HEADER MEMBRANE PROTEIN 12-JUL-19 6PS2 TITLE XFEL BETA2 AR STRUCTURE BY LIGAND EXCHANGE FROM TIMOLOL TO ALPRENOLOL. 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, ALPRENOLOL, MEMBRANE PROTEIN, B2AR, BETA2AR 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 6PS2 1 REMARK REVDAT 2 25-DEC-19 6PS2 1 JRNL REVDAT 1 13-NOV-19 6PS2 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. 2.40 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) : 2.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.82 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 22205 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) : 0.183 REMARK 3 R VALUE (WORKING SET) : 0.181 REMARK 3 FREE R VALUE : 0.224 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1110 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 : 11 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.52 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.34 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2864 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2490 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2722 REMARK 3 BIN R VALUE (WORKING SET) : 0.2470 REMARK 3 BIN FREE R VALUE : 0.2820 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.96 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 142 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 : 3526 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 266 REMARK 3 SOLVENT ATOMS : 36 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 89.28 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -13.76220 REMARK 3 B22 (A**2) : 5.24280 REMARK 3 B33 (A**2) : 8.51950 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) : 0.360 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.331 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.222 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.330 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.224 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 : 0.956 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3920 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 5291 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1832 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 72 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 562 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3920 ; 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 : 505 ; 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 : 4779 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.03 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.64 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.28 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): 8.7183 3.6358 25.9184 REMARK 3 T TENSOR REMARK 3 T11: 0.0114 T22: -0.2651 REMARK 3 T33: -0.2750 T12: -0.0237 REMARK 3 T13: -0.0230 T23: 0.0355 REMARK 3 L TENSOR REMARK 3 L11: 0.8897 L22: 0.8853 REMARK 3 L33: 2.8863 L12: -0.4335 REMARK 3 L13: -0.8596 L23: 0.6668 REMARK 3 S TENSOR REMARK 3 S11: -0.0249 S12: 0.0024 S13: 0.0524 REMARK 3 S21: 0.1198 S22: -0.0148 S23: -0.0586 REMARK 3 S31: -0.2753 S32: 0.0889 S33: 0.0398 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6PS2 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_1000242971. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-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 : 22282 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400 REMARK 200 RESOLUTION RANGE LOW (A) : 30.820 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 503.6 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.52 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 (%): 49.22 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42 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 ALPRENOLOL, 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 20.82500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.95000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.12000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.95000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.82500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.12000 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 ARG A 28 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 60 CD CE NZ REMARK 470 LYS A 97 CE NZ REMARK 470 LYS A 227 CE NZ REMARK 470 LYS A1016 CG CD CE NZ REMARK 470 LYS A1019 CG CD CE NZ REMARK 470 LYS A1048 CD CE NZ REMARK 470 LYS A1060 CD CE NZ REMARK 470 ASP A1061 OD1 OD2 REMARK 470 LYS A 267 CG CD CE NZ REMARK 470 ILE A 303 CG1 CG2 CD1 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 VAL A 86 -71.25 -108.94 REMARK 500 LYS A 140 -61.78 62.31 REMARK 500 PHE A 208 -53.17 -131.58 REMARK 500 PRO A1037 34.67 -86.20 REMARK 500 ARG A1125 66.23 -100.27 REMARK 500 ASP A 300 -39.73 82.61 REMARK 500 LEU A 302 14.71 80.15 REMARK 500 ARG A 304 -162.66 63.04 REMARK 500 LYS A 305 -43.05 -130.69 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 OLB A 1203 REMARK 610 OLB A 1204 REMARK 610 OLB A 1205 REMARK 610 OLB A 1206 REMARK 610 OLB A 1207 REMARK 610 OLB A 1208 REMARK 610 OLC A 1209 REMARK 610 OLB A 1210 REMARK 610 OLC A 1215 REMARK 610 OLC A 1216 REMARK 610 OLA A 1217 REMARK 610 OLA A 1218 REMARK 610 OLA A 1219 REMARK 610 OLA A 1220 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue JTZ A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLB A 1203 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLB A 1204 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLB A 1205 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLB A 1206 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLB A 1207 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLB 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 OLB A 1210 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1211 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1212 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1213 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1214 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1215 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC 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 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1218 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1219 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1220 DBREF 6PS2 A 1 230 UNP P07550 ADRB2_HUMAN 1 230 DBREF 6PS2 A 1002 1161 UNP D9IEF7 D9IEF7_BPT4 2 161 DBREF 6PS2 A 263 348 UNP P07550 ADRB2_HUMAN 263 348 SEQADV 6PS2 MET A -23 UNP P07550 INITIATING METHIONINE SEQADV 6PS2 LYS A -22 UNP P07550 EXPRESSION TAG SEQADV 6PS2 THR A -21 UNP P07550 EXPRESSION TAG SEQADV 6PS2 ILE A -20 UNP P07550 EXPRESSION TAG SEQADV 6PS2 ILE A -19 UNP P07550 EXPRESSION TAG SEQADV 6PS2 ALA A -18 UNP P07550 EXPRESSION TAG SEQADV 6PS2 LEU A -17 UNP P07550 EXPRESSION TAG SEQADV 6PS2 SER A -16 UNP P07550 EXPRESSION TAG SEQADV 6PS2 TYR A -15 UNP P07550 EXPRESSION TAG SEQADV 6PS2 ILE A -14 UNP P07550 EXPRESSION TAG SEQADV 6PS2 PHE A -13 UNP P07550 EXPRESSION TAG SEQADV 6PS2 CYS A -12 UNP P07550 EXPRESSION TAG SEQADV 6PS2 LEU A -11 UNP P07550 EXPRESSION TAG SEQADV 6PS2 VAL A -10 UNP P07550 EXPRESSION TAG SEQADV 6PS2 PHE A -9 UNP P07550 EXPRESSION TAG SEQADV 6PS2 ALA A -8 UNP P07550 EXPRESSION TAG SEQADV 6PS2 ASP A -7 UNP P07550 EXPRESSION TAG SEQADV 6PS2 TYR A -6 UNP P07550 EXPRESSION TAG SEQADV 6PS2 LYS A -5 UNP P07550 EXPRESSION TAG SEQADV 6PS2 ASP A -4 UNP P07550 EXPRESSION TAG SEQADV 6PS2 ASP A -3 UNP P07550 EXPRESSION TAG SEQADV 6PS2 ASP A -2 UNP P07550 EXPRESSION TAG SEQADV 6PS2 ASP A -1 UNP P07550 EXPRESSION TAG SEQADV 6PS2 ALA A 0 UNP P07550 EXPRESSION TAG SEQADV 6PS2 ARG A 16 UNP P07550 GLY 16 VARIANT SEQADV 6PS2 GLN A 27 UNP P07550 GLU 27 VARIANT SEQADV 6PS2 TRP A 122 UNP P07550 GLU 122 ENGINEERED MUTATION SEQADV 6PS2 GLU A 187 UNP P07550 ASN 187 ENGINEERED MUTATION SEQADV 6PS2 THR A 1054 UNP D9IEF7 CYS 54 ENGINEERED MUTATION SEQADV 6PS2 ALA A 1097 UNP D9IEF7 CYS 97 ENGINEERED MUTATION SEQADV 6PS2 HIS A 349 UNP P07550 EXPRESSION TAG SEQADV 6PS2 HIS A 350 UNP P07550 EXPRESSION TAG SEQADV 6PS2 HIS A 351 UNP P07550 EXPRESSION TAG SEQADV 6PS2 HIS A 352 UNP P07550 EXPRESSION TAG SEQADV 6PS2 HIS A 353 UNP P07550 EXPRESSION TAG SEQADV 6PS2 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 JTZ A1201 18 HET CLR A1202 28 HET OLB A1203 18 HET OLB A1204 12 HET OLB A1205 15 HET OLB A1206 13 HET OLB A1207 13 HET OLB A1208 13 HET OLC A1209 10 HET OLB A1210 18 HET SO4 A1211 5 HET SO4 A1212 5 HET SO4 A1213 5 HET SO4 A1214 5 HET OLC A1215 16 HET OLC A1216 21 HET OLA A1217 14 HET OLA A1218 14 HET OLA A1219 10 HET OLA A1220 13 HETNAM JTZ (2S)-1-[(1-METHYLETHYL)AMINO]-3-(2-PROP-2-EN-1- HETNAM 2 JTZ YLPHENOXY)PROPAN-2-OL HETNAM CLR CHOLESTEROL HETNAM OLB (2S)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM SO4 SULFATE ION HETNAM OLA OLEIC ACID HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 JTZ C15 H23 N O2 FORMUL 3 CLR C27 H46 O FORMUL 4 OLB 7(C21 H40 O4) FORMUL 10 OLC 3(C21 H40 O4) FORMUL 12 SO4 4(O4 S 2-) FORMUL 18 OLA 4(C18 H34 O2) FORMUL 22 HOH *36(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 ASN A 196 PHE A 208 1 13 HELIX 9 AA9 PHE A 208 GLN A 229 1 22 HELIX 10 AB1 ASN A 1002 GLY A 1012 1 11 HELIX 11 AB2 SER A 1038 GLY A 1051 1 14 HELIX 12 AB3 THR A 1059 ASN A 1081 1 23 HELIX 13 AB4 LEU A 1084 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 LEU A 266 GLN A 299 1 34 HELIX 21 AC3 LYS A 305 ASN A 318 1 14 HELIX 22 AC4 PHE A 321 TYR A 326 1 6 HELIX 23 AC5 SER A 329 LEU A 340 1 12 SHEET 1 AA1 3 ARG A1014 LYS A1019 0 SHEET 2 AA1 3 TYR A1025 GLY A1028 -1 O THR A1026 N TYR A1018 SHEET 3 AA1 3 HIS A1031 THR A1034 -1 O LEU A1033 N TYR A1025 SSBOND 1 CYS A 106 CYS A 191 1555 1555 2.03 SSBOND 2 CYS A 184 CYS A 190 1555 1555 2.03 SITE 1 AC1 10 THR A 110 ASP A 113 PHE A 193 SER A 203 SITE 2 AC1 10 SER A 207 TRP A 286 PHE A 289 PHE A 290 SITE 3 AC1 10 ASN A 293 ASN A 312 SITE 1 AC2 5 TYR A 70 CYS A 77 ILE A 154 TRP A 158 SITE 2 AC2 5 OLC A1215 SITE 1 AC3 2 ALA A 59 LYS A 60 SITE 1 AC4 6 PHE A 89 PHE A 101 TRP A 105 PHE A 217 SITE 2 AC4 6 OLA A1219 HOH A1313 SITE 1 AC5 7 VAL A 126 ASP A 130 PHE A 133 LEU A 144 SITE 2 AC5 7 LEU A 145 OLB A1210 HOH A1319 SITE 1 AC6 4 LYS A 273 GLY A 276 GLY A 280 OLA A1220 SITE 1 AC7 3 TRP A 173 ASN A 196 LEU A 340 SITE 1 AC8 3 CYS A 327 GLN A 337 LEU A 342 SITE 1 AC9 3 TRP A 122 VAL A 160 SER A 161 SITE 1 AD1 5 SER A 41 LEU A 95 PHE A 133 OLB A1205 SITE 2 AD1 5 OLA A1219 SITE 1 AD2 6 VAL A 67 THR A 68 ARG A 131 TYR A 141 SITE 2 AD2 6 GLN A 142 SER A 143 SITE 1 AD3 3 LYS A 270 LYS A 273 ARG A 328 SITE 1 AD4 5 PHE A1114 THR A1115 ASN A1116 SER A1117 SITE 2 AD4 5 ASN A1132 SITE 1 AD5 4 THR A1142 PRO A1143 ASN A1144 ARG A1145 SITE 1 AD6 3 ILE A 55 THR A 73 CLR A1202 SITE 1 AD7 4 PHE A 49 GLN A 197 LEU A 339 OLA A1218 SITE 1 AD8 1 ILE A 314 SITE 1 AD9 3 THR A 56 ILE A 298 OLC A1216 SITE 1 AE1 5 THR A 100 PHE A 217 ARG A 221 OLB A1204 SITE 2 AE1 5 OLB A1210 SITE 1 AE2 3 VAL A 216 PHE A 223 OLB A1206 CRYST1 41.650 76.240 171.900 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 0.024010 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013116 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005817 0.00000 ATOM 1 N ARG A 28 15.809 20.498 61.127 1.00144.91 N ANISOU 1 N ARG A 28 22253 18265 14542 -1239 -1399 -2247 N ATOM 2 CA ARG A 28 17.059 21.188 61.444 1.00147.07 C ANISOU 2 CA ARG A 28 22432 18729 14718 -1499 -1485 -2489 C ATOM 3 C ARG A 28 16.806 22.696 61.728 1.00151.16 C ANISOU 3 C ARG A 28 23203 19018 15214 -1719 -1399 -2657 C ATOM 4 O ARG A 28 15.745 23.043 62.258 1.00150.25 O ANISOU 4 O ARG A 28 23317 18698 15074 -1595 -1325 -2609 O ATOM 5 CB ARG A 28 18.084 20.985 60.310 1.00147.67 C ANISOU 5 CB ARG A 28 22285 18929 14895 -1670 -1512 -2510 C ATOM 6 N ASP A 29 17.787 23.574 61.410 1.00148.66 N ANISOU 6 N ASP A 29 22849 18741 14895 -2045 -1402 -2859 N ATOM 7 CA ASP A 29 17.696 25.020 61.630 1.00149.80 C ANISOU 7 CA ASP A 29 23241 18664 15011 -2290 -1310 -3037 C ATOM 8 C ASP A 29 16.982 25.726 60.446 1.00151.24 C ANISOU 8 C ASP A 29 23642 18457 15367 -2364 -1134 -2934 C ATOM 9 O ASP A 29 16.706 25.095 59.419 1.00148.42 O ANISOU 9 O ASP A 29 23201 18042 15149 -2259 -1099 -2747 O ATOM 10 CB ASP A 29 19.100 25.621 61.894 1.00154.53 C ANISOU 10 CB ASP A 29 23703 19497 15513 -2624 -1386 -3320 C ATOM 11 CG ASP A 29 19.927 25.993 60.671 1.00164.48 C ANISOU 11 CG ASP A 29 24863 20738 16896 -2913 -1331 -3379 C ATOM 12 OD1 ASP A 29 20.113 25.121 59.786 1.00162.60 O ANISOU 12 OD1 ASP A 29 24431 20586 16765 -2818 -1353 -3224 O ATOM 13 OD2 ASP A 29 20.428 27.140 60.621 1.00172.45 O ANISOU 13 OD2 ASP A 29 25986 21652 17886 -3243 -1263 -3588 O ATOM 14 N GLU A 30 16.693 27.041 60.616 1.00148.28 N ANISOU 14 N GLU A 30 23555 17815 14968 -2538 -1021 -3061 N ATOM 15 CA GLU A 30 16.007 27.943 59.678 1.00146.91 C ANISOU 15 CA GLU A 30 23654 17250 14915 -2606 -843 -2995 C ATOM 16 C GLU A 30 16.503 27.798 58.225 1.00148.56 C ANISOU 16 C GLU A 30 23745 17424 15276 -2738 -795 -2920 C ATOM 17 O GLU A 30 15.672 27.724 57.321 1.00146.31 O ANISOU 17 O GLU A 30 23564 16914 15113 -2597 -697 -2732 O ATOM 18 CB GLU A 30 16.172 29.404 60.140 1.00150.95 C ANISOU 18 CB GLU A 30 24447 17562 15344 -2868 -751 -3219 C ATOM 19 CG GLU A 30 15.151 30.377 59.571 1.00159.76 C ANISOU 19 CG GLU A 30 25930 18241 16529 -2835 -561 -3140 C ATOM 20 CD GLU A 30 15.467 31.844 59.803 1.00181.94 C ANISOU 20 CD GLU A 30 29034 20823 19270 -3135 -445 -3363 C ATOM 21 OE1 GLU A 30 15.635 32.241 60.980 1.00176.83 O ANISOU 21 OE1 GLU A 30 28458 20251 18479 -3201 -490 -3542 O ATOM 22 OE2 GLU A 30 15.525 32.604 58.809 1.00175.32 O ANISOU 22 OE2 GLU A 30 28375 19722 18517 -3301 -300 -3358 O ATOM 23 N VAL A 31 17.837 27.746 58.012 1.00145.45 N ANISOU 23 N VAL A 31 23127 17270 14868 -2997 -864 -3070 N ATOM 24 CA VAL A 31 