6493 -242 377 -35 C ATOM 783 C ASP A 130 -0.415 -3.868 24.246 1.00 61.30 C ANISOU 783 C ASP A 130 8878 7489 6923 -215 325 9 C ATOM 784 O ASP A 130 -0.723 -4.132 23.082 1.00 60.44 O ANISOU 784 O ASP A 130 8692 7469 6804 -238 324 -47 O ATOM 785 CB ASP A 130 -2.054 -2.503 25.582 1.00 59.55 C ANISOU 785 CB ASP A 130 8603 7396 6627 -122 310 -26 C ATOM 786 CG ASP A 130 -2.582 -1.839 24.330 1.00 64.74 C ANISOU 786 CG ASP A 130 9162 8195 7240 -47 256 -66 C ATOM 787 OD1 ASP A 130 -3.643 -2.263 23.843 1.00 66.43 O ANISOU 787 OD1 ASP A 130 9254 8567 7418 -87 288 -165 O ATOM 788 OD2 ASP A 130 -1.903 -0.930 23.809 1.00 65.20 O ANISOU 788 OD2 ASP A 130 9269 8212 7292 46 186 -1 O ATOM 789 N ARG A 131 0.832 -3.521 24.619 1.00 57.97 N ANISOU 789 N ARG A 131 8552 6947 6528 -170 283 104 N ATOM 790 CA ARG A 131 1.961 -3.461 23.693 1.00 57.41 C ANISOU 790 CA ARG A 131 8500 6833 6481 -149 240 150 C ATOM 791 C ARG A 131 2.363 -4.856 23.252 1.00 62.39 C ANISOU 791 C ARG A 131 9145 7418 7143 -228 305 129 C ATOM 792 O ARG A 131 2.806 -5.007 22.119 1.00 62.07 O ANISOU 792 O ARG A 131 9078 7396 7111 -229 287 124 O ATOM 793 CB ARG A 131 3.173 -2.720 24.301 1.00 55.32 C ANISOU 793 CB ARG A 131 8317 6476 6227 -96 185 240 C ATOM 794 CG ARG A 131 3.035 -1.198 24.436 1.00 54.95 C ANISOU 794 CG ARG A 131 8285 6448 6147 -20 121 264 C ATOM 795 CD ARG A 131 2.767 -0.478 23.126 1.00 54.42 C ANISOU 795 CD ARG A 131 8175 6450 6053 30 84 252 C ATOM 796 NE ARG A 131 1.330 -0.356 22.869 1.00 58.18 N ANISOU 796 NE ARG A 131 8573 7048 6485 63 97 184 N ATOM 797 CZ ARG A 131 0.799 -0.087 21.680 1.00 69.17 C ANISOU 797 CZ ARG A 131 9900 8544 7838 110 78 150 C ATOM 798 NH1 ARG A 131 1.574 0.089 20.620 1.00 58.09 N ANISOU 798 NH1 ARG A 131 8513 7121 6439 123 50 183 N ATOM 799 NH2 ARG A 131 -0.518 -0.002 21.544 1.00 53.59 N ANISOU 799 NH2 ARG A 131 7837 6712 5812 149 86 79 N ATOM 800 N TYR A 132 2.198 -5.874 24.126 1.00 60.27 N ANISOU 800 N TYR A 132 8933 7082 6884 -289 388 118 N ATOM 801 CA TYR A 132 2.527 -7.260 23.789 1.00 61.24 C ANISOU 801 CA TYR A 132 9104 7135 7028 -359 470 98 C ATOM 802 C TYR A 132 1.543 -7.813 22.761 1.00 66.12 C ANISOU 802 C TYR A 132 9638 7847 7637 -451 520 -13 C ATOM 803 O TYR A 132 1.969 -8.432 21.787 1.00 65.74 O ANISOU 803 O TYR A 132 9592 7785 7602 -479 538 -33 O ATOM 804 CB TYR A 132 2.568 -8.169 25.038 1.00 63.34 C ANISOU 804 CB TYR A 132 9484 7289 7293 -391 561 121 C ATOM 805 CG TYR A 132 2.738 -9.637 24.699 1.00 66.58 C ANISOU 805 CG TYR A 132 9973 7610 7714 -464 671 93 C ATOM 806 CD1 TYR A 132 3.996 -10.167 24.423 1.00 68.87 C ANISOU 806 CD1 TYR A 132 10340 7811 8017 -405 669 157 C ATOM 807 CD2 TYR A 132 1.635 -10.483 24.599 1.00 68.31 C ANISOU 807 CD2 TYR A 132 10189 7841 7923 -596 783 -7 C ATOM 808 CE1 TYR A 132 4.154 -11.508 24.072 1.00 71.12 C ANISOU 808 CE1 TYR A 132 10718 7998 8304 -457 778 131 C ATOM 809 CE2 TYR A 132 1.780 -11.820 24.232 1.00 70.20 C ANISOU 809 CE2 TYR A 132 10524 7980 8168 -676 899 -42 C ATOM 810 CZ TYR A 132 3.043 -12.331 23.979 1.00 78.99 C ANISOU 810 CZ TYR A 132 11735 8984 9294 -597 897 33 C ATOM 811 OH TYR A 132 3.198 -13.650 23.629 1.00 81.68 O ANISOU 811 OH TYR A 132 12194 9209 9633 -659 1020 2 O ATOM 812 N PHE A 133 0.233 -7.620 22.999 1.00 63.58 N ANISOU 812 N PHE A 133 9238 7634 7285 -500 545 -93 N ATOM 813 CA PHE A 133 -0.825 -8.099 22.119 1.00 64.69 C ANISOU 813 CA PHE A 133 9272 7906 7401 -597 591 -220 C ATOM 814 C PHE A 133 -0.778 -7.408 20.764 1.00 69.25 C ANISOU 814 C PHE A 133 9749 8606 7958 -532 501 -237 C ATOM 815 O PHE A 133 -1.168 -8.015 19.768 1.00 69.50 O ANISOU 815 O PHE A 133 9714 8719 7974 -608 533 -328 O ATOM 816 CB PHE A 133 -2.198 -7.923 22.773 1.00 67.46 C ANISOU 816 CB PHE A 133 9542 8378 7714 -649 630 -301 C ATOM 817 CG PHE A 133 -2.556 -9.061 23.698 1.00 69.97 C ANISOU 817 CG PHE A 133 9943 8601 8040 -782 768 -338 C ATOM 818 CD1 PHE A 133 -3.140 -10.221 23.205 1.00 74.15 C ANISOU 818 CD1 PHE A 133 10459 9153 8563 -948 882 -454 C ATOM 819 CD2 PHE A 133 -2.292 -8.980 25.060 1.00 72.22 C ANISOU 819 CD2 PHE A 133 10336 8771 8333 -747 791 -259 C ATOM 820 CE1 PHE A 133 -3.455 -11.281 24.058 1.00 76.17 C ANISOU 820 CE1 PHE A 133 10822 9297 8820 -1081 1029 -485 C ATOM 821 CE2 PHE A 133 -2.619 -10.036 25.915 1.00 76.01 C ANISOU 821 CE2 PHE A 133 10916 9153 8810 -864 930 -284 C ATOM 822 CZ PHE A 133 -3.197 -11.180 25.408 1.00 75.32 C ANISOU 822 CZ PHE A 133 10830 9072 8718 -1032 1054 -395 C ATOM 823 N ALA A 134 -0.263 -6.164 20.720 1.00 65.98 N ANISOU 823 N ALA A 134 9337 8196 7537 -398 398 -151 N ATOM 824 CA ALA A 134 -0.107 -5.380 19.493 1.00 65.88 C ANISOU 824 CA ALA A 134 9261 8274 7495 -315 317 -144 C ATOM 825 C ALA A 134 1.065 -5.900 18.655 1.00 69.29 C ANISOU 825 C ALA A 134 9745 8620 7962 -328 315 -105 C ATOM 826 O ALA A 134 0.867 -6.161 17.471 1.00 69.39 O ANISOU 826 O ALA A 134 9692 8720 7951 -347 312 -164 O ATOM 827 CB ALA A 134 0.091 -3.906 19.824 1.00 66.11 C ANISOU 827 CB ALA A 134 9314 8301 7502 -181 232 -63 C ATOM 828 N ILE A 135 2.269 -6.078 19.271 1.00 65.04 N ANISOU 828 N ILE A 135 9315 7928 7470 -312 318 -14 N ATOM 829 CA ILE A 135 3.494 -6.555 18.611 1.00 64.51 C ANISOU 829 CA ILE A 135 9296 7783 7431 -307 318 30 C ATOM 830 C ILE A 135 3.326 -8.017 18.116 1.00 70.14 C ANISOU 830 C ILE A 135 10021 8472 8156 -407 411 -46 C ATOM 831 O ILE A 135 3.904 -8.367 17.088 1.00 70.17 O ANISOU 831 O ILE A 135 10021 8477 8163 -407 410 -52 O ATOM 832 CB ILE A 135 4.778 -6.352 19.490 1.00 66.62 C ANISOU 832 CB ILE A 135 9654 7928 7728 -254 296 136 C ATOM 833 CG1 ILE A 135 6.074 -6.429 18.660 1.00 66.57 C ANISOU 833 CG1 ILE A 135 9663 7892 7737 -222 270 185 C ATOM 834 CG2 ILE A 135 4.855 -7.272 20.712 1.00 67.16 C ANISOU 834 CG2 ILE A 135 9807 7896 7814 -287 367 149 C ATOM 835 CD1 ILE A 135 6.735 -5.121 18.403 1.00 71.57 C ANISOU 835 CD1 ILE A 135 10285 8549 8360 -159 188 246 C ATOM 836 N THR A 136 2.511 -8.836 18.807 1.00 68.11 N ANISOU 836 N THR A 136 9785 8194 7898 -499 499 -109 N ATOM 837 CA THR A 136 2.272 -10.236 18.427 1.00 69.25 C ANISOU 837 CA THR A 136 9969 8294 8048 -616 610 -192 C ATOM 838 C THR A 136 1.168 -10.355 17.357 1.00 74.73 C ANISOU 838 C THR A 136 10535 9155 8703 -702 621 -327 C ATOM 839 O THR A 136 1.018 -11.425 16.756 1.00 75.61 O ANISOU 839 O THR A 136 10667 9248 8812 -809 705 -412 O ATOM 840 CB THR A 136 1.952 -11.100 19.655 1.00 77.96 C ANISOU 840 CB THR A 136 11178 9283 9161 -690 721 -200 C ATOM 841 OG1 THR A 136 0.881 -10.516 20.401 1.00 77.28 O ANISOU 841 OG1 THR A 136 11024 9286 9053 -714 713 -235 O ATOM 842 CG2 THR A 136 3.169 -11.323 20.543 1.00 75.69 C ANISOU 842 CG2 THR A 136 11029 8832 8896 -601 726 -77 C ATOM 843 N SER A 137 0.420 -9.257 17.105 1.00 71.23 N ANISOU 843 N SER A 137 9966 8879 8219 -646 537 -350 N ATOM 844 CA SER A 137 -0.648 -9.200 16.101 1.00 71.95 C ANISOU 844 CA SER A 137 9910 9175 8252 -692 525 -476 C ATOM 845 C SER A 137 -0.081 -8.785 14.725 1.00 76.06 C ANISOU 845 C SER A 137 10391 9758 8751 -613 450 -457 C ATOM 846 O SER A 137 0.994 -8.175 14.694 1.00 75.15 O ANISOU 846 O SER A 137 10343 9549 8661 -507 391 -337 O ATOM 847 CB SER A 137 -1.748 -8.230 16.541 1.00 75.45 C ANISOU 847 CB SER A 137 10243 9781 8646 -639 475 -505 C ATOM 848 OG SER A 137 -1.463 -6.874 16.235 1.00 82.19 O ANISOU 848 OG SER A 137 11073 10684 9472 -471 362 -418 O ATOM 849 N PRO A 138 -0.783 -9.053 13.585 1.00 72.87 N ANISOU 849 N PRO A 138 9874 9525 8290 -663 451 -576 N ATOM 850 CA PRO A 138 -0.254 -8.630 12.275 1.00 72.19 C ANISOU 850 CA PRO A 138 9756 9502 8172 -578 381 -552 C ATOM 851 C PRO A 138 -0.202 -7.109 12.099 1.00 74.26 C ANISOU 851 C PRO A 138 9986 9838 8391 -402 269 -461 C ATOM 852 O PRO A 138 0.496 -6.626 11.208 1.00 72.93 O ANISOU 852 O PRO A 138 9836 9667 8205 -317 217 -402 O ATOM 853 CB PRO A 138 -1.236 -9.255 11.276 1.00 75.49 C ANISOU 853 CB PRO A 138 10047 10115 8523 -677 409 -719 C ATOM 854 CG PRO A 138 -1.980 -10.288 12.037 1.00 80.75 C ANISOU 854 CG PRO A 138 10714 10760 9207 -853 522 -828 C ATOM 855 CD PRO A 138 -2.068 -9.760 13.422 1.00 75.76 C ANISOU 855 CD PRO A 138 10130 10046 8609 -807 518 -745 C ATOM 856 N PHE A 139 -0.927 -6.365 12.956 1.00 71.10 N ANISOU 856 N PHE A 139 9553 9492 7970 -347 243 -449 N ATOM 857 CA PHE A 139 -0.976 -4.898 12.972 1.00 70.73 C ANISOU 857 CA PHE A 139 9506 9492 7877 -176 155 -363 C ATOM 858 C PHE A 139 0.344 -4.318 13.521 1.00 71.63 C ANISOU 858 C PHE A 139 9764 9396 8055 -119 132 -215 C ATOM 859 O PHE A 139 0.702 -3.187 13.191 1.00 71.17 O ANISOU 859 O PHE A 139 9746 9333 7964 4 72 -133 O ATOM 860 CB PHE A 139 -2.187 -4.409 13.788 1.00 73.47 C ANISOU 860 CB PHE A 139 9777 9959 8179 -142 148 -409 C ATOM 861 CG PHE A 139 -3.501 -4.956 13.275 1.00 76.93 C ANISOU 861 CG PHE A 139 10046 10639 8544 -208 170 -572 C ATOM 862 CD1 PHE A 139 -4.105 -4.416 12.143 1.00 81.29 C ANISOU 862 CD1 PHE A 139 10483 11412 8989 -100 107 -621 C ATOM 863 CD2 PHE A 139 -4.122 -6.029 13.908 1.00 79.79 C ANISOU 863 CD2 PHE A 139 10365 11018 8935 -383 261 -680 C ATOM 864 CE1 PHE A 139 -5.307 -4.940 11.652 1.00 83.64 C ANISOU 864 CE1 PHE A 139 10602 11970 9207 -167 123 -788 C ATOM 865 CE2 PHE A 139 -5.327 -6.549 13.420 1.00 84.02 C ANISOU 865 CE2 PHE A 139 10731 11795 9396 -473 290 -849 C ATOM 866 CZ PHE A 139 -5.910 -6.002 12.295 1.00 83.09 C ANISOU 866 CZ PHE A 139 10477 11922 9171 -365 215 -907 C ATOM 867 N LYS A 140 1.060 -5.113 14.346 1.00 65.79 N ANISOU 867 N LYS A 140 9108 8493 7396 -210 188 -185 N ATOM 868 CA LYS A 140 2.375 -4.886 14.958 1.00 63.91 C ANISOU 868 CA LYS A 140 8988 8077 7219 -185 179 -68 C ATOM 869 C LYS A 140 2.450 -3.683 15.923 1.00 67.28 C ANISOU 869 C LYS A 140 9465 8456 7642 -101 133 12 C ATOM 870 O LYS A 140 2.924 -3.856 17.047 1.00 66.70 O ANISOU 870 O LYS A 140 9459 8269 7614 -128 153 57 O ATOM 871 CB LYS A 140 3.481 -4.768 13.901 1.00 64.84 C ANISOU 871 CB LYS A 140 9136 8160 7341 -153 153 -16 C ATOM 872 CG LYS A 140 4.760 -5.473 14.317 1.00 66.24 C ANISOU 872 CG LYS A 140 9395 8189 7584 -193 188 40 C ATOM 873 CD LYS A 140 5.786 -5.452 13.206 1.00 71.07 C ANISOU 873 CD LYS A 140 10017 8793 8195 -169 172 76 C ATOM 874 CE LYS A 140 6.953 -6.331 13.548 1.00 76.90 C ANISOU 874 CE LYS A 140 10817 9416 8985 -198 213 113 C ATOM 875 NZ LYS A 140 8.075 -6.170 12.591 1.00 84.22 N ANISOU 875 NZ LYS A 140 11749 10342 9910 -166 195 157 N ATOM 876 N TYR A 141 2.040 -2.482 15.506 1.00 63.31 N ANISOU 876 N TYR A 141 8945 8031 7078 5 76 33 N ATOM 877 CA TYR A 141 2.183 -1.317 16.376 1.00 62.31 C ANISOU 877 CA TYR A 141 8893 7838 6946 81 43 107 C ATOM 878 C TYR A 141 0.840 -0.671 16.730 1.00 67.35 C ANISOU 878 C TYR A 141 9479 8592 7519 159 28 65 C ATOM 879 O TYR A 141 0.802 0.325 17.460 1.00 66.67 O ANISOU 879 O TYR A 141 9460 8455 7417 232 6 116 O ATOM 880 CB TYR A 141 3.150 -0.321 15.727 1.00 62.76 C ANISOU 880 CB TYR A 141 9028 7832 6986 148 5 193 C ATOM 881 CG TYR A 141 4.489 -0.957 15.420 1.00 63.26 C ANISOU 881 CG TYR A 141 9123 7806 7108 74 21 229 C ATOM 882 CD1 TYR A 141 5.333 -1.380 16.446 1.00 64.79 C ANISOU 882 CD1 TYR A 141 9364 7891 7363 14 39 263 C ATOM 883 CD2 TYR A 141 4.882 -1.206 14.109 1.00 63.63 C ANISOU 883 CD2 TYR A 141 9145 7894 7138 75 19 223 C ATOM 884 CE1 TYR A 141 6.557 -1.987 16.172 1.00 65.25 C ANISOU 884 CE1 TYR A 141 9439 7892 7462 -31 53 293 C ATOM 885 CE2 TYR A 141 6.105 -1.813 13.822 1.00 63.91 C ANISOU 885 CE2 TYR A 141 9201 7860 7220 18 38 251 C ATOM 886 CZ TYR A 141 6.940 -2.202 14.859 1.00 70.34 C ANISOU 886 CZ TYR A 141 10057 8576 8093 -30 54 286 C ATOM 887 OH TYR A 141 8.146 -2.806 14.601 1.00 69.28 O ANISOU 887 OH TYR A 141 9934 8397 7994 -64 70 312 O ATOM 888 N GLN A 142 -0.256 -1.278 16.258 1.00 65.16 N ANISOU 888 N GLN A 142 9079 8478 7201 137 45 -39 N ATOM 889 CA GLN A 142 -1.615 -0.840 16.540 1.00 66.34 C ANISOU 889 CA GLN A 142 9141 8785 7279 206 35 -101 C ATOM 890 C GLN A 142 -2.216 -1.739 17.597 1.00 72.10 C ANISOU 890 C GLN A 142 9826 9524 8047 86 97 -171 C ATOM 891 O GLN A 142 -2.131 -2.964 17.479 1.00 72.78 O ANISOU 891 O GLN A 142 9883 9596 8176 -54 155 -231 O ATOM 892 CB GLN A 142 -2.482 -0.872 15.272 1.00 68.83 C ANISOU 892 CB GLN A 142 9327 9322 7504 263 10 -186 C ATOM 893 CG GLN A 142 -2.215 0.253 14.275 1.00 90.57 C ANISOU 893 CG GLN A 142 12130 12099 10182 429 -50 -115 C ATOM 894 CD GLN A 142 -3.030 0.118 13.001 1.00114.33 C ANISOU 894 CD GLN A 142 15006 15344 13090 492 -77 -201 C ATOM 895 OE1 GLN A 142 -3.705 -0.891 12.746 1.00109.49 O ANISOU 895 OE1 GLN A 142 14253 14880 12469 385 -51 -326 O ATOM 896 NE2 GLN A 142 -2.973 1.139 12.158 1.00110.11 N ANISOU 896 NE2 GLN A 142 14519 14850 12467 664 -125 -140 N ATOM 897 N SER A 143 -2.831 -1.140 18.624 1.00 68.90 N ANISOU 897 N SER A 143 9425 9132 7620 140 96 -165 N ATOM 898 CA SER A 143 -3.500 -1.885 19.685 1.00 69.09 C ANISOU 898 CA SER A 143 9410 9174 7668 34 163 -229 C ATOM 899 C SER A 143 -4.762 -2.560 19.153 1.00 74.52 C ANISOU 899 C SER A 143 9925 10088 8300 -33 198 -375 C ATOM 900 O SER A 143 -5.362 -2.080 18.186 1.00 75.21 O ANISOU 900 O SER A 143 9911 10359 8306 64 149 -420 O ATOM 901 CB SER A 143 -3.849 -0.958 20.844 1.00 72.68 C ANISOU 901 CB SER A 143 9911 9602 8103 124 148 -187 C ATOM 902 OG SER A 143 -4.934 -1.427 21.629 1.00 81.26 O ANISOU 902 OG SER A 143 10911 10793 9171 60 205 -274 O ATOM 903 N LEU A 144 -5.164 -3.666 19.798 1.00 70.87 N ANISOU 903 N LEU A 144 9436 9619 7872 -198 288 -451 N ATOM 904 CA LEU A 144 -6.358 -4.428 19.431 1.00 71.42 C ANISOU 904 CA LEU A 144 9343 9901 7892 -311 344 -610 C ATOM 905 C LEU A 144 -7.592 -3.838 20.109 1.00 75.06 C ANISOU 905 C LEU A 144 9692 10543 8283 -251 343 -669 C ATOM 906 O LEU A 144 -8.721 -4.178 19.749 1.00 76.18 O ANISOU 906 O LEU A 144 9661 10927 8358 -309 371 -810 O ATOM 907 CB LEU A 144 -6.182 -5.910 19.795 1.00 71.66 C ANISOU 907 CB LEU A 144 9424 9817 7987 -533 463 -666 C ATOM 908 CG LEU A 144 -4.959 -6.612 19.185 1.00 75.68 C ANISOU 908 CG LEU A 144 10050 10144 8561 -586 477 -612 C ATOM 909 CD1 LEU A 144 -4.679 -7.918 19.890 1.00 76.21 C ANISOU 909 CD1 LEU A 144 10226 10041 8687 -758 603 -629 C ATOM 910 CD2 LEU A 144 -5.119 -6.825 17.685 1.00 78.20 C ANISOU 910 CD2 LEU A 144 10265 10610 8836 -598 448 -693 C ATOM 911 N LEU A 145 -7.366 -2.936 21.079 1.00 70.00 N ANISOU 911 N LEU A 145 9146 9798 7652 -133 312 -568 N ATOM 912 CA LEU A 145 -8.419 -2.245 21.813 1.00 69.89 C ANISOU 912 CA LEU A 145 9053 9931 7572 -44 308 -604 C ATOM 913 C LEU A 145 -8.906 -1.033 21.041 1.00 74.51 C ANISOU 913 C LEU A 145 9563 10692 8055 181 213 -597 C ATOM 914 O LEU A 145 -8.116 -0.363 20.373 1.00 73.35 O ANISOU 914 O LEU A 145 9511 10451 7909 299 146 -502 O ATOM 915 CB LEU A 145 -7.919 -1.787 23.202 1.00 68.60 C ANISOU 915 CB LEU A 145 9042 9567 7457 -9 318 -498 C ATOM 916 CG LEU A 145 -7.496 -2.847 24.221 1.00 71.86 C ANISOU 916 CG LEU A 145 9550 9804 7949 -187 414 -487 C ATOM 917 CD1 LEU A 145 -6.658 -2.227 25.318 1.00 70.45 C ANISOU 917 CD1 LEU A 145 9539 9418 7811 -115 390 -360 C ATOM 918 CD2 LEU A 145 -8.697 -3.549 24.828 1.00 74.55 C ANISOU 918 CD2 LEU A 145 9777 10289 8259 -318 512 -612 C ATOM 919 N THR A 146 -10.206 -0.748 21.143 1.00 72.71 N ANISOU 919 N THR A 146 9170 10724 7731 247 214 -697 N ATOM 920 CA THR A 146 -10.812 0.446 20.567 1.00 73.57 C ANISOU 920 CA THR A 146 9212 11019 7720 499 131 -689 C ATOM 921 C THR A 146 -10.785 1.500 21.681 1.00 78.98 C ANISOU 921 C THR A 146 10022 11589 8399 646 118 -595 C ATOM 922 O THR A 146 -10.492 1.152 22.831 1.00 77.86 O ANISOU 922 O THR A 146 9963 11286 8335 529 174 -568 O ATOM 923 CB THR A 146 -12.214 0.160 19.989 1.00 81.60 C ANISOU 923 CB THR A 146 9966 12416 8620 506 135 -858 C ATOM 924 OG1 THR A 146 -13.128 -0.195 21.030 1.00 81.21 O ANISOU 924 OG1 THR A 146 9813 12483 8561 412 206 -950 O ATOM 925 CG2 THR A 146 -12.199 -0.900 18.888 1.00 79.40 C ANISOU 925 CG2 THR A 146 9577 12246 8346 341 152 -963 C ATOM 926 N LYS A 147 -11.058 2.777 21.354 1.00 77.52 N ANISOU 926 N LYS A 147 9865 11473 8115 906 51 -543 N ATOM 927 CA LYS A 147 -11.044 3.872 22.335 1.00 77.73 C ANISOU 927 CA LYS A 147 10028 11383 8123 1061 42 -457 C ATOM 928 C LYS A 147 -12.097 3.681 23.425 1.00 83.27 C ANISOU 928 C LYS A 147 10613 12230 8796 1032 95 -544 C ATOM 929 O LYS A 147 -11.858 4.078 24.568 1.00 82.14 O ANISOU 929 O LYS A 147 10596 11925 8689 1042 118 -484 O ATOM 930 CB LYS A 147 -11.251 5.231 21.657 1.00 81.43 C ANISOU 930 CB LYS A 147 10558 11911 8472 1358 -25 -395 C ATOM 931 CG LYS A 147 -10.104 5.648 20.751 1.00 95.65 C ANISOU 931 CG LYS A 147 12526 13518 10299 1399 -65 -285 C ATOM 932 CD LYS A 147 -10.334 7.036 20.172 1.00104.74 C ANISOU 932 CD LYS A 147 13777 14699 11320 1700 -112 -215 C ATOM 933 CE LYS A 147 -9.623 7.244 18.854 1.00110.87 C ANISOU 933 CE LYS A 147 14631 15418 12076 1752 -149 -153 C ATOM 934 NZ LYS A 147 -8.152 7.057 18.968 1.00112.69 N ANISOU 934 NZ LYS A 147 15037 15338 12440 1579 -132 -61 N ATOM 935 N ASN A 148 -13.248 3.062 23.076 1.00 81.91 N ANISOU 935 N ASN A 148 10196 12373 8553 984 117 -693 N ATOM 936 CA ASN A 148 -14.345 2.802 24.008 1.00 83.10 C ANISOU 936 CA ASN A 148 10202 12708 8664 937 178 -797 C ATOM 937 C ASN A 148 -13.889 1.862 25.129 1.00 84.99 C ANISOU 937 C ASN A 148 10522 12741 9028 679 269 -792 C ATOM 938 O ASN A 148 -13.911 2.267 26.293 1.00 83.36 O ANISOU 938 O ASN A 148 10407 12430 8835 713 296 -745 O ATOM 939 CB ASN A 148 -15.571 2.233 23.273 1.00 88.38 C ANISOU 939 CB ASN A 148 10577 13771 9231 901 188 -975 C ATOM 940 CG ASN A 148 -16.718 1.836 24.177 1.00123.23 C ANISOU 940 CG ASN A 148 14815 18403 13604 810 265 -1104 C ATOM 941 OD1 ASN A 148 -17.081 2.544 25.128 1.00121.16 O ANISOU 941 OD1 ASN A 148 14593 18134 13308 939 274 -1070 O ATOM 942 ND2 ASN A 148 -17.304 0.678 23.908 1.00118.62 N ANISOU 942 ND2 ASN A 148 14039 18012 13020 572 333 -1261 N ATOM 943 N LYS A 149 -13.426 0.640 24.772 1.00 81.37 N ANISOU 943 N LYS A 149 10054 12211 8653 437 318 -831 N ATOM 944 CA LYS A 149 -12.958 -0.362 25.738 1.00 80.33 C ANISOU 944 CA LYS A 149 10018 11876 8627 201 415 -821 C ATOM 945 C LYS A 149 -11.696 0.097 26.491 1.00 81.90 C ANISOU 945 C LYS A 149 10470 11738 8911 246 391 -656 C ATOM 946 O LYS A 149 -11.547 -0.270 27.653 1.00 80.89 O ANISOU 946 O LYS A 149 10425 11479 8830 148 457 -633 O ATOM 947 CB LYS A 149 -12.750 -1.753 25.109 1.00 82.59 C ANISOU 947 CB LYS A 149 10258 12153 8969 -45 480 -900 C ATOM 948 CG LYS A 149 -12.073 -1.782 23.747 1.00 92.85 C ANISOU 948 CG LYS A 149 11572 13428 10280 -11 411 -873 C ATOM 949 CD LYS A 149 -12.074 -3.183 23.118 1.00103.53 C ANISOU 949 CD LYS A 149 12859 14809 11670 -257 488 -980 C ATOM 950 CE LYS A 149 -13.359 -3.557 22.406 1.00115.16 C ANISOU 950 CE LYS A 149 14072 16639 13043 -322 510 -1169 C ATOM 951 NZ LYS A 149 -14.349 -4.189 23.321 1.00124.49 N ANISOU 951 NZ LYS A 149 15150 17945 14206 -494 626 -1291 N ATOM 952 N ALA A 150 -10.830 0.928 25.867 1.00 77.54 N ANISOU 952 N ALA A 150 10036 11061 8367 394 302 -549 N ATOM 953 CA ALA A 150 -9.640 1.487 26.525 1.00 75.79 C ANISOU 953 CA ALA A 150 10035 10551 8209 437 274 -408 C ATOM 954 C ALA A 150 -10.059 2.340 27.730 1.00 78.81 C ANISOU 954 C ALA A 150 10474 10918 8553 548 280 -381 C ATOM 955 O ALA A 150 -9.483 2.176 28.804 1.00 78.03 O ANISOU 955 O ALA A 150 10498 10637 8511 474 312 -326 O ATOM 956 CB ALA A 150 -8.825 2.317 25.543 1.00 75.99 C ANISOU 956 CB ALA A 150 10154 10489 8228 571 189 -320 C ATOM 957 N ARG A 151 -11.103 3.200 27.559 1.00 75.31 N ANISOU 957 N ARG A 151 9933 10679 8001 733 252 -427 N ATOM 958 CA ARG A 151 -11.681 4.053 28.610 1.00 75.06 C ANISOU 958 CA ARG A 151 9937 10670 7913 865 261 -417 C ATOM 959 C ARG A 151 -12.259 3.179 29.718 1.00 77.68 C ANISOU 959 C ARG A 151 10195 11052 8267 700 354 -489 C ATOM 960 O ARG A 151 -12.042 3.466 30.894 1.00 76.80 O ANISOU 960 O ARG A 151 10200 10807 8174 704 378 -440 O ATOM 961 CB ARG A 151 -12.772 4.983 28.044 1.00 77.67 C ANISOU 961 CB ARG A 151 10152 11251 8108 1107 220 -466 C ATOM 962 CG ARG A 151 -12.260 6.123 27.166 1.00 90.30 C ANISOU 962 CG ARG A 151 11881 12768 9660 1321 141 -375 C ATOM 963 CD ARG A 151 -13.404 6.979 26.646 1.00104.74 C ANISOU 963 CD ARG A 151 13601 14860 11337 1587 108 -421 C ATOM 964 NE ARG A 151 -12.973 7.901 25.592 1.00116.61 N ANISOU 964 NE ARG A 151 15222 16302 12782 1785 45 -340 N ATOM 965 CZ ARG A 151 -13.165 7.703 24.290 1.00132.85 C ANISOU 965 CZ ARG A 151 17168 18524 14786 1836 4 -372 C ATOM 966 NH1 ARG A 151 -13.789 6.613 23.860 1.00120.50 N ANISOU 966 NH1 ARG A 151 15362 17202 13219 1694 18 -496 N ATOM 967 NH2 ARG A 151 -12.739 8.597 23.407 1.00121.17 N ANISOU 967 NH2 ARG A 151 15827 16966 13248 2024 -43 -285 N ATOM 968 N VAL A 152 -12.948 2.081 29.327 1.00 74.02 N ANISOU 968 N VAL A 152 9549 10774 7800 540 412 -607 N ATOM 969 CA VAL A 152 -13.556 1.082 30.212 1.00 73.64 C ANISOU 969 CA VAL A 152 9424 10786 7768 344 524 -691 C ATOM 970 C VAL A 152 -12.446 0.438 31.058 1.00 75.10 C ANISOU 970 C VAL A 152 9808 10668 8060 194 570 -599 C ATOM 971 O VAL A 152 -12.610 0.349 32.273 1.00 74.85 O ANISOU 971 O VAL A 152 9834 10577 8031 153 631 -589 O ATOM 972 CB VAL A 152 -14.390 0.035 29.416 1.00 78.45 C ANISOU 972 CB VAL A 152 9816 11640 8353 180 581 -843 C ATOM 973 CG1 VAL A 152 -14.916 -1.080 30.319 1.00 78.96 C ANISOU 973 CG1 VAL A 152 9835 11725 8439 -60 720 -928 C ATOM 974 CG2 VAL A 152 -15.544 0.703 28.675 1.00 79.75 C ANISOU 974 CG2 VAL A 152 9762 12149 8390 350 530 -942 C ATOM 975 N ILE A 153 -11.307 0.053 30.430 1.00 69.94 N ANISOU 975 N ILE A 153 9260 9833 7482 134 538 -530 N ATOM 976 CA ILE A 153 -10.143 -0.535 31.109 1.00 68.76 C ANISOU 976 CA ILE A 153 9294 9413 7420 25 568 -437 C ATOM 977 C ILE A 153 -9.578 0.481 32.131 1.00 72.87 C ANISOU 977 C ILE A 153 9969 9781 7938 155 521 -334 C ATOM 978 O ILE A 153 -9.303 0.102 33.270 1.00 72.45 O ANISOU 978 O ILE A 153 10013 9608 7908 85 576 -300 O ATOM 979 CB ILE A 153 -9.050 -1.010 30.090 1.00 70.96 C ANISOU 979 CB ILE A 153 9633 9564 7764 -28 530 -389 C ATOM 980 CG1 ILE A 153 -9.537 -2.167 29.164 1.00 72.05 C ANISOU 980 CG1 ILE A 153 9641 9827 7909 -188 592 -498 C ATOM 981 CG2 ILE A 153 -7.719 -1.373 30.770 1.00 70.91 C ANISOU 981 CG2 ILE A 153 9818 9294 7832 -81 537 -278 C ATOM 982 CD1 ILE A 153 -9.776 -3.574 29.794 1.00 83.51 C ANISOU 982 CD1 ILE A 153 11110 11228 9390 -412 733 -556 C ATOM 983 N ILE A 154 -9.457 1.768 31.730 1.00 69.78 N ANISOU 983 N ILE A 154 9607 9398 7507 345 429 -291 N ATOM 984 CA ILE A 154 -8.922 2.854 32.561 1.00 69.71 C ANISOU 984 CA ILE A 154 9753 9246 7487 467 385 -206 C ATOM 985 C ILE A 154 -9.806 3.096 33.804 1.00 75.88 C ANISOU 985 C ILE A 154 10517 10098 8215 500 438 -243 C ATOM 986 O ILE A 154 -9.270 3.093 34.913 1.00 74.74 O ANISOU 986 O ILE A 154 10498 9806 8094 465 457 -191 O ATOM 987 CB ILE A 154 -8.695 4.158 31.740 1.00 72.76 C ANISOU 987 CB ILE A 154 10191 9622 7832 656 297 -161 C ATOM 988 CG1 ILE A 154 -7.503 3.990 30.769 1.00 72.01 C ANISOU 988 CG1 ILE A 154 10164 9398 7800 608 249 -100 C ATOM 989 CG2 ILE A 154 -8.479 5.376 32.656 1.00 73.01 C ANISOU 989 CG2 ILE A 154 10373 9539 7828 786 272 -105 C ATOM 990 CD1 ILE A 154 -7.600 4.792 29.484 1.00 76.93 C ANISOU 990 CD1 ILE A 154 10769 10088 8374 752 188 -91 C ATOM 991 N LEU A 155 -11.137 3.292 33.637 1.00 75.08 N ANISOU 991 N LEU A 155 10255 10236 8037 571 462 -336 N ATOM 992 CA LEU A 155 -12.015 3.526 34.793 1.00 76.50 C ANISOU 992 CA LEU A 155 10406 10502 8160 607 518 -378 C ATOM 993 C LEU A 155 -12.054 2.290 35.709 1.00 81.88 C ANISOU 993 C LEU A 155 11089 11140 8884 395 623 -403 C ATOM 994 O LEU A 155 -12.165 2.461 36.921 1.00 81.69 O ANISOU 994 O LEU A 155 11137 11061 8840 402 663 -385 O ATOM 995 CB LEU A 155 -13.439 3.997 34.417 1.00 78.23 C ANISOU 995 CB LEU A 155 10434 11017 8274 740 522 -478 C ATOM 996 CG LEU A 155 -14.245 3.186 33.405 1.00 84.33 C ANISOU 996 CG LEU A 155 10980 12037 9023 652 549 -594 C ATOM 997 CD1 LEU A 155 -15.259 2.288 34.100 1.00 85.74 C ANISOU 997 CD1 LEU A 155 11011 12387 9179 492 665 -707 C ATOM 998 CD2 LEU A 155 -14.968 4.108 32.439 1.00 88.23 C ANISOU 998 CD2 LEU A 155 11355 12753 9417 880 478 -633 C ATOM 999 N MET A 156 -11.874 1.071 35.143 1.00 79.72 N ANISOU 999 N MET A 156 10764 10862 8664 213 672 -435 N ATOM 1000 CA MET A 156 -11.837 -0.181 35.905 1.00 80.44 C ANISOU 1000 CA MET A 156 10892 10879 8792 9 787 -451 C ATOM 1001 C MET A 156 -10.613 -0.259 36.806 1.00 81.99 C ANISOU 1001 C MET A 156 11303 10812 9036 -3 778 -331 C ATOM 1002 O MET A 156 -10.755 -0.722 37.938 1.00 82.16 O ANISOU 1002 O MET A 156 11388 10781 9047 -74 861 -324 O ATOM 1003 CB MET A 156 -11.887 -1.403 34.995 1.00 83.69 C ANISOU 1003 CB MET A 156 11225 11331 9243 -171 845 -515 C ATOM 1004 CG MET A 156 -13.283 -1.866 34.724 1.00 90.09 C ANISOU 1004 CG MET A 156 11825 12409 9997 -266 928 -666 C ATOM 1005 SD MET A 156 -13.283 -3.481 33.928 1.00 96.24 S ANISOU 1005 SD MET A 156 12558 13186 10822 -533 1033 -750 S ATOM 1006 CE MET A 156 -13.347 -4.543 35.369 1.00 93.67 C ANISOU 1006 CE MET A 156 12369 12711 10511 -725 1205 -742 C ATOM 1007 N VAL A 157 -9.427 0.216 36.344 1.00 76.25 N ANISOU 1007 N VAL A 157 10684 9935 8354 71 679 -241 N ATOM 1008 CA VAL A 157 -8.233 0.196 37.198 1.00 74.80 C ANISOU 1008 CA VAL A 157 10683 9537 8203 68 660 -138 C ATOM 1009 C VAL A 157 -8.441 1.177 38.366 1.00 77.80 C ANISOU 1009 C VAL A 157 11129 9903 8528 178 643 -117 C ATOM 1010 O VAL A 157 -8.035 0.858 39.475 1.00 77.74 O ANISOU 1010 O VAL A 157 11229 9792 8516 140 680 -73 O ATOM 1011 CB VAL A 157 -6.849 0.399 36.502 1.00 77.78 C ANISOU 1011 CB VAL A 157 11148 9769 8634 96 568 -56 C ATOM 1012 CG1 VAL A 157 -6.698 -0.468 35.258 1.00 77.51 C ANISOU 1012 CG1 VAL A 157 11044 9761 8647 6 580 -83 C ATOM 1013 CG2 VAL A 157 -6.546 1.859 36.192 1.00 77.42 C ANISOU 1013 CG2 VAL A 157 11138 9711 8567 250 464 -24 C ATOM 1014 N TRP A 158 -9.125 2.321 38.129 1.00 73.46 N ANISOU 1014 N TRP A 158 10520 9466 7926 322 596 -150 N ATOM 1015 CA TRP A 158 -9.398 3.344 39.140 1.00 73.08 C ANISOU 1015 CA TRP A 158 10540 9409 7818 443 582 -140 C ATOM 1016 C TRP A 158 -10.475 2.902 40.141 1.00 76.94 C ANISOU 1016 C TRP A 158 10964 10012 8257 397 685 -201 C ATOM 1017 O TRP A 158 -10.367 3.246 41.316 1.00 76.44 O ANISOU 1017 O TRP A 158 11001 9882 8163 430 700 -173 O ATOM 1018 CB TRP A 158 -9.786 4.669 38.476 1.00 72.16 C ANISOU 1018 CB TRP A 158 10400 9365 7653 628 511 -153 C ATOM 1019 CG TRP A 158 -8.603 5.417 37.936 1.00 72.24 C ANISOU 1019 CG TRP A 158 10542 9213 7695 684 421 -77 C ATOM 1020 CD1 TRP A 158 -8.011 5.247 36.720 1.00 74.51 C ANISOU 1020 CD1 TRP A 158 10811 9472 8028 660 375 -55 C ATOM 1021 CD2 TRP A 158 -7.832 6.413 38.623 1.00 71.88 C ANISOU 1021 CD2 TRP A 158 10668 9009 7633 752 377 -22 C ATOM 1022 NE1 TRP A 158 -6.938 6.097 36.592 1.00 73.34 N ANISOU 1022 NE1 TRP A 158 10809 9163 7893 708 309 13 N ATOM 1023 CE2 TRP A 158 -6.802 6.822 37.747 1.00 75.14 C ANISOU 1023 CE2 TRP A 158 11155 9308 8084 758 310 29 C ATOM 1024 CE3 TRP A 158 -7.923 7.017 39.891 1.00 73.42 C ANISOU 1024 CE3 TRP A 158 10962 9154 7781 803 393 -19 C ATOM 1025 CZ2 TRP A 158 -5.869 7.806 38.098 1.00 74.28 C ANISOU 1025 CZ2 TRP A 158 11214 9041 7968 794 264 76 C ATOM 1026 CZ3 TRP A 158 -6.994 7.985 40.241 1.00 74.46 C ANISOU 1026 CZ3 TRP A 158 11261 9126 7904 845 341 27 C ATOM 1027 CH2 TRP A 158 -5.981 8.369 39.354 1.00 74.54 C ANISOU 1027 CH2 TRP A 158 11340 9028 7953 832 281 70 C ATOM 1028 N ILE A 159 -11.492 2.134 39.692 1.00 74.29 N ANISOU 1028 N ILE A 159 10462 9854 7910 309 760 -291 N ATOM 1029 CA ILE A 159 -12.564 1.607 40.554 1.00 75.24 C ANISOU 1029 CA ILE A 159 10504 10103 7983 232 877 -364 C ATOM 1030 C ILE A 159 -11.982 0.495 41.461 1.00 78.76 C ANISOU 1030 C ILE A 159 11076 10386 8463 70 965 -316 C ATOM 1031 O ILE A 159 -12.217 0.516 42.672 1.00 78.58 O ANISOU 1031 O ILE A 159 11118 10341 8398 69 1023 -306 O ATOM 1032 CB ILE A 159 -13.801 1.119 39.726 1.00 79.28 C ANISOU 1032 CB ILE A 159 10785 10875 8464 166 934 -492 C ATOM 1033 CG1 ILE A 159 -14.539 2.312 39.076 1.00 79.91 C ANISOU 1033 CG1 ILE A 159 10739 11149 8474 376 854 -539 C ATOM 1034 CG2 ILE A 159 -14.781 0.295 40.591 1.00 81.31 C ANISOU 1034 CG2 ILE A 159 10965 11247 8682 18 1082 -574 C ATOM 1035 CD1 ILE A 159 -15.370 1.966 37.855 1.00 86.32 C ANISOU 1035 CD1 ILE A 159 11330 12209 9261 346 859 -647 C ATOM 1036 N VAL A 160 -11.216 -0.453 40.875 1.00 74.64 N ANISOU 1036 N VAL A 160 10602 9752 8008 -50 976 -283 N ATOM 1037 CA VAL A 160 -10.591 -1.562 41.607 1.00 74.54 C ANISOU 1037 CA VAL A 160 10729 9574 8019 -178 1061 -227 C ATOM 1038 C VAL A 160 -9.467 -1.013 42.526 1.00 77.36 C ANISOU 1038 C VAL A 160 11266 9757 8372 -76 989 -116 C ATOM 1039 O VAL A 160 -9.373 -1.467 43.667 1.00 77.06 O ANISOU 1039 O VAL A 160 11334 9645 8301 -113 1062 -81 O ATOM 1040 CB VAL A 160 -10.103 -2.699 40.660 1.00 78.35 C ANISOU 1040 CB VAL A 160 11217 9988 8565 -312 1096 -226 C ATOM 1041 CG1 VAL A 160 -9.325 -3.774 41.415 1.00 78.13 C ANISOU 1041 CG1 VAL A 160 11371 9767 8550 -401 1179 -150 C ATOM 1042 CG2 VAL A 160 -11.281 -3.335 39.927 1.00 79.35 C ANISOU 1042 CG2 VAL A 160 11169 10298 8682 -446 1188 -356 C ATOM 1043 N SER A 161 -8.654 -0.027 42.050 1.00 73.04 N ANISOU 1043 N SER A 161 10751 9154 7845 46 854 -68 N ATOM 1044 CA SER A 161 -7.589 0.593 42.858 1.00 72.15 C ANISOU 1044 CA SER A 161 10788 8903 7720 129 780 16 C ATOM 1045 C SER A 161 -8.182 1.415 43.998 1.00 77.47 C ANISOU 1045 C SER A 161 11491 9621 8322 213 791 -2 C ATOM 1046 O SER A 161 -7.648 1.379 45.103 1.00 77.37 O ANISOU 1046 O SER A 161 11600 9520 8278 223 798 48 O ATOM 1047 CB SER A 161 -6.666 1.467 42.014 1.00 73.52 C ANISOU 1047 CB SER A 161 10984 9020 7930 211 651 53 C ATOM 1048 OG SER A 161 -5.873 0.682 41.142 1.00 78.93 O ANISOU 1048 OG SER A 161 11670 9641 8678 139 637 84 O ATOM 1049 N GLY A 162 -9.292 2.107 43.727 1.00 74.60 N ANISOU 1049 N GLY A 162 11015 9406 7925 282 797 -74 N ATOM 1050 CA GLY A 162 -10.020 2.898 44.713 1.00 75.14 C ANISOU 1050 CA GLY A 162 11094 9539 7918 374 817 -104 C ATOM 1051 C GLY A 162 -10.606 2.037 45.813 1.00 80.50 C ANISOU 1051 C GLY A 162 11781 10247 8556 280 943 -122 C ATOM 1052 O GLY A 162 -10.676 2.463 46.966 1.00 80.85 O ANISOU 1052 O GLY A 162 11908 10269 8543 334 959 -108 O ATOM 1053 N LEU A 163 -10.993 0.802 45.464 1.00 77.48 N ANISOU 1053 N LEU A 163 11332 9907 8202 129 1042 -153 N ATOM 1054 CA LEU A 163 -11.561 -0.172 46.386 1.00 78.37 C ANISOU 1054 CA LEU A 163 11465 10033 8277 8 1188 -171 C ATOM 1055 C LEU A 163 -10.473 -0.816 47.243 1.00 82.07 C ANISOU 1055 C LEU A 163 12130 10307 8745 -27 1207 -69 C ATOM 1056 O LEU A 163 -10.678 -0.980 48.440 1.00 82.76 O ANISOU 1056 O LEU A 163 12301 10374 8772 -32 1280 -52 O ATOM 1057 CB LEU A 163 -12.343 -1.236 45.603 1.00 79.24 C ANISOU 1057 CB LEU A 163 11445 10250 8413 -157 1296 -252 C ATOM 1058 CG LEU A 163 -13.879 -1.145 45.629 1.00 85.82 C ANISOU 1058 CG LEU A 163 12092 11325 9191 -193 1384 -377 C ATOM 1059 CD1 LEU A 163 -14.393 0.267 45.320 1.00 85.92 C ANISOU 1059 CD1 LEU A 163 11991 11489 9165 2 1277 -417 C ATOM 1060 CD2 LEU A 163 -14.485 -2.121 44.648 1.00 90.23 C ANISOU 1060 CD2 LEU A 163 12510 11995 9779 -366 1468 -469 C ATOM 1061 N THR A 164 -9.315 -1.151 46.654 1.00 77.34 N ANISOU 1061 N THR A 164 11603 9580 8205 -34 1139 -2 N ATOM 1062 CA THR A 164 -8.205 -1.771 47.387 1.00 76.93 C ANISOU 1062 CA THR A 164 11725 9364 8140 -39 1145 96 C ATOM 1063 C THR A 164 -7.372 -0.723 48.160 1.00 81.12 C ANISOU 1063 C THR A 164 12349 9842 8632 97 1028 149 C ATOM 1064 O THR A 164 -6.534 -1.105 48.985 1.00 81.12 O ANISOU 1064 O THR A 164 12483 9745 8594 118 1027 222 O ATOM 1065 CB THR A 164 -7.306 -2.590 46.444 1.00 83.52 C ANISOU 1065 CB THR A 164 12590 10103 9042 -93 1125 139 C ATOM 1066 OG1 THR A 164 -6.784 -1.741 45.422 1.00 83.31 O ANISOU 1066 OG1 THR A 164 12492 10093 9068 -24 987 136 O ATOM 1067 CG2 THR A 164 -8.020 -3.791 45.835 1.00 81.98 C ANISOU 1067 CG2 THR A 164 12345 9929 8875 -251 1262 87 C ATOM 1068 N SER A 165 -7.598 0.585 47.900 1.00 77.26 N ANISOU 1068 N SER A 165 11796 9419 8142 193 935 109 N ATOM 1069 CA SER A 165 -6.852 1.658 48.562 1.00 76.82 C ANISOU 1069 CA SER A 165 11831 9311 8048 301 832 140 C ATOM 1070 C SER A 165 -7.651 2.356 49.662 1.00 81.81 C ANISOU 1070 C SER A 165 12483 10003 8598 366 868 102 C ATOM 1071 O SER A 165 -7.068 2.687 50.694 1.00 81.53 O ANISOU 1071 O SER A 165 12560 9912 8505 413 838 136 O ATOM 1072 CB SER A 165 -6.371 2.694 47.552 1.00 78.93 C ANISOU 1072 CB SER A 165 12063 9568 8361 365 710 129 C ATOM 1073 OG SER A 165 -5.518 2.096 46.589 1.00 84.93 O ANISOU 1073 OG SER A 165 12810 10269 9189 311 672 167 O ATOM 1074 N PHE A 166 -8.962 2.588 49.450 1.00 79.12 N ANISOU 1074 N PHE A 166 12026 9792 8244 375 929 28 N ATOM 1075 CA PHE A 166 -9.808 3.283 50.424 1.00 79.86 C ANISOU 1075 CA PHE A 166 12125 9962 8258 450 968 -16 C ATOM 1076 C PHE A 166 -10.417 2.353 51.481 1.00 84.38 C ANISOU 1076 C PHE A 166 12722 10566 8774 370 1107 -17 C ATOM 1077 O PHE A 166 -10.410 2.724 52.655 1.00 84.17 O ANISOU 1077 O PHE A 166 12786 10522 8673 424 1121 -5 O ATOM 1078 CB PHE A 166 -10.921 4.070 49.724 1.00 82.20 C ANISOU 1078 CB PHE A 166 12280 10404 8547 528 964 -97 C ATOM 1079 CG PHE A 166 -10.504 5.453 49.283 1.00 83.39 C ANISOU 1079 CG PHE A 166 12474 10511 8698 668 845 -96 C ATOM 1080 CD1 PHE A 166 -9.693 5.631 48.167 1.00 85.52 C ANISOU 1080 CD1 PHE A 166 12749 10709 9037 666 756 -66 C ATOM 1081 CD2 PHE A 166 -10.935 6.579 49.973 1.00 86.32 C ANISOU 1081 CD2 PHE A 166 12897 10906 8996 799 834 -127 C ATOM 1082 CE1 PHE A 166 -9.304 6.911 47.761 1.00 86.21 C ANISOU 1082 CE1 PHE A 166 12900 10738 9117 782 665 -64 C ATOM 1083 CE2 PHE A 166 -10.551 7.861 49.562 1.00 89.11 C ANISOU 1083 CE2 PHE A 166 13323 11193 9342 922 743 -127 C ATOM 1084 CZ PHE A 166 -9.736 8.018 48.461 1.00 86.24 C ANISOU 1084 CZ PHE A 166 12973 10749 9046 908 662 -94 C ATOM 1085 N LEU A 167 -10.950 1.174 51.082 1.00 81.59 N ANISOU 1085 N LEU A 167 12298 10255 8450 235 1219 -36 N ATOM 1086 CA LEU A 167 -11.586 0.220 52.005 1.00 82.86 C ANISOU 1086 CA LEU A 167 12493 10435 8555 134 1377 -42 C ATOM 1087 C LEU A 167 -10.653 -0.268 53.138 1.00 86.78 C ANISOU 1087 C LEU A 167 13188 10783 9001 141 1394 55 C ATOM 1088 O LEU A 167 -11.103 -0.212 54.278 1.00 87.37 O ANISOU 1088 O LEU A 167 13319 10883 8993 158 1467 53 O ATOM 1089 CB LEU A 167 -12.191 -0.998 51.285 1.00 83.63 C ANISOU 1089 CB LEU A 167 12503 10578 8694 -37 1501 -84 C ATOM 1090 CG LEU A 167 -13.456 -0.773 50.452 1.00 89.28 C ANISOU 1090 CG LEU A 167 12998 11502 9423 -73 1536 -205 C ATOM 1091 CD1 LEU A 167 -13.705 -1.952 49.533 1.00 89.93 C ANISOU 1091 CD1 LEU A 167 13009 11602 9560 -253 1626 -245 C ATOM 1092 CD2 LEU A 167 -14.685 -0.546 51.341 1.00 93.30 C ANISOU 1092 CD2 LEU A 167 13436 12168 9847 -74 1643 -278 C ATOM 1093 N PRO A 168 -9.383 -0.711 52.920 1.00 82.38 N ANISOU 1093 N PRO A 168 12736 10089 8477 144 1329 139 N ATOM 1094 CA PRO A 168 -8.573 -1.171 54.064 1.00 82.33 C ANISOU 1094 CA PRO A 168 12908 9975 8397 177 1347 227 C ATOM 1095 C PRO A 168 -8.113 -0.045 54.999 1.00 86.04 C ANISOU 1095 C PRO A 168 13443 10452 8798 308 1243 237 C ATOM 1096 O PRO A 168 -7.624 -0.339 56.092 1.00 86.63 O ANISOU 1096 O PRO A 168 13652 10476 8788 346 1264 295 O ATOM 1097 CB PRO A 168 -7.378 -1.868 53.399 1.00 83.19 C ANISOU 1097 CB PRO A 168 13078 9972 8558 164 1293 300 C ATOM 1098 CG PRO A 168 -7.772 -2.064 51.971 1.00 87.25 C ANISOU 1098 CG PRO A 168 13455 10523 9173 82 1295 246 C ATOM 1099 CD PRO A 168 -8.638 -0.894 51.659 1.00 82.84 C ANISOU 1099 CD PRO A 168 12755 10095 8626 124 1245 158 C ATOM 1100 N ILE A 169 -8.300 1.230 54.602 1.00 81.58 N ANISOU 1100 N ILE A 169 12794 9946 8256 380 1142 178 N ATOM 1101 CA ILE A 169 -7.925 2.386 55.421 1.00 81.36 C ANISOU 1101 CA ILE A 169 12834 9917 8163 489 1053 169 C ATOM 1102 C ILE A 169 -9.176 2.947 56.149 1.00 87.47 C ANISOU 1102 C ILE A 169 13574 10791 8870 528 1130 102 C ATOM 1103 O ILE A 169 -9.102 3.196 57.357 1.00 87.84 O ANISOU 1103 O ILE A 169 13718 10832 8824 578 1144 113 O ATOM 1104 CB ILE A 169 -7.157 3.465 54.598 1.00 82.86 C ANISOU 1104 CB ILE A 169 13001 10075 8407 546 900 152 C ATOM 1105 CG1 ILE A 169 -5.740 2.944 54.231 1.00 81.90 C ANISOU 1105 CG1 ILE A 169 12931 9865 8320 520 822 221 C ATOM 1106 CG2 ILE A 169 -7.071 4.802 55.360 1.00 83.76 C ANISOU 1106 CG2 ILE A 169 13180 10193 8452 644 834 113 C ATOM 1107 CD1 ILE A 169 -4.986 3.709 53.139 1.00 86.76 C ANISOU 1107 CD1 ILE A 169 13506 10449 9009 532 698 209 C ATOM 1108 N GLN A 170 -10.307 3.126 55.425 1.00 84.75 N ANISOU 1108 N GLN A 170 13085 10554 8564 513 1179 31 N ATOM 1109 CA GLN A 170 -11.571 3.644 55.970 1.00 85.80 C ANISOU 1109 CA GLN A 170 13153 10813 8633 560 1254 -42 C ATOM 1110 C GLN A 170 -12.165 2.692 57.020 1.00 90.73 C ANISOU 1110 C GLN A 170 13817 11469 9187 480 1410 -31 C ATOM 1111 O GLN A 170 -12.667 3.156 58.046 1.00 90.68 O ANISOU 1111 O GLN A 170 13847 11513 9092 540 1452 -56 O ATOM 1112 CB GLN A 170 -12.588 3.893 54.841 1.00 87.39 C ANISOU 1112 CB GLN A 170 13169 11151 8883 563 1269 -120 C ATOM 1113 CG GLN A 170 -13.302 5.248 54.921 1.00106.48 C ANISOU 1113 CG GLN A 170 15540 13666 11253 718 1231 -188 C ATOM 1114 CD GLN A 170 -12.485 6.439 54.445 1.00127.60 C ANISOU 1114 CD GLN A 170 18290 16242 13950 836 1085 -173 C ATOM 1115 OE1 GLN A 170 -11.342 6.325 53.977 1.00120.67 O ANISOU 1115 OE1 GLN A 170 17480 15238 13131 797 1001 -118 O ATOM 1116 NE2 GLN A 170 -13.067 7.625 54.555 1.00123.16 N ANISOU 1116 NE2 GLN A 170 17724 15735 13335 984 1063 -225 N ATOM 1117 N MET A 171 -12.075 1.368 56.772 1.00 87.78 N ANISOU 1117 N MET A 171 13455 11053 8846 344 1502 7 N ATOM 1118 CA MET A 171 -12.562 0.324 57.679 1.00 89.17 C ANISOU 1118 CA MET A 171 13700 11227 8955 247 1671 27 C ATOM 1119 C MET A 171 -11.581 0.095 58.849 1.00 92.99 C ANISOU 1119 C MET A 171 14389 11585 9358 302 1656 123 C ATOM 1120 O MET A 171 -11.931 -0.589 59.818 1.00 93.84 O ANISOU 1120 O MET A 171 14589 11682 9384 258 1791 150 O ATOM 1121 CB MET A 171 -12.801 -0.996 56.921 1.00 92.01 C ANISOU 1121 CB MET A 171 14021 11564 9375 77 1787 28 C ATOM 1122 CG MET A 171 -13.936 -0.951 55.909 1.00 96.44 C ANISOU 1122 CG MET A 171 14366 12288 9990 -2 1833 -84 C ATOM 1123 SD MET A 171 -15.556 -0.557 56.611 1.00103.03 S ANISOU 1123 SD MET A 171 15067 13342 10739 -11 1960 -195 S ATOM 1124 CE MET A 171 -15.936 -2.097 57.474 1.00101.27 C ANISOU 1124 CE MET A 171 14963 13058 10457 -212 2199 -169 C ATOM 1125 N HIS A 172 -10.362 0.684 58.749 1.00 87.83 N ANISOU 1125 N HIS A 172 13802 10852 8719 399 1494 169 N ATOM 1126 CA HIS A 172 -9.241 0.646 59.703 1.00 87.30 C ANISOU 1126 CA HIS A 172 13899 10697 8572 474 1433 249 C ATOM 1127 C HIS A 172 -8.611 -0.757 59.795 1.00 89.24 C ANISOU 1127 C HIS A 172 14263 10841 8805 419 1507 345 C ATOM 1128 O HIS A 172 -8.060 -1.122 60.837 1.00 89.38 O ANISOU 1128 O HIS A 172 14428 10812 8719 476 1526 415 O ATOM 1129 CB HIS A 172 -9.637 1.173 61.103 1.00 89.38 C ANISOU 1129 CB HIS A 172 14239 11009 8711 546 1470 233 C ATOM 1130 CG HIS A 172 -10.197 2.562 61.101 1.00 92.89 C ANISOU 1130 CG HIS A 172 14601 11538 9154 623 1404 143 C ATOM 1131 ND1 HIS A 172 -11.416 2.845 61.688 1.00 95.87 N ANISOU 1131 ND1 HIS A 172 14933 12018 9474 633 1508 81 N ATOM 1132 CD2 HIS A 172 -9.694 3.700 60.568 1.00 93.96 C ANISOU 1132 CD2 HIS A 172 14706 11663 9331 696 1257 107 C ATOM 1133 CE1 HIS A 172 -11.610 4.141 61.505 1.00 95.22 C ANISOU 1133 CE1 HIS A 172 14801 11981 9398 730 1418 14 C ATOM 1134 NE2 HIS A 172 -10.605 4.695 60.827 1.00 94.39 N ANISOU 1134 NE2 HIS A 172 14712 11799 9351 765 1271 27 N ATOM 1135 N TRP A 173 -8.628 -1.504 58.673 1.00 83.89 N ANISOU 1135 N TRP A 173 13526 10126 8224 324 1541 350 N ATOM 1136 CA TRP A 173 -8.030 -2.836 58.555 1.00 83.49 C ANISOU 1136 CA TRP A 173 13592 9959 8170 276 1616 437 C ATOM 1137 C TRP A 173 -6.495 -2.772 58.593 1.00 83.73 C ANISOU 1137 C TRP A 173 13708 9923 8184 388 1470 516 C ATOM 1138 O TRP A 173 -5.844 -3.769 58.899 1.00 83.67 O ANISOU 1138 O TRP A 173 13839 9826 8124 410 1521 607 O ATOM 1139 CB TRP A 173 -8.477 -3.510 57.244 1.00 82.48 C ANISOU 1139 CB TRP A 173 13364 9820 8156 142 1680 401 C ATOM 1140 CG TRP A 173 -9.949 -3.796 57.117 1.00 84.86 C ANISOU 1140 CG TRP A 173 13567 10207 8468 5 1838 314 C ATOM 1141 CD1 TRP A 173 -10.870 -3.861 58.124 1.00 89.09 C ANISOU 1141 CD1 TRP A 173 14132 10801 8919 -27 1970 287 C ATOM 1142 CD2 TRP A 173 -10.647 -4.141 55.913 1.00 84.63 C ANISOU 1142 CD2 TRP A 173 13390 10232 8533 -127 1890 237 C ATOM 1143 NE1 TRP A 173 -12.104 -4.201 57.616 1.00 89.37 N ANISOU 1143 NE1 TRP A 173 14034 10934 8990 -177 2101 192 N ATOM 1144 CE2 TRP A 173 -11.996 -4.375 56.261 1.00 89.99 C ANISOU 1144 CE2 TRP A 173 13999 11018 9176 -241 2051 156 C ATOM 1145 CE3 TRP A 173 -10.262 -4.277 54.567 1.00 84.94 C ANISOU 1145 CE3 TRP A 173 13342 10254 8677 -163 1816 222 C ATOM 1146 CZ2 TRP A 173 -12.968 -4.708 55.308 1.00 89.76 C ANISOU 1146 CZ2 TRP A 173 13801 11095 9207 -390 2133 52 C ATOM 1147 CZ3 TRP A 173 -11.225 -4.601 53.624 1.00 86.81 C ANISOU 1147 CZ3 TRP A 173 13425 10584 8974 -303 1895 125 C ATOM 1148 CH2 TRP A 173 -12.559 -4.817 53.996 1.00 88.83 C ANISOU 1148 CH2 TRP A 173 13602 10961 9189 -416 2050 38 C ATOM 1149 N TYR A 174 -5.928 -1.606 58.257 1.00 77.67 N ANISOU 1149 N TYR A 174 12858 9202 7451 457 1297 479 N ATOM 1150 CA TYR A 174 -4.489 -1.348 58.213 1.00 76.19 C ANISOU 1150 CA TYR A 174 12711 8989 7250 546 1146 525 C ATOM 1151 C TYR A 174 -3.892 -1.143 59.610 1.00 80.58 C ANISOU 1151 C TYR A 174 13388 9566 7662 654 1110 565 C ATOM 1152 O TYR A 174 -2.699 -1.377 59.796 1.00 79.60 O ANISOU 1152 O TYR A 174 13324 9432 7490 730 1026 622 O ATOM 1153 CB TYR A 174 -4.217 -0.095 57.347 1.00 75.76 C ANISOU 1153 CB TYR A 174 12529 8975 7279 554 996 454 C ATOM 1154 CG TYR A 174 -4.490 1.222 58.048 1.00 77.35 C ANISOU 1154 CG TYR A 174 12723 9239 7428 610 934 388 C ATOM 1155 CD1 TYR A 174 -5.792 1.693 58.207 1.00 79.52 C ANISOU 1155 CD1 TYR A 174 12944 9566 7702 592 1011 322 C ATOM 1156 CD2 TYR A 174 -3.455 1.977 58.588 1.00 77.97 C ANISOU 1156 CD2 TYR A 174 12849 9332 7445 680 807 384 C ATOM 1157 CE1 TYR A 174 -6.052 2.894 58.865 1.00 79.89 C ANISOU 1157 CE1 TYR A 174 13002 9659 7693 658 964 262 C ATOM 1158 CE2 TYR A 174 -3.704 3.169 59.266 1.00 79.10 C ANISOU 1158 CE2 TYR A 174 13007 9516 7531 724 763 317 C ATOM 1159 CZ TYR A 174 -5.004 3.627 59.397 1.00 86.00 C ANISOU 1159 CZ TYR A 174 13844 10421 8409 719 843 260 C ATOM 1160 OH TYR A 174 -5.247 4.809 60.057 1.00 87.04 O ANISOU 1160 OH TYR A 174 14007 10584 8481 775 805 193 O ATOM 1161 N ARG A 175 -4.717 -0.655 60.562 1.00 78.04 N ANISOU 1161 N ARG A 175 13090 9294 7267 668 1167 525 N ATOM 1162 CA ARG A 175 -4.342 -0.271 61.923 1.00 78.79 C ANISOU 1162 CA ARG A 175 13287 9429 7219 766 1133 540 C ATOM 1163 C ARG A 175 -3.643 -1.360 62.728 1.00 85.51 C ANISOU 1163 C ARG A 175 14294 10243 7952 839 1182 648 C ATOM 1164 O ARG A 175 -4.040 -2.530 62.712 1.00 85.47 O ANISOU 1164 O ARG A 175 14370 10165 7940 799 1331 712 O ATOM 1165 CB ARG A 175 -5.556 0.235 62.708 1.00 78.65 C ANISOU 1165 CB ARG A 175 13270 9464 7151 755 1224 482 C ATOM 1166 CG ARG A 175 -5.954 1.637 62.300 1.00 85.46 C ANISOU 1166 CG ARG A 175 14018 10381 8072 757 1136 377 C ATOM 1167 CD ARG A 175 -6.744 2.363 63.361 1.00 92.58 C ANISOU 1167 CD ARG A 175 14949 11346 8881 801 1180 322 C ATOM 1168 NE ARG A 175 -7.088 3.711 62.909 1.00101.04 N ANISOU 1168 NE ARG A 175 15934 12452 10004 822 1100 226 N ATOM 1169 CZ ARG A 175 -7.911 4.537 63.546 1.00116.87 C ANISOU 1169 CZ ARG A 175 17940 14513 11953 867 1133 159 C ATOM 1170 NH1 ARG A 175 -8.489 4.166 64.683 1.00105.94 N ANISOU 1170 NH1 ARG A 175 16625 13167 10461 885 1243 172 N ATOM 1171 NH2 ARG A 175 -8.164 5.741 63.051 1.00104.82 N ANISOU 1171 NH2 ARG A 175 16357 12999 10470 903 1064 80 N ATOM 1172 N ALA A 176 -2.589 -0.931 63.445 1.00 83.89 N ANISOU 1172 N ALA A 176 14137 10094 7644 949 1058 663 N ATOM 1173 CA ALA A 176 -1.772 -1.754 64.335 1.00 85.16 C ANISOU 1173 CA ALA A 176 14441 10258 7659 1066 1068 761 C ATOM 1174 C ALA A 176 -2.337 -1.702 65.760 1.00 90.97 C ANISOU 1174 C ALA A 176 15291 11029 8245 1121 1152 771 C ATOM 1175 O ALA A 176 -3.161 -0.830 66.066 1.00 90.23 O ANISOU 1175 O ALA A 176 15147 10975 8162 1077 1164 688 O ATOM 1176 CB ALA A 176 -0.326 -1.281 64.308 1.00 85.65 C ANISOU 1176 CB ALA A 176 14463 10402 7678 1154 880 754 C ATOM 1177 N THR A 177 -1.902 -2.639 66.622 1.00 89.19 N ANISOU 1177 N THR A 177 15226 10788 7872 1229 1214 875 N ATOM 1178 CA THR A 177 -2.395 -2.778 67.993 1.00 90.53 C ANISOU 1178 CA THR A 177 15532 10982 7884 1291 1313 904 C ATOM 1179 C THR A 177 -1.369 -2.355 69.075 1.00 95.27 C ANISOU 1179 C THR A 177 16186 11705 8306 1452 1180 914 C ATOM 1180 O THR A 177 -1.650 -2.529 70.268 1.00 96.33 O ANISOU 1180 O THR A 177 16448 11867 8286 1527 1254 950 O ATOM 1181 CB THR A 177 -2.829 -4.234 68.215 1.00102.09 C ANISOU 1181 CB THR A 177 17170 12324 9295 1291 1521 1020 C ATOM 1182 OG1 THR A 177 -1.788 -5.104 67.762 1.00104.02 O ANISOU 1182 OG1 THR A 177 17479 12518 9525 1378 1487 1113 O ATOM 1183 CG2 THR A 177 -4.143 -4.570 67.515 1.00 99.72 C ANISOU 1183 CG2 THR A 177 16823 11935 9129 1107 1688 982 C ATOM 1184 N HIS A 178 -0.201 -1.800 68.682 1.00 90.95 N ANISOU 1184 N HIS A 178 15541 11245 7772 1497 990 877 N ATOM 1185 CA HIS A 178 0.807 -1.388 69.666 1.00 91.55 C ANISOU 1185 CA HIS A 178 15643 11470 7673 1635 857 866 C ATOM 1186 C HIS A 178 0.611 0.073 70.086 1.00 94.08 C ANISOU 1186 C HIS A 178 15879 11882 7988 1581 759 727 C ATOM 1187 O HIS A 178 0.032 0.857 69.333 1.00 91.82 O ANISOU 1187 O HIS A 178 15487 11549 7853 1454 748 640 O ATOM 1188 CB HIS A 178 2.236 -1.643 69.176 1.00 92.36 C ANISOU 1188 CB HIS A 178 15688 11648 7756 1720 713 894 C ATOM 1189 CG HIS A 178 2.601 -0.905 67.935 1.00 94.38 C ANISOU 1189 CG HIS A 178 15767 11907 8186 1601 596 805 C ATOM 1190 ND1 HIS A 178 3.219 0.329 67.990 1.00 96.05 N ANISOU 1190 ND1 HIS A 178 15865 12241 8391 1565 435 684 N ATOM 1191 CD2 HIS A 178 2.448 -1.264 66.641 1.00 95.05 C ANISOU 1191 CD2 HIS A 178 15786 11884 8443 1511 627 822 C ATOM 1192 CE1 HIS A 178 3.416 0.686 66.732 1.00 94.13 C ANISOU 1192 CE1 HIS A 178 15497 11952 8314 1458 378 638 C ATOM 1193 NE2 HIS A 178 2.963 -0.238 65.884 1.00 93.78 N ANISOU 1193 NE2 HIS A 178 15471 11777 8382 1427 485 719 N ATOM 1194 N GLN A 179 1.075 0.412 71.312 1.00 91.80 N ANISOU 1194 N GLN A 179 15650 11721 7510 1688 696 709 N ATOM 1195 CA GLN A 179 0.942 1.720 71.964 1.00 91.48 C ANISOU 1195 CA GLN A 179 15571 11769 7418 1656 617 579 C ATOM 1196 C GLN A 179 1.353 2.892 71.068 1.00 91.83 C ANISOU 1196 C GLN A 179 15465 11831 7596 1540 480 451 C ATOM 1197 O GLN A 179 0.557 3.818 70.913 1.00 90.13 O ANISOU 1197 O GLN A 179 15219 11566 7462 1449 502 361 O ATOM 1198 CB GLN A 179 1.711 1.769 73.298 1.00 94.86 C ANISOU 1198 CB GLN A 179 16073 12361 7609 1799 542 580 C ATOM 1199 CG GLN A 179 0.952 1.137 74.474 1.00114.02 C ANISOU 1199 CG GLN A 179 18668 14769 9885 1893 692 662 C ATOM 1200 CD GLN A 179 -0.352 1.835 74.812 1.00132.39 C ANISOU 1200 CD GLN A 179 21010 17036 12256 1801 793 590 C ATOM 1201 OE1 GLN A 179 -0.430 3.067 74.929 1.00126.36 O ANISOU 1201 OE1 GLN A 179 20178 16321 11510 1740 710 457 O ATOM 1202 NE2 GLN A 179 -1.413 1.056 74.959 1.00125.95 N ANISOU 1202 NE2 GLN A 179 20289 16113 11455 1786 984 673 N ATOM 1203 N GLU A 180 2.555 2.834 70.457 1.00 87.66 N ANISOU 1203 N GLU A 180 14851 11368 7087 1548 350 447 N ATOM 1204 CA GLU A 180 3.100 3.856 69.553 1.00 86.81 C ANISOU 1204 CA GLU A 180 14611 11275 7097 1431 226 333 C ATOM 1205 C GLU A 180 2.091 4.207 68.431 1.00 89.05 C ANISOU 1205 C GLU A 180 14846 11398 7590 1305 300 310 C ATOM 1206 O GLU A 180 1.934 5.384 68.096 1.00 87.88 O ANISOU 1206 O GLU A 180 14650 11229 7511 1213 251 198 O ATOM 1207 CB GLU A 180 4.433 3.357 68.957 1.00 88.42 C ANISOU 1207 CB GLU A 180 14733 11565 7297 1468 116 367 C ATOM 1208 CG GLU A 180 5.271 4.404 68.236 1.00101.73 C ANISOU 1208 CG GLU A 180 16287 13309 9056 1352 -24 242 C ATOM 1209 CD GLU A 180 6.081 5.365 69.090 1.00132.31 C ANISOU 1209 CD GLU A 180 20133 17356 12783 1339 -149 114 C ATOM 1210 OE1 GLU A 180 6.342 5.056 70.276 1.00128.60 O ANISOU 1210 OE1 GLU A 180 19723 17017 12122 1460 -164 132 O ATOM 1211 OE2 GLU A 180 6.486 6.421 68.552 1.00132.48 O ANISOU 1211 OE2 GLU A 180 20077 17386 12874 1204 -228 -9 O ATOM 1212 N ALA A 181 1.383 3.185 67.900 1.00 84.87 N ANISOU 1212 N ALA A 181 14340 10760 7145 1306 427 412 N ATOM 1213 CA ALA A 181 0.385 3.319 66.842 1.00 83.04 C ANISOU 1213 CA ALA A 181 14053 10405 7094 1202 506 398 C ATOM 1214 C ALA A 181 -0.949 3.897 67.349 1.00 87.05 C ANISOU 1214 C ALA A 181 14596 10880 7600 1176 606 346 C ATOM 1215 O ALA A 181 -1.335 4.975 66.900 1.00 85.83 O ANISOU 1215 O ALA A 181 14385 10702 7526 1115 573 251 O ATOM 1216 CB ALA A 181 0.146 1.974 66.180 1.00 83.31 C ANISOU 1216 CB ALA A 181 14101 10355 7198 1202 609 511 C ATOM 1217 N ILE A 182 -1.649 3.188 68.275 1.00 84.76 N ANISOU 1217 N ILE A 182 14405 10589 7212 1230 735 408 N ATOM 1218 CA ILE A 182 -2.968 3.569 68.819 1.00 84.96 C ANISOU 1218 CA ILE A 182 14460 10600 7221 1212 851 367 C ATOM 1219 C ILE A 182 -3.000 5.010 69.360 1.00 88.82 C ANISOU 1219 C ILE A 182 14945 11141 7660 1221 769 245 C ATOM 1220 O ILE A 182 -4.045 5.659 69.280 1.00 88.08 O ANISOU 1220 O ILE A 182 14828 11024 7613 1193 832 182 O ATOM 1221 CB ILE A 182 -3.521 2.571 69.875 1.00 89.47 C ANISOU 1221 CB ILE A 182 15156 11174 7664 1269 1001 454 C ATOM 1222 CG1 ILE A 182 -2.488 2.192 70.947 1.00 91.31 C ANISOU 1222 CG1 ILE A 182 15498 11484 7712 1392 941 510 C ATOM 1223 CG2 ILE A 182 -4.089 1.325 69.212 1.00 89.93 C ANISOU 1223 CG2 ILE A 182 15223 11141 7806 1212 1146 543 C ATOM 1224 CD1 ILE A 182 -2.566 2.970 72.219 1.00102.19 C ANISOU 1224 CD1 ILE A 182 16938 12953 8935 1454 913 447 C ATOM 1225 N ASN A 183 -1.868 5.501 69.896 1.00 86.11 N ANISOU 1225 N ASN A 183 14627 10877 7215 1260 636 205 N ATOM 1226 CA ASN A 183 -1.760 6.862 70.425 1.00 86.40 C ANISOU 1226 CA ASN A 183 14679 10955 7194 1252 558 78 C ATOM 1227 C ASN A 183 -1.658 7.885 69.300 1.00 89.54 C ANISOU 1227 C ASN A 183 14998 11288 7735 1164 487 -10 C ATOM 1228 O ASN A 183 -2.082 9.026 69.482 1.00 89.85 O ANISOU 1228 O ASN A 183 15064 11304 7769 1148 481 -111 O ATOM 1229 CB ASN A 183 -0.558 6.991 71.355 1.00 87.06 C ANISOU 1229 CB ASN A 183 14805 11163 7111 1306 443 53 C ATOM 1230 CG ASN A 183 -0.665 6.218 72.647 1.00108.19 C ANISOU 1230 CG ASN A 183 17585 13914 9608 1418 507 125 C ATOM 1231 OD1 ASN A 183 -1.737 6.079 73.250 1.00104.67 O ANISOU 1231 OD1 ASN A 183 17207 13439 9124 1445 634 145 O ATOM 1232 ND2 ASN A 183 0.468 5.735 73.126 1.00 99.49 N ANISOU 1232 ND2 ASN A 183 16497 12925 8378 1492 419 162 N ATOM 1233 N CYS A 184 -1.082 7.486 68.151 1.00 85.10 N ANISOU 1233 N CYS A 184 14353 10690 7292 1114 438 30 N ATOM 1234 CA CYS A 184 -0.935 8.348 66.978 1.00 84.14 C ANISOU 1234 CA CYS A 184 14163 10499 7307 1031 378 -37 C ATOM 1235 C CYS A 184 -2.295 8.510 66.273 1.00 87.57 C ANISOU 1235 C CYS A 184 14566 10846 7860 1020 483 -37 C ATOM 1236 O CYS A 184 -2.561 9.586 65.734 1.00 86.81 O ANISOU 1236 O CYS A 184 14464 10695 7826 992 461 -116 O ATOM 1237 CB CYS A 184 0.138 7.804 66.034 1.00 83.60 C ANISOU 1237 CB CYS A 184 14016 10437 7313 990 296 8 C ATOM 1238 SG CYS A 184 0.299 8.702 64.465 1.00 86.20 S ANISOU 1238 SG CYS A 184 14266 10670 7814 886 240 -53 S ATOM 1239 N TYR A 185 -3.162 7.464 66.305 1.00 84.10 N ANISOU 1239 N TYR A 185 14112 10403 7438 1043 604 45 N ATOM 1240 CA TYR A 185 -4.497 7.496 65.684 1.00 83.45 C ANISOU 1240 CA TYR A 185 13974 10282 7452 1030 710 38 C ATOM 1241 C TYR A 185 -5.438 8.458 66.414 1.00 87.62 C ANISOU 1241 C TYR A 185 14548 10828 7914 1080 761 -43 C ATOM 1242 O TYR A 185 -6.187 9.192 65.763 1.00 87.05 O ANISOU 1242 O TYR A 185 14432 10729 7915 1087 782 -98 O ATOM 1243 CB TYR A 185 -5.143 6.095 65.627 1.00 84.79 C ANISOU 1243 CB TYR A 185 14121 10455 7641 1015 839 131 C ATOM 1244 CG TYR A 185 -4.331 5.038 64.908 1.00 85.98 C ANISOU 1244 CG TYR A 185 14243 10573 7851 977 813 216 C ATOM 1245 CD1 TYR A 185 -3.884 5.240 63.604 1.00 86.76 C ANISOU 1245 CD1 TYR A 185 14255 10630 8080 926 737 205 C ATOM 1246 CD2 TYR A 185 -4.074 3.808 65.500 1.00 87.32 C ANISOU 1246 CD2 TYR A 185 14485 10747 7945 1002 879 312 C ATOM 1247 CE1 TYR A 185 -3.132 4.272 62.941 1.00 86.90 C ANISOU 1247 CE1 TYR A 185 14249 10621 8149 900 716 280 C ATOM 1248 CE2 TYR A 185 -3.328 2.830 64.846 1.00 87.61 C ANISOU 1248 CE2 TYR A 185 14512 10746 8028 987 862 392 C ATOM 1249 CZ TYR A 185 -2.860 3.065 63.564 1.00 92.90 C ANISOU 1249 CZ TYR A 185 15084 11384 8829 934 779 373 C ATOM 1250 OH TYR A 185 -2.132 2.095 62.916 1.00 91.35 O ANISOU 1250 OH TYR A 185 14880 11154 8675 926 767 449 O ATOM 1251 N ALA A 186 -5.394 8.446 67.761 1.00 84.69 N ANISOU 1251 N ALA A 186 14271 10511 7397 1130 783 -48 N ATOM 1252 CA ALA A 186 -6.207 9.287 68.640 1.00 85.22 C ANISOU 1252 CA ALA A 186 14398 10605 7376 1189 835 -123 C ATOM 1253 C ALA A 186 -5.799 10.762 68.547 1.00 88.52 C ANISOU 1253 C ALA A 186 14864 10981 7788 1194 738 -233 C ATOM 1254 O ALA A 186 -6.662 11.639 68.633 1.00 88.63 O ANISOU 1254 O ALA A 186 14902 10978 7796 1243 785 -302 O ATOM 1255 CB ALA A 186 -6.084 8.802 70.075 1.00 87.13 C ANISOU 1255 CB ALA A 186 14736 10916 7455 1237 873 -92 C ATOM 1256 N GLU A 187 -4.489 11.028 68.382 1.00 84.39 N ANISOU 1256 N GLU A 187 14360 10446 7260 1144 613 -253 N ATOM 1257 CA GLU A 187 -3.950 12.377 68.271 1.00 84.65 C ANISOU 1257 CA GLU A 187 14453 10427 7283 1114 529 -364 C ATOM 1258 C GLU A 187 -4.192 12.922 66.873 1.00 89.35 C ANISOU 1258 C GLU A 187 15000 10924 8026 1085 521 -380 C ATOM 1259 O GLU A 187 -3.810 12.286 65.887 1.00 88.36 O ANISOU 1259 O GLU A 187 14783 10783 8005 1036 492 -318 O ATOM 1260 CB GLU A 187 -2.454 12.398 68.610 1.00 86.18 C ANISOU 1260 CB GLU A 187 14667 10672 7408 1053 406 -390 C ATOM 1261 N GLU A 188 -4.839 14.098 66.784 1.00 87.29 N ANISOU 1261 N GLU A 188 14809 10594 7765 1128 552 -462 N ATOM 1262 CA GLU A 188 -5.107 14.762 65.503 1.00 86.91 C ANISOU 1262 CA GLU A 188 14742 10447 7833 1128 550 -480 C ATOM 1263 C GLU A 188 -3.818 15.415 64.973 1.00 91.93 C ANISOU 1263 C GLU A 188 15426 11007 8497 1022 446 -529 C ATOM 1264 O GLU A 188 -3.739 15.764 63.793 1.00 91.21 O ANISOU 1264 O GLU A 188 15314 10833 8508 998 430 -525 O ATOM 1265 CB GLU A 188 -6.241 15.796 65.637 1.00 89.05 C ANISOU 1265 CB GLU A 188 15091 10672 8073 1239 626 -546 C ATOM 1266 CG GLU A 188 -7.633 15.192 65.576 1.00 97.82 C ANISOU 1266 CG GLU A 188 16100 11863 9203 1334 732 -499 C ATOM 1267 CD GLU A 188 -8.110 14.549 66.864 1.00117.31 C ANISOU 1267 CD GLU A 188 18570 14438 11567 1365 800 -482 C ATOM 1268 N THR A 189 -2.806 15.552 65.858 1.00 89.46 N ANISOU 1268 N THR A 189 15169 10738 8082 956 379 -580 N ATOM 1269 CA THR A 189 -1.479 16.113 65.583 1.00 89.16 C ANISOU 1269 CA THR A 189 15165 10671 8042 831 282 -647 C ATOM 1270 C THR A 189 -0.579 15.105 64.846 1.00 89.65 C ANISOU 1270 C THR A 189 15091 10792 8181 761 213 -567 C ATOM 1271 O THR A 189 0.394 15.511 64.211 1.00 88.75 O ANISOU 1271 O THR A 189 14970 10647 8104 655 145 -609 O ATOM 1272 CB THR A 189 -0.809 16.549 66.900 1.00101.72 C ANISOU 1272 CB THR A 189 16843 12332 9476 791 239 -742 C ATOM 1273 OG1 THR A 189 -0.797 15.454 67.826 1.00102.19 O ANISOU 1273 OG1 THR A 189 16842 12535 9451 847 236 -674 O ATOM 1274 CG2 THR A 189 -1.480 17.764 67.526 1.00102.96 C ANISOU 1274 CG2 THR A 189 17161 12403 9556 836 299 -846 C ATOM 1275 N CYS A 190 -0.894 13.800 64.953 1.00 84.48 N ANISOU 1275 N CYS A 190 14340 10219 7540 818 240 -457 N ATOM 1276 CA CYS A 190 -0.119 12.713 64.357 1.00 83.25 C ANISOU 1276 CA CYS A 190 14070 10120 7442 779 189 -372 C ATOM 1277 C CYS A 190 -0.822 12.132 63.138 1.00 86.14 C ANISOU 1277 C CYS A 190 14350 10425 7954 797 243 -289 C ATOM 1278 O CYS A 190 -2.042 11.944 63.155 1.00 86.03 O ANISOU 1278 O CYS A 190 14330 10394 7962 867 336 -261 O ATOM 1279 CB CYS A 190 0.152 11.628 65.398 1.00 83.98 C ANISOU 1279 CB CYS A 190 14145 10338 7426 833 187 -309 C ATOM 1280 SG CYS A 190 1.367 10.383 64.885 1.00 87.20 S ANISOU 1280 SG CYS A 190 14444 10828 7860 809 111 -217 S ATOM 1281 N CYS A 191 -0.033 11.831 62.089 1.00 81.67 N ANISOU 1281 N CYS A 191 13708 9844 7479 730 184 -259 N ATOM 1282 CA CYS A 191 -0.470 11.191 60.843 1.00 80.14 C ANISOU 1282 CA CYS A 191 13422 9607 7420 730 219 -184 C ATOM 1283 C CYS A 191 0.685 10.329 60.286 1.00 83.02 C ANISOU 1283 C CYS A 191 13702 10017 7824 675 149 -127 C ATOM 1284 O CYS A 191 0.901 10.254 59.073 1.00 81.69 O ANISOU 1284 O CYS A 191 13472 9802 7766 631 130 -105 O ATOM 1285 CB CYS A 191 -0.972 12.215 59.826 1.00 79.97 C ANISOU 1285 CB CYS A 191 13421 9479 7486 722 234 -229 C ATOM 1286 SG CYS A 191 -1.889 11.503 58.429 1.00 82.51 S ANISOU 1286 SG CYS A 191 13626 9774 7949 751 294 -152 S ATOM 1287 N ASP A 192 1.431 9.679 61.198 1.00 80.18 N ANISOU 1287 N ASP A 192 13344 9758 7361 693 110 -103 N ATOM 1288 CA ASP A 192 2.503 8.760 60.840 1.00 79.64 C ANISOU 1288 CA ASP A 192 13202 9756 7303 679 49 -43 C ATOM 1289 C ASP A 192 1.846 7.453 60.446 1.00 82.15 C ANISOU 1289 C ASP A 192 13482 10049 7682 729 134 70 C ATOM 1290 O ASP A 192 0.989 6.949 61.179 1.00 81.38 O ANISOU 1290 O ASP A 192 13431 9955 7534 790 222 109 O ATOM 1291 CB ASP A 192 3.496 8.576 62.001 1.00 82.99 C ANISOU 1291 CB ASP A 192 13645 10316 7572 708 -21 -61 C ATOM 1292 CG ASP A 192 4.272 9.817 62.411 1.00 97.89 C ANISOU 1292 CG ASP A 192 15559 12249 9387 629 -106 -192 C ATOM 1293 OD1 ASP A 192 3.967 10.918 61.885 1.00 98.30 O ANISOU 1293 OD1 ASP A 192 15648 12197 9503 554 -97 -269 O ATOM 1294 OD2 ASP A 192 5.179 9.692 63.263 1.00106.67 O ANISOU 1294 OD2 ASP A 192 16661 13502 10367 643 -178 -222 O ATOM 1295 N PHE A 193 2.178 6.949 59.254 1.00 78.41 N ANISOU 1295 N PHE A 193 12931 9543 7318 693 120 115 N ATOM 1296 CA PHE A 193 1.572 5.731 58.741 1.00 77.80 C ANISOU 1296 CA PHE A 193 12823 9430 7308 717 206 209 C ATOM 1297 C PHE A 193 2.046 4.512 59.521 1.00 82.04 C ANISOU 1297 C PHE A 193 13397 10025 7748 789 226 293 C ATOM 1298 O PHE A 193 3.136 3.983 59.287 1.00 82.01 O ANISOU 1298 O PHE A 193 13362 10069 7728 807 162 330 O ATOM 1299 CB PHE A 193 1.836 5.568 57.240 1.00 78.59 C ANISOU 1299 CB PHE A 193 12837 9480 7544 659 183 226 C ATOM 1300 CG PHE A 193 0.926 4.610 56.503 1.00 79.82 C ANISOU 1300 CG PHE A 193 12957 9583 7790 654 284 287 C ATOM 1301 CD1 PHE A 193 -0.457 4.687 56.643 1.00 82.94 C ANISOU 1301 CD1 PHE A 193 13360 9953 8201 660 384 272 C ATOM 1302 CD2 PHE A 193 1.446 3.684 55.607 1.00 82.05 C ANISOU 1302 CD2 PHE A 193 13188 9848 8140 636 280 347 C ATOM 1303 CE1 PHE A 193 -1.297 3.817 55.940 1.00 83.49 C ANISOU 1303 CE1 PHE A 193 13380 9995 8348 632 480 309 C ATOM 1304 CE2 PHE A 193 0.602 2.842 54.874 1.00 84.50 C ANISOU 1304 CE2 PHE A 193 13466 10109 8533 610 377 386 C ATOM 1305 CZ PHE A 193 -0.764 2.918 55.044 1.00 82.53 C ANISOU 1305 CZ PHE A 193 13216 9846 8294 600 476 362 C ATOM 1306 N PHE A 194 1.233 4.121 60.505 1.00 78.43 N ANISOU 1306 N PHE A 194 13017 9570 7213 842 319 321 N ATOM 1307 CA PHE A 194 1.454 2.939 61.324 1.00 78.48 C ANISOU 1307 CA PHE A 194 13096 9608 7114 926 372 413 C ATOM 1308 C PHE A 194 0.519 1.866 60.814 1.00 82.11 C ANISOU 1308 C PHE A 194 13569 9980 7648 904 513 484 C ATOM 1309 O PHE A 194 -0.671 2.136 60.617 1.00 81.51 O ANISOU 1309 O PHE A 194 13473 9863 7632 852 596 449 O ATOM 1310 CB PHE A 194 1.228 3.229 62.819 1.00 81.04 C ANISOU 1310 CB PHE A 194 13514 9995 7284 992 390 394 C ATOM 1311 CG PHE A 194 2.324 4.015 63.497 1.00 82.78 C ANISOU 1311 CG PHE A 194 13732 10328 7393 1019 255 328 C ATOM 1312 CD1 PHE A 194 3.525 3.408 63.845 1.00 86.25 C ANISOU 1312 CD1 PHE A 194 14171 10868 7730 1097 180 373 C ATOM 1313 CD2 PHE A 194 2.139 5.350 63.832 1.00 84.78 C ANISOU 1313 CD2 PHE A 194 13988 10595 7628 973 208 215 C ATOM 1314 CE1 PHE A 194 4.535 4.132 64.484 1.00 87.84 C ANISOU 1314 CE1 PHE A 194 14350 11208 7818 1110 54 295 C ATOM 1315 CE2 PHE A 194 3.145 6.070 64.483 1.00 88.39 C ANISOU 1315 CE2 PHE A 194 14446 11163 7976 974 92 137 C ATOM 1316 CZ PHE A 194 4.339 5.458 64.797 1.00 87.05 C ANISOU 1316 CZ PHE A 194 14250 11116 7707 1035 12 173 C ATOM 1317 N THR A 195 1.061 0.678 60.516 1.00 78.53 N ANISOU 1317 N THR A 195 13142 9503 7193 938 540 574 N ATOM 1318 CA THR A 195 0.266 -0.430 59.989 1.00 78.11 C ANISOU 1318 CA THR A 195 13116 9355 7208 897 684 636 C ATOM 1319 C THR A 195 0.610 -1.758 60.639 1.00 82.75 C ANISOU 1319 C THR A 195 13838 9914 7689 986 768 747 C ATOM 1320 O THR A 195 1.708 -1.920 61.178 1.00 83.36 O ANISOU 1320 O THR A 195 13958 10057 7658 1097 686 787 O ATOM 1321 CB THR A 195 0.469 -0.589 58.469 1.00 86.28 C ANISOU 1321 CB THR A 195 14048 10341 8392 824 655 629 C ATOM 1322 OG1 THR A 195 1.837 -0.899 58.196 1.00 85.92 O ANISOU 1322 OG1 THR A 195 13993 10328 8323 885 555 670 O ATOM 1323 CG2 THR A 195 0.002 0.615 57.670 1.00 84.41 C ANISOU 1323 CG2 THR A 195 13696 10113 8264 744 596 533 C ATOM 1324 N ASN A 196 -0.315 -2.731 60.530 1.00 78.63 N ANISOU 1324 N ASN A 196 13386 9297 7193 936 938 793 N ATOM 1325 CA ASN A 196 -0.079 -4.104 60.964 1.00 78.76 C ANISOU 1325 CA ASN A 196 13562 9242 7121 1007 1052 907 C ATOM 1326 C ASN A 196 0.704 -4.807 59.844 1.00 82.45 C ANISOU 1326 C ASN A 196 14005 9655 7665 1013 1023 951 C ATOM 1327 O ASN A 196 0.574 -4.429 58.674 1.00 81.05 O ANISOU 1327 O ASN A 196 13695 9468 7631 913 977 892 O ATOM 1328 CB ASN A 196 -1.383 -4.827 61.310 1.00 76.03 C ANISOU 1328 CB ASN A 196 13313 8808 6767 925 1262 926 C ATOM 1329 CG ASN A 196 -2.419 -4.879 60.213 1.00 85.74 C ANISOU 1329 CG ASN A 196 14436 9989 8151 756 1344 860 C ATOM 1330 OD1 ASN A 196 -2.252 -5.530 59.181 1.00 74.18 O ANISOU 1330 OD1 ASN A 196 12951 8456 6777 701 1371 877 O ATOM 1331 ND2 ASN A 196 -3.566 -4.288 60.469 1.00 79.03 N ANISOU 1331 ND2 ASN A 196 13524 9184 7320 676 1402 784 N ATOM 1332 N GLN A 197 1.515 -5.812 60.197 1.00 79.53 N ANISOU 1332 N GLN A 197 13770 9256 7193 1143 1050 1056 N ATOM 1333 CA GLN A 197 2.384 -6.533 59.265 1.00 78.39 C ANISOU 1333 CA GLN A 197 13622 9069 7094 1185 1022 1107 C ATOM 1334 C GLN A 197 1.609 -7.228 58.114 1.00 80.51 C ANISOU 1334 C GLN A 197 13885 9200 7507 1037 1152 1099 C ATOM 1335 O GLN A 197 2.179 -7.384 57.035 1.00 79.32 O ANISOU 1335 O GLN A 197 13659 9035 7445 1022 1093 1095 O ATOM 1336 CB GLN A 197 3.274 -7.528 60.035 1.00 81.36 C ANISOU 1336 CB GLN A 197 14174 9439 7301 1385 1050 1229 C ATOM 1337 CG GLN A 197 4.441 -6.823 60.744 1.00 96.66 C ANISOU 1337 CG GLN A 197 16048 11563 9113 1537 866 1219 C ATOM 1338 CD GLN A 197 4.990 -7.568 61.930 1.00116.60 C ANISOU 1338 CD GLN A 197 18753 14122 11427 1750 902 1326 C ATOM 1339 N ALA A 198 0.315 -7.570 58.311 1.00 77.02 N ANISOU 1339 N ALA A 198 13503 8675 7086 917 1321 1082 N ATOM 1340 CA ALA A 198 -0.523 -8.220 57.291 1.00 76.31 C ANISOU 1340 CA ALA A 198 13398 8478 7119 754 1455 1053 C ATOM 1341 C ALA A 198 -0.902 -7.259 56.158 1.00 78.21 C ANISOU 1341 C ALA A 198 13413 8789 7516 631 1354 941 C ATOM 1342 O ALA A 198 -0.825 -7.652 54.993 1.00 77.41 O ANISOU 1342 O ALA A 198 13256 8639 7517 561 1363 927 O ATOM 1343 CB ALA A 198 -1.779 -8.800 57.921 1.00 78.23 C ANISOU 1343 CB ALA A 198 13756 8646 7322 651 1666 1052 C ATOM 1344 N TYR A 199 -1.310 -6.012 56.495 1.00 73.42 N ANISOU 1344 N TYR A 199 12688 8290 6917 615 1266 864 N ATOM 1345 CA TYR A 199 -1.675 -4.988 55.515 1.00 71.49 C ANISOU 1345 CA TYR A 199 12252 8113 6799 530 1171 764 C ATOM 1346 C TYR A 199 -0.435 -4.577 54.695 1.00 75.70 C ANISOU 1346 C TYR A 199 12704 8675 7384 585 1004 769 C ATOM 1347 O TYR A 199 -0.513 -4.507 53.468 1.00 74.66 O ANISOU 1347 O TYR A 199 12467 8531 7367 510 978 731 O ATOM 1348 CB TYR A 199 -2.332 -3.757 56.194 1.00 71.93 C ANISOU 1348 CB TYR A 199 12241 8262 6827 531 1126 691 C ATOM 1349 CG TYR A 199 -2.533 -2.569 55.268 1.00 71.90 C ANISOU 1349 CG TYR A 199 12069 8321 6928 488 1012 600 C ATOM 1350 CD1 TYR A 199 -3.682 -2.445 54.494 1.00 73.22 C ANISOU 1350 CD1 TYR A 199 12129 8508 7182 385 1078 530 C ATOM 1351 CD2 TYR A 199 -1.560 -1.576 55.155 1.00 71.89 C ANISOU 1351 CD2 TYR A 199 12021 8366 6929 552 845 582 C ATOM 1352 CE1 TYR A 199 -3.857 -1.369 53.623 1.00 72.66 C ANISOU 1352 CE1 TYR A 199 11923 8493 7193 373 979 458 C ATOM 1353 CE2 TYR A 199 -1.719 -0.505 54.277 1.00 71.69 C ANISOU 1353 CE2 TYR A 199 11873 8374 6992 516 758 507 C ATOM 1354 CZ TYR A 199 -2.869 -0.402 53.515 1.00 77.77 C ANISOU 1354 CZ TYR A 199 12552 9154 7842 440 823 452 C ATOM 1355 OH TYR A 199 -3.025 0.663 52.661 1.00 76.52 O ANISOU 1355 OH TYR A 199 12292 9029 7754 432 740 388 O ATOM 1356 N ALA A 200 0.703 -4.331 55.372 1.00 73.26 N ANISOU 1356 N ALA A 200 12437 8416 6981 712 895 811 N ATOM 1357 CA ALA A 200 1.960 -3.889 54.757 1.00 72.85 C ANISOU 1357 CA ALA A 200 12302 8421 6956 762 737 806 C ATOM 1358 C ALA A 200 2.581 -4.922 53.793 1.00 77.59 C ANISOU 1358 C ALA A 200 12918 8956 7608 773 760 863 C ATOM 1359 O ALA A 200 3.498 -4.574 53.050 1.00 76.56 O ANISOU 1359 O ALA A 200 12694 8873 7522 789 642 849 O ATOM 1360 CB ALA A 200 2.965 -3.517 55.835 1.00 74.30 C ANISOU 1360 CB ALA A 200 12526 8702 7005 891 633 829 C ATOM 1361 N ILE A 201 2.084 -6.171 53.796 1.00 75.69 N ANISOU 1361 N ILE A 201 12800 8604 7356 758 920 922 N ATOM 1362 CA ILE A 201 2.556 -7.228 52.902 1.00 75.82 C ANISOU 1362 CA ILE A 201 12858 8534 7415 766 969 973 C ATOM 1363 C ILE A 201 1.512 -7.451 51.796 1.00 79.33 C ANISOU 1363 C ILE A 201 13237 8910 7994 594 1062 912 C ATOM 1364 O ILE A 201 1.876 -7.458 50.618 1.00 78.18 O ANISOU 1364 O ILE A 201 13001 8761 7942 556 1009 889 O ATOM 1365 CB ILE A 201 2.900 -8.535 53.682 1.00 80.58 C ANISOU 1365 CB ILE A 201 13678 9046 7890 887 1089 1086 C ATOM 1366 CG1 ILE A 201 4.196 -8.379 54.522 1.00 81.97 C ANISOU 1366 CG1 ILE A 201 13889 9328 7928 1089 966 1146 C ATOM 1367 CG2 ILE A 201 2.974 -9.765 52.759 1.00 81.57 C ANISOU 1367 CG2 ILE A 201 13889 9035 8067 860 1202 1129 C ATOM 1368 CD1 ILE A 201 5.556 -8.452 53.732 1.00 92.24 C ANISOU 1368 CD1 ILE A 201 15108 10695 9244 1184 837 1165 C ATOM 1369 N ALA A 202 0.224 -7.624 52.178 1.00 76.50 N ANISOU 1369 N ALA A 202 12914 8515 7636 490 1199 878 N ATOM 1370 CA ALA A 202 -0.885 -7.863 51.250 1.00 76.09 C ANISOU 1370 CA ALA A 202 12788 8433 7690 319 1299 804 C ATOM 1371 C ALA A 202 -1.074 -6.703 50.264 1.00 79.02 C ANISOU 1371 C ALA A 202 12950 8905 8170 264 1167 713 C ATOM 1372 O ALA A 202 -1.040 -6.937 49.054 1.00 77.67 O ANISOU 1372 O ALA A 202 12704 8717 8089 199 1159 685 O ATOM 1373 CB ALA A 202 -2.174 -8.113 52.017 1.00 77.75 C ANISOU 1373 CB ALA A 202 13055 8629 7859 226 1458 774 C ATOM 1374 N SER A 203 -1.232 -5.461 50.771 1.00 75.84 N ANISOU 1374 N SER A 203 12469 8598 7748 301 1068 671 N ATOM 1375 CA SER A 203 -1.419 -4.277 49.927 1.00 75.11 C ANISOU 1375 CA SER A 203 12212 8587 7739 270 953 593 C ATOM 1376 C SER A 203 -0.173 -3.968 49.086 1.00 78.15 C ANISOU 1376 C SER A 203 12545 8978 8172 318 815 612 C ATOM 1377 O SER A 203 -0.323 -3.476 47.975 1.00 76.40 O ANISOU 1377 O SER A 203 12209 8782 8038 268 763 562 O ATOM 1378 CB SER A 203 -1.800 -3.059 50.764 1.00 79.54 C ANISOU 1378 CB SER A 203 12743 9225 8253 312 894 550 C ATOM 1379 OG SER A 203 -0.725 -2.613 51.574 1.00 89.56 O ANISOU 1379 OG SER A 203 14072 10512 9445 416 792 590 O ATOM 1380 N SER A 204 1.040 -4.263 49.599 1.00 75.27 N ANISOU 1380 N SER A 204 12259 8601 7739 419 758 682 N ATOM 1381 CA SER A 204 2.293 -4.014 48.879 1.00 74.35 C ANISOU 1381 CA SER A 204 12084 8511 7653 463 633 696 C ATOM 1382 C SER A 204 2.480 -4.956 47.683 1.00 77.44 C ANISOU 1382 C SER A 204 12464 8839 8121 422 679 717 C ATOM 1383 O SER A 204 3.004 -4.523 46.653 1.00 76.50 O ANISOU 1383 O SER A 204 12246 8747 8073 403 591 692 O ATOM 1384 CB SER A 204 3.490 -4.132 49.813 1.00 78.79 C ANISOU 1384 CB SER A 204 12718 9114 8105 590 565 756 C ATOM 1385 OG SER A 204 3.476 -3.079 50.762 1.00 90.44 O ANISOU 1385 OG SER A 204 14183 10664 9515 616 496 719 O ATOM 1386 N ILE A 205 2.064 -6.231 47.806 1.00 73.46 N ANISOU 1386 N ILE A 205 12071 8243 7598 404 824 758 N ATOM 1387 CA ILE A 205 2.236 -7.162 46.692 1.00 72.41 C ANISOU 1387 CA ILE A 205 11945 8039 7531 361 879 771 C ATOM 1388 C ILE A 205 1.070 -7.018 45.699 1.00 75.00 C ANISOU 1388 C ILE A 205 12167 8371 7959 210 933 684 C ATOM 1389 O ILE A 205 1.317 -7.059 44.502 1.00 74.27 O ANISOU 1389 O ILE A 205 11995 8280 7944 172 895 660 O ATOM 1390 CB ILE A 205 2.514 -8.645 47.090 1.00 76.23 C ANISOU 1390 CB ILE A 205 12615 8403 7946 414 1013 855 C ATOM 1391 CG1 ILE A 205 1.332 -9.314 47.802 1.00 77.72 C ANISOU 1391 CG1 ILE A 205 12922 8512 8094 334 1193 852 C ATOM 1392 CG2 ILE A 205 3.804 -8.779 47.913 1.00 77.01 C ANISOU 1392 CG2 ILE A 205 12796 8530 7933 598 939 942 C ATOM 1393 CD1 ILE A 205 1.102 -10.726 47.322 1.00 88.10 C ANISOU 1393 CD1 ILE A 205 14372 9683 9420 271 1361 876 C ATOM 1394 N VAL A 206 -0.163 -6.791 46.178 1.00 71.25 N ANISOU 1394 N VAL A 206 11677 7920 7476 134 1011 632 N ATOM 1395 CA VAL A 206 -1.352 -6.642 45.327 1.00 70.66 C ANISOU 1395 CA VAL A 206 11482 7890 7474 3 1062 539 C ATOM 1396 C VAL A 206 -1.337 -5.279 44.606 1.00 72.15 C ANISOU 1396 C VAL A 206 11512 8182 7720 22 915 484 C ATOM 1397 O VAL A 206 -1.647 -5.221 43.416 1.00 71.38 O ANISOU 1397 O VAL A 206 11310 8116 7694 -40 902 432 O ATOM 1398 CB VAL A 206 -2.657 -6.866 46.148 1.00 75.88 C ANISOU 1398 CB VAL A 206 12172 8568 8092 -77 1200 497 C ATOM 1399 CG1 VAL A 206 -3.903 -6.364 45.418 1.00 75.57 C ANISOU 1399 CG1 VAL A 206 11966 8640 8109 -182 1218 385 C ATOM 1400 CG2 VAL A 206 -2.815 -8.339 46.517 1.00 76.96 C ANISOU 1400 CG2 VAL A 206 12474 8580 8188 -139 1379 537 C ATOM 1401 N SER A 207 -0.971 -4.202 45.310 1.00 67.96 N ANISOU 1401 N SER A 207 10975 7696 7149 108 813 493 N ATOM 1402 CA SER A 207 -0.952 -2.862 44.728 1.00 66.79 C ANISOU 1402 CA SER A 207 10716 7619 7041 130 692 445 C ATOM 1403 C SER A 207 0.347 -2.518 43.992 1.00 69.40 C ANISOU 1403 C SER A 207 11024 7939 7407 171 572 475 C ATOM 1404 O SER A 207 0.332 -1.551 43.229 1.00 68.80 O ANISOU 1404 O SER A 207 10866 7901 7373 170 494 436 O ATOM 1405 CB SER A 207 -1.192 -1.803 45.803 1.00 70.15 C ANISOU 1405 CB SER A 207 11162 8088 7404 189 649 429 C ATOM 1406 OG SER A 207 -2.497 -1.865 46.354 1.00 79.08 O ANISOU 1406 OG SER A 207 12283 9259 8507 154 749 386 O ATOM 1407 N PHE A 208 1.463 -3.257 44.217 1.00 64.87 N ANISOU 1407 N PHE A 208 10523 7319 6805 216 560 542 N ATOM 1408 CA PHE A 208 2.723 -2.877 43.580 1.00 63.54 C ANISOU 1408 CA PHE A 208 10316 7167 6661 252 446 561 C ATOM 1409 C PHE A 208 3.533 -4.027 42.975 1.00 66.92 C ANISOU 1409 C PHE A 208 10771 7549 7104 267 471 613 C ATOM 1410 O PHE A 208 3.947 -3.899 41.827 1.00 66.10 O ANISOU 1410 O PHE A 208 10596 7455 7065 242 423 599 O ATOM 1411 CB PHE A 208 3.615 -2.107 44.575 1.00 65.42 C ANISOU 1411 CB PHE A 208 10583 7450 6823 323 352 576 C ATOM 1412 CG PHE A 208 4.998 -1.765 44.068 1.00 66.36 C ANISOU 1412 CG PHE A 208 10656 7609 6950 349 243 587 C ATOM 1413 CD1 PHE A 208 5.197 -0.683 43.217 1.00 68.46 C ANISOU 1413 CD1 PHE A 208 10844 7898 7271 302 166 540 C ATOM 1414 CD2 PHE A 208 6.103 -2.520 44.447 1.00 68.59 C ANISOU 1414 CD2 PHE A 208 10977 7912 7173 425 224 644 C ATOM 1415 CE1 PHE A 208 6.473 -0.375 42.739 1.00 69.14 C ANISOU 1415 CE1 PHE A 208 10883 8028 7360 304 78 542 C ATOM 1416 CE2 PHE A 208 7.379 -2.208 43.972 1.00 71.24 C ANISOU 1416 CE2 PHE A 208 11247 8313 7508 443 125 644 C ATOM 1417 CZ PHE A 208 7.555 -1.139 43.119 1.00 68.68 C ANISOU 1417 CZ PHE A 208 10839 8011 7246 370 56 589 C ATOM 1418 N TYR A 209 3.861 -5.074 43.754 1.00 63.84 N ANISOU 1418 N TYR A 209 10497 7112 6648 326 539 676 N ATOM 1419 CA TYR A 209 4.744 -6.154 43.294 1.00 63.22 C ANISOU 1419 CA TYR A 209 10469 6986 6565 376 563 733 C ATOM 1420 C TYR A 209 4.168 -7.017 42.173 1.00 66.30 C ANISOU 1420 C TYR A 209 10857 7302 7031 288 659 713 C ATOM 1421 O TYR A 209 4.906 -7.330 41.235 1.00 64.95 O ANISOU 1421 O TYR A 209 10654 7125 6898 303 627 725 O ATOM 1422 CB TYR A 209 5.191 -7.043 44.453 1.00 64.76 C ANISOU 1422 CB TYR A 209 10813 7142 6650 487 621 813 C ATOM 1423 CG TYR A 209 6.256 -6.399 45.311 1.00 66.25 C ANISOU 1423 CG TYR A 209 10987 7433 6751 602 500 838 C ATOM 1424 CD1 TYR A 209 7.567 -6.275 44.855 1.00 67.95 C ANISOU 1424 CD1 TYR A 209 11136 7724 6958 672 395 853 C ATOM 1425 CD2 TYR A 209 5.960 -5.925 46.585 1.00 67.61 C ANISOU 1425 CD2 TYR A 209 11205 7642 6843 635 494 838 C ATOM 1426 CE1 TYR A 209 8.554 -5.684 45.642 1.00 69.42 C ANISOU 1426 CE1 TYR A 209 11289 8034 7054 761 284 859 C ATOM 1427 CE2 TYR A 209 6.942 -5.345 47.388 1.00 69.08 C ANISOU 1427 CE2 TYR A 209 11371 7939 6937 731 382 848 C ATOM 1428 CZ TYR A 209 8.238 -5.224 46.910 1.00 76.86 C ANISOU 1428 CZ TYR A 209 12279 9012 7914 789 276 854 C ATOM 1429 OH TYR A 209 9.210 -4.650 47.692 1.00 78.32 O ANISOU 1429 OH TYR A 209 12424 9334 8000 867 166 845 O ATOM 1430 N VAL A 210 2.878 -7.396 42.260 1.00 63.30 N ANISOU 1430 N VAL A 210 10503 6879 6667 190 779 673 N ATOM 1431 CA VAL A 210 2.202 -8.212 41.245 1.00 63.35 C ANISOU 1431 CA VAL A 210 10501 6832 6737 79 882 631 C ATOM 1432 C VAL A 210 2.173 -7.426 39.912 1.00 66.71 C ANISOU 1432 C VAL A 210 10765 7334 7249 30 786 569 C ATOM 1433 O VAL A 210 2.756 -7.946 38.962 1.00 66.12 O ANISOU 1433 O VAL A 210 10682 7229 7212 28 781 579 O ATOM 1434 CB VAL A 210 0.804 -8.733 41.695 1.00 67.97 C ANISOU 1434 CB VAL A 210 11132 7383 7308 -35 1036 584 C ATOM 1435 CG1 VAL A 210 -0.050 -9.179 40.510 1.00 67.72 C ANISOU 1435 CG1 VAL A 210 11025 7357 7348 -181 1111 499 C ATOM 1436 CG2 VAL A 210 0.944 -9.864 42.717 1.00 68.75 C ANISOU 1436 CG2 VAL A 210 11434 7363 7324 3 1169 657 C ATOM 1437 N PRO A 211 1.645 -6.167 39.814 1.00 63.63 N ANISOU 1437 N PRO A 211 10259 7037 6881 13 706 516 N ATOM 1438 CA PRO A 211 1.700 -5.463 38.517 1.00 62.74 C ANISOU 1438 CA PRO A 211 10019 6984 6835 -12 622 471 C ATOM 1439 C PRO A 211 3.131 -5.183 38.025 1.00 65.69 C ANISOU 1439 C PRO A 211 10380 7358 7222 57 515 518 C ATOM 1440 O PRO A 211 3.333 -5.151 36.812 1.00 64.24 O ANISOU 1440 O PRO A 211 10127 7189 7092 28 485 497 O ATOM 1441 CB PRO A 211 0.924 -4.163 38.772 1.00 64.29 C ANISOU 1441 CB PRO A 211 10139 7262 7025 -8 568 422 C ATOM 1442 CG PRO A 211 0.929 -3.983 40.237 1.00 69.13 C ANISOU 1442 CG PRO A 211 10835 7862 7569 41 580 453 C ATOM 1443 CD PRO A 211 0.926 -5.356 40.823 1.00 65.58 C ANISOU 1443 CD PRO A 211 10499 7333 7086 24 699 493 C ATOM 1444 N LEU A 212 4.113 -5.016 38.945 1.00 62.48 N ANISOU 1444 N LEU A 212 10032 6950 6759 143 461 574 N ATOM 1445 CA LEU A 212 5.525 -4.769 38.610 1.00 62.09 C ANISOU 1445 CA LEU A 212 9956 6931 6706 204 363 609 C ATOM 1446 C LEU A 212 6.163 -6.007 37.952 1.00 66.43 C ANISOU 1446 C LEU A 212 10542 7430 7267 228 411 647 C ATOM 1447 O LEU A 212 6.814 -5.858 36.917 1.00 66.00 O ANISOU 1447 O LEU A 212 10420 7403 7256 222 357 641 O ATOM 1448 CB LEU A 212 6.328 -4.334 39.868 1.00 62.55 C ANISOU 1448 CB LEU A 212 10055 7031 6681 287 299 644 C ATOM 1449 CG LEU A 212 7.834 -4.649 39.959 1.00 67.20 C ANISOU 1449 CG LEU A 212 10644 7665 7223 376 236 692 C ATOM 1450 CD1 LEU A 212 8.640 -3.765 39.061 1.00 66.74 C ANISOU 1450 CD1 LEU A 212 10478 7675 7206 344 135 661 C ATOM 1451 CD2 LEU A 212 8.332 -4.467 41.355 1.00 69.92 C ANISOU 1451 CD2 LEU A 212 11038 8062 7465 459 200 719 C ATOM 1452 N VAL A 213 5.998 -7.202 38.565 1.00 63.39 N ANISOU 1452 N VAL A 213 10280 6966 6838 259 519 688 N ATOM 1453 CA VAL A 213 6.551 -8.473 38.082 1.00 63.91 C ANISOU 1453 CA VAL A 213 10423 6959 6900 299 588 730 C ATOM 1454 C VAL A 213 5.958 -8.792 36.694 1.00 68.08 C ANISOU 1454 C VAL A 213 10896 7457 7514 188 635 672 C ATOM 1455 O VAL A 213 6.709 -9.144 35.781 1.00 67.26 O ANISOU 1455 O VAL A 213 10769 7350 7436 213 614 683 O ATOM 1456 CB VAL A 213 6.336 -9.624 39.118 1.00 68.79 C ANISOU 1456 CB VAL A 213 11222 7475 7441 353 717 787 C ATOM 1457 CG1 VAL A 213 6.527 -11.009 38.499 1.00 68.97 C ANISOU 1457 CG1 VAL A 213 11357 7381 7467 364 832 814 C ATOM 1458 CG2 VAL A 213 7.253 -9.450 40.326 1.00 69.15 C ANISOU 1458 CG2 VAL A 213 11319 7572 7384 503 654 855 C ATOM 1459 N ILE A 214 4.630 -8.629 36.531 1.00 65.35 N ANISOU 1459 N ILE A 214 10516 7111 7204 71 694 605 N ATOM 1460 CA ILE A 214 3.963 -8.888 35.255 1.00 65.79 C ANISOU 1460 CA ILE A 214 10502 7168 7326 -38 736 535 C ATOM 1461 C ILE A 214 4.536 -7.930 34.185 1.00 70.96 C ANISOU 1461 C ILE A 214 11023 7909 8029 -23 606 518 C ATOM 1462 O ILE A 214 5.019 -8.400 33.159 1.00 70.64 O ANISOU 1462 O ILE A 214 10966 7853 8021 -30 607 515 O ATOM 1463 CB ILE A 214 2.413 -8.821 35.379 1.00 69.22 C ANISOU 1463 CB ILE A 214 10900 7630 7772 -159 816 454 C ATOM 1464 CG1 ILE A 214 1.894 -9.943 36.321 1.00 70.74 C ANISOU 1464 CG1 ILE A 214 11244 7718 7915 -199 974 469 C ATOM 1465 CG2 ILE A 214 1.753 -8.925 33.993 1.00 69.97 C ANISOU 1465 CG2 ILE A 214 10888 7773 7924 -264 834 368 C ATOM 1466 CD1 ILE A 214 0.427 -9.822 36.786 1.00 77.76 C ANISOU 1466 CD1 ILE A 214 12099 8652 8795 -313 1058 394 C ATOM 1467 N MET A 215 4.554 -6.614 34.473 1.00 68.13 N ANISOU 1467 N MET A 215 10592 7628 7668 2 503 511 N ATOM 1468 CA MET A 215 5.066 -5.538 33.616 1.00 67.27 C ANISOU 1468 CA MET A 215 10382 7587 7591 14 391 499 C ATOM 1469 C MET A 215 6.501 -5.802 33.130 1.00 71.59 C ANISOU 1469 C MET A 215 10928 8132 8141 69 340 545 C ATOM 1470 O MET A 215 6.750 -5.662 31.939 1.00 70.25 O ANISOU 1470 O MET A 215 10694 7985 8013 45 311 526 O ATOM 1471 CB MET A 215 5.012 -4.216 34.392 1.00 69.42 C ANISOU 1471 CB MET A 215 10634 7905 7835 43 314 497 C ATOM 1472 CG MET A 215 5.240 -2.977 33.562 1.00 72.48 C ANISOU 1472 CG MET A 215 10946 8343 8249 38 224 474 C ATOM 1473 SD MET A 215 5.644 -1.584 34.641 1.00 76.50 S ANISOU 1473 SD MET A 215 11480 8875 8710 75 143 482 S ATOM 1474 CE MET A 215 7.359 -1.930 34.952 1.00 73.29 C ANISOU 1474 CE MET A 215 11088 8484 8276 114 91 532 C ATOM 1475 N VAL A 216 7.430 -6.186 34.035 1.00 70.42 N ANISOU 1475 N VAL A 216 10846 7972 7939 153 330 603 N ATOM 1476 CA VAL A 216 8.836 -6.433 33.676 1.00 71.13 C ANISOU 1476 CA VAL A 216 10919 8092 8015 224 279 644 C ATOM 1477 C VAL A 216 8.970 -7.704 32.812 1.00 77.19 C ANISOU 1477 C VAL A 216 11728 8796 8805 230 359 654 C ATOM 1478 O VAL A 216 9.791 -7.713 31.895 1.00 77.05 O ANISOU 1478 O VAL A 216 11653 8814 8810 247 318 657 O ATOM 1479 CB VAL A 216 9.842 -6.439 34.873 1.00 75.84 C ANISOU 1479 CB VAL A 216 11553 8734 8528 331 234 696 C ATOM 1480 CG1 VAL A 216 9.901 -5.079 35.558 1.00 75.38 C ANISOU 1480 CG1 VAL A 216 11445 8749 8448 309 146 671 C ATOM 1481 CG2 VAL A 216 9.552 -7.543 35.889 1.00 76.60 C ANISOU 1481 CG2 VAL A 216 11786 8754 8563 400 329 742 C ATOM 1482 N PHE A 217 8.155 -8.746 33.076 1.00 75.30 N ANISOU 1482 N PHE A 217 11592 8460 8560 204 480 652 N ATOM 1483 CA PHE A 217 8.176 -9.999 32.317 1.00 75.93 C ANISOU 1483 CA PHE A 217 11741 8455 8656 195 577 651 C ATOM 1484 C PHE A 217 7.550 -9.812 30.926 1.00 77.93 C ANISOU 1484 C PHE A 217 11900 8730 8982 81 579 577 C ATOM 1485 O PHE A 217 8.061 -10.366 29.949 1.00 77.71 O ANISOU 1485 O PHE A 217 11868 8684 8975 89 594 573 O ATOM 1486 CB PHE A 217 7.451 -11.112 33.098 1.00 79.51 C ANISOU 1486 CB PHE A 217 12354 8786 9072 180 723 663 C ATOM 1487 CG PHE A 217 6.988 -12.291 32.274 1.00 82.92 C ANISOU 1487 CG PHE A 217 12864 9112 9530 103 853 627 C ATOM 1488 CD1 PHE A 217 7.891 -13.261 31.848 1.00 87.73 C ANISOU 1488 CD1 PHE A 217 13565 9649 10117 190 898 670 C ATOM 1489 CD2 PHE A 217 5.649 -12.436 31.929 1.00 86.18 C ANISOU 1489 CD2 PHE A 217 13258 9507 9980 -57 936 540 C ATOM 1490 CE1 PHE A 217 7.463 -14.348 31.080 1.00 89.71 C ANISOU 1490 CE1 PHE A 217 13907 9790 10390 110 1027 627 C ATOM 1491 CE2 PHE A 217 5.221 -13.526 31.166 1.00 90.31 C ANISOU 1491 CE2 PHE A 217 13852 9939 10521 -151 1062 489 C ATOM 1492 CZ PHE A 217 6.131 -14.475 30.747 1.00 89.21 C ANISOU 1492 CZ PHE A 217 13824 9706 10365 -72 1110 533 C ATOM 1493 N VAL A 218 6.436 -9.055 30.850 1.00 72.76 N ANISOU 1493 N VAL A 218 11171 8121 8354 -11 567 516 N ATOM 1494 CA VAL A 218 5.692 -8.791 29.615 1.00 71.29 C ANISOU 1494 CA VAL A 218 10885 7984 8217 -105 564 440 C ATOM 1495 C VAL A 218 6.456 -7.783 28.737 1.00 72.90 C ANISOU 1495 C VAL A 218 10985 8268 8445 -70 444 449 C ATOM 1496 O VAL A 218 6.574 -8.027 27.538 1.00 72.76 O ANISOU 1496 O VAL A 218 10923 8265 8457 -99 446 421 O ATOM 1497 CB VAL A 218 4.228 -8.338 29.898 1.00 74.97 C ANISOU 1497 CB VAL A 218 11302 8497 8684 -189 593 373 C ATOM 1498 CG1 VAL A 218 3.495 -7.955 28.620 1.00 74.38 C ANISOU 1498 CG1 VAL A 218 11108 8510 8642 -258 572 294 C ATOM 1499 CG2 VAL A 218 3.450 -9.421 30.632 1.00 75.73 C ANISOU 1499 CG2 VAL A 218 11501 8515 8757 -254 732 352 C ATOM 1500 N TYR A 219 6.993 -6.683 29.312 1.00 67.94 N ANISOU 1500 N TYR A 219 10327 7687 7799 -18 350 483 N ATOM 1501 CA TYR A 219 7.700 -5.683 28.509 1.00 66.80 C ANISOU 1501 CA TYR A 219 10102 7605 7672 -6 255 487 C ATOM 1502 C TYR A 219 9.092 -6.128 28.051 1.00 71.30 C ANISOU 1502 C TYR A 219 10670 8182 8240 45 232 528 C ATOM 1503 O TYR A 219 9.614 -5.547 27.098 1.00 70.45 O ANISOU 1503 O TYR A 219 10495 8121 8152 33 179 522 O ATOM 1504 CB TYR A 219 7.781 -4.313 29.189 1.00 67.17 C ANISOU 1504 CB TYR A 219 10131 7693 7699 9 178 495 C ATOM 1505 CG TYR A 219 