18.484 27.624 56.696 1.00144.35 C ANISOU 24 CA VAL A 31 22853 17138 14857 -3156 -823 -3029 C ATOM 25 C VAL A 31 17.976 26.370 55.963 1.00144.27 C ANISOU 25 C VAL A 31 22674 17183 14959 -2864 -859 -2766 C ATOM 26 O VAL A 31 17.659 26.447 54.774 1.00142.87 O ANISOU 26 O VAL A 31 22558 16812 14914 -2863 -758 -2636 O ATOM 27 CB VAL A 31 20.033 27.628 56.822 1.00150.55 C ANISOU 27 CB VAL A 31 23370 18253 15577 -3455 -917 -3252 C ATOM 28 CG1 VAL A 31 20.714 27.311 55.487 1.00149.74 C ANISOU 28 CG1 VAL A 31 23085 18207 15604 -3584 -887 -3193 C ATOM 29 CG2 VAL A 31 20.534 28.961 57.375 1.00153.63 C ANISOU 29 CG2 VAL A 31 23946 18557 15872 -3798 -852 -3527 C ATOM 30 N TRP A 32 17.872 25.239 56.680 1.00138.47 N ANISOU 30 N TRP A 32 21749 16700 14163 -2615 -993 -2691 N ATOM 31 CA TRP A 32 17.406 23.977 56.116 1.00134.75 C ANISOU 31 CA TRP A 32 21123 16293 13782 -2342 -1027 -2458 C ATOM 32 C TRP A 32 15.902 24.016 55.835 1.00131.24 C ANISOU 32 C TRP A 32 20905 15545 13415 -2111 -916 -2266 C ATOM 33 O TRP A 32 15.506 23.583 54.764 1.00129.48 O ANISOU 33 O TRP A 32 20647 15227 13320 -2022 -863 -2102 O ATOM 34 CB TRP A 32 17.759 22.801 57.043 1.00134.23 C ANISOU 34 CB TRP A 32 20824 16570 13608 -2148 -1187 -2444 C ATOM 35 CG TRP A 32 17.401 21.441 56.506 1.00133.30 C ANISOU 35 CG TRP A 32 20548 16529 13571 -1887 -1217 -2220 C ATOM 36 CD1 TRP A 32 18.063 20.736 55.542 1.00135.58 C ANISOU 36 CD1 TRP A 32 20617 16951 13946 -1909 -1247 -2154 C ATOM 37 CD2 TRP A 32 16.327 20.600 56.954 1.00131.77 C ANISOU 37 CD2 TRP A 32 20406 16291 13369 -1573 -1215 -2044 C ATOM 38 NE1 TRP A 32 17.446 19.520 55.334 1.00133.12 N ANISOU 38 NE1 TRP A 32 20233 16663 13684 -1629 -1260 -1948 N ATOM 39 CE2 TRP A 32 16.380 19.409 56.193 1.00134.25 C ANISOU 39 CE2 TRP A 32 20539 16700 13771 -1428 -1237 -1879 C ATOM 40 CE3 TRP A 32 15.300 20.750 57.905 1.00132.97 C ANISOU 40 CE3 TRP A 32 20748 16325 13448 -1407 -1183 -2013 C ATOM 41 CZ2 TRP A 32 15.464 18.363 56.375 1.00131.90 C ANISOU 41 CZ2 TRP A 32 20247 16381 13489 -1142 -1226 -1693 C ATOM 42 CZ3 TRP A 32 14.396 19.715 58.086 1.00132.68 C ANISOU 42 CZ3 TRP A 32 20704 16281 13428 -1122 -1173 -1826 C ATOM 43 CH2 TRP A 32 14.474 18.545 57.320 1.00131.72 C ANISOU 43 CH2 TRP A 32 20406 16246 13394 -1001 -1190 -1671 C ATOM 44 N VAL A 33 15.078 24.543 56.766 1.00123.75 N ANISOU 44 N VAL A 33 20178 14458 12384 -2015 -881 -2296 N ATOM 45 CA VAL A 33 13.611 24.609 56.630 1.00119.98 C ANISOU 45 CA VAL A 33 19903 13725 11958 -1781 -779 -2132 C ATOM 46 C VAL A 33 13.205 25.476 55.422 1.00120.96 C ANISOU 46 C VAL A 33 20220 13543 12197 -1870 -632 -2082 C ATOM 47 O VAL A 33 12.299 25.075 54.683 1.00119.30 O ANISOU 47 O VAL A 33 20030 13216 12084 -1679 -574 -1900 O ATOM 48 CB VAL A 33 12.910 25.079 57.932 1.00124.16 C ANISOU 48 CB VAL A 33 20630 14186 12358 -1677 -769 -2198 C ATOM 49 CG1 VAL A 33 11.388 24.977 57.821 1.00121.82 C ANISOU 49 CG1 VAL A 33 20493 13683 12111 -1407 -674 -2024 C ATOM 50 CG2 VAL A 33 13.403 24.282 59.136 1.00124.56 C ANISOU 50 CG2 VAL A 33 20505 14546 12275 -1597 -914 -2258 C ATOM 51 N VAL A 34 13.889 26.621 55.197 1.00116.83 N ANISOU 51 N VAL A 34 19833 12899 11658 -2158 -570 -2244 N ATOM 52 CA VAL A 34 13.602 27.512 54.064 1.00115.75 C ANISOU 52 CA VAL A 34 19910 12460 11611 -2252 -418 -2203 C ATOM 53 C VAL A 34 13.994 26.804 52.747 1.00117.13 C ANISOU 53 C VAL A 34 19879 12708 11916 -2267 -425 -2079 C ATOM 54 O VAL A 34 13.145 26.669 51.867 1.00114.96 O ANISOU 54 O VAL A 34 19674 12273 11732 -2100 -351 -1909 O ATOM 55 CB VAL A 34 14.259 28.905 54.203 1.00122.08 C ANISOU 55 CB VAL A 34 20936 13099 12352 -2573 -331 -2414 C ATOM 56 CG1 VAL A 34 14.040 29.749 52.952 1.00121.96 C ANISOU 56 CG1 VAL A 34 21146 12769 12423 -2663 -165 -2356 C ATOM 57 CG2 VAL A 34 13.725 29.637 55.429 1.00123.50 C ANISOU 57 CG2 VAL A 34 21354 13166 12404 -2533 -307 -2523 C ATOM 58 N GLY A 35 15.240 26.325 52.659 1.00113.24 N ANISOU 58 N GLY A 35 19126 12478 11423 -2446 -519 -2167 N ATOM 59 CA GLY A 35 15.764 25.594 51.505 1.00111.43 C ANISOU 59 CA GLY A 35 18674 12359 11304 -2472 -539 -2070 C ATOM 60 C GLY A 35 14.959 24.356 51.146 1.00111.77 C ANISOU 60 C GLY A 35 18580 12466 11420 -2159 -581 -1850 C ATOM 61 O GLY A 35 14.755 24.076 49.965 1.00109.56 O ANISOU 61 O GLY A 35 18266 12111 11251 -2115 -529 -1720 O ATOM 62 N MET A 36 14.474 23.624 52.173 1.00107.97 N ANISOU 62 N MET A 36 18034 12118 10872 -1946 -666 -1813 N ATOM 63 CA MET A 36 13.622 22.443 52.045 1.00105.58 C ANISOU 63 CA MET A 36 17626 11869 10619 -1654 -693 -1621 C ATOM 64 C MET A 36 12.216 22.859 51.592 1.00104.79 C ANISOU 64 C MET A 36 17748 11492 10577 -1489 -573 -1496 C ATOM 65 O MET A 36 11.566 22.118 50.863 1.00101.23 O ANISOU 65 O MET A 36 17222 11027 10214 -1321 -553 -1336 O ATOM 66 CB MET A 36 13.555 21.688 53.378 1.00108.93 C ANISOU 66 CB MET A 36 17958 12497 10933 -1501 -798 -1638 C ATOM 67 CG MET A 36 13.073 20.271 53.251 1.00112.14 C ANISOU 67 CG MET A 36 18203 13023 11384 -1255 -838 -1465 C ATOM 68 SD MET A 36 14.447 19.111 53.102 1.00118.05 S ANISOU 68 SD MET A 36 18625 14109 12120 -1293 -971 -1478 S ATOM 69 CE MET A 36 14.713 19.110 51.286 1.00113.44 C ANISOU 69 CE MET A 36 17967 13429 11706 -1405 -903 -1394 C ATOM 70 N GLY A 37 11.771 24.036 52.040 1.00101.24 N ANISOU 70 N GLY A 37 17565 10835 10068 -1534 -494 -1578 N ATOM 71 CA GLY A 37 10.480 24.600 51.672 1.00 99.44 C ANISOU 71 CA GLY A 37 17567 10347 9869 -1372 -377 -1482 C ATOM 72 C GLY A 37 10.432 24.991 50.210 1.00100.88 C ANISOU 72 C GLY A 37 17813 10362 10154 -1424 -285 -1405 C ATOM 73 O GLY A 37 9.435 24.719 49.539 1.00 98.97 O ANISOU 73 O GLY A 37 17595 10035 9975 -1223 -234 -1258 O ATOM 74 N ILE A 38 11.519 25.627 49.706 1.00 97.54 N ANISOU 74 N ILE A 38 17413 9906 9743 -1700 -259 -1510 N ATOM 75 CA ILE A 38 11.666 26.061 48.318 1.00 97.30 C ANISOU 75 CA ILE A 38 17454 9718 9797 -1787 -165 -1452 C ATOM 76 C ILE A 38 11.690 24.839 47.395 1.00101.50 C ANISOU 76 C ILE A 38 17721 10410 10433 -1678 -220 -1306 C ATOM 77 O ILE A 38 10.974 24.818 46.391 1.00101.24 O ANISOU 77 O ILE A 38 17747 10252 10468 -1546 -151 -1174 O ATOM 78 CB ILE A 38 12.936 26.940 48.121 1.00102.18 C ANISOU 78 CB ILE A 38 18135 10295 10393 -2140 -123 -1618 C ATOM 79 CG1 ILE A 38 12.880 28.220 48.987 1.00104.87 C ANISOU 79 CG1 ILE A 38 18774 10444 10628 -2264 -48 -1773 C ATOM 80 CG2 ILE A 38 13.157 27.292 46.629 1.00101.43 C ANISOU 80 CG2 ILE A 38 18103 10050 10385 -2234 -18 -1547 C ATOM 81 CD1 ILE A 38 14.273 28.861 49.314 1.00112.90 C ANISOU 81 CD1 ILE A 38 19778 11526 11592 -2644 -50 -1997 C ATOM 82 N VAL A 39 12.524 23.836 47.737 1.00 97.61 N ANISOU 82 N VAL A 39 16945 10198 9943 -1727 -342 -1335 N ATOM 83 CA VAL A 39 12.723 22.598 46.981 1.00 95.41 C ANISOU 83 CA VAL A 39 16405 10094 9751 -1643 -403 -1217 C ATOM 84 C VAL A 39 11.382 21.864 46.825 1.00 95.57 C ANISOU 84 C VAL A 39 16419 10080 9813 -1345 -390 -1051 C ATOM 85 O VAL A 39 11.061 21.464 45.714 1.00 94.40 O ANISOU 85 O VAL A 39 16214 9900 9753 -1271 -357 -935 O ATOM 86 CB VAL A 39 13.838 21.724 47.636 1.00100.10 C ANISOU 86 CB VAL A 39 16730 10998 10305 -1719 -537 -1295 C ATOM 87 CG1 VAL A 39 13.667 20.231 47.351 1.00 97.77 C ANISOU 87 CG1 VAL A 39 16201 10882 10066 -1526 -608 -1156 C ATOM 88 CG2 VAL A 39 15.220 22.198 47.194 1.00101.57 C ANISOU 88 CG2 VAL A 39 16837 11260 10494 -2016 -541 -1425 C ATOM 89 N MET A 40 10.591 21.740 47.906 1.00 90.40 N ANISOU 89 N MET A 40 15826 9430 9091 -1187 -408 -1050 N ATOM 90 CA MET A 40 9.287 21.074 47.883 1.00 87.57 C ANISOU 90 CA MET A 40 15456 9053 8762 -924 -387 -915 C ATOM 91 C MET A 40 8.259 21.870 47.070 1.00 89.21 C ANISOU 91 C MET A 40 15863 9030 9004 -826 -272 -847 C ATOM 92 O MET A 40 7.397 21.267 46.436 1.00 86.34 O ANISOU 92 O MET A 40 15432 8673 8699 -652 -250 -725 O ATOM 93 CB MET A 40 8.780 20.826 49.299 1.00 90.08 C ANISOU 93 CB MET A 40 15801 9438 8988 -802 -424 -945 C ATOM 94 CG MET A 40 9.397 19.622 49.922 1.00 93.99 C ANISOU 94 CG MET A 40 16075 10180 9459 -781 -530 -943 C ATOM 95 SD MET A 40 9.252 19.698 51.702 1.00101.33 S ANISOU 95 SD MET A 40 17077 11183 10241 -720 -578 -1033 S ATOM 96 CE MET A 40 9.365 17.991 52.081 1.00 97.30 C ANISOU 96 CE MET A 40 16335 10910 9726 -571 -657 -938 C ATOM 97 N SER A 41 8.367 23.212 47.068 1.00 87.26 N ANISOU 97 N SER A 41 15861 8583 8710 -935 -198 -928 N ATOM 98 CA SER A 41 7.500 24.095 46.283 1.00 87.04 C ANISOU 98 CA SER A 41 16057 8321 8692 -834 -82 -869 C ATOM 99 C SER A 41 7.778 23.882 44.800 1.00 89.97 C ANISOU 99 C SER A 41 16352 8676 9156 -871 -55 -783 C ATOM 100 O SER A 41 6.827 23.735 44.037 1.00 89.48 O ANISOU 100 O SER A 41 16306 8562 9129 -681 -11 -670 O ATOM 101 CB SER A 41 7.707 25.558 46.670 1.00 90.94 C ANISOU 101 CB SER A 41 16854 8594 9105 -962 0 -985 C ATOM 102 OG SER A 41 7.417 25.746 48.043 1.00 94.86 O ANISOU 102 OG SER A 41 17422 9109 9510 -918 -26 -1067 O ATOM 103 N LEU A 42 9.074 23.785 44.405 1.00 86.19 N ANISOU 103 N LEU A 42 15766 8271 8711 -1108 -86 -840 N ATOM 104 CA LEU A 42 9.488 23.553 43.011 1.00 85.12 C ANISOU 104 CA LEU A 42 15547 8136 8659 -1166 -61 -767 C ATOM 105 C LEU A 42 9.021 22.192 42.529 1.00 83.99 C ANISOU 105 C LEU A 42 15157 8165 8590 -992 -124 -643 C ATOM 106 O LEU A 42 8.514 22.087 41.415 1.00 83.99 O ANISOU 106 O LEU A 42 15161 8111 8643 -891 -78 -542 O ATOM 107 CB LEU A 42 11.015 23.699 42.811 1.00 86.63 C ANISOU 107 CB LEU A 42 15652 8401 8863 -1466 -82 -871 C ATOM 108 CG LEU A 42 11.625 25.100 43.080 1.00 94.51 C ANISOU 108 CG LEU A 42 16899 9215 9796 -1702 3 -1010 C ATOM 109 CD1 LEU A 42 13.136 25.037 43.155 1.00 95.78 C ANISOU 109 CD1 LEU A 42 16904 9530 9959 -2001 -42 -1139 C ATOM 110 CD2 LEU A 42 11.181 26.131 42.041 1.00 97.61 C ANISOU 110 CD2 LEU A 42 17572 9323 10192 -1689 151 -953 C ATOM 111 N ILE A 43 9.131 21.173 43.369 1.00 77.91 N ANISOU 111 N ILE A 43 14194 7594 7816 -946 -219 -652 N ATOM 112 CA ILE A 43 8.685 19.820 43.035 1.00 75.90 C ANISOU 112 CA ILE A 43 13722 7494 7623 -791 -267 -544 C ATOM 113 C ILE A 43 7.139 19.826 42.814 1.00 80.72 C ANISOU 113 C ILE A 43 14414 8017 8239 -551 -208 -452 C ATOM 114 O ILE A 43 6.694 19.296 41.804 1.00 79.77 O ANISOU 114 O ILE A 43 14205 7920 8183 -459 -191 -360 O ATOM 115 CB ILE A 43 9.175 18.778 44.087 1.00 77.75 C ANISOU 115 CB ILE A 43 13771 7941 7830 -790 -368 -576 C ATOM 116 CG1 ILE A 43 10.721 18.667 44.030 1.00 79.21 C ANISOU 116 CG1 ILE A 43 13827 8256 8015 -1005 -432 -658 C ATOM 117 CG2 ILE A 43 8.539 17.402 43.862 1.00 74.56 C ANISOU 117 CG2 ILE A 43 13191 7658 7479 -617 -392 -464 C ATOM 118 CD1 ILE A 43 11.417 18.061 45.299 1.00 91.79 C ANISOU 118 CD1 ILE A 43 15294 10050 9533 -1028 -534 -734 C ATOM 119 N VAL A 44 6.349 20.493 43.691 1.00 78.29 N ANISOU 119 N VAL A 44 14276 7612 7857 -455 -172 -487 N ATOM 120 CA VAL A 44 4.885 20.600 43.536 1.00 77.05 C ANISOU 120 CA VAL A 44 14193 7391 7690 -223 -113 -416 C ATOM 121 C VAL A 44 4.562 21.333 42.207 1.00 81.48 C ANISOU 121 C VAL A 44 14878 7807 8275 -178 -37 -361 C ATOM 122 O VAL A 44 3.736 20.848 41.423 1.00 79.00 O ANISOU 122 O VAL A 44 14477 7539 7999 -21 -22 -274 O ATOM 123 CB VAL A 44 4.208 21.280 44.764 1.00 80.87 C ANISOU 123 CB VAL A 44 14850 7798 8078 -135 -84 -475 C ATOM 124 CG1 VAL A 44 2.759 21.680 44.472 1.00 80.40 C ANISOU 124 CG1 VAL A 44 14897 7657 7995 101 -9 -416 C ATOM 125 CG2 VAL A 44 4.266 20.375 45.982 1.00 79.83 C ANISOU 125 CG2 VAL A 44 14584 7829 7919 -121 -152 -502 C ATOM 126 N LEU A 45 5.255 22.465 41.941 1.00 80.31 N ANISOU 126 N LEU A 45 14928 7490 8096 -325 13 -415 N ATOM 127 CA LEU A 45 5.052 23.256 40.727 1.00 80.55 C ANISOU 127 CA LEU A 45 15120 7357 8129 -288 98 -362 C ATOM 128 C LEU A 45 5.401 22.446 39.478 1.00 81.18 C ANISOU 128 C LEU A 45 15006 7542 8298 -313 72 -284 C ATOM 129 O LEU A 45 4.573 22.393 38.569 1.00 78.93 O ANISOU 129 O LEU A 45 14727 7240 8024 -139 107 -198 O ATOM 130 CB LEU A 45 5.837 24.570 40.771 1.00 82.95 C ANISOU 130 CB LEU A 45 15688 7450 8381 -476 171 -445 C ATOM 131 CG LEU A 45 5.349 25.592 41.797 1.00 90.13 C ANISOU 131 CG LEU A 45 16855 8199 9190 -426 226 -517 C ATOM 132 CD1 LEU A 45 6.411 26.639 42.076 1.00 92.32 C ANISOU 132 CD1 LEU A 45 17339 8315 9424 -692 280 -635 C ATOM 133 CD2 LEU A 45 4.040 26.235 41.368 1.00 94.43 C ANISOU 133 CD2 LEU A 45 17597 8601 9681 -152 311 -440 C ATOM 134 N ALA A 46 6.572 21.760 39.467 1.00 77.01 N ANISOU 134 N ALA A 46 14293 7142 7824 -509 7 -317 N ATOM 135 CA ALA A 46 7.025 20.899 38.355 1.00 75.08 C ANISOU 135 CA ALA A 46 13851 7013 7663 -545 -23 -251 C ATOM 136 C ALA A 46 6.061 19.749 38.063 1.00 75.43 C ANISOU 136 C ALA A 46 13707 7201 7752 -344 -59 -165 C ATOM 137 O ALA A 46 5.856 19.436 36.902 1.00 75.92 O ANISOU 137 O ALA A 46 13704 7283 7858 -286 -44 -93 O ATOM 138 CB ALA A 46 8.405 20.323 38.642 1.00 75.64 C ANISOU 138 CB ALA A 46 13749 7224 7767 -763 -93 -314 C ATOM 139 N ILE A 47 5.503 19.102 39.091 1.00 70.29 N ANISOU 139 N ILE A 47 12969 6652 7087 -252 -102 -177 N ATOM 140 CA ILE A 47 4.582 17.979 38.901 1.00 68.58 C ANISOU 140 CA ILE A 47 12577 6571 6910 -90 -121 -111 C ATOM 141 C ILE A 47 3.271 18.454 38.258 1.00 72.61 C ANISOU 141 C ILE A 47 13176 7015 7396 112 -59 -60 C ATOM 142 O ILE A 47 2.808 17.816 37.318 1.00 73.02 O ANISOU 142 O ILE A 47 13102 7149 7493 196 -59 -1 O ATOM 143 CB ILE A 47 4.319 17.228 40.229 1.00 71.53 C ANISOU 143 CB ILE A 47 12862 7053 7262 -52 -163 -139 C ATOM 144 CG1 ILE A 47 5.582 16.556 40.777 1.00 71.66 C ANISOU 144 CG1 ILE A 47 12758 7178 7293 -210 -236 -178 C ATOM 145 CG2 ILE A 47 3.183 16.221 40.090 1.00 71.82 C ANISOU 145 CG2 ILE A 47 12759 7202 7329 110 -152 -82 C ATOM 146 CD1 ILE A 47 5.441 16.139 42.284 1.00 78.10 C ANISOU 146 CD1 ILE A 47 13558 8066 8049 -175 -270 -219 C ATOM 147 N VAL A 48 2.681 19.543 38.766 1.00 69.91 N ANISOU 147 N VAL A 48 13047 6541 6976 199 -8 -88 N ATOM 148 CA VAL A 48 1.408 20.120 