7.559 -3.196 28.193 1.00 67.63 C ANISOU 1505 CG TYR A 219 10125 7793 7777 -19 125 468 C ATOM 1506 CD1 TYR A 219 6.300 -2.966 27.644 1.00 69.26 C ANISOU 1506 CD1 TYR A 219 10299 8022 7994 -47 149 419 C ATOM 1507 CD2 TYR A 219 8.621 -2.421 27.737 1.00 67.98 C ANISOU 1507 CD2 TYR A 219 10144 7865 7821 -14 60 488 C ATOM 1508 CE1 TYR A 219 6.094 -1.966 26.698 1.00 69.42 C ANISOU 1508 CE1 TYR A 219 10278 8083 8017 -44 105 403 C ATOM 1509 CE2 TYR A 219 8.425 -1.410 26.797 1.00 68.58 C ANISOU 1509 CE2 TYR A 219 10191 7961 7906 -34 28 470 C ATOM 1510 CZ TYR A 219 7.159 -1.188 26.281 1.00 76.02 C ANISOU 1510 CZ TYR A 219 11116 8917 8852 -36 49 434 C ATOM 1511 OH TYR A 219 6.950 -0.208 25.347 1.00 78.13 O ANISOU 1511 OH TYR A 219 11369 9205 9112 -28 20 425 O ATOM 1512 N SER A 220 9.680 -7.157 28.680 1.00 69.55 N ANISOU 1512 N SER A 220 10522 7918 7987 110 276 569 N ATOM 1513 CA SER A 220 10.966 -7.684 28.213 1.00 70.37 C ANISOU 1513 CA SER A 220 10617 8042 8078 180 261 605 C ATOM 1514 C SER A 220 10.730 -8.517 26.944 1.00 75.75 C ANISOU 1514 C SER A 220 11303 8681 8798 144 324 575 C ATOM 1515 O SER A 220 11.606 -8.586 26.080 1.00 75.11 O ANISOU 1515 O SER A 220 11175 8640 8725 171 297 582 O ATOM 1516 CB SER A 220 11.674 -8.493 29.295 1.00 74.69 C ANISOU 1516 CB SER A 220 11250 8568 8561 294 287 663 C ATOM 1517 OG SER A 220 10.793 -9.371 29.975 1.00 85.52 O ANISOU 1517 OG SER A 220 12742 9834 9917 291 389 669 O ATOM 1518 N ARG A 221 9.515 -9.096 26.816 1.00 73.84 N ANISOU 1518 N ARG A 221 11109 8372 8576 70 410 530 N ATOM 1519 CA ARG A 221 9.084 -9.866 25.650 1.00 74.40 C ANISOU 1519 CA ARG A 221 11182 8408 8677 8 478 480 C ATOM 1520 C ARG A 221 8.795 -8.944 24.464 1.00 78.49 C ANISOU 1520 C ARG A 221 11579 9013 9229 -50 411 433 C ATOM 1521 O ARG A 221 9.083 -9.340 23.335 1.00 78.02 O ANISOU 1521 O ARG A 221 11495 8962 9186 -63 424 411 O ATOM 1522 CB ARG A 221 7.843 -10.725 25.960 1.00 75.85 C ANISOU 1522 CB ARG A 221 11446 8512 8860 -76 597 430 C ATOM 1523 CG ARG A 221 8.143 -12.131 26.508 1.00 90.84 C ANISOU 1523 CG ARG A 221 13510 10280 10727 -32 714 464 C ATOM 1524 CD ARG A 221 8.716 -13.117 25.484 1.00101.08 C ANISOU 1524 CD ARG A 221 14856 11520 12029 -15 772 455 C ATOM 1525 NE ARG A 221 7.902 -13.216 24.267 1.00107.95 N ANISOU 1525 NE ARG A 221 15660 12417 12939 -145 801 358 N ATOM 1526 CZ ARG A 221 6.897 -14.070 24.094 1.00119.91 C ANISOU 1526 CZ ARG A 221 17241 13862 14455 -267 924 282 C ATOM 1527 NH1 ARG A 221 6.562 -14.919 25.059 1.00109.43 N ANISOU 1527 NH1 ARG A 221 16069 12411 13098 -282 1043 296 N ATOM 1528 NH2 ARG A 221 6.217 -14.080 22.955 1.00102.60 N ANISOU 1528 NH2 ARG A 221 14965 11731 12289 -380 934 185 N ATOM 1529 N VAL A 222 8.240 -7.719 24.706 1.00 74.93 N ANISOU 1529 N VAL A 222 11064 8624 8781 -75 346 420 N ATOM 1530 CA VAL A 222 7.925 -6.768 23.620 1.00 74.55 C ANISOU 1530 CA VAL A 222 10923 8654 8749 -106 288 386 C ATOM 1531 C VAL A 222 9.230 -6.290 22.956 1.00 78.09 C ANISOU 1531 C VAL A 222 11335 9135 9201 -65 223 427 C ATOM 1532 O VAL A 222 9.243 -6.073 21.749 1.00 77.29 O ANISOU 1532 O VAL A 222 11183 9074 9110 -85 208 404 O ATOM 1533 CB VAL A 222 6.992 -5.573 23.997 1.00 78.25 C ANISOU 1533 CB VAL A 222 11354 9170 9206 -119 244 365 C ATOM 1534 CG1 VAL A 222 5.868 -5.998 24.937 1.00 78.32 C ANISOU 1534 CG1 VAL A 222 11395 9159 9205 -153 307 332 C ATOM 1535 CG2 VAL A 222 7.762 -4.385 24.562 1.00 77.81 C ANISOU 1535 CG2 VAL A 222 11301 9126 9137 -75 165 416 C ATOM 1536 N PHE A 223 10.317 -6.161 23.741 1.00 75.11 N ANISOU 1536 N PHE A 223 10977 8756 8804 -11 190 481 N ATOM 1537 CA PHE A 223 11.634 -5.767 23.255 1.00 74.91 C ANISOU 1537 CA PHE A 223 10906 8783 8774 17 138 511 C ATOM 1538 C PHE A 223 12.263 -6.915 22.473 1.00 78.48 C ANISOU 1538 C PHE A 223 11364 9224 9231 51 183 514 C ATOM 1539 O PHE A 223 12.902 -6.677 21.449 1.00 77.69 O ANISOU 1539 O PHE A 223 11208 9171 9138 45 160 512 O ATOM 1540 CB PHE A 223 12.533 -5.336 24.426 1.00 77.09 C ANISOU 1540 CB PHE A 223 11185 9090 9014 61 90 550 C ATOM 1541 CG PHE A 223 12.303 -3.938 24.958 1.00 78.65 C ANISOU 1541 CG PHE A 223 11371 9310 9202 20 34 543 C ATOM 1542 CD1 PHE A 223 11.540 -3.017 24.244 1.00 81.58 C ANISOU 1542 CD1 PHE A 223 11730 9676 9592 -31 21 517 C ATOM 1543 CD2 PHE A 223 12.887 -3.527 26.147 1.00 81.42 C ANISOU 1543 CD2 PHE A 223 11730 9691 9516 42 -5 561 C ATOM 1544 CE1 PHE A 223 11.346 -1.721 24.727 1.00 82.59 C ANISOU 1544 CE1 PHE A 223 11874 9805 9703 -57 -19 513 C ATOM 1545 CE2 PHE A 223 12.684 -2.233 26.634 1.00 84.35 C ANISOU 1545 CE2 PHE A 223 12106 10069 9874 -4 -48 547 C ATOM 1546 CZ PHE A 223 11.922 -1.336 25.917 1.00 82.16 C ANISOU 1546 CZ PHE A 223 11836 9764 9618 -52 -50 525 C ATOM 1547 N GLN A 224 12.059 -8.160 22.955 1.00 75.30 N ANISOU 1547 N GLN A 224 11042 8750 8819 87 258 520 N ATOM 1548 CA GLN A 224 12.517 -9.393 22.317 1.00 75.51 C ANISOU 1548 CA GLN A 224 11112 8736 8843 128 323 520 C ATOM 1549 C GLN A 224 11.824 -9.553 20.963 1.00 79.33 C ANISOU 1549 C GLN A 224 11564 9217 9359 48 353 458 C ATOM 1550 O GLN A 224 12.489 -9.841 19.964 1.00 79.75 O ANISOU 1550 O GLN A 224 11590 9295 9416 68 355 455 O ATOM 1551 CB GLN A 224 12.227 -10.608 23.218 1.00 77.50 C ANISOU 1551 CB GLN A 224 11495 8882 9071 172 416 537 C ATOM 1552 CG GLN A 224 13.325 -10.921 24.228 1.00 96.50 C ANISOU 1552 CG GLN A 224 13944 11298 11421 307 401 607 C ATOM 1553 CD GLN A 224 12.943 -12.020 25.198 1.00122.63 C ANISOU 1553 CD GLN A 224 17411 14490 14694 360 501 634 C ATOM 1554 OE1 GLN A 224 12.306 -13.023 24.843 1.00119.45 O ANISOU 1554 OE1 GLN A 224 17111 13973 14302 319 611 604 O ATOM 1555 NE2 GLN A 224 13.367 -11.876 26.446 1.00117.52 N ANISOU 1555 NE2 GLN A 224 16794 13864 13993 450 472 688 N ATOM 1556 N GLU A 225 10.489 -9.320 20.932 1.00 74.22 N ANISOU 1556 N GLU A 225 10911 8561 8728 -37 372 405 N ATOM 1557 CA GLU A 225 9.650 -9.428 19.740 1.00 73.17 C ANISOU 1557 CA GLU A 225 10735 8456 8610 -114 396 332 C ATOM 1558 C GLU A 225 10.024 -8.384 18.696 1.00 74.15 C ANISOU 1558 C GLU A 225 10766 8671 8737 -110 316 336 C ATOM 1559 O GLU A 225 10.240 -8.749 17.550 1.00 73.26 O ANISOU 1559 O GLU A 225 10629 8579 8626 -120 331 309 O ATOM 1560 CB GLU A 225 8.158 -9.324 20.094 1.00 74.70 C ANISOU 1560 CB GLU A 225 10921 8657 8804 -194 426 270 C ATOM 1561 CG GLU A 225 7.563 -10.607 20.661 1.00 86.17 C ANISOU 1561 CG GLU A 225 12472 10016 10253 -244 543 234 C ATOM 1562 CD GLU A 225 7.551 -11.831 19.763 1.00107.57 C ANISOU 1562 CD GLU A 225 15232 12673 12965 -292 635 178 C ATOM 1563 OE1 GLU A 225 7.369 -11.679 18.533 1.00 95.92 O ANISOU 1563 OE1 GLU A 225 13678 11271 11494 -330 612 124 O ATOM 1564 OE2 GLU A 225 7.689 -12.952 20.303 1.00107.84 O ANISOU 1564 OE2 GLU A 225 15397 12588 12991 -291 736 187 O ATOM 1565 N ALA A 226 10.135 -7.102 19.093 1.00 69.38 N ANISOU 1565 N ALA A 226 10124 8110 8126 -96 241 370 N ATOM 1566 CA ALA A 226 10.487 -5.988 18.208 1.00 68.15 C ANISOU 1566 CA ALA A 226 9911 8020 7964 -95 178 382 C ATOM 1567 C ALA A 226 11.808 -6.248 17.463 1.00 71.54 C ANISOU 1567 C ALA A 226 10320 8470 8394 -68 173 410 C ATOM 1568 O ALA A 226 11.875 -6.017 16.253 1.00 71.53 O ANISOU 1568 O ALA A 226 10281 8510 8387 -81 166 394 O ATOM 1569 CB ALA A 226 10.576 -4.696 19.006 1.00 68.36 C ANISOU 1569 CB ALA A 226 9939 8055 7978 -86 119 418 C ATOM 1570 N LYS A 227 12.826 -6.780 18.179 1.00 66.95 N ANISOU 1570 N LYS A 227 9760 7870 7809 -20 180 449 N ATOM 1571 CA LYS A 227 14.153 -7.106 17.656 1.00 66.39 C ANISOU 1571 CA LYS A 227 9658 7839 7728 23 178 474 C ATOM 1572 C LYS A 227 14.105 -8.341 16.739 1.00 71.10 C ANISOU 1572 C LYS A 227 10280 8406 8331 39 244 443 C ATOM 1573 O LYS A 227 14.634 -8.279 15.626 1.00 70.26 O ANISOU 1573 O LYS A 227 10128 8346 8220 37 240 436 O ATOM 1574 CB LYS A 227 15.139 -7.330 18.817 1.00 68.70 C ANISOU 1574 CB LYS A 227 9959 8146 7998 92 163 519 C ATOM 1575 CG LYS A 227 16.609 -7.238 18.429 1.00 80.49 C ANISOU 1575 CG LYS A 227 11382 9732 9468 133 137 541 C ATOM 1576 N ARG A 228 13.472 -9.453 17.197 1.00 68.75 N ANISOU 1576 N ARG A 228 10062 8022 8036 46 315 421 N ATOM 1577 CA ARG A 228 13.379 -10.699 16.423 1.00 69.14 C ANISOU 1577 CA ARG A 228 10164 8019 8086 49 396 382 C ATOM 1578 C ARG A 228 12.478 -10.545 15.175 1.00 72.44 C ANISOU 1578 C ARG A 228 10538 8471 8513 -38 403 310 C ATOM 1579 O ARG A 228 12.732 -11.207 14.165 1.00 72.26 O ANISOU 1579 O ARG A 228 10522 8448 8486 -37 442 277 O ATOM 1580 CB ARG A 228 12.913 -11.890 17.298 1.00 70.00 C ANISOU 1580 CB ARG A 228 10398 8010 8189 63 488 374 C ATOM 1581 CG ARG A 228 11.409 -11.990 17.553 1.00 82.96 C ANISOU 1581 CG ARG A 228 12068 9609 9844 -45 531 310 C ATOM 1582 CD ARG A 228 10.988 -13.395 17.934 1.00100.24 C ANISOU 1582 CD ARG A 228 14397 11666 12023 -64 658 280 C ATOM 1583 NE ARG A 228 9.563 -13.622 17.680 1.00112.90 N ANISOU 1583 NE ARG A 228 16000 13261 13637 -203 714 184 N ATOM 1584 CZ ARG A 228 9.080 -14.298 16.641 1.00127.73 C ANISOU 1584 CZ ARG A 228 17885 15132 15515 -287 778 95 C ATOM 1585 NH1 ARG A 228 7.770 -14.447 16.490 1.00115.22 N ANISOU 1585 NH1 ARG A 228 16276 13572 13929 -422 824 -4 N ATOM 1586 NH2 ARG A 228 9.902 -14.839 15.750 1.00115.63 N ANISOU 1586 NH2 ARG A 228 16378 13582 13977 -239 798 97 N ATOM 1587 N GLN A 229 11.453 -9.669 15.246 1.00 68.43 N ANISOU 1587 N GLN A 229 9986 8004 8010 -99 363 283 N ATOM 1588 CA GLN A 229 10.504 -9.428 14.163 1.00 68.39 C ANISOU 1588 CA GLN A 229 9927 8062 7995 -161 359 213 C ATOM 1589 C GLN A 229 11.019 -8.398 13.151 1.00 72.41 C ANISOU 1589 C GLN A 229 10368 8658 8488 -138 292 239 C ATOM 1590 O GLN A 229 10.341 -8.149 12.145 1.00 72.27 O ANISOU 1590 O GLN A 229 10305 8707 8447 -165 282 190 O ATOM 1591 CB GLN A 229 9.135 -9.007 14.705 1.00 69.78 C ANISOU 1591 CB GLN A 229 10084 8262 8166 -213 352 170 C ATOM 1592 CG GLN A 229 8.252 -10.181 15.093 1.00 87.94 C ANISOU 1592 CG GLN A 229 12437 10506 10471 -284 445 98 C ATOM 1593 CD GLN A 229 6.796 -9.891 14.829 1.00111.27 C ANISOU 1593 CD GLN A 229 15321 13552 13404 -357 443 10 C ATOM 1594 OE1 GLN A 229 6.369 -9.688 13.683 1.00110.25 O ANISOU 1594 OE1 GLN A 229 15117 13524 13248 -377 421 -48 O ATOM 1595 NE2 GLN A 229 5.997 -9.893 15.884 1.00101.45 N ANISOU 1595 NE2 GLN A 229 14093 12290 12162 -393 468 -6 N ATOM 1596 N LEU A 230 12.222 -7.828 13.387 1.00 68.88 N ANISOU 1596 N LEU A 230 9912 8216 8043 -91 253 311 N ATOM 1597 CA LEU A 230 12.840 -6.906 12.434 1.00 68.79 C ANISOU 1597 CA LEU A 230 9853 8271 8013 -84 210 338 C ATOM 1598 C LEU A 230 13.120 -7.660 11.135 1.00 73.86 C ANISOU 1598 C LEU A 230 10480 8941 8643 -81 247 302 C ATOM 1599 O LEU A 230 13.570 -8.811 11.169 1.00 74.06 O ANISOU 1599 O LEU A 230 10536 8925 8679 -60 300 289 O ATOM 1600 CB LEU A 230 14.126 -6.271 12.993 1.00 68.68 C ANISOU 1600 CB LEU A 230 9826 8269 8000 -60 177 404 C ATOM 1601 CG LEU A 230 13.973 -4.927 13.717 1.00 72.87 C ANISOU 1601 CG LEU A 230 10362 8801 8524 -82 126 437 C ATOM 1602 CD1 LEU A 230 15.135 -4.679 14.656 1.00 72.89 C ANISOU 1602 CD1 LEU A 230 10352 8816 8528 -73 105 478 C ATOM 1603 CD2 LEU A 230 13.843 -3.768 12.731 1.00 74.84 C ANISOU 1603 CD2 LEU A 230 10605 9086 8745 -104 104 446 C ATOM 1604 N ASN A1002 12.751 -7.051 10.006 1.00 70.39 N ANISOU 1604 N ASN A1002 10006 8566 8173 -95 226 284 N ATOM 1605 CA ASN A1002 12.916 -7.638 8.679 1.00 70.41 C ANISOU 1605 CA ASN A1002 9990 8610 8153 -95 256 243 C ATOM 1606 C ASN A1002 13.525 -6.612 7.719 1.00 74.28 C ANISOU 1606 C ASN A1002 10451 9163 8608 -80 224 286 C ATOM 1607 O ASN A1002 13.829 -5.493 8.135 1.00 73.58 O ANISOU 1607 O ASN A1002 10368 9073 8515 -80 187 342 O ATOM 1608 CB ASN A1002 11.575 -8.181 8.149 1.00 70.65 C ANISOU 1608 CB ASN A1002 10010 8671 8162 -134 278 151 C ATOM 1609 CG ASN A1002 10.424 -7.210 8.213 1.00 85.34 C ANISOU 1609 CG ASN A1002 11841 10593 9993 -138 230 137 C ATOM 1610 OD1 ASN A1002 10.363 -6.231 7.471 1.00 76.55 O ANISOU 1610 OD1 ASN A1002 10706 9546 8835 -104 189 162 O ATOM 1611 ND2 ASN A1002 9.478 -7.472 9.099 1.00 78.00 N ANISOU 1611 ND2 ASN A1002 10915 9645 9078 -170 241 97 N ATOM 1612 N ILE A1003 13.699 -6.995 6.441 1.00 71.13 N ANISOU 1612 N ILE A1003 10033 8813 8178 -75 246 255 N ATOM 1613 CA ILE A1003 14.294 -6.162 5.391 1.00 70.72 C ANISOU 1613 CA ILE A1003 9967 8821 8084 -63 232 292 C ATOM 1614 C ILE A1003 13.505 -4.847 5.175 1.00 73.13 C ANISOU 1614 C ILE A1003 10287 9155 8343 -52 190 316 C ATOM 1615 O ILE A1003 14.131 -3.801 5.007 1.00 72.28 O ANISOU 1615 O ILE A1003 10203 9045 8213 -52 181 379 O ATOM 1616 CB ILE A1003 14.493 -6.967 4.058 1.00 74.18 C ANISOU 1616 CB ILE A1003 10386 9309 8491 -54 269 243 C ATOM 1617 CG1 ILE A1003 15.220 -6.142 2.968 1.00 74.75 C ANISOU 1617 CG1 ILE A1003 10449 9440 8513 -41 266 288 C ATOM 1618 CG2 ILE A1003 13.195 -7.584 3.512 1.00 74.78 C ANISOU 1618 CG2 ILE A1003 10452 9422 8537 -69 276 150 C ATOM 1619 CD1 ILE A1003 16.639 -5.715 3.294 1.00 79.47 C ANISOU 1619 CD1 ILE A1003 11036 10029 9130 -50 277 355 C ATOM 1620 N PHE A1004 12.160 -4.900 5.212 1.00 69.46 N ANISOU 1620 N PHE A1004 9814 8720 7856 -42 171 264 N ATOM 1621 CA PHE A1004 11.267 -3.754 4.997 1.00 69.39 C ANISOU 1621 CA PHE A1004 9821 8756 7788 2 132 280 C ATOM 1622 C PHE A1004 11.469 -2.673 6.064 1.00 71.82 C ANISOU 1622 C PHE A1004 10182 8991 8116 5 110 351 C ATOM 1623 O PHE A1004 11.553 -1.491 5.718 1.00 71.70 O ANISOU 1623 O PHE A1004 10222 8971 8051 39 100 407 O ATOM 1624 CB PHE A1004 9.797 -4.206 4.950 1.00 71.68 C ANISOU 1624 CB PHE A1004 10063 9122 8049 11 118 192 C ATOM 1625 CG PHE A1004 9.535 -5.295 3.935 1.00 74.09 C ANISOU 1625 CG PHE A1004 10318 9504 8330 -14 145 102 C ATOM 1626 CD1 PHE A1004 9.687 -6.637 4.273 1.00 77.21 C ANISOU 1626 CD1 PHE A1004 10706 9849 8781 -83 194 41 C ATOM 1627 CD2 PHE A1004 9.152 -4.980 2.638 1.00 77.43 C ANISOU 1627 CD2 PHE A1004 10715 10041 8664 35 127 78 C ATOM 1628 CE1 PHE A1004 9.465 -7.643 3.330 1.00 78.76 C ANISOU 1628 CE1 PHE A1004 10872 10101 8950 -118 230 -51 C ATOM 1629 CE2 PHE A1004 8.909 -5.989 1.701 1.00 81.00 C ANISOU 1629 CE2 PHE A1004 11119 10572 9087 2 151 -18 C ATOM 1630 CZ PHE A1004 9.080 -7.313 2.049 1.00 78.89 C ANISOU 1630 CZ PHE A1004 10848 10244 8882 -82 205 -85 C ATOM 1631 N GLU A1005 11.589 -3.081 7.344 1.00 66.60 N ANISOU 1631 N GLU A1005 9519 8266 7519 -30 112 349 N ATOM 1632 CA GLU A1005 11.834 -2.162 8.457 1.00 65.55 C ANISOU 1632 CA GLU A1005 9433 8067 7406 -38 93 404 C ATOM 1633 C GLU A1005 13.285 -1.670 8.426 1.00 68.35 C ANISOU 1633 C GLU A1005 9808 8390 7771 -75 107 462 C ATOM 1634 O GLU A1005 13.522 -0.489 8.670 1.00 68.22 O ANISOU 1634 O GLU A1005 9850 8337 7733 -87 100 509 O ATOM 1635 CB GLU A1005 11.506 -2.821 9.801 1.00 66.57 C ANISOU 1635 CB GLU A1005 9551 8152 7589 -59 93 381 C ATOM 1636 CG GLU A1005 10.015 -3.017 10.014 1.00 76.71 C ANISOU 1636 CG GLU A1005 10817 9473 8858 -40 84 323 C ATOM 1637 CD GLU A1005 9.589 -3.634 11.332 1.00 91.73 C ANISOU 1637 CD GLU A1005 12719 11329 10805 -68 96 299 C ATOM 1638 OE1 GLU A1005 8.437 -3.378 11.747 1.00 80.23 O ANISOU 1638 OE1 GLU A1005 11252 9902 9330 -55 84 266 O ATOM 1639 OE2 GLU A1005 10.381 -4.401 11.929 1.00 84.97 O ANISOU 1639 OE2 GLU A1005 11875 10416 9994 -94 121 311 O ATOM 1640 N MET A1006 14.240 -2.573 8.089 1.00 64.29 N ANISOU 1640 N MET A1006 9249 7897 7282 -95 133 452 N ATOM 1641 CA MET A1006 15.686 -2.318 7.962 1.00 64.21 C ANISOU 1641 CA MET A1006 9223 7898 7274 -132 151 490 C ATOM 1642 C MET A1006 15.965 -1.256 6.876 1.00 69.53 C ANISOU 1642 C MET A1006 9937 8589 7891 -147 167 525 C ATOM 1643 O MET A1006 16.722 -0.314 7.123 1.00 69.27 O ANISOU 1643 O MET A1006 9936 8536 7849 -203 179 563 O ATOM 1644 CB MET A1006 16.423 -3.633 7.630 1.00 66.24 C ANISOU 1644 CB MET A1006 9421 8192 7554 -117 179 463 C ATOM 1645 CG MET A1006 17.931 -3.521 7.564 1.00 69.61 C ANISOU 1645 CG MET A1006 9804 8666 7980 -144 196 490 C ATOM 1646 SD MET A1006 18.631 -4.903 6.630 1.00 73.52 S ANISOU 1646 SD MET A1006 10245 9217 8472 -95 239 459 S ATOM 1647 CE MET A1006 20.308 -4.820 7.139 1.00 70.44 C ANISOU 1647 CE MET A1006 9780 8903 8082 -107 246 485 C ATOM 1648 N LEU A1007 15.345 -1.408 5.688 1.00 66.44 N ANISOU 1648 N LEU A1007 9553 8237 7456 -103 174 507 N ATOM 1649 CA LEU A1007 15.513 -0.466 4.586 1.00 66.91 C ANISOU 1649 CA LEU A1007 9668 8310 7446 -97 196 546 C ATOM 1650 C LEU A1007 14.821 0.863 4.876 1.00 72.12 C ANISOU 1650 C LEU A1007 10430 8911 8061 -73 184 587 C ATOM 1651 O LEU A1007 15.328 1.895 4.433 1.00 72.61 O ANISOU 1651 O LEU A1007 10574 8937 8076 -98 220 638 O ATOM 1652 CB LEU A1007 15.034 -1.040 3.248 1.00 66.95 C ANISOU 1652 CB LEU A1007 9649 8388 7400 -42 202 513 C ATOM 1653 CG LEU A1007 15.980 -2.017 2.553 1.00 70.94 C ANISOU 1653 CG LEU A1007 10090 8943 7921 -64 236 488 C ATOM 1654 CD1 LEU A1007 15.303 -2.668 1.366 1.00 71.14 C ANISOU 1654 CD1 LEU A1007 10093 9041 7897 -12 237 437 C ATOM 1655 CD2 LEU A1007 17.282 -1.343 2.136 1.00 72.19 C ANISOU 1655 CD2 LEU A1007 10265 9105 8060 -117 279 540 C ATOM 1656 N ARG A1008 13.701 0.864 5.643 1.00 68.50 N ANISOU 1656 N ARG A1008 9977 8437 7613 -26 146 566 N ATOM 1657 CA ARG A1008 13.064 2.134 5.994 1.00 68.83 C ANISOU 1657 CA ARG A1008 10124 8419 7608 15 138 606 C ATOM 1658 C ARG A1008 13.978 2.910 6.957 1.00 72.79 C ANISOU 1658 C ARG A1008 10684 8830 8143 -75 159 643 C ATOM 1659 O ARG A1008 13.993 4.137 6.914 1.00 73.24 O ANISOU 1659 O ARG A1008 10865 8815 8150 -75 186 689 O ATOM 1660 CB ARG A1008 11.646 1.977 6.569 1.00 69.36 C ANISOU 1660 CB ARG A1008 10171 8512 7670 92 95 569 C ATOM 1661 CG ARG A1008 10.940 3.336 6.611 1.00 82.20 C ANISOU 1661 CG ARG A1008 11918 10094 9220 176 93 615 C ATOM 1662 CD ARG A1008 9.558 3.358 7.210 1.00 93.81 C ANISOU 1662 CD ARG A1008 13366 11605 10672 263 52 580 C ATOM 1663 NE ARG A1008 9.199 4.732 7.565 1.00106.48 N ANISOU 1663 NE ARG A1008 15110 13131 12218 334 61 635 N ATOM 1664 CZ ARG A1008 7.956 5.180 7.715 1.00125.56 C ANISOU 1664 CZ ARG A1008 17546 15592 14570 462 35 626 C ATOM 1665 NH1 ARG A1008 6.922 4.367 7.526 1.00114.65 N ANISOU 1665 NH1 ARG A1008 16034 14354 13174 518 -5 555 N ATOM 1666 NH2 ARG A1008 7.736 6.447 8.042 1.00114.37 N ANISOU 1666 NH2 ARG A1008 16279 14082 13095 535 54 682 N ATOM 1667 N ILE A1009 14.776 2.195 7.778 1.00 68.49 N ANISOU 1667 N ILE A1009 10057 8293 7671 -150 153 619 N ATOM 1668 CA ILE A1009 15.744 2.805 8.693 1.00 68.35 C ANISOU 1668 CA ILE A1009 10063 8228 7678 -246 167 636 C ATOM 1669 C ILE A1009 16.875 3.451 7.862 1.00 74.48 C ANISOU 1669 C ILE A1009 10875 9008 8418 -327 224 664 C ATOM 1670 O ILE A1009 17.114 4.652 7.996 1.00 75.03 O ANISOU 1670 O ILE A1009 11054 9001 8451 -386 261 692 O ATOM 1671 CB ILE A1009 16.280 1.773 9.739 1.00 70.44 C ANISOU 1671 CB ILE A1009 10219 8532 8011 -276 140 602 C ATOM 1672 CG1 ILE A1009 15.205 1.443 10.797 1.00 69.97 C ANISOU 1672 CG1 ILE A1009 10162 8442 7981 -223 100 582 C ATOM 1673 CG2 ILE A1009 17.593 2.250 10.405 1.00 71.02 C ANISOU 1673 CG2 ILE A1009 10274 8615 8094 -383 156 605 C ATOM 1674 CD1 ILE A1009 15.325 0.063 11.428 1.00 74.97 C ANISOU 1674 CD1 ILE A1009 10707 9113 8667 -205 85 549 C ATOM 1675 N ASP A1010 17.528 2.660 6.988 1.00 72.01 N ANISOU 1675 N ASP A1010 10478 8775 8109 -333 241 652 N ATOM 1676 CA ASP A1010 18.666 3.068 6.163 1.00 73.09 C ANISOU 1676 CA ASP A1010 10618 8939 8212 -415 301 669 C ATOM 1677 C ASP A1010 18.331 4.133 5.108 1.00 79.04 C ANISOU 1677 C ASP A1010 11515 9633 8885 -400 351 717 C ATOM 1678 O ASP A1010 19.120 5.065 4.933 1.00 79.42 O ANISOU 1678 O ASP A1010 11638 9640 8899 -503 416 741 O ATOM 1679 CB ASP A1010 19.280 1.843 5.474 1.00 74.74 C ANISOU 1679 CB ASP A1010 10704 9255 8441 -394 303 642 C ATOM 1680 CG ASP A1010 19.870 0.825 6.430 1.00 82.97 C ANISOU 1680 CG ASP A1010 11624 10357 9545 -398 272 605 C ATOM 1681 OD1 ASP A1010 20.755 1.198 7.224 1.00 83.50 O ANISOU 1681 OD1 ASP A1010 11656 10447 9624 -480 277 599 O ATOM 1682 OD2 ASP A1010 19.474 -0.348 6.357 1.00 88.31 O ANISOU 1682 OD2 ASP A1010 12245 11060 10248 -318 248 578 O ATOM 1683 N GLU A1011 17.191 3.993 4.404 1.00 76.51 N ANISOU 1683 N GLU A1011 11234 9315 8523 -274 328 728 N ATOM 1684 CA GLU A1011 16.783 4.912 3.332 1.00 77.49 C ANISOU 1684 CA GLU A1011 11497 9397 8550 -217 372 779 C ATOM 1685 C GLU A1011 15.839 6.038 3.799 1.00 83.66 C ANISOU 1685 C GLU A1011 12433 10073 9282 -150 371 817 C ATOM 1686 O GLU A1011 15.828 7.109 3.183 1.00 84.67 O ANISOU 1686 O GLU A1011 12723 10123 9324 -131 432 874 O ATOM 1687 CB GLU A1011 16.107 4.148 2.174 1.00 78.37 C ANISOU 1687 CB GLU A1011 11556 9602 8618 -100 347 764 C ATOM 1688 CG GLU A1011 16.979 3.113 1.479 1.00 85.60 C ANISOU 1688 CG GLU A1011 12351 10611 9561 -144 361 731 C ATOM 1689 CD GLU A1011 17.969 3.609 0.442 1.00103.24 C ANISOU 1689 CD GLU A1011 14637 12851 11739 -204 440 770 C ATOM 1690 OE1 GLU A1011 18.125 4.842 0.284 1.00 94.98 O ANISOU 1690 OE1 GLU A1011 13739 11717 10633 -237 498 827 O ATOM 1691 OE2 GLU A1011 18.626 2.749 -0.188 1.00 99.06 O ANISOU 1691 OE2 GLU A1011 14007 12408 11223 -223 452 741 O ATOM 1692 N GLY A1012 15.035 5.775 4.828 1.00 80.36 N ANISOU 1692 N GLY A1012 11974 9651 8908 -104 309 788 N ATOM 1693 CA GLY A1012 14.053 6.730 5.329 1.00 81.23 C ANISOU 1693 CA GLY A1012 12215 9678 8972 -18 302 816 C ATOM 1694 C GLY A1012 12.821 6.795 4.446 1.00 87.66 C ANISOU 1694 C GLY A1012 13061 10549 9696 161 276 830 C ATOM 1695 O GLY A1012 12.660 5.971 3.544 1.00 86.64 O ANISOU 1695 O GLY A1012 12834 10532 9552 204 255 803 O ATOM 1696 N LEU A1013 11.933 7.768 4.707 1.00 86.98 N ANISOU 1696 N LEU A1013 13109 10399 9541 273 278 865 N ATOM 1697 CA LEU A1013 10.723 7.968 3.909 1.00 88.05 C ANISOU 1697 CA LEU A1013 13277 10611 9568 470 251 879 C ATOM 1698 C LEU A1013 10.452 9.459 3.730 1.00 94.18 C ANISOU 1698 C LEU A1013 14295 11260 10230 574 311 962 C ATOM 1699 O LEU A1013 10.224 10.187 4.701 1.00 94.26 O ANISOU 1699 O LEU A1013 14406 11161 10247 577 324 976 O ATOM 1700 CB LEU A1013 9.493 7.241 4.500 1.00 87.55 C ANISOU 1700 CB LEU A1013 13072 10666 9528 558 168 810 C ATOM 1701 CG LEU A1013 8.121 7.522 3.845 1.00 93.21 C ANISOU 1701 CG LEU A1013 13798 11499 10119 773 131 809 C ATOM 1702 CD1 LEU A1013 8.020 6.925 2.447 1.00 93.88 C ANISOU 1702 CD1 LEU A1013 13806 11726 10138 830 118 789 C ATOM 1703 CD2 LEU A1013 6.994 6.999 4.699 1.00 95.22 C ANISOU 1703 CD2 LEU A1013 13923 11853 10403 824 65 737 C ATOM 1704 N ARG A1014 10.504 9.898 2.471 1.00 92.15 N ANISOU 1704 N ARG A1014 14143 11009 9863 661 356 1017 N ATOM 1705 CA ARG A1014 10.255 11.269 2.046 1.00 93.80 C ANISOU 1705 CA ARG A1014 14611 11092 9936 787 429 1108 C ATOM 1706 C ARG A1014 9.290 11.207 0.871 1.00 99.10 C ANISOU 1706 C ARG A1014 15277 11908 10469 1019 394 1127 C ATOM 1707 O ARG A1014 9.658 10.728 -0.204 1.00 98.85 O ANISOU 1707 O ARG A1014 15191 11962 10407 1010 400 1127 O ATOM 1708 CB ARG A1014 11.573 11.986 1.688 1.00 95.12 C ANISOU 1708 CB ARG A1014 14949 11097 10096 628 548 1165 C ATOM 1709 CG ARG A1014 12.519 12.173 2.870 1.00107.08 C ANISOU 1709 CG ARG A1014 16469 12489 11726 399 585 1136 C ATOM 1710 CD ARG A1014 13.802 12.874 2.480 1.00122.46 C ANISOU 1710 CD ARG A1014 18567 14304 13657 221 710 1175 C ATOM 1711 NE ARG A1014 14.792 12.816 3.558 1.00134.61 N ANISOU 1711 NE ARG A1014 20043 15793 15310 -16 728 1121 N ATOM 1712 CZ ARG A1014 15.932 13.498 3.574 1.00151.17 C ANISOU 1712 CZ ARG A1014 22255 17778 17405 -216 838 1128 C ATOM 1713 NH1 ARG A1014 16.770 13.378 4.595 1.00140.64 N ANISOU 1713 NH1 ARG A1014 20830 16441 16167 -420 838 1064 N ATOM 1714 NH2 ARG A1014 16.242 14.312 2.570 1.00137.89 N ANISOU 1714 NH2 ARG A1014 20780 15994 15617 -216 954 1196 N ATOM 1715 N LEU A1015 8.035 11.635 1.094 1.00 96.69 N ANISOU 1715 N LEU A1015 15009 11654 10076 1233 350 1134 N ATOM 1716 CA LEU A1015 6.961 11.595 0.096 1.00 97.65 C ANISOU 1716 CA LEU A1015 15100 11955 10046 1482 302 1138 C ATOM 1717 C LEU A1015 7.175 12.615 -1.054 1.00103.59 C ANISOU 1717 C LEU A1015 16105 12622 10633 1621 389 1251 C ATOM 1718 O LEU A1015 6.541 12.487 -2.106 1.00104.11 O ANISOU 1718 O LEU A1015 16140 12852 10566 1810 354 1258 O ATOM 1719 CB LEU A1015 5.580 11.800 0.765 1.00 97.98 C ANISOU 1719 CB LEU A1015 15098 12094 10035 1675 233 1108 C ATOM 1720 CG LEU A1015 4.943 10.615 1.562 1.00101.34 C ANISOU 1720 CG LEU A1015 15239 12693 10574 1604 133 983 C ATOM 1721 CD1 LEU A1015 4.894 9.309 0.755 1.00100.84 C ANISOU 1721 CD1 LEU A1015 14942 12837 10534 1546 75 896 C ATOM 1722 CD2 LEU A1015 5.587 10.413 2.931 1.00102.73 C ANISOU 1722 CD2 LEU A1015 15391 12722 10919 1387 147 956 C ATOM 1723 N LYS A1016 8.091 13.588 -0.867 1.00100.64 N ANISOU 1723 N LYS A1016 15981 11998 10262 1516 508 1331 N ATOM 1724 CA LYS A1016 8.444 14.591 -1.877 1.00102.23 C ANISOU 1724 CA LYS A1016 16459 12070 10312 1609 622 1444 C ATOM 1725 C LYS A1016 9.750 14.191 -2.587 1.00104.90 C ANISOU 1725 C LYS A1016 16773 12377 10706 1390 686 1447 C ATOM 1726 O LYS A1016 10.582 13.499 -1.997 1.00103.19 O ANISOU 1726 O LYS A1016 16398 12156 10652 1143 673 1380 O ATOM 1727 CB LYS A1016 8.558 16.003 -1.257 1.00106.41 C ANISOU 1727 CB LYS A1016 17313 12328 10788 1632 735 1528 C ATOM 1728 CG LYS A1016 9.530 16.125 -0.078 1.00122.36 C ANISOU 1728 CG LYS A1016 19348 14172 12970 1337 786 1490 C ATOM 1729 N ILE A1017 9.922 14.626 -3.848 1.00102.07 N ANISOU 1729 N ILE A1017 16571 12006 10204 1493 757 1526 N ATOM 1730 CA ILE A1017 11.117 14.338 -4.647 1.00101.58 C ANISOU 1730 CA ILE A1017 16505 11922 10169 1309 831 1537 C ATOM 1731 C ILE A1017 12.308 15.141 -4.077 1.00105.28 C ANISOU 1731 C ILE A1017 17166 12135 10703 1061 971 1573 C ATOM 1732 O ILE A1017 12.204 16.352 -3.866 1.00106.40 O ANISOU 1732 O ILE A1017 17601 12072 10757 1118 1073 1651 O ATOM 1733 CB ILE A1017 10.878 14.564 -6.176 1.00106.22 C ANISOU 1733 CB ILE A1017 17205 12584 10569 1506 865 1611 C ATOM 1734 CG1 ILE A1017 12.098 14.159 -7.020 1.00106.44 C ANISOU 1734 CG1 ILE A1017 17201 12613 10628 1313 938 1613 C ATOM 1735 CG2 ILE A1017 10.385 15.977 -6.526 1.00109.45 C ANISOU 1735 CG2 ILE A1017 17974 12831 10783 1735 965 1740 C ATOM 1736 N TYR A1018 13.412 14.436 -3.784 1.00100.31 N ANISOU 1736 N TYR A1018 16363 11528 10223 787 976 1505 N ATOM 1737 CA TYR A1018 14.629 14.992 -3.187 1.00100.44 C ANISOU 1737 CA TYR A1018 16483 11363 10315 512 1093 1504 C ATOM 1738 C TYR A1018 15.891 14.415 -3.849 1.00104.86 C ANISOU 1738 C TYR A1018 16927 11988 10926 303 1144 1476 C ATOM 1739 O TYR A1018 15.791 13.520 -4.687 1.00103.35 O ANISOU 1739 O TYR A1018 16571 11973 10725 375 1081 1456 O ATOM 1740 CB TYR A1018 14.641 14.709 -1.662 1.00100.10 C ANISOU 1740 CB TYR A1018 16303 11309 10424 385 1023 1423 C ATOM 1741 CG TYR A1018 14.817 13.247 -1.298 1.00 99.57 C ANISOU 1741 CG TYR A1018 15888 11444 10502 303 897 1321 C ATOM 1742 CD1 TYR A1018 13.737 12.367 -1.316 1.00100.39 C ANISOU 1742 CD1 TYR A1018 15809 11720 10615 479 763 1280 C ATOM 1743 CD2 TYR A1018 16.060 12.745 -0.920 1.00 99.56 C ANISOU 1743 CD2 TYR A1018 15745 11464 10618 49 919 1262 C ATOM 1744 CE1 TYR A1018 13.898 11.017 -1.007 1.00 99.27 C ANISOU 1744 CE1 TYR A1018 15383 11738 10597 400 667 1188 C ATOM 1745 CE2 TYR A1018 16.232 11.397 -0.606 1.00 98.71 C ANISOU 1745 CE2 TYR A1018 15348 11529 10631 -2 814 1178 C ATOM 1746 CZ TYR A1018 15.146 10.537 -0.645 1.00104.60 C ANISOU 1746 CZ TYR A1018 15945 12412 11385 171 693 1144 C ATOM 1747 OH TYR A1018 15.300 9.209 -0.326 1.00103.47 O ANISOU 1747 OH TYR A1018 15549 12412 11353 117 607 1063 O ATOM 1748 N LYS A1019 17.076 14.913 -3.449 1.00103.46 N ANISOU 1748 N LYS A1019 16826 11682 10802 40 1259 1466 N ATOM 1749 CA LYS A1019 18.368 14.441 -3.946 1.00103.90 C ANISOU 1749 CA LYS A1019 16762 11808 10907 -178 1318 1430 C ATOM 1750 C LYS A1019 19.093 13.656 -2.849 1.00107.99 C ANISOU 1750 C LYS A1019 17018 12418 11596 -384 1250 1323 C ATOM 1751 O LYS A1019 19.163 14.115 -1.704 1.00107.80 O ANISOU 1751 O LYS A1019 17033 12297 11628 -483 1256 1293 O ATOM 1752 CB LYS A1019 19.228 15.613 -4.445 1.00108.36 C ANISOU 1752 CB LYS A1019 17608 12185 11380 -332 1517 1493 C ATOM 1753 N ASP A1020 19.622 12.470 -3.199 1.00104.32 N ANISOU 1753 N ASP A1020 16293 12142 11203 -432 1188 1264 N ATOM 1754 CA ASP A1020 20.336 11.595 -2.265 1.00103.31 C ANISOU 1754 CA ASP A1020 15907 12126 11220 -589 1121 1168 C ATOM 1755 C ASP A1020 21.805 12.053 -2.065 1.00110.13 C ANISOU 1755 C ASP A1020 16776 12960 12108 -869 1241 1136 C ATOM 1756 O ASP A1020 22.190 13.116 -2.565 1.00111.49 O ANISOU 1756 O ASP A1020 17175 12996 12190 -959 1384 1187 O ATOM 1757 CB ASP A1020 20.265 10.125 -2.745 1.00103.53 C ANISOU 1757 CB ASP A1020 15678 12358 11301 -504 1015 1119 C ATOM 1758 CG ASP A1020 20.955 9.780 -4.063 1.00111.94 C ANISOU 1758 CG ASP A1020 16709 13511 12312 -527 1077 1133 C ATOM 1759 OD1 ASP A1020 21.491 10.700 -4.721 1.00114.22 O ANISOU 1759 OD1 ASP A1020 17179 13706 12512 -607 1210 1188 O ATOM 1760 OD2 ASP A1020 20.961 8.586 -4.432 1.00114.88 O ANISOU 1760 OD2 ASP A1020 16884 14039 12726 -469 1001 1086 O ATOM 1761 N THR A1021 22.616 11.247 -1.334 1.00106.91 N ANISOU 1761 N THR A1021 16121 12687 11812 -1005 1187 1048 N ATOM 1762 CA THR A1021 24.039 11.511 -1.073 1.00107.98 C ANISOU 1762 CA THR A1021 16194 12862 11972 -1269 1280 993 C ATOM 1763 C THR A1021 24.847 11.484 -2.383 1.00113.47 C ANISOU 1763 C THR A1021 16894 13618 12600 -1337 1384 1013 C ATOM 1764 O THR A1021 25.790 12.264 -2.537 1.00114.80 O ANISOU 1764 O THR A1021 17149 13741 12729 -1551 1523 1003 O ATOM 1765 CB THR A1021 24.594 10.498 -0.068 1.00114.21 C ANISOU 1765 CB THR A1021 16696 13820 12878 -1332 1176 899 C ATOM 1766 N GLU A1022 24.450 10.605 -3.329 1.00109.27 N ANISOU 1766 N GLU A1022 16276 13189 12051 -1163 1325 1037 N ATOM 1767 CA GLU A1022 25.070 10.449 -4.646 1.00109.91 C ANISOU 1767 CA GLU A1022 16354 13341 12064 -1186 1409 1060 C ATOM 1768 C GLU A1022 24.806 11.676 -5.546 1.00115.46 C ANISOU 1768 C GLU A1022 17374 13867 12629 -1174 1548 1157 C ATOM 1769 O GLU A1022 25.578 11.929 -6.474 1.00116.32 O ANISOU 1769 O GLU A1022 17534 13992 12670 -1274 1669 1177 O ATOM 1770 CB GLU A1022 24.561 9.169 -5.321 1.00109.97 C ANISOU 1770 CB GLU A1022 16201 13496 12088 -988 1297 1051 C ATOM 1771 N GLY A1023 23.732 12.416 -5.253 1.00111.88 N ANISOU 1771 N GLY A1023 17133 13248 12128 -1043 1535 1218 N ATOM 1772 CA GLY A1023 23.344 13.623 -5.977 1.00113.22 C ANISOU 1772 CA GLY A1023 17639 13226 12155 -987 1663 1321 C ATOM 1773 C GLY A1023 22.156 13.472 -6.907 1.00116.31 C ANISOU 1773 C GLY A1023 18122 13627 12445 -687 1604 1399 C ATOM 1774 O GLY A1023 21.580 14.477 -7.337 1.00117.01 O ANISOU 1774 O GLY A1023 18503 13552 12405 -575 1685 1493 O ATOM 1775 N TYR A1024 21.783 12.217 -7.227 1.00111.10 N ANISOU 1775 N TYR A1024 17220 13162 11830 -552 1466 1357 N ATOM 1776 CA TYR A1024 20.670 11.899 -8.126 1.00110.50 C ANISOU 1776 CA TYR A1024 17176 13151 11660 -279 1392 1404 C ATOM 1777 C TYR A1024 19.310 12.020 -7.424 1.00112.08 C ANISOU 1777 C TYR A1024 17410 13316 11858 -82 1280 1412 C ATOM 1778 O TYR A1024 19.241 11.960 -6.194 1.00110.46 O ANISOU 1778 O TYR A1024 17130 13079 11762 -156 1226 1362 O ATOM 1779 CB TYR A1024 20.830 10.486 -8.712 1.00110.78 C ANISOU 1779 CB TYR A1024 16939 13407 11744 -239 1300 1336 C ATOM 1780 CG TYR A1024 22.202 10.182 -9.276 1.00113.50 C ANISOU 1780 CG TYR A1024 17195 13823 12107 -427 1393 1310 C ATOM 1781 CD1 TYR A1024 22.581 10.646 -10.533 1.00117.23 C ANISOU 1781 CD1 TYR A1024 17816 14275 12450 -423 1513 1376 C ATOM 1782 CD2 TYR A1024 23.098 9.378 -8.580 1.00113.37 C ANISOU 1782 CD2 TYR A1024 16937 13911 12227 -590 1358 1218 C ATOM 1783 CE1 TYR A1024 23.836 10.350 -11.066 1.00119.00 C ANISOU 1783 CE1 TYR A1024 17946 14582 12688 -596 1602 1346 C ATOM 1784 CE2 TYR A1024 24.357 9.077 -9.101 1.00115.04 C ANISOU 1784 CE2 TYR A1024 17048 14216 12447 -747 1441 1188 C ATOM 1785 CZ TYR A1024 24.721 9.564 -10.345 1.00125.01 C ANISOU 1785 CZ TYR A1024 18454 15459 13587 -756 1564 1249 C ATOM 1786 OH TYR A1024 25.960 9.268 -10.863 1.00127.43 O ANISOU 1786 OH TYR A1024 18650 15870 13896 -913 1651 1214 O ATOM 1787 N TYR A1025 18.228 12.181 -8.218 1.00108.13 N ANISOU 1787 N TYR A1025 17014 12842 11227 174 1245 1471 N ATOM 1788 CA TYR A1025 16.856 12.318 -7.723 1.00106.92 C ANISOU 1788 CA TYR A1025 16889 12693 11044 391 1142 1479 C ATOM 1789 C TYR A1025 16.307 10.989 -7.180 1.00106.98 C ANISOU 1789 C TYR A1025 16590 12886 11171 429 976 1372 C ATOM 1790 O TYR A1025 16.406 9.954 -7.844 1.00105.78 O ANISOU 1790 O TYR A1025 16256 12900 11036 442 922 1320 O ATOM 1791 CB TYR A1025 15.932 12.873 -8.819 1.00109.60 C ANISOU 1791 CB TYR A1025 17416 13041 11185 664 1156 1568 C ATOM 1792 CG TYR A1025 16.173 14.334 -9.136 1.00113.55 C ANISOU 1792 CG TYR A1025 18281 13312 11550 678 1322 1687 C ATOM 1793 CD1 TYR A1025 15.568 15.341 -8.390 1.00116.20 C ANISOU 1793 CD1 TYR A1025 18831 13475 11843 764 1353 1738 C ATOM 1794 CD2 TYR A1025 16.994 14.710 -10.197 1.00115.78 C ANISOU 1794 CD2 TYR A1025 18710 13540 11739 607 1461 1750 C ATOM 1795 CE1 TYR A1025 15.791 16.687 -8.675 1.00119.09 C ANISOU 1795 CE1 TYR A1025 19566 13604 12078 776 1523 1849 C ATOM 1796 CE2 TYR A1025 17.216 16.055 -10.497 1.00118.85 C ANISOU 1796 CE2 TYR A1025 19465 13697 11996 610 1634 1862 C ATOM 1797 CZ TYR A1025 16.610 17.040 -9.735 1.00127.35 C ANISOU 1797 CZ TYR A1025 20767 14588 13032 696 1667 1911 C ATOM 1798 OH TYR A1025 16.826 18.366 -10.029 1.00131.32 O ANISOU 1798 OH TYR A1025 21661 14838 13398 700 1853 2022 O ATOM 1799 N THR A1026 15.732 11.041 -5.961 1.00101.30 N ANISOU 1799 N THR A1026 15831 12128 10530 439 907 1339 N ATOM 1800 CA THR A1026 15.147 9.913 -5.223 1.00 98.74 C ANISOU 1800 CA THR A1026 15255 11943 10321 460 767 1242 C ATOM 1801 C THR A1026 13.775 10.341 -4.627 1.00101.53 C ANISOU 1801 C THR A1026 15666 12284 10627 651 697 1252 C ATOM 1802 O THR A1026 13.502 11.540 -4.528 1.00102.00 O ANISOU 1802 O THR A1026 15963 12197 10595 730 763 1332 O ATOM 1803 CB THR A1026 16.148 9.443 -4.132 1.00103.80 C ANISOU 1803 CB THR A1026 15758 12553 11128 224 768 1178 C ATOM 1804 OG1 THR A1026 17.471 9.405 -4.669 1.00104.17 O ANISOU 1804 OG1 THR A1026 15799 12593 11189 55 860 1184 O ATOM 1805 CG2 THR A1026 15.814 8.078 -3.562 1.00 99.72 C ANISOU 1805 CG2 THR A1026 14981 12179 10728 223 647 1080 C ATOM 1806 N ILE A1027 12.911 9.356 -4.267 1.00 96.22 N ANISOU 1806 N ILE A1027 14783 11767 10008 726 573 1169 N ATOM 1807 CA ILE A1027 11.585 9.562 -3.656 1.00 95.46 C ANISOU 1807 CA ILE A1027 14684 11708 9878 895 495 1155 C ATOM 1808 C ILE A1027 11.174 8.299 -2.848 1.00 96.62 C ANISOU 1808 C ILE A1027 14571 11983 10158 835 389 1040 C ATOM 1809 O ILE A1027 11.605 7.192 -3.172 1.00 95.54 O ANISOU 1809 O ILE A1027 14266 11947 10089 743 363 975 O ATOM 1810 CB ILE A1027 10.501 9.983 -4.705 1.00 99.79 C ANISOU 1810 CB ILE A1027 15317 12362 10238 1165 473 1197 C ATOM 1811 CG1 ILE A1027 9.256 10.607 -4.014 1.00100.74 C ANISOU 1811 CG1 ILE A1027 15496 12483 10295 1354 424 1208 C ATOM 1812 CG2 ILE A1027 10.128 8.833 -5.658 1.00 99.89 C ANISOU 1812 CG2 ILE A1027 15124 12609 10220 1221 398 1120 C ATOM 1813 CD1 ILE A1027 8.429 11.588 -4.830 1.00111.07 C ANISOU 1813 CD1 ILE A1027 16999 13812 11393 1635 446 1295 C ATOM 1814 N GLY A1028 10.355 8.497 -1.810 1.00 91.97 N ANISOU 1814 N GLY A1028 13969 11378 9596 891 339 1020 N ATOM 1815 CA GLY A1028 9.846 7.434 -0.948 1.00 90.07 C ANISOU 1815 CA GLY A1028 13517 11238 9467 843 253 919 C ATOM 1816 C GLY A1028 10.919 6.767 -0.117 1.00 91.28 C ANISOU 1816 C GLY A1028 13579 11323 9781 623 266 882 C ATOM 1817 O GLY A1028 11.632 7.437 0.637 1.00 90.88 O ANISOU 1817 O GLY A1028 13630 11123 9779 518 316 922 O ATOM 1818 N ILE A1029 11.049 5.441 -0.260 1.00 85.63 N ANISOU 1818 N ILE A1029 12676 10722 9138 555 226 801 N ATOM 1819 CA ILE A1029 12.066 4.686 0.467 1.00 83.84 C ANISOU 1819 CA ILE A1029 12355 10452 9048 379 236 766 C ATOM 1820 C ILE A1029 13.147 4.246 -0.538 1.00 86.67 C ANISOU 1820 C ILE A1029 12686 10841 9405 305 282 771 C ATOM 1821 O ILE A1029 13.040 3.182 -1.161 1.00 86.21 O ANISOU 1821 O ILE A1029 12507 10895 9354 315 257 710 O ATOM 1822 CB ILE A1029 11.487 3.508 1.311 1.00 85.80 C ANISOU 1822 CB ILE A1029 12440 10771 9389 352 171 675 C ATOM 1823 CG1 ILE A1029 10.281 3.958 2.169 1.00 86.16 C ANISOU 1823 CG1 ILE A1029 12505 10815 9417 441 127 665 C ATOM 1824 CG2 ILE A1029 12.575 2.893 2.202 1.00 85.57 C ANISOU 1824 CG2 ILE A1029 12347 10681 9485 200 187 658 C ATOM 1825 CD1 ILE A1029 9.197 2.920 2.325 1.00 92.22 C ANISOU 1825 CD1 ILE A1029 13123 11716 10199 477 69 569 C ATOM 1826 N GLY A1030 14.147 5.113 -0.699 1.00 82.35 N ANISOU 1826 N GLY A1030 12258 10192 8840 229 358 839 N ATOM 1827 CA GLY A1030 15.307 4.921 -1.565 1.00 82.02 C ANISOU 1827 CA GLY A1030 12206 10167 8791 143 421 853 C ATOM 1828 C GLY A1030 15.044 4.514 -3.001 1.00 85.49 C ANISOU 1828 C GLY A1030 12626 10716 9140 236 421 847 C ATOM 1829 O GLY A1030 15.809 3.723 -3.561 1.00 84.79 O ANISOU 1829 O GLY A1030 12444 10692 9079 173 440 815 O ATOM 1830 N HIS A1031 13.968 5.048 -3.610 1.00 82.28 N ANISOU 1830 N HIS A1031 12304 10343 8615 399 401 875 N ATOM 1831 CA HIS A1031 13.626 4.743 -4.997 1.00 82.40 C ANISOU 1831 CA HIS A1031 12305 10481 8522 506 396 867 C ATOM 1832 C HIS A1031 14.241 5.785 -5.921 1.00 88.17 C ANISOU 1832 C HIS A1031 13220 11138 9143 523 490 965 C ATOM 1833 O HIS A1031 13.761 6.920 -5.979 1.00 88.75 O ANISOU 1833 O HIS A1031 13471 11131 9117 627 519 1041 O ATOM 1834 CB HIS A1031 12.103 4.653 -5.203 1.00 83.05 C ANISOU 1834 CB HIS A1031 12353 10685 8518 685 315 830 C ATOM 1835 CG HIS A1031 11.708 4.208 -6.577 1.00 86.94 C ANISOU 1835 CG HIS A1031 12800 11337 8896 790 296 800 C ATOM 1836 ND1 HIS A1031 11.307 2.913 -6.825 1.00 88.06 N ANISOU 1836 ND1 HIS A1031 12759 11629 9070 772 238 684 N ATOM 1837 CD2 HIS A1031 11.679 4.902 -7.738 1.00 89.86 C ANISOU 1837 CD2 HIS A1031 13295 11734 9114 909 335 868 C ATOM 1838 CE1 HIS A1031 11.045 2.856 -8.119 1.00 88.38 C ANISOU 1838 CE1 HIS A1031 12805 11796 8981 874 236 678 C ATOM 1839 NE2 HIS A1031 11.259 4.028 -8.711 1.00 89.80 N ANISOU 1839 NE2 HIS A1031 13166 11911 9044 968 290 791 N ATOM 1840 N LEU A1032 15.300 5.388 -6.647 1.00 85.34 N ANISOU 1840 N LEU A1032 12828 10804 8795 425 547 964 N ATOM 1841 CA LEU A1032 15.989 6.234 -7.617 1.00 86.65 C ANISOU 1841 CA LEU A1032 13156 10910 8856 417 651 1049 C ATOM 1842 C LEU A1032 15.088 6.423 -8.840 1.00 91.92 C ANISOU 1842 C LEU A1032 13892 11674 9357 620 633 1077 C ATOM 1843 O LEU A1032 14.612 5.443 -9.421 1.00 91.24 O ANISOU 1843 O LEU A1032 13662 11751 9255 687 565 1003 O ATOM 1844 CB LEU A1032 17.347 5.611 -7.998 1.00 86.68 C ANISOU 1844 CB LEU A1032 13065 10946 8922 256 710 1022 C ATOM 1845 CG LEU A1032 18.129 6.249 -9.151 1.00 93.08 C ANISOU 1845 CG LEU A1032 14011 11730 9627 229 825 1093 C ATOM 1846 CD1 LEU A1032 18.753 7.568 -8.737 1.00 94.16 C ANISOU 1846 CD1 LEU A1032 14344 11689 9744 120 936 1173 C ATOM 1847 CD2 LEU A1032 19.199 5.309 -9.652 1.00 95.80 C ANISOU 1847 CD2 LEU A1032 14206 12171 10023 119 853 1041 C ATOM 1848 N LEU A1033 14.839 7.683 -9.206 1.00 90.37 N ANISOU 1848 N LEU A1033 13926 11379 9030 723 697 1179 N ATOM 1849 CA LEU A1033 13.969 8.038 -10.324 1.00 91.87 C ANISOU 1849 CA LEU A1033 14211 11660 9035 950 684 1223 C ATOM 1850 C LEU A1033 14.730 8.086 -11.644 1.00 98.33 C ANISOU 1850 C LEU A1033 15100 12503 9758 937 770 1267 C ATOM 1851 O LEU A1033 14.359 7.385 -12.585 1.00 97.93 O ANISOU 1851 O LEU A1033 14948 12626 9635 1034 719 1221 O ATOM 1852 CB LEU A1033 13.302 9.391 -10.063 1.00 92.97 C ANISOU 1852 CB LEU A1033 14591 11671 9063 1100 720 1322 C ATOM 1853 CG LEU A1033 12.385 9.453 -8.863 1.00 96.56 C ANISOU 1853 CG LEU A1033 14992 12116 9579 1157 635 1285 C ATOM 1854 CD1 LEU A1033 12.654 10.693 -8.056 1.00 97.21 C ANISOU 1854 CD1 LEU A1033 15304 11965 9667 1114 723 1370 C ATOM 1855 CD2 LEU A1033 10.943 9.363 -9.288 1.00 99.45 C ANISOU 1855 CD2 LEU A1033 15311 12662 9813 1419 537 1262 C ATOM 1856 N THR A1034 15.774 8.934 -11.718 1.00 97.21 N ANISOU 1856 N THR A1034 15137 12192 9608 810 906 1350 N ATOM 1857 CA THR A1034 16.588 9.126 -12.916 1.00 98.90 C ANISOU 1857 CA THR A1034 15446 12406 9726 776 1013 1403 C ATOM 1858 C THR A1034 18.022 9.536 -12.545 1.00104.89 C ANISOU 1858 C THR A1034 16264 13018 10571 516 1145 1427 C ATOM 1859 O THR A1034 18.275 10.040 -11.448 1.00103.81 O ANISOU 1859 O THR A1034 16173 12745 10523 396 1170 1431 O ATOM 1860 CB THR A1034 15.924 10.157 -13.875 1.00107.97 C ANISOU 1860 CB THR A1034 16852 13518 10652 1004 1067 1517 C ATOM 1861 OG1 THR A1034 16.542 10.074 -15.162 1.00108.09 O ANISOU 1861 OG1 THR A1034 16917 13586 10564 1001 1147 1552 O ATOM 1862 CG2 THR A1034 15.977 11.601 -13.352 1.00106.99 C ANISOU 1862 CG2 THR A1034 17025 13152 10477 1003 1179 1627 C ATOM 1863 N LYS A1035 18.945 9.330 -13.490 1.00104.31 N ANISOU 1863 N LYS A1035 16185 12987 10461 430 1230 1436 N ATOM 1864 CA LYS A1035 20.361 9.681 -13.385 1.00105.70 C ANISOU 1864 CA LYS A1035 16399 13072 10691 182 1367 1449 C ATOM 1865 C LYS A1035 20.575 11.116 -13.914 1.00113.60 C ANISOU 1865 C LYS A1035 17732 13888 11542 180 1532 1574 C ATOM 1866 O LYS A1035 21.636 11.706 -13.691 1.00114.07 O ANISOU 1866 O LYS A1035 17877 13833 11631 -42 1668 1591 O ATOM 1867 CB LYS A1035 21.232 8.669 -14.169 1.00108.17 C ANISOU 1867 CB LYS A1035 16526 13543 11032 99 1379 1390 C ATOM 1868 CG LYS A1035 20.857 7.195 -13.976 1.00120.77 C ANISOU 1868 CG LYS A1035 17840 15317 12728 155 1228 1276 C ATOM 1869 CD LYS A1035 19.987 6.667 -15.128 1.00129.74 C ANISOU 1869 CD LYS A1035 18957 16596 13742 365 1162 1266 C ATOM 1870 CE LYS A1035 19.050 5.573 -14.678 1.00135.57 C ANISOU 1870 CE LYS A1035 19496 17459 14555 458 1005 1163 C ATOM 1871 NZ LYS A1035 17.994 5.303 -15.689 1.00141.88 N ANISOU 1871 NZ LYS A1035 20300 18397 15213 669 937 1151 N ATOM 1872 N SER A1036 19.550 11.668 -14.606 1.00112.29 N ANISOU 1872 N SER A1036 17757 13701 11209 431 1524 1657 N ATOM 1873 CA SER A1036 19.559 12.997 -15.215 1.00114.95 C ANISOU 1873 CA SER A1036 18447 13857 11372 494 1679 1789 C ATOM 1874 C SER A1036 19.442 14.117 -14.174 1.00120.89 C ANISOU 1874 C SER A1036 19415 14375 12143 434 1749 1838 C ATOM 1875 O SER A1036 18.516 14.095 -13.358 1.00119.62 O ANISOU 1875 O SER A1036 19213 14215 12023 557 1635 1816 O ATOM 1876 CB SER A1036 18.434 13.123 -16.239 1.00119.42 C ANISOU 1876 CB SER A1036 19123 14508 11741 821 1629 1856 C ATOM 1877 OG SER A1036 18.420 14.400 -16.857 1.00130.12 O ANISOU 1877 OG SER A1036 20847 15682 12911 912 1786 1996 O ATOM 1878 N PRO A1037 20.335 15.138 -14.225 1.00119.94 N ANISOU 1878 N PRO A1037 19542 14050 11981 248 1945 1901 N ATOM 1879 CA PRO A1037 20.228 16.253 -13.271 1.00120.76 C ANISOU 1879 CA PRO A1037 19882 13911 12090 184 2027 1942 C ATOM 1880 C PRO A1037 19.192 17.275 -13.760 1.00126.45 C ANISOU 1880 C PRO A1037 20949 14490 12606 478 2077 2075 C ATOM 1881 O PRO A1037 19.525 18.416 -14.103 1.00128.58 O ANISOU 1881 O PRO A1037 21569 14533 12752 439 2269 2174 O ATOM 1882 CB PRO A1037 21.662 16.810 -13.204 1.00123.68 C ANISOU 1882 CB PRO A1037 20350 14147 12495 -161 2223 1935 C ATOM 1883 CG PRO A1037 22.423 16.155 -14.335 1.00128.09 C ANISOU 1883 CG PRO A1037 20781 14863 13023 -225 2263 1922 C ATOM 1884 CD PRO A1037 21.475 15.330 -15.143 1.00122.76 C ANISOU 1884 CD PRO A1037 19979 14385 12280 76 2110 1931 C ATOM 1885 N SER A1038 17.916 16.837 -13.802 1.00121.65 N ANISOU 1885 N SER A1038 20240 14026 11954 780 1907 2071 N ATOM 1886 CA SER A1038 16.767 17.623 -14.248 1.00122.81 C ANISOU 1886 CA SER A1038 20652 14111 11899 1122 1910 2183 C ATOM 1887 C SER A1038 15.507 17.200 -13.489 1.00124.38 C ANISOU 1887 C SER A1038 20677 14441 12142 1333 1715 2127 C ATOM 1888 O SER A1038 15.145 16.021 -13.504 1.00122.19 O ANISOU 1888 O SER A1038 20066 14414 11946 1369 1549 2027 O ATOM 1889 CB SER A1038 16.569 17.463 -15.753 1.00127.78 C ANISOU 1889 CB SER A1038 21338 14869 12343 1325 1925 2249 C ATOM 1890 OG SER A1038 15.491 18.248 -16.234 1.00139.06 O ANISOU 1890 OG SER A1038 23029 16256 13552 1680 1933 2362 O ATOM 1891 N LEU A1039 14.856 18.171 -12.815 1.00121.30 N ANISOU 1891 N LEU A1039 20521 13875 11693 1462 1748 2189 N ATOM 1892 CA LEU A1039 13.648 17.981 -12.006 1.00119.90 C ANISOU 1892 CA LEU A1039 20222 13793 11541 1663 1589 2146 C ATOM 1893 C LEU A1039 12.448 17.503 -12.846 1.00123.23 C ANISOU 1893 C LEU A1039 20530 14479 11814 2015 1449 2150 C ATOM 1894 O LEU A1039 11.743 16.596 -12.402 1.00121.00 O ANISOU 1894 O LEU A1039 19944 14414 11618 2072 1274 2044 O ATOM 1895 CB LEU A1039 13.290 19.280 -11.252 1.00121.38 C ANISOU 1895 CB LEU A1039 20744 13711 11665 1741 1689 2227 C ATOM 1896 CG LEU A1039 12.177 19.193 -10.195 1.00125.08 C ANISOU 1896 CG LEU A1039 21100 14245 12182 1902 1547 2177 C ATOM 1897 CD1 LEU A1039 12.662 18.513 -8.925 1.00122.78 C ANISOU 1897 CD1 LEU A1039 20542 13970 12141 1607 1474 2050 C ATOM 1898 CD2 LEU A1039 11.640 20.570 -9.858 1.00129.81 C ANISOU 1898 CD2 LEU A1039 22089 14595 12638 2090 1656 2288 C ATOM 1899 N ASN A1040 12.212 18.105 -14.039 1.00121.55 N ANISOU 1899 N ASN A1040 20560 14254 11369 2248 1528 2266 N ATOM 1900 CA ASN A1040 11.094 17.717 -14.914 1.00121.55 C ANISOU 1900 CA ASN A1040 20458 14529 11197 2594 1399 2268 C ATOM 1901 C ASN A1040 11.296 16.295 -15.469 1.00122.12 C ANISOU 1901 C ASN A1040 20156 14887 11358 2490 1275 2144 C ATOM 1902 O ASN A1040 10.311 15.574 -15.650 1.00120.98 O ANISOU 1902 O ASN A1040 19774 15019 11174 2675 1111 2066 O ATOM 1903 CB ASN A1040 10.854 18.734 -16.052 1.00125.75 C ANISOU 1903 CB ASN A1040 21358 14975 11445 2878 1521 2429 C ATOM 1904 CG ASN A1040 12.055 19.138 -16.886 1.00153.74 C ANISOU 1904 CG ASN A1040 25131 18342 14941 2702 1715 2513 C ATOM 1905 OD1 ASN A1040 12.953 18.346 -17.184 1.00149.36 O ANISOU 1905 OD1 ASN A1040 24377 17863 14508 2443 1718 2442 O ATOM 1906 ND2 ASN A1040 12.052 20.377 -17.351 1.00148.11 N ANISOU 1906 ND2 ASN A1040 24850 17398 14026 2861 1887 2671 N ATOM 1907 N ALA A1041 12.571 15.890 -15.695 1.00116.82 N ANISOU 1907 N ALA A1041 19429 14153 10805 2186 1358 2118 N ATOM 1908 CA ALA A1041 12.951 14.557 -16.174 1.00114.62 C ANISOU 1908 CA ALA A1041 18823 14104 10623 2056 1268 2002 C ATOM 1909 C ALA A1041 12.596 13.490 -15.136 1.00115.02 C ANISOU 1909 C ALA A1041 18527 14295 10878 1947 1106 1852 C ATOM 1910 O ALA A1041 12.123 12.415 -15.508 1.00113.65 O ANISOU 1910 O ALA A1041 18088 14376 10717 2003 975 1750 O ATOM 1911 CB ALA A1041 14.440 14.512 -16.486 1.00115.25 C ANISOU 1911 CB ALA A1041 18946 14058 10783 1757 1411 2015 C ATOM 1912 N ALA A1042 12.804 13.805 -13.836 1.00109.89 N ANISOU 1912 N ALA A1042 17897 13477 10378 1794 1123 1837 N ATOM 1913 CA ALA A1042 12.504 12.939 -12.690 1.00107.03 C ANISOU 1913 CA ALA A1042 17254 13204 10209 1685 992 1711 C ATOM 1914 C ALA A1042 11.008 12.916 -12.398 1.00110.15 C ANISOU 1914 C ALA A1042 17579 13747 10527 1954 860 1683 C ATOM 1915 O ALA A1042 10.495 11.908 -11.910 1.00107.71 O ANISOU 1915 O ALA A1042 16989 13613 10325 1925 727 1561 O ATOM 1916 CB ALA A1042 13.262 13.422 -11.465 1.00106.98 C ANISOU 1916 CB ALA A1042 17325 12967 10358 1446 1068 1717 C ATOM 1917 N LYS A1043 10.315 14.033 -12.688 1.00108.79 N ANISOU 1917 N LYS A1043 17670 13503 10161 2216 905 1794 N ATOM 1918 CA LYS A1043 8.877 14.191 -12.487 1.00109.22 C ANISOU 1918 CA LYS A1043 17686 13708 10104 2511 793 1781 C ATOM 1919 C LYS A1043 8.102 13.386 -13.531 1.00113.49 C ANISOU 1919 C LYS A1043 18022 14581 10520 2701 673 1714 C ATOM 1920 O LYS A1043 7.009 12.903 -13.235 1.00112.94 O ANISOU 1920 O LYS A1043 17746 14732 10434 2837 538 1623 O ATOM 1921 CB LYS A1043 8.492 15.677 -12.548 1.00114.10 C ANISOU 1921 CB LYS A1043 18681 14136 10537 2749 897 1932 C ATOM 1922 CG LYS A1043 7.221 16.014 -11.781 1.00129.15 C ANISOU 1922 CG LYS A1043 20567 16112 12391 2985 805 1917 C ATOM 1923 N SER A1044 8.672 13.238 -14.744 1.00110.64 N ANISOU 1923 N SER A1044 17709 14263 10065 2699 728 1749 N ATOM 1924 CA SER A1044 8.068 12.488 -15.845 1.00110.92 C ANISOU 1924 CA SER A1044 17565 14609 9969 2859 628 1682 C ATOM 1925 C SER A1044 8.117 10.981 -15.568 1.00112.17 C ANISOU 1925 C SER A1044 17351 14956 10311 2650 514 1504 C ATOM 1926 O SER A1044 7.098 10.304 -15.720 1.00111.76 O ANISOU 1926 O SER A1044 17077 15180 10207 2774 381 1393 O ATOM 1927 CB SER A1044 8.763 12.813 -17.163 1.00116.03 C ANISOU 1927 CB SER A1044 18398 15220 10470 2900 737 1778 C ATOM 1928 OG SER A1044 8.718 14.205 -17.434 1.00127.83 O ANISOU 1928 OG SER A1044 20268 16519 11784 3095 860 1949 O ATOM 1929 N GLU A1045 9.285 10.469 -15.122 1.00106.41 N ANISOU 1929 N GLU A1045 16561 14081 9789 2333 570 1471 N ATOM 1930 CA GLU A1045 9.487 9.053 -14.800 1.00103.90 C ANISOU 1930 CA GLU A1045 15932 13892 9652 2125 487 1316 C ATOM 1931 C GLU A1045 8.717 8.661 -13.528 1.00105.90 C ANISOU 1931 C GLU A1045 16016 14187 10033 2094 387 1223 C ATOM 1932 O GLU A1045 8.457 7.475 -13.316 1.00103.76 O ANISOU 1932 O GLU A1045 15487 14072 9863 1993 299 1083 O ATOM 1933 CB GLU A1045 10.985 8.735 -14.659 1.00104.12 C ANISOU 1933 CB GLU A1045 15966 13751 9843 1832 585 1323 C ATOM 1934 CG GLU A1045 11.362 7.320 -15.080 1.00112.73 C ANISOU 1934 CG GLU A1045 16806 15001 11024 1692 534 1195 C ATOM 1935 CD GLU A1045 11.199 6.954 -16.546 1.00129.29 C ANISOU 1935 CD GLU A1045 18876 17290 12957 1816 521 1176 C ATOM 1936 OE1 GLU A1045 11.360 7.844 -17.413 1.00122.46 O ANISOU 1936 OE1 GLU A1045 18227 16379 11922 1949 601 1295 O ATOM 1937 OE2 GLU A1045 10.937 5.762 -16.828 1.00119.14 O ANISOU 1937 OE2 GLU A1045 17363 16194 11710 1774 440 1041 O ATOM 1938 N LEU A1046 8.325 9.660 -12.710 1.00103.35 N ANISOU 1938 N LEU A1046 15852 13723 9694 2184 409 1299 N ATOM 1939 CA LEU A1046 7.532 9.478 -11.493 1.00102.43 C ANISOU 1939 CA LEU A1046 15608 13636 9673 2184 325 1228 C ATOM 1940 C LEU A1046 6.094 9.118 -11.861 1.00108.17 C ANISOU 1940 C LEU A1046 16169 14667 10262 2416 200 1143 C ATOM 1941 O LEU A1046 5.562 8.137 -11.340 1.00106.23 O ANISOU 1941 O LEU A1046 15672 14575 10117 2331 107 1004 O ATOM 1942 CB LEU A1046 7.556 10.763 -10.640 1.00102.85 C ANISOU 1942 CB LEU A1046 15912 13445 9720 2235 399 1343 C ATOM 1943 CG LEU A1046 7.589 10.618 -9.114 1.00105.70 C ANISOU 1943 CG LEU A1046 16196 13692 10273 2071 376 1294 C ATOM 1944 CD1 LEU A1046 7.977 11.920 -8.471 1.00106.39 C ANISOU 1944 CD1 LEU A1046 16572 13498 10353 2069 484 1413 C ATOM 1945 CD2 LEU A1046 6.267 10.152 -8.554 1.00107.75 C ANISOU 1945 CD2 LEU A1046 16256 14157 10527 2195 249 1194 C ATOM 1946 N ASP A1047 5.472 9.917 -12.764 1.00108.24 N ANISOU 1946 N ASP A1047 16323 14770 10032 2709 203 1223 N ATOM 1947 CA ASP A1047 4.098 9.737 -13.243 1.00110.04 C ANISOU 1947 CA ASP A1047 16404 15323 10083 2971 87 1149 C ATOM 1948 C ASP A1047 3.930 8.402 -13.971 1.00114.39 C ANISOU 1948 C ASP A1047 16674 16147 10642 2882 4 992 C ATOM 1949 O ASP A1047 2.875 7.777 -13.861 1.00114.07 O ANISOU 1949 O ASP A1047 16398 16376 10567 2944 -106 856 O ATOM 1950 CB ASP A1047 3.687 10.896 -14.175 1.00114.67 C ANISOU 1950 CB ASP A1047 17238 15937 10395 3313 125 1287 C ATOM 1951 CG ASP A1047 3.738 12.284 -13.557 1.00125.93 C ANISOU 1951 CG ASP A1047 18981 17091 11777 3439 219 1444 C ATOM 1952 OD1 ASP A1047 3.351 12.424 -12.379 1.00125.30 O ANISOU 1952 OD1 ASP A1047 18862 16944 11801 3404 192 1416 O ATOM 1953 OD2 ASP A1047 4.115 13.237 -14.271 1.00133.73 O ANISOU 1953 OD2 ASP A1047 20266 17935 12610 3584 324 1593 O ATOM 1954 N LYS A1048 4.979 7.964 -14.696 1.00111.36 N ANISOU 1954 N LYS A1048 16316 15692 10303 2725 66 1004 N ATOM 1955 CA LYS A1048 5.008 6.714 -15.461 1.00111.31 C ANISOU 1955 CA LYS A1048 16084 15903 10306 2623 11 863 C ATOM 1956 C LYS A1048 5.034 5.477 -14.549 1.00114.15 C ANISOU 1956 C LYS A1048 16199 16282 10891 2360 -38 707 C ATOM 1957 O LYS A1048 4.588 4.408 -14.970 1.00113.82 O ANISOU 1957 O LYS A1048 15938 16468 10840 2308 -106 554 O ATOM 1958 CB LYS A1048 6.216 6.690 -16.413 1.00114.08 C ANISOU 1958 CB LYS A1048 16560 16139 10645 2532 107 935 C ATOM 1959 CG LYS A1048 6.079 7.631 -17.606 1.00133.00 C ANISOU 1959 CG LYS A1048 19164 18586 12783 2800 148 1059 C ATOM 1960 N ALA A1049 5.547 5.622 -13.311 1.00109.92 N ANISOU 1960 N ALA A1049 15710 15506 10546 2195 4 744 N ATOM 1961 CA ALA A1049 5.645 4.534 -12.336 1.00108.25 C ANISOU 1961 CA ALA A1049 15308 15275 10547 1958 -27 619 C ATOM 1962 C ALA A1049 4.330 4.303 -11.578 1.00113.35 C ANISOU 1962 C ALA A1049 15790 16088 11187 2023 -120 515 C ATOM 1963 O ALA A1049 4.019 3.155 -11.254 1.00112.03 O ANISOU 1963 O ALA A1049 15416 16032 11118 1875 -164 365 O ATOM 1964 CB ALA A1049 6.764 4.821 -11.348 1.00107.46 C ANISOU 1964 CB ALA A1049 15326 14870 10633 1770 55 703 C ATOM 1965 N ILE A1050 3.574 5.383 -11.283 1.00111.94 N ANISOU 1965 N ILE A1050 15715 15924 10894 2242 -139 591 N ATOM 1966 CA ILE A1050 2.308 5.316 -10.539 1.00112.51 C ANISOU 1966 CA ILE A1050 15639 16164 10944 2328 -221 503 C ATOM 1967 C ILE A1050 1.120 5.099 -11.494 1.00119.95 C ANISOU 1967 C ILE A1050 16423 17479 11672 2533 -311 401 C ATOM 1968 O ILE A1050 0.299 4.211 -11.258 1.00119.70 O ANISOU 1968 O ILE A1050 16148 17671 11662 2464 -382 233 O ATOM 1969 CB ILE A1050 2.082 6.584 -9.652 1.00115.71 C ANISOU 1969 CB ILE A1050 16231 16400 11332 2469 -194 630 C ATOM 1970 CG1 ILE A1050 3.367 7.019 -8.885 1.00114.63 C ANISOU 1970 CG1 ILE A1050 16289 15896 11368 2283 -92 745 C ATOM 1971 CG2 ILE A1050 0.875 6.420 -8.706 1.00116.28 C ANISOU 1971 CG2 ILE A1050 16137 16629 11416 2520 -271 530 C ATOM 1972 CD1 ILE A1050 3.881 6.095 -7.753 1.00118.82 C ANISOU 1972 CD1 ILE A1050 16691 16311 12143 1992 -89 664 C ATOM 1973 N GLY A1051 1.031 5.927 -12.531 1.00119.29 N ANISOU 1973 N GLY A1051 16483 17463 11378 2782 -303 500 N ATOM 1974 CA GLY A1051 -0.052 5.887 -13.506 1.00121.75 C ANISOU 1974 CA GLY A1051 16665 18143 11451 3021 -390 422 C ATOM 1975 C GLY A1051 -1.029 7.036 -13.348 1.00128.66 C ANISOU 1975 C GLY A1051 17628 19118 12137 3357 -425 501 C ATOM 1976 O GLY A1051 -2.195 6.918 -13.738 1.00130.20 O ANISOU 1976 O GLY A1051 17643 19669 12157 3548 -520 398 O ATOM 1977 N ARG A1052 -0.552 8.159 -12.772 1.00125.27 N ANISOU 1977 N ARG A1052 17477 18383 11736 3431 -344 678 N ATOM 1978 CA ARG A1052 -1.327 9.381 -12.543 1.00126.78 C ANISOU 1978 CA ARG A1052 17821 18592 11756 3759 -350 782 C ATOM 1979 C ARG A1052 -0.407 10.608 -12.507 1.00131.44 C ANISOU 1979 C ARG A1052 18801 18803 12336 3822 -219 1000 C ATOM 1980 O ARG A1052 0.806 10.460 -12.319 1.00129.35 O ANISOU 1980 O ARG A1052 18645 18257 12246 3560 -131 1050 O ATOM 1981 CB ARG A1052 -2.148 9.284 -11.236 1.00125.88 C ANISOU 1981 CB ARG A1052 17559 18532 11737 3732 -402 699 C ATOM 1982 CG ARG A1052 -1.317 9.277 -9.950 1.00132.27 C ANISOU 1982 CG ARG A1052 18462 18985 12811 3456 -330 740 C ATOM 1983 CD ARG A1052 -2.136 9.690 -8.747 1.00138.99 C ANISOU 1983 CD ARG A1052 19280 19842 13689 3537 -358 724 C ATOM 1984 NE ARG A1052 -1.286 10.068 -7.617 1.00143.90 N ANISOU 1984 NE ARG A1052 20076 20089 14510 3347 -274 809 N ATOM 1985 CZ ARG A1052 -0.963 11.318 -7.305 1.00157.60 C ANISOU 1985 CZ ARG A1052 22118 21563 16201 3476 -191 970 C ATOM 1986 NH1 ARG A1052 -0.188 11.568 -6.259 1.00142.33 N ANISOU 1986 NH1 ARG A1052 20312 19317 14451 3273 -120 1021 N ATOM 1987 NH2 ARG A1052 -1.427 12.332 -8.028 1.00146.56 N ANISOU 1987 NH2 ARG A1052 20907 20215 14564 3816 -176 1076 N ATOM 1988 N ASN A1053 -0.988 11.815 -12.673 1.00130.62 N ANISOU 1988 N ASN A1053 18910 18698 12022 4170 -200 1124 N ATOM 1989 CA ASN A1053 -0.240 13.068 -12.596 1.00131.27 C ANISOU 1989 CA ASN A1053 19394 18411 12072 4244 -61 1327 C ATOM 1990 C ASN A1053 0.014 13.357 -11.116 1.00133.67 C ANISOU 1990 C ASN A1053 19764 18445 12581 4069 -17 1343 C ATOM 1991 O ASN A1053 -0.888 13.782 -10.386 1.00133.73 O ANISOU 1991 O ASN A1053 19753 18517 12542 4240 -59 1332 O ATOM 1992 CB ASN A1053 -0.981 14.212 -13.307 1.00135.78 C ANISOU 1992 CB ASN A1053 20188 19069 12332 4694 -48 1453 C ATOM 1993 CG ASN A1053 -0.157 15.466 -13.514 1.00160.32 C ANISOU 1993 CG ASN A1053 23748 21796 15372 4772 119 1666 C ATOM 1994 OD1 ASN A1053 1.063 15.430 -13.730 1.00153.90 O ANISOU 1994 OD1 ASN A1053 23075 20726 14676 4520 225 1723 O ATOM 1995 ND2 ASN A1053 -0.822 16.611 -13.490 1.00154.13 N ANISOU 1995 ND2 ASN A1053 23207 20973 14382 5132 152 1784 N ATOM 1996 N THR A1054 1.230 13.024 -10.666 1.00128.36 N ANISOU 1996 N THR A1054 19132 17502 12135 3720 59 1351 N ATOM 1997 CA THR A1054 1.668 13.126 -9.275 1.00126.38 C ANISOU 1997 CA THR A1054 18916 17000 12101 3495 100 1349 C ATOM 1998 C THR A1054 1.977 14.567 -8.867 1.00131.30 C ANISOU 1998 C THR A1054 19921 17302 12666 3606 224 1514 C ATOM 1999 O THR A1054 1.678 14.935 -7.732 1.00130.30 O ANISOU 1999 O THR A1054 19827 17067 12614 3596 226 1511 O ATOM 2000 CB THR A1054 2.886 12.217 -9.028 1.00130.90 C ANISOU 2000 CB THR A1054 19385 17438 12914 3101 133 1293 C ATOM 2001 OG1 THR A1054 4.012 12.706 -9.761 1.00129.81 O ANISOU 2001 OG1 THR A1054 19482 17090 12748 3032 253 1409 O ATOM 2002 CG2 THR A1054 2.614 10.757 -9.392 1.00128.13 C ANISOU 2002 CG2 THR A1054 18686 17372 12627 2978 27 1127 C ATOM 2003 N ASN A1055 2.596 15.364 -9.775 1.00129.57 N ANISOU 2003 N ASN A1055 20000 16919 12314 3696 339 1654 N ATOM 2004 CA ASN A1055 3.021 16.765 -9.585 1.00130.92 C ANISOU 2004 CA ASN A1055 20586 16749 12408 3781 491 1819 C ATOM 2005 C ASN A1055 4.199 16.861 -8.579 1.00132.96 C ANISOU 2005 C ASN A1055 20934 16681 12904 3409 589 1824 C ATOM 2006 O ASN A1055 4.568 17.963 -8.161 1.00133.42 O ANISOU 2006 O ASN A1055 21316 16440 12937 3415 718 1931 O ATOM 2007 CB ASN A1055 1.849 17.686 -9.159 1.00134.05 C ANISOU 2007 CB ASN A1055 21120 17175 12638 4138 473 1872 C ATOM 2008 CG ASN A1055 0.680 17.691 -10.113 1.00159.15 C ANISOU 2008 CG ASN A1055 24216 20696 15558 4533 377 1868 C ATOM 2009 OD1 ASN A1055 -0.294 16.948 -9.944 1.00153.82 O ANISOU 2009 OD1 ASN A1055 23211 20357 14876 4615 229 1736 O ATOM 2010 ND2 ASN A1055 0.745 18.538 -11.131 1.00152.45 N ANISOU 2010 ND2 ASN A1055 23665 19779 14480 4788 465 2010 N ATOM 2011 N GLY A1056 4.794 15.713 -8.244 1.00127.23 N ANISOU 2011 N GLY A1056 19928 16020 12392 3095 533 1706 N ATOM 2012 CA GLY A1056 5.920 15.611 -7.322 1.00125.38 C ANISOU 2012 CA GLY A1056 19713 15545 12381 2742 603 1689 C ATOM 2013 C GLY A1056 5.583 15.133 -5.921 1.00127.18 C ANISOU 2013 C GLY A1056 19744 15793 12784 2616 522 1588 C ATOM 2014 O GLY A1056 6.492 14.954 -5.105 1.00125.34 O ANISOU 2014 O GLY A1056 19493 15394 12734 2329 564 1561 O ATOM 2015 N VAL A1057 4.281 14.929 -5.622 1.00123.61 N ANISOU 2015 N VAL A1057 19139 15558 12270 2830 408 1528 N ATOM 2016 CA VAL A1057 3.815 14.470 -4.306 1.00121.77 C ANISOU 2016 CA VAL A1057 18717 15366 12184 2735 332 1431 C ATOM 2017 C VAL A1057 3.274 13.034 -4.405 1.00123.32 C ANISOU 2017 C VAL A1057 18532 15872 12451 2672 198 1279 C ATOM 2018 O VAL A1057 2.637 12.677 -5.399 1.00123.62 O ANISOU 2018 O VAL A1057 18457 16158 12353 2841 136 1246 O ATOM 2019 CB VAL A1057 2.795 15.424 -3.617 1.00127.08 C ANISOU 2019 CB VAL A1057 19527 16008 12750 2991 328 1472 C ATOM 2020 CG1 VAL A1057 3.485 16.683 -3.097 1.00127.70 C ANISOU 2020 CG1 VAL A1057 19970 15723 12829 2948 472 1590 C ATOM 2021 CG2 VAL A1057 1.618 15.779 -4.528 1.00129.01 C ANISOU 2021 CG2 VAL A1057 19785 16487 12745 3379 276 1501 C ATOM 2022 N ILE A1058 3.550 12.216 -3.371 1.00117.34 N ANISOU 2022 N ILE A1058 17589 15094 11900 2423 162 1185 N ATOM 2023 CA ILE A1058 3.153 10.804 -3.303 1.00115.51 C ANISOU 2023 CA ILE A1058 17024 15103 11761 2311 59 1037 C ATOM 2024 C ILE A1058 2.482 10.498 -1.948 1.00117.00 C ANISOU 2024 C ILE A1058 17074 15326 12055 2261 4 957 C ATOM 2025 O ILE A1058 2.741 11.194 -0.967 1.00115.99 O ANISOU 2025 O ILE A1058 17093 14991 11989 2221 52 1011 O ATOM 2026 CB ILE A1058 4.418 9.917 -3.585 1.00117.25 C ANISOU 2026 CB ILE A1058 17170 15251 12130 2028 92 1008 C ATOM 2027 CG1 ILE A1058 4.767 9.891 -5.094 1.00118.72 C ANISOU 2027 CG1 ILE A1058 17405 15512 12191 2100 117 1046 C ATOM 2028 CG2 ILE A1058 4.354 8.488 -3.010 1.00116.21 C ANISOU 2028 CG2 ILE A1058 16754 15239 12160 1828 23 867 C ATOM 2029 CD1 ILE A1058 3.617 9.455 -6.057 1.00127.32 C ANISOU 2029 CD1 ILE A1058 18334 16924 13116 2314 26 975 C ATOM 2030 N THR A1059 1.589 9.486 -1.920 1.00112.48 N ANISOU 2030 N THR A1059 16225 15020 11492 2264 -89 823 N ATOM 2031 CA THR A1059 0.908 9.045 -0.702 1.00111.16 C ANISOU 2031 CA THR A1059 15902 14913 11421 2201 -137 733 C ATOM 2032 C THR A1059 1.577 7.761 -0.175 1.00111.70 C ANISOU 2032 C THR A1059 15803 14944 11692 1895 -141 642 C ATOM 2033 O THR A1059 2.200 7.033 -0.950 1.00110.83 O ANISOU 2033 O THR A1059 15632 14864 11613 1782 -135 615 O ATOM 2034 CB THR A1059 -0.615 8.884 -0.920 1.00121.50 C ANISOU 2034 CB THR A1059 17030 16546 12589 2414 -222 641 C ATOM 2035 OG1 THR A1059 -1.242 8.698 0.350 1.00122.16 O ANISOU 2035 OG1 THR A1059 17010 16651 12756 2365 -248 575 O ATOM 2036 CG2 THR A1059 -0.981 7.727 -1.851 1.00119.28 C ANISOU 2036 CG2 THR A1059 16506 16543 12273 2366 -282 513 C ATOM 2037 N LYS A1060 1.425 7.486 1.139 1.00106.27 N ANISOU 2037 N LYS A1060 15053 14194 11131 1779 -149 598 N ATOM 2038 CA LYS A1060 1.980 6.323 1.847 1.00104.02 C ANISOU 2038 CA LYS A1060 14634 13859 11030 1516 -148 522 C ATOM 2039 C LYS A1060 1.632 4.992 1.162 1.00106.63 C ANISOU 2039 C LYS A1060 14744 14404 11367 1437 -188 394 C ATOM 2040 O LYS A1060 2.473 4.093 1.130 1.00104.64 O ANISOU 2040 O LYS A1060 14445 14082 11230 1246 -164 364 O ATOM 2041 CB LYS A1060 1.491 6.300 3.304 1.00105.92 C ANISOU 2041 CB LYS A1060 14831 14057 11354 1469 -159 487 C ATOM 2042 N ASP A1061 0.408 4.877 0.608 1.00104.34 N ANISOU 2042 N ASP A1061 14320 14380 10943 1587 -244 313 N ATOM 2043 CA ASP A1061 -0.065 3.687 -0.104 1.00104.39 C ANISOU 2043 CA ASP A1061 14116 14618 10928 1516 -279 173 C ATOM 2044 C ASP A1061 0.760 3.458 -1.380 1.00108.00 C ANISOU 2044 C ASP A1061 14620 15065 11351 1495 -260 202 C ATOM 2045 O ASP A1061 1.147 2.320 -1.656 1.00107.22 O ANISOU 2045 O ASP A1061 14419 14990 11332 1321 -250 118 O ATOM 2046 CB ASP A1061 -1.561 3.818 -0.439 1.00107.86 C ANISOU 2046 CB ASP A1061 14405 15373 11204 1702 -345 81 C ATOM 2047 N GLU A1062 1.056 4.547 -2.126 1.00104.44 N ANISOU 2047 N GLU A1062 14341 14562 10780 1672 -245 324 N ATOM 2048 CA GLU A1062 1.843 4.526 -3.361 1.00103.97 C ANISOU 2048 CA GLU A1062 14354 14484 10666 1677 -218 371 C ATOM 2049 C GLU A1062 3.323 4.225 -3.074 1.00105.23 C ANISOU 2049 C GLU A1062 14605 14389 10990 1460 -149 428 C ATOM 2050 O GLU A1062 3.909 3.383 -3.758 1.00104.39 O ANISOU 2050 O GLU A1062 14434 14310 10918 1347 -136 383 O ATOM 2051 CB GLU A1062 1.700 5.857 -4.118 1.00106.85 C ANISOU 2051 CB GLU A1062 14907 14844 10847 1935 -205 497 C ATOM 2052 CG GLU A1062 0.405 5.980 -4.908 1.00118.90 C ANISOU 2052 CG GLU A1062 16322 16685 12168 2177 -278 434 C ATOM 2053 CD GLU A1062 -0.061 7.385 -5.253 1.00139.06 C ANISOU 2053 CD GLU A1062 19064 19242 14529 2486 -273 557 C ATOM 2054 OE1 GLU A1062 0.625 8.364 -4.876 1.00125.94 O ANISOU 2054 OE1 GLU A1062 17653 17306 12893 2507 -199 699 O ATOM 2055 OE2 GLU A1062 -1.146 7.507 -5.865 1.00137.02 O ANISOU 2055 OE2 GLU A1062 18706 19268 14087 2711 -339 506 O ATOM 2056 N ALA A1063 3.912 4.893 -2.056 1.00100.46 N ANISOU 2056 N ALA A1063 14139 13554 10478 1404 -106 516 N ATOM 2057 CA ALA A1063 5.311 4.725 -1.637 1.00 98.92 C ANISOU 2057 CA ALA A1063 14019 13137 10428 1208 -43 567 C ATOM 2058 C ALA A1063 5.604 3.293 -1.152 1.00100.69 C ANISOU 2058 C ALA A1063 14075 13382 10802 1007 -54 461 C ATOM 2059 O ALA A1063 6.665 2.755 -1.473 1.00 99.30 O ANISOU 2059 O ALA A1063 13900 13134 10696 880 -16 468 O ATOM 2060 CB ALA A1063 5.657 5.726 -0.542 1.00 99.38 C ANISOU 2060 CB ALA A1063 14235 12986 10538 1195 -6 657 C ATOM 2061 N GLU A1064 4.662 2.681 -0.393 1.00 96.57 N ANISOU 2061 N GLU A1064 13416 12958 10318 984 -97 363 N ATOM 2062 CA GLU A1064 4.780 1.309 0.110 1.00 94.98 C ANISOU 2062 CA GLU A1064 13078 12770 10242 807 -95 260 C ATOM 2063 C GLU A1064 4.694 0.312 -1.050 1.00 98.10 C ANISOU 2063 C GLU A1064 13363 13317 10594 774 -101 166 C ATOM 2064 O GLU A1064 5.432 -0.677 -1.057 1.00 97.21 O ANISOU 2064 O GLU A1064 13216 13143 10576 629 -68 127 O ATOM 2065 CB GLU A1064 3.700 1.012 1.164 1.00 96.19 C ANISOU 2065 CB GLU A1064 13130 12992 10424 795 -126 180 C ATOM 2066 N LYS A1065 3.817 0.597 -2.042 1.00 94.56 N ANISOU 2066 N LYS A1065 12868 13071 9991 920 -142 130 N ATOM 2067 CA LYS A1065 3.610 -0.221 -3.240 1.00 94.61 C ANISOU 2067 CA LYS A1065 12769 13254 9925 909 -155 32 C ATOM 2068 C LYS A1065 4.879 -0.257 -4.100 1.00 96.84 C ANISOU 2068 C LYS A1065 13145 13430 10219 871 -108 102 C ATOM 2069 O LYS A1065 5.249 -1.321 -4.608 1.00 96.28 O ANISOU 2069 O LYS A1065 13005 13391 10185 760 -88 23 O ATOM 2070 CB LYS A1065 2.420 0.310 -4.057 1.00 98.78 C ANISOU 2070 CB LYS A1065 13235 14036 10262 1107 -215 -7 C ATOM 2071 N LEU A1066 5.553 0.904 -4.229 1.00 92.02 N ANISOU 2071 N LEU A1066 12702 12687 9576 956 -81 248 N ATOM 2072 CA LEU A1066 6.796 1.068 -4.980 1.00 90.99 C ANISOU 2072 CA LEU A1066 12673 12449 9448 921 -25 328 C ATOM 2073 C LEU A1066 7.967 0.413 -4.260 1.00 91.86 C ANISOU 2073 C LEU A1066 12784 12389 9728 731 23 335 C ATOM 2074 O LEU A1066 8.870 -0.104 -4.914 1.00 90.97 O ANISOU 2074 O LEU A1066 12670 12255 9638 661 61 333 O ATOM 2075 CB LEU A1066 7.083 2.558 -5.197 1.00 91.73 C ANISOU 2075 CB LEU A1066 12959 12441 9452 1051 5 475 C ATOM 2076 CG LEU A1066 7.173 3.016 -6.648 1.00 98.06 C ANISOU 2076 CG LEU A1066 13836 13326 10094 1181 20 523 C ATOM 2077 CD1 LEU A1066 5.802 3.027 -7.314 1.00 99.72 C ANISOU 2077 CD1 LEU A1066 13960 13788 10142 1367 -53 455 C ATOM 2078 CD2 LEU A1066 7.787 4.391 -6.735 1.00101.39 C ANISOU 2078 CD2 LEU A1066 14488 13576 10461 1252 86 677 C ATOM 2079 N PHE A1067 7.950 0.441 -2.917 1.00 86.68 N ANISOU 2079 N PHE A1067 12128 11625 9181 663 21 341 N ATOM 2080 CA PHE A1067 8.975 -0.150 -2.059 1.00 84.95 C ANISOU 2080 CA PHE A1067 11904 11262 9113 508 58 348 C ATOM 2081 C PHE A1067 8.927 -1.681 -2.125 1.00 89.27 C ANISOU 2081 C PHE A1067 12326 11869 9724 408 61 230 C ATOM 2082 O PHE A1067 9.982 -2.319 -2.111 1.00 88.21 O ANISOU 2082 O PHE A1067 12192 11657 9666 316 102 235 O ATOM 2083 CB PHE A1067 8.793 0.344 -0.614 1.00 85.65 C ANISOU 2083 CB PHE A1067 12028 11241 9274 486 48 381 C ATOM 2084 CG PHE A1067 9.756 -0.196 0.418 1.00 85.42 C ANISOU 2084 CG PHE A1067 11990 11081 9385 349 77 389 C ATOM 2085 CD1 PHE A1067 11.130 -0.069 0.247 1.00 87.72 C ANISOU 2085 CD1 PHE A1067 12331 11284 9716 280 123 449 C ATOM 2086 CD2 PHE A1067 9.289 -0.769 1.592 1.00 86.49 C ANISOU 2086 CD2 PHE A1067 12067 11193 9601 296 59 338 C ATOM 2087 CE1 PHE A1067 12.018 -0.559 1.205 1.00 87.60 C ANISOU 2087 CE1 PHE A1067 12293 11179 9811 176 143 452 C ATOM 2088 CE2 PHE A1067 10.178 -1.246 2.557 1.00 88.43 C ANISOU 2088 CE2 PHE A1067 12313 11329 9958 195 83 351 C ATOM 2089 CZ PHE A1067 11.537 -1.138 2.357 1.00 86.17 C ANISOU 2089 CZ PHE A1067 12064 10974 9703 143 120 407 C ATOM 2090 N ASN A1068 7.706 -2.259 -2.212 1.00 87.00 N ANISOU 2090 N ASN A1068 11936 11724 9395 426 24 119 N ATOM 2091 CA ASN A1068 7.467 -3.702 -2.301 1.00 86.98 C ANISOU 2091 CA ASN A1068 11832 11779 9437 321 39 -10 C ATOM 2092 C ASN A1068 8.023 -4.295 -3.600 1.00 90.98 C ANISOU 2092 C ASN A1068 12327 12344 9899 308 65 -45 C ATOM 2093 O ASN A1068 8.631 -5.364 -3.555 1.00 90.06 O ANISOU 2093 O ASN A1068 12196 12165 9857 208 110 -93 O ATOM 2094 CB ASN A1068 5.973 -4.021 -2.182 1.00 89.34 C ANISOU 2094 CB ASN A1068 12022 12243 9681 334 0 -130 C ATOM 2095 CG ASN A1068 5.403 -3.893 -0.788 1.00112.69 C ANISOU 2095 CG ASN A1068 14966 15144 12705 304 -10 -133 C ATOM 2096 OD1 ASN A1068 4.298 -3.377 -0.598 1.00109.19 O ANISOU 2096 OD1 ASN A1068 14472 14824 12193 382 -54 -163 O ATOM 2097 ND2 ASN A1068 6.109 -4.401 0.218 1.00102.95 N ANISOU 2097 ND2 ASN A1068 13774 13742 11600 201 31 -107 N ATOM 2098 N GLN A1069 7.821 -3.613 -4.747 1.00 88.30 N ANISOU 2098 N GLN A1069 12003 12119 9428 422 41 -19 N ATOM 2099 CA GLN A1069 8.328 -4.090 -6.038 1.00 88.65 C ANISOU 2099 CA GLN A1069 12041 12229 9414 421 65 -48 C ATOM 2100 C GLN A1069 9.848 -3.867 -6.148 1.00 91.42 C ANISOU 2100 C GLN A1069 12484 12428 9824 387 122 60 C ATOM 2101 O GLN A1069 10.525 -4.635 -6.835 1.00 91.03 O ANISOU 2101 O GLN A1069 12420 12383 9783 339 160 24 O ATOM 2102 CB GLN A1069 7.573 -3.465 -7.238 1.00 91.32 C ANISOU 2102 CB GLN A1069 12364 12759 9575 564 22 -59 C ATOM 2103 CG GLN A1069 7.576 -1.940 -7.326 1.00105.65 C ANISOU 2103 CG GLN A1069 14293 14543 11305 714 6 82 C ATOM 2104 N ASP A1070 10.374 -2.837 -5.457 1.00 87.28 N ANISOU 2104 N ASP A1070 12049 11777 9335 406 131 181 N ATOM 2105 CA ASP A1070 11.798 -2.500 -5.430 1.00 86.70 C ANISOU 2105 CA ASP A1070 12050 11576 9314 358 186 276 C ATOM 2106 C ASP A1070 12.619 -3.570 -4.710 1.00 89.70 C ANISOU 2106 C ASP A1070 12384 11872 9827 243 219 240 C ATOM 2107 O ASP A1070 13.632 -4.032 -5.245 1.00 88.82 O ANISOU 2107 O ASP A1070 12269 11747 9730 207 265 245 O ATOM 2108 CB ASP A1070 12.005 -1.144 -4.744 1.00 88.30 C ANISOU 2108 CB ASP A1070 12359 11671 9519 386 190 392 C ATOM 2109 CG ASP A1070 12.079 0.044 -5.674 1.00 98.47 C ANISOU 2109 CG ASP A1070 13763 12970 10681 483 211 482 C ATOM 2110 OD1 ASP A1070 11.508 -0.032 -6.788 1.00100.20 O ANISOU 2110 OD1 ASP A1070 13969 13321 10783 577 193 452 O ATOM 2111 OD2 ASP A1070 12.680 1.063 -5.280 1.00103.89 O ANISOU 2111 OD2 ASP A1070 14563 13536 11376 466 249 579 O ATOM 2112 N VAL A1071 12.173 -3.963 -3.498 1.00 85.83 N ANISOU 2112 N VAL A1071 11861 11329 9421 199 200 205 N ATOM 2113 CA VAL A1071 12.824 -4.981 -2.673 1.00 84.95 C ANISOU 2113 CA VAL A1071 11722 11132 9423 115 231 176 C ATOM 2114 C VAL A1071 12.626 -6.376 -3.321 1.00 88.37 C ANISOU 2114 C VAL A1071 12103 11621 9851 83 257 62 C ATOM 2115 O VAL A1071 13.479 -7.247 -3.143 1.00 87.77 O ANISOU 2115 O VAL A1071 12028 11482 9838 43 303 49 O ATOM 2116 CB VAL A1071 12.353 -4.910 -1.195 1.00 88.48 C ANISOU 2116 CB VAL A1071 12169 11504 9946 86 207 180 C ATOM 2117 CG1 VAL A1071 10.915 -5.387 -1.027 1.00 88.65 C ANISOU 2117 CG1 VAL A1071 12140 11599 9946 86 178 81 C ATOM 2118 CG2 VAL A1071 13.298 -5.662 -0.263 1.00 87.83 C ANISOU 2118 CG2 VAL A1071 12086 11319 9966 27 242 190 C ATOM 2119 N ASP A1072 11.535 -6.561 -4.105 1.00 85.02 N ANISOU 2119 N ASP A1072 11638 11323 9343 107 231 -24 N ATOM 2120 CA ASP A1072 11.267 -7.808 -4.823 1.00 85.18 C ANISOU 2120 CA ASP A1072 11616 11407 9343 62 261 -148 C ATOM 2121 C ASP A1072 12.222 -7.928 -6.005 1.00 87.62 C ANISOU 2121 C ASP A1072 11945 11743 9606 88 296 -127 C ATOM 2122 O ASP A1072 12.658 -9.031 -6.316 1.00 87.19 O ANISOU 2122 O ASP A1072 11888 11664 9576 45 347 -194 O ATOM 2123 CB ASP A1072 9.805 -7.893 -5.293 1.00 88.32 C ANISOU 2123 CB ASP A1072 11944 11964 9651 71 219 -260 C ATOM 2124 CG ASP A1072 9.453 -9.220 -5.941 1.00103.49 C ANISOU 2124 CG ASP A1072 13823 13949 11550 -8 258 -411 C ATOM 2125 OD1 ASP A1072 9.403 -10.241 -5.217 1.00104.39 O ANISOU 2125 OD1 ASP A1072 13949 13969 11746 -104 308 -478 O ATOM 2126 OD2 ASP A1072 9.266 -9.245 -7.179 1.00111.68 O ANISOU 2126 OD2 ASP A1072 14830 15121 12484 27 247 -463 O ATOM 2127 N ALA A1073 12.551 -6.792 -6.653 1.00 83.60 N ANISOU 2127 N ALA A1073 11467 11274 9024 162 278 -34 N ATOM 2128 CA ALA A1073 13.485 -6.742 -7.780 1.00 83.71 C ANISOU 2128 CA ALA A1073 11504 11317 8984 188 316 -1 C ATOM 2129 C ALA A1073 14.913 -7.015 -7.310 1.00 86.46 C ANISOU 2129 C ALA A1073 11874 11552 9426 145 371 59 C ATOM 2130 O ALA A1073 15.702 -7.586 -8.066 1.00 86.12 O ANISOU 2130 O ALA A1073 11826 11528 9368 142 418 41 O ATOM 2131 CB ALA A1073 13.410 -5.388 -8.463 1.00 84.98 C ANISOU 2131 CB ALA A1073 11717 11533 9039 274 295 92 C ATOM 2132 N ALA A1074 15.233 -6.617 -6.056 1.00 82.21 N ANISOU 2132 N ALA A1074 11350 10912 8973 117 364 123 N ATOM 2133 CA ALA A1074 16.541 -6.811 -5.428 1.00 81.53 C ANISOU 2133 CA ALA A1074 11264 10745 8968 84 405 175 C ATOM 2134 C ALA A1074 16.810 -8.291 -5.172 1.00 86.05 C ANISOU 2134 C ALA A1074 11813 11283 9599 66 442 97 C ATOM 2135 O ALA A1074 17.907 -8.757 -5.472 1.00 86.06 O ANISOU 2135 O ALA A1074 11804 11282 9611 75 490 108 O ATOM 2136 CB ALA A1074 16.626 -6.025 -4.129 1.00 81.47 C ANISOU 2136 CB ALA A1074 11275 10657 9022 61 379 245 C ATOM 2137 N VAL A1075 15.804 -9.037 -4.661 1.00 83.11 N ANISOU 2137 N VAL A1075 11440 10884 9255 41 429 15 N ATOM 2138 CA VAL A1075 15.938 -10.472 -4.393 1.00 83.39 C ANISOU 2138 CA VAL A1075 11489 10858 9337 21 482 -63 C ATOM 2139 C VAL A1075 15.922 -11.248 -5.736 1.00 88.93 C ANISOU 2139 C VAL A1075 12192 11626 9973 25 522 -150 C ATOM 2140 O VAL A1075 16.673 -12.214 -5.874 1.00 88.96 O ANISOU 2140 O VAL A1075 12222 11583 9997 38 584 -177 O ATOM 2141 CB VAL A1075 14.916 -11.016 -3.344 1.00 87.03 C ANISOU 2141 CB VAL A1075 11967 11253 9849 -28 476 -122 C ATOM 2142 CG1 VAL A1075 13.468 -10.940 -3.826 1.00 87.25 C ANISOU 2142 CG1 VAL A1075 11963 11373 9816 -64 442 -215 C ATOM 2143 CG2 VAL A1075 15.270 -12.430 -2.899 1.00 87.19 C ANISOU 2143 CG2 VAL A1075 12040 11170 9920 -41 550 -176 C ATOM 2144 N ARG A1076 15.124 -10.787 -6.729 1.00 86.61 N ANISOU 2144 N ARG A1076 11871 11447 9589 28 487 -190 N ATOM 2145 CA ARG A1076 15.033 -11.387 -8.065 1.00 87.85 C ANISOU 2145 CA ARG A1076 12022 11691 9665 31 516 -277 C ATOM 2146 C ARG A1076 16.403 -11.373 -8.760 1.00 92.70 C ANISOU 2146 C ARG A1076 12648 12309 10264 78 561 -217 C ATOM 2147 O ARG A1076 16.811 -12.387 -9.331 1.00 93.23 O ANISOU 2147 O ARG A1076 12734 12369 10321 79 620 -285 O ATOM 2148 CB ARG A1076 13.996 -10.647 -8.928 1.00 89.82 C ANISOU 2148 CB ARG A1076 12233 12090 9804 53 456 -308 C ATOM 2149 CG ARG A1076 12.571 -11.174 -8.803 1.00104.38 C ANISOU 2149 CG ARG A1076 14037 13998 11622 -5 432 -441 C ATOM 2150 CD ARG A1076 11.590 -10.309 -9.577 1.00119.65 C ANISOU 2150 CD ARG A1076 15917 16110 13432 50 361 -459 C ATOM 2151 NE ARG A1076 11.721 -10.495 -11.024 1.00135.77 N ANISOU 2151 NE ARG A1076 17948 18274 15363 83 371 -509 N ATOM 2152 CZ ARG A1076 11.166 -9.707 -11.941 1.00155.11 C ANISOU 2152 CZ ARG A1076 20367 20887 17680 167 317 -502 C ATOM 2153 NH1 ARG A1076 10.439 -8.659 -11.574 1.00145.46 N ANISOU 2153 NH1 ARG A1076 19129 19722 16418 235 252 -444 N ATOM 2154 NH2 ARG A1076 11.341 -9.957 -13.232 1.00143.76 N ANISOU 2154 NH2 ARG A1076 18925 19559 16141 197 331 -550 N ATOM 2155 N GLY A1077 17.095 -10.236 -8.666 1.00 88.94 N ANISOU 2155 N GLY A1077 12166 11841 9786 110 543 -95 N ATOM 2156 CA GLY A1077 18.417 -10.021 -9.242 1.00 88.94 C ANISOU 2156 CA GLY A1077 12162 11862 9768 140 588 -31 C ATOM 2157 C GLY A1077 19.497 -10.903 -8.649 1.00 92.05 C ANISOU 2157 C GLY A1077 12551 12186 10237 150 642 -28 C ATOM 2158 O GLY A1077 20.389 -11.349 -9.375 1.00 92.72 O ANISOU 2158 O GLY A1077 12627 12309 10294 183 695 -36 O ATOM 2159 N ILE A1078 19.408 -11.169 -7.326 1.00 86.78 N ANISOU 2159 N ILE A1078 11891 11426 9655 137 629 -17 N ATOM 2160 CA ILE A1078 20.333 -12.027 -6.572 1.00 86.28 C ANISOU 2160 CA ILE A1078 11832 11296 9654 174 675 -10 C ATOM 2161 C ILE A1078 20.273 -13.471 -7.122 1.00 91.11 C ANISOU 2161 C ILE A1078 12494 11874 10250 201 741 -111 C ATOM 2162 O ILE A1078 21.319 -14.057 -7.418 1.00 91.46 O ANISOU 2162 O ILE A1078 12536 11928 10285 265 796 -107 O ATOM 2163 CB ILE A1078 20.022 -11.971 -5.039 1.00 88.23 C ANISOU 2163 CB ILE A1078 12092 11452 9981 158 643 20 C ATOM 2164 CG1 ILE A1078 20.484 -10.630 -4.428 1.00 87.86 C ANISOU 2164 CG1 ILE A1078 11999 11431 9951 137 597 122 C ATOM 2165 CG2 ILE A1078 20.656 -13.147 -4.289 1.00 88.69 C ANISOU 2165 CG2 ILE A1078 12183 11429 10085 217 696 5 C ATOM 2166 CD1 ILE A1078 19.829 -10.216 -3.084 1.00 90.94 C ANISOU 2166 CD1 ILE A1078 12404 11750 10400 106 547 148 C ATOM 2167 N LEU A1079 19.045 -14.015 -7.277 1.00 87.36 N ANISOU 2167 N LEU A1079 12061 11368 9762 148 739 -209 N ATOM 2168 CA LEU A1079 18.767 -15.377 -7.748 1.00 87.69 C ANISOU 2168 CA LEU A1079 12172 11359 9786 140 810 -326 C ATOM 2169 C LEU A1079 19.164 -15.585 -9.224 1.00 91.64 C ANISOU 2169 C LEU A1079 12663 11952 10204 166 843 -371 C ATOM 2170 O LEU A1079 19.372 -16.726 -9.646 1.00 92.17 O ANISOU 2170 O LEU A1079 12796 11971 10255 184 919 -452 O ATOM 2171 CB LEU A1079 17.277 -15.720 -7.540 1.00 87.75 C ANISOU 2171 CB LEU A1079 12208 11341 9793 44 797 -431 C ATOM 2172 CG LEU A1079 16.739 -15.611 -6.098 1.00 91.63 C ANISOU 2172 CG LEU A1079 12717 11739 10360 8 773 -401 C ATOM 2173 CD1 LEU A1079 15.232 -15.512 -6.083 1.00 91.89 C ANISOU 2173 CD1 LEU A1079 12729 11814 10372 -91 739 -493 C ATOM 2174 CD2 LEU A1079 17.210 -16.766 -5.227 1.00 94.14 C ANISOU 2174 CD2 LEU A1079 13135 11899 10734 38 855 -409 C ATOM 2175 N ARG A1080 19.284 -14.488 -9.991 1.00 87.29 N ANISOU 2175 N ARG A1080 12048 11524 9596 172 796 -317 N ATOM 2176 CA ARG A1080 19.677 -14.516 -11.399 1.00 87.64 C ANISOU 2176 CA ARG A1080 12080 11669 9552 201 824 -344 C ATOM 2177 C ARG A1080 21.204 -14.356 -11.530 1.00 89.25 C ANISOU 2177 C ARG A1080 12255 11896 9762 273 866 -258 C ATOM 2178 O ARG A1080 21.805 -15.018 -12.380 1.00 89.72 O ANISOU 2178 O ARG A1080 12328 11986 9775 317 927 -301 O ATOM 2179 CB ARG A1080 18.923 -13.429 -12.179 1.00 89.74 C ANISOU 2179 CB ARG A1080 12307 12056 9735 179 758 -330 C ATOM 2180 CG ARG A1080 19.094 -13.479 -13.703 1.00106.44 C ANISOU 2180 CG ARG A1080 14417 14287 11737 207 783 -372 C ATOM 2181 CD ARG A1080 18.611 -12.205 -14.399 1.00124.15 C ANISOU 2181 CD ARG A1080 16636 16647 13888 222 723 -316 C ATOM 2182 NE ARG A1080 18.739 -11.008 -13.558 1.00138.53 N ANISOU 2182 NE ARG A1080 18450 18433 15754 222 682 -190 N ATOM 2183 CZ ARG A1080 19.857 -10.303 -13.402 1.00155.64 C ANISOU 2183 CZ ARG A1080 20612 20582 17942 235 709 -77 C ATOM 2184 NH1 ARG A1080 19.874 -9.251 -12.593 1.00143.50 N ANISOU 2184 NH1 ARG A1080 19079 19002 16442 217 676 19 N ATOM 2185 NH2 ARG A1080 20.969 -10.655 -14.036 1.00144.28 N ANISOU 2185 NH2 ARG A1080 19162 19174 16483 258 775 -69 N ATOM 2186 N ASN A1081 21.825 -13.502 -10.683 1.00 83.18 N ANISOU 2186 N ASN A1081 11440 11121 9043 279 838 -147 N ATOM 2187 CA ASN A1081 23.275 -13.282 -10.675 1.00 82.38 C ANISOU 2187 CA ASN A1081 11286 11069 8946 330 875 -74 C ATOM 2188 C ASN A1081 23.990 -14.532 -10.145 1.00 85.69 C ANISOU 2188 C ASN A1081 11726 11426 9404 412 934 -106 C ATOM 2189 O ASN A1081 23.712 -14.973 -9.029 1.00 84.60 O ANISOU 2189 O ASN A1081 11624 11188 9331 421 924 -108 O ATOM 2190 CB ASN A1081 23.641 -12.047 -9.849 1.00 80.03 C ANISOU 2190 CB ASN A1081 10934 10786 8686 291 831 31 C ATOM 2191 CG ASN A1081 25.090 -11.650 -9.969 1.00 98.08 C ANISOU 2191 CG ASN A1081 13145 13163 10960 312 871 93 C ATOM 2192 OD1 ASN A1081 25.951 -12.114 -9.217 1.00 89.22 O ANISOU 2192 OD1 ASN A1081 11978 12043 9878 363 891 106 O ATOM 2193 ND2 ASN A1081 25.393 -10.786 -10.924 1.00 91.87 N ANISOU 2193 ND2 ASN A1081 12340 12462 10106 275 888 129 N ATOM 2194 N ALA A1082 24.898 -15.101 -10.962 1.00 82.66 N ANISOU 2194 N ALA A1082 11331 11102 8973 483 1000 -128 N ATOM 2195 CA ALA A1082 25.659 -16.322 -10.672 1.00 82.80 C ANISOU 2195 CA ALA A1082 11383 11073 9003 596 1070 -158 C ATOM 2196 C ALA A1082 26.625 -16.173 -9.487 1.00 85.35 C ANISOU 2196 C ALA A1082 11642 11413 9375 664 1061 -79 C ATOM 2197 O ALA A1082 26.915 -17.170 -8.825 1.00 84.79 O ANISOU 2197 O ALA A1082 11626 11265 9324 767 1100 -94 O ATOM 2198 CB ALA A1082 26.432 -16.758 -11.907 1.00 84.60 C ANISOU 2198 CB ALA A1082 11599 11390 9156 662 1138 -193 C ATOM 2199 N LYS A1083 27.123 -14.949 -9.228 1.00 81.26 N ANISOU 2199 N LYS A1083 11015 10997 8865 610 1015 1 N ATOM 2200 CA LYS A1083 28.065 -14.674 -8.141 1.00 80.92 C ANISOU 2200 CA LYS A1083 10884 11009 8855 655 999 64 C ATOM 2201 C LYS A1083 27.370 -14.408 -6.794 1.00 83.08 C ANISOU 2201 C LYS A1083 11188 11181 9199 614 937 94 C ATOM 2202 O LYS A1083 27.963 -14.702 -5.753 1.00 82.79 O ANISOU 2202 O LYS A1083 11120 11149 9187 691 932 122 O ATOM 2203 CB LYS A1083 28.981 -13.491 -8.501 1.00 83.91 C ANISOU 2203 CB LYS A1083 11132 11549 9201 590 995 120 C ATOM 2204 CG LYS A1083 30.199 -13.882 -9.341 1.00103.31 C ANISOU 2204 CG LYS A1083 13511 14148 11593 672 1067 105 C ATOM 2205 CD LYS A1083 31.373 -14.346 -8.467 1.00115.88 C ANISOU 2205 CD LYS A1083 15005 15835 13188 794 1081 121 C ATOM 2206 CE LYS A1083 32.464 -15.028 -9.256 1.00126.48 C ANISOU 2206 CE LYS A1083 16285 17310 14462 918 1157 91 C ATOM 2207 NZ LYS A1083 33.434 -15.718 -8.362 1.00132.91 N ANISOU 2207 NZ LYS A1083 17027 18207 15267 1087 1169 98 N ATOM 2208 N LEU A1084 26.129 -13.867 -6.806 1.00 78.35 N ANISOU 2208 N LEU A1084 10645 10503 8622 505 889 86 N ATOM 2209 CA LEU A1084 25.367 -13.547 -5.585 1.00 76.91 C ANISOU 2209 CA LEU A1084 10492 10228 8502 459 831 110 C ATOM 2210 C LEU A1084 24.437 -14.676 -5.134 1.00 80.82 C ANISOU 2210 C LEU A1084 11106 10575 9028 486 850 48 C ATOM 2211 O LEU A1084 24.132 -14.765 -3.945 1.00 79.83 O ANISOU 2211 O LEU A1084 11008 10372 8952 490 825 70 O ATOM 2212 CB LEU A1084 24.529 -12.269 -5.764 1.00 75.87 C ANISOU 2212 CB LEU A1084 10355 10102 8370 337 772 138 C ATOM 2213 CG LEU A1084 25.249 -10.958 -6.064 1.00 80.22 C ANISOU 2213 CG LEU A1084 10827 10760 8893 276 761 204 C ATOM 2214 CD1 LEU A1084 24.249 -9.864 -6.291 1.00 79.85 C ANISOU 2214 CD1 LEU A1084 10821 10685 8832 188 715 228 C ATOM 2215 CD2 LEU A1084 26.186 -10.552 -4.937 1.00 82.30 C ANISOU 2215 CD2 LEU A1084 11011 11069 9192 276 746 256 C ATOM 2216 N LYS A1085 23.951 -15.499 -6.078 1.00 78.43 N ANISOU 2216 N LYS A1085 10877 