38.314 1.00 70.38 C ANISOU 148 CA VAL A 48 13210 6544 6985 424 51 -49 C ATOM 149 C VAL A 48 1.540 20.637 36.874 1.00 79.03 C ANISOU 149 C VAL A 48 14386 7556 8087 448 91 7 C ATOM 150 O VAL A 48 0.807 20.169 35.996 1.00 78.63 O ANISOU 150 O VAL A 48 14222 7600 8052 590 90 63 O ATOM 151 CB VAL A 48 0.905 21.238 39.294 1.00 74.34 C ANISOU 151 CB VAL A 48 13951 6905 7389 506 100 -99 C ATOM 152 CG1 VAL A 48 -0.242 22.053 38.693 1.00 74.58 C ANISOU 152 CG1 VAL A 48 14131 6855 7350 748 169 -57 C ATOM 153 CG2 VAL A 48 0.492 20.653 40.647 1.00 73.10 C ANISOU 153 CG2 VAL A 48 13703 6855 7216 535 69 -141 C ATOM 154 N PHE A 49 2.463 21.605 36.638 1.00 78.89 N ANISOU 154 N PHE A 49 14567 7362 8046 303 132 -14 N ATOM 155 CA PHE A 49 2.694 22.236 35.334 1.00 79.20 C ANISOU 155 CA PHE A 49 14733 7285 8076 309 189 39 C ATOM 156 C PHE A 49 2.924 21.166 34.312 1.00 76.02 C ANISOU 156 C PHE A 49 14090 7040 7754 286 142 93 C ATOM 157 O PHE A 49 2.213 21.108 33.316 1.00 74.96 O ANISOU 157 O PHE A 49 13937 6938 7607 453 160 157 O ATOM 158 CB PHE A 49 3.882 23.232 35.390 1.00 84.04 C ANISOU 158 CB PHE A 49 15560 7703 8667 81 244 -12 C ATOM 159 CG PHE A 49 4.274 23.939 34.099 1.00 89.01 C ANISOU 159 CG PHE A 49 16353 8185 9279 49 325 40 C ATOM 160 CD1 PHE A 49 5.167 23.350 33.202 1.00 91.64 C ANISOU 160 CD1 PHE A 49 16536 8598 9687 -102 302 65 C ATOM 161 CD2 PHE A 49 3.823 25.231 33.823 1.00 94.73 C ANISOU 161 CD2 PHE A 49 17407 8679 9906 164 433 61 C ATOM 162 CE1 PHE A 49 5.560 24.024 32.038 1.00 93.79 C ANISOU 162 CE1 PHE A 49 16973 8728 9937 -141 388 113 C ATOM 163 CE2 PHE A 49 4.224 25.906 32.657 1.00 98.31 C ANISOU 163 CE2 PHE A 49 18042 8979 10333 131 522 114 C ATOM 164 CZ PHE A 49 5.096 25.302 31.784 1.00 95.35 C ANISOU 164 CZ PHE A 49 17505 8689 10033 -29 500 138 C ATOM 165 N GLY A 50 3.886 20.308 34.589 1.00 70.09 N ANISOU 165 N GLY A 50 13155 6399 7078 96 80 63 N ATOM 166 CA GLY A 50 4.267 19.216 33.709 1.00 68.85 C ANISOU 166 CA GLY A 50 12770 6390 7001 51 35 106 C ATOM 167 C GLY A 50 3.136 18.298 33.303 1.00 72.35 C ANISOU 167 C GLY A 50 13039 6986 7465 241 10 152 C ATOM 168 O GLY A 50 3.039 17.943 32.130 1.00 70.97 O ANISOU 168 O GLY A 50 12785 6864 7316 286 12 203 O ATOM 169 N ASN A 51 2.281 17.894 34.265 1.00 69.43 N ANISOU 169 N ASN A 51 12605 6694 7080 344 -8 128 N ATOM 170 CA ASN A 51 1.192 16.952 33.994 1.00 68.68 C ANISOU 170 CA ASN A 51 12327 6763 7007 495 -23 151 C ATOM 171 C ASN A 51 -0.054 17.622 33.421 1.00 73.79 C ANISOU 171 C ASN A 51 13059 7397 7582 726 20 176 C ATOM 172 O ASN A 51 -0.762 16.980 32.644 1.00 72.11 O ANISOU 172 O ASN A 51 12694 7322 7385 831 11 198 O ATOM 173 CB ASN A 51 0.869 16.116 35.219 1.00 68.76 C ANISOU 173 CB ASN A 51 12217 6875 7032 486 -50 113 C ATOM 174 CG ASN A 51 1.916 15.055 35.382 1.00 73.98 C ANISOU 174 CG ASN A 51 12729 7615 7766 317 -99 110 C ATOM 175 OD1 ASN A 51 1.994 14.114 34.590 1.00 63.34 O ANISOU 175 OD1 ASN A 51 11221 6367 6476 301 -115 139 O ATOM 176 ND2 ASN A 51 2.845 15.277 36.283 1.00 59.79 N ANISOU 176 ND2 ASN A 51 10992 5768 5958 186 -124 71 N ATOM 177 N VAL A 52 -0.292 18.909 33.730 1.00 73.17 N ANISOU 177 N VAL A 52 13224 7159 7419 808 69 169 N ATOM 178 CA VAL A 52 -1.387 19.665 33.101 1.00 73.77 C ANISOU 178 CA VAL A 52 13410 7212 7406 1056 114 200 C ATOM 179 C VAL A 52 -1.059 19.722 31.611 1.00 80.19 C ANISOU 179 C VAL A 52 14227 8016 8227 1066 122 259 C ATOM 180 O VAL A 52 -1.915 19.396 30.792 1.00 82.08 O ANISOU 180 O VAL A 52 14355 8389 8444 1237 113 285 O ATOM 181 CB VAL A 52 -1.634 21.070 33.727 1.00 76.93 C ANISOU 181 CB VAL A 52 14111 7416 7705 1151 177 185 C ATOM 182 CG1 VAL A 52 -2.538 21.931 32.852 1.00 77.02 C ANISOU 182 CG1 VAL A 52 14272 7382 7612 1416 229 233 C ATOM 183 CG2 VAL A 52 -2.239 20.931 35.108 1.00 76.59 C ANISOU 183 CG2 VAL A 52 14037 7423 7641 1195 169 128 C ATOM 184 N LEU A 53 0.214 20.006 31.285 1.00 76.19 N ANISOU 184 N LEU A 53 13814 7381 7755 867 134 271 N ATOM 185 CA LEU A 53 0.748 20.096 29.929 1.00 76.41 C ANISOU 185 CA LEU A 53 13865 7377 7792 835 151 327 C ATOM 186 C LEU A 53 0.505 18.807 29.124 1.00 76.99 C ANISOU 186 C LEU A 53 13654 7669 7931 856 94 346 C ATOM 187 O LEU A 53 -0.036 18.859 28.021 1.00 76.96 O ANISOU 187 O LEU A 53 13637 7718 7885 1008 103 389 O ATOM 188 CB LEU A 53 2.247 20.388 30.034 1.00 77.12 C ANISOU 188 CB LEU A 53 14043 7333 7926 562 169 310 C ATOM 189 CG LEU A 53 2.954 20.985 28.845 1.00 83.39 C ANISOU 189 CG LEU A 53 14978 8006 8702 499 228 359 C ATOM 190 CD1 LEU A 53 2.287 22.291 28.382 1.00 85.59 C ANISOU 190 CD1 LEU A 53 15559 8105 8858 697 318 405 C ATOM 191 CD2 LEU A 53 4.397 21.236 29.197 1.00 87.17 C ANISOU 191 CD2 LEU A 53 15513 8384 9226 207 246 315 C ATOM 192 N VAL A 54 0.841 17.661 29.709 1.00 70.76 N ANISOU 192 N VAL A 54 12649 7006 7231 721 38 310 N ATOM 193 CA VAL A 54 0.666 16.339 29.110 1.00 68.27 C ANISOU 193 CA VAL A 54 12074 6883 6984 713 -7 314 C ATOM 194 C VAL A 54 -0.823 16.075 28.837 1.00 73.03 C ANISOU 194 C VAL A 54 12573 7634 7540 937 -10 307 C ATOM 195 O VAL A 54 -1.167 15.671 27.732 1.00 73.79 O ANISOU 195 O VAL A 54 12564 7839 7634 1011 -21 327 O ATOM 196 CB VAL A 54 1.308 15.255 30.005 1.00 70.25 C ANISOU 196 CB VAL A 54 12163 7208 7321 539 -51 277 C ATOM 197 CG1 VAL A 54 0.977 13.850 29.504 1.00 69.11 C ANISOU 197 CG1 VAL A 54 11773 7246 7238 543 -81 275 C ATOM 198 CG2 VAL A 54 2.820 15.457 30.089 1.00 69.76 C ANISOU 198 CG2 VAL A 54 12162 7049 7297 327 -58 276 C ATOM 199 N AILE A 55 -1.696 16.350 29.818 0.50 70.69 N ANISOU 199 N AILE A 55 12307 7352 7198 1045 2 271 N ATOM 200 N BILE A 55 -1.697 16.352 29.814 0.50 70.76 N ANISOU 200 N BILE A 55 12317 7361 7207 1046 2 271 N ATOM 201 CA AILE A 55 -3.136 16.122 29.700 0.50 70.80 C ANISOU 201 CA AILE A 55 12205 7533 7163 1251 4 246 C ATOM 202 CA BILE A 55 -3.134 16.116 29.687 0.50 70.90 C ANISOU 202 CA BILE A 55 12217 7547 7176 1251 4 246 C ATOM 203 C AILE A 55 -3.721 17.050 28.632 0.50 76.52 C ANISOU 203 C AILE A 55 13048 8242 7783 1470 26 286 C ATOM 204 C BILE A 55 -3.724 17.052 28.629 0.50 76.58 C ANISOU 204 C BILE A 55 13056 8250 7791 1471 26 286 C ATOM 205 O AILE A 55 -4.474 16.570 27.786 0.50 76.73 O ANISOU 205 O AILE A 55 12916 8448 7788 1591 6 278 O ATOM 206 O BILE A 55 -4.483 16.578 27.785 0.50 76.80 O ANISOU 206 O BILE A 55 12927 8457 7797 1593 7 278 O ATOM 207 CB AILE A 55 -3.861 16.237 31.075 0.50 73.91 C ANISOU 207 CB AILE A 55 12610 7944 7528 1308 21 196 C ATOM 208 CB BILE A 55 -3.855 16.202 31.064 0.50 74.03 C ANISOU 208 CB BILE A 55 12619 7963 7546 1305 20 196 C ATOM 209 CG1AILE A 55 -3.393 15.121 32.032 0.50 72.24 C ANISOU 209 CG1AILE A 55 12259 7782 7409 1116 0 162 C ATOM 210 CG1BILE A 55 -3.404 15.036 31.967 0.50 72.42 C ANISOU 210 CG1BILE A 55 12265 7816 7436 1113 -1 162 C ATOM 211 CG2AILE A 55 -5.392 16.189 30.913 0.50 76.06 C ANISOU 211 CG2AILE A 55 12770 8398 7730 1538 32 163 C ATOM 212 CG2BILE A 55 -5.388 16.191 30.906 0.50 76.21 C ANISOU 212 CG2BILE A 55 12789 8417 7749 1538 32 163 C ATOM 213 CD1AILE A 55 -3.616 15.407 33.532 0.50 78.08 C ANISOU 213 CD1AILE A 55 13079 8468 8121 1114 20 125 C ATOM 214 CD1BILE A 55 -3.595 15.254 33.451 0.50 79.18 C ANISOU 214 CD1BILE A 55 13191 8623 8270 1103 16 125 C ATOM 215 N THR A 56 -3.320 18.340 28.630 1.00 74.20 N ANISOU 215 N THR A 56 13038 7735 7421 1514 70 326 N ATOM 216 CA THR A 56 -3.793 19.368 27.677 1.00 74.46 C ANISOU 216 CA THR A 56 13250 7707 7334 1741 107 378 C ATOM 217 C THR A 56 -3.365 19.033 26.238 1.00 76.73 C ANISOU 217 C THR A 56 13477 8042 7635 1721 92 426 C ATOM 218 O THR A 56 -4.177 19.181 25.322 1.00 77.01 O ANISOU 218 O THR A 56 13485 8191 7584 1943 87 446 O ATOM 219 CB THR A 56 -3.329 20.768 28.127 1.00 76.20 C ANISOU 219 CB THR A 56 13819 7649 7485 1748 177 405 C ATOM 220 OG1 THR A 56 -3.853 20.987 29.428 1.00 74.80 O ANISOU 220 OG1 THR A 56 13673 7460 7289 1789 185 354 O ATOM 221 CG2 THR A 56 -3.834 21.888 27.228 1.00 75.82 C ANISOU 221 CG2 THR A 56 14005 7508 7296 2006 232 468 C ATOM 222 N ALA A 57 -2.125 18.550 26.053 1.00 71.90 N ANISOU 222 N ALA A 57 12829 7367 7122 1467 82 438 N ATOM 223 CA ALA A 57 -1.580 18.170 24.744 1.00 70.73 C ANISOU 223 CA ALA A 57 12620 7258 6997 1418 72 480 C ATOM 224 C ALA A 57 -2.378 17.011 24.125 1.00 75.93 C ANISOU 224 C ALA A 57 12988 8186 7677 1498 14 448 C ATOM 225 O ALA A 57 -2.683 17.054 22.942 1.00 76.44 O ANISOU 225 O ALA A 57 13033 8327 7682 1628 9 479 O ATOM 226 CB ALA A 57 -0.114 17.782 24.886 1.00 70.05 C ANISOU 226 CB ALA A 57 12518 7078 7017 1123 70 482 C ATOM 227 N ILE A 58 -2.723 15.983 24.918 1.00 73.11 N ANISOU 227 N ILE A 58 12413 7969 7396 1419 -23 383 N ATOM 228 CA ILE A 58 -3.496 14.839 24.401 1.00 72.41 C ANISOU 228 CA ILE A 58 12051 8131 7331 1462 -63 334 C ATOM 229 C ILE A 58 -4.983 15.271 24.198 1.00 80.53 C ANISOU 229 C ILE A 58 13045 9313 8241 1744 -64 304 C ATOM 230 O ILE A 58 -5.634 14.763 23.286 1.00 81.90 O ANISOU 230 O ILE A 58 13051 9685 8381 1842 -92 276 O ATOM 231 CB ILE A 58 -3.342 13.567 25.301 1.00 72.27 C ANISOU 231 CB ILE A 58 11836 8195 7429 1272 -81 275 C ATOM 232 CG1 ILE A 58 -1.861 13.102 25.357 1.00 69.26 C ANISOU 232 CG1 ILE A 58 11471 7698 7148 1031 -88 305 C ATOM 233 CG2 ILE A 58 -4.248 12.427 24.819 1.00 72.24 C ANISOU 233 CG2 ILE A 58 11568 8437 7441 1306 -102 209 C ATOM 234 CD1 ILE A 58 -1.505 12.339 26.551 1.00 68.90 C ANISOU 234 CD1 ILE A 58 11350 7646 7181 876 -94 270 C ATOM 235 N ALA A 59 -5.486 16.224 25.005 1.00 78.11 N ANISOU 235 N ALA A 59 12897 8922 7861 1878 -34 306 N ATOM 236 CA ALA A 59 -6.865 16.709 24.916 1.00 79.95 C ANISOU 236 CA ALA A 59 13105 9304 7969 2166 -33 276 C ATOM 237 C ALA A 59 -7.117 17.564 23.675 1.00 88.10 C ANISOU 237 C ALA A 59 14272 10332 8868 2404 -28 336 C ATOM 238 O ALA A 59 -8.242 17.574 23.177 1.00 90.17 O ANISOU 238 O ALA A 59 14417 10813 9031 2640 -51 301 O ATOM 239 CB ALA A 59 -7.212 17.516 26.150 1.00 81.09 C ANISOU 239 CB ALA A 59 13407 9335 8070 2242 5 266 C ATOM 240 N LYS A 60 -6.085 18.277 23.178 1.00 84.76 N ANISOU 240 N LYS A 60 14095 9672 8436 2345 7 423 N ATOM 241 CA LYS A 60 -6.224 19.207 22.064 1.00 85.77 C ANISOU 241 CA LYS A 60 14417 9746 8426 2572 32 497 C ATOM 242 C LYS A 60 -5.644 18.719 20.753 1.00 90.71 C ANISOU 242 C LYS A 60 14974 10420 9071 2505 11 533 C ATOM 243 O LYS A 60 -6.140 19.149 19.717 1.00 94.27 O ANISOU 243 O LYS A 60 15480 10945 9393 2742 9 571 O ATOM 244 CB LYS A 60 -5.591 20.564 22.411 1.00 87.67 C ANISOU 244 CB LYS A 60 15041 9658 8610 2585 115 571 C ATOM 245 CG LYS A 60 -6.501 21.446 23.239 1.00 92.00 C ANISOU 245 CG LYS A 60 15735 10168 9053 2814 147 557 C ATOM 246 N PHE A 61 -4.597 17.891 20.755 1.00 83.83 N ANISOU 246 N PHE A 61 14001 9507 8342 2209 -2 527 N ATOM 247 CA PHE A 61 -4.018 17.479 19.479 1.00 83.29 C ANISOU 247 CA PHE A 61 13884 9477 8284 2154 -14 564 C ATOM 248 C PHE A 61 -4.424 16.065 19.091 1.00 87.27 C ANISOU 248 C PHE A 61 14046 10256 8856 2092 -83 486 C ATOM 249 O PHE A 61 -3.879 15.087 19.611 1.00 85.93 O ANISOU 249 O PHE A 61 13724 10102 8824 1851 -100 444 O ATOM 250 CB PHE A 61 -2.489 17.634 19.474 1.00 84.16 C ANISOU 250 CB PHE A 61 14142 9353 8484 1890 31 618 C ATOM 251 CG PHE A 61 -2.056 19.058 19.695 1.00 87.06 C ANISOU 251 CG PHE A 61 14865 9440 8775 1930 116 686 C ATOM 252 CD1 PHE A 61 -2.093 19.983 18.660 1.00 92.31 C ANISOU 252 CD1 PHE A 61 15761 10007 9307 2110 171 768 C ATOM 253 CD2 PHE A 61 -1.637 19.486 20.944 1.00 88.70 C ANISOU 253 CD2 PHE A 61 15191 9478 9031 1793 148 666 C ATOM 254 CE1 PHE A 61 -1.730 21.315 18.878 1.00 94.45 C ANISOU 254 CE1 PHE A 61 16391 9995 9499 2143 270 829 C ATOM 255 CE2 PHE A 61 -1.267 20.814 21.159 1.00 92.86 C ANISOU 255 CE2 PHE A 61 16062 9738 9484 1817 237 716 C ATOM 256 CZ PHE A 61 -1.324 21.719 20.129 1.00 92.67 C ANISOU 256 CZ PHE A 61 16278 9602 9332 1988 304 797 C ATOM 257 N GLU A 62 -5.391 15.985 18.154 1.00 85.51 N ANISOU 257 N GLU A 62 13715 10251 8523 2321 -119 464 N ATOM 258 CA GLU A 62 -5.971 14.797 17.495 1.00 85.36 C ANISOU 258 CA GLU A 62 13386 10521 8524 2314 -179 379 C ATOM 259 C GLU A 62 -4.941 13.690 17.200 1.00 87.31 C ANISOU 259 C GLU A 62 13511 10748 8915 2027 -189 370 C ATOM 260 O GLU A 62 -5.243 12.521 17.409 1.00 86.46 O ANISOU 260 O GLU A 62 13158 10804 8889 1907 -217 280 O ATOM 261 CB GLU A 62 -6.654 15.211 16.176 1.00 88.95 C ANISOU 261 CB GLU A 62 13847 11136 8814 2594 -205 396 C ATOM 262 CG GLU A 62 -5.760 15.938 15.150 1.00107.40 C ANISOU 262 CG GLU A 62 16432 13287 11089 2632 -167 514 C ATOM 263 CD GLU A 62 -5.121 17.263 15.552 1.00119.13 C ANISOU 263 CD GLU A 62 18281 14449 12533 2660 -86 622 C ATOM 264 OE1 GLU A 62 -3.879 17.409 15.425 1.00 83.86 O ANISOU 264 OE1 GLU A 62 13962 9764 8139 2454 -36 686 O ATOM 265 OE2 GLU A 62 -5.864 18.120 16.085 1.00110.33 O ANISOU 265 OE2 GLU A 62 17297 13305 11319 2871 -67 630 O ATOM 266 N ARG A 63 -3.735 14.058 16.730 1.00 83.93 N ANISOU 266 N ARG A 63 13260 10118 8513 1919 -155 458 N ATOM 267 CA ARG A 63 -2.646 13.120 16.414 1.00 82.79 C ANISOU 267 CA ARG A 63 13022 9943 8492 1668 -158 459 C ATOM 268 C ARG A 63 -2.195 12.334 17.629 1.00 83.50 C ANISOU 268 C ARG A 63 13012 9989 8727 1436 -159 413 C ATOM 269 O ARG A 63 -1.705 11.217 17.467 1.00 82.95 O ANISOU 269 O ARG A 63 12784 9979 8752 1267 -174 380 O ATOM 270 CB ARG A 63 -1.423 13.830 15.782 1.00 87.21 C ANISOU 270 CB ARG A 63 13805 10289 9040 1598 -108 561 C ATOM 271 CG ARG A 63 -1.043 15.184 16.402 1.00107.43 C ANISOU 271 CG ARG A 63 16663 12598 11557 1623 -44 631 C ATOM 272 CD ARG A 63 0.462 15.390 16.430 1.00122.30 C ANISOU 272 CD ARG A 63 18677 14274 13518 1384 7 682 C ATOM 273 NE ARG A 63 0.857 16.706 15.916 1.00131.46 N ANISOU 273 NE ARG A 63 20143 15228 14576 1458 88 771 N ATOM 274 CZ ARG A 63 1.195 16.952 14.653 1.00142.21 C ANISOU 274 CZ ARG A 63 21593 16570 15869 1512 122 834 C ATOM 275 NH1 ARG A 63 1.173 15.981 13.750 1.00131.73 N ANISOU 275 NH1 ARG