10233 8690 490 899 -33 N ATOM 2217 CA LYS A1085 23.042 -16.617 -5.812 1.00 78.71 C ANISOU 2217 CA LYS A1085 11038 10126 8743 485 939 -113 C ATOM 2218 C LYS A1085 23.621 -17.634 -4.782 1.00 83.44 C ANISOU 2218 C LYS A1085 11710 10625 9370 604 993 -96 C ATOM 2219 O LYS A1085 22.860 -18.006 -3.884 1.00 82.63 O ANISOU 2219 O LYS A1085 11689 10398 9307 574 996 -111 O ATOM 2220 CB LYS A1085 22.671 -17.335 -7.123 1.00 82.16 C ANISOU 2220 CB LYS A1085 11532 10561 9123 468 996 -213 C ATOM 2221 CG LYS A1085 21.506 -18.309 -7.018 1.00 96.21 C ANISOU 2221 CG LYS A1085 13436 12208 10911 404 1039 -321 C ATOM 2222 CD LYS A1085 21.346 -19.093 -8.312 1.00106.15 C ANISOU 2222 CD LYS A1085 14752 13476 12104 393 1105 -430 C ATOM 2223 CE LYS A1085 20.650 -20.413 -8.111 1.00117.41 C ANISOU 2223 CE LYS A1085 16333 14742 13536 355 1193 -541 C ATOM 2224 NZ LYS A1085 21.520 -21.407 -7.422 1.00129.16 N ANISOU 2224 NZ LYS A1085 17934 16100 15041 490 1281 -510 N ATOM 2225 N PRO A1086 24.905 -18.109 -4.858 1.00 80.86 N ANISOU 2225 N PRO A1086 11360 10350 9013 746 1039 -66 N ATOM 2226 CA PRO A1086 25.368 -19.097 -3.870 1.00 81.39 C ANISOU 2226 CA PRO A1086 11516 10321 9088 887 1091 -47 C ATOM 2227 C PRO A1086 25.661 -18.494 -2.497 1.00 85.22 C ANISOU 2227 C PRO A1086 11936 10833 9611 913 1027 38 C ATOM 2228 O PRO A1086 25.539 -19.208 -1.500 1.00 84.81 O ANISOU 2228 O PRO A1086 11986 10663 9573 990 1057 51 O ATOM 2229 CB PRO A1086 26.646 -19.669 -4.499 1.00 84.28 C ANISOU 2229 CB PRO A1086 11856 10775 9393 1046 1153 -44 C ATOM 2230 CG PRO A1086 26.710 -19.115 -5.886 1.00 88.53 C ANISOU 2230 CG PRO A1086 12313 11430 9896 966 1145 -76 C ATOM 2231 CD PRO A1086 25.975 -17.828 -5.833 1.00 82.79 C ANISOU 2231 CD PRO A1086 11505 10748 9204 800 1054 -51 C ATOM 2232 N VAL A1087 26.040 -17.195 -2.435 1.00 81.98 N ANISOU 2232 N VAL A1087 11368 10568 9211 845 946 93 N ATOM 2233 CA VAL A1087 26.330 -16.532 -1.157 1.00 81.62 C ANISOU 2233 CA VAL A1087 11252 10563 9196 850 882 162 C ATOM 2234 C VAL A1087 25.009 -16.347 -0.383 1.00 85.34 C ANISOU 2234 C VAL A1087 11807 10895 9724 746 847 155 C ATOM 2235 O VAL A1087 24.996 -16.519 0.831 1.00 84.99 O ANISOU 2235 O VAL A1087 11794 10796 9701 795 833 191 O ATOM 2236 CB VAL A1087 27.170 -15.216 -1.249 1.00 85.17 C ANISOU 2236 CB VAL A1087 11523 11201 9635 792 823 212 C ATOM 2237 CG1 VAL A1087 28.442 -15.420 -2.065 1.00 86.16 C ANISOU 2237 CG1 VAL A1087 11555 11482 9701 882 866 208 C ATOM 2238 CG2 VAL A1087 26.370 -14.038 -1.790 1.00 83.95 C ANISOU 2238 CG2 VAL A1087 11346 11051 9501 616 775 212 C ATOM 2239 N TYR A1088 23.902 -16.082 -1.103 1.00 81.60 N ANISOU 2239 N TYR A1088 11370 10373 9261 616 839 104 N ATOM 2240 CA TYR A1088 22.557 -15.895 -0.562 1.00 80.80 C ANISOU 2240 CA TYR A1088 11330 10168 9202 508 809 81 C ATOM 2241 C TYR A1088 22.037 -17.173 0.104 1.00 85.02 C ANISOU 2241 C TYR A1088 12017 10537 9751 551 880 40 C ATOM 2242 O TYR A1088 21.471 -17.106 1.200 1.00 83.85 O ANISOU 2242 O TYR A1088 11909 10311 9640 523 860 60 O ATOM 2243 CB TYR A1088 21.615 -15.465 -1.695 1.00 81.90 C ANISOU 2243 CB TYR A1088 11460 10334 9323 391 793 21 C ATOM 2244 CG TYR A1088 20.260 -14.972 -1.238 1.00 83.26 C ANISOU 2244 CG TYR A1088 11651 10459 9525 281 745 -1 C ATOM 2245 CD1 TYR A1088 20.128 -13.755 -0.573 1.00 84.42 C ANISOU 2245 CD1 TYR A1088 11731 10648 9697 239 668 66 C ATOM 2246 CD2 TYR A1088 19.101 -15.682 -1.535 1.00 84.48 C ANISOU 2246 CD2 TYR A1088 11883 10540 9674 212 781 -98 C ATOM 2247 CE1 TYR A1088 18.881 -13.286 -0.165 1.00 84.90 C ANISOU 2247 CE1 TYR A1088 11804 10675 9777 155 625 46 C ATOM 2248 CE2 TYR A1088 17.847 -15.219 -1.139 1.00 84.96 C ANISOU 2248 CE2 TYR A1088 11938 10589 9753 115 738 -126 C ATOM 2249 CZ TYR A1088 17.742 -14.020 -0.453 1.00 91.95 C ANISOU 2249 CZ TYR A1088 12758 11516 10663 98 658 -50 C ATOM 2250 OH TYR A1088 16.511 -13.560 -0.051 1.00 92.46 O ANISOU 2250 OH TYR A1088 12815 11577 10738 21 616 -77 O ATOM 2251 N ASP A1089 22.254 -18.330 -0.553 1.00 82.90 N ANISOU 2251 N ASP A1089 11845 10205 9448 616 971 -17 N ATOM 2252 CA ASP A1089 21.830 -19.650 -0.083 1.00 83.55 C ANISOU 2252 CA ASP A1089 12109 10105 9530 654 1068 -63 C ATOM 2253 C ASP A1089 22.603 -20.090 1.169 1.00 87.42 C ANISOU 2253 C ASP A1089 12652 10544 10019 814 1089 16 C ATOM 2254 O ASP A1089 22.017 -20.725 2.047 1.00 87.32 O ANISOU 2254 O ASP A1089 12777 10377 10022 813 1139 10 O ATOM 2255 CB ASP A1089 21.991 -20.697 -1.201 1.00 86.60 C ANISOU 2255 CB ASP A1089 12593 10443 9870 690 1168 -145 C ATOM 2256 CG ASP A1089 21.161 -20.437 -2.451 1.00 96.57 C ANISOU 2256 CG ASP A1089 13819 11757 11117 541 1156 -240 C ATOM 2257 OD1 ASP A1089 20.014 -19.941 -2.318 1.00 96.12 O ANISOU 2257 OD1 ASP A1089 13737 11699 11085 395 1110 -278 O ATOM 2258 OD2 ASP A1089 21.641 -20.764 -3.560 1.00102.98 O ANISOU 2258 OD2 ASP A1089 14628 12619 11882 579 1195 -280 O ATOM 2259 N SER A1090 23.901 -19.742 1.256 1.00 83.79 N ANISOU 2259 N SER A1090 12079 10225 9532 948 1054 87 N ATOM 2260 CA SER A1090 24.764 -20.095 2.386 1.00 84.00 C ANISOU 2260 CA SER A1090 12125 10256 9536 1127 1060 162 C ATOM 2261 C SER A1090 24.429 -19.294 3.647 1.00 87.15 C ANISOU 2261 C SER A1090 12469 10669 9975 1073 978 219 C ATOM 2262 O SER A1090 24.649 -19.789 4.756 1.00 87.91 O ANISOU 2262 O SER A1090 12643 10702 10056 1193 998 266 O ATOM 2263 CB SER A1090 26.232 -19.886 2.023 1.00 88.02 C ANISOU 2263 CB SER A1090 12492 10959 9993 1270 1040 203 C ATOM 2264 OG SER A1090 26.534 -18.521 1.789 1.00 95.59 O ANISOU 2264 OG SER A1090 13250 12098 10969 1161 943 227 O ATOM 2265 N LEU A1091 23.919 -18.060 3.478 1.00 82.00 N ANISOU 2265 N LEU A1091 11694 10096 9365 907 890 218 N ATOM 2266 CA LEU A1091 23.591 -17.148 4.580 1.00 80.56 C ANISOU 2266 CA LEU A1091 11453 9937 9220 842 809 266 C ATOM 2267 C LEU A1091 22.306 -17.526 5.318 1.00 83.01 C ANISOU 2267 C LEU A1091 11900 10074 9568 766 835 242 C ATOM 2268 O LEU A1091 21.511 -18.334 4.837 1.00 83.47 O ANISOU 2268 O LEU A1091 12082 10004 9629 715 911 173 O ATOM 2269 CB LEU A1091 23.467 -15.693 4.076 1.00 79.60 C ANISOU 2269 CB LEU A1091 11182 9942 9121 699 722 272 C ATOM 2270 CG LEU A1091 24.745 -15.001 3.595 1.00 84.65 C ANISOU 2270 CG LEU A1091 11666 10771 9727 732 689 303 C ATOM 2271 CD1 LEU A1091 24.417 -13.774 2.771 1.00 84.12 C ANISOU 2271 CD1 LEU A1091 11515 10773 9672 580 642 296 C ATOM 2272 CD2 LEU A1091 25.682 -14.663 4.746 1.00 87.18 C ANISOU 2272 CD2 LEU A1091 11899 11195 10032 813 644 360 C ATOM 2273 N ASP A1092 22.117 -16.917 6.497 1.00 77.67 N ANISOU 2273 N ASP A1092 11193 9403 8915 748 776 291 N ATOM 2274 CA ASP A1092 20.945 -17.066 7.353 1.00 76.59 C ANISOU 2274 CA ASP A1092 11158 9130 8812 670 789 277 C ATOM 2275 C ASP A1092 19.966 -15.912 7.074 1.00 79.13 C ANISOU 2275 C ASP A1092 11394 9496 9176 495 716 250 C ATOM 2276 O ASP A1092 20.353 -14.917 6.457 1.00 77.91 O ANISOU 2276 O ASP A1092 11112 9470 9019 455 652 264 O ATOM 2277 CB ASP A1092 21.350 -17.128 8.835 1.00 78.31 C ANISOU 2277 CB ASP A1092 11403 9332 9018 776 772 349 C ATOM 2278 CG ASP A1092 22.460 -16.174 9.211 1.00 86.11 C ANISOU 2278 CG ASP A1092 12225 10505 9988 834 679 409 C ATOM 2279 OD1 ASP A1092 22.162 -14.995 9.475 1.00 85.24 O ANISOU 2279 OD1 ASP A1092 12017 10461 9908 721 598 419 O ATOM 2280 OD2 ASP A1092 23.629 -16.606 9.225 1.00 92.30 O ANISOU 2280 OD2 ASP A1092 12978 11373 10720 992 693 439 O ATOM 2281 N ALA A1093 18.702 -16.061 7.514 1.00 75.49 N ANISOU 2281 N ALA A1093 11009 8931 8743 396 736 211 N ATOM 2282 CA ALA A1093 17.591 -15.128 7.296 1.00 74.27 C ANISOU 2282 CA ALA A1093 10791 8813 8615 251 679 175 C ATOM 2283 C ALA A1093 17.939 -13.651 7.558 1.00 77.38 C ANISOU 2283 C ALA A1093 11057 9326 9019 234 573 238 C ATOM 2284 O ALA A1093 17.554 -12.795 6.757 1.00 76.64 O ANISOU 2284 O ALA A1093 10892 9304 8921 160 528 219 O ATOM 2285 CB ALA A1093 16.402 -15.529 8.153 1.00 74.92 C ANISOU 2285 CB ALA A1093 10964 8782 8719 179 716 140 C ATOM 2286 N VAL A1094 18.652 -13.357 8.661 1.00 73.48 N ANISOU 2286 N VAL A1094 10542 8850 8527 302 540 306 N ATOM 2287 CA VAL A1094 19.025 -11.986 9.038 1.00 72.26 C ANISOU 2287 CA VAL A1094 10283 8794 8378 270 452 356 C ATOM 2288 C VAL A1094 20.186 -11.478 8.139 1.00 75.49 C ANISOU 2288 C VAL A1094 10591 9331 8760 290 432 375 C ATOM 2289 O VAL A1094 20.107 -10.353 7.643 1.00 74.79 O ANISOU 2289 O VAL A1094 10440 9305 8671 210 388 382 O ATOM 2290 CB VAL A1094 19.307 -11.843 10.565 1.00 76.03 C ANISOU 2290 CB VAL A1094 10770 9259 8859 320 423 407 C ATOM 2291 CG1 VAL A1094 20.152 -12.990 11.110 1.00 76.89 C ANISOU 2291 CG1 VAL A1094 10934 9344 8936 466 473 432 C ATOM 2292 CG2 VAL A1094 19.896 -10.481 10.933 1.00 75.36 C ANISOU 2292 CG2 VAL A1094 10579 9283 8771 281 344 446 C ATOM 2293 N ARG A1095 21.212 -12.316 7.877 1.00 71.60 N ANISOU 2293 N ARG A1095 10094 8874 8239 398 475 380 N ATOM 2294 CA ARG A1095 22.346 -11.948 7.020 1.00 70.85 C ANISOU 2294 CA ARG A1095 9896 8913 8112 418 468 390 C ATOM 2295 C ARG A1095 21.930 -11.797 5.556 1.00 73.74 C ANISOU 2295 C ARG A1095 10260 9286 8472 348 488 349 C ATOM 2296 O ARG A1095 22.565 -11.035 4.826 1.00 73.02 O ANISOU 2296 O ARG A1095 10084 9300 8360 312 472 362 O ATOM 2297 CB ARG A1095 23.479 -12.964 7.143 1.00 70.65 C ANISOU 2297 CB ARG A1095 9865 8933 8047 575 511 403 C ATOM 2298 CG ARG A1095 24.378 -12.712 8.337 1.00 75.72 C ANISOU 2298 CG ARG A1095 10436 9670 8665 652 469 449 C ATOM 2299 CD ARG A1095 25.363 -13.842 8.494 1.00 80.23 C ANISOU 2299 CD ARG A1095 11019 10285 9182 844 515 462 C ATOM 2300 NE ARG A1095 26.274 -13.623 9.615 1.00 81.74 N ANISOU 2300 NE ARG A1095 11121 10605 9331 937 468 500 N ATOM 2301 CZ ARG A1095 26.229 -14.283 10.767 1.00 88.23 C ANISOU 2301 CZ ARG A1095 12024 11371 10128 1063 475 531 C ATOM 2302 NH1 ARG A1095 25.317 -15.226 10.964 1.00 74.77 N ANISOU 2302 NH1 ARG A1095 10504 9464 8442 1100 540 531 N ATOM 2303 NH2 ARG A1095 27.095 -14.007 11.730 1.00 71.56 N ANISOU 2303 NH2 ARG A1095 9812 9411 7966 1149 423 559 N ATOM 2304 N ARG A1096 20.858 -12.507 5.136 1.00 70.36 N ANISOU 2304 N ARG A1096 9926 8754 8055 322 528 295 N ATOM 2305 CA ARG A1096 20.292 -12.429 3.787 1.00 70.00 C ANISOU 2305 CA ARG A1096 9881 8724 7993 258 543 244 C ATOM 2306 C ARG A1096 19.747 -11.020 3.555 1.00 72.93 C ANISOU 2306 C ARG A1096 10200 9146 8364 163 478 263 C ATOM 2307 O ARG A1096 20.006 -10.437 2.501 1.00 72.98 O ANISOU 2307 O ARG A1096 10163 9228 8338 138 472 266 O ATOM 2308 CB ARG A1096 19.198 -13.489 3.576 1.00 71.26 C ANISOU 2308 CB ARG A1096 10144 8774 8158 233 599 166 C ATOM 2309 CG ARG A1096 19.730 -14.839 3.100 1.00 86.13 C ANISOU 2309 CG ARG A1096 12099 10607 10017 315 686 129 C ATOM 2310 CD ARG A1096 18.606 -15.791 2.725 1.00 98.50 C ANISOU 2310 CD ARG A1096 13771 12070 11583 250 752 32 C ATOM 2311 NE ARG A1096 18.160 -16.582 3.873 1.00109.62 N ANISOU 2311 NE ARG A1096 15295 13339 13016 260 803 27 N ATOM 2312 CZ ARG A1096 18.459 -17.863 4.066 1.00126.61 C ANISOU 2312 CZ ARG A1096 17581 15372 15153 335 903 7 C ATOM 2313 NH1 ARG A1096 19.193 -18.523 3.177 1.00114.58 N ANISOU 2313 NH1 ARG A1096 16086 13856 13593 411 958 -15 N ATOM 2314 NH2 ARG A1096 18.018 -18.498 5.143 1.00115.34 N ANISOU 2314 NH2 ARG A1096 16273 13810 13741 340 956 11 N ATOM 2315 N ALA A1097 19.064 -10.448 4.579 1.00 68.43 N ANISOU 2315 N ALA A1097 9643 8532 7823 123 435 283 N ATOM 2316 CA ALA A1097 18.511 -9.090 4.559 1.00 67.29 C ANISOU 2316 CA ALA A1097 9475 8418 7676 54 378 308 C ATOM 2317 C ALA A1097 19.626 -8.065 4.334 1.00 71.34 C ANISOU 2317 C ALA A1097 9925 9013 8168 39 359 364 C ATOM 2318 O ALA A1097 19.473 -7.183 3.490 1.00 71.24 O ANISOU 2318 O ALA A1097 9906 9037 8123 -3 349 375 O ATOM 2319 CB ALA A1097 17.767 -8.799 5.854 1.00 67.26 C ANISOU 2319 CB ALA A1097 9500 8350 7705 32 345 320 C ATOM 2320 N ALA A1098 20.778 -8.243 5.018 1.00 67.45 N ANISOU 2320 N ALA A1098 9386 8558 7683 76 363 393 N ATOM 2321 CA ALA A1098 21.959 -7.390 4.876 1.00 67.16 C ANISOU 2321 CA ALA A1098 9272 8623 7623 44 356 428 C ATOM 2322 C ALA A1098 22.486 -7.405 3.431 1.00 71.12 C ANISOU 2322 C ALA A1098 9744 9195 8084 39 396 418 C ATOM 2323 O ALA A1098 22.885 -6.352 2.928 1.00 71.23 O ANISOU 2323 O ALA A1098 9734 9261 8071 -33 398 442 O ATOM 2324 CB ALA A1098 23.043 -7.834 5.843 1.00 68.29 C ANISOU 2324 CB ALA A1098 9353 8827 7768 105 353 442 C ATOM 2325 N LEU A1099 22.431 -8.578 2.750 1.00 67.30 N ANISOU 2325 N LEU A1099 9278 8700 7590 110 436 379 N ATOM 2326 CA LEU A1099 22.859 -8.722 1.354 1.00 67.29 C ANISOU 2326 CA LEU A1099 9257 8765 7547 116 477 362 C ATOM 2327 C LEU A1099 21.846 -8.053 0.415 1.00 70.76 C ANISOU 2327 C LEU A1099 9745 9181 7960 57 467 352 C ATOM 2328 O LEU A1099 22.268 -7.364 -0.520 1.00 70.79 O ANISOU 2328 O LEU A1099 9729 9249 7919 22 484 372 O ATOM 2329 CB LEU A1099 23.072 -10.203 0.977 1.00 67.73 C ANISOU 2329 CB LEU A1099 9334 8805 7595 215 528 316 C ATOM 2330 CG LEU A1099 23.557 -10.502 -0.454 1.00 72.83 C ANISOU 2330 CG LEU A1099 9959 9520 8192 235 576 290 C ATOM 2331 CD1 LEU A1099 25.020 -10.136 -0.640 1.00 73.68 C ANISOU 2331 CD1 LEU A1099 9962 9762 8270 251 595 322 C ATOM 2332 CD2 LEU A1099 23.349 -11.952 -0.797 1.00 75.44 C ANISOU 2332 CD2 LEU A1099 10355 9790 8517 317 629 232 C ATOM 2333 N ILE A1100 20.520 -8.242 0.673 1.00 66.41 N ANISOU 2333 N ILE A1100 9255 8552 7427 49 442 322 N ATOM 2334 CA ILE A1100 19.420 -7.638 -0.108 1.00 65.72 C ANISOU 2334 CA ILE A1100 9203 8465 7301 17 421 306 C ATOM 2335 C ILE A1100 19.593 -6.121 -0.092 1.00 67.39 C ANISOU 2335 C ILE A1100 9422 8695 7489 -29 397 374 C ATOM 2336 O ILE A1100 19.554 -5.498 -1.149 1.00 67.13 O ANISOU 2336 O ILE A1100 9407 8703 7396 -37 409 389 O ATOM 2337 CB ILE A1100 18.003 -8.061 0.413 1.00 68.68 C ANISOU 2337 CB ILE A1100 9619 8779 7698 12 395 255 C ATOM 2338 CG1 ILE A1100 17.755 -9.581 0.244 1.00 69.30 C ANISOU 2338 CG1 ILE A1100 9718 8823 7789 34 441 175 C ATOM 2339 CG2 ILE A1100 16.876 -7.240 -0.266 1.00 69.37 C ANISOU 2339 CG2 ILE A1100 9723 8903 7731 -2 361 244 C ATOM 2340 CD1 ILE A1100 16.842 -10.190 1.288 1.00 74.08 C ANISOU 2340 CD1 ILE A1100 10363 9345 8438 16 441 136 C ATOM 2341 N ASN A1101 19.815 -5.553 1.120 1.00 62.53 N ANISOU 2341 N ASN A1101 8804 8041 6913 -60 372 412 N ATOM 2342 CA ASN A1101 20.043 -4.135 1.414 1.00 61.88 C ANISOU 2342 CA ASN A1101 8747 7950 6816 -120 360 470 C ATOM 2343 C ASN A1101 21.136 -3.551 0.507 1.00 66.04 C ANISOU 2343 C ASN A1101 9254 8542 7296 -163 408 499 C ATOM 2344 O ASN A1101 20.949 -2.483 -0.091 1.00 66.07 O ANISOU 2344 O ASN A1101 9323 8532 7248 -197 423 537 O ATOM 2345 CB ASN A1101 20.439 -3.985 2.885 1.00 61.46 C ANISOU 2345 CB ASN A1101 8670 7868 6814 -147 336 485 C ATOM 2346 CG ASN A1101 20.522 -2.569 3.393 1.00 79.84 C ANISOU 2346 CG ASN A1101 11041 10164 9131 -221 326 530 C ATOM 2347 OD1 ASN A1101 21.278 -1.723 2.891 1.00 72.43 O ANISOU 2347 OD1 ASN A1101 10109 9255 8156 -287 362 557 O ATOM 2348 ND2 ASN A1101 19.803 -2.312 4.464 1.00 70.63 N ANISOU 2348 ND2 ASN A1101 9909 8932 7996 -220 286 533 N ATOM 2349 N MET A1102 22.272 -4.267 0.408 1.00 62.06 N ANISOU 2349 N MET A1102 8667 8111 6801 -154 439 483 N ATOM 2350 CA MET A1102 23.416 -3.887 -0.420 1.00 62.00 C ANISOU 2350 CA MET A1102 8618 8191 6750 -199 493 499 C ATOM 2351 C MET A1102 23.040 -3.838 -1.904 1.00 64.98 C ANISOU 2351 C MET A1102 9044 8583 7064 -177 525 498 C ATOM 2352 O MET A1102 23.473 -2.928 -2.601 1.00 64.37 O ANISOU 2352 O MET A1102 8996 8529 6934 -236 568 534 O ATOM 2353 CB MET A1102 24.580 -4.857 -0.193 1.00 64.38 C ANISOU 2353 CB MET A1102 8807 8587 7067 -158 514 472 C ATOM 2354 CG MET A1102 25.415 -4.503 1.005 1.00 67.23 C ANISOU 2354 CG MET A1102 9095 8996 7452 -204 498 481 C ATOM 2355 SD MET A1102 26.908 -5.503 1.107 1.00 71.33 S ANISOU 2355 SD MET A1102 9467 9676 7960 -132 525 451 S ATOM 2356 CE MET A1102 27.968 -4.627 -0.012 1.00 68.85 C ANISOU 2356 CE MET A1102 9093 9484 7583 -243 596 457 C ATOM 2357 N VAL A1103 22.237 -4.815 -2.373 1.00 61.71 N ANISOU 2357 N VAL A1103 8643 8156 6648 -98 509 453 N ATOM 2358 CA VAL A1103 21.758 -4.921 -3.756 1.00 62.34 C ANISOU 2358 CA VAL A1103 8760 8267 6661 -64 529 436 C ATOM 2359 C VAL A1103 20.736 -3.799 -4.027 1.00 67.79 C ANISOU 2359 C VAL A1103 9542 8916 7300 -70 503 473 C ATOM 2360 O VAL A1103 20.752 -3.214 -5.110 1.00 68.45 O ANISOU 2360 O VAL A1103 9673 9032 7305 -65 534 500 O ATOM 2361 CB VAL A1103 21.189 -6.341 -4.053 1.00 66.04 C ANISOU 2361 CB VAL A1103 9215 8737 7141 4 523 358 C ATOM 2362 CG1 VAL A1103 20.419 -6.393 -5.373 1.00 66.09 C ANISOU 2362 CG1 VAL A1103 9258 8783 7069 34 527 325 C ATOM 2363 CG2 VAL A1103 22.306 -7.381 -4.051 1.00 66.29 C ANISOU 2363 CG2 VAL A1103 9183 8809 7196 38 567 332 C ATOM 2364 N PHE A1104 19.886 -3.477 -3.036 1.00 64.07 N ANISOU 2364 N PHE A1104 9101 8376 6865 -70 453 478 N ATOM 2365 CA PHE A1104 18.879 -2.420 -3.123 1.00 63.98 C ANISOU 2365 CA PHE A1104 9178 8326 6803 -50 426 514 C ATOM 2366 C PHE A1104 19.542 -1.046 -3.377 1.00 70.49 C ANISOU 2366 C PHE A1104 10081 9121 7579 -105 473 593 C ATOM 2367 O PHE A1104 19.080 -0.287 -4.237 1.00 70.87 O ANISOU 2367 O PHE A1104 10221 9169 7539 -64 489 631 O ATOM 2368 CB PHE A1104 18.059 -2.397 -1.822 1.00 64.61 C ANISOU 2368 CB PHE A1104 9262 8342 6943 -47 371 502 C ATOM 2369 CG PHE A1104 16.899 -1.433 -1.778 1.00 65.99 C ANISOU 2369 CG PHE A1104 9520 8488 7067 -1 338 529 C ATOM 2370 CD1 PHE A1104 15.628 -1.831 -2.177 1.00 68.86 C ANISOU 2370 CD1 PHE A1104 9870 8903 7389 73 297 476 C ATOM 2371 CD2 PHE A1104 17.066 -0.139 -1.293 1.00 68.22 C ANISOU 2371 CD2 PHE A1104 9890 8697 7335 -30 350 599 C ATOM 2372 CE1 PHE A1104 14.548 -0.948 -2.109 1.00 69.96 C ANISOU 2372 CE1 PHE A1104 10072 9040 7469 141 262 499 C ATOM 2373 CE2 PHE A1104 15.987 0.745 -1.228 1.00 71.26 C ANISOU 2373 CE2 PHE A1104 10363 9049 7662 38 323 627 C ATOM 2374 CZ PHE A1104 14.735 0.336 -1.639 1.00 69.44 C ANISOU 2374 CZ PHE A1104 10107 8889 7387 135 276 580 C ATOM 2375 N GLN A1105 20.641 -0.760 -2.650 1.00 67.87 N ANISOU 2375 N GLN A1105 9718 8773 7295 -197 503 614 N ATOM 2376 CA GLN A1105 21.388 0.496 -2.703 1.00 68.44 C ANISOU 2376 CA GLN A1105 9863 8811 7332 -291 563 672 C ATOM 2377 C GLN A1105 22.362 0.586 -3.896 1.00 74.25 C ANISOU 2377 C GLN A1105 10590 9615 8006 -331 642 686 C ATOM 2378 O GLN A1105 22.306 1.559 -4.646 1.00 74.71 O ANISOU 2378 O GLN A1105 10767 9635 7983 -347 696 739 O ATOM 2379 CB GLN A1105 22.165 0.682 -1.385 1.00 69.30 C ANISOU 2379 CB GLN A1105 9916 8905 7512 -388 560 665 C ATOM 2380 CG GLN A1105 22.809 2.059 -1.220 1.00 78.14 C ANISOU 2380 CG GLN A1105 11121 9972 8597 -515 625 708 C ATOM 2381 CD GLN A1105 23.860 2.119 -0.136 1.00 95.69 C ANISOU 2381 CD GLN A1105 13248 12237 10874 -631 631 680 C ATOM 2382 OE1 GLN A1105 24.319 1.105 0.405 1.00 91.18 O ANISOU 2382 OE1 GLN A1105 12536 11753 10357 -603 592 636 O ATOM 2383 NE2 GLN A1105 24.284 3.326 0.194 1.00 90.30 N ANISOU 2383 NE2 GLN A1105 12646 11496 10166 -762 686 701 N ATOM 2384 N MET A1106 23.270 -0.385 -4.036 1.00 72.46 N ANISOU 2384 N MET A1106 10235 9485 7813 -342 656 643 N ATOM 2385 CA MET A1106 24.334 -0.373 -5.043 1.00 74.41 C ANISOU 2385 CA MET A1106 10447 9817 8008 -388 735 648 C ATOM 2386 C MET A1106 23.951 -1.027 -6.364 1.00 79.31 C ANISOU 2386 C MET A1106 11076 10487 8569 -292 743 632 C ATOM 2387 O MET A1106 24.473 -0.624 -7.407 1.00 80.89 O ANISOU 2387 O MET A1106 11312 10728 8695 -320 815 659 O ATOM 2388 CB MET A1106 25.596 -1.061 -4.497 1.00 77.40 C ANISOU 2388 CB MET A1106 10670 10300 8440 -433 749 606 C ATOM 2389 CG MET A1106 26.145 -0.418 -3.229 1.00 81.71 C ANISOU 2389 CG MET A1106 11183 10833 9030 -541 744 609 C ATOM 2390 SD MET A1106 27.593 -1.283 -2.586 1.00 86.94 S ANISOU 2390 SD MET A1106 11640 11662 9732 -558 748 554 S ATOM 2391 CE MET A1106 28.843 -0.705 -3.752 1.00 85.53 C ANISOU 2391 CE MET A1106 11422 11600 9475 -674 864 558 C ATOM 2392 N GLY A1107 23.086 -2.032 -6.317 1.00 74.25 N ANISOU 2392 N GLY A1107 10406 9849 7955 -192 679 583 N ATOM 2393 CA GLY A1107 22.675 -2.764 -7.507 1.00 74.23 C ANISOU 2393 CA GLY A1107 10403 9904 7896 -109 682 546 C ATOM 2394 C GLY A1107 23.213 -4.176 -7.497 1.00 78.54 C ANISOU 2394 C GLY A1107 10842 10511 8490 -74 686 477 C ATOM 2395 O GLY A1107 24.128 -4.486 -6.731 1.00 78.46 O ANISOU 2395 O GLY A1107 10753 10521 8539 -105 698 472 O ATOM 2396 N GLU A1108 22.655 -5.035 -8.354 1.00 75.40 N ANISOU 2396 N GLU A1108 10445 10147 8054 -2 678 421 N ATOM 2397 CA GLU A1108 23.033 -6.446 -8.465 1.00 75.27 C ANISOU 2397 CA GLU A1108 10362 10167 8070 45 693 349 C ATOM 2398 C GLU A1108 24.502 -6.603 -8.900 1.00 78.67 C ANISOU 2398 C GLU A1108 10724 10681 8485 32 764 361 C ATOM 2399 O GLU A1108 25.249 -7.342 -8.262 1.00 77.50 O ANISOU 2399 O GLU A1108 10505 10553 8391 55 775 339 O ATOM 2400 CB GLU A1108 22.098 -7.179 -9.449 1.00 77.04 C ANISOU 2400 CB GLU A1108 10617 10415 8239 103 682 278 C ATOM 2401 CG GLU A1108 20.617 -7.036 -9.133 1.00 86.79 C ANISOU 2401 CG GLU A1108 11896 11609 9471 115 615 251 C ATOM 2402 N THR A1109 24.916 -5.885 -9.958 1.00 76.15 N ANISOU 2402 N THR A1109 10429 10421 8085 3 815 398 N ATOM 2403 CA THR A1109 26.278 -5.962 -10.491 1.00 76.75 C ANISOU 2403 CA THR A1109 10433 10596 8132 -19 891 405 C ATOM 2404 C THR A1109 27.301 -5.269 -9.559 1.00 80.58 C ANISOU 2404 C THR A1109 10850 11107 8658 -112 913 445 C ATOM 2405 O THR A1109 28.475 -5.646 -9.571 1.00 80.90 O ANISOU 2405 O THR A1109 10785 11253 8701 -116 960 427 O ATOM 2406 CB THR A1109 26.332 -5.421 -11.935 1.00 83.15 C ANISOU 2406 CB THR A1109 11302 11458 8833 -27 948 430 C ATOM 2407 OG1 THR A1109 27.486 -5.953 -12.579 1.00 83.82 O ANISOU 2407 OG1 THR A1109 11305 11652 8890 -18 1019 406 O ATOM 2408 CG2 THR A1109 26.338 -3.895 -12.020 1.00 81.35 C ANISOU 2408 CG2 THR A1109 11159 11192 8557 -117 979 515 C ATOM 2409 N GLY A1110 26.844 -4.278 -8.784 1.00 76.06 N ANISOU 2409 N GLY A1110 10335 10452 8111 -181 881 490 N ATOM 2410 CA GLY A1110 27.677 -3.523 -7.856 1.00 75.77 C ANISOU 2410 CA GLY A1110 10248 10434 8108 -290 899 516 C ATOM 2411 C GLY A1110 28.267 -4.387 -6.761 1.00 78.92 C ANISOU 2411 C GLY A1110 10522 10886 8580 -251 865 475 C ATOM 2412 O GLY A1110 29.489 -4.418 -6.587 1.00 78.77 O ANISOU 2412 O GLY A1110 10384 10990 8555 -291 906 461 O ATOM 2413 N VAL A1111 27.390 -5.135 -6.053 1.00 74.60 N ANISOU 2413 N VAL A1111 9999 10256 8090 -165 794 452 N ATOM 2414 CA VAL A1111 27.731 -6.030 -4.937 1.00 74.07 C ANISOU 2414 CA VAL A1111 9851 10208 8085 -100 758 421 C ATOM 2415 C VAL A1111 28.586 -7.217 -5.434 1.00 79.13 C ANISOU 2415 C VAL A1111 10408 10952 8706 4 799 379 C ATOM 2416 O VAL A1111 29.462 -7.685 -4.701 1.00 79.49 O ANISOU 2416 O VAL A1111 10352 11082 8768 50 798 365 O ATOM 2417 CB VAL A1111 26.466 -6.509 -4.173 1.00 76.45 C ANISOU 2417 CB VAL A1111 10229 10377 8442 -44 690 409 C ATOM 2418 CG1 VAL A1111 26.835 -7.238 -2.882 1.00 76.05 C ANISOU 2418 CG1 VAL A1111 10118 10330 8446 17 659 394 C ATOM 2419 CG2 VAL A1111 25.548 -5.337 -3.859 1.00 75.52 C ANISOU 2419 CG2 VAL A1111 10200 10166 8329 -123 654 449 C ATOM 2420 N ALA A1112 28.365 -7.661 -6.687 1.00 75.70 N ANISOU 2420 N ALA A1112 10015 10524 8224 47 836 357 N ATOM 2421 CA ALA A1112 29.115 -8.753 -7.315 1.00 76.31 C ANISOU 2421 CA ALA A1112 10035 10689 8272 150 885 315 C ATOM 2422 C ALA A1112 30.612 -8.400 -7.471 1.00 81.51 C ANISOU 2422 C ALA A1112 10556 11523 8891 117 941 323 C ATOM 2423 O ALA A1112 31.435 -9.298 -7.672 1.00 82.44 O ANISOU 2423 O ALA A1112 10595 11740 8987 221 977 290 O ATOM 2424 CB ALA A1112 28.506 -9.094 -8.667 1.00 77.10 C ANISOU 2424 CB ALA A1112 10214 10762 8319 178 913 287 C ATOM 2425 N GLY A1113 30.937 -7.111 -7.334 1.00 77.63 N ANISOU 2425 N GLY A1113 10040 11068 8388 -29 953 361 N ATOM 2426 CA GLY A1113 32.299 -6.595 -7.407 1.00 78.58 C ANISOU 2426 CA GLY A1113 10024 11363 8469 -109 1012 359 C ATOM 2427 C GLY A1113 33.141 -6.946 -6.197 1.00 82.46 C ANISOU 2427 C GLY A1113 10372 11969 8988 -69 983 335 C ATOM 2428 O GLY A1113 34.369 -6.995 -6.288 1.00 83.44 O ANISOU 2428 O GLY A1113 10344 12288 9070 -75 1028 308 O ATOM 2429 N PHE A1114 32.482 -7.215 -5.057 1.00 78.04 N ANISOU 2429 N PHE A1114 9856 11306 8491 -18 907 342 N ATOM 2430 CA PHE A1114 33.126 -7.584 -3.795 1.00 78.41 C ANISOU 2430 CA PHE A1114 9787 11448 8558 44 867 325 C ATOM 2431 C PHE A1114 33.493 -9.080 -3.790 1.00 83.75 C ANISOU 2431 C PHE A1114 10427 12174 9221 263 872 297 C ATOM 2432 O PHE A1114 33.203 -9.786 -2.821 1.00 82.91 O ANISOU 2432 O PHE A1114 10348 12007 9147 380 825 298 O ATOM 2433 CB PHE A1114 32.206 -7.243 -2.607 1.00 78.94 C ANISOU 2433 CB PHE A1114 9937 11369 8689 12 791 349 C ATOM 2434 CG PHE A1114 31.871 -5.781 -2.467 1.00 80.25 C ANISOU 2434 CG PHE A1114 10153 11476 8863 -183 789 377 C ATOM 2435 CD1 PHE A1114 32.730 -4.915 -1.801 1.00 84.47 C ANISOU 2435 CD1 PHE A1114 10579 12133 9383 -313 797 364 C ATOM 2436 CD2 PHE A1114 30.682 -5.273 -2.970 1.00 81.52 C ANISOU 2436 CD2 PHE A1114 10475 11461 9038 -232 783 410 C ATOM 2437 CE1 PHE A1114 32.417 -3.559 -1.669 1.00 85.43 C ANISOU 2437 CE1 PHE A1114 10777 12175 9508 -498 810 387 C ATOM 2438 CE2 PHE A1114 30.370 -3.918 -2.840 1.00 84.41 C ANISOU 2438 CE2 PHE A1114 10913 11758 9401 -389 790 442 C ATOM 2439 CZ PHE A1114 31.238 -3.070 -2.188 1.00 83.45 C ANISOU 2439 CZ PHE A1114 10708 11731 9270 -525 809 432 C ATOM 2440 N THR A1115 34.161 -9.546 -4.869 1.00 81.84 N ANISOU 2440 N THR A1115 10133 12039 8922 322 939 273 N ATOM 2441 CA THR A1115 34.587 -10.932 -5.108 1.00 82.36 C ANISOU 2441 CA THR A1115 10183 12153 8959 535 966 244 C ATOM 2442 C THR A1115 35.220 -11.583 -3.861 1.00 86.08 C ANISOU 2442 C THR A1115 10563 12717 9425 688 930 238 C ATOM 2443 O THR A1115 34.880 -12.728 -3.549 1.00 85.92 O ANISOU 2443 O THR A1115 10637 12595 9415 867 926 235 O ATOM 2444 CB THR A1115 35.541 -11.008 -6.312 1.00 93.19 C ANISOU 2444 CB THR A1115 11457 13693 10256 546 1047 217 C ATOM 2445 OG1 THR A1115 36.554 -10.002 -6.194 1.00 95.06 O ANISOU 2445 OG1 THR A1115 11524 14135 10458 407 1068 212 O ATOM 2446 CG2 THR A1115 34.809 -10.865 -7.646 1.00 91.15 C ANISOU 2446 CG2 THR A1115 11327 13319 9987 481 1087 219 C ATOM 2447 N ASN A1116 36.087 -10.841 -3.131 1.00 82.01 N ANISOU 2447 N ASN A1116 9880 12390 8889 614 908 233 N ATOM 2448 CA ASN A1116 36.750 -11.329 -1.917 1.00 81.84 C ANISOU 2448 CA ASN A1116 9750 12501 8846 759 865 226 C ATOM 2449 C ASN A1116 35.773 -11.445 -0.743 1.00 81.49 C ANISOU 2449 C ASN A1116 9831 12265 8864 782 794 258 C ATOM 2450 O ASN A1116 35.740 -12.493 -0.105 1.00 80.60 O ANISOU 2450 O ASN A1116 9769 12114 8743 987 780 267 O ATOM 2451 CB ASN A1116 37.932 -10.426 -1.525 1.00 85.55 C ANISOU 2451 CB ASN A1116 9987 13253 9265 643 861 193 C ATOM 2452 CG ASN A1116 39.060 -10.356 -2.533 1.00112.23 C ANISOU 2452 CG ASN A1116 13205 16868 12568 627 937 152 C ATOM 2453 OD1 ASN A1116 39.389 -11.327 -3.227 1.00105.86 O ANISOU 2453 OD1 ASN A1116 12400 16102 11719 808 983 142 O ATOM 2454 ND2 ASN A1116 39.722 -9.210 -2.589 1.00106.43 N ANISOU 2454 ND2 ASN A1116 12326 16304 11807 408 960 121 N ATOM 2455 N SER A1117 34.985 -10.378 -0.467 1.00 75.96 N ANISOU 2455 N SER A1117 9196 11443 8222 580 758 278 N ATOM 2456 CA SER A1117 34.010 -10.289 0.634 1.00 74.09 C ANISOU 2456 CA SER A1117 9071 11033 8046 568 693 307 C ATOM 2457 C SER A1117 32.931 -11.363 0.558 1.00 77.20 C ANISOU 2457 C SER A1117 9656 11197 8479 695 697 321 C ATOM 2458 O SER A1117 32.562 -11.923 1.589 1.00 76.80 O ANISOU 2458 O SER A1117 9669 11063 8448 797 663 337 O ATOM 2459 CB SER A1117 33.338 -8.920 0.654 1.00 75.97 C ANISOU 2459 CB SER A1117 9358 11177 8328 332 671 323 C ATOM 2460 OG SER A1117 34.279 -7.867 0.764 1.00 85.58 O ANISOU 2460 OG SER A1117 10424 12581 9510 180 681 301 O ATOM 2461 N LEU A1118 32.422 -11.637 -0.657 1.00 73.16 N ANISOU 2461 N LEU A1118 9239 10587 7972 678 745 310 N ATOM 2462 CA LEU A1118 31.383 -12.633 -0.915 1.00 72.12 C ANISOU 2462 CA LEU A1118 9285 10249 7869 762 763 302 C ATOM 2463 C LEU A1118 31.910 -14.039 -0.633 1.00 78.00 C ANISOU 2463 C LEU A1118 10054 11005 8576 994 801 292 C ATOM 2464 O LEU A1118 31.182 -14.861 -0.068 1.00 77.33 O ANISOU 2464 O LEU A1118 10114 10751 8518 1078 805 295 O ATOM 2465 CB LEU A1118 30.878 -12.517 -2.364 1.00 71.65 C ANISOU 2465 CB LEU A1118 9290 10133 7802 683 805 280 C ATOM 2466 CG LEU A1118 30.229 -11.185 -2.768 1.00 74.67 C ANISOU 2466 CG LEU A1118 9687 10478 8205 484 779 299 C ATOM 2467 CD1 LEU A1118 30.313 -10.978 -4.262 1.00 75.01 C ANISOU 2467 CD1 LEU A1118 9735 10562 8203 436 831 283 C ATOM 2468 CD2 LEU A1118 28.794 -11.088 -2.285 1.00 74.95 C ANISOU 2468 CD2 LEU A1118 9856 10325 8297 433 733 305 C ATOM 2469 N ARG A1119 33.191 -14.297 -0.990 1.00 76.61 N ANISOU 2469 N ARG A1119 9743 11032 8331 1102 836 279 N ATOM 2470 CA ARG A1119 33.887 -15.562 -0.740 1.00 78.10 C ANISOU 2470 CA ARG A1119 9942 11268 8462 1356 876 274 C ATOM 2471 C ARG A1119 33.972 -15.800 0.779 1.00 82.65 C ANISOU 2471 C ARG A1119 10520 11845 9037 1467 827 307 C ATOM 2472 O ARG A1119 33.717 -16.915 1.237 1.00 83.14 O ANISOU 2472 O ARG A1119 10727 11777 9087 1647 858 319 O ATOM 2473 CB ARG A1119 35.288 -15.540 -1.390 1.00 80.84 C ANISOU 2473 CB ARG A1119 10103 11884 8728 1431 913 251 C ATOM 2474 CG ARG A1119 36.062 -16.858 -1.296 1.00 97.64 C ANISOU 2474 CG ARG A1119 12243 14077 10779 1726 964 245 C ATOM 2475 CD ARG A1119 37.525 -16.705 -1.686 1.00115.47 C ANISOU 2475 CD ARG A1119 14270 16656 12948 1805 986 221 C ATOM 2476 NE ARG A1119 37.710 -16.700 -3.140 1.00129.63 N ANISOU 2476 NE ARG A1119 16052 18480 14722 1750 1053 187 N ATOM 2477 CZ ARG A1119 37.963 -15.613 -3.863 1.00144.00 C ANISOU 2477 CZ ARG A1119 17746 20421 16547 1535 1056 171 C ATOM 2478 NH1 ARG A1119 38.110 -15.708 -5.180 1.00130.30 N ANISOU 2478 NH1 ARG A1119 16019 18705 14784 1507 1123 144 N ATOM 2479 NH2 ARG A1119 38.078 -14.426 -3.281 1.00130.92 N ANISOU 2479 NH2 ARG A1119 15969 18860 14916 1345 1000 180 N ATOM 2480 N MET A1120 34.276 -14.730 1.549 1.00 78.73 N ANISOU 2480 N MET A1120 9882 11481 8550 1349 757 320 N ATOM 2481 CA MET A1120 34.389 -14.737 3.012 1.00 78.66 C ANISOU 2481 CA MET A1120 9848 11506 8532 1426 698 347 C ATOM 2482 C MET A1120 33.041 -15.002 3.686 1.00 80.97 C ANISOU 2482 C MET A1120 10348 11522 8895 1397 681 375 C ATOM 2483 O MET A1120 33.012 -15.594 4.765 1.00 80.79 O ANISOU 2483 O MET A1120 10385 11460 8853 1544 666 403 O ATOM 2484 CB MET A1120 34.953 -13.400 3.536 1.00 81.14 C ANISOU 2484 CB MET A1120 9966 12022 8842 1255 634 337 C ATOM 2485 CG MET A1120 36.345 -13.060 3.062 1.00 86.55 C ANISOU 2485 CG MET A1120 10419 13017 9450 1259 651 298 C ATOM 2486 SD MET A1120 37.623 -14.199 3.627 1.00 93.30 S ANISOU 2486 SD MET A1120 11149 14117 10184 1596 657 292 S ATOM 2487 CE MET A1120 39.067 -13.411 2.929 1.00 91.65 C ANISOU 2487 CE MET A1120 10638 14287 9900 1494 676 227 C ATOM 2488 N LEU A1121 31.933 -14.535 3.072 1.00 75.89 N ANISOU 2488 N LEU A1121 9806 10703 8324 1211 685 366 N ATOM 2489 CA LEU A1121 30.589 -14.716 3.620 1.00 74.50 C ANISOU 2489 CA LEU A1121 9808 10286 8214 1158 673 379 C ATOM 2490 C LEU A1121 30.125 -16.162 3.450 1.00 80.17 C ANISOU 2490 C LEU A1121 10714 10825 8923 1311 747 369 C ATOM 2491 O LEU A1121 29.460 -16.688 4.340 1.00 79.57 O ANISOU 2491 O LEU A1121 10772 10596 8867 1360 752 387 O ATOM 2492 CB LEU A1121 29.588 -13.736 2.989 1.00 73.01 C ANISOU 2492 CB LEU A1121 9650 10004 8087 930 651 367 C ATOM 2493 CG LEU A1121 29.775 -12.249 3.345 1.00 76.67 C ANISOU 2493 CG LEU A1121 9992 10574 8567 759 587 382 C ATOM 2494 CD1 LEU A1121 28.936 -11.356 2.448 1.00 75.32 C ANISOU 2494 CD1 LEU A1121 9865 10323 8431 577 586 374 C ATOM 2495 CD2 LEU A1121 29.485 -11.975 4.817 1.00 77.95 C ANISOU 2495 CD2 LEU A1121 10164 10701 8751 757 528 408 C ATOM 2496 N GLN A1122 30.507 -16.811 2.332 1.00 78.93 N ANISOU 2496 N GLN A1122 10576 10685 8730 1384 815 338 N ATOM 2497 CA GLN A1122 30.200 -18.219 2.058 1.00 80.12 C ANISOU 2497 CA GLN A1122 10915 10666 8859 1530 905 317 C ATOM 2498 C GLN A1122 30.954 -19.121 3.034 1.00 86.61 C ANISOU 2498 C GLN A1122 11777 11516 9616 1786 930 356 C ATOM 2499 O GLN A1122 30.357 -20.028 3.621 1.00 86.99 O ANISOU 2499 O GLN A1122 12022 11364 9666 1873 981 366 O ATOM 2500 CB GLN A1122 30.571 -18.581 0.614 1.00 82.14 C ANISOU 2500 CB GLN A1122 11163 10965 9081 1549 969 271 C ATOM 2501 CG GLN A1122 29.388 -18.587 -0.339 1.00 98.09 C ANISOU 2501 CG GLN A1122 13297 12826 11148 1383 996 218 C ATOM 2502 CD GLN A1122 29.747 -19.193 -1.674 1.00121.33 C ANISOU 2502 CD GLN A1122 16265 15790 14044 1436 1071 168 C ATOM 2503 OE1 GLN A1122 29.315 -20.299 -2.012 1.00118.61 O ANISOU 2503 OE1 GLN A1122 16095 15284 13686 1501 1153 123 O ATOM 2504 NE2 GLN A1122 30.547 -18.485 -2.465 1.00114.64 N ANISOU 2504 NE2 GLN A1122 15252 15140 13167 1401 1053 169 N ATOM 2505 N GLN A1123 32.260 -18.829 3.244 1.00 84.25 N ANISOU 2505 N GLN A1123 11286 11475 9251 1903 896 376 N ATOM 2506 CA GLN A1123 33.159 -19.553 4.152 1.00 85.42 C ANISOU 2506 CA GLN A1123 11423 11721 9311 2177 905 414 C ATOM 2507 C GLN A1123 32.818 -19.242 5.621 1.00 88.33 C ANISOU 2507 C GLN A1123 11807 12059 9694 2174 839 460 C ATOM 2508 O GLN A1123 33.411 -19.827 6.535 1.00 89.24 O ANISOU 2508 O GLN A1123 11935 12239 9731 2406 840 499 O ATOM 2509 CB GLN A1123 34.625 -19.216 3.835 1.00 87.82 C ANISOU 2509 CB GLN A1123 11477 12357 9534 2275 882 404 C ATOM 2510 CG GLN A1123 35.099 -19.801 2.502 1.00 97.45 C ANISOU 2510 CG GLN A1123 12703 13609 10713 2353 963 366 C ATOM 2511 CD GLN A1123 36.318 -19.119 1.927 1.00115.04 C ANISOU 2511 CD GLN A1123 14659 16165 12888 2336 939 339 C ATOM 2512 OE1 GLN A1123 36.904 -18.201 2.516 1.00112.52 O ANISOU 2512 OE1 GLN A1123 14130 16068 12553 2262 864 341 O ATOM 2513 NE2 GLN A1123 36.735 -19.565 0.754 1.00106.69 N ANISOU 2513 NE2 GLN A1123 13596 15146 11793 2396 1010 305 N ATOM 2514 N LYS A1124 31.834 -18.336 5.828 1.00 82.70 N ANISOU 2514 N LYS A1124 11101 11248 9073 1925 786 454 N ATOM 2515 CA LYS A1124 31.271 -17.900 7.108 1.00 81.79 C ANISOU 2515 CA LYS A1124 11013 11074 8990 1868 725 488 C ATOM 2516 C LYS A1124 32.346 -17.231 8.010 1.00 86.54 C ANISOU 2516 C LYS A1124 11399 11952 9529 1932 640 508 C ATOM 2517 O LYS A1124 32.311 -17.364 9.238 1.00 86.74 O ANISOU 2517 O LYS A1124 11457 11973 9527 2026 607 545 O ATOM 2518 CB LYS A1124 30.550 -19.076 7.812 1.00 84.75 C ANISOU 2518 CB LYS A1124 11645 11201 9358 2006 793 518 C ATOM 2519 CG LYS A1124 29.329 -19.577 7.031 1.00 96.41 C ANISOU 2519 CG LYS A1124 13318 12411 10901 1878 870 478 C ATOM 2520 CD LYS A1124 28.552 -20.661 7.766 1.00105.17 C ANISOU 2520 CD LYS A1124 14689 13265 12006 1966 951 497 C ATOM 2521 CE LYS A1124 27.235 -20.974 7.093 1.00113.88 C ANISOU 2521 CE LYS A1124 15954 14135 13179 1782 1017 438 C ATOM 2522 NZ LYS A1124 27.413 -21.715 5.813 1.00123.52 N ANISOU 2522 NZ LYS A1124 17244 15309 14378 1819 1105 384 N ATOM 2523 N ARG A1125 33.272 -16.475 7.376 1.00 83.26 N ANISOU 2523 N ARG A1125 10762 11784 9089 1861 610 475 N ATOM 2524 CA ARG A1125 34.364 -15.722 8.014 1.00 83.89 C ANISOU 2524 CA ARG A1125 10599 12169 9107 1869 537 465 C ATOM 2525 C ARG A1125 33.925 -14.257 8.132 1.00 86.47 C ANISOU 2525 C ARG A1125 10841 12508 9507 1568 474 445 C ATOM 2526 O ARG A1125 34.459 -13.377 7.450 1.00 86.52 O ANISOU 2526 O ARG A1125 10690 12671 9515 1411 466 407 O ATOM 2527 CB ARG A1125 35.683 -15.854 7.212 1.00 84.82 C ANISOU 2527 CB ARG A1125 10528 12557 9141 1969 562 430 C ATOM 2528 CG ARG A1125 36.027 -17.264 6.727 1.00 94.22 C ANISOU 2528 CG ARG A1125 11831 13703 10267 2249 646 444 C ATOM 2529 CD ARG A1125 37.452 -17.677 7.051 1.00105.06 C ANISOU 2529 CD ARG A1125 13021 15393 11504 2509 636 439 C ATOM 2530 NE ARG A1125 38.456 -16.780 6.470 1.00111.71 N ANISOU 2530 NE ARG A1125 13579 16552 12315 2383 610 380 N ATOM 2531 CZ ARG A1125 39.084 -16.988 5.318 1.00122.84 C ANISOU 2531 CZ ARG A1125 14909 18074 13691 2414 668 346 C ATOM 2532 NH1 ARG A1125 39.991 -16.123 4.886 1.00111.68 N ANISOU 2532 NH1 ARG A1125 13234 16955 12245 2279 650 290 N ATOM 2533 NH2 ARG A1125 38.814 -18.064 4.589 1.00105.85 N ANISOU 2533 NH2 ARG A1125 12943 15741 11534 2572 753 362 N ATOM 2534 N TRP A1126 32.919 -14.016 8.985 1.00 81.15 N ANISOU 2534 N TRP A1126 10290 11654 8891 1491 440 472 N ATOM 2535 CA TRP A1126 32.249 -12.731 9.187 1.00 79.31 C ANISOU 2535 CA TRP A1126 10038 11367 8731 1229 389 461 C ATOM 2536 C TRP A1126 33.191 -11.552 9.465 1.00 84.46 C ANISOU 2536 C TRP A1126 10464 12281 9347 1098 334 425 C ATOM 2537 O TRP A1126 33.090 -10.546 8.758 1.00 83.48 O ANISOU 2537 O TRP A1126 10294 12162 9263 881 340 399 O ATOM 2538 CB TRP A1126 31.198 -12.829 10.301 1.00 76.77 C ANISOU 2538 CB TRP A1126 9866 10852 8450 1228 361 496 C ATOM 2539 CG TRP A1126 30.417 -14.111 10.307 1.00 77.32 C ANISOU 2539 CG TRP A1126 10155 10690 8535 1372 424 525 C ATOM 2540 CD1 TRP A1126 30.372 -15.032 11.310 1.00 80.85 C ANISOU 2540 CD1 TRP A1126 10709 11073 8936 1568 438 564 C ATOM 2541 CD2 TRP A1126 29.620 -14.643 9.238 1.00 76.50 C ANISOU 2541 CD2 TRP A1126 10192 10393 8480 1329 494 511 C ATOM 2542 NE1 TRP A1126 29.582 -16.095 10.944 1.00 80.12 N ANISOU 2542 NE1 TRP A1126 10832 10743 8869 1634 523 574 N ATOM 2543 CE2 TRP A1126 29.108 -15.883 9.676 1.00 80.76 C ANISOU 2543 CE2 TRP A1126 10928 10750 9009 1484 555 534 C ATOM 2544 CE3 TRP A1126 29.283 -14.190 7.951 1.00 76.92 C ANISOU 2544 CE3 TRP A1126 10232 10414 8578 1174 515 476 C ATOM 2545 CZ2 TRP A1126 28.246 -16.656 8.890 1.00 79.71 C ANISOU 2545 CZ2 TRP A1126 10969 10405 8913 1462 636 512 C ATOM 2546 CZ3 TRP A1126 28.469 -14.980 7.156 1.00 77.94 C ANISOU 2546 CZ3 TRP A1126 10519 10356 8737 1176 585 458 C ATOM 2547 CH2 TRP A1126 27.959 -16.196 7.625 1.00 78.89 C ANISOU 2547 CH2 TRP A1126 10824 10300 8850 1308 645 469 C ATOM 2548 N ASP A1127 34.094 -11.663 10.459 1.00 82.79 N ANISOU 2548 N ASP A1127 10118 12286 9052 1225 288 417 N ATOM 2549 CA ASP A1127 35.013 -10.577 10.826 1.00 83.56 C ANISOU 2549 CA ASP A1127 9989 12654 9104 1086 239 364 C ATOM 2550 C ASP A1127 36.033 -10.283 9.710 1.00 87.43 C ANISOU 2550 C ASP A1127 10305 13359 9555 1020 280 313 C ATOM 2551 O ASP A1127 36.404 -9.122 9.520 1.00 86.84 O ANISOU 2551 O ASP A1127 10106 13403 9485 787 274 263 O ATOM 2552 CB ASP A1127 35.712 -10.876 12.158 1.00 87.10 C ANISOU 2552 CB ASP A1127 10330 13309 9457 1259 177 360 C ATOM 2553 CG ASP A1127 34.747 -10.870 13.331 1.00 99.31 C ANISOU 2553 CG ASP A1127 12029 14666 11039 1268 133 402 C ATOM 2554 OD1 ASP A1127 33.971 -11.842 13.467 1.00 99.97 O ANISOU 2554 OD1 ASP A1127 12314 14522 11147 1421 166 462 O ATOM 2555 OD2 ASP A1127 34.735 -9.874 14.085 1.00105.71 O ANISOU 2555 OD2 ASP A1127 12766 15547 11854 1108 77 372 O ATOM 2556 N GLU A1128 36.432 -11.316 8.943 1.00 84.38 N ANISOU 2556 N GLU A1128 9928 13001 9131 1213 334 323 N ATOM 2557 CA GLU A1128 37.350 -11.171 7.813 1.00 85.13 C ANISOU 2557 CA GLU A1128 9871 13288 9186 1173 384 278 C ATOM 2558 C GLU A1128 36.634 -10.537 6.613 1.00 87.81 C ANISOU 2558 C GLU A1128 10314 13437 9612 947 435 280 C ATOM 2559 O GLU A1128 37.279 -9.868 5.807 1.00 87.84 O ANISOU 2559 O GLU A1128 10189 13590 9597 800 471 238 O ATOM 2560 CB GLU A1128 37.969 -12.519 7.435 1.00 87.79 C ANISOU 2560 CB GLU A1128 10203 13708 9447 1477 427 291 C ATOM 2561 CG GLU A1128 39.158 -12.863 8.311 1.00100.41 C ANISOU 2561 CG GLU A1128 11600 15634 10919 1685 384 267 C ATOM 2562 CD GLU A1128 39.741 -14.239 8.075 1.00120.70 C ANISOU 2562 CD GLU A1128 14189 18274 13398 2032 427 289 C ATOM 2563 OE1 GLU A1128 39.210 -15.211 8.660 1.00121.03 O ANISOU 2563 OE1 GLU A1128 14426 18128 13431 2251 433 351 O ATOM 2564 OE2 GLU A1128 40.731 -14.347 7.316 1.00110.56 O ANISOU 2564 OE2 GLU A1128 12734 17230 12045 2087 463 246 O ATOM 2565 N ALA A1129 35.303 -10.738 6.505 1.00 83.07 N ANISOU 2565 N ALA A1129 9944 12522 9098 920 441 325 N ATOM 2566 CA ALA A1129 34.471 -10.138 5.459 1.00 81.63 C ANISOU 2566 CA ALA A1129 9873 12156 8988 729 478 331 C ATOM 2567 C ALA A1129 34.289 -8.644 5.745 1.00 85.80 C ANISOU 2567 C ALA A1129 10362 12689 9547 466 449 317 C ATOM 2568 O ALA A1129 34.372 -7.824 4.829 1.00 85.32 O ANISOU 2568 O ALA A1129 10285 12639 9495 290 490 302 O ATOM 2569 CB ALA A1129 33.116 -10.835 5.398 1.00 80.79 C ANISOU 2569 CB ALA A1129 9999 11751 8948 789 487 370 C ATOM 2570 N ALA A1130 34.091 -8.307 7.038 1.00 82.74 N ANISOU 2570 N ALA A1130 9971 12299 9167 448 386 321 N ATOM 2571 CA ALA A1130 33.874 -6.964 7.575 1.00 82.42 C ANISOU 2571 CA ALA A1130 9917 12246 9151 221 356 305 C ATOM 2572 C ALA A1130 34.995 -5.979 7.217 1.00 88.36 C ANISOU 2572 C ALA A1130 10488 13232 9853 38 385 245 C ATOM 2573 O ALA A1130 34.689 -4.867 6.782 1.00 87.77 O ANISOU 2573 O ALA A1130 10468 13072 9807 -183 416 240 O ATOM 2574 CB ALA A1130 33.725 -7.038 9.081 1.00 83.06 C ANISOU 2574 CB ALA A1130 9995 12339 9225 286 284 311 C ATOM 2575 N VAL A1131 36.279 -6.380 7.400 1.00 86.66 N ANISOU 2575 N VAL A1131 10062 13312 9553 132 382 198 N ATOM 2576 CA VAL A1131 37.453 -5.537 7.112 1.00 87.95 C ANISOU 2576 CA VAL A1131 10021 13743 9654 -46 417 122 C ATOM 2577 C VAL A1131 37.535 -5.205 5.609 1.00 91.95 C ANISOU 2577 C VAL A1131 10557 14207 10172 -167 508 123 C ATOM 2578 O VAL A1131 37.851 -4.066 5.263 1.00 91.90 O ANISOU 2578 O VAL A1131 10513 14247 10157 -418 557 85 O ATOM 2579 CB VAL A1131 38.804 -6.103 7.643 1.00 93.61 C ANISOU 2579 CB VAL A1131 10479 14824 10262 104 390 62 C ATOM 2580 CG1 VAL A1131 38.928 -5.917 9.150 1.00 93.68 C ANISOU 2580 CG1 VAL A1131 10416 14939 10238 127 305 36 C ATOM 2581 CG2 VAL A1131 39.022 -7.564 7.253 1.00 93.73 C ANISOU 2581 CG2 VAL A1131 10498 14872 10244 418 399 98 C ATOM 2582 N ASN A1132 37.223 -6.181 4.732 1.00 88.50 N ANISOU 2582 N ASN A1132 10207 13671 9750 4 538 165 N ATOM 2583 CA ASN A1132 37.230 -5.987 3.279 1.00 88.67 C ANISOU 2583 CA ASN A1132 10271 13645 9775 -80 621 172 C ATOM 2584 C ASN A1132 36.102 -5.046 2.870 1.00 90.88 C ANISOU 2584 C ASN A1132 10753 13655 10122 -266 640 213 C ATOM 2585 O ASN A1132 36.296 -4.198 1.994 1.00 91.00 O ANISOU 2585 O ASN A1132 10779 13674 10123 -447 710 204 O ATOM 2586 CB ASN A1132 37.112 -7.324 2.539 1.00 90.47 C ANISOU 2586 CB ASN A1132 10552 13826 9996 160 643 199 C ATOM 2587 CG ASN A1132 38.352 -8.179 2.598 1.00120.48 C ANISOU 2587 CG ASN A1132 14156 17910 13710 350 651 160 C ATOM 2588 OD1 ASN A1132 38.318 -9.322 3.063 1.00118.46 O ANISOU 2588 OD1 ASN A1132 13927 17643 13437 603 621 180 O ATOM 2589 ND2 ASN A1132 39.470 -7.663 2.097 1.00113.73 N ANISOU 2589 ND2 ASN A1132 13107 17315 12791 238 701 102 N ATOM 2590 N LEU A1133 34.935 -5.183 3.532 1.00 85.17 N ANISOU 2590 N LEU A1133 10192 12707 9463 -214 581 257 N ATOM 2591 CA LEU A1133 33.764 -4.343 3.305 1.00 83.30 C ANISOU 2591 CA LEU A1133 10145 12223 9282 -349 585 298 C ATOM 2592 C LEU A1133 34.034 -2.930 3.826 1.00 87.93 C ANISOU 2592 C LEU A1133 10709 12843 9859 -585 596 272 C ATOM 2593 O LEU A1133 33.503 -1.971 3.266 1.00 87.37 O ANISOU 2593 O LEU A1133 10767 12628 9800 -738 640 295 O ATOM 2594 CB LEU A1133 32.510 -4.951 3.955 1.00 81.57 C ANISOU 2594 CB LEU A1133 10076 11792 9123 -221 522 340 C ATOM 2595 CG LEU A1133 31.898 -6.169 3.250 1.00 85.04 C ANISOU 2595 CG LEU A1133 10609 12121 9582 -45 534 363 C ATOM 2596 CD1 LEU A1133 31.078 -6.998 4.213 1.00 84.02 C ANISOU 2596 CD1 LEU A1133 10570 11860 9493 96 479 383 C ATOM 2597 CD2 LEU A1133 31.061 -5.759 2.045 1.00 86.46 C ANISOU 2597 CD2 LEU A1133 10922 12150 9778 -124 574 386 C ATOM 2598 N ALA A1134 34.889 -2.800 4.871 1.00 85.34 N ANISOU 2598 N ALA A1134 10218 12711 9496 -613 561 219 N ATOM 2599 CA ALA A1134 35.309 -1.511 5.425 1.00 85.98 C ANISOU 2599 CA ALA A1134 10255 12857 9556 -853 578 170 C ATOM 2600 C ALA A1134 36.272 -0.834 4.451 1.00 91.91 C ANISOU 2600 C ALA A1134 10916 13754 10253 -1039 680 125 C ATOM 2601 O ALA A1134 36.209 0.384 4.272 1.00 91.97 O ANISOU 2601 O ALA A1134 11007 13681 10255 -1273 742 114 O ATOM 2602 CB ALA A1134 35.968 -1.704 6.782 1.00 87.43 C ANISOU 2602 CB ALA A1134 10273 13242 9705 -812 508 115 C ATOM 2603 N LYS A1135 37.133 -1.645 3.788 1.00 89.66 N ANISOU 2603 N LYS A1135 10476 13669 9921 -929 707 102 N ATOM 2604 CA LYS A1135 38.106 -1.212 2.779 1.00 91.08 C ANISOU 2604 CA LYS A1135 10549 14016 10042 -1076 810 57 C ATOM 2605 C LYS A1135 37.393 -1.078 1.421 1.00 94.60 C ANISOU 2605 C LYS A1135 11188 14245 10512 -1090 878 125 C ATOM 2606 O LYS A1135 37.677 -1.835 0.485 1.00 94.78 O ANISOU 2606 O LYS A1135 11168 14334 10512 -969 911 135 O ATOM 2607 CB LYS A1135 39.288 -2.207 2.701 1.00 94.77 C ANISOU 2607 CB LYS A1135 10764 14803 10442 -917 803 3 C ATOM 2608 CG LYS A1135 40.329 -2.064 3.815 1.00107.70 C ANISOU 2608 CG LYS A1135 12157 16747 12016 -959 761 -90 C ATOM 2609 CD LYS A1135 41.272 -3.277 3.885 1.00117.71 C ANISOU 2609 CD LYS A1135 13202 18309 13214 -705 729 -123 C ATOM 2610 CE LYS A1135 42.408 -3.246 2.880 1.00129.40 C ANISOU 2610 CE LYS A1135 14497 20050 14620 -773 822 -184 C ATOM 2611 NZ LYS A1135 43.191 -4.511 2.892 1.00137.44 N ANISOU 2611 NZ LYS A1135 15329 21325 15568 -476 790 -203 N ATOM 2612 N SER A1136 36.438 -0.128 1.329 1.00 90.14 N ANISOU 2612 N SER A1136 10840 13425 9984 -1221 899 173 N ATOM 2613 CA SER A1136 35.649 0.106 0.116 1.00 89.16 C ANISOU 2613 CA SER A1136 10913 13094 9868 -1225 955 242 C ATOM 2614 C SER A1136 35.183 1.567 -0.011 1.00 92.72 C ANISOU 2614 C SER A1136 11554 13363 10314 -1447 1023 268 C ATOM 2615 O SER A1136 35.204 2.318 0.968 1.00 92.21 O ANISOU 2615 O SER A1136 11501 13276 10258 -1579 1009 239 O ATOM 2616 CB SER A1136 34.436 -0.824 0.086 1.00 90.83 C ANISOU 2616 CB SER A1136 11251 13123 10137 -996 875 303 C ATOM 2617 OG SER A1136 33.455 -0.456 1.043 1.00 97.69 O ANISOU 2617 OG SER A1136 12242 13816 11058 -998 808 331 O ATOM 2618 N ARG A1137 34.745 1.948 -1.228 1.00 89.39 N ANISOU 2618 N ARG A1137 11291 12804 9868 -1473 1098 323 N ATOM 2619 CA ARG A1137 34.215 3.277 -1.550 1.00 89.63 C ANISOU 2619 CA ARG A1137 11546 12633 9877 -1639 1176 367 C ATOM 2620 C ARG A1137 32.807 3.441 -0.957 1.00 92.28 C ANISOU 2620 C ARG A1137 12065 12733 10266 -1539 1093 426 C ATOM 2621 O ARG A1137 32.403 4.562 -0.636 1.00 92.05 O ANISOU 2621 O ARG A1137 12199 12550 10228 -1667 1131 446 O ATOM 2622 CB ARG A1137 34.184 3.510 -3.075 1.00 90.48 C ANISOU 2622 CB ARG A1137 11765 12686 9925 -1655 1279 416 C ATOM 2623 CG ARG A1137 35.519 3.271 -3.779 1.00103.51 C ANISOU 2623 CG ARG A1137 13236 14575 11520 -1739 1367 361 C ATOM 2624 CD ARG A1137 35.545 3.831 -5.187 1.00114.41 C ANISOU 2624 CD ARG A1137 14759 15884 12829 -1813 1494 409 C ATOM 2625 NE ARG A1137 35.974 5.231 -5.202 1.00124.49 N ANISOU 2625 NE ARG A1137 16148 17100 14054 -2088 1626 400 N ATOM 2626 CZ ARG A1137 36.205 5.937 -6.304 1.00139.03 C ANISOU 2626 CZ ARG A1137 18123 18884 15817 -2209 1769 435 C ATOM 2627 NH1 ARG A1137 36.592 7.203 -6.217 1.00126.02 N ANISOU 2627 NH1 ARG A1137 16597 17162 14122 -2471 1901 422 N ATOM 2628 NH2 ARG A1137 36.053 5.384 -7.502 1.00126.88 N ANISOU 2628 NH2 ARG A1137 16610 17357 14241 -2073 1790 481 N ATOM 2629 N TRP A1138 32.067 2.312 -0.822 1.00 87.45 N ANISOU 2629 N TRP A1138 11431 12093 9703 -1312 989 448 N ATOM 2630 CA TRP A1138 30.711 2.225 -0.270 1.00 85.47 C ANISOU 2630 CA TRP A1138 11316 11655 9503 -1194 903 492 C ATOM 2631 C TRP A1138 30.709 2.610 1.214 1.00 91.13 C ANISOU 2631 C TRP A1138 12006 12363 10258 -1260 849 461 C ATOM 2632 O TRP A1138 29.785 3.289 1.673 1.00 90.09 O ANISOU 2632 O TRP A1138 12031 12056 10144 -1275 829 495 O ATOM 2633 CB TRP A1138 30.146 0.804 -0.471 1.00 82.36 C ANISOU 2633 CB TRP A1138 10874 11273 9147 -968 825 499 C ATOM 2634 CG TRP A1138 28.966 0.462 0.396 1.00 81.52 C ANISOU 2634 CG TRP A1138 10840 11036 9099 -855 730 517 C ATOM 2635 CD1 TRP A1138 27.745 1.073 0.403 1.00 83.67 C ANISOU 2635 CD1 TRP A1138 11285 11127 9377 -841 711 562 C ATOM 2636 CD2 TRP A1138 28.897 -0.587 1.371 1.00 80.35 C ANISOU 2636 CD2 TRP A1138 10595 10934 9002 -733 648 490 C ATOM 2637 NE1 TRP A1138 26.923 0.476 1.331 1.00 81.71 N ANISOU 2637 NE1 TRP A1138 11040 10820 9187 -734 623 558 N ATOM 2638 CE2 TRP A1138 27.600 -0.552 1.932 1.00 82.86 C ANISOU 2638 CE2 TRP A1138 11031 11090 9360 -670 588 517 C ATOM 2639 CE3 TRP A1138 29.801 -1.564 1.817 1.00 81.77 C ANISOU 2639 CE3 TRP A1138 10604 11277 9186 -656 626 448 C ATOM 2640 CZ2 TRP A1138 27.183 -1.466 2.905 1.00 81.13 C ANISOU 2640 CZ2 TRP A1138 10776 10858 9192 -554 514 503 C ATOM 2641 CZ3 TRP A1138 29.392 -2.455 2.796 1.00 82.29 C ANISOU 2641 CZ3 TRP A1138 10648 11322 9297 -523 552 442 C ATOM 2642 CH2 TRP A1138 28.100 -2.397 3.335 1.00 81.68 C ANISOU 2642 CH2 TRP A1138 10700 11070 9264 -484 501 470 C ATOM 2643 N TYR A1139 31.742 2.174 1.953 1.00 89.66 N ANISOU 2643 N TYR A1139 11617 12376 10075 -1286 825 395 N ATOM 2644 CA TYR A1139 31.898 2.475 3.371 1.00 90.26 C ANISOU 2644 CA TYR A1139 11637 12486 10172 -1347 772 353 C ATOM 2645 C TYR A1139 32.208 3.962 3.570 1.00 95.92 C ANISOU 2645 C TYR A1139 12441 13150 10854 -1601 854 329 C ATOM 2646 O TYR A1139 31.716 4.559 4.523 1.00 95.19 O ANISOU 2646 O TYR A1139 12434 12951 10782 -1653 822 326 O ATOM 2647 CB TYR A1139 32.997 1.595 3.994 1.00 92.57 C ANISOU 2647 CB TYR A1139 11679 13042 10453 -1289 728 286 C ATOM 2648 CG TYR A1139 33.174 1.791 5.486 1.00 95.26 C ANISOU 2648 CG TYR A1139 11945 13446 10803 -1327 662 240 C ATOM 2649 CD1 TYR A1139 32.347 1.138 6.397 1.00 96.05 C ANISOU 2649 CD1 TYR A1139 12084 13457 10952 -1160 564 268 C ATOM 2650 CD2 TYR A1139 34.183 2.607 5.988 1.00 97.81 C ANISOU 2650 CD2 TYR A1139 12156 13930 11080 -1536 701 159 C ATOM 2651 CE1 TYR A1139 32.508 1.311 7.772 1.00 97.33 C ANISOU 2651 CE1 TYR A1139 12183 13683 11114 -1185 502 228 C ATOM 2652 CE2 TYR A1139 34.352 2.790 7.360 1.00 99.11 C ANISOU 2652 CE2 TYR A1139 12247 14169 11243 -1571 636 108 C ATOM 2653 CZ TYR A1139 33.515 2.135 8.250 1.00105.11 C ANISOU 2653 CZ TYR A1139 13053 14835 12049 -1386 534 147 C ATOM 2654 OH TYR A1139 33.684 2.305 9.604 1.00105.64 O ANISOU 2654 OH TYR A1139 13051 14982 12106 -1411 470 98 O ATOM 2655 N ASN A1140 33.016 4.553 2.672 1.00 94.39 N ANISOU 2655 N ASN A1140 12239 13023 10603 -1764 969 309 N ATOM 2656 CA ASN A1140 33.404 5.961 2.741 1.00 95.92 C ANISOU 2656 CA ASN A1140 12534 13157 10752 -2031 1077 279 C ATOM 2657 C ASN A1140 32.209 6.879 2.442 1.00 99.53 C ANISOU 2657 C ASN A1140 13297 13311 11210 -2035 1116 363 C ATOM 2658 O ASN A1140 31.971 7.827 3.195 1.00 99.36 O ANISOU 2658 O ASN A1140 13396 13169 11185 -2162 1137 349 O ATOM 2659 CB ASN A1140 34.567 6.251 1.778 1.00 99.09 C ANISOU 2659 CB ASN A1140 12851 13712 11088 -2199 1204 238 C ATOM 2660 CG ASN A1140 35.841 5.479 2.061 1.00122.76 C ANISOU 2660 CG ASN A1140 15534 17042 14066 -2206 1179 145 C ATOM 2661 OD1 ASN A1140 36.195 5.187 3.213 1.00115.75 O ANISOU 2661 OD1 ASN A1140 14488 16300 13193 -2193 1097 80 O ATOM 2662 ND2 ASN A1140 36.587 5.166 1.009 1.00115.96 N ANISOU 2662 ND2 ASN A1140 14575 16324 13161 -2221 1252 133 N ATOM 2663 N GLN A1141 31.449 6.571 1.368 1.00 95.51 N ANISOU 2663 N GLN A1141 12907 12687 10694 -1883 1121 446 N ATOM 2664 CA GLN A1141 30.285 7.337 0.917 1.00 95.10 C ANISOU 2664 CA GLN A1141 13134 12379 10623 -1836 1152 532 C ATOM 2665 C GLN A1141 29.121 7.297 1.926 1.00 97.44 C ANISOU 2665 C GLN A1141 13510 12540 10973 -1710 1045 557 C ATOM 2666 O GLN A1141 28.552 8.350 2.225 1.00 96.93 O ANISOU 2666 O GLN A1141 13649 12293 10887 -1771 1084 586 O ATOM 2667 CB GLN A1141 29.820 6.845 -0.460 1.00 96.26 C ANISOU 2667 CB GLN A1141 13340 12496 10739 -1683 1166 599 C ATOM 2668 CG GLN A1141 30.612 7.467 -1.613 1.00119.44 C ANISOU 2668 CG GLN A1141 16335 15452 13593 -1831 1315 609 C ATOM 2669 CD GLN A1141 30.204 6.972 -2.985 1.00141.70 C ANISOU 2669 CD GLN A1141 19207 18261 16372 -1678 1329 671 C ATOM 2670 OE1 GLN A1141 29.017 6.825 -3.308 1.00136.86 O ANISOU 2670 OE1 GLN A1141 18720 17525 15755 -1498 1271 734 O ATOM 2671 NE2 GLN A1141 31.188 6.763 -3.849 1.00134.81 N ANISOU 2671 NE2 GLN A1141 18237 17529 15455 -1753 1411 648 N ATOM 2672 N THR A1142 28.774 6.100 2.447 1.00 92.91 N ANISOU 2672 N THR A1142 12791 12050 10462 -1535 920 544 N ATOM 2673 CA THR A1142 27.694 5.930 3.426 1.00 91.50 C ANISOU 2673 CA THR A1142 12666 11766 10336 -1415 820 561 C ATOM 2674 C THR A1142 28.249 5.175 4.652 1.00 95.88 C ANISOU 2674 C THR A1142 13018 12474 10940 -1404 737 495 C ATOM 2675 O THR A1142 28.049 3.965 4.761 1.00 94.48 O ANISOU 2675 O THR A1142 12729 12369 10801 -1240 659 494 O ATOM 2676 CB THR A1142 26.472 5.245 2.789 1.00 96.30 C ANISOU 2676 CB THR A1142 13341 12292 10957 -1200 762 619 C ATOM 2677 OG1 THR A1142 26.902 4.137 1.998 1.00 94.42 O ANISOU 2677 OG1 THR A1142 12966 12188 10722 -1115 753 607 O ATOM 2678 CG2 THR A1142 25.648 6.197 1.940 1.00 95.65 C ANISOU 2678 CG2 THR A1142 13489 12038 10814 -1183 823 689 C ATOM 2679 N PRO A1143 28.961 5.866 5.578 1.00 93.98 N ANISOU 2679 N PRO A1143 12734 12286 10688 -1576 757 436 N ATOM 2680 CA PRO A1143 29.560 5.155 6.724 1.00 93.62 C ANISOU 2680 CA PRO A1143 12486 12416 10669 -1551 676 372 C ATOM 2681 C PRO A1143 28.567 4.716 7.797 1.00 95.41 C ANISOU 2681 C PRO A1143 12747 12557 10949 -1406 571 392 C ATOM 2682 O PRO A1143 28.733 3.616 8.320 1.00 94.24 O ANISOU 2682 O PRO A1143 12455 12525 10825 -1274 495 376 O ATOM 2683 CB PRO A1143 30.574 6.155 7.281 1.00 97.18 C ANISOU 2683 CB PRO A1143 12891 12955 11077 -1799 738 293 C ATOM 2684 CG PRO A1143 30.063 7.485 6.874 1.00102.32 C ANISOU 2684 CG PRO A1143 13792 13384 11701 -1935 835 328 C ATOM 2685 CD PRO A1143 29.316 7.302 5.586 1.00 97.19 C ANISOU 2685 CD PRO A1143 13276 12607 11046 -1805 864 417 C ATOM 2686 N ASN A1144 27.557 5.550 8.134 1.00 91.26 N ANISOU 2686 N ASN A1144 12415 11830 10432 -1423 573 427 N ATOM 2687 CA ASN A1144 26.567 5.200 9.160 1.00 89.70 C ANISOU 2687 CA ASN A1144 12252 11549 10279 -1296 482 443 C ATOM 2688 C ASN A1144 25.688 4.020 8.698 1.00 90.21 C ANISOU 2688 C ASN A1144 12307 11585 10382 -1082 426 490 C ATOM 2689 O ASN A1144 25.303 3.196 9.527 1.00 89.34 O ANISOU 2689 O ASN A1144 12139 11495 10310 -967 351 485 O ATOM 2690 CB ASN A1144 25.711 6.411 9.583 1.00 92.87 C ANISOU 2690 CB ASN A1144 12863 11753 10672 -1358 507 465 C ATOM 2691 CG ASN A1144 24.991 7.124 8.460 1.00128.72 C ANISOU 2691 CG ASN A1144 17603 16127 15179 -1342 576 530 C ATOM 2692 OD1 ASN A1144 23.801 6.898 8.209 1.00125.79 O ANISOU 2692 OD1 ASN A1144 17322 15652 14821 -1186 538 583 O ATOM 2693 ND2 ASN A1144 25.683 8.043 7.795 1.00123.23 N ANISOU 2693 ND2 ASN A1144 16985 15408 14430 -1505 684 525 N ATOM 2694 N ARG A1145 25.425 3.910 7.382 1.00 84.56 N ANISOU 2694 N ARG A1145 11648 10831 9650 -1037 468 528 N ATOM 2695 CA ARG A1145 24.629 2.821 6.820 1.00 82.03 C ANISOU 2695 CA ARG A1145 11319 10494 9356 -861 426 556 C ATOM 2696 C ARG A1145 25.466 1.547 6.684 1.00 83.73 C ANISOU 2696 C ARG A1145 11360 10870 9584 -791 408 526 C ATOM 2697 O ARG A1145 24.992 0.481 7.079 1.00 82.49 O ANISOU 2697 O ARG A1145 11164 10714 9463 -658 353 524 O ATOM 2698 CB ARG A1145 24.029 3.216 5.461 1.00 81.06 C ANISOU 2698 CB ARG A1145 11320 10284 9193 -834 476 602 C ATOM 2699 CG ARG A1145 23.002 2.213 4.942 1.00 82.65 C ANISOU 2699 CG ARG A1145 11525 10463 9414 -667 430 617 C ATOM 2700 CD ARG A1145 22.832 2.305 3.447 1.00 79.29 C ANISOU 2700 CD ARG A1145 11158 10032 8937 -637 478 644 C ATOM 2701 NE ARG A1145 21.774 1.417 2.970 1.00 75.38 N ANISOU 2701 NE ARG A1145 10665 9525 8450 -494 433 642 N ATOM 2702 CZ ARG A1145 20.779 1.809 2.184 1.00 89.48 C ANISOU 2702 CZ ARG A1145 12558 11252 10188 -429 437 671 C ATOM 2703 NH1 ARG A1145 20.699 3.069 1.779 1.00 80.79 N ANISOU 2703 NH1 ARG A1145 11594 10078 9026 -472 487 718 N ATOM 2704 NH2 ARG A1145 19.857 0.940 1.790 1.00 75.18 N ANISOU 2704 NH2 ARG A1145 10724 9459 8380 -317 395 649 N ATOM 2705 N ALA A1146 26.693 1.654 6.119 1.00 79.56 N ANISOU 2705 N ALA A1146 10735 10475 9019 -878 463 501 N ATOM 2706 CA ALA A1146 27.598 0.521 5.907 1.00 78.99 C ANISOU 2706 CA ALA A1146 10495 10572 8944 -801 456 471 C ATOM 2707 C ALA A1146 27.977 -0.183 7.208 1.00 81.57 C ANISOU 2707 C ALA A1146 10705 10998 9291 -731 389 440 C ATOM 2708 O ALA A1146 27.921 -1.413 7.244 1.00 80.58 O ANISOU 2708 O ALA A1146 10527 10908 9181 -573 359 442 O ATOM 2709 CB ALA A1146 28.854 0.965 5.178 1.00 81.10 C ANISOU 2709 CB ALA A1146 10675 10981 9160 -929 532 443 C ATOM 2710 N LYS A1147 28.327 0.583 8.277 1.00 77.98 N ANISOU 2710 N LYS A1147 10224 10578 8826 -841 372 410 N ATOM 2711 CA LYS A1147 28.706 0.027 9.586 1.00 77.55 C ANISOU 2711 CA LYS A1147 10060 10631 8773 -773 306 380 C ATOM 2712 C LYS A1147 27.583 -0.871 10.152 1.00 77.61 C ANISOU 2712 C LYS A1147 10149 10512 8829 -601 247 418 C ATOM 2713 O LYS A1147 27.885 -1.945 10.674 1.00 76.51 O ANISOU 2713 O LYS A1147 9928 10455 8686 -460 212 413 O ATOM 2714 CB LYS A1147 29.126 1.123 10.598 1.00 81.49 C ANISOU 2714 CB LYS A1147 10539 11175 9249 -939 299 334 C ATOM 2715 CG LYS A1147 28.008 2.046 11.111 1.00101.65 C ANISOU 2715 CG LYS A1147 13273 13519 11831 -1002 290 359 C ATOM 2716 CD LYS A1147 28.402 2.820 12.373 1.00113.37 C ANISOU 2716 CD LYS A1147 14726 15058 13292 -1126 267 304 C ATOM 2717 CE LYS A1147 28.216 2.030 13.653 1.00122.72 C ANISOU 2717 CE LYS A1147 15848 16294 14487 -988 180 300 C ATOM 2718 NZ LYS A1147 26.779 1.848 14.003 1.00127.68 N ANISOU 2718 NZ LYS A1147 16632 16715 15167 -881 146 356 N ATOM 2719 N ARG A1148 26.302 -0.465 9.974 1.00 71.98 N ANISOU 2719 N ARG A1148 9596 9603 8151 -606 246 455 N ATOM 2720 CA ARG A1148 25.128 -1.225 10.411 1.00 70.15 C ANISOU 2720 CA ARG A1148 9444 9250 7962 -474 205 482 C ATOM 2721 C ARG A1148 25.009 -2.547 9.646 1.00 73.32 C ANISOU 2721 C ARG A1148 9826 9659 8374 -336 217 490 C ATOM 2722 O ARG A1148 24.783 -3.584 10.269 1.00 72.63 O ANISOU 2722 O ARG A1148 9732 9561 8302 -215 193 492 O ATOM 2723 CB ARG A1148 23.838 -0.408 10.241 1.00 68.27 C ANISOU 2723 CB ARG A1148 9359 8838 7743 -514 207 509 C ATOM 2724 CG ARG A1148 23.634 0.674 11.292 1.00 74.28 C ANISOU 2724 CG ARG A1148 10177 9546 8502 -608 188 503 C ATOM 2725 CD ARG A1148 22.184 1.136 11.379 1.00 77.79 C ANISOU 2725 CD ARG A1148 10767 9826 8965 -579 176 532 C ATOM 2726 NE ARG A1148 21.703 1.766 10.144 1.00 81.83 N ANISOU 2726 NE ARG A1148 11374 10264 9454 -600 220 559 N ATOM 2727 CZ ARG A1148 21.802 3.064 9.866 1.00 96.73 C ANISOU 2727 CZ ARG A1148 13359 12091 11305 -706 265 572 C ATOM 2728 NH1 ARG A1148 21.334 3.538 8.721 1.00 86.59 N ANISOU 2728 NH1 ARG A1148 12172 10741 9987 -693 307 606 N ATOM 2729 NH2 ARG A1148 22.375 3.894 10.728 1.00 84.45 N ANISOU 2729 NH2 ARG A1148 11813 10538 9738 -824 274 549 N ATOM 2730 N VAL A1149 25.187 -2.512 8.309 1.00 69.83 N ANISOU 2730 N VAL A1149 9385 9230 7914 -357 265 494 N ATOM 2731 CA VAL A1149 25.094 -3.692 7.437 1.00 69.48 C ANISOU 2731 CA VAL A1149 9334 9192 7874 -242 287 492 C ATOM 2732 C VAL A1149 26.265 -4.647 7.738 1.00 73.48 C ANISOU 2732 C VAL A1149 9716 9847 8358 -149 289 473 C ATOM 2733 O VAL A1149 26.053 -5.858 7.835 1.00 72.83 O ANISOU 2733 O VAL A1149 9650 9736 8284 -12 289 473 O ATOM 2734 CB VAL A1149 25.012 -3.311 5.931 1.00 73.62 C ANISOU 2734 CB VAL A1149 9893 9705 8374 -290 336 499 C ATOM 2735 CG1 VAL A1149 24.814 -4.544 5.051 1.00 73.25 C ANISOU 2735 CG1 VAL A1149 9849 9656 8327 -176 358 487 C ATOM 2736 CG2 VAL A1149 23.890 -2.307 5.681 1.00 72.91 C ANISOU 2736 CG2 VAL A1149 9932 9486 8287 -354 332 524 C ATOM 2737 N ILE A1150 27.478 -4.091 7.932 1.00 70.51 N ANISOU 2737 N ILE A1150 9218 9630 7942 -221 295 452 N ATOM 2738 CA ILE A1150 28.693 -4.840 8.260 1.00 71.09 C ANISOU 2738 CA ILE A1150 9146 9892 7975 -126 292 428 C ATOM 2739 C ILE A1150 28.506 -5.525 9.633 1.00 74.84 C ANISOU 2739 C ILE A1150 9626 10356 8455 -1 239 436 C ATOM 2740 O ILE A1150 28.808 -6.714 9.749 1.00 74.70 O ANISOU 2740 O ILE A1150 9587 10378 8417 171 243 442 O ATOM 2741 CB ILE A1150 29.938 -3.907 8.176 1.00 75.31 C ANISOU 2741 CB ILE A1150 9538 10618 8460 -268 311 389 C ATOM 2742 CG1 ILE A1150 30.334 -3.691 6.691 1.00 76.08 C ANISOU 2742 CG1 ILE A1150 9619 10752 8536 -333 382 385 C ATOM 2743 CG2 ILE A1150 31.127 -4.434 8.989 1.00 77.11 C ANISOU 2743 CG2 ILE A1150 9590 11076 8633 -178 282 354 C ATOM 2744 CD1 ILE A1150 31.054 -2.371 6.352 1.00 83.72 C ANISOU 2744 CD1 ILE A1150 10534 11807 9469 -551 430 356 C ATOM 2745 N THR A1151 27.944 -4.806 10.635 1.00 71.51 N ANISOU 2745 N THR A1151 9254 9863 8054 -76 197 441 N ATOM 2746 CA THR A1151 27.666 -5.360 11.971 1.00 71.47 C ANISOU 2746 CA THR A1151 9271 9835 8050 33 150 453 C ATOM 2747 C THR A1151 26.672 -6.525 11.839 1.00 75.85 C ANISOU 2747 C THR A1151 9956 10224 8640 169 168 484 C ATOM 2748 O THR A1151 26.896 -7.572 12.444 1.00 76.23 O ANISOU 2748 O THR A1151 10008 10293 8665 328 166 497 O ATOM 2749 CB THR A1151 27.160 -4.269 12.942 1.00 75.05 C ANISOU 2749 CB THR A1151 9767 10230 8519 -91 110 449 C ATOM 2750 OG1 THR A1151 28.149 -3.248 13.043 1.00 74.38 O ANISOU 2750 OG1 THR A1151 9568 10300 8394 -234 107 406 O ATOM 2751 CG2 THR A1151 26.872 -4.803 14.338 1.00 72.45 C ANISOU 2751 CG2 THR A1151 9463 9882 8183 18 63 463 C ATOM 2752 N THR A1152 25.618 -6.360 11.005 1.00 71.92 N ANISOU 2752 N THR A1152 9565 9573 8188 108 193 492 N ATOM 2753 CA THR A1152 24.595 -7.380 10.752 1.00 71.48 C ANISOU 2753 CA THR A1152 9627 9367 8164 194 220 500 C ATOM 2754 C THR A1152 25.256 -8.647 10.169 1.00 77.76 C ANISOU 2754 C THR A1152 10403 10211 8931 334 266 494 C ATOM 2755 O THR A1152 24.828 -9.753 10.501 1.00 78.26 O ANISOU 2755 O THR A1152 10555 10181 9000 447 292 501 O ATOM 2756 CB THR A1152 23.482 -6.813 9.855 1.00 76.33 C ANISOU 2756 CB THR A1152 10322 9867 8813 94 233 495 C ATOM 2757 OG1 THR A1152 22.990 -5.609 10.440 1.00 73.12 O ANISOU 2757 OG1 THR A1152 9939 9422 8420 -11 195 504 O ATOM 2758 CG2 THR A1152 22.315 -7.778 9.667 1.00 74.04 C ANISOU 2758 CG2 THR A1152 10140 9441 8552 150 259 483 C ATOM 2759 N PHE A1153 26.317 -8.494 9.353 1.00 75.05 N ANISOU 2759 N PHE A1153 9953 10011 8553 329 284 481 N ATOM 2760 CA PHE A1153 27.040 -9.642 8.801 1.00 75.79 C ANISOU 2760 CA PHE A1153 10021 10167 8609 475 330 474 C ATOM 2761 C PHE A1153 27.915 -10.309 9.866 1.00 80.83 C ANISOU 2761 C PHE A1153 10602 10916 9196 637 313 487 C ATOM 2762 O PHE A1153 28.064 -11.528 9.850 1.00 80.85 O ANISOU 2762 O PHE A1153 10663 10884 9172 807 354 496 O ATOM 2763 CB PHE A1153 27.898 -9.237 7.591 1.00 78.12 C ANISOU 2763 CB PHE A1153 10212 10596 8876 420 358 454 C ATOM 2764 CG PHE A1153 27.157 -9.106 6.280 1.00 78.94 C ANISOU 2764 CG PHE A1153 10391 10598 9005 343 395 444 C ATOM 2765 CD1 PHE A1153 26.461 -10.186 5.742 1.00 81.58 C ANISOU 2765 CD1 PHE A1153 10836 10809 9353 425 436 432 C ATOM 2766 CD2 PHE A1153 27.202 -7.923 5.554 1.00 80.85 C ANISOU 2766 CD2 PHE A1153 10599 10875 9244 190 397 442 C ATOM 2767 CE1 PHE A1153 25.793 -10.070 4.521 1.00 82.04 C ANISOU 2767 CE1 PHE A1153 10948 10802 9420 358 464 412 C ATOM 2768 CE2 PHE A1153 26.531 -7.807 4.333 1.00 83.20 C ANISOU 2768 CE2 PHE A1153 10968 11096 9549 142 428 436 C ATOM 2769 CZ PHE A1153 25.837 -8.884 3.821 1.00 81.03 C ANISOU 2769 CZ PHE A1153 10780 10724 9285 228 455 418 C ATOM 2770 N ARG A1154 28.489 -9.511 10.784 1.00 78.35 N ANISOU 2770 N ARG A1154 10180 10733 8856 589 257 485 N ATOM 2771 CA ARG A1154 29.365 -9.994 11.853 1.00 79.52 C ANISOU 2771 CA ARG A1154 10248 11028 8936 743 227 493 C ATOM 2772 C ARG A1154 28.585 -10.708 12.947 1.00 83.89 C ANISOU 2772 C ARG A1154 10944 11431 9498 856 221 530 C ATOM 2773 O ARG A1154 28.811 -11.891 13.198 1.00 84.43 O ANISOU 2773 O ARG A1154 11075 11482 9524 1058 254 554 O ATOM 2774 CB ARG A1154 30.153 -8.834 12.481 1.00 80.11 C ANISOU 2774 CB ARG A1154 10159 11303 8976 625 169 463 C ATOM 2775 CG ARG A1154 31.294 -8.295 11.643 1.00 89.64 C ANISOU 2775 CG ARG A1154 11192 12724 10143 544 185 419 C ATOM 2776 CD ARG A1154 32.350 -7.634 12.509 1.00 99.21 C ANISOU 2776 CD ARG A1154 12217 14192 11286 500 135 375 C ATOM 2777 NE ARG A1154 31.818 -6.531 13.316 1.00105.74 N ANISOU 2777 NE ARG A1154 13078 14955 12145 324 93 363 N ATOM 2778 CZ ARG A1154 31.922 -6.455 14.639 1.00117.02 C ANISOU 2778 CZ ARG A1154 14473 16453 13536 368 34 356 C ATOM 2779 NH1 ARG A1154 32.546 -7.407 15.321 1.00102.46 N ANISOU 2779 NH1 ARG A1154 12562 14753 11615 593 7 366 N ATOM 2780 NH2 ARG A1154 31.409 -5.419 15.290 1.00103.91 N ANISOU 2780 NH2 ARG A1154 12855 14721 11906 200 3 341 N ATOM 2781 N THR A1155 27.692 -9.966 13.614 1.00 79.94 N ANISOU 2781 N THR A1155 10503 10824 9045 730 185 535 N ATOM 2782 CA THR A1155 26.879 -10.416 14.736 1.00 79.73 C ANISOU 2782 CA THR A1155 10604 10660 9029 796 177 566 C ATOM 2783 C THR A1155 25.814 -11.417 14.303 1.00 83.32 C ANISOU 2783 C THR A1155 11241 10891 9527 841 247 580 C ATOM 2784 O THR A1155 25.527 -12.355 15.047 1.00 84.14 O ANISOU 2784 O THR A1155 11460 10900 9609 974 278 609 O ATOM 2785 CB THR A1155 26.227 -9.214 15.436 1.00 89.44 C ANISOU 2785 CB THR A1155 11836 11851 10298 630 123 559 C ATOM 2786 OG1 THR A1155 25.378 -8.527 14.513 1.00 90.29 O ANISOU 2786 OG1 THR A1155 11990 11844 10472 468 139 543 O ATOM 2787 CG2 THR A1155 27.247 -8.249 16.038 1.00 88.89 C ANISOU 2787 CG2 THR A1155 11603 11995 10178 569 61 533 C ATOM 2788 N GLY A1156 25.227 -11.207 13.129 1.00 78.61 N ANISOU 2788 N GLY A1156 10673 10213 8983 727 277 555 N ATOM 2789 CA GLY A1156 24.161 -12.065 12.625 1.00 78.11 C ANISOU 2789 CA GLY A1156 10763 9957 8957 732 343 545 C ATOM 2790 C GLY A1156 22.877 -11.878 13.405 1.00 81.52 C ANISOU 2790 C GLY A1156 11299 10242 9433 655 336 548 C ATOM 2791 O GLY A1156 22.095 -12.818 13.551 1.00 81.57 O ANISOU 2791 O GLY A1156 11444 10098 9452 692 397 543 O ATOM 2792 N THR A1157 22.695 -10.669 13.967 1.00 77.35 N ANISOU 2792 N THR A1157 10708 9760 8923 547 268 552 N ATOM 2793 CA THR A1157 21.549 -10.247 14.779 1.00 76.48 C ANISOU 2793 CA THR A1157 10670 9542 8848 470 249 555 C ATOM 2794 C THR A1157 21.037 -8.894 14.255 1.00 79.87 C ANISOU 2794 C THR A1157 11051 9984 9312 311 207 536 C ATOM 2795 O THR A1157 21.572 -8.387 13.266 1.00 80.05 O ANISOU 2795 O THR A1157 11002 10084 9329 262 203 525 O ATOM 2796 CB THR A1157 21.933 -10.173 16.277 1.00 83.74 C ANISOU 2796 CB THR A1157 11582 10506 9732 541 210 587 C ATOM 2797 OG1 THR A1157 23.039 -9.291 16.448 1.00 81.88 O ANISOU 2797 OG1 THR A1157 11202 10447 9460 520 149 586 O ATOM 2798 CG2 THR A1157 22.251 -11.535 16.887 1.00 83.36 C ANISOU 2798 CG2 THR A1157 11620 10417 9636 722 261 617 C ATOM 2799 N TRP A1158 20.007 -8.316 14.907 1.00 75.01 N ANISOU 2799 N TRP A1158 10487 9291 8724 241 184 535 N ATOM 2800 CA TRP A1158 19.422 -7.026 14.524 1.00 73.76 C ANISOU 2800 CA TRP A1158 10312 9128 8587 118 151 524 C ATOM 2801 C TRP A1158 19.852 -5.904 15.482 1.00 76.37 C ANISOU 2801 C TRP A1158 10599 9514 8902 68 96 538 C ATOM 2802 O TRP A1158 19.282 -4.810 15.452 1.00 74.98 O ANISOU 2802 O TRP A1158 10444 9308 8738 -21 73 534 O ATOM 2803 CB TRP A1158 17.890 -7.134 14.495 1.00 71.88 C ANISOU 2803 CB TRP A1158 10156 8775 8379 81 168 502 C ATOM 2804 CG TRP A1158 17.353 -7.958 13.367 1.00 72.90 C ANISOU 2804 CG TRP A1158 10316 8866 8518 84 219 466 C ATOM 2805 CD1 TRP A1158 16.777 -9.189 13.455 1.00 76.05 C ANISOU 2805 CD1 TRP A1158 10787 9184 8926 119 278 440 C ATOM 2806 CD2 TRP A1158 17.330 -7.600 11.979 1.00 72.71 C ANISOU 2806 CD2 TRP A1158 10259 8881 8488 44 223 447 C ATOM 2807 NE1 TRP A1158 16.384 -9.618 12.209 1.00 75.72 N ANISOU 2807 NE1 TRP A1158 10751 9135 8884 92 314 395 N ATOM 2808 CE2 TRP A1158 16.724 -8.668 11.281 1.00 76.90 C ANISOU 2808 CE2 TRP A1158 10831 9365 9022 56 277 401 C ATOM 2809 CE3 TRP A1158 17.765 -6.477 11.253 1.00 73.91 C ANISOU 2809 CE3 TRP A1158 10361 9099 8624 -6 194 461 C ATOM 2810 CZ2 TRP A1158 16.544 -8.649 9.892 1.00 76.15 C ANISOU 2810 CZ2 TRP A1158 10716 9304 8913 30 291 368 C ATOM 2811 CZ3 TRP A1158 17.581 -6.457 9.879 1.00 75.40 C ANISOU 2811 CZ3 TRP A1158 10541 9310 8796 -24 213 440 C ATOM 2812 CH2 TRP A1158 16.973 -7.531 9.213 1.00 76.15 C ANISOU 2812 CH2 TRP A1158 10664 9375 8894 -1 255 393 C ATOM 2813 N ASP A1159 20.886 -6.172 16.301 1.00 73.43 N ANISOU 2813 N ASP A1159 10172 9235 8495 132 76 550 N ATOM 2814 CA ASP A1159 21.418 -5.282 17.338 1.00 73.40 C ANISOU 2814 CA ASP A1159 10117 9309 8464 89 25 550 C ATOM 2815 C ASP A1159 21.946 -3.930 16.801 1.00 75.55 C ANISOU 2815 C ASP A1159 10328 9649 8728 -49 8 529 C ATOM 2816 O ASP A1159 21.996 -2.969 17.569 1.00 74.64 O ANISOU 2816 O ASP A1159 10211 9549 8601 -127 -23 518 O ATOM 2817 CB ASP A1159 22.507 -6.003 18.157 1.00 76.59 C ANISOU 2817 CB ASP A1159 10454 9835 8811 209 8 559 C ATOM 2818 CG ASP A1159 22.052 -7.300 18.822 1.00 88.96 C ANISOU 2818 CG ASP A1159 12114 11317 10370 354 38 589 C ATOM 2819 OD1 ASP A1159 20.870 -7.376 19.244 1.00 88.63 O ANISOU 2819 OD1 ASP A1159 12176 11136 10362 331 54 595 O ATOM 2820 OD2 ASP A1159 22.886 -8.224 18.954 1.00 96.92 O ANISOU 2820 OD2 ASP A1159 13095 12401 11329 494 52 605 O ATOM 2821 N ALA A1160 22.314 -3.840 15.506 1.00 71.87 N ANISOU 2821 N ALA A1160 9829 9213 8264 -85 39 522 N ATOM 2822 CA ALA A1160 22.773 -2.574 14.915 1.00 71.74 C ANISOU 2822 CA ALA A1160 9783 9239 8235 -224 44 507 C ATOM 2823 C ALA A1160 21.580 -1.681 14.584 1.00 74.32 C ANISOU 2823 C ALA A1160 10225 9425 8588 -294 52 518 C ATOM 2824 O ALA A1160 21.714 -0.456 14.536 1.00 73.47 O ANISOU 2824 O ALA A1160 10145 9305 8466 -408 58 511 O ATOM 2825 CB ALA A1160 23.598 -2.835 13.664 1.00 72.90 C ANISOU 2825 CB ALA A1160 9860 9473 8366 -228 82 500 C ATOM 2826 N TYR A1161 20.408 -2.307 14.384 1.00 70.79 N ANISOU 2826 N TYR A1161 9851 8876 8172 -225 59 529 N ATOM 2827 CA TYR A1161 19.144 -1.648 14.056 1.00 70.37 C ANISOU 2827 CA TYR A1161 9892 8713 8132 -252 61 536 C ATOM 2828 C TYR A1161 18.241 -1.563 15.301 1.00 75.44 C ANISOU 2828 C TYR A1161 10589 9286 8790 -231 34 536 C ATOM 2829 O TYR A1161 17.033 -1.347 15.181 1.00 74.38 O ANISOU 2829 O TYR A1161 10520 9075 8664 -218 34 536 O ATOM 2830 CB TYR A1161 18.457 -2.386 12.885 1.00 70.63 C ANISOU 2830 CB TYR A1161 9943 8718 8176 -201 89 531 C ATOM 2831 CG TYR A1161 19.232 -2.244 11.592 1.00 71.79 C ANISOU 2831 CG TYR A1161 10052 8925 8300 -229 119 533 C ATOM 2832 CD1 TYR A1161 20.293 -3.097 11.295 1.00 74.08 C ANISOU 2832 CD1 TYR A1161 10262 9301 8584 -193 136 525 C ATOM 2833 CD2 TYR A1161 18.955 -1.213 10.699 1.00 72.17 C ANISOU 2833 CD2 TYR A1161 10152 8947 8322 -282 134 546 C ATOM 2834 CE1 TYR A1161 21.059 -2.925 10.143 1.00 74.83 C ANISOU 2834 CE1 TYR A1161 10316 9463 8654 -224 168 525 C ATOM 2835 CE2 TYR A1161 19.707 -1.039 9.537 1.00 73.26 C ANISOU 2835 CE2 TYR A1161 10264 9140 8432 -313 170 551 C ATOM 2836 CZ TYR A1161 20.750 -1.907 9.256 1.00 79.12 C ANISOU 2836 CZ TYR A1161 10912 9974 9175 -291 187 538 C ATOM 2837 OH TYR A1161 21.498 -1.754 8.114 1.00 77.58 O ANISOU 2837 OH TYR A1161 10685 9842 8949 -324 227 540 O ATOM 2838 N LYS A 263 18.856 -1.695 16.498 1.00 73.62 N ANISOU 2838 N LYS A 263 10323 9099 8550 -222 8 534 N ATOM 2839 CA LYS A 263 18.194 -1.608 17.800 1.00 73.61 C ANISOU 2839 CA LYS A 263 10368 9047 8553 -203 -17 535 C ATOM 2840 C LYS A 263 17.623 -0.211 18.002 1.00 78.05 C ANISOU 2840 C LYS A 263 11001 9547 9108 -280 -27 533 C ATOM 2841 O LYS A 263 18.366 0.775 17.928 1.00 78.06 O ANISOU 2841 O LYS A 263 10996 9578 9085 -369 -27 524 O ATOM 2842 CB LYS A 263 19.180 -1.939 18.934 1.00 76.56 C ANISOU 2842 CB LYS A 263 10680 9510 8899 -175 -45 532 C ATOM 2843 CG LYS A 263 18.974 -3.295 19.585 1.00 89.67 C ANISOU 2843 CG LYS A 263 12353 11157 10562 -55 -37 548 C ATOM 2844 CD LYS A 263 19.989 -3.501 20.707 1.00 99.60 C ANISOU 2844 CD LYS A 263 13550 12524 11771 -6 -70 549 C ATOM 2845 CE LYS A 263 19.845 -4.839 21.387 1.00109.57 C ANISOU 2845 CE LYS A 263 14852 13762 13019 133 -52 576 C ATOM 2846 NZ LYS A 263 20.817 -4.993 22.503 1.00118.98 N ANISOU 2846 NZ LYS A 263 15985 15079 14144 207 -91 581 N ATOM 2847 N PHE A 264 16.291 -0.138 18.214 1.00 74.14 N ANISOU 2847 N PHE A 264 10576 8966 8627 -247 -27 535 N ATOM 2848 CA PHE A 264 15.503 1.075 18.469 1.00 73.68 C ANISOU 2848 CA PHE A 264 10603 8837 8556 -279 -32 536 C ATOM 2849 C PHE A 264 15.785 2.186 17.441 1.00 77.40 C ANISOU 2849 C PHE A 264 11119 9287 9001 -339 -9 545 C ATOM 2850 O PHE A 264 15.922 3.355 17.806 1.00 77.06 O ANISOU 2850 O PHE A 264 11146 9200 8932 -402 -4 545 O ATOM 2851 CB PHE A 264 15.736 1.589 19.909 1.00 75.54 C ANISOU 2851 CB PHE A 264 10858 9067 8777 -309 -58 527 C ATOM 2852 CG PHE A 264 15.539 0.551 20.989 1.00 76.60 C ANISOU 2852 CG PHE A 264 10963 9218 8922 -244 -74 526 C ATOM 2853 CD1 PHE A 264 14.263 0.139 21.356 1.00 78.80 C ANISOU 2853 CD1 PHE A 264 11285 9438 9217 -189 -65 525 C ATOM 2854 CD2 PHE A 264 16.629 -0.008 21.646 1.00 79.11 C ANISOU 2854 CD2 PHE A 264 11215 9620 9224 -233 -92 524 C ATOM 2855 CE1 PHE A 264 14.082 -0.820 22.355 1.00 79.77 C ANISOU 2855 CE1 PHE A 264 11403 9562 9344 -136 -63 528 C ATOM 2856 CE2 PHE A 264 16.448 -0.968 22.645 1.00 81.80 C ANISOU 2856 CE2 PHE A 264 11554 9966 9561 -154 -98 533 C ATOM 2857 CZ PHE A 264 15.176 -1.365 22.994 1.00 79.46 C ANISOU 2857 CZ PHE A 264 11321 9587 9285 -113 -78 538 C ATOM 2858 N CYS A 265 15.870 1.812 16.157 1.00 73.98 N ANISOU 2858 N CYS A 265 10660 8879 8569 -322 13 553 N ATOM 2859 CA CYS A 265 16.125 2.760 15.074 1.00 74.09 C ANISOU 2859 CA CYS A 265 10729 8873 8550 -368 45 570 C ATOM 2860 C CYS A 265 14.815 3.188 14.415 1.00 74.77 C ANISOU 2860 C CYS A 265 10897 8902 8612 -295 51 585 C ATOM 2861 O CYS A 265 14.705 4.329 13.962 1.00 74.80 O ANISOU 2861 O CYS A 265 11002 8847 8571 -311 78 608 O ATOM 2862 CB CYS A 265 17.098 2.172 14.059 1.00 75.22 C ANISOU 2862 CB CYS A 265 10793 9092 8693 -389 67 570 C ATOM 2863 SG CYS A 265 18.813 2.109 14.634 1.00 80.17 S ANISOU 2863 SG CYS A 265 11323 9821 9318 -482 67 549 S ATOM 2864 N LEU A 266 13.822 2.279 14.382 1.00 68.40 N ANISOU 2864 N LEU A 266 10049 8117 7823 -214 33 567 N ATOM 2865 CA LEU A 266 12.489 2.518 13.832 1.00 66.99 C ANISOU 2865 CA LEU A 266 9910 7930 7613 -133 30 565 C ATOM 2866 C LEU A 266 11.724 3.471 14.743 1.00 69.21 C ANISOU 2866 C LEU A 266 10275 8149 7872 -105 19 572 C ATOM 2867 O LEU A 266 11.915 3.415 15.960 1.00 69.15 O ANISOU 2867 O LEU A 266 10264 8118 7893 -139 5 562 O ATOM 2868 CB LEU A 266 11.738 1.178 13.697 1.00 66.34 C ANISOU 2868 CB LEU A 266 9743 7906 7558 -88 22 523 C ATOM 2869 CG LEU A 266 10.598 1.132 12.683 1.00 70.90 C ANISOU 2869 CG LEU A 266 10310 8535 8092 -17 20 500 C ATOM 2870 CD1 LEU A 266 11.126 0.979 11.258 1.00 71.12 C ANISOU 2870 CD1 LEU A 266 10322 8606 8095 -17 38 508 C ATOM 2871 CD2 LEU A 266 9.633 0.012 13.007 1.00 72.54 C ANISOU 2871 CD2 LEU A 266 10448 8790 8324 -2 18 441 C ATOM 2872 N LYS A 267 10.864 4.335 14.167 1.00 64.24 N ANISOU 2872 N LYS A 267 9725 7500 7184 -29 25 588 N ATOM 2873 CA LYS A 267 10.055 5.305 14.916 1.00 63.88 C ANISOU 2873 CA LYS A 267 9774 7395 7103 26 21 597 C ATOM 2874 C LYS A 267 9.143 4.602 15.934 1.00 66.73 C ANISOU 2874 C LYS A 267 10065 7794 7496 59 -7 556 C ATOM 2875 O LYS A 267 9.057 5.028 17.092 1.00 65.43 O ANISOU 2875 O LYS A 267 9944 7577 7338 45 -13 555 O ATOM 2876 CB LYS A 267 9.218 6.169 13.961 1.00 66.64 C ANISOU 2876 CB LYS A 267 10212 7741 7368 143 34 623 C ATOM 2877 N GLU A 268 8.523 3.489 15.506 1.00 63.13 N ANISOU 2877 N GLU A 268 9502 7428 7055 87 -17 518 N ATOM 2878 CA GLU A 268 7.623 2.667 16.311 1.00 62.75 C ANISOU 2878 CA GLU A 268 9383 7424 7033 100 -26 471 C ATOM 2879 C GLU A 268 8.374 1.965 17.447 1.00 67.05 C ANISOU 2879 C GLU A 268 9907 7929 7641 21 -23 469 C ATOM 2880 O GLU A 268 7.772 1.671 18.482 1.00 67.05 O ANISOU 2880 O GLU A 268 9896 7925 7654 26 -24 448 O ATOM 2881 CB GLU A 268 6.896 1.649 15.428 1.00 64.05 C ANISOU 2881 CB GLU A 268 9448 7693 7193 120 -22 419 C ATOM 2882 CG GLU A 268 5.848 2.271 14.513 1.00 74.51 C ANISOU 2882 CG GLU A 268 10771 9102 8438 225 -35 405 C ATOM 2883 CD GLU A 268 6.329 2.892 13.213 1.00 95.39 C ANISOU 2883 CD GLU A 268 13465 11749 11031 266 -33 446 C ATOM 2884 OE1 GLU A 268 5.529 3.616 12.576 1.00 95.59 O ANISOU 2884 OE1 GLU A 268 13517 11831 10973 381 -44 451 O ATOM 2885 OE2 GLU A 268 7.496 2.657 12.824 1.00 85.14 O ANISOU 2885 OE2 GLU A 268 12178 10404 9768 194 -18 473 O ATOM 2886 N HIS A 269 9.690 1.735 17.265 1.00 63.47 N ANISOU 2886 N HIS A 269 9447 7455 7214 -41 -19 493 N ATOM 2887 CA HIS A 269 10.577 1.126 18.258 1.00 62.88 C ANISOU 2887 CA HIS A 269 9350 7364 7178 -92 -21 497 C ATOM 2888 C HIS A 269 10.996 2.161 19.298 1.00 67.17 C ANISOU 2888 C HIS A 269 9958 7856 7708 -122 -36 515 C ATOM 2889 O HIS A 269 11.069 1.825 20.483 1.00 66.65 O ANISOU 2889 O HIS A 269 9886 7783 7656 -130 -46 509 O ATOM 2890 CB HIS A 269 11.802 0.496 17.582 1.00 63.49 C ANISOU 2890 CB HIS A 269 9378 7471 7275 -129 -11 507 C ATOM 2891 CG HIS A 269 11.516 -0.822 16.929 1.00 66.55 C ANISOU 2891 CG HIS A 269 9709 7896 7683 -108 11 481 C ATOM 2892 ND1 HIS A 269 12.450 -1.838 16.931 1.00 68.25 N ANISOU 2892 ND1 HIS A 269 9884 8126 7921 -117 27 484 N ATOM 2893 CD2 HIS A 269 10.401 -1.254 16.291 1.00 68.08 C ANISOU 2893 CD2 HIS A 269 9882 8116 7868 -81 25 444 C ATOM 2894 CE1 HIS A 269 11.889 -2.838 16.274 1.00 67.67 C ANISOU 2894 CE1 HIS A 269 9788 8066 7858 -101 57 450 C ATOM 2895 NE2 HIS A 269 10.653 -2.536 15.879 1.00 67.89 N ANISOU 2895 NE2 HIS A 269 9819 8109 7869 -91 56 420 N ATOM 2896 N LYS A 270 11.244 3.428 18.862 1.00 64.22 N ANISOU 2896 N LYS A 270 9661 7442 7299 -140 -31 535 N ATOM 2897 CA LYS A 270 11.577 4.559 19.743 1.00 64.19 C ANISOU 2897 CA LYS A 270 9743 7374 7271 -183 -33 541 C ATOM 2898 C LYS A 270 10.448 4.749 20.759 1.00 67.17 C ANISOU 2898 C LYS A 270 10157 7725 7639 -123 -44 527 C ATOM 2899 O LYS A 270 10.718 4.989 21.934 1.00 67.19 O ANISOU 2899 O LYS A 270 10183 7704 7642 -158 -55 518 O ATOM 2900 CB LYS A 270 11.788 5.866 18.946 1.00 67.60 C ANISOU 2900 CB LYS A 270 10287 7742 7657 -203 -3 564 C ATOM 2901 CG LYS A 270 12.796 5.809 17.803 1.00 82.75 C ANISOU 2901 CG LYS A 270 12181 9687 9574 -263 20 578 C ATOM 2902 CD LYS A 270 14.200 6.197 18.215 1.00 93.18 C ANISOU 2902 CD LYS A 270 13497 11010 10896 -395 32 566 C ATOM 2903 CE LYS A 270 15.067 6.433 17.006 1.00106.14 C ANISOU 2903 CE LYS A 270 15140 12666 12521 -459 72 580 C ATOM 2904 NZ LYS A 270 16.509 6.303 17.341 1.00119.25 N ANISOU 2904 NZ LYS A 270 16719 14398 14191 -584 75 552 N ATOM 2905 N ALA A 271 9.182 4.595 20.288 1.00 62.55 N ANISOU 2905 N ALA A 271 9563 7164 7039 -33 -41 520 N ATOM 2906 CA ALA A 271 7.943 4.679 21.065 1.00 61.88 C ANISOU 2906 CA ALA A 271 9489 7084 6938 36 -46 499 C ATOM 2907 C ALA A 271 7.907 3.597 22.151 1.00 64.79 C ANISOU 2907 C ALA A 271 9791 7479 7349 7 -50 477 C ATOM 2908 O ALA A 271 7.444 3.860 23.268 1.00 64.78 O ANISOU 2908 O ALA A 271 9821 7456 7336 22 -53 467 O ATOM 2909 CB ALA A 271 6.744 4.537 20.139 1.00 62.64 C ANISOU 2909 CB ALA A 271 9548 7249 7005 129 -42 482 C ATOM 2910 N LEU A 272 8.426 2.393 21.830 1.00 59.82 N ANISOU 2910 N LEU A 272 9084 6888 6758 -29 -44 473 N ATOM 2911 CA LEU A 272 8.508 1.280 22.774 1.00 59.04 C ANISOU 2911 CA LEU A 272 8947 6798 6689 -47 -34 462 C ATOM 2912 C LEU A 272 9.622 1.529 23.782 1.00 63.44 C ANISOU 2912 C LEU A 272 9530 7330 7243 -84 -55 483 C ATOM 2913 O LEU A 272 9.474 1.170 24.952 1.00 63.16 O ANISOU 2913 O LEU A 272 9506 7288 7206 -76 -54 480 O ATOM 2914 CB LEU A 272 8.720 -0.060 22.059 1.00 58.66 C ANISOU 2914 CB LEU A 272 8835 6783 6672 -59 -9 452 C ATOM 2915 CG LEU A 272 7.589 -0.525 21.144 1.00 62.95 C ANISOU 2915 CG LEU A 272 9334 7372 7211 -40 15 411 C ATOM 2916 CD1 LEU A 272 8.083 -1.577 20.164 1.00 62.70 C ANISOU 2916 CD1 LEU A 272 9257 7361 7203 -64 39 401 C ATOM 2917 CD2 LEU A 272 6.382 -1.014 21.945 1.00 65.07 C ANISOU 2917 CD2 LEU A 272 9591 7656 7478 -36 45 371 C ATOM 2918 N LYS A 273 10.726 2.164 23.335 1.00 60.14 N ANISOU 2918 N LYS A 273 9121 6911 6817 -129 -71 498 N ATOM 2919 CA LYS A 273 11.850 2.511 24.204 1.00 60.56 C ANISOU 2919 CA LYS A 273 9179 6974 6855 -181 -94 500 C ATOM 2920 C LYS A 273 11.411 3.589 25.209 1.00 65.54 C ANISOU 2920 C LYS A 273 9892 7555 7455 -189 -103 488 C ATOM 2921 O LYS A 273 11.703 3.454 26.397 1.00 65.08 O ANISOU 2921 O LYS A 273 9833 7513 7383 -197 -120 479 O ATOM 2922 CB LYS A 273 13.067 2.976 23.383 1.00 62.86 C ANISOU 2922 CB LYS A 273 9451 7293 7141 -249 -96 504 C ATOM 2923 CG LYS A 273 14.360 3.061 24.191 1.00 71.32 C ANISOU 2923 CG LYS A 273 10482 8424 8191 -309 -121 490 C ATOM 2924 CD LYS A 273 15.531 3.423 23.304 1.00 81.64 C ANISOU 2924 CD LYS A 273 11749 9780 9490 -388 -113 484 C ATOM 2925 CE LYS A 273 16.802 3.641 24.083 1.00 91.47 C ANISOU 2925 CE LYS A 273 12935 11117 10701 -461 -138 453 C ATOM 2926 NZ LYS A 273 17.946 3.959 23.188 1.00100.49 N ANISOU 2926 NZ LYS A 273 14022 12326 11832 -551 -122 437 N ATOM 2927 N THR A 274 10.676 4.624 24.733 1.00 62.82 N ANISOU 2927 N THR A 274 9626 7152 7091 -172 -89 487 N ATOM 2928 CA THR A 274 10.157 5.726 25.557 1.00 63.29 C ANISOU 2928 CA THR A 274 9785 7148 7113 -164 -87 475 C ATOM 2929 C THR A 274 9.271 5.163 26.677 1.00 66.88 C ANISOU 2929 C THR A 274 10223 7618 7569 -108 -92 463 C ATOM 2930 O THR A 274 9.445 5.537 27.838 1.00 67.16 O ANISOU 2930 O THR A 274 10298 7637 7582 -128 -103 449 O ATOM 2931 CB THR A 274 9.396 6.752 24.697 1.00 71.54 C ANISOU 2931 CB THR A 274 10924 8131 8127 -112 -62 486 C ATOM 2932 OG1 THR A 274 10.170 7.078 23.542 1.00 73.79 O ANISOU 2932 OG1 THR A 274 11223 8404 8409 -161 -46 504 O ATOM 2933 CG2 THR A 274 9.074 8.024 25.459 1.00 70.83 C ANISOU 2933 CG2 THR A 274 10968 7955 7991 -105 -48 475 C ATOM 2934 N LEU A 275 8.363 4.231 