A 63 20061 15428 14562 1507 73 814 N ATOM 276 NH2 ARG A 63 1.553 18.170 14.283 1.00126.66 N ANISOU 276 NH2 ARG A 63 19932 14389 13804 1568 215 916 N ATOM 277 N LEU A 64 -2.336 12.919 18.835 1.00 77.95 N ANISOU 277 N LEU A 64 12414 9176 8030 1438 -139 414 N ATOM 278 CA LEU A 64 -1.936 12.290 20.099 1.00 75.54 C ANISOU 278 CA LEU A 64 12040 8821 7840 1244 -138 376 C ATOM 279 C LEU A 64 -3.100 11.496 20.737 1.00 79.34 C ANISOU 279 C LEU A 64 12318 9493 8336 1283 -157 282 C ATOM 280 O LEU A 64 -2.891 10.851 21.770 1.00 76.67 O ANISOU 280 O LEU A 64 11915 9131 8083 1137 -151 248 O ATOM 281 CB LEU A 64 -1.401 13.333 21.098 1.00 74.83 C ANISOU 281 CB LEU A 64 12176 8510 7745 1205 -102 418 C ATOM 282 CG LEU A 64 -0.150 14.123 20.691 1.00 77.91 C ANISOU 282 CG LEU A 64 12775 8695 8134 1109 -63 494 C ATOM 283 CD1 LEU A 64 0.023 15.339 21.583 1.00 78.62 C ANISOU 283 CD1 LEU A 64 13107 8584 8181 1121 -19 517 C ATOM 284 CD2 LEU A 64 1.091 13.275 20.763 1.00 74.89 C ANISOU 284 CD2 LEU A 64 12299 8289 7869 863 -73 491 C ATOM 285 N GLN A 65 -4.321 11.523 20.118 1.00 75.29 N ANISOU 285 N GLN A 65 11699 9177 7729 1479 -177 235 N ATOM 286 CA GLN A 65 -5.455 10.784 20.671 1.00 73.07 C ANISOU 286 CA GLN A 65 11210 9097 7457 1500 -184 132 C ATOM 287 C GLN A 65 -5.398 9.323 20.244 1.00 74.78 C ANISOU 287 C GLN A 65 11204 9453 7757 1339 -193 62 C ATOM 288 O GLN A 65 -6.153 8.866 19.393 1.00 74.72 O ANISOU 288 O GLN A 65 11032 9655 7701 1412 -215 -6 O ATOM 289 CB GLN A 65 -6.771 11.432 20.313 1.00 75.01 C ANISOU 289 CB GLN A 65 11420 9517 7564 1771 -200 95 C ATOM 290 CG GLN A 65 -7.177 12.434 21.354 1.00 83.47 C ANISOU 290 CG GLN A 65 12642 10491 8581 1892 -175 115 C ATOM 291 CD GLN A 65 -7.868 13.610 20.740 1.00 94.09 C ANISOU 291 CD GLN A 65 14110 11877 9765 2196 -182 149 C ATOM 292 OE1 GLN A 65 -8.353 13.559 19.612 1.00 93.81 O ANISOU 292 OE1 GLN A 65 13986 12013 9643 2343 -215 133 O ATOM 293 NE2 GLN A 65 -7.946 14.694 21.477 1.00 82.45 N ANISOU 293 NE2 GLN A 65 12847 10247 8234 2310 -150 195 N ATOM 294 N THR A 66 -4.487 8.591 20.872 1.00 69.48 N ANISOU 294 N THR A 66 10534 8663 7203 1122 -174 74 N ATOM 295 CA THR A 66 -4.261 7.178 20.638 1.00 68.08 C ANISOU 295 CA THR A 66 10192 8563 7113 952 -166 19 C ATOM 296 C THR A 66 -4.579 6.401 21.911 1.00 72.54 C ANISOU 296 C THR A 66 10683 9132 7745 834 -126 -37 C ATOM 297 O THR A 66 -4.657 6.998 22.997 1.00 74.84 O ANISOU 297 O THR A 66 11073 9333 8029 860 -113 -15 O ATOM 298 CB THR A 66 -2.805 6.963 20.182 1.00 71.92 C ANISOU 298 CB THR A 66 10760 8901 7665 820 -170 94 C ATOM 299 OG1 THR A 66 -1.938 7.137 21.300 1.00 66.14 O ANISOU 299 OG1 THR A 66 10144 7992 6993 711 -155 143 O ATOM 300 CG2 THR A 66 -2.390 7.898 19.020 1.00 67.54 C ANISOU 300 CG2 THR A 66 10321 8303 7036 930 -192 166 C ATOM 301 N VAL A 67 -4.730 5.068 21.788 1.00 67.11 N ANISOU 301 N VAL A 67 9842 8538 7119 700 -99 -109 N ATOM 302 CA VAL A 67 -4.991 4.140 22.907 1.00 66.25 C ANISOU 302 CA VAL A 67 9674 8424 7073 569 -41 -162 C ATOM 303 C VAL A 67 -3.856 4.281 23.952 1.00 67.18 C ANISOU 303 C VAL A 67 9950 8327 7248 484 -35 -76 C ATOM 304 O VAL A 67 -4.147 4.427 25.136 1.00 66.71 O ANISOU 304 O VAL A 67 9932 8225 7188 480 -8 -81 O ATOM 305 CB VAL A 67 -5.160 2.658 22.426 1.00 69.72 C ANISOU 305 CB VAL A 67 9961 8962 7566 425 1 -246 C ATOM 306 CG1 VAL A 67 -5.078 1.688 23.604 1.00 69.65 C ANISOU 306 CG1 VAL A 67 9959 8878 7627 276 76 -268 C ATOM 307 CG2 VAL A 67 -6.475 2.469 21.680 1.00 70.00 C ANISOU 307 CG2 VAL A 67 9813 9244 7539 490 3 -365 C ATOM 308 N THR A 68 -2.579 4.295 23.499 1.00 62.39 N ANISOU 308 N THR A 68 9424 7603 6679 424 -62 -2 N ATOM 309 CA THR A 68 -1.416 4.438 24.378 1.00 61.60 C ANISOU 309 CA THR A 68 9450 7333 6621 344 -67 68 C ATOM 310 C THR A 68 -1.475 5.733 25.160 1.00 67.01 C ANISOU 310 C THR A 68 10272 7931 7258 428 -84 105 C ATOM 311 O THR A 68 -1.246 5.709 26.372 1.00 67.92 O ANISOU 311 O THR A 68 10447 7970 7390 381 -70 113 O ATOM 312 CB THR A 68 -0.106 4.333 23.590 1.00 68.11 C ANISOU 312 CB THR A 68 10311 8086 7480 279 -94 128 C ATOM 313 OG1 THR A 68 -0.075 3.052 22.936 1.00 69.44 O ANISOU 313 OG1 THR A 68 10362 8329 7692 205 -71 88 O ATOM 314 CG2 THR A 68 1.151 4.512 24.483 1.00 60.78 C ANISOU 314 CG2 THR A 68 9491 7017 6586 197 -106 186 C ATOM 315 N ASN A 69 -1.824 6.850 24.497 1.00 63.75 N ANISOU 315 N ASN A 69 9921 7527 6775 560 -108 124 N ATOM 316 CA ASN A 69 -1.860 8.145 25.149 1.00 63.70 C ANISOU 316 CA ASN A 69 10075 7415 6713 646 -113 159 C ATOM 317 C ASN A 69 -3.074 8.303 26.056 1.00 69.17 C ANISOU 317 C ASN A 69 10739 8179 7365 737 -89 105 C ATOM 318 O ASN A 69 -3.044 9.180 26.915 1.00 69.79 O ANISOU 318 O ASN A 69 10952 8155 7409 780 -85 126 O ATOM 319 CB ASN A 69 -1.752 9.255 24.139 1.00 64.68 C ANISOU 319 CB ASN A 69 10309 7499 6768 761 -131 208 C ATOM 320 CG ASN A 69 -0.436 9.256 23.407 1.00 79.73 C ANISOU 320 CG ASN A 69 12271 9312 8712 656 -142 265 C ATOM 321 OD1 ASN A 69 0.609 8.824 23.914 1.00 70.16 O ANISOU 321 OD1 ASN A 69 11068 8022 7568 504 -144 281 O ATOM 322 ND2 ASN A 69 -0.460 9.722 22.183 1.00 74.18 N ANISOU 322 ND2 ASN A 69 11601 8628 7957 742 -148 296 N ATOM 323 N TYR A 70 -4.098 7.427 25.931 1.00 67.25 N ANISOU 323 N TYR A 70 10319 8109 7125 747 -66 28 N ATOM 324 CA TYR A 70 -5.229 7.407 26.867 1.00 68.23 C ANISOU 324 CA TYR A 70 10389 8319 7218 804 -30 -35 C ATOM 325 C TYR A 70 -4.712 6.832 28.179 1.00 71.39 C ANISOU 325 C TYR A 70 10833 8614 7678 666 3 -26 C ATOM 326 O TYR A 70 -5.082 7.321 29.249 1.00 72.54 O ANISOU 326 O TYR A 70 11047 8722 7792 711 22 -32 O ATOM 327 CB TYR A 70 -6.416 6.594 26.333 1.00 71.23 C ANISOU 327 CB TYR A 70 10554 8926 7584 823 -4 -135 C ATOM 328 CG TYR A 70 -7.350 7.336 25.401 1.00 78.37 C ANISOU 328 CG TYR A 70 11400 9988 8389 1022 -36 -166 C ATOM 329 CD1 TYR A 70 -6.938 8.493 24.736 1.00 81.41 C ANISOU 329 CD1 TYR A 70 11934 10288 8711 1161 -81 -89 C ATOM 330 CD2 TYR A 70 -8.633 6.863 25.149 1.00 81.18 C ANISOU 330 CD2 TYR A 70 11552 10587 8704 1072 -15 -278 C ATOM 331 CE1 TYR A 70 -7.790 9.169 23.866 1.00 82.92 C ANISOU 331 CE1 TYR A 70 12089 10626 8793 1374 -108 -110 C ATOM 332 CE2 TYR A 70 -9.487 7.524 24.269 1.00 83.79 C ANISOU 332 CE2 TYR A 70 11815 11094 8927 1278 -53 -312 C ATOM 333 CZ TYR A 70 -9.064 8.682 23.637 1.00 92.78 C ANISOU 333 CZ TYR A 70 13119 12137 9995 1444 -102 -221 C ATOM 334 OH TYR A 70 -9.913 9.343 22.783 1.00 98.74 O ANISOU 334 OH TYR A 70 13825 13066 10625 1678 -138 -247 O ATOM 335 N PHE A 71 -3.810 5.824 28.097 1.00 65.61 N ANISOU 335 N PHE A 71 10074 7832 7021 514 9 -7 N ATOM 336 CA PHE A 71 -3.156 5.232 29.271 1.00 64.52 C ANISOU 336 CA PHE A 71 9992 7593 6927 401 34 13 C ATOM 337 C PHE A 71 -2.170 6.244 29.891 1.00 68.14 C ANISOU 337 C PHE A 71 10622 7898 7370 408 -10 78 C ATOM 338 O PHE A 71 -2.152 6.384 31.109 1.00 68.05 O ANISOU 338 O PHE A 71 10682 7830 7345 398 5 79 O ATOM 339 CB PHE A 71 -2.452 3.911 28.924 1.00 65.45 C ANISOU 339 CB PHE A 71 10048 7706 7115 270 53 18 C ATOM 340 CG PHE A 71 -3.360 2.823 28.417 1.00 66.53 C ANISOU 340 CG PHE A 71 10032 7975 7270 226 112 -60 C ATOM 341 CD1 PHE A 71 -4.582 2.571 29.030 1.00 70.39 C ANISOU 341 CD1 PHE A 71 10451 8558 7736 237 176 -134 C ATOM 342 CD2 PHE A 71 -2.995 2.046 27.335 1.00 67.20 C ANISOU 342 CD2 PHE A 71 10044 8096 7395 164 110 -70 C ATOM 343 CE1 PHE A 71 -5.437 1.577 28.546 1.00 71.29 C ANISOU 343 CE1 PHE A 71 10416 8806 7864 171 240 -224 C ATOM 344 CE2 PHE A 71 -3.843 1.040 26.863 1.00 70.47 C ANISOU 344 CE2 PHE A 71 10322 8632 7822 105 171 -158 C ATOM 345 CZ PHE A 71 -5.056 0.809 27.477 1.00 69.32 C ANISOU 345 CZ PHE A 71 10102 8583 7653 100 237 -239 C ATOM 346 N ILE A 72 -1.413 6.999 29.053 1.00 65.08 N ANISOU 346 N ILE A 72 10304 7447 6975 424 -56 125 N ATOM 347 CA ILE A 72 -0.507 8.080 29.502 1.00 64.35 C ANISOU 347 CA ILE A 72 10377 7212 6860 412 -88 171 C ATOM 348 C ILE A 72 -1.346 9.179 30.202 1.00 68.12 C ANISOU 348 C ILE A 72 10959 7658 7265 533 -74 155 C ATOM 349 O ILE A 72 -0.902 9.701 31.231 1.00 66.82 O ANISOU 349 O ILE A 72 10912 7393 7085 503 -79 162 O ATOM 350 CB ILE A 72 0.377 8.615 28.346 1.00 66.23 C ANISOU 350 CB ILE A 72 10665 7396 7102 391 -118 217 C ATOM 351 CG1 ILE A 72 1.498 7.598 28.074 1.00 64.32 C ANISOU 351 CG1 ILE A 72 10348 7160 6930 256 -132 234 C ATOM 352 CG2 ILE A 72 0.937 10.046 28.634 1.00 65.56 C ANISOU 352 CG2 ILE A 72 10773 7166 6970 402 -128 247 C ATOM 353 CD1 ILE A 72 1.828 7.441 26.705 1.00 67.17 C ANISOU 353 CD1 ILE A 72 10659 7555 7307 249 -142 255 C ATOM 354 N THR A 73 -2.586 9.447 29.707 1.00 65.90 N ANISOU 354 N THR A 73 10624 7480 6935 675 -57 124 N ATOM 355 CA THR A 73 -3.525 10.368 30.372 1.00 67.15 C ANISOU 355 CA THR A 73 10861 7635 7016 816 -37 102 C ATOM 356 C THR A 73 -3.868 9.813 31.776 1.00 71.36 C ANISOU 356 C THR A 73 11365 8185 7562 767 -4 65 C ATOM 357 O THR A 73 -3.800 10.571 32.736 1.00 71.76 O ANISOU 357 O THR A 73 11551 8141 7574 797 1 70 O ATOM 358 CB THR A 73 -4.769 10.621 29.519 1.00 73.96 C ANISOU 358 CB THR A 73 11637 8648 7816 990 -30 70 C ATOM 359 OG1 THR A 73 -4.327 11.171 28.290 1.00 76.83 O ANISOU 359 OG1 THR A 73 12061 8974 8157 1039 -58 116 O ATOM 360 CG2 THR A 73 -5.756 11.580 30.182 1.00 72.38 C ANISOU 360 CG2 THR A 73 11516 8458 7526 1164 -8 47 C ATOM 361 N SER A 74 -4.168 8.495 31.903 1.00 68.63 N ANISOU 361 N SER A 74 10863 7944 7268 683 27 29 N ATOM 362 CA SER A 74 -4.442 7.853 33.202 1.00 68.69 C ANISOU 362 CA SER A 74 10857 7958 7286 626 74 1 C ATOM 363 C SER A 74 -3.266 8.135 34.179 1.00 73.04 C ANISOU 363 C SER A 74 11557 8354 7842 550 46 46 C ATOM 364 O SER A 74 -3.472 8.634 35.288 1.00 72.97 O ANISOU 364 O SER A 74 11640 8298 7788 585 60 37 O ATOM 365 CB SER A 74 -4.671 6.350 33.017 1.00 71.59 C ANISOU 365 CB SER A 74 11070 8419 7710 519 123 -32 C ATOM 366 OG SER A 74 -4.849 5.643 34.237 1.00 78.75 O ANISOU 366 OG SER A 74 11987 9314 8623 456 183 -48 O ATOM 367 N LEU A 75 -2.042 7.902 33.701 1.00 70.14 N ANISOU 367 N LEU A 75 11208 7922 7519 454 3 89 N ATOM 368 CA LEU A 75 -0.773 8.095 34.392 1.00 70.58 C ANISOU 368 CA LEU A 75 11369 7870 7580 370 -36 120 C ATOM 369 C LEU A 75 -0.553 9.545 34.795 1.00 71.85 C ANISOU 369 C LEU A 75 11692 7924 7683 414 -61 123 C ATOM 370 O LEU A 75 -0.216 9.803 35.938 1.00 72.15 O ANISOU 370 O LEU A 75 11817 7906 7691 388 -68 113 O ATOM 371 CB LEU A 75 0.354 7.648 33.441 1.00 71.15 C ANISOU 371 CB LEU A 75 11395 7932 7706 279 -74 155 C ATOM 372 CG LEU A 75 1.524 6.903 34.037 1.00 76.79 C ANISOU 372 CG LEU A 75 12107 8623 8446 178 -97 175 C ATOM 373 CD1 LEU A 75 1.053 5.670 34.786 1.00 77.36 C ANISOU 373 CD1 LEU A 75 12123 8745 8527 171 -45 164 C ATOM 374 CD2 LEU A 75 2.489 6.490 32.950 1.00 77.68 C ANISOU 374 CD2 LEU A 75 12158 8748 8607 111 -127 204 C ATOM 375 N ALA A 76 -0.758 10.483 33.875 1.00 67.80 N ANISOU 375 N ALA A 76 11233 7381 7146 485 -69 134 N ATOM 376 CA ALA A 76 -0.580 11.911 34.129 1.00 68.28 C ANISOU 376 CA ALA A 76 11480 7317 7147 529 -74 137 C ATOM 377 C ALA A 76 -1.635 12.453 35.120 1.00 71.75 C ANISOU 377 C ALA A 76 11988 7753 7519 649 -40 103 C ATOM 378 O ALA A 76 -1.296 13.335 35.901 1.00 72.02 O ANISOU 378 O ALA A 76 12182 7674 7508 640 -42 92 O ATOM 379 CB ALA A 76 -0.599 12.687 32.821 1.00 69.44 C ANISOU 379 CB ALA A 76 11684 7426 7275 593 -74 167 C ATOM 380 N CYS A 77 -2.860 11.869 35.159 1.00 68.87 N ANISOU 380 N CYS A 77 11498 7522 7147 742 -4 76 N ATOM 381 CA CYS A 77 -3.923 12.205 36.134 1.00 70.51 C ANISOU 381 CA CYS A 77 11737 7761 7294 854 38 37 C ATOM 382 C CYS A 77 -3.483 11.810 37.539 1.00 73.08 C ANISOU 382 C CYS A 77 12102 8044 7620 762 43 24 C ATOM 383 O CYS A 77 -3.562 12.626 38.450 1.00 75.69 O ANISOU 383 O CYS A 77 12571 8296 7891 806 50 8 O ATOM 384 CB CYS A 77 -5.240 11.529 35.773 1.00 71.99 C ANISOU 384 CB CYS A 77 11744 8129 7478 943 79 -1 C ATOM 385 SG CYS A 77 -6.132 12.334 34.430 1.00 77.69 S ANISOU 385 SG CYS A 77 12444 8933 8142 1138 74 -4 S ATOM 386 N ALA A 78 -3.012 10.563 37.708 1.00 65.18 N ANISOU 386 N ALA A 78 10993 7093 6679 643 42 33 N ATOM 387 CA ALA A 78 -2.472 10.040 38.948 1.00 63.42 C ANISOU 387 CA ALA A 78 10806 6840 6450 564 43 31 C ATOM 388 C ALA A 78 -1.360 10.950 39.434 1.00 66.31 C ANISOU 388 C ALA A 78 11327 7083 6786 512 -13 37 C ATOM 389 O ALA A 78 -1.384 11.356 40.583 1.00 66.03 O ANISOU 389 O ALA A 78 11390 7004 6693 527 -9 13 O ATOM 390 CB ALA A 78 -1.950 8.620 38.735 1.00 62.71 C ANISOU 390 CB ALA A 78 10598 6805 6425 460 47 53 C ATOM 391 N ASP A 79 -0.446 11.358 38.533 1.00 63.33 N ANISOU 391 N ASP A 79 10974 6651 6438 448 -59 59 N ATOM 392 CA ASP A 79 0.655 12.270 38.866 1.00 63.79 C ANISOU 392 CA ASP A 79 11171 6599 6469 368 -104 48 C ATOM 393 C ASP A 79 0.165 13.691 39.250 1.00 68.31 C ANISOU 393 C ASP A 79 11925 7064 6967 450 -81 19 C ATOM 394 O ASP A 79 0.738 14.288 40.152 1.00 67.25 O ANISOU 394 O ASP A 79 11911 6854 6787 394 -99 -15 O ATOM 395 CB ASP A 79 1.658 12.309 37.716 1.00 65.45 C ANISOU 395 CB ASP A 79 11351 6789 6730 274 -139 75 C ATOM 396 CG ASP A 79 2.420 11.001 37.596 1.00 73.81 C ANISOU 396 CG ASP A 79 12263 7935 7846 185 -169 96 C ATOM 397 OD1 ASP A 79 2.679 10.381 38.620 1.00 78.52 O ANISOU 397 OD1 ASP A 79 12841 8568 8425 162 -180 86 O ATOM 398 OD2 ASP A 79 2.769 10.617 36.474 1.00 75.91 O ANISOU 398 OD2 ASP A 79 12446 8230 8165 151 -177 125 O ATOM 399 N ALEU A 80 -0.889 14.206 38.585 0.50 65.69 N ANISOU 399 N ALEU A 80 11613 6732 6613 590 -41 28 N ATOM 400 N BLEU A 80 -0.895 14.203 38.586 0.50 66.68 N ANISOU 400 N BLEU A 80 11739 6859 6739 591 -41 28 N ATOM 401 CA ALEU A 80 -1.471 15.523 38.876 0.50 66.36 C ANISOU 401 CA ALEU A 80 11882 6713 6617 706 -7 7 C ATOM 402 CA BLEU A 80 -1.490 15.518 38.870 0.50 67.87 C ANISOU 402 CA BLEU A 80 12072 6906 6808 709 -7 7 C ATOM 403 C ALEU A 80 -2.161 15.505 40.250 0.50 71.52 C ANISOU 403 C ALEU A 80 12566 7391 7216 771 19 -32 C ATOM 404 C BLEU A 80 -2.181 15.514 40.236 0.50 72.21 C ANISOU 404 C BLEU A 80 12655 7480 7304 775 20 -32 C ATOM 405 O ALEU A 80 -2.044 16.472 40.999 0.50 72.35 O ANISOU 405 O ALEU A 80 12850 7384 7256 786 28 -64 O ATOM 406 O BLEU A 80 -2.111 16.507 40.954 0.50 73.09 O ANISOU 406 O BLEU A 80 12945 7477 7347 797 31 -63 O ATOM 407 CB ALEU A 80 -2.460 15.936 37.761 0.50 66.42 C ANISOU 407 CB ALEU A 80 11881 6751 6604 874 25 31 C ATOM 408 CB BLEU A 80 -2.509 15.903 37.779 0.50 68.41 C ANISOU 408 CB BLEU A 80 12127 7010 6856 878 26 31 C ATOM 409 CG ALEU A 80 -3.290 17.207 37.990 0.50 71.83 C ANISOU 409 CG ALEU A 80 12751 7351 7192 1053 70 17 C ATOM 410 CG BLEU A 80 -2.390 17.272 37.089 0.50 74.54 C ANISOU 410 CG BLEU A 80 13111 7635 7576 951 46 50 C ATOM 411 CD1ALEU A 80 -2.463 18.458 37.769 0.50 72.87 C ANISOU 411 CD1ALEU A 80 13127 7275 7284 1005 79 25 C ATOM 412 CD1BLEU A 80 -3.681 17.610 36.371 0.50 75.76 C ANISOU 412 CD1BLEU A 80 13249 7861 7675 1183 80 64 C ATOM 413 CD2ALEU A 80 -4.540 17.212 37.131 0.50 73.19 C ANISOU 413 CD2ALEU A 80 12835 7642 7332 1257 96 30 C ATOM 414 CD2BLEU A 80 -2.082 18.404 38.069 0.50 78.04 C ANISOU 414 CD2BLEU A 80 13794 7908 7950 935 68 15 C ATOM 415 N VAL A 81 -2.862 14.400 40.578 1.00 68.66 N ANISOU 415 N VAL A 81 12039 7171 6878 800 40 -35 N ATOM 416 CA VAL A 81 -3.566 14.205 41.857 1.00 69.30 C ANISOU 416 CA VAL A 81 12128 7294 6909 856 78 -68 C ATOM 417 C VAL A 81 -2.491 14.105 42.969 1.00 76.99 C ANISOU 417 C VAL A 81 13182 8205 7865 729 40 -83 C ATOM 418 O VAL A 81 -2.603 14.786 43.989 1.00 78.86 O ANISOU 418 O VAL A 81 13554 8381 8029 764 50 -119 O ATOM 419 CB VAL A 81 -4.533 12.986 41.799 1.00 71.65 C ANISOU 419 CB VAL A 81 12229 7757 7240 889 127 -70 C ATOM 420 CG1 VAL A 81 -5.120 12.669 43.178 1.00 71.63 C ANISOU 420 CG1 VAL A 81 12237 7792 7186 917 178 -100 C ATOM 421 CG2 VAL A 81 -5.662 13.233 40.791 1.00 71.36 C ANISOU 421 CG2 VAL A 81 12107 7810 7197 1029 159 -77 C ATOM 422 N MET A 82 -1.411 13.343 42.715 1.00 73.73 N ANISOU 422 N MET A 82 12692 7812 7509 593 -10 -59 N ATOM 423 CA MET A 82 -0.226 13.257 43.556 1.00 74.29 C ANISOU 423 CA MET A 82 12816 7853 7559 477 -64 -77 C ATOM 424 C MET A 82 0.321 14.690 43.835 1.00 80.14 C ANISOU 424 C MET A 82 13746 8461 8242 443 -87 -123 C ATOM 425 O MET A 82 0.524 15.051 44.994 1.00 82.02 O ANISOU 425 O MET A 82 14083 8669 8411 429 -98 -168 O ATOM 426 CB MET A 82 0.825 12.385 42.850 1.00 76.50 C ANISOU 426 CB MET A 82 12975 8183 7910 363 -112 -42 C ATOM 427 CG MET A 82 1.810 11.716 43.775 1.00 82.21 C ANISOU 427 CG MET A 82 13678 8951 8609 285 -160 -50 C ATOM 428 SD MET A 82 1.059 10.483 44.882 1.00 88.13 S ANISOU 428 SD MET A 82 14378 9784 9324 359 -105 -31 S ATOM 429 CE MET A 82 2.367 9.301 44.974 1.00 84.91 C ANISOU 429 CE MET A 82 13884 9447 8931 281 -162 2 C ATOM 430 N GLY A 83 0.449 15.507 42.784 1.00 76.18 N ANISOU 430 N GLY A 83 13308 7875 7760 437 -83 -114 N ATOM 431 CA GLY A 83 0.938 16.887 42.843 1.00 76.40 C ANISOU 431 CA GLY A 83 13539 7751 7739 391 -81 -156 C ATOM 432 C GLY A 83 0.048 17.920 43.516 1.00 78.73 C ANISOU 432 C GLY A 83 14015 7951 7948 519 -28 -191 C ATOM 433 O GLY A 83 0.567 18.812 44.181 1.00 78.60 O ANISOU 433 O GLY A 83 14169 7824 7872 452 -31 -249 O ATOM 434 N LEU A 84 -1.284 17.831 43.343 1.00 74.33 N ANISOU 434 N LEU A 84 13421 7443 7376 702 23 -166 N ATOM 435 CA LEU A 84 -2.263 18.748 43.943 1.00 74.66 C ANISOU 435 CA LEU A 84 13619 7419 7329 861 79 -196 C ATOM 436 C LEU A 84 -2.723 18.325 45.365 1.00 78.90 C ANISOU 436 C LEU A 84 14133 8026 7817 896 90 -232 C ATOM 437 O LEU A 84 -2.762 19.158 46.272 1.00 78.90 O ANISOU 437 O LEU A 84 14308 7933 7737 922 108 -283 O ATOM 438 CB LEU A 84 -3.506 18.849 43.052 1.00 74.67 C ANISOU 438 CB LEU A 84 13568 7476 7326 1060 127 -159 C ATOM 439 CG LEU A 84 -3.387 19.623 41.759 1.00 81.16 C ANISOU 439 CG LEU A 84 14485 8202 8150 1105 139 -123 C ATOM 440 CD1 LEU A 84 -4.603 19.385 40.892 1.00 82.06 C ANISOU 440 CD1 LEU A 84 14477 8442 8258 1303 167 -89 C ATOM 441 CD2 LEU A 84 -3.251 21.120 42.010 1.00 84.21 C ANISOU 441 CD2 LEU A 84 15171 8378 8448 1149 181 -150 C ATOM 442 N ALA A 85 -3.117 17.042 45.532 1.00 74.86 N ANISOU 442 N ALA A 85 13421 7673 7348 901 92 -207 N ATOM 443 CA ALA A 85 -3.680 16.479 46.763 1.00 74.17 C ANISOU 443 CA ALA A 85 13298 7667 7217 944 122 -228 C ATOM 444 C ALA A 85 -2.681 15.742 47.662 1.00 76.24 C ANISOU 444 C ALA A 85 13535 7957 7476 806 73 -236 C ATOM 445 O ALA A 85 -3.010 15.510 48.829 1.00 77.09 O ANISOU 445 O ALA A 85 13671 8099 7521 842 98 -259 O ATOM 446 CB ALA A 85 -4.817 15.520 46.413 1.00 74.10 C ANISOU 446 CB ALA A 85 13100 7811 7245 1033 178 -201 C ATOM 447 N VAL A 86 -1.515 15.312 47.167 1.00 70.33 N ANISOU 447 N VAL A 86 12726 7213 6784 667 7 -217 N ATOM 448 CA VAL A 86 -0.679 14.536 48.094 1.00 69.10 C ANISOU 448 CA VAL A 86 12536 7115 6605 578 -38 -224 C ATOM 449 C VAL A 86 0.563 15.310 48.546 1.00 74.40 C ANISOU 449 C VAL A 86 13322 7717 7229 460 -111 -283 C ATOM 450 O VAL A 86 0.612 15.737 49.695 1.00 74.53 O ANISOU 450 O VAL A 86 13449 7713 7156 471 -117 -337 O ATOM 451 CB VAL A 86 -0.320 13.137 47.557 1.00 69.51 C ANISOU 451 CB VAL A 86 12408 7269 6733 526 -52 -165 C ATOM 452 CG1 VAL A 86 0.518 12.366 48.574 1.00 69.02 C ANISOU 452 CG1 VAL A 86 12333 7268 6624 474 -95 -167 C ATOM 453 CG2 VAL A 86 -1.588 12.365 47.206 1.00 68.33 C ANISOU 453 CG2 VAL A 86 12147 7192 6622 618 32 -129 C ATOM 454 N VAL A 87 1.539 15.503 47.640 1.00 71.35 N ANISOU 454 N VAL A 87 12908 7305 6898 343 -161 -282 N ATOM 455 CA VAL A 87 2.824 16.158 47.890 1.00 70.66 C ANISOU 455 CA VAL A 87 12892 7177 6776 194 -227 -349 C ATOM 456 C VAL A 87 2.667 17.484 48.697 1.00 76.95 C ANISOU 456 C VAL A 87 13904 7852 7481 195 -206 -433 C ATOM 457 O VAL A 87 3.430 17.624 49.657 1.00 77.78 O ANISOU 457 O VAL A 87 14050 7989 7516 112 -258 -504 O ATOM 458 CB VAL A 87 3.642 16.351 46.592 1.00 71.96 C ANISOU 458 CB VAL A 87 13009 7312 7019 77 -251 -335 C ATOM 459 CG1 VAL A 87 4.975 16.995 46.890 1.00 72.62 C ANISOU 459 CG1 VAL A 87 13150 7377 7066 -100 -310 -420 C ATOM 460 CG2 VAL A 87 3.874 15.018 45.898 1.00 70.05 C ANISOU 460 CG2 VAL A 87 12564 7193 6858 74 -274 -261 C ATOM 461 N PRO A 88 1.714 18.432 48.420 1.00 74.23 N ANISOU 461 N PRO A 88 13704 7380 7119 298 -133 -434 N ATOM 462 CA PRO A 88 1.653 19.656 49.259 1.00 75.33 C ANISOU 462 CA PRO A 88 14068 7394 7162 296 -109 -520 C ATOM 463 C PRO A 88 1.354 19.367 50.734 1.00 79.73 C ANISOU 463 C PRO A 88 14645 8019 7629 355 -118 -559 C ATOM 464 O PRO A 88 2.016 19.957 51.592 1.00 80.64 O ANISOU 464 O PRO A 88 14873 8100 7666 263 -151 -650 O ATOM 465 CB PRO A 88 0.528 20.487 48.622 1.00 77.16 C ANISOU 465 CB PRO A 88 14427 7501 7389 450 -22 -490 C ATOM 466 CG PRO A 88 0.377 19.947 47.252 1.00 80.21 C ANISOU 466 CG PRO A 88 14672 7931 7873 473 -18 -406 C ATOM 467 CD PRO A 88 0.702 18.486 47.341 1.00 74.46 C ANISOU 467 CD PRO A 88 13709 7380 7203 427 -71 -366 C ATOM 468 N PHE A 89 0.398 18.446 51.037 1.00 76.08 N ANISOU 468 N PHE A 89 14073 7661 7174 495 -84 -498 N ATOM 469 CA PHE A 89 0.042 18.104 52.432 1.00 76.83 C ANISOU 469 CA PHE A 89 14192 7821 7178 563 -77 -525 C ATOM 470 C PHE A 89 1.172 17.334 53.129 1.00 80.17 C ANISOU 470 C PHE A 89 14534 8358 7570 455 -163 -544 C ATOM 471 O PHE A 89 1.357 17.497 54.323 1.00 80.94 O ANISOU 471 O PHE A 89 14712 8478 7564 459 -184 -603 O ATOM 472 CB PHE A 89 -1.299 17.338 52.519 1.00 77.90 C ANISOU 472 CB PHE A 89 14235 8035 7327 724 2 -459 C ATOM 473 CG PHE A 89 -2.439 18.183 51.998 1.00 79.86 C ANISOU 473 CG PHE A 89 14564 8203 7577 860 80 -456 C ATOM 474 CD1 PHE A 89 -3.023 19.166 52.800 1.00 83.07 C ANISOU 474 CD1 PHE A 89 15150 8527 7885 957 126 -514 C ATOM 475 CD2 PHE A 89 -2.847 18.086 50.667 1.00 80.55 C ANISOU 475 CD2 PHE A 89 14560 8294 7751 899 102 -401 C ATOM 476 CE1 PHE A 89 -4.027 20.001 52.298 1.00 83.52 C ANISOU 476 CE1 PHE A 89 15293 8511 7928 1108 196 -511 C ATOM 477 CE2 PHE A 89 -3.867 18.904 50.172 1.00 83.60 C ANISOU 477 CE2 PHE A 89 15022 8622 8119 1050 167 -400 C ATOM 478 CZ PHE A 89 -4.442 19.864 50.990 1.00 82.87 C ANISOU 478 CZ PHE A 89 15111 8449 7926 1160 213 -453 C ATOM 479 N GLY A 90 1.943 16.572 52.368 1.00 76.09 N ANISOU 479 N GLY A 90 13867 7914 7130 369 -214 -501 N ATOM 480 CA GLY A 90 3.093 15.840 52.876 1.00 76.73 C ANISOU 480 CA GLY A 90 13858 8117 7178 285 -301 -516 C ATOM 481 C GLY A 90 4.226 16.774 53.248 1.00 83.34 C ANISOU 481 C GLY A 90 14779 8933 7952 139 -375 -630 C ATOM 482 O GLY A 90 4.852 16.609 54.295 1.00 83.77 O ANISOU 482 O GLY A 90 14840 9081 7909 115 -438 -688 O ATOM 483 N ALA A 91 4.473 17.780 52.397 1.00 81.52 N ANISOU 483 N ALA A 91 14623 8580 7770 39 -362 -668 N ATOM 484 CA ALA A 91 5.509 18.800 52.579 1.00 82.85 C ANISOU 484 CA ALA A 91 14887 8701 7890 -137 -407 -790 C ATOM 485 C ALA A 91 5.232 19.601 53.837 1.00 89.13 C ANISOU 485 C ALA A 91 15863 9442 8563 -114 -395 -886 C ATOM 486 O ALA A 91 6.129 19.749 54.670 1.00 89.70 O ANISOU 486 O ALA A 91 15938 9598 8547 -218 -468 -988 O ATOM 487 CB ALA A 91 5.562 19.714 51.360 1.00 83.65 C ANISOU 487 CB ALA A 91 15072 8644 8066 -223 -356 -791 C ATOM 488 N ALA A 92 3.965 20.054 54.007 1.00 86.83 N ANISOU 488 N ALA A 92 15706 9032 8255 36 -305 -856 N ATOM 489 CA ALA A 92 3.513 20.803 55.189 1.00 88.22 C ANISOU 489 CA ALA A 92 16065 9142 8311 90 -277 -937 C ATOM 490 C ALA A 92 3.710 19.972 56.456 1.00 91.22 C ANISOU 490 C ALA A 92 16371 9691 8598 138 -336 -952 C ATOM 491 O ALA A 92 4.142 20.511 57.463 1.00 92.93 O ANISOU 491 O ALA A 92 16690 9917 8701 83 -373 -1063 O ATOM 492 CB ALA A 92 2.048 21.220 55.043 1.00 88.88 C ANISOU 492 CB ALA A 92 16263 9106 8400 278 -168 -883 C ATOM 493 N HIS A 93 3.457 18.657 56.379 1.00 86.37 N ANISOU 493 N HIS A 93 15587 9208 8024 233 -343 -846 N ATOM 494 CA HIS A 93 3.636 17.698 57.468 1.00 86.14 C ANISOU 494 CA HIS A 93 15489 9334 7905 300 -386 -832 C ATOM 495 C HIS A 93 5.127 17.616 57.904 1.00 92.39 C ANISOU 495 C HIS A 93 16218 10258 8627 163 -511 -921 C ATOM 496 O HIS A 93 5.397 17.591 59.098 1.00 93.78 O ANISOU 496 O HIS A 93 16441 10521 8672 190 -556 -985 O ATOM 497 CB HIS A 93 3.105 16.322 57.032 1.00 84.76 C ANISOU 497 CB HIS A 93 15161 9240 7805 407 -348 -695 C ATOM 498 CG HIS A 93 3.051 15.272 58.103 1.00 88.49 C ANISOU 498 CG HIS A 93 15599 9839 8185 508 -355 -656 C ATOM 499 ND1 HIS A 93 3.611 15.467 59.357 1.00 91.52 N ANISOU 499 ND1 HIS A 93 16056 10296 8421 509 -417 -736 N ATOM 500 CD2 HIS A 93 2.491 14.041 58.066 1.00 89.39 C ANISOU 500 CD2 HIS A 93 15625 10010 8328 609 -297 -546 C ATOM 501 CE1 HIS A 93 3.387 14.352 60.026 1.00 90.80 C ANISOU 501 CE1 HIS A 93 15928 10302 8270 625 -397 -662 C ATOM 502 NE2 HIS A 93 2.710 13.468 59.296 1.00 89.69 N ANISOU 502 NE2 HIS A 93 15700 10145 8235 682 -317 -547 N ATOM 503 N ILE A 94 6.076 17.601 56.951 1.00 89.37 N ANISOU 503 N ILE A 94 15727 9905 8324 23 -566 -932 N ATOM 504 CA ILE A 94 7.516 17.552 57.239 1.00 89.94 C ANISOU 504 CA ILE A 94 15708 10130 8335 -115 -684 -1028 C ATOM 505 C ILE A 94 7.984 18.865 57.893 1.00 94.91 C ANISOU 505 C ILE A 94 16486 10706 8868 -256 -709 -1199 C ATOM 506 O ILE A 94 8.579 18.817 58.971 1.00 96.40 O ANISOU 506 O ILE A 94 16668 11034 8924 -270 -788 -1291 O ATOM 507 CB ILE A 94 8.316 17.221 55.949 1.00 92.37 C ANISOU 507 CB ILE A 94 15856 10478 8761 -229 -717 -994 C ATOM 508 CG1 ILE A 94 8.186 15.722 55.626 1.00 91.55 C ANISOU 508 CG1 ILE A 94 15590 10486 8707 -97 -722 -853 C ATOM 509 CG2 ILE A 94 9.797 17.631 56.044 1.00 93.99 C ANISOU 509 CG2 ILE A 94 15987 10809 8914 -425 -820 -1132 C ATOM 510 CD1 ILE A 94 7.854 15.430 54.259 1.00 96.04 C ANISOU 510 CD1 ILE A 94 16087 10978 9425 -103 -667 -756 C ATOM 511 N LEU A 95 7.703 20.019 57.252 1.00 91.22 N ANISOU 511 N LEU A 95 16164 10038 8459 -353 -638 -1243 N ATOM 512 CA LEU A 95 8.119 21.351 57.706 1.00 92.98 C ANISOU 512 CA LEU A 95 16561 10165 8605 -513 -635 -1408 C ATOM 513 C LEU A 95 7.520 21.734 59.070 1.00 97.40 C ANISOU 513 C LEU A 95 17280 10702 9026 -411 -620 -1472 C ATOM 514 O LEU A 95 8.271 22.168 59.948 1.00 98.29 O ANISOU 514 O LEU A 95 17428 10897 9020 -523 -688 -1621 O ATOM 515 CB LEU A 95 7.798 22.432 56.660 1.00 93.05 C ANISOU 515 CB LEU A 95 16725 9928 8702 -601 -535 -1413 C ATOM 516 CG LEU A 95 8.485 22.312 55.281 1.00 96.14 C ANISOU 516 CG LEU A 95 16997 10315 9218 -737 -538 -1374 C ATOM 517 CD1 LEU A 95 7.955 23.349 54.340 1.00 96.40 C ANISOU 517 CD1 LEU A 95 17222 10088 9317 -768 -422 -1356 C ATOM 518 CD2 LEU A 95 10.000 22.462 55.380 1.00 98.02 C ANISOU 518 CD2 LEU A 95 17127 10697 9418 -980 -628 -1514 C ATOM 519 N MET A 96 6.204 21.524 59.264 1.00 92.58 N ANISOU 519 N MET A 96 16748 10005 8424 -203 -536 -1368 N ATOM 520 CA MET A 96 5.526 21.826 60.527 1.00 93.41 C ANISOU 520 CA MET A 96 17002 10089 8400 -85 -508 -1414 C ATOM 521 C MET A 96 5.764 20.758 61.603 1.00 97.20 C ANISOU 521 C MET A 96 17368 10790 8775 15 -585 -1395 C ATOM 522 O MET A 96 5.332 20.954 62.741 1.00 96.00 O ANISOU 522 O MET A 96 17332 10647 8498 105 -571 -1441 O ATOM 523 CB MET A 96 4.024 21.998 60.308 1.00 95.10 C ANISOU 523 CB MET A 96 17326 10149 8657 103 -382 -1314 C ATOM 524 CG MET A 96 3.666 23.322 59.728 1.00100.19 C ANISOU 524 CG MET A 96 18174 10560 9332 54 -298 -1364 C ATOM 525 SD MET A 96 2.146 23.155 58.794 1.00104.04 S ANISOU 525 SD MET A 96 18665 10938 9926 270 -177 -1206 S ATOM 526 CE MET A 96 1.081 24.158 59.768 1.00102.49 C ANISOU 526 CE MET A 96 18728 10604 9610 418 -84 -1269 C ATOM 527 N LYS A 97 6.421 19.623 61.239 1.00 94.13 N ANISOU 527 N LYS A 97 16766 10572 8427 15 -656 -1321 N ATOM 528 CA LYS A 97 6.727 18.463 62.098 1.00 94.17 C ANISOU 528 CA LYS A 97 16660 10787 8334 130 -725 -1279 C ATOM 529 C LYS A 97 5.467 17.914 62.799 1.00 97.59 C ANISOU 529 C LYS A 97 17169 11188 8723 345 -633 -1176 C ATOM 530 O LYS A 97 5.580 17.276 63.842 1.00 97.76 O ANISOU 530 O LYS A 97 17186 