26.323 1.00 61.88 N ANISOU 2934 N LEU A 275 9529 7023 6959 -49 -78 463 N ATOM 2935 CA LEU A 275 7.448 3.566 27.246 1.00 61.05 C ANISOU 2935 CA LEU A 275 9403 6937 6855 -10 -64 448 C ATOM 2936 C LEU A 275 8.213 2.700 28.253 1.00 65.41 C ANISOU 2936 C LEU A 275 9931 7505 7416 -40 -71 457 C ATOM 2937 O LEU A 275 7.787 2.589 29.400 1.00 65.34 O ANISOU 2937 O LEU A 275 9948 7491 7389 -21 -65 450 O ATOM 2938 CB LEU A 275 6.458 2.717 26.446 1.00 60.66 C ANISOU 2938 CB LEU A 275 9286 6936 6825 25 -37 432 C ATOM 2939 CG LEU A 275 5.031 3.234 26.254 1.00 64.97 C ANISOU 2939 CG LEU A 275 9835 7512 7340 95 -24 405 C ATOM 2940 CD1 LEU A 275 4.992 4.694 25.824 1.00 65.17 C ANISOU 2940 CD1 LEU A 275 9943 7496 7322 144 -40 419 C ATOM 2941 CD2 LEU A 275 4.316 2.397 25.228 1.00 67.14 C ANISOU 2941 CD2 LEU A 275 10020 7862 7626 106 -2 376 C ATOM 2942 N GLY A 276 9.344 2.134 27.820 1.00 62.31 N ANISOU 2942 N GLY A 276 9494 7139 7040 -72 -82 473 N ATOM 2943 CA GLY A 276 10.234 1.333 28.655 1.00 62.10 C ANISOU 2943 CA GLY A 276 9444 7146 7006 -72 -93 487 C ATOM 2944 C GLY A 276 10.982 2.173 29.676 1.00 66.38 C ANISOU 2944 C GLY A 276 10014 7702 7504 -104 -132 477 C ATOM 2945 O GLY A 276 11.298 1.689 30.767 1.00 66.47 O ANISOU 2945 O GLY A 276 10024 7745 7486 -79 -142 482 O ATOM 2946 N ILE A 277 11.266 3.449 29.324 1.00 62.50 N ANISOU 2946 N ILE A 277 9560 7187 7001 -162 -146 458 N ATOM 2947 CA ILE A 277 11.938 4.430 30.186 1.00 62.13 C ANISOU 2947 CA ILE A 277 9552 7145 6908 -223 -173 428 C ATOM 2948 C ILE A 277 10.924 4.932 31.242 1.00 64.97 C ANISOU 2948 C ILE A 277 9991 7453 7242 -187 -166 414 C ATOM 2949 O ILE A 277 11.300 5.102 32.407 1.00 65.58 O ANISOU 2949 O ILE A 277 10082 7558 7276 -202 -188 393 O ATOM 2950 CB ILE A 277 12.583 5.580 29.341 1.00 65.21 C ANISOU 2950 CB ILE A 277 9978 7507 7293 -315 -168 409 C ATOM 2951 CG1 ILE A 277 13.756 5.023 28.500 1.00 65.24 C ANISOU 2951 CG1 ILE A 277 9885 7591 7312 -357 -177 416 C ATOM 2952 CG2 ILE A 277 13.084 6.741 30.232 1.00 66.63 C ANISOU 2952 CG2 ILE A 277 10225 7670 7420 -402 -178 361 C ATOM 2953 CD1 ILE A 277 14.036 5.723 27.221 1.00 69.76 C ANISOU 2953 CD1 ILE A 277 10485 8125 7896 -419 -150 417 C ATOM 2954 N ILE A 278 9.643 5.128 30.841 1.00 59.59 N ANISOU 2954 N ILE A 278 9352 6715 6576 -131 -135 421 N ATOM 2955 CA ILE A 278 8.546 5.567 31.714 1.00 59.08 C ANISOU 2955 CA ILE A 278 9351 6612 6484 -80 -120 407 C ATOM 2956 C ILE A 278 8.343 4.516 32.821 1.00 62.29 C ANISOU 2956 C ILE A 278 9722 7062 6883 -46 -117 414 C ATOM 2957 O ILE A 278 8.340 4.863 34.003 1.00 62.19 O ANISOU 2957 O ILE A 278 9753 7047 6828 -44 -128 398 O ATOM 2958 CB ILE A 278 7.247 5.841 30.886 1.00 62.06 C ANISOU 2958 CB ILE A 278 9747 6960 6872 -10 -89 409 C ATOM 2959 CG1 ILE A 278 7.368 7.123 30.008 1.00 62.62 C ANISOU 2959 CG1 ILE A 278 9903 6966 6924 -18 -83 409 C ATOM 2960 CG2 ILE A 278 5.978 5.865 31.758 1.00 63.11 C ANISOU 2960 CG2 ILE A 278 9903 7096 6981 60 -67 393 C ATOM 2961 CD1 ILE A 278 7.186 8.477 30.742 1.00 72.50 C ANISOU 2961 CD1 ILE A 278 11289 8136 8122 -15 -73 386 C ATOM 2962 N MET A 279 8.234 3.236 32.425 1.00 58.70 N ANISOU 2962 N MET A 279 9201 6639 6462 -22 -97 438 N ATOM 2963 CA MET A 279 8.093 2.075 33.316 1.00 58.50 C ANISOU 2963 CA MET A 279 9164 6636 6427 13 -75 455 C ATOM 2964 C MET A 279 9.329 1.898 34.195 1.00 64.31 C ANISOU 2964 C MET A 279 9897 7419 7121 9 -114 466 C ATOM 2965 O MET A 279 9.197 1.686 35.395 1.00 65.24 O ANISOU 2965 O MET A 279 10048 7547 7194 41 -111 470 O ATOM 2966 CB MET A 279 7.886 0.791 32.492 1.00 60.06 C ANISOU 2966 CB MET A 279 9314 6840 6667 25 -33 474 C ATOM 2967 CG MET A 279 6.567 0.717 31.796 1.00 62.63 C ANISOU 2967 CG MET A 279 9621 7154 7020 29 10 450 C ATOM 2968 SD MET A 279 6.528 -0.663 30.652 1.00 65.46 S ANISOU 2968 SD MET A 279 9925 7521 7424 13 56 454 S ATOM 2969 CE MET A 279 5.009 -0.309 29.820 1.00 62.03 C ANISOU 2969 CE MET A 279 9450 7118 7002 12 84 405 C ATOM 2970 N GLY A 280 10.504 1.988 33.570 1.00 61.34 N ANISOU 2970 N GLY A 280 9473 7085 6750 -27 -149 467 N ATOM 2971 CA GLY A 280 11.815 1.818 34.184 1.00 61.82 C ANISOU 2971 CA GLY A 280 9495 7232 6762 -28 -194 467 C ATOM 2972 C GLY A 280 12.189 2.813 35.260 1.00 66.46 C ANISOU 2972 C GLY A 280 10112 7852 7287 -67 -234 426 C ATOM 2973 O GLY A 280 12.785 2.423 36.269 1.00 66.04 O ANISOU 2973 O GLY A 280 10042 7879 7172 -29 -262 428 O ATOM 2974 N THR A 281 11.879 4.109 35.052 1.00 63.59 N ANISOU 2974 N THR A 281 9802 7431 6930 -139 -234 387 N ATOM 2975 CA THR A 281 12.207 5.116 36.070 1.00 64.50 C ANISOU 2975 CA THR A 281 9963 7563 6982 -192 -263 335 C ATOM 2976 C THR A 281 11.234 5.006 37.242 1.00 68.29 C ANISOU 2976 C THR A 281 10506 8011 7430 -124 -247 340 C ATOM 2977 O THR A 281 11.644 5.232 38.381 1.00 69.11 O ANISOU 2977 O THR A 281 10621 8170 7465 -131 -277 311 O ATOM 2978 CB THR A 281 12.258 6.535 35.506 1.00 71.14 C ANISOU 2978 CB THR A 281 10871 8331 7828 -292 -252 291 C ATOM 2979 OG1 THR A 281 11.024 6.831 34.861 1.00 72.71 O ANISOU 2979 OG1 THR A 281 11138 8419 8068 -244 -208 314 O ATOM 2980 CG2 THR A 281 13.437 6.747 34.559 1.00 68.19 C ANISOU 2980 CG2 THR A 281 10436 8006 7466 -386 -264 274 C ATOM 2981 N PHE A 282 9.964 4.629 36.970 1.00 62.94 N ANISOU 2981 N PHE A 282 9859 7262 6794 -63 -198 371 N ATOM 2982 CA PHE A 282 8.940 4.447 38.000 1.00 62.31 C ANISOU 2982 CA PHE A 282 9831 7159 6686 -2 -169 375 C ATOM 2983 C PHE A 282 9.402 3.415 39.029 1.00 65.96 C ANISOU 2983 C PHE A 282 10273 7690 7098 50 -178 402 C ATOM 2984 O PHE A 282 9.343 3.690 40.233 1.00 66.61 O ANISOU 2984 O PHE A 282 10399 7794 7116 68 -189 385 O ATOM 2985 CB PHE A 282 7.600 4.022 37.374 1.00 63.35 C ANISOU 2985 CB PHE A 282 9963 7238 6868 43 -111 395 C ATOM 2986 CG PHE A 282 6.461 3.887 38.360 1.00 64.74 C ANISOU 2986 CG PHE A 282 10182 7401 7015 93 -70 390 C ATOM 2987 CD1 PHE A 282 5.654 4.975 38.667 1.00 67.80 C ANISOU 2987 CD1 PHE A 282 10629 7751 7381 108 -61 355 C ATOM 2988 CD2 PHE A 282 6.179 2.666 38.960 1.00 66.47 C ANISOU 2988 CD2 PHE A 282 10393 7640 7224 130 -29 421 C ATOM 2989 CE1 PHE A 282 4.592 4.847 39.566 1.00 68.99 C ANISOU 2989 CE1 PHE A 282 10809 7904 7500 156 -18 347 C ATOM 2990 CE2 PHE A 282 5.128 2.544 39.872 1.00 69.64 C ANISOU 2990 CE2 PHE A 282 10834 8032 7594 164 20 414 C ATOM 2991 CZ PHE A 282 4.330 3.630 40.157 1.00 68.00 C ANISOU 2991 CZ PHE A 282 10663 7807 7367 176 23 375 C ATOM 2992 N THR A 283 9.869 2.239 38.534 1.00 61.19 N ANISOU 2992 N THR A 283 9615 7117 6516 85 -169 447 N ATOM 2993 CA ATHR A 283 10.332 1.140 39.389 0.50 61.11 C ANISOU 2993 CA ATHR A 283 9606 7163 6450 164 -165 487 C ATOM 2994 CA BTHR A 283 10.373 1.121 39.335 0.50 61.07 C ANISOU 2994 CA BTHR A 283 9597 7159 6446 163 -166 488 C ATOM 2995 C THR A 283 11.645 1.521 40.089 1.00 64.78 C ANISOU 2995 C THR A 283 10032 7747 6835 162 -241 462 C ATOM 2996 O THR A 283 11.859 1.066 41.204 1.00 64.68 O ANISOU 2996 O THR A 283 10043 7790 6742 235 -250 480 O ATOM 2997 CB ATHR A 283 10.414 -0.215 38.642 0.50 67.71 C ANISOU 2997 CB ATHR A 283 10421 7981 7324 212 -120 540 C ATOM 2998 CB BTHR A 283 10.626 -0.095 38.431 0.50 67.28 C ANISOU 2998 CB BTHR A 283 10349 7937 7276 201 -133 535 C ATOM 2999 OG1ATHR A 283 11.014 -1.196 39.490 0.50 67.58 O ANISOU 2999 OG1ATHR A 283 10428 8015 7235 309 -116 585 O ATOM 3000 OG1BTHR A 283 11.574 0.256 37.422 0.50 67.76 O ANISOU 3000 OG1BTHR A 283 10334 8045 7366 153 -178 519 O ATOM 3001 CG2ATHR A 283 11.178 -0.146 37.343 0.50 65.90 C ANISOU 3001 CG2ATHR A 283 10116 7776 7145 171 -148 535 C ATOM 3002 CG2BTHR A 283 9.361 -0.595 37.774 0.50 63.95 C ANISOU 3002 CG2BTHR A 283 9955 7421 6922 190 -54 546 C ATOM 3003 N LEU A 284 12.491 2.377 39.465 1.00 60.63 N ANISOU 3003 N LEU A 284 9448 7268 6320 74 -291 415 N ATOM 3004 CA ALEU A 284 13.752 2.878 40.028 0.50 61.25 C ANISOU 3004 CA ALEU A 284 9467 7485 6320 36 -361 365 C ATOM 3005 CA BLEU A 284 13.732 2.801 40.105 0.50 61.29 C ANISOU 3005 CA BLEU A 284 9475 7493 6321 46 -360 368 C ATOM 3006 C LEU A 284 13.453 3.832 41.194 1.00 65.75 C ANISOU 3006 C LEU A 284 10100 8054 6826 -1 -379 309 C ATOM 3007 O LEU A 284 14.223 3.909 42.149 1.00 67.31 O ANISOU 3007 O LEU A 284 10264 8380 6929 10 -430 275 O ATOM 3008 CB ALEU A 284 14.556 3.594 38.902 0.50 61.31 C ANISOU 3008 CB ALEU A 284 9408 7519 6367 -80 -384 321 C ATOM 3009 CB BLEU A 284 14.763 3.317 39.090 0.50 61.49 C ANISOU 3009 CB BLEU A 284 9413 7578 6371 -53 -393 328 C ATOM 3010 CG ALEU A 284 15.872 4.378 39.185 0.50 67.07 C ANISOU 3010 CG ALEU A 284 10061 8394 7028 -182 -445 239 C ATOM 3011 CG BLEU A 284 15.513 2.229 38.297 0.50 66.01 C ANISOU 3011 CG BLEU A 284 9897 8222 6961 11 -396 374 C ATOM 3012 CD1ALEU A 284 15.613 5.813 39.648 0.50 67.72 C ANISOU 3012 CD1ALEU A 284 10224 8417 7088 -307 -443 160 C ATOM 3013 CD1BLEU A 284 16.203 2.813 37.093 0.50 66.08 C ANISOU 3013 CD1BLEU A 284 9838 8253 7016 -100 -406 339 C ATOM 3014 CD2ALEU A 284 16.867 3.605 40.047 0.50 70.45 C ANISOU 3014 CD2ALEU A 284 10396 9016 7355 -93 -501 240 C ATOM 3015 CD2BLEU A 284 16.528 1.488 39.169 0.50 69.18 C ANISOU 3015 CD2BLEU A 284 10229 8798 7259 114 -445 383 C ATOM 3016 N CYS A 285 12.333 4.571 41.096 1.00 60.74 N ANISOU 3016 N CYS A 285 9556 7287 6236 -38 -337 296 N ATOM 3017 CA CYS A 285 11.912 5.559 42.084 1.00 60.51 C ANISOU 3017 CA CYS A 285 9607 7230 6154 -71 -340 241 C ATOM 3018 C CYS A 285 11.084 4.935 43.225 1.00 64.78 C ANISOU 3018 C CYS A 285 10202 7762 6650 35 -313 277 C ATOM 3019 O CYS A 285 11.150 5.434 44.349 1.00 64.98 O ANISOU 3019 O CYS A 285 10267 7827 6595 31 -336 235 O ATOM 3020 CB CYS A 285 11.136 6.684 41.407 1.00 60.26 C ANISOU 3020 CB CYS A 285 9656 7063 6178 -137 -302 212 C ATOM 3021 SG CYS A 285 12.136 7.749 40.333 1.00 64.20 S ANISOU 3021 SG CYS A 285 10141 7552 6701 -287 -319 154 S ATOM 3022 N TRP A 286 10.289 3.879 42.946 1.00 61.39 N ANISOU 3022 N TRP A 286 9781 7279 6266 116 -258 348 N ATOM 3023 CA TRP A 286 9.413 3.280 43.959 1.00 61.55 C ANISOU 3023 CA TRP A 286 9864 7277 6246 198 -210 382 C ATOM 3024 C TRP A 286 9.951 2.019 44.630 1.00 66.62 C ANISOU 3024 C TRP A 286 10499 7992 6822 298 -209 441 C ATOM 3025 O TRP A 286 9.661 1.815 45.808 1.00 67.01 O ANISOU 3025 O TRP A 286 10606 8060 6793 358 -194 452 O ATOM 3026 CB TRP A 286 8.035 2.980 43.376 1.00 59.60 C ANISOU 3026 CB TRP A 286 9646 6925 6075 209 -130 407 C ATOM 3027 CG TRP A 286 7.193 4.209 43.236 1.00 60.68 C ANISOU 3027 CG TRP A 286 9823 6998 6233 168 -120 356 C ATOM 3028 CD1 TRP A 286 6.870 4.848 42.078 1.00 63.09 C ANISOU 3028 CD1 TRP A 286 10117 7247 6606 128 -114 338 C ATOM 3029 CD2 TRP A 286 6.650 5.007 44.300 1.00 61.23 C ANISOU 3029 CD2 TRP A 286 9965 7055 6243 179 -114 316 C ATOM 3030 NE1 TRP A 286 6.087 5.947 42.346 1.00 62.70 N ANISOU 3030 NE1 TRP A 286 10135 7147 6541 129 -99 296 N ATOM 3031 CE2 TRP A 286 5.945 6.075 43.704 1.00 64.81 C ANISOU 3031 CE2 TRP A 286 10455 7438 6734 155 -99 279 C ATOM 3032 CE3 TRP A 286 6.666 4.907 45.704 1.00 63.25 C ANISOU 3032 CE3 TRP A 286 10268 7355 6409 219 -117 311 C ATOM 3033 CZ2 TRP A 286 5.277 7.045 44.460 1.00 64.66 C ANISOU 3033 CZ2 TRP A 286 10517 7383 6667 172 -84 234 C ATOM 3034 CZ3 TRP A 286 6.007 5.871 46.451 1.00 65.08 C ANISOU 3034 CZ3 TRP A 286 10572 7556 6598 221 -105 262 C ATOM 3035 CH2 TRP A 286 5.339 6.935 45.830 1.00 65.49 C ANISOU 3035 CH2 TRP A 286 10661 7531 6691 198 -88 223 C ATOM 3036 N LEU A 287 10.715 1.182 43.905 1.00 63.66 N ANISOU 3036 N LEU A 287 10065 7654 6468 329 -218 481 N ATOM 3037 CA LEU A 287 11.288 -0.066 44.426 1.00 64.41 C ANISOU 3037 CA LEU A 287 10171 7810 6492 451 -209 546 C ATOM 3038 C LEU A 287 12.068 0.130 45.755 1.00 69.65 C ANISOU 3038 C LEU A 287 10833 8612 7019 515 -274 528 C ATOM 3039 O LEU A 287 11.818 -0.673 46.656 1.00 69.56 O ANISOU 3039 O LEU A 287 10898 8598 6933 626 -234 584 O ATOM 3040 CB LEU A 287 12.188 -0.749 43.380 1.00 64.43 C ANISOU 3040 CB LEU A 287 10100 7852 6529 475 -225 575 C ATOM 3041 CG LEU A 287 12.549 -2.209 43.605 1.00 70.15 C ANISOU 3041 CG LEU A 287 10865 8589 7199 619 -184 658 C ATOM 3042 CD1 LEU A 287 11.356 -3.132 43.344 1.00 70.16 C ANISOU 3042 CD1 LEU A 287 10969 8428 7260 630 -63 711 C ATOM 3043 CD2 LEU A 287 13.729 -2.603 42.741 1.00 72.40 C ANISOU 3043 CD2 LEU A 287 11057 8963 7490 653 -227 667 C ATOM 3044 N PRO A 288 12.957 1.157 45.949 1.00 67.03 N ANISOU 3044 N PRO A 288 10426 8402 6642 444 -364 448 N ATOM 3045 CA PRO A 288 13.660 1.272 47.245 1.00 68.17 C ANISOU 3045 CA PRO A 288 10557 8701 6642 508 -426 422 C ATOM 3046 C PRO A 288 12.714 1.486 48.431 1.00 72.30 C ANISOU 3046 C PRO A 288 11191 9169 7111 537 -390 422 C ATOM 3047 O PRO A 288 12.961 0.933 49.501 1.00 72.97 O ANISOU 3047 O PRO A 288 11309 9340 7076 656 -400 455 O ATOM 3048 CB PRO A 288 14.586 2.478 47.046 1.00 70.29 C ANISOU 3048 CB PRO A 288 10727 9085 6894 372 -510 312 C ATOM 3049 CG PRO A 288 14.731 2.621 45.583 1.00 73.63 C ANISOU 3049 CG PRO A 288 11096 9443 7437 284 -496 310 C ATOM 3050 CD PRO A 288 13.413 2.214 45.018 1.00 67.98 C ANISOU 3050 CD PRO A 288 10472 8531 6827 301 -406 374 C ATOM 3051 N PHE A 289 11.621 2.248 48.231 1.00 68.21 N ANISOU 3051 N PHE A 289 10732 8513 6672 444 -343 391 N ATOM 3052 CA PHE A 289 10.614 2.500 49.258 1.00 68.15 C ANISOU 3052 CA PHE A 289 10824 8447 6623 466 -299 388 C ATOM 3053 C PHE A 289 9.819 1.225 49.549 1.00 73.65 C ANISOU 3053 C PHE A 289 11599 9068 7315 574 -204 485 C ATOM 3054 O PHE A 289 9.555 0.930 50.717 1.00 73.97 O ANISOU 3054 O PHE A 289 11713 9133 7258 653 -181 508 O ATOM 3055 CB PHE A 289 9.668 3.649 48.839 1.00 68.79 C ANISOU 3055 CB PHE A 289 10941 8410 6787 357 -270 329 C ATOM 3056 CG PHE A 289 8.407 3.771 49.667 1.00 69.89 C ANISOU 3056 CG PHE A 289 11175 8474 6904 391 -203 334 C ATOM 3057 CD1 PHE A 289 8.422 4.419 50.898 1.00 73.68 C ANISOU 3057 CD1 PHE A 289 11706 9006 7282 399 -229 283 C ATOM 3058 CD2 PHE A 289 7.207 3.230 49.222 1.00 70.68 C ANISOU 3058 CD2 PHE A 289 11307 8468 7080 408 -111 381 C ATOM 3059 CE1 PHE A 289 7.259 4.515 51.671 1.00 74.39 C ANISOU 3059 CE1 PHE A 289 11881 9035 7347 435 -162 288 C ATOM 3060 CE2 PHE A 289 6.049 3.322 49.997 1.00 73.48 C ANISOU 3060 CE2 PHE A 289 11734 8776 7408 436 -43 379 C ATOM 3061 CZ PHE A 289 6.081 3.968 51.215 1.00 72.47 C ANISOU 3061 CZ PHE A 289 11661 8695 7181 454 -68 336 C ATOM 3062 N PHE A 290 9.416 0.489 48.496 1.00 70.53 N ANISOU 3062 N PHE A 290 11198 8579 7020 568 -142 535 N ATOM 3063 CA PHE A 290 8.623 -0.726 48.659 1.00 70.95 C ANISOU 3063 CA PHE A 290 11337 8543 7077 636 -32 614 C ATOM 3064 C PHE A 290 9.453 -1.898 49.206 1.00 79.33 C ANISOU 3064 C PHE A 290 12442 9665 8037 779 -27 692 C ATOM 3065 O PHE A 290 8.873 -2.798 49.819 1.00 79.50 O ANISOU 3065 O PHE A 290 12576 9620 8012 851 68 757 O ATOM 3066 CB PHE A 290 7.909 -1.104 47.361 1.00 71.16 C ANISOU 3066 CB PHE A 290 11343 8458 7235 569 36 626 C ATOM 3067 CG PHE A 290 6.636 -0.317 47.140 1.00 71.49 C ANISOU 3067 CG PHE A 290 11386 8431 7345 482 76 574 C ATOM 3068 CD1 PHE A 290 5.435 -0.731 47.706 1.00 74.15 C ANISOU 3068 CD1 PHE A 290 11794 8709 7672 488 178 588 C ATOM 3069 CD2 PHE A 290 6.637 0.835 46.362 1.00 72.27 C ANISOU 3069 CD2 PHE A 290 11421 8530 7510 402 19 511 C ATOM 3070 CE1 PHE A 290 4.260 -0.001 47.505 1.00 74.10 C ANISOU 3070 CE1 PHE A 290 11771 8668 7715 427 212 535 C ATOM 3071 CE2 PHE A 290 5.459 1.558 46.153 1.00 74.24 C ANISOU 3071 CE2 PHE A 290 11677 8725 7807 356 57 468 C ATOM 3072 CZ PHE A 290 4.279 1.136 46.727 1.00 72.38 C ANISOU 3072 CZ PHE A 290 11489 8455 7556 374 148 478 C ATOM 3073 N ILE A 291 10.796 -1.870 49.026 1.00 78.68 N ANISOU 3073 N ILE A 291 12275 9713 7906 826 -122 685 N ATOM 3074 CA ILE A 291 11.706 -2.883 49.571 1.00 80.69 C ANISOU 3074 CA ILE A 291 12559 10059 8040 995 -133 755 C ATOM 3075 C ILE A 291 11.849 -2.625 51.077 1.00 88.62 C ANISOU 3075 C ILE A 291 13611 11167 8893 1077 -168 748 C ATOM 3076 O ILE A 291 11.670 -3.553 51.865 1.00 89.53 O ANISOU 3076 O ILE A 291 13846 11258 8913 1214 -102 829 O ATOM 3077 CB ILE A 291 13.075 -2.912 48.820 1.00 84.05 C ANISOU 3077 CB ILE A 291 12854 10621 8460 1021 -225 739 C ATOM 3078 CG1 ILE A 291 12.958 -3.733 47.512 1.00 83.79 C ANISOU 3078 CG1 ILE A 291 12824 10474 8538 1012 -160 787 C ATOM 3079 CG2 ILE A 291 14.225 -3.435 49.715 1.00 86.27 C ANISOU 3079 CG2 ILE A 291 13121 11091 8569 1205 -288 772 C ATOM 3080 CD1 ILE A 291 14.168 -3.668 46.546 1.00 90.87 C ANISOU 3080 CD1 ILE A 291 13581 11487 9457 1011 -239 762 C ATOM 3081 N VAL A 292 12.115 -1.356 51.474 1.00 87.12 N ANISOU 3081 N VAL A 292 13344 11081 8678 988 -261 649 N ATOM 3082 CA VAL A 292 12.266 -0.959 52.879 1.00 88.99 C ANISOU 3082 CA VAL A 292 13612 11431 8768 1046 -304 620 C ATOM 3083 C VAL A 292 10.929 -1.148 53.647 1.00 94.51 C ANISOU 3083 C VAL A 292 14458 11992 9461 1058 -196 659 C ATOM 3084 O VAL A 292 10.940 -1.257 54.873 1.00 95.04 O ANISOU 3084 O VAL A 292 14593 12127 9391 1153 -198 675 O ATOM 3085 CB VAL A 292 12.842 0.479 53.014 1.00 93.28 C ANISOU 3085 CB VAL A 292 14047 12101 9295 917 -415 488 C ATOM 3086 CG1 VAL A 292 11.749 1.545 53.128 1.00 92.41 C ANISOU 3086 CG1 VAL A 292 13991 11863 9257 780 -379 424 C ATOM 3087 CG2 VAL A 292 13.805 0.565 54.186 1.00 94.86 C ANISOU 3087 CG2 VAL A 292 14208 12526 9309 1014 -505 455 C ATOM 3088 N ASN A 293 9.799 -1.219 52.914 1.00 91.64 N ANISOU 3088 N ASN A 293 14134 11451 9234 965 -101 671 N ATOM 3089 CA ASN A 293 8.472 -1.427 53.484 1.00 92.14 C ANISOU 3089 CA ASN A 293 14313 11394 9304 957 13 698 C ATOM 3090 C ASN A 293 8.283 -2.896 53.888 1.00 98.40 C ANISOU 3090 C ASN A 293 15235 12122 10030 1083 123 812 C ATOM 3091 O ASN A 293 7.735 -3.162 54.960 1.00 98.72 O ANISOU 3091 O ASN A 293 15388 12143 9980 1141 189 845 O ATOM 3092 CB ASN A 293 7.386 -0.992 52.495 1.00 91.27 C ANISOU 3092 CB ASN A 293 14174 11154 9349 818 70 660 C ATOM 3093 CG ASN A 293 6.070 -0.645 53.149 1.00107.94 C ANISOU 3093 CG ASN A 293 16354 13198 11459 780 151 638 C ATOM 3094 OD1 ASN A 293 5.996 0.192 54.057 1.00 96.42 O ANISOU 3094 OD1 ASN A 293 14911 11795 9928 782 111 588 O ATOM 3095 ND2 ASN A 293 4.995 -1.260 52.679 1.00100.63 N ANISOU 3095 ND2 ASN A 293 15463 12163 10610 738 269 666 N ATOM 3096 N ILE A 294 8.751 -3.843 53.042 1.00 96.23 N ANISOU 3096 N ILE A 294 14961 11808 9796 1128 150 872 N ATOM 3097 CA ILE A 294 8.635 -5.288 53.293 1.00 97.83 C ANISOU 3097 CA ILE A 294 15314 11920 9938 1248 271 983 C ATOM 3098 C ILE A 294 9.827 -5.815 54.139 1.00104.98 C ANISOU 3098 C ILE A 294 16262 12960 10665 1458 212 1046 C ATOM 3099 O ILE A 294 9.871 -7.007 54.442 1.00105.36 O ANISOU 3099 O ILE A 294 16460 12936 10634 1594 311 1148 O ATOM 3100 CB ILE A 294 8.426 -6.122 51.992 1.00100.39 C ANISOU 3100 CB ILE A 294 15647 12113 10385 1197 353 1015 C ATOM 3101 CG1 ILE A 294 9.543 -5.903 50.949 1.00100.52 C ANISOU 3101 CG1 ILE A 294 15522 12218 10454 1201 239 989 C ATOM 3102 CG2 ILE A 294 7.045 -5.875 51.391 1.00100.01 C ANISOU 3102 CG2 ILE A 294 15589 11938 10472 1021 443 966 C ATOM 3103 CD1 ILE A 294 10.512 -7.046 50.826 1.00110.36 C ANISOU 3103 CD1 ILE A 294 16827 13483 11621 1372 253 1076 C ATOM 3104 N VAL A 295 10.768 -4.931 54.526 1.00103.39 N ANISOU 3104 N VAL A 295 15935 12956 10391 1485 60 981 N ATOM 3105 CA VAL A 295 11.907 -5.269 55.389 1.00105.49 C ANISOU 3105 CA VAL A 295 16206 13407 10470 1685 -17 1018 C ATOM 3106 C VAL A 295 11.520 -4.884 56.827 1.00112.96 C ANISOU 3106 C VAL A 295 17229 14408 11284 1729 -17 1008 C ATOM 3107 O VAL A 295 11.846 -5.611 57.768 1.00114.19 O ANISOU 3107 O VAL A 295 17496 14621 11272 1923 7 1089 O ATOM 3108 CB VAL A 295 13.228 -4.605 54.906 1.00109.12 C ANISOU 3108 CB VAL A 295 16463 14081 10918 1676 -179 939 C ATOM 3109 CG1 VAL A 295 14.296 -4.583 56.000 1.00110.57 C ANISOU 3109 CG1 VAL A 295 16607 14515 10890 1852 -284 934 C ATOM 3110 CG2 VAL A 295 13.763 -5.310 53.664 1.00108.46 C ANISOU 3110 CG2 VAL A 295 16334 13960 10916 1703 -166 980 C ATOM 3111 N HIS A 296 10.774 -3.764 56.975 1.00110.85 N ANISOU 3111 N HIS A 296 16917 14113 11089 1560 -33 915 N ATOM 3112 CA HIS A 296 10.262 -3.217 58.238 1.00112.41 C ANISOU 3112 CA HIS A 296 17177 14347 11185 1566 -29 884 C ATOM 3113 C HIS A 296 9.374 -4.224 58.986 1.00117.79 C ANISOU 3113 C HIS A 296 18062 14894 11799 1660 129 993 C ATOM 3114 O HIS A 296 9.385 -4.236 60.218 1.00119.30 O ANISOU 3114 O HIS A 296 18335 15161 11834 1765 129 1012 O ATOM 3115 CB HIS A 296 9.469 -1.920 57.971 1.00112.49 C ANISOU 3115 CB HIS A 296 17120 14303 11318 1362 -46 771 C ATOM 3116 CG HIS A 296 8.868 -1.300 59.200 1.00116.95 C ANISOU 3116 CG HIS A 296 17751 14894 11790 1359 -34 732 C ATOM 3117 ND1 HIS A 296 9.613 -0.484 60.035 1.00119.87 N ANISOU 3117 ND1 HIS A 296 18063 15448 12034 1381 -154 651 N ATOM 3118 CD2 HIS A 296 7.615 -1.410 59.701 1.00118.85 C ANISOU 3118 CD2 HIS A 296 18105 15010 12043 1333 86 756 C ATOM 3119 CE1 HIS A 296 8.791 -0.121 61.006 1.00119.73 C ANISOU 3119 CE1 HIS A 296 18136 15399 11959 1375 -104 634 C ATOM 3120 NE2 HIS A 296 7.580 -0.655 60.850 1.00119.50 N ANISOU 3120 NE2 HIS A 296 18208 15190 12008 1351 41 697 N ATOM 3121 N VAL A 297 8.603 -5.046 58.246 1.00113.49 N ANISOU 3121 N VAL A 297 17600 14154 11366 1610 268 1055 N ATOM 3122 CA VAL A 297 7.680 -6.039 58.809 1.00114.12 C ANISOU 3122 CA VAL A 297 17881 14079 11400 1656 446 1148 C ATOM 3123 C VAL A 297 8.435 -7.186 59.522 1.00120.07 C ANISOU 3123 C VAL A 297 18788 14862 11970 1897 483 1272 C ATOM 3124 O VAL A 297 7.960 -7.658 60.559 1.00121.02 O ANISOU 3124 O VAL A 297 19079 14936 11969 1981 585 1337 O ATOM 3125 CB VAL A 297 6.673 -6.586 57.764 1.00116.96 C ANISOU 3125 CB VAL A 297 18276 14236 11927 1510 588 1159 C ATOM 3126 CG1 VAL A 297 5.644 -5.528 57.391 1.00115.36 C ANISOU 3126 CG1 VAL A 297 17965 14006 11860 1311 584 1052 C ATOM 3127 CG2 VAL A 297 7.373 -7.117 56.522 1.00116.25 C ANISOU 3127 CG2 VAL A 297 18128 14118 11922 1519 562 1181 C ATOM 3128 N ILE A 298 9.600 -7.610 58.985 1.00116.90 N ANISOU 3128 N ILE A 298 18332 14545 11538 2019 404 1304 N ATOM 3129 CA ILE A 298 10.416 -8.681 59.567 1.00118.68 C ANISOU 3129 CA ILE A 298 18697 14817 11579 2283 428 1423 C ATOM 3130 C ILE A 298 11.168 -8.130 60.799 1.00124.73 C ANISOU 3130 C ILE A 298 19417 15830 12146 2434 296 1401 C ATOM 3131 O ILE A 298 11.086 -8.726 61.874 1.00126.06 O ANISOU 3131 O ILE A 298 19760 15995 12140 2605 366 1489 O ATOM 3132 CB ILE A 298 11.355 -9.321 58.497 1.00121.62 C ANISOU 3132 CB ILE A 298 19017 15203 11990 2368 394 1459 C ATOM 3133 CG1 ILE A 298 10.565 -10.271 57.569 1.00121.06 C ANISOU 3133 CG1 ILE A 298 19081 14862 12055 2278 573 1516 C ATOM 3134 CG2 ILE A 298 12.525 -10.084 59.133 1.00124.77 C ANISOU 3134 CG2 ILE A 298 19489 15750 12170 2679 351 1554 C ATOM 3135 CD1 ILE A 298 10.157 -9.709 56.262 1.00123.04 C ANISOU 3135 CD1 ILE A 298 19173 15050 12527 2042 550 1423 C ATOM 3136 N GLN A 299 11.875 -6.997 60.640 1.00121.45 N ANISOU 3136 N GLN A 299 18774 15623 11750 2362 115 1279 N ATOM 3137 CA GLN A 299 12.603 -6.319 61.714 1.00122.91 C ANISOU 3137 CA GLN A 299 18877 16067 11756 2459 -24 1221 C ATOM 3138 C GLN A 299 12.266 -4.824 61.648 1.00126.10 C ANISOU 3138 C GLN A 299 19125 16523 12266 2220 -114 1064 C ATOM 3139 O GLN A 299 12.549 -4.167 60.644 1.00124.35 O ANISOU 3139 O GLN A 299 18741 16319 12186 2065 -187 977 O ATOM 3140 CB GLN A 299 14.123 -6.606 61.636 1.00125.62 C ANISOU 3140 CB GLN A 299 19103 16660 11965 2655 -157 1228 C ATOM 3141 CG GLN A 299 15.067 -5.607 62.342 1.00143.78 C ANISOU 3141 CG GLN A 299 21216 19286 14126 2674 -345 1106 C ATOM 3142 CD GLN A 299 14.988 -5.508 63.851 1.00166.63 C ANISOU 3142 CD GLN A 299 24201 22303 16808 2808 -359 1116 C ATOM 3143 OE1 GLN A 299 13.941 -5.222 64.443 1.00161.93 O ANISOU 3143 OE1 GLN A 299 23724 21568 16236 2717 -275 1115 O ATOM 3144 NE2 GLN A 299 16.140 -5.593 64.498 1.00162.00 N ANISOU 3144 NE2 GLN A 299 23528 22018 16005 3011 -484 1103 N ATOM 3145 N ASP A 300 11.622 -4.312 62.709 1.00123.78 N ANISOU 3145 N ASP A 300 18898 16234 11897 2194 -94 1033 N ATOM 3146 CA ASP A 300 11.168 -2.924 62.814 1.00123.13 C ANISOU 3146 CA ASP A 300 18718 16174 11893 1990 -153 893 C ATOM 3147 C ASP A 300 12.293 -1.929 63.136 1.00128.47 C ANISOU 3147 C ASP A 300 19219 17121 12475 1972 -336 764 C ATOM 3148 O ASP A 300 12.182 -0.757 62.768 1.00127.20 O ANISOU 3148 O ASP A 300 18951 16964 12417 1775 -395 636 O ATOM 3149 CB ASP A 300 10.072 -2.814 63.883 1.00125.43 C ANISOU 3149 CB ASP A 300 19158 16377 12124 1986 -54 910 C ATOM 3150 N ASN A 301 13.354 -2.383 63.830 1.00127.21 N ANISOU 3150 N ASN A 301 19035 17190 12111 2177 -418 792 N ATOM 3151 CA ASN A 301 14.471 -1.536 64.259 1.00128.29 C ANISOU 3151 CA ASN A 301 18996 17627 12123 2169 -590 659 C ATOM 3152 C ASN A 301 15.605 -1.402 63.213 1.00132.29 C ANISOU 3152 C ASN A 301 19302 18276 12686 2124 -696 600 C ATOM 3153 O ASN A 301 16.503 -0.581 63.418 1.00133.03 O ANISOU 3153 O ASN A 301 19226 18617 12702 2059 -832 464 O ATOM 3154 CB ASN A 301 15.049 -2.071 65.568 1.00131.06 C ANISOU 3154 CB ASN A 301 19401 18195 12202 2425 -633 709 C ATOM 3155 N LEU A 302 15.557 -2.171 62.101 1.00127.50 N ANISOU 3155 N LEU A 302 18711 17520 12212 2141 -630 690 N ATOM 3156 CA LEU A 302 16.587 -2.169 61.048 1.00126.84 C ANISOU 3156 CA LEU A 302 18450 17558 12186 2113 -713 649 C ATOM 3157 C LEU A 302 16.711 -0.841 60.291 1.00128.65 C ANISOU 3157 C LEU A 302 18520 17799 12563 1828 -782 490 C ATOM 3158 O LEU A 302 17.809 -0.517 59.831 1.00128.78 O ANISOU 3158 O LEU A 302 18353 18021 12558 1789 -888 407 O ATOM 3159 CB LEU A 302 16.321 -3.280 60.026 1.00125.95 C ANISOU 3159 CB LEU A 302 18422 17240 12193 2182 -606 782 C ATOM 3160 N ILE A 303 15.599 -0.097 60.129 1.00122.81 N ANISOU 3160 N ILE A 303 17854 16841 11967 1636 -714 450 N ATOM 3161 CA ILE A 303 15.597 1.158 59.372 1.00121.07 C ANISOU 3161 CA ILE A 303 17528 16584 11888 1377 -755 314 C ATOM 3162 C ILE A 303 14.795 2.255 60.078 1.00123.31 C ANISOU 3162 C ILE A 303 17882 16796 12176 1240 -740 223 C ATOM 3163 O ILE A 303 13.708 2.007 60.608 1.00122.51 O ANISOU 3163 O ILE A 303 17930 16536 12081 1286 -645 289 O ATOM 3164 CB ILE A 303 15.108 0.948 57.916 1.00122.38 C ANISOU 3164 CB ILE A 303 17699 16528 12272 1277 -681 363 C ATOM 3165 CG1 ILE A 303 14.032 -0.166 57.807 1.00121.95 C ANISOU 3165 CG1 ILE A 303 17812 16244 12278 1384 -540 514 C ATOM 3166 CG2 ILE A 303 16.295 0.653 57.003 1.00123.50 C ANISOU 3166 CG2 ILE A 303 17686 16813 12428 1292 -751 352 C ATOM 3167 CD1 ILE A 303 12.595 0.320 57.867 1.00127.54 C ANISOU 3167 CD1 ILE A 303 18633 16732 13096 1264 -442 506 C ATOM 3168 N ARG A 304 15.356 3.476 60.062 1.00118.97 N ANISOU 3168 N ARG A 304 17225 16361 11617 1065 -825 64 N ATOM 3169 CA ARG A 304 14.819 4.678 60.701 1.00118.28 C ANISOU 3169 CA ARG A 304 17194 16228 11518 921 -824 -52 C ATOM 3170 C ARG A 304 13.611 5.262 59.948 1.00118.24 C ANISOU 3170 C ARG A 304 17287 15932 11708 780 -725 -47 C ATOM 3171 O ARG A 304 13.329 4.856 58.820 1.00116.59 O ANISOU 3171 O ARG A 304 17070 15581 11647 761 -675 23 O ATOM 3172 CB ARG A 304 15.928 5.737 60.813 1.00120.10 C ANISOU 3172 CB ARG A 304 17284 16676 11674 765 -937 -231 C ATOM 3173 CG ARG A 304 16.028 6.366 62.195 1.00132.13 C ANISOU 3173 CG ARG A 304 18833 18349 13021 760 -986 -336 C ATOM 3174 N LYS A 305 12.900 6.214 60.588 1.00113.23 N ANISOU 3174 N LYS A 305 16743 15220 11061 695 -699 -125 N ATOM 3175 CA LYS A 305 11.731 6.898 60.026 1.00110.95 C ANISOU 3175 CA LYS A 305 16549 14682 10924 585 -610 -134 C ATOM 3176 C LYS A 305 12.145 7.986 59.027 1.00112.90 C ANISOU 3176 C LYS A 305 16741 14880 11275 386 -638 -243 C ATOM 3177 O LYS A 305 11.367 8.320 58.131 1.00111.32 O ANISOU 3177 O LYS A 305 16592 14482 11224 321 -570 -222 O ATOM 3178 CB LYS A 305 10.875 7.512 61.144 1.00113.84 C ANISOU 3178 CB LYS A 305 17039 14999 11217 591 -570 -180 C ATOM 3179 N GLU A 306 13.366 8.537 59.188 1.00109.22 N ANISOU 3179 N GLU A 306 16173 14605 10722 289 -733 -363 N ATOM 3180 CA GLU A 306 13.933 9.589 58.337 1.00108.04 C ANISOU 3180 CA GLU A 306 15975 14430 10644 79 -755 -480 C ATOM 3181 C GLU A 306 14.225 9.076 56.928 1.00107.85 C ANISOU 3181 C GLU A 306 15868 14353 10757 64 -745 -408 C ATOM 3182 O GLU A 306 14.024 9.819 55.969 1.00106.56 O ANISOU 3182 O GLU A 306 15735 14038 10713 -75 -706 -444 O ATOM 3183 CB GLU A 306 15.217 10.171 58.959 1.00111.35 C ANISOU 3183 CB GLU A 306 16287 15106 10914 -28 -854 -636 C ATOM 3184 CG GLU A 306 14.981 11.196 60.060 1.00122.62 C ANISOU 3184 CG GLU A 306 17810 16544 12235 -112 -855 -765 C ATOM 3185 CD GLU A 306 14.457 10.695 61.395 1.00143.76 C ANISOU 3185 CD GLU A 306 20554 19286 14782 63 -857 -717 C ATOM 3186 OE1 GLU A 306 14.712 9.519 61.747 1.00137.06 O ANISOU 3186 OE1 GLU A 306 19643 18574 13858 252 -890 -611 O ATOM 3187 OE2 GLU A 306 13.800 11.494 62.101 1.00139.09 O ANISOU 3187 OE2 GLU A 306 20090 18603 14153 16 -819 -786 O ATOM 3188 N VAL A 307 14.703 7.819 56.801 1.00102.44 N ANISOU 3188 N VAL A 307 15092 13787 10044 214 -774 -305 N ATOM 3189 CA VAL A 307 15.016 7.218 55.498 1.00100.29 C ANISOU 3189 CA VAL A 307 14740 13475 9890 217 -764 -234 C ATOM 3190 C VAL A 307 13.730 6.723 54.811 1.00 99.65 C ANISOU 3190 C VAL A 307 14764 13142 9956 277 -661 -111 C ATOM 3191 O VAL A 307 13.715 6.608 53.589 1.00 98.26 O ANISOU 3191 O VAL A 307 14555 12874 9907 228 -636 -78 O ATOM 3192 CB VAL A 307 16.106 6.104 55.541 1.00105.10 C ANISOU 3192 CB VAL A 307 15213 14312 10408 358 -833 -181 C ATOM 3193 CG1 VAL A 307 17.458 6.667 55.971 1.00106.79 C ANISOU 3193 CG1 VAL A 307 15279 14809 10486 273 -940 -323 C ATOM 3194 CG2 VAL A 307 15.699 4.926 56.421 1.00105.27 C ANISOU 3194 CG2 VAL A 307 15303 14357 10336 593 -809 -57 C ATOM 3195 N TYR A 308 12.662 6.447 55.587 1.00 94.08 N ANISOU 3195 N TYR A 308 14177 12342 9227 374 -600 -54 N ATOM 3196 CA TYR A 308 11.375 5.971 55.070 1.00 91.66 C ANISOU 3196 CA TYR A 308 13958 11829 9041 423 -497 45 C ATOM 3197 C TYR A 308 10.659 7.072 54.268 1.00 92.99 C ANISOU 3197 C TYR A 308 14174 11824 9332 287 -454 -11 C ATOM 3198 O TYR A 308 10.115 6.793 53.197 1.00 91.35 O ANISOU 3198 O TYR A 308 13964 11493 9252 280 -403 46 O ATOM 3199 CB TYR A 308 10.486 5.466 56.220 1.00 93.05 C ANISOU 3199 CB TYR A 308 14239 11977 9138 546 -439 102 C ATOM 3200 CG TYR A 308 9.219 4.771 55.769 1.00 93.72 C ANISOU 3200 CG TYR A 308 14393 11888 9326 596 -327 201 C ATOM 3201 CD1 TYR A 308 9.222 3.420 55.434 1.00 95.65 C ANISOU 3201 CD1 TYR A 308 14635 12117 9590 697 -282 314 C ATOM 3202 CD2 TYR A 308 8.007 5.456 55.711 1.00 93.65 C ANISOU 3202 CD2 TYR A 308 14458 11741 9385 544 -258 174 C ATOM 3203 CE1 TYR A 308 8.056 2.772 55.030 1.00 95.92 C ANISOU 3203 CE1 TYR A 308 14729 12002 9713 715 -169 388 C ATOM 3204 CE2 TYR A 308 6.834 4.818 55.313 1.00 93.55 C ANISOU 3204 CE2 TYR A 308 14485 11604 9456 579 -155 248 C ATOM 3205 CZ TYR A 308 6.862 3.474 54.978 1.00101.76 C ANISOU 3205 CZ TYR A 308 15515 12633 10518 651 -109 350 C ATOM 3206 OH TYR A 308 5.708 2.843 54.583 1.00103.02 O ANISOU 3206 OH TYR A 308 15709 12679 10755 659 1 405 O ATOM 3207 N ILE A 309 10.664 8.313 54.788 1.00 89.15 N ANISOU 3207 N ILE A 309 13740 11333 8799 188 -472 -124 N ATOM 3208 CA ILE A 309 10.047 9.482 54.154 1.00 88.15 C ANISOU 3208 CA ILE A 309 13692 11041 8762 77 -428 -183 C ATOM 3209 C ILE A 309 10.886 9.887 52.920 1.00 90.86 C ANISOU 3209 C ILE A 309 13965 11377 9182 -49 -457 -219 C ATOM 3210 O ILE A 309 10.309 10.246 51.886 1.00 90.41 O ANISOU 3210 O ILE A 309 13947 11168 9238 -84 -406 -198 O ATOM 3211 CB ILE A 309 9.871 10.645 55.185 1.00 92.40 C ANISOU 3211 CB ILE A 309 14332 11570 9206 18 -429 -296 C ATOM 3212 CG1 ILE A 309 8.861 10.252 56.291 1.00 92.89 C ANISOU 3212 CG1 ILE A 309 14471 11618 9204 149 -383 -250 C ATOM 3213 CG2 ILE A 309 9.455 11.973 54.513 1.00 93.07 C ANISOU 3213 CG2 ILE A 309 14518 11482 9361 -98 -383 -368 C ATOM 3214 CD1 ILE A 309 9.098 10.905 57.659 1.00102.03 C ANISOU 3214 CD1 ILE A 309 15688 12865 10214 130 -415 -349 C ATOM 3215 N LEU A 310 12.233 9.791 53.022 1.00 86.29 N ANISOU 3215 N LEU A 310 13275 10977 8534 -108 -536 -273 N ATOM 3216 CA LEU A 310 13.174 10.130 51.947 1.00 85.28 C ANISOU 3216 CA LEU A 310 13063 10879 8461 -239 -564 -317 C ATOM 3217 C LEU A 310 12.945 9.255 50.702 1.00 86.61 C ANISOU 3217 C LEU A 310 13180 10974 8754 -175 -534 -203 C ATOM 3218 O LEU A 310 12.845 9.791 49.597 1.00 85.75 O ANISOU 3218 O LEU A 310 13091 10749 8743 -266 -501 -212 O ATOM 3219 CB LEU A 310 14.629 10.009 52.438 1.00 86.59 C ANISOU 3219 CB LEU A 310 13091 11302 8509 -288 -657 -396 C ATOM 3220 CG LEU A 310 15.732 10.437 51.458 1.00 91.62 C ANISOU 3220 CG LEU A 310 13624 12008 9179 -450 -685 -467 C ATOM 3221 CD1 LEU A 310 15.752 11.951 51.251 1.00 92.31 C ANISOU 3221 CD1 LEU A 310 13813 11979 9281 -663 -646 -595 C ATOM 3222 CD2 LEU A 310 17.081 9.962 51.934 1.00 95.80 C ANISOU 3222 CD2 LEU A 310 13978 12836 9585 -442 -779 -520 C ATOM 3223 N LEU A 311 12.826 7.928 50.887 1.00 81.66 N ANISOU 3223 N LEU A 311 12504 10406 8116 -19 -537 -98 N ATOM 3224 CA LEU A 311 12.580 6.977 49.801 1.00 79.67 C ANISOU 3224 CA LEU A 311 12212 10087 7970 46 -501 7 C ATOM 3225 C LEU A 311 11.160 7.150 49.235 1.00 80.99 C ANISOU 3225 C LEU A 311 12477 10049 8247 57 -415 52 C ATOM 3226 O LEU A 311 10.952 6.911 48.045 1.00 79.52 O ANISOU 3226 O LEU A 311 12265 9783 8165 43 -386 95 O ATOM 3227 CB LEU A 311 12.824 5.526 50.259 1.00 79.78 C ANISOU 3227 CB LEU A 311 12182 10203 7926 210 -511 101 C ATOM 3228 CG LEU A 311 14.267 5.166 50.667 1.00 85.20 C ANISOU 3228 CG LEU A 311 12750 11126 8498 244 -601 72 C ATOM 3229 CD1 LEU A 311 14.314 3.832 51.370 1.00 85.60 C ANISOU 3229 CD1 LEU A 311 12810 11252 8461 443 -596 172 C ATOM 3230 CD2 LEU A 311 15.218 5.174 49.476 1.00 86.82 C ANISOU 3230 CD2 LEU A 311 12834 11390 8762 168 -634 52 C ATOM 3231 N ASN A 312 10.201 7.610 50.070 1.00 76.64 N ANISOU 3231 N ASN A 312 12029 9427 7662 84 -377 35 N ATOM 3232 CA ASN A 312 8.827 7.889 49.640 1.00 75.06 C ANISOU 3232 CA ASN A 312 11908 9066 7544 105 -298 61 C ATOM 3233 C ASN A 312 8.817 9.133 48.749 1.00 78.12 C ANISOU 3233 C ASN A 312 12338 9352 7992 -4 -291 -1 C ATOM 3234 O ASN A 312 8.028 9.209 47.804 1.00 76.81 O ANISOU 3234 O ASN A 312 12192 9079 7915 13 -242 34 O ATOM 3235 CB ASN A 312 7.902 8.084 50.852 1.00 74.25 C ANISOU 3235 CB ASN A 312 11898 8942 7373 169 -260 51 C ATOM 3236 CG ASN A 312 6.423 7.834 50.604 1.00 84.37 C ANISOU 3236 CG ASN A 312 13222 10116 8717 236 -174 101 C ATOM 3237 OD1 ASN A 312 5.706 7.360 51.489 1.00 77.56 O ANISOU 3237 OD1 ASN A 312 12397 9265 7807 312 -130 129 O ATOM 3238 ND2 ASN A 312 5.909 8.176 49.425 1.00 70.05 N ANISOU 3238 ND2 ASN A 312 11403 8210 7003 211 -143 106 N ATOM 3239 N TRP A 313 9.707 10.099 49.052 1.00 74.81 N ANISOU 3239 N TRP A 313 11939 8973 7514 -117 -334 -97 N ATOM 3240 CA TRP A 313 9.853 11.341 48.300 1.00 74.22 C ANISOU 3240 CA TRP A 313 11934 8791 7475 -237 -315 -163 C ATOM 3241 C TRP A 313 10.612 11.113 46.992 1.00 76.20 C ANISOU 3241 C TRP A 313 12099 9054 7801 -305 -330 -141 C ATOM 3242 O TRP A 313 10.436 11.892 46.055 1.00 75.79 O ANISOU 3242 O TRP A 313 12113 8878 7805 -367 -292 -155 O ATOM 3243 CB TRP A 313 10.500 12.435 49.160 1.00 74.30 C ANISOU 3243 CB TRP A 313 12011 8831 7387 -356 -338 -286 C ATOM 3244 CG TRP A 313 9.461 13.239 49.879 1.00 75.51 C ANISOU 3244 CG TRP A 313 12317 8867 7504 -315 -285 -319 C ATOM 3245 CD1 TRP A 313 8.739 12.852 50.969 1.00 78.56 C ANISOU 3245 CD1 TRP A 313 12728 9287 7835 -203 -278 -298 C ATOM 3246 CD2 TRP A 313 8.917 14.498 49.463 1.00 75.59 C ANISOU 3246 CD2 TRP A 313 12487 8698 7535 -360 -221 -365 C ATOM 3247 NE1 TRP A 313 7.802 13.807 51.280 1.00 78.37 N ANISOU 3247 NE1 TRP A 313 12853 9129 7794 -179 -218 -335 N ATOM 3248 CE2 TRP A 313 7.899 14.838 50.382 1.00 79.79 C ANISOU 3248 CE2 TRP A 313 13124 9174 8017 -266 -183 -376 C ATOM 3249 CE3 TRP A 313 9.207 15.390 48.416 1.00 77.01 C ANISOU 3249 CE3 TRP A 313 12745 8755 7760 -464 -185 -396 C ATOM 3250 CZ2 TRP A 313 7.176 16.031 50.290 1.00 79.60 C ANISOU 3250 CZ2 TRP A 313 13279 8980 7985 -259 -114 -419 C ATOM 3251 CZ3 TRP A 313 8.492 16.573 48.329 1.00 79.04 C ANISOU 3251 CZ3 TRP A 313 13195 8830 8006 -458 -111 -433 C ATOM 3252 CH2 TRP A 313 7.492 16.885 49.260 1.00 80.02 C ANISOU 3252 CH2 TRP A 313 13420 8907 8079 -350 -79 -444 C ATOM 3253 N ILE A 314 11.414 10.029 46.914 1.00 72.16 N ANISOU 3253 N ILE A 314 11449 8685 7283 -276 -380 -100 N ATOM 3254 CA ILE A 314 12.130 9.603 45.703 1.00 71.58 C ANISOU 3254 CA ILE A 314 11278 8644 7277 -316 -394 -70 C ATOM 3255 C ILE A 314 11.054 9.073 44.726 1.00 74.03 C ANISOU 3255 C ILE A 314 11606 8828 7693 -228 -338 23 C ATOM 3256 O ILE A 314 11.147 9.297 43.519 1.00 72.89 O ANISOU 3256 O ILE A 314 11452 8621 7620 -276 -320 35 O ATOM 3257 CB ILE A 314 13.261 8.580 46.055 1.00 75.19 C ANISOU 3257 CB ILE A 314 11590 9304 7676 -279 -462 -55 C ATOM 3258 CG1 ILE A 314 14.503 9.331 46.595 1.00 77.14 C ANISOU 3258 CG1 ILE A 314 11785 9699 7826 -413 -521 -174 C ATOM 3259 CG2 ILE A 314 13.651 7.676 44.870 1.00 74.84 C ANISOU 3259 CG2 ILE A 314 11447 9281 7708 -246 -463 16 C ATOM 3260 CD1 ILE A 314 15.313 8.591 47.675 1.00 85.31 C ANISOU 3260 CD1 ILE A 314 12715 10960 8739 -335 -594 -186 C ATOM 3261 N GLY A 315 10.011 8.456 45.283 1.00 70.33 N ANISOU 3261 N GLY A 315 11169 8330 7224 -110 -306 77 N ATOM 3262 CA GLY A 315 8.848 7.994 44.539 1.00 69.07 C ANISOU 3262 CA GLY A 315 11022 8075 7146 -36 -247 143 C ATOM 3263 C GLY A 315 7.956 9.158 44.140 1.00 73.18 C ANISOU 3263 C GLY A 315 11645 8467 7692 -50 -203 111 C ATOM 3264 O GLY A 315 7.363 9.136 43.059 1.00 72.05 O ANISOU 3264 O GLY A 315 11498 8259 7621 -26 -170 144 O ATOM 3265 N TYR A 316 7.863 10.195 45.010 1.00 70.63 N ANISOU 3265 N TYR A 316 11423 8111 7302 -79 -201 44 N ATOM 3266 CA TYR A 316 7.062 11.402 44.771 1.00 70.91 C ANISOU 3266 CA TYR A 316 11587 8015 7340 -73 -153 11 C ATOM 3267 C TYR A 316 7.583 12.245 43.610 1.00 75.90 C ANISOU 3267 C TYR A 316 12265 8564 8010 -161 -144 -11 C ATOM 3268 O TYR A 316 6.775 12.784 42.859 1.00 75.74 O ANISOU 3268 O TYR A 316 12318 8438 8020 -107 -98 8 O ATOM 3269 CB TYR A 316 7.019 12.301 46.015 1.00 73.22 C ANISOU 3269 CB TYR A 316 11991 8288 7542 -95 -150 -65 C ATOM 3270 CG TYR A 316 6.114 11.866 47.148 1.00 74.62 C ANISOU 3270 CG TYR A 316 12178 8501 7673 11 -132 -50 C ATOM 3271 CD1 TYR A 316 4.985 11.088 46.906 1.00 75.47 C ANISOU 3271 CD1 TYR A 316 12240 8610 7825 122 -90 17 C ATOM 3272 CD2 TYR A 316 6.322 12.327 48.442 1.00 76.30 C ANISOU 3272 CD2 TYR A 316 12455 8744 7790 -10 -146 -113 C ATOM 3273 CE1 TYR A 316 4.125 10.725 47.941 1.00 75.94 C ANISOU 3273 CE1 TYR A 316 12313 8702 7838 206 -59 26 C ATOM 3274 CE2 TYR A 316 5.472 11.969 49.484 1.00 77.36 C ANISOU 3274 CE2 TYR A 316 12608 8909 7877 87 -121 -98 C ATOM 3275 CZ TYR A 316 4.371 11.170 49.229 1.00 83.97 C ANISOU 3275 CZ TYR A 316 13398 9744 8761 194 -74 -27 C ATOM 3276 OH TYR A 316 3.542 10.823 50.265 1.00 85.71 O ANISOU 3276 OH TYR A 316 13638 9998 8929 275 -38 -17 O ATOM 3277 N VAL A 317 8.921 12.399 43.487 1.00 73.22 N ANISOU 3277 N VAL A 317 11887 8279 7655 -294 -184 -53 N ATOM 3278 CA VAL A 317 9.546 13.218 42.437 1.00 73.58 C ANISOU 3278 CA VAL A 317 11983 8247 7726 -406 -164 -81 C ATOM 3279 C VAL A 317 9.389 12.560 41.048 1.00 76.61 C ANISOU 3279 C VAL A 317 12289 8623 8198 -360 -156 -3 C ATOM 3280 O VAL A 317 9.569 13.246 40.038 1.00 76.60 O ANISOU 3280 O VAL A 317 12353 8531 8222 -414 -123 -5 O ATOM 3281 CB VAL A 317 11.027 13.599 42.726 1.00 78.69 C ANISOU 3281 CB VAL A 317 12597 8979 8324 -583 -200 -167 C ATOM 3282 CG1 VAL A 317 11.135 14.513 43.943 1.00 79.75 C ANISOU 3282 CG1 VAL A 317 12840 9097 8366 -653 -195 -264 C ATOM 3283 CG2 VAL A 317 11.922 12.372 42.880 1.00 78.27 C ANISOU 3283 CG2 VAL A 317 12351 9119 8270 -581 -271 -144 C ATOM 3284 N ASN A 318 9.030 11.252 41.000 1.00 71.93 N ANISOU 3284 N ASN A 318 11571 8115 7644 -263 -177 65 N ATOM 3285 CA ASN A 318 8.796 10.500 39.760 1.00 70.69 C ANISOU 3285 CA ASN A 318 11335 7960 7565 -216 -168 132 C ATOM 3286 C ASN A 318 7.580 11.055 39.012 1.00 74.81 C ANISOU 3286 C ASN A 318 11940 8371 8113 -132 -116 156 C ATOM 3287 O ASN A 318 7.556 11.078 37.776 1.00 74.60 O ANISOU 3287 O ASN A 318 11900 8311 8132 -129 -101 186 O ATOM 3288 CB ASN A 318 8.597 9.017 40.059 1.00 68.90 C ANISOU 3288 CB ASN A 318 10989 7830 7358 -137 -185 186 C ATOM 3289 CG ASN A 318 8.276 8.197 38.840 1.00 82.55 C ANISOU 3289 CG ASN A 318 12644 9560 9163 -95 -169 244 C ATOM 3290 OD1 ASN A 318 7.107 7.937 38.527 1.00 71.65 O ANISOU 3290 OD1 ASN A 318 11267 8147 7810 -16 -131 270 O ATOM 3291 ND2 ASN A 318 9.308 7.862 38.081 1.00 74.92 N ANISOU 3291 ND2 ASN A 318 11606 8638 8224 -155 -194 253 N ATOM 3292 N SER A 319 6.586 11.515 39.784 1.00 71.21 N