11344 8616 448 -669 -1169 O ATOM 531 CB LYS A 97 7.827 18.795 63.132 1.00 98.67 C ANISOU 531 CB LYS A 97 17232 11519 8741 39 -845 -1439 C ATOM 532 CG LYS A 97 9.250 18.567 62.618 1.00121.01 C ANISOU 532 CG LYS A 97 19876 14516 11587 -116 -962 -1502 C ATOM 533 CD LYS A 97 9.843 19.790 61.906 1.00135.52 C ANISOU 533 CD LYS A 97 21756 16247 13488 -368 -961 -1636 C ATOM 534 N MET A 98 4.277 18.140 62.208 1.00 93.61 N ANISOU 534 N MET A 98 16729 10520 8319 415 -513 -1099 N ATOM 535 CA MET A 98 2.985 17.716 62.750 1.00 93.89 C ANISOU 535 CA MET A 98 16824 10523 8326 599 -407 -1013 C ATOM 536 C MET A 98 1.902 17.743 61.671 1.00 94.56 C ANISOU 536 C MET A 98 16889 10481 8557 652 -296 -919 C ATOM 537 O MET A 98 2.113 18.296 60.579 1.00 93.19 O ANISOU 537 O MET A 98 16700 10218 8490 556 -300 -929 O ATOM 538 CB MET A 98 2.573 18.633 63.919 1.00 99.00 C ANISOU 538 CB MET A 98 17667 11116 8833 643 -381 -1117 C ATOM 539 CG MET A 98 1.952 19.940 63.461 1.00104.99 C ANISOU 539 CG MET A 98 18578 11676 9639 614 -308 -1174 C ATOM 540 SD MET A 98 1.732 21.189 64.728 1.00114.27 S ANISOU 540 SD MET A 98 20003 12767 10648 627 -290 -1326 S ATOM 541 CE MET A 98 0.918 20.213 66.063 1.00111.13 C ANISOU 541 CE MET A 98 19605 12498 10123 838 -243 -1255 C ATOM 542 N TRP A 99 0.720 17.195 62.003 1.00 89.05 N ANISOU 542 N TRP A 99 16198 9783 7852 806 -192 -837 N ATOM 543 CA TRP A 99 -0.412 17.187 61.081 1.00 87.11 C ANISOU 543 CA TRP A 99 15917 9457 7725 874 -86 -761 C ATOM 544 C TRP A 99 -1.467 18.200 61.563 1.00 92.68 C ANISOU 544 C TRP A 99 16786 10057 8371 975 1 -812 C ATOM 545 O TRP A 99 -2.057 18.035 62.639 1.00 92.78 O ANISOU 545 O TRP A 99 16865 10108 8280 1079 53 -818 O ATOM 546 CB TRP A 99 -0.977 15.775 60.947 1.00 83.23 C ANISOU 546 CB TRP A 99 15287 9057 7281 954 -22 -640 C ATOM 547 CG TRP A 99 -2.086 15.665 59.954 1.00 81.86 C ANISOU 547 CG TRP A 99 15038 8838 7225 1009 77 -575 C ATOM 548 CD1 TRP A 99 -3.423 15.676 60.218 1.00 84.51 C ANISOU 548 CD1 TRP A 99 15394 9167 7546 1132 197 -556 C ATOM 549 CD2 TRP A 99 -1.954 15.495 58.531 1.00 79.90 C ANISOU 549 CD2 TRP A 99 14668 8569 7120 947 64 -529 C ATOM 550 NE1 TRP A 99 -4.134 15.501 59.055 1.00 82.98 N ANISOU 550 NE1 TRP A 99 15087 8967 7475 1151 253 -505 N ATOM 551 CE2 TRP A 99 -3.258 15.370 58.004 1.00 83.00 C ANISOU 551 CE2 TRP A 99 15006 8955 7575 1042 173 -484 C ATOM 552 CE3 TRP A 99 -0.858 15.384 57.656 1.00 79.54 C ANISOU 552 CE3 TRP A 99 14543 8528 7152 823 -27 -523 C ATOM 553 CZ2 TRP A 99 -3.497 15.184 56.638 1.00 80.02 C ANISOU 553 CZ2 TRP A 99 14507 8572 7326 1020 186 -438 C ATOM 554 CZ3 TRP A 99 -1.100 15.207 56.306 1.00 78.86 C ANISOU 554 CZ3 TRP A 99 14348 8419 7197 800 -7 -469 C ATOM 555 CH2 TRP A 99 -2.406 15.131 55.808 1.00 78.80 C ANISOU 555 CH2 TRP A 99 14298 8401 7242 901 96 -429 C ATOM 556 N THR A 100 -1.671 19.268 60.778 1.00 88.89 N ANISOU 556 N THR A 100 16384 9442 7947 951 21 -849 N ATOM 557 CA THR A 100 -2.587 20.350 61.160 1.00 89.18 C ANISOU 557 CA THR A 100 16599 9365 7921 1059 101 -904 C ATOM 558 C THR A 100 -3.929 20.282 60.421 1.00 91.86 C ANISOU 558 C THR A 100 16881 9687 8334 1206 209 -828 C ATOM 559 O THR A 100 -4.710 21.235 60.518 1.00 92.39 O ANISOU 559 O THR A 100 17088 9658 8357 1317 278 -867 O ATOM 560 CB THR A 100 -1.911 21.700 60.930 1.00 94.84 C ANISOU 560 CB THR A 100 17491 9928 8617 950 63 -1009 C ATOM 561 OG1 THR A 100 -1.728 21.919 59.527 1.00 91.84 O ANISOU 561 OG1 THR A 100 17060 9474 8362 889 60 -968 O ATOM 562 CG2 THR A 100 -0.597 21.814 61.670 1.00 93.92 C ANISOU 562 CG2 THR A 100 17411 9856 8418 790 -45 -1108 C ATOM 563 N PHE A 101 -4.223 19.139 59.745 1.00 86.65 N ANISOU 563 N PHE A 101 16018 9131 7774 1217 229 -730 N ATOM 564 CA PHE A 101 -5.425 18.988 58.921 1.00 85.65 C ANISOU 564 CA PHE A 101 15796 9024 7722 1335 320 -670 C ATOM 565 C PHE A 101 -6.483 18.011 59.505 1.00 90.62 C ANISOU 565 C PHE A 101 16318 9785 8329 1439 418 -623 C ATOM 566 O PHE A 101 -7.524 17.795 58.875 1.00 89.89 O ANISOU 566 O PHE A 101 16117 9746 8293 1529 497 -587 O ATOM 567 CB PHE A 101 -5.028 18.567 57.484 1.00 85.46 C ANISOU 567 CB PHE A 101 15624 9008 7837 1253 280 -610 C ATOM 568 CG PHE A 101 -3.874 19.361 56.905 1.00 86.56 C ANISOU 568 CG PHE A 101 15853 9033 8003 1119 192 -651 C ATOM 569 CD1 PHE A 101 -4.061 20.665 56.447 1.00 89.80 C ANISOU 569 CD1 PHE A 101 16426 9294 8400 1157 215 -695 C ATOM 570 CD2 PHE A 101 -2.598 18.806 56.817 1.00 87.21 C ANISOU 570 CD2 PHE A 101 15862 9159 8117 958 97 -649 C ATOM 571 CE1 PHE A 101 -2.995 21.393 55.893 1.00 90.12 C ANISOU 571 CE1 PHE A 101 16560 9217 8464 1012 155 -737 C ATOM 572 CE2 PHE A 101 -1.526 19.545 56.286 1.00 89.57 C ANISOU 572 CE2 PHE A 101 16229 9365 8437 816 26 -699 C ATOM 573 CZ PHE A 101 -1.734 20.831 55.824 1.00 88.04 C ANISOU 573 CZ PHE A 101 16204 9012 8237 831 61 -743 C ATOM 574 N GLY A 102 -6.228 17.464 60.693 1.00 88.82 N ANISOU 574 N GLY A 102 16123 9614 8010 1427 418 -630 N ATOM 575 CA GLY A 102 -7.162 16.552 61.351 1.00 89.88 C ANISOU 575 CA GLY A 102 16186 9856 8109 1508 527 -588 C ATOM 576 C GLY A 102 -7.146 15.113 60.856 1.00 93.78 C ANISOU 576 C GLY A 102 16497 10444 8689 1446 554 -501 C ATOM 577 O GLY A 102 -6.635 14.829 59.773 1.00 90.84 O ANISOU 577 O GLY A 102 16022 10065 8427 1363 498 -466 O ATOM 578 N ASN A 103 -7.740 14.194 61.643 1.00 92.77 N ANISOU 578 N ASN A 103 16340 10398 8509 1484 655 -466 N ATOM 579 CA ASN A 103 -7.773 12.751 61.365 1.00 92.54 C ANISOU 579 CA ASN A 103 16178 10442 8541 1424 711 -385 C ATOM 580 C ASN A 103 -8.549 12.356 60.113 1.00 97.10 C ANISOU 580 C ASN A 103 16575 11066 9252 1406 774 -359 C ATOM 581 O ASN A 103 -8.204 11.334 59.524 1.00 95.80 O ANISOU 581 O ASN A 103 16306 10928 9166 1320 775 -301 O ATOM 582 CB ASN A 103 -8.312 11.978 62.562 1.00 93.03 C ANISOU 582 CB ASN A 103 16288 10560 8499 1471 829 -361 C ATOM 583 CG ASN A 103 -7.274 11.823 63.647 1.00114.78 C ANISOU 583 CG ASN A 103 19182 13299 11129 1468 754 -356 C ATOM 584 OD1 ASN A 103 -6.156 12.330 63.534 1.00111.84 O ANISOU 584 OD1 ASN A 103 18857 12889 10748 1422 610 -386 O ATOM 585 ND2 ASN A 103 -7.618 11.143 64.728 1.00104.08 N ANISOU 585 ND2 ASN A 103 17896 11982 9666 1517 853 -326 N ATOM 586 N PHE A 104 -9.577 13.133 59.704 1.00 95.25 N ANISOU 586 N PHE A 104 16304 10850 9035 1494 826 -403 N ATOM 587 CA PHE A 104 -10.333 12.798 58.500 1.00 94.64 C ANISOU 587 CA PHE A 104 16042 10845 9070 1488 876 -391 C ATOM 588 C PHE A 104 -9.483 13.023 57.254 1.00 95.34 C ANISOU 588 C PHE A 104 16085 10876 9262 1417 757 -371 C ATOM 589 O PHE A 104 -9.429 12.127 56.414 1.00 94.94 O ANISOU 589 O PHE A 104 15892 10875 9308 1338 767 -330 O ATOM 590 CB PHE A 104 -11.667 13.566 58.376 1.00 98.12 C ANISOU 590 CB PHE A 104 16442 11351 9486 1629 957 -446 C ATOM 591 CG PHE A 104 -12.440 13.128 57.145 1.00100.05 C ANISOU 591 CG PHE A 104 16472 11707 9834 1623 1004 -443 C ATOM 592 CD1 PHE A 104 -13.200 11.960 57.158 1.00104.08 C ANISOU 592 CD1 PHE A 104 16824 12345 10375 1563 1128 -435 C ATOM 593 CD2 PHE A 104 -12.346 13.840 55.953 1.00102.07 C ANISOU 593 CD2 PHE A 104 16690 11939 10153 1663 925 -450 C ATOM 594 CE1 PHE A 104 -13.869 11.527 56.010 1.00104.82 C ANISOU 594 CE1 PHE A 104 16709 12557 10560 1540 1165 -448 C ATOM 595 CE2 PHE A 104 -13.011 13.402 54.803 1.00104.96 C ANISOU 595 CE2 PHE A 104 16851 12425 10604 1661 957 -452 C ATOM 596 CZ PHE A 104 -13.773 12.254 54.842 1.00103.47 C ANISOU 596 CZ PHE A 104 16491 12378 10444 1596 1072 -457 C ATOM 597 N TRP A 105 -8.854 14.212 57.109 1.00 89.55 N ANISOU 597 N TRP A 105 15479 10037 8507 1440 656 -404 N ATOM 598 CA TRP A 105 -8.026 14.473 55.941 1.00 87.35 C ANISOU 598 CA TRP A 105 15170 9698 8319 1365 555 -387 C ATOM 599 C TRP A 105 -6.780 13.581 55.980 1.00 89.27 C ANISOU 599 C TRP A 105 15389 9935 8595 1226 481 -343 C ATOM 600 O TRP A 105 -6.288 13.227 54.919 1.00 89.96 O ANISOU 600 O TRP A 105 15379 10023 8779 1150 433 -309 O ATOM 601 CB TRP A 105 -7.672 15.966 55.738 1.00 86.45 C ANISOU 601 CB TRP A 105 15216 9457 8173 1408 488 -437 C ATOM 602 CG TRP A 105 -6.881 16.223 54.478 1.00 86.19 C ANISOU 602 CG TRP A 105 15154 9362 8233 1325 404 -416 C ATOM 603 CD1 TRP A 105 -5.574 16.602 54.401 1.00 88.72 C ANISOU 603 CD1 TRP A 105 15562 9591 8558 1206 305 -430 C ATOM 604 CD2 TRP A 105 -7.294 15.941 53.135 1.00 85.19 C ANISOU 604 CD2 TRP A 105 14878 9285 8205 1338 416 -379 C ATOM 605 NE1 TRP A 105 -5.154 16.606 53.096 1.00 86.99 N ANISOU 605 NE1 TRP A 105 15268 9348 8436 1145 261 -398 N ATOM 606 CE2 TRP A 105 -6.186 16.196 52.295 1.00 88.41 C ANISOU 606 CE2 TRP A 105 15308 9611 8674 1230 325 -363 C ATOM 607 CE3 TRP A 105 -8.498 15.502 52.554 1.00 86.38 C ANISOU 607 CE3 TRP A 105 14871 9556 8393 1427 496 -366 C ATOM 608 CZ2 TRP A 105 -6.256 16.062 50.902 1.00 87.06 C ANISOU 608 CZ2 TRP A 105 15025 9460 8596 1221 312 -327 C ATOM 609 CZ3 TRP A 105 -8.560 15.355 51.178 1.00 87.28 C ANISOU 609 CZ3 TRP A 105 14864 9702 8596 1417 474 -338 C ATOM 610 CH2 TRP A 105 -7.452 15.642 50.367 1.00 87.34 C ANISOU 610 CH2 TRP A 105 14913 9612 8659 1322 384 -314 C ATOM 611 N CYS A 106 -6.356 13.123 57.161 1.00 83.40 N ANISOU 611 N CYS A 106 14722 9202 7765 1209 482 -339 N ATOM 612 CA CYS A 106 -5.215 12.215 57.314 1.00 81.57 C ANISOU 612 CA CYS A 106 14470 8986 7538 1114 417 -295 C ATOM 613 C CYS A 106 -5.504 10.876 56.647 1.00 86.73 C ANISOU 613 C CYS A 106 14970 9703 8280 1070 484 -226 C ATOM 614 O CYS A 106 -4.678 10.406 55.860 1.00 85.66 O ANISOU 614 O CYS A 106 14764 9566 8219 990 417 -191 O ATOM 615 CB CYS A 106 -4.846 12.031 58.786 1.00 81.44 C ANISOU 615 CB CYS A 106 14577 8982 7383 1142 413 -306 C ATOM 616 SG CYS A 106 -3.667 10.690 59.088 1.00 84.04 S ANISOU 616 SG CYS A 106 14878 9362 7690 1081 361 -238 S ATOM 617 N GLU A 107 -6.661 10.259 56.964 1.00 85.18 N ANISOU 617 N GLU A 107 14726 9565 8073 1114 623 -214 N ATOM 618 CA GLU A 107 -7.044 8.968 56.389 1.00 85.39 C ANISOU 618 CA GLU A 107 14620 9646 8177 1056 712 -163 C ATOM 619 C GLU A 107 -7.383 9.124 54.897 1.00 89.16 C ANISOU 619 C GLU A 107 14947 10148 8780 1024 695 -172 C ATOM 620 O GLU A 107 -7.022 8.256 54.095 1.00 88.60 O ANISOU 620 O GLU A 107 14782 10091 8793 944 690 -131 O ATOM 621 CB GLU A 107 -8.196 8.315 57.175 1.00 87.87 C ANISOU 621 CB GLU A 107 14930 10019 8438 1088 880 -163 C ATOM 622 CG GLU A 107 -7.768 7.817 58.555 1.00 98.54 C ANISOU 622 CG GLU A 107 16429 11346 9665 1110 910 -130 C ATOM 623 CD GLU A 107 -8.696 6.881 59.312 1.00112.18 C ANISOU 623 CD GLU A 107 18170 13113 11339 1113 1093 -109 C ATOM 624 OE1 GLU A 107 -9.929 6.950 59.103 1.00106.47 O ANISOU 624 OE1 GLU A 107 17351 12456 10646 1119 1209 -151 O ATOM 625 OE2 GLU A 107 -8.185 6.084 60.132 1.00 94.90 O ANISOU 625 OE2 GLU A 107 16092 10895 9070 1113 1126 -54 O ATOM 626 N PHE A 108 -7.995 10.254 54.522 1.00 86.49 N ANISOU 626 N PHE A 108 14605 9813 8446 1100 681 -223 N ATOM 627 CA PHE A 108 -8.343 10.556 53.134 1.00 86.52 C ANISOU 627 CA PHE A 108 14484 9846 8545 1103 659 -233 C ATOM 628 C PHE A 108 -7.084 10.730 52.254 1.00 85.08 C ANISOU 628 C PHE A 108 14308 9590 8428 1026 530 -204 C ATOM 629 O PHE A 108 -7.027 10.164 51.168 1.00 83.48 O ANISOU 629 O PHE A 108 13979 9422 8318 969 524 -180 O ATOM 630 CB PHE A 108 -9.234 11.810 53.044 1.00 90.45 C ANISOU 630 CB PHE A 108 15011 10353 9001 1239 672 -289 C ATOM 631 CG PHE A 108 -10.223 11.689 51.911 1.00 94.01 C ANISOU 631 CG PHE A 108 15284 10915 9519 1279 720 -307 C ATOM 632 CD1 PHE A 108 -9.900 12.131 50.637 1.00 97.31 C ANISOU 632 CD1 PHE A 108 15659 11311 10004 1282 642 -297 C ATOM 633 CD2 PHE A 108 -11.449 11.059 52.100 1.00 99.08 C ANISOU 633 CD2 PHE A 108 15794 11699 10153 1303 847 -337 C ATOM 634 CE1 PHE A 108 -10.797 11.980 49.578 1.00 99.05 C ANISOU 634 CE1 PHE A 108 15708 11654 10272 1329 677 -317 C ATOM 635 CE2 PHE A 108 -12.349 10.911 51.041 1.00102.47 C ANISOU 635 CE2 PHE A 108 16036 12263 10636 1334 884 -369 C ATOM 636 CZ PHE A 108 -12.017 11.376 49.787 1.00 99.89 C ANISOU 636 CZ PHE A 108 15668 11918 10366 1356 793 -358 C ATOM 637 N TRP A 109 -6.090 11.504 52.751 1.00 78.29 N ANISOU 637 N TRP A 109 13593 8639 7516 1015 434 -216 N ATOM 638 CA TRP A 109 -4.796 11.826 52.158 1.00 75.06 C ANISOU 638 CA TRP A 109 13211 8162 7145 931 315 -206 C ATOM 639 C TRP A 109 -4.016 10.543 51.905 1.00 76.91 C ANISOU 639 C TRP A 109 13356 8436 7431 837 294 -150 C ATOM 640 O TRP A 109 -3.597 10.296 50.777 1.00 76.87 O ANISOU 640 O TRP A 109 13259 8433 7515 777 254 -125 O ATOM 641 CB TRP A 109 -4.021 12.783 53.096 1.00 73.79 C ANISOU 641 CB TRP A 109 13223 7923 6890 927 242 -253 C ATOM 642 CG TRP A 109 -2.622 13.083 52.663 1.00 74.52 C ANISOU 642 CG TRP A 109 13339 7967 7008 817 127 -259 C ATOM 643 CD1 TRP A 109 -2.241 13.869 51.621 1.00 76.91 C ANISOU 643 CD1 TRP A 109 13650 8203 7370 774 79 -272 C ATOM 644 CD2 TRP A 109 -1.421 12.571 53.238 1.00 75.01 C ANISOU 644 CD2 TRP A 109 13410 8059 7033 740 51 -255 C ATOM 645 NE1 TRP A 109 -0.874 13.878 51.509 1.00 75.79 N ANISOU 645 NE1 TRP A 109 13512 8049 7235 654 -16 -282 N ATOM 646 CE2 TRP A 109 -0.342 13.095 52.490 1.00 78.23 C ANISOU 646 CE2 TRP A 109 13812 8428 7484 637 -42 -276 C ATOM 647 CE3 TRP A 109 -1.148 11.681 54.291 1.00 77.50 C ANISOU 647 CE3 TRP A 109 13735 8439 7273 757 56 -234 C ATOM 648 CZ2 TRP A 109 0.995 12.778 52.770 1.00 78.56 C ANISOU 648 CZ2 TRP A 109 13834 8517 7498 549 -136 -288 C ATOM 649 CZ3 TRP A 109 0.174 11.346 54.554 1.00 79.98 C ANISOU 649 CZ3 TRP A 109 14041 8795 7552 691 -42 -237 C ATOM 650 CH2 TRP A 109 1.230 11.882 53.790 1.00 80.45 C ANISOU 650 CH2 TRP A 109 14070 8839 7660 587 -140 -268 C ATOM 651 N THR A 110 -3.855 9.722 52.945 1.00 73.00 N ANISOU 651 N THR A 110 12898 7969 6871 837 328 -128 N ATOM 652 CA THR A 110 -3.178 8.428 52.907 1.00 72.49 C ANISOU 652 CA THR A 110 12782 7933 6827 780 327 -68 C ATOM 653 C THR A 110 -3.771 7.566 51.776 1.00 76.00 C ANISOU 653 C THR A 