ANISOU 3292 N SER A 319 11567 7873 7618 -54 -88 140 N ATOM 3293 CA SER A 319 5.333 12.116 39.349 1.00 71.09 C ANISOU 3293 CA SER A 319 11631 7779 7600 58 -40 152 C ATOM 3294 C SER A 319 5.562 13.374 38.457 1.00 76.24 C ANISOU 3294 C SER A 319 12424 8305 8240 30 -8 139 C ATOM 3295 O SER A 319 4.640 13.807 37.762 1.00 75.76 O ANISOU 3295 O SER A 319 12420 8189 8176 143 29 164 O ATOM 3296 CB SER A 319 4.511 12.465 40.584 1.00 75.07 C ANISOU 3296 CB SER A 319 12203 8274 8045 129 -20 123 C ATOM 3297 OG SER A 319 3.249 13.027 40.283 1.00 86.62 O ANISOU 3297 OG SER A 319 13731 9688 9491 261 26 130 O ATOM 3298 N GLY A 320 6.787 13.911 38.467 1.00 74.06 N ANISOU 3298 N GLY A 320 12198 7993 7949 -118 -16 100 N ATOM 3299 CA GLY A 320 7.183 15.075 37.678 1.00 75.11 C ANISOU 3299 CA GLY A 320 12481 7992 8064 -181 30 83 C ATOM 3300 C GLY A 320 8.169 14.799 36.557 1.00 80.04 C ANISOU 3300 C GLY A 320 13036 8639 8735 -285 20 102 C ATOM 3301 O GLY A 320 8.453 15.698 35.758 1.00 80.63 O ANISOU 3301 O GLY A 320 13241 8598 8796 -335 71 99 O ATOM 3302 N PHE A 321 8.704 13.558 36.490 1.00 76.14 N ANISOU 3302 N PHE A 321 12353 8289 8289 -312 -37 125 N ATOM 3303 CA PHE A 321 9.671 13.142 35.470 1.00 75.65 C ANISOU 3303 CA PHE A 321 12200 8274 8270 -400 -51 143 C ATOM 3304 C PHE A 321 8.986 12.703 34.190 1.00 79.09 C ANISOU 3304 C PHE A 321 12599 8698 8756 -294 -36 212 C ATOM 3305 O PHE A 321 9.491 13.016 33.113 1.00 78.78 O ANISOU 3305 O PHE A 321 12585 8618 8731 -348 -13 226 O ATOM 3306 CB PHE A 321 10.588 12.013 35.982 1.00 76.97 C ANISOU 3306 CB PHE A 321 12189 8603 8451 -455 -115 135 C ATOM 3307 CG PHE A 321 11.502 12.377 37.131 1.00 79.51 C ANISOU 3307 CG PHE A 321 12513 8985 8711 -572 -142 57 C ATOM 3308 CD1 PHE A 321 12.021 13.664 37.252 1.00 84.13 C ANISOU 3308 CD1 PHE A 321 13231 9487 9249 -708 -104 -17 C ATOM 3309 CD2 PHE A 321 11.885 11.422 38.063 1.00 81.38 C ANISOU 3309 CD2 PHE A 321 12624 9368 8929 -549 -200 53 C ATOM 3310 CE1 PHE A 321 12.864 13.998 38.317 1.00 86.22 C ANISOU 3310 CE1 PHE A 321 13484 9829 9449 -831 -130 -106 C ATOM 3311 CE2 PHE A 321 12.729 11.757 39.127 1.00 85.39 C ANISOU 3311 CE2 PHE A 321 13119 9960 9364 -646 -232 -26 C ATOM 3312 CZ PHE A 321 13.213 13.042 39.246 1.00 84.87 C ANISOU 3312 CZ PHE A 321 13166 9827 9253 -794 -201 -111 C ATOM 3313 N ASN A 322 7.845 11.985 34.304 1.00 75.88 N ANISOU 3313 N ASN A 322 12129 8334 8368 -153 -45 248 N ATOM 3314 CA ASN A 322 7.053 11.468 33.181 1.00 75.50 C ANISOU 3314 CA ASN A 322 12022 8306 8357 -49 -35 299 C ATOM 3315 C ASN A 322 6.803 12.533 32.099 1.00 79.25 C ANISOU 3315 C ASN A 322 12631 8673 8808 -10 10 316 C ATOM 3316 O ASN A 322 7.111 12.231 30.947 1.00 78.87 O ANISOU 3316 O ASN A 322 12534 8643 8791 -22 10 347 O ATOM 3317 CB ASN A 322 5.722 10.859 33.654 1.00 78.56 C ANISOU 3317 CB ASN A 322 12354 8751 8746 81 -34 309 C ATOM 3318 CG ASN A 322 5.848 9.518 34.330 1.00108.89 C ANISOU 3318 CG ASN A 322 16058 12695 12618 62 -62 314 C ATOM 3319 OD1 ASN A 322 6.926 8.919 34.396 1.00102.42 O ANISOU 3319 OD1 ASN A 322 15173 11920 11821 -24 -90 317 O ATOM 3320 ND2 ASN A 322 4.738 9.013 34.843 1.00105.66 N ANISOU 3320 ND2 ASN A 322 15610 12332 12205 146 -46 314 N ATOM 3321 N PRO A 323 6.339 13.779 32.408 1.00 76.20 N ANISOU 3321 N PRO A 323 12426 8167 8360 37 54 299 N ATOM 3322 CA PRO A 323 6.136 14.774 31.334 1.00 76.75 C ANISOU 3322 CA PRO A 323 12649 8121 8393 93 108 327 C ATOM 3323 C PRO A 323 7.408 15.110 30.544 1.00 80.75 C ANISOU 3323 C PRO A 323 13200 8570 8911 -62 131 328 C ATOM 3324 O PRO A 323 7.325 15.297 29.329 1.00 80.09 O ANISOU 3324 O PRO A 323 13155 8452 8823 -15 157 371 O ATOM 3325 CB PRO A 323 5.618 15.997 32.088 1.00 79.56 C ANISOU 3325 CB PRO A 323 13209 8347 8673 152 158 300 C ATOM 3326 CG PRO A 323 4.994 15.438 33.312 1.00 83.54 C ANISOU 3326 CG PRO A 323 13621 8941 9181 201 122 273 C ATOM 3327 CD PRO A 323 5.905 14.334 33.709 1.00 78.17 C ANISOU 3327 CD PRO A 323 12766 8376 8561 64 66 259 C ATOM 3328 N LEU A 324 8.577 15.144 31.218 1.00 77.83 N ANISOU 3328 N LEU A 324 12812 8210 8549 -245 119 276 N ATOM 3329 CA LEU A 324 9.875 15.428 30.597 1.00 78.33 C ANISOU 3329 CA LEU A 324 12893 8250 8620 -421 143 258 C ATOM 3330 C LEU A 324 10.325 14.276 29.690 1.00 81.41 C ANISOU 3330 C LEU A 324 13091 8769 9073 -431 100 296 C ATOM 3331 O LEU A 324 10.988 14.523 28.681 1.00 80.97 O ANISOU 3331 O LEU A 324 13060 8683 9021 -507 133 310 O ATOM 3332 CB LEU A 324 10.952 15.709 31.660 1.00 79.15 C ANISOU 3332 CB LEU A 324 12994 8378 8703 -609 134 175 C ATOM 3333 CG LEU A 324 10.748 16.944 32.547 1.00 85.53 C ANISOU 3333 CG LEU A 324 14011 9045 9441 -647 189 117 C ATOM 3334 CD1 LEU A 324 11.520 16.811 33.845 1.00 86.30 C ANISOU 3334 CD1 LEU A 324 14033 9236 9519 -785 147 32 C ATOM 3335 CD2 LEU A 324 11.137 18.235 31.821 1.00 89.63 C ANISOU 3335 CD2 LEU A 324 14761 9379 9913 -744 292 104 C ATOM 3336 N ILE A 325 9.951 13.024 30.042 1.00 77.04 N ANISOU 3336 N ILE A 325 12358 8349 8564 -355 36 313 N ATOM 3337 CA ILE A 325 10.284 11.821 29.265 1.00 75.77 C ANISOU 3337 CA ILE A 325 12023 8304 8461 -349 0 346 C ATOM 3338 C ILE A 325 9.460 11.812 27.959 1.00 80.02 C ANISOU 3338 C ILE A 325 12585 8814 9006 -230 23 399 C ATOM 3339 O ILE A 325 9.937 11.276 26.958 1.00 79.89 O ANISOU 3339 O ILE A 325 12488 8845 9021 -256 19 423 O ATOM 3340 CB ILE A 325 10.110 10.507 30.089 1.00 77.71 C ANISOU 3340 CB ILE A 325 12109 8675 8740 -306 -56 346 C ATOM 3341 CG1 ILE A 325 10.924 10.549 31.402 1.00 78.40 C ANISOU 3341 CG1 ILE A 325 12177 8809 8802 -401 -85 294 C ATOM 3342 CG2 ILE A 325 10.494 9.264 29.267 1.00 77.30 C ANISOU 3342 CG2 ILE A 325 11905 8723 8742 -300 -81 377 C ATOM 3343 CD1 ILE A 325 10.357 9.721 32.559 1.00 82.97 C ANISOU 3343 CD1 ILE A 325 12690 9454 9379 -324 -118 295 C ATOM 3344 N TYR A 326 8.263 12.446 27.943 1.00 76.74 N ANISOU 3344 N TYR A 326 12279 8330 8550 -94 50 415 N ATOM 3345 CA TYR A 326 7.436 12.512 26.730 1.00 76.44 C ANISOU 3345 CA TYR A 326 12259 8289 8496 40 67 460 C ATOM 3346 C TYR A 326 8.064 13.414 25.656 1.00 80.64 C ANISOU 3346 C TYR A 326 12929 8715 8994 -6 121 485 C ATOM 3347 O TYR A 326 7.699 13.282 24.489 1.00 80.61 O ANISOU 3347 O TYR A 326 12913 8735 8981 81 129 526 O ATOM 3348 CB TYR A 326 5.992 12.945 27.032 1.00 77.92 C ANISOU 3348 CB TYR A 326 12510 8462 8632 219 78 465 C ATOM 3349 CG TYR A 326 5.266 12.008 27.972 1.00 79.17 C ANISOU 3349 CG TYR A 326 12529 8733 8820 262 38 439 C ATOM 3350 CD1 TYR A 326 5.303 10.628 27.781 1.00 80.20 C ANISOU 3350 CD1 TYR A 326 12473 8988 9012 233 2 439 C ATOM 3351 CD2 TYR A 326 4.528 12.498 29.040 1.00 80.73 C ANISOU 3351 CD2 TYR A 326 12794 8903 8978 331 49 416 C ATOM 3352 CE1 TYR A 326 4.641 9.761 28.649 1.00 80.89 C ANISOU 3352 CE1 TYR A 326 12455 9161 9120 260 -16 416 C ATOM 3353 CE2 TYR A 326 3.879 11.640 29.926 1.00 81.33 C ANISOU 3353 CE2 TYR A 326 12747 9079 9075 359 24 393 C ATOM 3354 CZ TYR A 326 3.945 10.271 29.732 1.00 88.63 C ANISOU 3354 CZ TYR A 326 13497 10117 10060 318 -5 394 C ATOM 3355 OH TYR A 326 3.290 9.429 30.599 1.00 90.78 O ANISOU 3355 OH TYR A 326 13673 10472 10347 336 -11 373 O ATOM 3356 N CYS A 327 9.055 14.261 26.028 1.00 77.65 N ANISOU 3356 N CYS A 327 12673 8234 8595 -157 162 457 N ATOM 3357 CA CYS A 327 9.791 15.134 25.106 1.00 78.52 C ANISOU 3357 CA CYS A 327 12930 8232 8671 -243 233 473 C ATOM 3358 C CYS A 327 10.578 14.301 24.086 1.00 80.23 C ANISOU 3358 C CYS A 327 12999 8548 8936 -315 213 492 C ATOM 3359 O CYS A 327 11.022 14.845 23.073 1.00 80.89 O ANISOU 3359 O CYS A 327 13181 8560 8992 -356 271 519 O ATOM 3360 CB CYS A 327 10.710 16.091 25.863 1.00 80.36 C ANISOU 3360 CB CYS A 327 13301 8356 8874 -427 285 414 C ATOM 3361 SG CYS A 327 9.852 17.460 26.688 1.00 85.66 S ANISOU 3361 SG CYS A 327 14243 8842 9463 -341 350 399 S ATOM 3362 N ARG A 328 10.727 12.985 24.345 1.00 74.43 N ANISOU 3362 N ARG A 328 12043 7970 8268 -322 140 480 N ATOM 3363 CA ARG A 328 11.391 12.030 23.453 1.00 73.35 C ANISOU 3363 CA ARG A 328 11752 7939 8177 -365 116 496 C ATOM 3364 C ARG A 328 10.564 11.859 22.172 1.00 77.51 C ANISOU 3364 C ARG A 328 12286 8472 8691 -222 125 549 C ATOM 3365 O ARG A 328 11.134 11.783 21.083 1.00 77.83 O ANISOU 3365 O ARG A 328 12316 8524 8733 -261 148 572 O ATOM 3366 CB ARG A 328 11.601 10.678 24.155 1.00 70.68 C ANISOU 3366 CB ARG A 328 11213 7744 7899 -375 47 474 C ATOM 3367 CG ARG A 328 12.692 10.703 25.227 1.00 76.47 C ANISOU 3367 CG ARG A 328 11904 8515 8634 -519 29 422 C ATOM 3368 CD ARG A 328 12.885 9.364 25.922 1.00 79.65 C ANISOU 3368 CD ARG A 328 12132 9053 9079 -496 -33 412 C ATOM 3369 NE ARG A 328 12.950 8.246 24.977 1.00 88.58 N ANISOU 3369 NE ARG A 328 13141 10264 10253 -447 -48 445 N ATOM 3370 CZ ARG A 328 14.048 7.848 24.340 1.00101.70 C ANISOU 3370 CZ ARG A 328 14717 11995 11928 -521 -49 442 C ATOM 3371 NH1 ARG A 328 15.209 8.458 24.556 1.00 91.28 N ANISOU 3371 NH1 ARG A 328 13401 10697 10583 -660 -37 404 N ATOM 3372 NH2 ARG A 328 13.998 6.824 23.499 1.00 83.01 N ANISOU 3372 NH2 ARG A 328 12255 9689 9597 -463 -58 470 N ATOM 3373 N SER A 329 9.221 11.840 22.305 1.00 73.47 N ANISOU 3373 N SER A 329 11790 7970 8157 -55 109 563 N ATOM 3374 CA SER A 329 8.305 11.737 21.173 1.00 73.19 C ANISOU 3374 CA SER A 329 11750 7970 8089 99 111 601 C ATOM 3375 C SER A 329 8.217 13.077 20.437 1.00 78.84 C ANISOU 3375 C SER A 329 12687 8550 8719 157 180 643 C ATOM 3376 O SER A 329 8.014 14.113 21.081 1.00 79.42 O ANISOU 3376 O SER A 329 12932 8501 8744 176 221 640 O ATOM 3377 CB SER A 329 6.917 11.292 21.624 1.00 76.15 C ANISOU 3377 CB SER A 329 12050 8428 8456 249 74 587 C ATOM 3378 OG SER A 329 5.985 11.373 20.555 1.00 85.22 O ANISOU 3378 OG SER A 329 13200 9629 9549 408 76 613 O ATOM 3379 N PRO A 330 8.338 13.079 19.088 1.00 75.96 N ANISOU 3379 N PRO A 330 12336 8197 8326 196 202 683 N ATOM 3380 CA PRO A 330 8.220 14.345 18.340 1.00 77.06 C ANISOU 3380 CA PRO A 330 12712 8198 8370 272 279 734 C ATOM 3381 C PRO A 330 6.788 14.872 18.344 1.00 81.28 C ANISOU 3381 C PRO A 330 13334 8730 8820 513 277 758 C ATOM 3382 O PRO A 330 6.594 16.081 18.254 1.00 82.25 O ANISOU 3382 O PRO A 330 13695 8702 8855 592 348 794 O ATOM 3383 CB PRO A 330 8.672 13.973 16.922 1.00 78.77 C ANISOU 3383 CB PRO A 330 12884 8466 8581 262 290 769 C ATOM 3384 CG PRO A 330 9.268 12.598 17.033 1.00 82.00 C ANISOU 3384 CG PRO A 330 13046 9019 9091 143 227 728 C ATOM 3385 CD PRO A 330 8.573 11.947 18.174 1.00 76.66 C ANISOU 3385 CD PRO A 330 12247 8420 8460 181 164 685 C ATOM 3386 N ASP A 331 5.792 13.966 18.471 1.00 77.04 N ANISOU 3386 N ASP A 331 12607 8362 8303 629 204 733 N ATOM 3387 CA ASP A 331 4.370 14.308 18.521 1.00 77.45 C ANISOU 3387 CA ASP A 331 12684 8471 8272 863 191 740 C ATOM 3388 C ASP A 331 4.075 15.151 19.763 1.00 80.67 C ANISOU 3388 C ASP A 331 13234 8763 8656 887 219 726 C ATOM 3389 O ASP A 331 3.412 16.184 19.647 1.00 81.28 O ANISOU 3389 O ASP A 331 13496 8759 8629 1063 263 760 O ATOM 3390 CB ASP A 331 3.495 13.040 18.490 1.00 78.58 C ANISOU 3390 CB ASP A 331 12567 8838 8453 921 114 693 C ATOM 3391 CG ASP A 331 3.474 12.316 17.155 1.00 89.39 C ANISOU 3391 CG ASP A 331 13813 10335 9816 948 89 700 C ATOM 3392 OD1 ASP A 331 3.420 12.999 16.104 1.00 90.50 O ANISOU 3392 OD1 ASP A 331 14076 10442 9867 1060 121 752 O ATOM 3393 OD2 ASP A 331 3.440 11.068 17.160 1.00 94.83 O ANISOU 3393 OD2 ASP A 331 14295 11158 10578 869 43 652 O ATOM 3394 N PHE A 332 4.621 14.740 20.931 1.00 75.53 N ANISOU 3394 N PHE A 332 12511 8098 8090 719 199 677 N ATOM 3395 CA PHE A 332 4.478 15.459 22.199 1.00 75.41 C ANISOU 3395 CA PHE A 332 12619 7976 8058 710 223 653 C ATOM 3396 C PHE A 332 5.310 16.736 22.199 1.00 79.28 C ANISOU 3396 C PHE A 332 13376 8245 8502 624 311 673 C ATOM 3397 O PHE A 332 4.863 17.742 22.746 1.00 79.69 O ANISOU 3397 O PHE A 332 13622 8172 8483 711 360 676 O ATOM 3398 CB PHE A 332 4.872 14.577 23.390 1.00 76.16 C ANISOU 3398 CB PHE A 332 12552 8139 8247 557 174 596 C ATOM 3399 CG PHE A 332 3.771 13.679 23.897 1.00 77.22 C ANISOU 3399 CG PHE A 332 12504 8435 8401 657 118 565 C ATOM 3400 CD1 PHE A 332 2.825 14.153 24.801 1.00 80.80 C ANISOU 3400 CD1 PHE A 332 13010 8882 8808 775 125 546 C ATOM 3401 CD2 PHE A 332 3.686 12.355 23.484 1.00 78.69 C ANISOU 3401 CD2 PHE A 332 12471 8776 8649 624 70 550 C ATOM 3402 CE1 PHE A 332 1.804 13.320 25.270 1.00 81.36 C ANISOU 3402 CE1 PHE A 332 12907 9113 8893 850 85 511 C ATOM 3403 CE2 PHE A 332 2.667 11.522 23.956 1.00 81.14 C ANISOU 3403 CE2 PHE A 332 12625 9230 8975 690 36 513 C ATOM 3404 CZ PHE A 332 1.732 12.010 24.846 1.00 79.69 C ANISOU 3404 CZ PHE A 332 12485 9051 8744 798 44 493 C ATOM 3405 N ARG A 333 6.512 16.695 21.579 1.00 74.98 N ANISOU 3405 N ARG A 333 12847 7652 7991 449 339 682 N ATOM 3406 CA ARG A 333 7.423 17.839 21.461 1.00 75.55 C ANISOU 3406 CA ARG A 333 13164 7520 8019 321 438 691 C ATOM 3407 C ARG A 333 6.750 18.995 20.713 1.00 80.64 C ANISOU 3407 C ARG A 333 14077 8021 8541 516 521 757 C ATOM 3408 O ARG A 333 6.729 20.116 21.220 1.00 81.78 O ANISOU 3408 O ARG A 333 14472 7980 8622 520 603 755 O ATOM 3409 CB ARG A 333 8.720 17.429 20.754 1.00 74.52 C ANISOU 3409 CB ARG A 333 12958 7414 7942 116 450 688 C ATOM 3410 CG ARG A 333 9.973 17.754 21.555 1.00 84.20 C ANISOU 3410 CG ARG A 333 14220 8568 9203 -148 486 624 C ATOM 3411 CD ARG A 333 11.243 17.516 20.758 1.00 95.76 C ANISOU 3411 CD ARG A 333 15627 10059 10698 -339 514 620 C ATOM 3412 NE ARG A 333 11.479 16.094 20.498 1.00104.60 N ANISOU 3412 NE ARG A 333 16458 11384 11901 -349 420 615 N ATOM 3413 CZ ARG A 333 12.337 15.625 19.597 1.00120.84 C ANISOU 3413 CZ ARG A 333 18421 13507 13984 -447 427 624 C ATOM 3414 NH1 ARG A 333 13.057 16.461 18.856 1.00110.55 N ANISOU 3414 NH1 ARG A 333 17280 12089 12634 -556 525 639 N ATOM 3415 NH2 ARG A 333 12.480 14.318 19.427 1.00107.43 N ANISOU 3415 NH2 ARG A 333 16479 11985 12357 -437 345 617 N ATOM 3416 N ILE A 334 6.157 18.704 19.538 1.00 77.16 N ANISOU 3416 N ILE A 334 13588 7671 8058 692 502 814 N ATOM 3417 CA ILE A 334 5.435 19.664 18.699 1.00 78.74 C ANISOU 3417 CA ILE A 334 14020 7775 8124 927 569 887 C ATOM 3418 C ILE A 334 4.214 20.204 19.477 1.00 82.36 C ANISOU 3418 C ILE A 334 14564 8220 8510 1152 565 883 C ATOM 3419 O ILE A 334 3.923 21.401 19.394 1.00 83.73 O ANISOU 3419 O ILE A 334 15031 8211 8570 1285 657 927 O ATOM 3420 CB ILE A 334 5.066 18.993 17.331 1.00 81.84 C ANISOU 3420 CB ILE A 334 14274 8331 8491 1061 523 932 C ATOM 3421 CG1 ILE A 334 6.059 19.396 16.221 1.00 83.37 C ANISOU 3421 CG1 ILE A 334 14613 8409 8657 955 606 983 C ATOM 3422 CG2 ILE A 334 3.611 19.215 16.880 1.00 83.21 C ANISOU 3422 CG2 ILE A 334 14464 8606 8547 1398 497 971 C ATOM 3423 CD1 ILE A 334 7.239 18.437 16.025 1.00 90.26 C ANISOU 3423 CD1 ILE A 334 15280 9364 9649 692 572 944 C ATOM 3424 N ALA A 335 3.544 19.326 20.259 1.00 76.68 N ANISOU 3424 N ALA A 335 13599 7684 7852 1186 468 830 N ATOM 3425 CA ALA A 335 2.374 19.651 21.069 1.00 76.60 C ANISOU 3425 CA ALA A 335 13612 7708 7784 1384 453 813 C ATOM 3426 C ALA A 335 2.731 20.635 22.177 1.00 81.63 C ANISOU 3426 C ALA A 335 14481 8129 8406 1299 527 788 C ATOM 3427 O ALA A 335 2.038 21.640 22.342 1.00 82.76 O ANISOU 3427 O ALA A 335 14847 8159 8439 1496 587 815 O ATOM 3428 CB ALA A 335 1.780 18.383 21.665 1.00 75.64 C ANISOU 3428 CB ALA A 335 13168 7826 7746 1374 347 753 C ATOM 3429 N PHE A 336 3.831 20.361 22.907 1.00 77.51 N ANISOU 3429 N PHE A 336 13911 7554 7983 1012 524 734 N ATOM 3430 CA PHE A 336 4.313 21.184 24.015 1.00 77.93 C ANISOU 3430 CA PHE A 336 14154 7426 8031 880 587 689 C ATOM 3431 C PHE A 336 4.675 22.579 23.545 1.00 83.91 C ANISOU 3431 C PHE A 336 15278 7917 8687 888 723 729 C ATOM 3432 O PHE A 336 4.180 23.545 24.118 1.00 85.11 O ANISOU 3432 O PHE A 336 15663 7918 8757 999 790 726 O ATOM 3433 CB PHE A 336 5.515 20.525 24.718 1.00 78.52 C ANISOU 3433 CB PHE A 336 14073 7542 8220 571 549 620 C ATOM 3434 CG PHE A 336 5.236 19.241 25.471 1.00 78.19 C ANISOU 3434 CG PHE A 336 13723 7716 8268 548 435 577 C ATOM 3435 CD1 PHE A 336 3.952 18.934 25.913 1.00 80.65 C ANISOU 3435 CD1 PHE A 336 13944 8141 8559 752 388 575 C ATOM 3436 CD2 PHE A 336 6.259 18.344 25.749 1.00 79.39 C ANISOU 3436 CD2 PHE A 336 13685 7962 8518 325 384 536 C ATOM 3437 CE1 PHE A 336 3.698 17.754 26.614 1.00 80.32 C ANISOU 3437 CE1 PHE A 336 13642 8281 8594 716 303 536 C ATOM 3438 CE2 PHE A 336 6.005 17.162 26.451 1.00 80.78 C ANISOU 3438 CE2 PHE A 336 13611 8316 8766 315 294 505 C ATOM 3439 CZ PHE A 336 4.727 16.876 26.881 1.00 78.58 C ANISOU 3439 CZ PHE A 336 13262 8126 8468 501 259 505 C ATOM 3440 N GLN A 337 5.488 22.679 22.475 1.00 81.03 N ANISOU 3440 N GLN A 337 14977 7491 8321 783 773 767 N ATOM 3441 CA GLN A 337 5.931 23.937 21.860 1.00 82.87 C ANISOU 3441 CA GLN A 337 15570 7461 8456 765 921 811 C ATOM 3442 C GLN A 337 4.748 24.834 21.478 1.00 87.65 C ANISOU 3442 C GLN A 337 16426 7965 8915 1111 981 887 C ATOM 3443 O GLN A 337 4.797 26.037 21.741 1.00 89.25 O ANISOU 3443 O GLN A 337 16972 7913 9027 1130 1108 896 O ATOM 3444 CB GLN A 337 6.792 23.657 20.619 1.00 84.23 C ANISOU 3444 CB GLN A 337 15709 7646 8648 641 946 851 C ATOM 3445 CG GLN A 337 8.197 23.155 20.944 1.00100.98 C ANISOU 3445 CG GLN A 337 17681 9804 10881 281 934 775 C ATOM 3446 CD GLN A 337 9.027 22.834 19.721 1.00122.36 C ANISOU 3446 CD GLN A 337 20338 12545 13607 167 959 811 C ATOM 3447 OE1 GLN A 337 8.617 23.034 18.568 1.00119.13 O ANISOU 3447 OE1 GLN A 337 20028 12111 13124 344 994 896 O ATOM 3448 NE2 GLN A 337 10.228 22.328 19.952 1.00114.55 N ANISOU 3448 NE2 GLN A 337 19189 11625 12708 -123 941 744 N ATOM 3449 N GLU A 338 3.686 24.240 20.884 1.00 83.25 N ANISOU 3449 N GLU A 338 15694 7614 8325 1385 894 934 N ATOM 3450 CA GLU A 338 2.468 24.939 20.468 1.00 84.68 C ANISOU 3450 CA GLU A 338 16050 7771 8354 1758 927 1004 C ATOM 3451 C GLU A 338 1.702 25.469 21.689 1.00 88.97 C ANISOU 3451 C GLU A 338 16687 8262 8857 1884 937 965 C ATOM 3452 O GLU A 338 1.257 26.620 21.673 1.00 90.42 O ANISOU 3452 O GLU A 338 17199 8251 8905 2082 1043 1010 O ATOM 3453 CB GLU A 338 1.568 24.020 19.610 1.00 85.22 C ANISOU 3453 CB GLU A 338 15840 8134 8406 1983 813 1036 C ATOM 3454 CG GLU A 338 0.338 24.697 19.010 1.00 98.29 C ANISOU 3454 CG GLU A 338 17647 9815 9885 2391 838 1109 C ATOM 3455 CD GLU A 338 0.578 25.961 18.203 1.00123.78 C ANISOU 3455 CD GLU A 338 21291 12773 12966 2517 986 1204 C ATOM 3456 OE1 GLU A 338 1.408 25.925 17.264 1.00118.55 O ANISOU 3456 OE1 GLU A 338 20689 12042 12314 2384 1029 1246 O ATOM 3457 OE2 GLU A 338 -0.095 26.979 18.485 1.00121.11 O ANISOU 3457 OE2 GLU A 338 21228 12295 12494 2762 1063 1241 O ATOM 3458 N LEU A 339 1.566 24.637 22.741 1.00 83.81 N ANISOU 3458 N LEU A 339 15760 7772 8311 1774 837 884 N ATOM 3459 CA LEU A 339 0.868 25.006 23.973 1.00 84.19 C ANISOU 3459 CA LEU A 339 15858 7798 8332 1871 838 838 C ATOM 3460 C LEU A 339 1.660 26.034 24.780 1.00 90.44 C ANISOU 3460 C LEU A 339 16956 8295 9111 1682 954 799 C ATOM 3461 O LEU A 339 1.050 26.854 25.464 1.00 91.77 O ANISOU 3461 O LEU A 339 17330 8344 9194 1834 1012 791 O ATOM 3462 CB LEU A 339 0.566 23.774 24.844 1.00 82.18 C ANISOU 3462 CB LEU A 339 15231 7800 8195 1788 707 764 C ATOM 3463 CG LEU A 339 -0.427 22.742 24.293 1.00 85.83 C ANISOU 3463 CG LEU A 339 15381 8568 8662 1972 598 775 C ATOM 3464 CD1 LEU A 339 -0.512 21.554 25.207 1.00 84.09 C ANISOU 3464 CD1 LEU A 339 14842 8545 8564 1828 499 700 C ATOM 3465 CD2 LEU A 339 -1.819 23.335 24.082 1.00 89.71 C ANISOU 3465 CD2 LEU A 339 15955 9126 9005 2353 612 811 C ATOM 3466 N LEU A 340 3.004 26.006 24.694 1.00 87.47 N ANISOU 3466 N LEU A 340 16612 7812 8811 1352 993 768 N ATOM 3467 CA LEU A 340 3.864 26.955 25.407 1.00 89.08 C ANISOU 3467 CA LEU A 340 17092 7753 9001 1123 1109 712 C ATOM 3468 C LEU A 340 4.130 28.210 24.558 1.00 97.29 C ANISOU 3468 C LEU A 340 18549 8499 9919 1171 1278 777 C ATOM 3469 O LEU A 340 4.679 29.182 25.079 1.00 98.20 O ANISOU 3469 O LEU A 340 18960 8358 9993 1015 1404 732 O ATOM 3470 CB LEU A 340 5.185 26.303 25.864 1.00 87.67 C ANISOU 3470 CB LEU A 340 16719 7636 8954 733 1067 627 C ATOM 3471 CG LEU A 340 5.083 25.210 26.952 1.00 90.12 C ANISOU 3471 CG LEU A 340 16687 8182 9373 654 927 554 C ATOM 3472 CD1 LEU A 340 6.449 24.672 27.313 1.00 89.44 C ANISOU 3472 CD1 LEU A 340 16443 8152 9389 299 896 478 C ATOM 3473 CD2 LEU A 340 4.396 25.718 28.208 1.00 92.40 C ANISOU 3473 CD2 LEU A 340 17080 8412 9617 749 939 506 C ATOM 3474 N CYS A 341 3.690 28.194 23.273 1.00 96.50 N ANISOU 3474 N CYS A 341 18482 8435 9750 1395 1286 880 N ATOM 3475 CA CYS A 341 3.766 29.276 22.276 1.00 99.94 C ANISOU 3475 CA CYS A 341 19307 8618 10049 1512 1442 969 C ATOM 3476 C CYS A 341 5.199 29.818 22.145 1.00103.99 C ANISOU 3476 C CYS A 341 20027 8896 10590 1138 1574 931 C ATOM 3477 O CYS A 341 5.474 30.971 22.500 1.00104.95 O ANISOU 3477 O CYS A 341 20526 8718 10631 1068 1732 913 O ATOM 3478 CB CYS A 341 2.767 30.393 22.588 1.00103.40 C ANISOU 3478 CB CYS A 341 20085 8872 10329 1832 1537 1011 C ATOM 3479 SG CYS A 341 1.156 29.812 23.190 1.00106.95 S ANISOU 3479 SG CYS A 341 20266 9615 10756 2205 1386 1009 S ATOM 3480 N LEU A 342 6.103 28.974 21.620 1.00 99.08 N ANISOU 3480 N LEU A 342 19153 8418 10075 897 1515 913 N ATOM 3481 CA LEU A 342 7.516 29.312 21.431 1.00123.57 C ANISOU 3481 CA LEU A 342 22373 11366 13212 521 1624 865 C ATOM 3482 C LEU A 342 7.871 29.419 19.941 1.00145.36 C ANISOU 3482 C LEU A 342 25237 14073 15919 547 1697 960 C ATOM 3483 O LEU A 342 7.474 28.574 19.137 1.00100.67 O ANISOU 3483 O LEU A 342 19337 8631 10281 711 1588 1021 O ATOM 3484 CB LEU A 342 8.420 28.270 22.123 1.00121.38 C ANISOU 3484 CB LEU A 342 21717 11306 13095 198 1504 755 C ATOM 3485 CG LEU A 342 8.042 27.854 23.552 1.00124.59 C ANISOU 3485 CG LEU A 342 21935 11837 13566 189 1396 668 C ATOM 3486 CD1 LEU A 342 8.640 26.513 23.898 1.00122.26 C ANISOU 3486 CD1 LEU A 342 21211 11828 13416 0 1243 605 C ATOM 3487 CD2 LEU A 342 8.451 28.905 24.575 1.00128.90 C ANISOU 3487 CD2 LEU A 342 22761 12148 14068 7 1515 579 C TER 3488 LEU A 342 HETATM 3489 C5 TIM A1201 3.219 1.514 50.804 1.00 74.58 C HETATM 3490 C6 TIM A1201 3.140 1.737 52.304 1.00 75.33 C HETATM 3491 O1 TIM A1201 2.751 0.510 52.955 1.00 76.03 O HETATM 3492 C2 TIM A1201 1.439 0.075 52.550 1.00 75.63 C HETATM 3493 C3 TIM A1201 1.344 -0.131 51.042 1.00 75.33 C HETATM 3494 N4 TIM A1201 1.974 0.951 50.273 1.00 74.70 N HETATM 3495 C7 TIM A1201 1.441 1.337 49.055 1.00 74.08 C HETATM 3496 N8 TIM A1201 0.949 0.443 48.180 1.00 74.18 N HETATM 3497 S9 TIM A1201 0.418 1.308 46.854 1.00 74.30 S HETATM 3498 N10 TIM A1201 0.804 2.847 47.336 1.00 74.13 N HETATM 3499 C11 TIM A1201 1.363 2.695 48.545 1.00 73.50 C HETATM 3500 O12 TIM A1201 1.764 3.835 49.185 1.00 71.35 O HETATM 3501 C13 TIM A1201 2.865 4.529 48.568 1.00 68.32 C HETATM 3502 C14 TIM A1201 3.328 5.700 49.434 1.00 67.04 C HETATM 3503 O15 TIM A1201 3.557 6.819 48.581 1.00 65.67 O HETATM 3504 C16 TIM A1201 2.383 6.059 50.605 1.00 67.75 C HETATM 3505 N17 TIM A1201 2.872 7.229 51.383 1.00 68.22 N HETATM 3506 C18 TIM A1201 2.546 7.359 52.841 1.00 68.05 C HETATM 3507 C19 TIM A1201 1.065 7.290 53.244 1.00 67.99 C HETATM 3508 C20 TIM A1201 3.277 6.324 53.664 1.00 67.81 C HETATM 3509 C21 TIM A1201 3.064 8.732 53.294 1.00 67.94 C HETATM 3510 S SO4 A1202 -1.968 2.875 19.488 1.00 78.35 S HETATM 3511 O1 SO4 A1202 -0.671 3.245 18.921 1.00 78.88 O HETATM 3512 O2 SO4 A1202 -3.054 3.268 18.584 1.00 78.10 O HETATM 3513 O3 SO4 A1202 -2.009 1.434 19.678 1.00 78.59 O HETATM 3514 O4 SO4 A1202 -2.136 3.547 20.766 1.00 77.99 O HETATM 3515 S SO4 A1203 16.874 6.658 21.207 1.00146.90 S HETATM 3516 O1 SO4 A1203 16.862 7.759 20.241 1.00146.69 O HETATM 3517 O2 SO4 A1203 17.838 5.637 20.789 1.00146.99 O HETATM 3518 O3 SO4 A1203 15.540 6.069 21.282 1.00146.96 O HETATM 3519 O4 SO4 A1203 17.254 7.171 22.522 1.00147.25 O HETATM 3520 S SO4 A1204 36.553 -6.848 -2.076 1.00161.36 S HETATM 3521 O1 SO4 A1204 35.795 -5.766 -2.697 1.00161.52 O HETATM 3522 O2 SO4 A1204 37.489 -7.403 -3.054 1.00161.66 O HETATM 3523 O3 SO4 A1204 35.647 -7.900 -1.629 1.00161.06 O HETATM 3524 O4 SO4 A1204 37.289 -6.318 -0.927 1.00161.51 O HETATM 3525 S SO4 A1205 24.193 8.084 4.913 1.00208.62 S HETATM 3526 O1 SO4 A1205 25.650 8.104 4.999 1.00208.70 O HETATM 3527 O2 SO4 A1205 23.773 8.654 3.634 1.00208.83 O HETATM 3528 O3 SO4 A1205 23.718 6.703 5.015 1.00208.88 O HETATM 3529 O4 SO4 A1205 23.631 8.880 6.002 1.00208.74 O HETATM 3530 C1 CLR A1206 -11.399 9.934 30.333 1.00114.72 C HETATM 3531 C2 CLR A1206 -11.145 9.830 28.817 1.00114.65 C HETATM 3532 C3 CLR A1206 -9.657 9.849 28.455 1.00114.48 C HETATM 3533 C4 CLR A1206 -8.951 8.696 29.165 1.00114.14 C HETATM 3534 C5 CLR A1206 -9.163 8.839 30.665 1.00114.10 C HETATM 3535 C6 CLR A1206 -8.050 8.821 31.433 1.00113.70 C HETATM 3536 C7 CLR A1206 -8.012 9.443 32.815 1.00113.57 C HETATM 3537 C8 CLR A1206 -9.328 9.157 33.545 1.00113.87 C HETATM 3538 C9 CLR A1206 -10.500 9.668 32.666 1.00114.43 C HETATM 3539 C10 CLR A1206 -10.579 9.002 31.257 1.00114.46 C HETATM 3540 C11 CLR A1206 -11.844 9.623 33.446 1.00114.74 C HETATM 3541 C12 CLR A1206 -11.799 10.174 34.890 1.00114.45 C HETATM 3542 C13 CLR A1206 -10.666 9.588 35.757 1.00113.56 C HETATM 3543 C14 CLR A1206 -9.389 9.816 34.936 1.00113.56 C HETATM 3544 C15 CLR A1206 -8.254 9.551 35.918 1.00112.98 C HETATM 3545 C16 CLR A1206 -8.784 10.189 37.199 1.00112.62 C HETATM 3546 C17 CLR A1206 -10.297 10.426 37.014 1.00112.84 C HETATM 3547 C18 CLR A1206 -10.969 8.101 36.082 1.00112.95 C HETATM 3548 C19 CLR A1206 -11.247 7.615 31.295 1.00114.39 C HETATM 3549 C20 CLR A1206 -11.119 10.255 38.321 1.00112.26 C HETATM 3550 C21 CLR A1206 -12.566 10.747 38.209 1.00112.76 C HETATM 3551 C22 CLR A1206 -10.488 10.983 39.515 1.00110.64 C HETATM 3552 C23 CLR A1206 -10.403 10.133 40.780 1.00108.97 C HETATM 3553 C24 CLR A1206 -10.162 11.037 41.985 1.00107.83 C HETATM 3554 C25 CLR A1206 -10.804 10.509 43.264 1.00106.46 C HETATM 3555 C26 CLR A1206 -9.902 10.788 44.461 1.00105.87 C HETATM 3556 C27 CLR A1206 -12.182 11.123 43.491 1.00106.19 C HETATM 3557 O1 CLR A1206 -9.481 9.740 27.038 1.00114.64 O HETATM 3558 C10 OLC A1207 -5.732 -3.337 41.170 1.00 86.93 C HETATM 3559 C9 OLC A1207 -5.993 -3.234 39.860 1.00 87.04 C HETATM 3560 C11 OLC A1207 -5.558 -4.648 41.908 1.00 87.19 C HETATM 3561 C8 OLC A1207 -6.169 -4.408 38.916 1.00 87.03 C HETATM 3562 C7 OLC A1207 -7.338 -4.128 37.979 1.00 86.43 C HETATM 3563 C6 OLC A1207 -7.197 -4.894 36.671 1.00 85.80 C HETATM 3564 C5 OLC A1207 -7.787 -4.079 35.528 1.00 86.12 C HETATM 3565 C4 OLC A1207 -8.282 -4.972 34.398 1.00 87.15 C HETATM 3566 C3 OLC A1207 -9.612 -4.457 33.861 1.00 88.48 C HETATM 3567 C2 OLC A1207 -10.305 -5.518 33.013 1.00 89.23 C HETATM 3568 C8 OLC A1208 -3.024 -9.027 34.123 1.00 98.48 C HETATM 3569 C24 OLC A1208 -7.336 -8.019 24.271 1.00107.61 C HETATM 3570 C7 OLC A1208 -3.228 -7.629 33.553 1.00 99.68 C HETATM 3571 C6 OLC A1208 -4.542 -7.542 32.780 1.00101.05 C HETATM 3572 C5 OLC A1208 -4.725 -6.186 32.103 1.00101.24 C HETATM 3573 C4 OLC A1208 -5.692 -6.281 30.927 1.00101.48 C HETATM 3574 C3 OLC A1208 -5.085 -5.656 29.675 1.00102.60 C HETATM 3575 C2 OLC A1208 -6.004 -5.795 28.460 1.00103.91 C HETATM 3576 C21 OLC A1208 -5.291 -6.982 25.299 1.00106.36 C HETATM 3577 C1 OLC A1208 -5.328 -5.415 27.151 1.00105.34 C HETATM 3578 C22 OLC A1208 -6.034 -7.276 23.996 1.00106.76 C HETATM 3579 O19 OLC A1208 -4.344 -4.683 27.118 1.00105.40 O HETATM 3580 O25 OLC A1208 -7.975 -8.334 23.027 1.00108.21 O HETATM 3581 O23 OLC A1208 -6.310 -6.073 23.271 1.00106.68 O HETATM 3582 O20 OLC A1208 -5.838 -5.854 25.992 1.00106.12 O HETATM 3583 C9 OLC A1209 -8.870 17.335 39.095 1.00105.85 C HETATM 3584 C8 OLC A1209 -8.137 16.613 37.988 1.00106.42 C HETATM 3585 C24 OLC A1209 -10.035 13.180 25.305 1.00112.98 C HETATM 3586 C7 OLC A1209 -9.114 16.249 36.876 1.00106.90 C HETATM 3587 C6 OLC A1209 -8.385 15.884 35.588 1.00106.99 C HETATM 3588 C5 OLC A1209 -9.373 15.455 34.510 1.00107.37 C HETATM 3589 C4 OLC A1209 -8.664 15.132 33.201 1.00107.80 C HETATM 3590 C3 OLC A1209 -9.362 14.001 32.453 1.00108.59 C HETATM 3591 C2 OLC A1209 -9.965 14.492 31.136 1.00110.30 C HETATM 3592 C21 OLC A1209 -9.418 13.576 27.689 1.00113.53 C HETATM 3593 C1 OLC A1209 -9.020 14.371 29.950 1.00112.48 C HETATM 3594 C22 OLC A1209 -10.459 13.851 26.608 1.00113.82 C HETATM 3595 O19 OLC A1209 -7.833 14.110 30.098 1.00113.19 O HETATM 3596 O25 OLC A1209 -11.017 13.445 24.296 1.00112.16 O HETATM 3597 O23 OLC A1209 -11.728 13.329 27.018 1.00114.52 O HETATM 3598 O20 OLC A1209 -9.483 14.579 28.710 1.00113.35 O HETATM 3599 C10 OLC A1210 0.931 25.348 36.206 1.00101.58 C HETATM 3600 C9 OLC A1210 0.168 25.059 35.143 1.00102.80 C HETATM 3601 C11 OLC A1210 1.714 26.636 36.361 1.00101.22 C HETATM 3602 C8 OLC A1210 -0.021 25.992 33.960 1.00104.49 C HETATM 3603 C24 OLC A1210 -4.584 26.095 23.002 1.00124.83 C HETATM 3604 C12 OLC A1210 2.747 26.494 37.473 1.00101.76 C HETATM 3605 C7 OLC A1210 -0.319 25.206 32.689 1.00105.90 C HETATM 3606 C13 OLC A1210 4.182 26.419 36.953 1.00101.83 C HETATM 3607 C6 OLC A1210 0.531 25.681 31.519 1.00107.68 C HETATM 3608 C14 OLC A1210 4.878 27.776 36.924 1.00101.63 C HETATM 3609 C5 OLC A1210 0.070 25.019 30.227 1.00110.27 C HETATM 3610 C4 OLC A1210 -0.306 26.050 29.164 1.00113.18 C HETATM 3611 C3 OLC A1210 -1.802 26.364 29.162 1.00115.52 C HETATM 3612 C2 OLC A1210 -2.569 25.475 28.186 1.00117.58 C HETATM 3613 C21 OLC A1210 -4.745 25.966 25.509 1.00123.47 C HETATM 3614 C1 OLC A1210 -2.761 26.181 26.864 1.00120.13 C HETATM 3615 C22 OLC A1210 -4.876 26.870 24.286 1.00124.47 C HETATM 3616 O19 OLC A1210 -1.814 26.348 26.109 1.00120.61 O HETATM 3617 O25 OLC A1210 -5.702 25.275 22.637 1.00124.95 O HETATM 3618 O23 OLC A1210 -6.186 27.448 24.242 1.00124.75 O HETATM 3619 O20 OLC A1210 -3.968 26.629 26.512 1.00122.08 O HETATM 3620 C10 OLC A1211 -7.749 19.918 36.338 1.00106.98 C HETATM 3621 C9 OLC A1211 -7.699 19.567 35.046 1.00107.99 C HETATM 3622 C11 OLC A1211 -6.928 21.026 36.966 1.00106.17 C HETATM 3623 C8 OLC A1211 -6.813 20.222 34.007 1.00109.24 C HETATM 3624 C24 OLC A1211 -11.511 19.939 23.065 1.00122.11 C HETATM 3625 C7 OLC A1211 -6.883 19.419 32.715 1.00110.12 C HETATM 3626 C6 OLC A1211 -6.936 20.327 31.492 1.00111.23 C HETATM 3627 C5 OLC A1211 -8.201 20.076 30.674 1.00113.10 C HETATM 3628 C4 OLC A1211 -7.913 19.335 29.367 1.00115.12 C HETATM 3629 C3 OLC A1211 -7.766 20.290 28.183 1.00117.07 C HETATM 3630 C2 OLC A1211 -9.062 20.408 27.380 1.00119.23 C HETATM 3631 C21 OLC A1211 -10.188 21.625 24.304 1.00121.67 C HETATM 3632 C1 OLC A1211 -8.965 21.532 26.370 1.00121.15 C HETATM 3633 C22 OLC A1211 -10.253 20.801 23.025 1.00121.68 C HETATM 3634 O19 OLC A1211 -8.829 22.693 26.738 1.00122.01 O HETATM 3635 O25 OLC A1211 -11.461 18.957 22.023 1.00122.23 O HETATM 3636 O23 OLC A1211 -10.316 21.691 21.905 1.00121.09 O HETATM 3637 O20 OLC A1211 -9.033 21.260 25.063 1.00121.51 O HETATM 3638 C24 OLC A1212 5.148 31.190 27.960 1.00114.74 C HETATM 3639 C6 OLC A1212 6.613 30.992 37.747 1.00104.01 C HETATM 3640 C5 OLC A1212 6.674 32.292 36.956 1.00104.17 C HETATM 3641 C4 OLC A1212 5.669 32.284 35.812 1.00105.13 C HETATM 3642 C3 OLC A1212 6.354 32.578 34.483 1.00106.87 C HETATM 3643 C2 OLC A1212 5.618 31.917 33.316 1.00108.93 C HETATM 3644 C21 OLC A1212 5.555 30.388 30.287 1.00113.20 C HETATM 3645 C1 OLC A1212 6.528 31.577 32.145 1.00111.06 C HETATM 3646 C22 OLC A1212 6.001 30.273 28.831 1.00114.11 C HETATM 3647 O19 OLC A1212 7.706 31.276 32.304 1.00111.59 O HETATM 3648 O25 OLC A1212 5.659 31.222 26.621 1.00115.17 O HETATM 3649 O23 OLC A1212 7.394 30.585 28.695 1.00114.38 O HETATM 3650 O20 OLC A1212 6.041 31.589 30.900 1.00112.39 O HETATM 3651 C24 OLC A1213 16.545 1.109 28.106 1.00127.89 C HETATM 3652 C6 OLC A1213 17.002 6.988 33.169 1.00123.70 C HETATM 3653 C5 OLC A1213 17.530 5.572 32.971 1.00124.21 C HETATM 3654 C4 OLC A1213 16.435 4.650 32.452 1.00124.65 C HETATM 3655 C3 OLC A1213 16.336 3.391 33.303 1.00125.35 C HETATM 3656 C2 OLC A1213 15.257 2.456 32.768 1.00126.34 C HETATM 3657 C21 OLC A1213 15.417 0.234 30.175 1.00127.74 C HETATM 3658 C1 OLC A1213 15.864 1.124 32.381 1.00127.51 C HETATM 3659 C22 OLC A1213 15.250 1.079 28.913 1.00127.93 C HETATM 3660 O19 OLC A1213 16.016 0.247 33.220 1.00127.92 O HETATM 3661 O25 OLC A1213 16.344 1.878 26.915 1.00127.83 O HETATM 3662 O23 OLC A1213 14.207 0.528 28.099 1.00127.84 O HETATM 3663 O20 OLC A1213 16.256 0.901 31.123 1.00127.80 O HETATM 3664 C1 OLA A1214 -6.628 24.842 30.091 1.00 99.66 C HETATM 3665 O1 OLA A1214 -7.674 24.878 29.405 1.00 99.61 O HETATM 3666 O2 OLA A1214 -5.622 24.262 29.623 1.00100.25 O HETATM 3667 C2 OLA A1214 -6.577 25.503 31.450 1.00 98.85 C HETATM 3668 C3 OLA A1214 -6.480 24.465 32.564 1.00 98.14 C HETATM 3669 C4 OLA A1214 -5.776 25.046 33.786 1.00 97.65 C HETATM 3670 C5 OLA A1214 -6.025 24.187 35.020 1.00 98.00 C HETATM 3671 C6 OLA A1214 -4.948 24.408 36.077 1.00 98.43 C HETATM 3672 C7 OLA A1214 -5.559 24.693 37.447 1.00 98.24 C HETATM 3673 C8 OLA A1214 -4.921 23.846 38.544 1.00 98.39 C HETATM 3674 C9 OLA A1214 -3.836 24.642 39.242 1.00 99.14 C HETATM 3675 C10 OLA A1214 -3.856 25.034 40.525 1.00 99.72 C HETATM 3676 C11 OLA A1214 -4.974 24.764 41.510 1.00100.33 C HETATM 3677 C12 OLA A1214 -4.457 24.981 42.929 1.00100.58 C HETATM 3678 C1 OLA A1215 3.074 -13.247 27.938 1.00 94.09 C HETATM 3679 O1 OLA A1215 2.584 -14.320 27.520 1.00 94.48 O HETATM 3680 O2 OLA A1215 4.322 -13.165 28.027 1.00 94.24 O HETATM 3681 C2 OLA A1215 2.200 -12.060 28.306 1.00 93.27 C HETATM 3682 C3 OLA A1215 0.902 -12.466 29.009 1.00 92.11 C HETATM 3683 C4 OLA A1215 0.876 -12.128 30.499 1.00 91.25 C HETATM 3684 C5 OLA A1215 1.359 -13.303 31.351 1.00 90.54 C HETATM 3685 C6 OLA A1215 0.803 -13.268 32.772 1.00 88.88 C HETATM 3686 C7 OLA A1215 1.646 -14.128 33.709 1.00 87.00 C HETATM 3687 C8 OLA A1215 0.872 -14.471 34.976 1.00 86.06 C HETATM 3688 C1 OLA A1216 13.854 14.660 56.390 1.00106.22 C HETATM 3689 O1 OLA A1216 15.063 14.840 56.653 1.00106.76 O HETATM 3690 O2 OLA A1216 13.132 14.077 57.227 1.00106.79 O HETATM 3691 C2 OLA A1216 13.268 15.148 55.087 1.00104.76 C HETATM 3692 C3 OLA A1216 13.345 14.048 54.031 1.00103.37 C HETATM 3693 C4 OLA A1216 12.433 14.352 52.845 1.00102.63 C HETATM 3694 C5 OLA A1216 13.166 15.110 51.741 1.00102.44 C HETATM 3695 C6 OLA A1216 12.192 15.626 50.687 1.00103.02 C HETATM 3696 C7 OLA A1216 12.840 16.674 49.784 1.00103.37 C HETATM 3697 C8 OLA A1216 13.158 16.115 48.397 1.00103.68 C HETATM 3698 C9 OLA A1216 14.620 15.716 48.338 1.00104.06 C HETATM 3699 C10 OLA A1216 15.229 15.135 47.295 1.00104.42 C HETATM 3700 C11 OLA A1216 14.563 14.773 45.984 1.00104.76 C HETATM 3701 C12 OLA A1216 15.418 15.292 44.833 1.00104.69 C HETATM 3702 C1 OLA A1217 14.210 -5.670 29.573 1.00105.23 C HETATM 3703 O1 OLA A1217 14.555 -5.985 28.411 1.00105.45 O HETATM 3704 O2 OLA A1217 14.590 -6.407 30.517 1.00106.34 O HETATM 3705 C2 OLA A1217 13.360 -4.428 29.795 1.00103.02 C HETATM 3706 C3 OLA A1217 12.940 -4.242 31.252 1.00101.05 C HETATM 3707 C4 OLA A1217 11.505 -3.738 31.385 1.00 99.29 C HETATM 3708 C5 OLA A1217 11.460 -2.325 31.963 1.00 97.85 C HETATM 3709 C6 OLA A1217 11.239 -2.328 33.473 1.00 96.65 C HETATM 3710 C7 OLA A1217 12.485 -1.873 34.231 1.00 96.14 C HETATM 3711 C8 OLA A1217 13.237 -3.038 34.870 1.00 96.32 C HETATM 3712 C9 OLA A1217 13.037 -3.038 36.372 1.00 96.28 C HETATM 3713 C10 OLA A1217 13.528 -3.951 37.223 1.00 95.98 C HETATM 3714 C11 OLA A1217 14.370 -5.148 36.832 1.00 95.32 C HETATM 3715 O HOH A1301 8.146 6.972 35.727 1.00 39.17 O HETATM 3716 O HOH A1302 -4.023 10.096 63.487 1.00 78.62 O HETATM 3717 O HOH A1303 22.329 -5.800 13.210 1.00 67.03 O HETATM 3718 O HOH A1304 3.203 7.766 38.230 1.00 61.96 O HETATM 3719 O HOH A1305 14.512 -0.374 14.878 1.00 45.69 O HETATM 3720 O HOH A1306 12.318 4.929 46.770 1.00 65.77 O HETATM 3721 O HOH A1307 -0.266 1.004 24.814 1.00 42.18 O HETATM 3722 O HOH A1308 -11.472 7.449 61.815 1.00 80.94 O HETATM 3723 O HOH A1309 -12.185 6.484 59.363 1.00 72.38 O HETATM 3724 O HOH A1310 0.458 19.538 58.918 1.00 93.18 O CONECT 601 1286 CONECT 1238 1280 CONECT 1280 1238 CONECT 1286 601 CONECT 3489 3490 3494 CONECT 3490 3489 3491 CONECT 3491 3490 3492 CONECT 3492 3491 3493 CONECT 3493 3492 3494 CONECT 3494 3489 3493 3495 CONECT 3495 3494 3496 3499 CONECT 3496 3495 3497 CONECT 3497 3496 3498 CONECT 3498 3497 3499 CONECT 3499 3495 3498 3500 CONECT 3500 3499 3501 CONECT 3501 3500 3502 CONECT 3502 3501 3503 3504 CONECT 3503 3502 CONECT 3504 3502 3505 CONECT 3505 3504 3506 CONECT 3506 3505 3507 3508 3509 CONECT 3507 3506 CONECT 3508 3506 CONECT 3509 3506 CONECT 3510 3511 3512 3513 3514 CONECT 3511 3510 CONECT 3512 3510 CONECT 3513 3510 CONECT 3514 3510 CONECT 3515 3516 3517 3518 3519 CONECT 3516 3515 CONECT 3517 3515 CONECT 3518 3515 CONECT 3519 3515 CONECT 3520 3521 3522 3523 3524 CONECT 3521 3520 CONECT 3522 3520 CONECT 3523 3520 CONECT 3524 3520 CONECT 3525 3526 3527 3528 3529 CONECT 3526 3525 CONECT 3527 3525 CONECT 3528 3525 CONECT 3529 3525 CONECT 3530 3531 3539 CONECT 3531 3530 3532 CONECT 3532 3531 3533 3557 CONECT 3533 3532 3534 CONECT 3534 3533 3535 3539 CONECT 3535 3534 3536 CONECT 3536 3535 3537 CONECT 3537 3536 3538 3543 CONECT 3538 3537 3539 3540 CONECT 3539 3530 3534 3538 3548 CONECT 3540 3538 3541 CONECT 3541 3540 3542 CONECT 3542 3541 3543 3546 3547 CONECT 3543 3537 3542 3544 CONECT 3544 3543 3545 CONECT 3545 3544 3546 CONECT 3546 3542 3545 3549 CONECT 3547 3542 CONECT 3548 3539 CONECT 3549 3546 3550 3551 CONECT 3550 3549 CONECT 3551 3549 3552 CONECT 3552 3551 3553 CONECT 3553 3552 3554 CONECT 3554 3553 3555 3556 CONECT 3555 3554 CONECT 3556 3554 CONECT 3557 3532 CONECT 3558 3559 3560 CONECT 3559 3558 3561 CONECT 3560 3558 CONECT 3561 3559 3562 CONECT 3562 3561 3563 CONECT 3563 3562 3564 CONECT 3564 3563 3565 CONECT 3565 3564 3566 CONECT 3566 3565 3567 CONECT 3567 3566 CONECT 3568 3570 CONECT 3569 3578 3580 CONECT 3570 3568 3571 CONECT 3571 3570 3572 CONECT 3572 3571 3573 CONECT 3573 3572 3574 CONECT 3574 3573 3575 CONECT 3575 3574 3577 CONECT 3576 3578 3582 CONECT 3577 3575 3579 3582 CONECT 3578 3569 3576 3581 CONECT 3579 3577 CONECT 3580 3569 CONECT 3581 3578 CONECT 3582 3576 3577 CONECT 3583 3584 CONECT 3584 3583 3586 CONECT 3585 3594 3596 CONECT 3586 3584 3587 CONECT 3587 3586 3588 CONECT 3588 3587 3589 CONECT 3589 3588 3590 CONECT 3590 3589 3591 CONECT 3591 3590 3593 CONECT 3592 3594 3598 CONECT 3593 3591 3595 3598 CONECT 3594 3585 3592 3597 CONECT 3595 3593 CONECT 3596 3585 CONECT 3597 3594 CONECT 3598 3592 3593 CONECT 3599 3600 3601 CONECT 3600 3599 3602 CONECT 3601 3599 3604 CONECT 3602 3600 3605 CONECT 3603 3615 3617 CONECT 3604 3601 3606 CONECT 3605 3602 3607 CONECT 3606 3604 3608 CONECT 3607 3605 3609 CONECT 3608 3606 CONECT 3609 3607 3610 CONECT 3610 3609 3611 CONECT 3611 3610 3612 CONECT 3612 3611 3614 CONECT 3613 3615 3619 CONECT 3614 3612 3616 3619 CONECT 3615 3603 3613 3618 CONECT 3616 3614 CONECT 3617 3603 CONECT 3618 3615 CONECT 3619 3613 3614 CONECT 3620 3621 3622 CONECT 3621 3620 3623 CONECT 3622 3620 CONECT 3623 3621 3625 CONECT 3624 3633 3635 CONECT 3625 3623 3626 CONECT 3626 3625 3627 CONECT 3627 3626 3628 CONECT 3628 3627 3629 CONECT 3629 3628 3630 CONECT 3630 3629 3632 CONECT 3631 3633 3637 CONECT 3632 3630 3634 3637 CONECT 3633 3624 3631 3636 CONECT 3634 3632 CONECT 3635 3624 CONECT 3636 3633 CONECT 3637 3631 3632 CONECT 3638 3646 3648 CONECT 3639 3640 CONECT 3640 3639 3641 CONECT 3641 3640 3642 CONECT 3642 3641 3643 CONECT 3643 3642 3645 CONECT 3644 3646 3650 CONECT 3645 3643 3647 3650 CONECT 3646 3638 3644 3649 CONECT 3647 3645 CONECT 3648 3638 CONECT 3649 3646 CONECT 3650 3644 3645 CONECT 3651 3659 3661 CONECT 3652 3653 CONECT 3653 3652 3654 CONECT 3654 3653 3655 CONECT 3655 3654 3656 CONECT 3656 3655 3658 CONECT 3657 3659 3663 CONECT 3658 3656 3660 3663 CONECT 3659 3651 3657 3662 CONECT 3660 3658 CONECT 3661 3651 CONECT 3662 3659 CONECT 3663 3657 3658 CONECT 3664 3665 3666 3667 CONECT 3665 3664 CONECT 3666 3664 CONECT 3667 3664 3668 CONECT 3668 3667 3669 CONECT 3669 3668 3670 CONECT 3670 3669 3671 CONECT 3671 3670 3672 CONECT 3672 3671 3673 CONECT 3673 3672 3674 CONECT 3674 3673 3675 CONECT 3675 3674 3676 CONECT 3676 3675 3677 CONECT 3677 3676 CONECT 3678 3679 3680 3681 CONECT 3679 3678 CONECT 3680 3678 CONECT 3681 3678 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 CONECT 3702 3703 3704 3705 CONECT 3703 3702 CONECT 3704 3702 CONECT 3705 3702 3706 CONECT 3706 3705 3707 CONECT 3707 3706 3708 CONECT 3708 3707 3709 CONECT 3709 3708 3710 CONECT 3710 3709 3711 CONECT 3711 3710 3712 CONECT 3712 3711 3713 CONECT 3713 3712 3714 CONECT 3714 3713 MASTER 439 0 17 25 3 0 23 6 3714 1 230 39 END