110 13081 8415 7382 740 399 -36 C ATOM 654 O THR A 110 -3.005 7.020 50.979 1.00 74.49 O ANISOU 654 O THR A 110 12823 8223 7256 677 350 -2 O ATOM 655 CB THR A 110 -3.297 7.747 54.299 1.00 76.43 C ANISOU 655 CB THR A 110 13374 8450 7216 827 393 -47 C ATOM 656 OG1 THR A 110 -2.625 8.552 55.272 1.00 78.68 O ANISOU 656 OG1 THR A 110 13784 8716 7394 858 308 -87 O ATOM 657 CG2 THR A 110 -2.752 6.322 54.323 1.00 64.80 C ANISOU 657 CG2 THR A 110 11878 6996 5747 797 423 24 C ATOM 658 N SER A 111 -5.130 7.488 51.691 1.00 73.34 N ANISOU 658 N SER A 111 12685 8120 7059 775 514 -59 N ATOM 659 CA SER A 111 -5.858 6.710 50.681 1.00 72.49 C ANISOU 659 CA SER A 111 12428 8071 7044 731 593 -53 C ATOM 660 C SER A 111 -5.593 7.211 49.261 1.00 75.59 C ANISOU 660 C SER A 111 12728 8465 7527 709 510 -61 C ATOM 661 O SER A 111 -5.357 6.373 48.384 1.00 75.84 O ANISOU 661 O SER A 111 12663 8517 7635 639 516 -34 O ATOM 662 CB SER A 111 -7.359 6.718 50.948 1.00 76.40 C ANISOU 662 CB SER A 111 12866 8643 7520 776 722 -99 C ATOM 663 OG SER A 111 -7.699 6.251 52.242 1.00 85.69 O ANISOU 663 OG SER A 111 14130 9818 8610 792 819 -92 O ATOM 664 N ILE A 112 -5.627 8.554 49.029 1.00 70.78 N ANISOU 664 N ILE A 112 12164 7826 6901 771 442 -95 N ATOM 665 CA ILE A 112 -5.398 9.155 47.695 1.00 69.84 C ANISOU 665 CA ILE A 112 11988 7696 6852 766 371 -97 C ATOM 666 C ILE A 112 -3.972 8.818 47.219 1.00 70.32 C ANISOU 666 C ILE A 112 12053 7706 6958 669 278 -56 C ATOM 667 O ILE A 112 -3.783 8.414 46.079 1.00 70.32 O ANISOU 667 O ILE A 112 11951 7730 7037 623 262 -36 O ATOM 668 CB ILE A 112 -5.668 10.693 47.664 1.00 73.46 C ANISOU 668 CB ILE A 112 12545 8101 7264 863 333 -136 C ATOM 669 CG1 ILE A 112 -7.152 11.018 47.881 1.00 75.34 C ANISOU 669 CG1 ILE A 112 12746 8418 7461 984 424 -178 C ATOM 670 CG2 ILE A 112 -5.172 11.302 46.365 1.00 72.01 C ANISOU 670 CG2 ILE A 112 12346 7876 7138 849 261 -124 C ATOM 671 CD1 ILE A 112 -7.446 12.553 48.254 1.00 85.14 C ANISOU 671 CD1 ILE A 112 14140 9588 8623 1112 404 -216 C ATOM 672 N ASP A 113 -2.994 8.970 48.109 1.00 65.22 N ANISOU 672 N ASP A 113 11516 7011 6255 644 219 -50 N ATOM 673 CA ASP A 113 -1.590 8.653 47.891 1.00 64.23 C ANISOU 673 CA ASP A 113 11389 6866 6148 563 130 -22 C ATOM 674 C ASP A 113 -1.450 7.170 47.428 1.00 68.68 C ANISOU 674 C ASP A 113 11847 7478 6770 518 171 29 C ATOM 675 O ASP A 113 -0.822 6.909 46.388 1.00 68.11 O ANISOU 675 O ASP A 113 11698 7411 6769 463 125 51 O ATOM 676 CB ASP A 113 -0.838 8.913 49.214 1.00 66.08 C ANISOU 676 CB ASP A 113 11744 7082 6281 567 80 -40 C ATOM 677 CG ASP A 113 0.652 8.673 49.243 1.00 73.85 C ANISOU 677 CG ASP A 113 12725 8079 7253 500 -21 -29 C ATOM 678 OD1 ASP A 113 1.156 7.938 48.380 1.00 75.99 O ANISOU 678 OD1 ASP A 113 12900 8379 7595 454 -38 10 O ATOM 679 OD2 ASP A 113 1.291 9.113 50.190 1.00 78.61 O ANISOU 679 OD2 ASP A 113 13416 8684 7769 499 -79 -64 O ATOM 680 N VAL A 114 -2.067 6.227 48.189 1.00 64.69 N ANISOU 680 N VAL A 114 11350 6999 6230 542 270 47 N ATOM 681 CA VAL A 114 -2.056 4.788 47.920 1.00 64.62 C ANISOU 681 CA VAL A 114 11282 7011 6258 502 341 92 C ATOM 682 C VAL A 114 -2.728 4.533 46.560 1.00 69.98 C ANISOU 682 C VAL A 114 11823 7725 7040 460 382 80 C ATOM 683 O VAL A 114 -2.191 3.766 45.756 1.00 68.63 O ANISOU 683 O VAL A 114 11590 7557 6930 406 371 110 O ATOM 684 CB VAL A 114 -2.706 3.961 49.077 1.00 68.92 C ANISOU 684 CB VAL A 114 11897 7558 6732 532 464 108 C ATOM 685 CG1 VAL A 114 -2.787 2.482 48.729 1.00 67.86 C ANISOU 685 CG1 VAL A 114 11726 7420 6637 480 563 150 C ATOM 686 CG2 VAL A 114 -1.940 4.141 50.393 1.00 69.64 C ANISOU 686 CG2 VAL A 114 12127 7628 6708 587 413 124 C ATOM 687 N LEU A 115 -3.862 5.216 46.288 1.00 67.97 N ANISOU 687 N LEU A 115 11520 7508 6795 497 421 31 N ATOM 688 CA LEU A 115 -4.604 5.104 45.026 1.00 67.70 C ANISOU 688 CA LEU A 115 11345 7539 6839 478 451 5 C ATOM 689 C LEU A 115 -3.753 5.523 43.843 1.00 71.69 C ANISOU 689 C LEU A 115 11812 8022 7404 453 345 22 C ATOM 690 O LEU A 115 -3.830 4.880 42.810 1.00 71.48 O ANISOU 690 O LEU A 115 11678 8034 7445 405 361 25 O ATOM 691 CB LEU A 115 -5.909 5.946 45.067 1.00 68.30 C ANISOU 691 CB LEU A 115 11385 7680 6888 560 496 -55 C ATOM 692 CG LEU A 115 -6.666 6.184 43.743 1.00 71.88 C ANISOU 692 CG LEU A 115 11694 8223 7395 583 497 -93 C ATOM 693 CD1 LEU A 115 -7.135 4.885 43.115 1.00 71.13 C ANISOU 693 CD1 LEU A 115 11458 8208 7360 490 582 -110 C ATOM 694 CD2 LEU A 115 -7.828 7.098 43.948 1.00 73.97 C ANISOU 694 CD2 LEU A 115 11941 8558 7606 700 529 -148 C ATOM 695 N CYS A 116 -2.966 6.600 43.986 1.00 69.30 N ANISOU 695 N CYS A 116 11601 7658 7073 477 247 26 N ATOM 696 CA CYS A 116 -2.129 7.161 42.919 1.00 68.67 C ANISOU 696 CA CYS A 116 11505 7547 7039 446 156 40 C ATOM 697 C CYS A 116 -1.006 6.222 42.547 1.00 71.32 C ANISOU 697 C CYS A 116 11800 7880 7418 365 119 82 C ATOM 698 O CYS A 116 -0.751 6.056 41.363 1.00 71.59 O ANISOU 698 O CYS A 116 11754 7930 7517 329 96 94 O ATOM 699 CB CYS A 116 -1.596 8.538 43.307 1.00 69.11 C ANISOU 699 CB CYS A 116 11688 7526 7044 470 83 22 C ATOM 700 SG CYS A 116 -2.824 9.862 43.180 1.00 73.22 S ANISOU 700 SG CYS A 116 12262 8033 7523 591 115 -21 S ATOM 701 N VAL A 117 -0.373 5.579 43.530 1.00 67.24 N ANISOU 701 N VAL A 117 11338 7352 6857 351 118 105 N ATOM 702 CA VAL A 117 0.722 4.648 43.282 1.00 66.61 C ANISOU 702 CA VAL A 117 11229 7280 6800 304 85 147 C ATOM 703 C VAL A 117 0.162 3.414 42.624 1.00 68.91 C ANISOU 703 C VAL A 117 11436 7598 7150 278 174 165 C ATOM 704 O VAL A 117 0.660 3.046 41.572 1.00 69.70 O ANISOU 704 O VAL A 117 11461 7709 7311 237 148 182 O ATOM 705 CB VAL A 117 1.520 4.320 44.568 1.00 72.14 C ANISOU 705 CB VAL A 117 12020 7976 7414 328 58 166 C ATOM 706 CG1 VAL A 117 2.574 3.226 44.327 1.00 72.11 C ANISOU 706 CG1 VAL A 117 11984 7995 7420 313 35 214 C ATOM 707 CG2 VAL A 117 2.147 5.579 45.147 1.00 72.17 C ANISOU 707 CG2 VAL A 117 12098 7964 7359 329 -36 128 C ATOM 708 N THR A 118 -0.914 2.827 43.187 1.00 64.82 N ANISOU 708 N THR A 118 10926 7090 6613 293 288 153 N ATOM 709 CA THR A 118 -1.575 1.621 42.672 1.00 63.69 C ANISOU 709 CA THR A 118 10714 6968 6518 245 399 152 C ATOM 710 C THR A 118 -2.100 1.861 41.250 1.00 65.08 C ANISOU 710 C THR A 118 10757 7199 6772 213 389 116 C ATOM 711 O THR A 118 -1.770 1.069 40.369 1.00 64.01 O ANISOU 711 O THR A 118 10560 7068 6691 161 400 128 O ATOM 712 CB THR A 118 -2.677 1.127 43.621 1.00 67.54 C ANISOU 712 CB THR A 118 11240 7462 6961 250 532 131 C ATOM 713 OG1 THR A 118 -2.158 1.087 44.948 1.00 70.13 O ANISOU 713 OG1 THR A 118 11705 7743 7200 300 527 168 O ATOM 714 CG2 THR A 118 -3.173 -0.256 43.260 1.00 65.86 C ANISOU 714 CG2 THR A 118 10989 7250 6786 174 664 128 C ATOM 715 N ALA A 119 -2.878 2.949 41.019 1.00 61.45 N ANISOU 715 N ALA A 119 10261 6781 6306 260 369 71 N ATOM 716 CA ALA A 119 -3.425 3.272 39.687 1.00 60.77 C ANISOU 716 CA ALA A 119 10055 6763 6272 262 354 36 C ATOM 717 C ALA A 119 -2.301 3.462 38.653 1.00 64.86 C ANISOU 717 C ALA A 119 10558 7251 6836 236 257 73 C ATOM 718 O ALA A 119 -2.434 2.960 37.542 1.00 65.16 O ANISOU 718 O ALA A 119 10496 7335 6927 199 268 62 O ATOM 719 CB ALA A 119 -4.310 4.506 39.740 1.00 61.40 C ANISOU 719 CB ALA A 119 10132 6884 6313 355 339 -5 C ATOM 720 N SER A 120 -1.176 4.111 39.039 1.00 60.93 N ANISOU 720 N SER A 120 10153 6683 6313 243 170 109 N ATOM 721 CA SER A 120 -0.015 4.322 38.176 1.00 60.21 C ANISOU 721 CA SER A 120 10050 6568 6258 205 86 139 C ATOM 722 C SER A 120 0.602 3.006 37.722 1.00 66.89 C ANISOU 722 C SER A 120 10840 7426 7149 148 105 169 C ATOM 723 O SER A 120 0.660 2.752 36.519 1.00 66.07 O ANISOU 723 O SER A 120 10653 7351 7098 120 99 168 O ATOM 724 CB SER A 120 1.046 5.146 38.888 1.00 62.47 C ANISOU 724 CB SER A 120 10439 6796 6499 202 5 153 C ATOM 725 OG SER A 120 0.611 6.482 39.030 1.00 75.56 O ANISOU 725 OG SER A 120 12166 8421 8122 248 -15 125 O ATOM 726 N ILE A 121 1.043 2.162 38.688 1.00 65.34 N ANISOU 726 N ILE A 121 10701 7206 6920 143 134 195 N ATOM 727 CA ILE A 121 1.707 0.897 38.405 1.00 64.50 C ANISOU 727 CA ILE A 121 10575 7094 6837 113 159 231 C ATOM 728 C ILE A 121 0.775 -0.050 37.624 1.00 69.39 C ANISOU 728 C ILE A 121 11119 7738 7510 70 260 205 C ATOM 729 O ILE A 121 1.263 -0.721 36.709 1.00 69.64 O ANISOU 729 O ILE A 121 11099 7773 7586 36 259 219 O ATOM 730 CB ILE A 121 2.330 0.237 39.681 1.00 67.28 C ANISOU 730 CB ILE A 121 11029 7415 7120 150 174 270 C ATOM 731 CG1 ILE A 121 3.148 -1.061 39.363 1.00 66.74 C ANISOU 731 CG1 ILE A 121 10961 7334 7062 149 198 315 C ATOM 732 CG2 ILE A 121 1.304 -0.026 40.732 1.00 68.00 C ANISOU 732 CG2 ILE A 121 11188 7486 7164 172 272 256 C ATOM 733 CD1 ILE A 121 4.342 -0.881 38.464 1.00 64.20 C ANISOU 733 CD1 ILE A 121 10574 7046 6773 137 100 332 C ATOM 734 N TRP A 122 -0.539 -0.082 37.930 1.00 65.70 N ANISOU 734 N TRP A 122 10632 7296 7034 66 347 159 N ATOM 735 CA TRP A 122 -1.433 -0.973 37.189 1.00 65.74 C ANISOU 735 CA TRP A 122 10549 7343 7084 2 446 113 C ATOM 736 C TRP A 122 -1.631 -0.487 35.757 1.00 68.95 C ANISOU 736 C TRP A 122 10835 7821 7541 -6 391 80 C ATOM 737 O TRP A 122 -1.768 -1.324 34.859 1.00 69.07 O ANISOU 737 O TRP A 122 10779 7865 7601 -66 435 56 O ATOM 738 CB TRP A 122 -2.766 -1.176 37.902 1.00 65.69 C ANISOU 738 CB TRP A 122 10537 7370 7051 -14 562 59 C ATOM 739 CG TRP A 122 -2.728 -2.324 38.864 1.00 67.82 C ANISOU 739 CG TRP A 122 10913 7566 7290 -49 677 85 C ATOM 740 CD1 TRP A 122 -2.662 -2.253 40.226 1.00 70.98 C ANISOU 740 CD1 TRP A 122 11435 7915 7620 -2 705 118 C ATOM 741 CD2 TRP A 122 -2.617 -3.720 38.528 1.00 68.47 C ANISOU 741 CD2 TRP A 122 11016 7600 7398 -126 780 89 C ATOM 742 NE1 TRP A 122 -2.548 -3.517 40.762 1.00 70.76 N ANISOU 742 NE1 TRP A 122 11507 7809 7567 -38 823 148 N ATOM 743 CE2 TRP A 122 -2.549 -4.438 39.744 1.00 72.62 C ANISOU 743 CE2 TRP A 122 11690 8038 7863 -117 878 130 C ATOM 744 CE3 TRP A 122 -2.638 -4.441 37.315 1.00 69.76 C ANISOU 744 CE3 TRP A 122 11099 7782 7624 -203 809 57 C ATOM 745 CZ2 TRP A 122 -2.500 -5.836 39.784 1.00 72.82 C ANISOU 745 CZ2 TRP A 122 11801 7979 7888 -179 1013 145 C ATOM 746 CZ3 TRP A 122 -2.577 -5.829 37.357 1.00 71.52 C ANISOU 746 CZ3 TRP A 122 11398 7924 7851 -273 939 64 C ATOM 747 CH2 TRP A 122 -2.491 -6.510 38.575 1.00 72.88 C ANISOU 747 CH2 TRP A 122 11734 7994 7961 -259 1042 110 C ATOM 748 N THR A 123 -1.596 0.853 35.531 1.00 64.94 N ANISOU 748 N THR A 123 10321 7335 7019 57 300 80 N ATOM 749 CA THR A 123 -1.715 1.460 34.197 1.00 64.36 C ANISOU 749 CA THR A 123 10160 7319 6973 75 243 61 C ATOM 750 C THR A 123 -0.492 1.051 33.345 1.00 68.15 C ANISOU 750 C THR A 123 10632 7765 7495 34 191 106 C ATOM 751 O THR A 123 -0.653 0.648 32.184 1.00 68.37 O ANISOU 751 O THR A 123 10571 7846 7561 6 198 84 O ATOM 752 CB THR A 123 -1.885 2.979 34.311 1.00 68.40 C ANISOU 752 CB THR A 123 10718 7827 7445 163 175 63 C ATOM 753 OG1 THR A 123 -3.096 3.228 35.015 1.00 67.55 O ANISOU 753 OG1 THR A 123 10601 7769 7297 212 233 15 O ATOM 754 CG2 THR A 123 -1.946 3.664 32.965 1.00 63.55 C ANISOU 754 CG2 THR A 123 10048 7257 6842 203 122 57 C ATOM 755 N LEU A 124 0.707 1.111 33.943 1.00 63.85 N ANISOU 755 N LEU A 124 10173 7150 6938 31 141 161 N ATOM 756 CA LEU A 124 1.970 0.701 33.338 1.00 63.78 C ANISOU 756 CA LEU A 124 10155 7121 6958 0 95 202 C ATOM 757 C LEU A 124 1.943 -0.770 32.948 1.00 67.69 C ANISOU 757 C LEU A 124 10613 7620 7486 -43 170 200 C ATOM 758 O LEU A 124 2.455 -1.142 31.890 1.00 69.56 O ANISOU 758 O LEU A 124 10796 7874 7760 -69 153 207 O ATOM 759 CB LEU A 124 3.137 0.978 34.296 1.00 64.32 C ANISOU 759 CB LEU A 124 10307 7145 6986 13 35 244 C ATOM 760 CG LEU A 124 3.545 2.464 34.451 1.00 69.38 C ANISOU 760 CG LEU A 124 10993 7769 7601 24 -48 242 C ATOM 761 CD1 LEU A 124 4.622 2.606 35.479 1.00 70.34 C ANISOU 761 CD1 LEU A 124 11178 7872 7675 23 -101 261 C ATOM 762 CD2 LEU A 124 4.036 3.040 33.142 1.00 67.61 C ANISOU 762 CD2 LEU A 124 10721 7556 7413 -3 -96 248 C ATOM 763 N CYS A 125 1.300 -1.588 33.762 1.00 62.94 N ANISOU 763 N CYS A 125 10051 6997 6867 -56 265 185 N ATOM 764 CA CYS A 125 1.117 -3.021 33.510 1.00 62.45 C ANISOU 764 CA CYS A 125 9987 6914 6827 -109 367 174 C ATOM 765 C CYS A 125 0.171 -3.212 32.300 1.00 65.41 C ANISOU 765 C CYS A 125 10241 7364 7247 -166 407 101 C ATOM 766 O CYS A 125 0.460 -4.025 31.435 1.00 64.57 O ANISOU 766 O CYS A 125 10103 7257 7176 -209 433 93 O ATOM 767 CB CYS A 125 0.589 -3.714 34.769 1.00 63.15 C ANISOU 767 CB CYS A 125 10170 6948 6874 -114 475 174 C ATOM 768 SG CYS A 125 0.462 -5.515 34.647 1.00 67.50 S ANISOU 768 SG CYS A 125 10780 7429 7439 -184 629 168 S ATOM 769 N VAL A 126 -0.917 -2.418 32.214 1.00 62.67 N ANISOU 769 N VAL A 126 9824 7096 6891 -153 403 45 N ATOM 770 CA VAL A 126 -1.881 -2.464 31.112 1.00 62.42 C ANISOU 770 CA VAL A 126 9660 7175 6883 -185 426 -35 C ATOM 771 C VAL A 126 -1.168 -2.027 29.801 1.00 67.91 C ANISOU 771 C VAL A 126 10303 7897 7602 -160 331 -12 C ATOM 772 O VAL A 126 -1.288 -2.731 28.790 1.00 69.35 O ANISOU 772 O VAL A 126 10412 8125 7814 -212 359 -52 O ATOM 773 CB VAL A 126 -3.152 -1.637 31.446 1.00 66.24 C ANISOU 773 CB VAL A 126 10083 7754 7331 -142 436 -95 C ATOM 774 CG1 VAL A 126 -4.050 -1.432 30.220 1.00 66.37 C ANISOU 774 CG1 VAL A 126 9946 7920 7351 -136 425 -177 C ATOM 775 CG2 VAL A 126 -3.934 -2.289 32.587 1.00 66.39 C ANISOU 775 CG2 VAL A 126 10134 7759 7330 -194 557 -132 C ATOM 776 N ILE A 127 -0.376 -0.934 29.839 1.00 63.17 N ANISOU 776 N ILE A 127 9753 7262 6986 -93 230 49 N ATOM 777 CA ILE A 127 0.424 -0.465 28.702 1.00 61.71 C ANISOU 777 CA ILE A 127 9542 7085 6818 -76 151 81 C ATOM 778 C ILE A 127 1.312 -1.639 28.196 1.00 64.24 C ANISOU 778 C ILE A 127 9858 7374 7178 -135 174 102 C ATOM 779 O ILE A 127 1.282 -1.949 27.013 1.00 64.68 O ANISOU 779 O ILE A 127 9841 7480 7255 -155 173 78 O ATOM 780 CB ILE A 127 1.270 0.804 29.075 1.00 64.56 C ANISOU 780 CB ILE A 127 9989 7388 7155 -26 64 141 C ATOM 781 CG1 ILE A 127 0.377 2.046 29.229 1.00 65.23 C ANISOU 781 CG1 ILE A 127 10088 7500 7195 50 43 119 C ATOM 782 CG2 ILE A 127 2.357 1.095 28.028 1.00 65.23 C ANISOU 782 CG2 ILE A 127 10064 7463 7259 -38 3 182 C ATOM 783 CD1 ILE A 127 1.029 3.266 29.921 1.00 63.44 C ANISOU 783 CD1 ILE A 127 9978 7191 6936 83 -15 162 C ATOM 784 N ALA A 128 2.052 -2.305 29.096 1.00 60.45 N ANISOU 784 N ALA A 128 9458 6815 6694 -147 198 145 N ATOM 785 CA ALA A 128 2.947 -3.423 28.769 1.00 60.47 C ANISOU 785 CA ALA A 128 9479 6779 6718 -173 225 173 C ATOM 786 C ALA A 128 2.204 -4.562 28.055 1.00 65.47 C ANISOU 786 C ALA A 128 10065 7433 7380 -239 322 110 C ATOM 787 O ALA A 128 2.657 -5.000 26.993 1.00 65.58 O ANISOU 787 O ALA A 128 10036 7463 7419 -257 314 106 O ATOM 788 CB ALA A 128 3.632 -3.950 30.033 1.00 61.10 C ANISOU 788 CB ALA A 128 9666 6783 6766 -145 246 224 C ATOM 789 N VAL A 129 1.063 -5.021 28.621 1.00 61.48 N ANISOU 789 N VAL A 129 9563 6931 6866 -284 417 52 N ATOM 790 CA VAL A 129 0.236 -6.106 28.069 1.00 61.49 C ANISOU 790 CA VAL A 129 9520 6954 6888 -377 528 -31 C ATOM 791 C VAL A 129 -0.331 -5.679 26.668 1.00 66.13 C ANISOU 791 C VAL A 129 9961 7672 7492 -392 482 -101 C ATOM 792 O VAL A 129 -0.249 -6.457 25.704 1.00 63.98 O ANISOU 792 O VAL A 129 9650 7416 7242 -447 516 -142 O ATOM 793 CB VAL A 129 -0.859 -6.533 29.086 1.00 64.52 C ANISOU 793 CB VAL A 129 9937 7325 7254 -434 645 -84 C ATOM 794 CG1 VAL A 129 -1.898 -7.453 28.458 1.00 64.34 C ANISOU 794 CG1 VAL A 129 9839 7357 7250 -558 762 -199 C ATOM 795 CG2 VAL A 129 -0.223 -7.196 30.303 1.00 63.94 C ANISOU 795 CG2 VAL A 129 10028 7113 7154 -413 706 -10 C ATOM 796 N ASP A 130 -0.820 -4.423 26.563 1.00 62.58 N ANISOU 796 N ASP A 130 9448 7310 7020 -327 403 -109 N ATOM 797 CA ASP A 130 -1.320 -3.844 25.317 1.00 61.24 C ANISOU 797 CA ASP A 130 9157 7269 6842 -299 347 -160 C ATOM 798 C ASP A 130 -0.198 -3.819 24.244 1.00 63.66 C ANISOU 798 C ASP A 130 9467 7553 7166 -279 281 -107 C ATOM 799 O ASP A 130 -0.435 -4.222 23.099 1.00 61.25 O ANISOU 799 O ASP A 130 9080 7325 6867 -308 288 -162 O ATOM 800 CB ASP A 130 -1.876 -2.429 25.569 1.00 62.05 C ANISOU 800 CB ASP A 130 9239 7434 6902 -197 277 -152 C ATOM 801 CG ASP A 130 -2.409 -1.773 24.323 1.00 71.78 C ANISOU 801 CG ASP A 130 10366 8803 8105 -133 219 -195 C ATOM 802 OD1 ASP A 130 -3.390 -2.301 23.750 1.00 73.48 O ANISOU 802 OD1 ASP A 130 10458 9150 8310 -173 263 -299 O ATOM 803 OD2 ASP A 130 -1.825 -0.747 23.896 1.00 77.00 O ANISOU 803 OD2 ASP A 130 11069 9441 8745 -47 135 -128 O ATOM 804 N ARG A 131 1.027 -3.388 24.627 1.00 61.03 N ANISOU 804 N ARG A 131 9224 7126 6838 -237 223 -9 N ATOM 805 CA ARG A 131 2.164 -3.365 23.696 1.00 60.32 C ANISOU 805 CA ARG A 131 9135 7020 6763 -225 170 41 C ATOM 806 C ARG A 131 2.561 -4.767 23.302 1.00 65.63 C ANISOU 806 C ARG A 131 9811 7661 7465 -286 238 23 C ATOM 807 O ARG A 131 2.999 -4.938 22.173 1.00 67.02 O ANISOU 807 O ARG A 131 9944 7870 7651 -289 216 21 O ATOM 808 CB ARG A 131 3.381 -2.598 24.247 1.00 59.09 C ANISOU 808 CB ARG A 131 9056 6794 6602 -185 100 132 C ATOM 809 CG ARG A 131 3.270 -1.073 24.211 1.00 61.62 C ANISOU 809 CG ARG A 131 9391 7130 6892 -129 29 155 C ATOM 810 CD ARG A 131 2.889 -0.535 22.842 1.00 59.39 C ANISOU 810 CD ARG A 131 9047 6925 6594 -96 0 135 C ATOM 811 NE ARG A 131 1.439 -0.414 22.687 1.00 58.48 N ANISOU 811 NE ARG A 131 8867 6901 6451 -62 23 62 N ATOM 812 CZ ARG A 131 0.828 -0.095 21.550 1.00 73.57 C ANISOU 812 CZ ARG A 131 10708 8915 8331 -14 3 25 C ATOM 813 NH1 ARG A 131 1.533 0.099 20.440 1.00 64.39 N ANISOU 813 NH1 ARG A 131 9542 7757 7164 -1 -31 59 N ATOM 814 NH2 ARG A 131 -0.491 0.011 21.508 1.00 54.51 N ANISOU 814 NH2 ARG A 131 8218 6612 5882 27 20 -51 N ATOM 815 N TYR A 132 2.355 -5.781 24.183 1.00 62.89 N ANISOU 815 N TYR A 132 9527 7244 7125 -331 329 8 N ATOM 816 CA TYR A 132 2.652 -7.179 23.838 1.00 63.03 C ANISOU 816 CA TYR A 132 9580 7208 7162 -386 416 -13 C ATOM 817 C TYR A 132 1.691 -7.693 22.768 1.00 67.10 C ANISOU 817 C TYR A 132 10000 7807 7687 -464 468 -123 C ATOM 818 O TYR A 132 2.122 -8.355 21.836 1.00 66.19 O ANISOU 818 O TYR A 132 9875 7690 7585 -488 485 -139 O ATOM 819 CB TYR A 132 2.608 -8.119 25.073 1.00 64.48 C ANISOU 819 CB TYR A 132 9885 7277 7335 -409 519 2 C ATOM 820 CG TYR A 132 2.687 -9.583 24.685 1.00 66.28 C ANISOU 820 CG TYR A 132 10175 7434 7576 -471 636 -33 C ATOM 821 CD1 TYR A 132 3.908 -10.174 24.366 1.00 68.40 C ANISOU 821 CD1 TYR A 132 10507 7639 7843 -416 628 29 C ATOM 822 CD2 TYR A 132 1.532 -10.347 24.527 1.00 67.66 C ANISOU 822 CD2 TYR A 132 10334 7616 7759 -589 755 -141 C ATOM 823 CE1 TYR A 132 3.982 -11.504 23.951 1.00 70.28 C ANISOU 823 CE1 TYR A 132 10819 7798 8085 -462 741 -5 C ATOM 824 CE2 TYR A 132 1.594 -11.674 24.103 1.00 69.34 C ANISOU 824 CE2 TYR A 132 10618 7747 7979 -661 874 -184 C ATOM 825 CZ TYR A 132 2.822 -12.248 23.809 1.00 78.47 C ANISOU 825 CZ TYR A 132 11862 8820 9133 -591 867 -112 C ATOM 826 OH TYR A 132 2.892 -13.560 23.390 1.00 83.20 O ANISOU 826 OH TYR A 132 12556 9323 9734 -651 992 -153 O ATOM 827 N PHE A 133 0.386 -7.475 22.966 1.00 66.27 N ANISOU 827 N PHE A 133 9826 7784 7571 -508 501 -207 N ATOM 828 CA PHE A 133 -0.643 -7.942 22.058 1.00 68.14 C ANISOU 828 CA PHE A 133 9950 8135 7805 -591 550 -334 C ATOM 829 C PHE A 133 -0.565 -7.239 20.714 1.00 75.30 C ANISOU 829 C PHE A 133 10750 9165 8697 -533 449 -347 C ATOM 830 O PHE A 133 -0.878 -7.854 19.701 1.00 76.69 O ANISOU 830 O PHE A 133 10854 9413 8871 -593 478 -433 O ATOM 831 CB PHE A 133 -2.018 -7.781 22.681 1.00 70.81 C ANISOU 831 CB PHE A 133 10221 8558 8125 -640 604 -424 C ATOM 832 CG PHE A 133 -2.359 -8.925 23.600 1.00 73.35 C ANISOU 832 CG PHE A 133 10634 8776 8461 -754 755 -461 C ATOM 833 CD1 PHE A 133 -2.815 -10.133 23.093 1.00 77.61 C ANISOU 833 CD1 PHE A 133 11161 9314 9012 -895 875 -569 C ATOM 834 CD2 PHE A 133 -2.226 -8.797 24.973 1.00 75.73 C ANISOU 834 CD2 PHE A 133 11047 8973 8753 -725 786 -391 C ATOM 835 CE1 PHE A 133 -3.126 -11.189 23.943 1.00 80.00 C ANISOU 835 CE1 PHE A 133 11577 9496 9321 -1009 1035 -601 C ATOM 836 CE2 PHE A 133 -2.563 -9.847 25.824 1.00 79.52 C ANISOU 836 CE2 PHE A 133 11631 9348 9234 -824 939 -419 C ATOM 837 CZ PHE A 133 -3.006 -11.034 25.304 1.00 79.05 C ANISOU 837 CZ PHE A 133 11574 9272 9189 -968 1068 -521 C ATOM 838 N ALA A 134 -0.079 -5.994 20.696 1.00 72.46 N ANISOU 838 N ALA A 134 10395 8816 8318 -421 340 -261 N ATOM 839 CA ALA A 134 0.113 -5.234 19.472 1.00 72.55 C ANISOU 839 CA ALA A 134 10342 8920 8305 -350 252 -250 C ATOM 840 C ALA A 134 1.260 -5.835 18.672 1.00 76.86 C ANISOU 840 C ALA A 134 10921 9407 8873 -366 249 -209 C ATOM 841 O ALA A 134 1.035 -6.244 17.528 1.00 78.84 O ANISOU 841 O ALA A 134 11101 9741 9113 -390 254 -274 O ATOM 842 CB ALA A 134 0.388 -3.765 19.788 1.00 72.70 C ANISOU 842 CB ALA A 134 10398 8928 8296 -240 161 -164 C ATOM 843 N ILE A 135 2.470 -5.956 19.292 1.00 69.79 N ANISOU 843 N ILE A 135 10128 8384 8004 -351 243 -111 N ATOM 844 CA ILE A 135 3.699 -6.452 18.653 1.00 67.70 C ANISOU 844 CA ILE A 135 9896 8070 7756 -345 237 -61 C ATOM 845 C ILE A 135 3.534 -7.911 18.185 1.00 73.68 C ANISOU 845 C ILE A 135 10657 8808 8530 -422 332 -135 C ATOM 846 O ILE A 135 4.268 -8.347 17.303 1.00 74.58 O ANISOU 846 O ILE A 135 10770 8919 8648 -416 331 -124 O ATOM 847 CB ILE A 135 4.960 -6.243 19.556 1.00 69.03 C ANISOU 847 CB ILE A 135 10153 8139 7936 -303 208 45 C ATOM 848 CG1 ILE A 135 6.265 -6.282 18.750 1.00 69.31 C ANISOU 848 CG1 ILE A 135 10186 8173 7976 -274 172 101 C ATOM 849 CG2 ILE A 135 5.026 -7.192 20.748 1.00 68.23 C ANISOU 849 CG2 ILE A 135 10141 7939 7845 -325 285 53 C ATOM 850 CD1 ILE A 135 6.921 -4.980 18.548 1.00 73.31 C ANISOU 850 CD1 ILE A 135 10681 8706 8469 -234 86 165 C ATOM 851 N THR A 136 2.589 -8.658 18.749 1.00 70.57 N ANISOU 851 N THR A 136 10274 8397 8142 -500 424 -214 N ATOM 852 CA THR A 136 2.413 -10.046 18.337 1.00 70.96 C ANISOU 852 CA THR A 136 10352 8405 8203 -592 533 -292 C ATOM 853 C THR A 136 1.273 -10.201 17.343 1.00 76.81 C ANISOU 853 C THR A 136 10968 9289 8928 -669 551 -432 C ATOM 854 O THR A 136 1.017 -11.323 16.909 1.00 78.18 O ANISOU 854 O THR A 136 11156 9440 9107 -768 647 -521 O ATOM 855 CB THR A 136 2.209 -10.957 19.546 1.00 72.20 C ANISOU 855 CB THR A 136 10629 8432 8372 -650 652 -296 C ATOM 856 OG1 THR A 136 1.079 -10.498 20.300 1.00 68.04 O ANISOU 856 OG1 THR A 136 10058 7958 7837 -689 668 -346 O ATOM 857 CG2 THR A 136 3.471 -11.085 20.385 1.00 67.06 C ANISOU 857 CG2 THR A 136 10107 7651 7722 -559 641 -168 C ATOM 858 N SER A 137 0.596 -9.105 16.980 1.00 74.05 N ANISOU 858 N SER A 137 10501 9086 8547 -620 464 -455 N ATOM 859 CA SER A 137 -0.500 -9.178 16.025 1.00 75.76 C ANISOU 859 CA SER A 137 10577 9477 8729 -669 465 -594 C ATOM 860 C SER A 137 -0.014 -8.782 14.621 1.00 81.59 C ANISOU 860 C SER A 137 11261 10303 9437 -596 381 -579 C ATOM 861 O SER A 137 1.005 -8.090 14.502 1.00 80.94 O ANISOU 861 O SER A 137 11233 10164 9357 -499 310 -456 O ATOM 862 CB SER A 137 -1.673 -8.296 16.464 1.00 79.74 C ANISOU 862 CB SER A 137 10983 10117 9200 -637 429 -642 C ATOM 863 OG SER A 137 -1.549 -6.931 16.090 1.00 87.44 O ANISOU 863 OG SER A 137 11921 11168 10133 -490 308 -570 O ATOM 864 N PRO A 138 -0.758 -9.154 13.546 1.00 79.22 N ANISOU 864 N PRO A 138 10846 10154 9098 -645 388 -711 N ATOM 865 CA PRO A 138 -0.349 -8.746 12.198 1.00 78.59 C ANISOU 865 CA PRO A 138 10719 10167 8975 -564 309 -697 C ATOM 866 C PRO A 138 -0.228 -7.228 12.039 1.00 81.51 C ANISOU 866 C PRO A 138 11073 10597 9299 -406 194 -598 C ATOM 867 O PRO A 138 0.434 -6.778 11.107 1.00 81.16 O ANISOU 867 O PRO A 138 11039 10572 9224 -327 137 -538 O ATOM 868 CB PRO A 138 -1.481 -9.288 11.324 1.00 81.62 C ANISOU 868 CB PRO A 138 10963 10740 9311 -641 333 -878 C ATOM 869 CG PRO A 138 -2.055 -10.387 12.084 1.00 86.37 C ANISOU 869 CG PRO A 138 11580 11282 9954 -807 458 -981 C ATOM 870 CD PRO A 138 -1.997 -9.961 13.493 1.00 81.57 C ANISOU 870 CD PRO A 138 11050 10559 9385 -782 472 -888 C ATOM 871 N PHE A 139 -0.854 -6.448 12.952 1.00 78.14 N ANISOU 871 N PHE A 139 10635 10191 8864 -360 171 -579 N ATOM 872 CA PHE A 139 -0.850 -4.981 12.951 1.00 78.30 C ANISOU 872 CA PHE A 139 10669 10246 8835 -210 79 -490 C ATOM 873 C PHE A 139 0.470 -4.421 13.526 1.00 79.86 C ANISOU 873 C PHE A 139 11007 10259 9075 -172 58 -332 C ATOM 874 O PHE A 139 0.843 -3.300 13.211 1.00 81.38 O ANISOU 874 O PHE A 139 11243 10447 9231 -66 -6 -247 O ATOM 875 CB PHE A 139 -2.118 -4.433 13.639 1.00 81.30 C ANISOU 875 CB PHE A 139 10976 10736 9180 -171 71 -551 C ATOM 876 CG PHE A 139 -3.394 -5.035 13.088 1.00 84.76 C ANISOU 876 CG PHE A 139 11249 11385 9572 -225 96 -726 C ATOM 877 CD1 PHE A 139 -3.962 -4.553 11.912 1.00 89.26 C ANISOU 877 CD1 PHE A 139 11710 12159 10047 -119 27 -785 C ATOM 878 CD2 PHE A 139 -4.000 -6.120 13.718 1.00 87.38 C ANISOU 878 CD2 PHE A 139 11535 11717 9947 -387 196 -840 C ATOM 879 CE1 PHE A 139 -5.122 -5.136 11.382 1.00 91.40 C ANISOU 879 CE1 PHE A 139 11805 12656 10266 -175 44 -966 C ATOM 880 CE2 PHE A 139 -5.166 -6.694 13.194 1.00 91.62 C ANISOU 880 CE2 PHE A 139 11907 12464 10442 -464 228 -1022 C ATOM 881 CZ PHE A 139 -5.714 -6.204 12.026 1.00 90.86 C ANISOU 881 CZ PHE A 139 11679 12593 10249 -360 145 -1090 C ATOM 882 N LYS A 140 1.190 -5.213 14.324 1.00 73.52 N ANISOU 882 N LYS A 140 10280 9312 8342 -258 115 -297 N ATOM 883 CA LYS A 140 2.489 -4.929 14.937 1.00 71.55 C ANISOU 883 CA LYS A 140 10141 8912 8132 -241 101 -171 C ATOM 884 C LYS A 140 2.544 -3.720 15.947 1.00 74.68 C ANISOU 884 C LYS A 140 10598 9255 8521 -179 55 -92 C ATOM 885 O LYS A 140 2.915 -3.938 17.105 1.00 74.61 O ANISOU 885 O LYS A 140 10654 9144 8549 -211 80 -55 O ATOM 886 CB LYS A 140 3.567 -4.743 13.873 1.00 72.16 C ANISOU 886 CB LYS A 140 10235 8982 8199 -207 66 -110 C ATOM 887 CG LYS A 140 4.933 -5.134 14.383 1.00 72.45 C ANISOU 887 CG LYS A 140 10350 8894 8285 -232 83 -27 C ATOM 888 CD LYS A 140 5.576 -6.112 13.487 1.00 74.76 C ANISOU 888 CD LYS A 140 10631 9186 8587 -260 118 -46 C ATOM 889 CE LYS A 140 6.762 -5.475 12.848 1.00 80.23 C ANISOU 889 CE LYS A 140 11342 9873 9270 -216 75 41 C ATOM 890 NZ LYS A 140 8.008 -6.208 13.150 1.00 85.94 N ANISOU 890 NZ LYS A 140 12105 10521 10028 -229 104 89 N ATOM 891 N TYR A 141 2.260 -2.481 15.535 1.00 68.53 N ANISOU 891 N TYR A 141 9818 8532 7689 -85 -6 -63 N ATOM 892 CA TYR A 141 2.417 -1.365 16.474 1.00 66.52 C ANISOU 892 CA TYR A 141 9646 8203 7427 -35 -39 9 C ATOM 893 C TYR A 141 1.100 -0.712 16.874 1.00 71.83 C ANISOU 893 C TYR A 141 10286 8954 8052 34 -50 -39 C ATOM 894 O TYR A 141 1.116 0.293 17.579 1.00 72.83 O ANISOU 894 O TYR A 141 10490 9022 8161 90 -75 14 O ATOM 895 CB TYR A 141 3.367 -0.327 15.849 1.00 66.96 C ANISOU 895 CB TYR A 141 9773 8212 7456 16 -84 101 C ATOM 896 CG TYR A 141 4.674 -0.959 15.427 1.00 68.09 C ANISOU 896 CG TYR A 141 9928 8304 7641 -48 -72 142 C ATOM 897 CD1 TYR A 141 5.532 -1.528 16.370 1.00 69.49 C ANISOU 897 CD1 TYR A 141 10137 8392 7872 -112 -52 172 C ATOM 898 CD2 TYR A 141 5.015 -1.073 14.081 1.00 68.90 C ANISOU 898 CD2 TYR A 141 10000 8461 7719 -32 -77 144 C ATOM 899 CE1 TYR A 141 6.729 -2.127 15.992 1.00 68.72 C ANISOU 899 CE1 TYR A 141 10038 8269 7803 -150 -41 205 C ATOM 900 CE2 TYR A 141 6.203 -1.690 13.689 1.00 69.49 C ANISOU 900 CE2 TYR A 141 10075 8500 7827 -83 -60 176 C ATOM 901 CZ TYR A 141 7.057 -2.209 14.653 1.00 77.37 C ANISOU 901 CZ TYR A 141 11101 9418 8880 -138 -43 206 C ATOM 902 OH TYR A 141 8.222 -2.829 14.307 1.00 79.81 O ANISOU 902 OH TYR A 141 11402 9710 9213 -168 -27 234 O ATOM 903 N GLN A 142 -0.034 -1.275 16.455 1.00 69.02 N ANISOU 903 N GLN A 142 9815 8740 7671 30 -29 -147 N ATOM 904 CA GLN A 142 -1.355 -0.722 16.762 1.00 69.26 C ANISOU 904 CA GLN A 142 9783 8886 7645 106 -39 -210 C ATOM 905 C GLN A 142 -2.041 -1.559 17.814 1.00 73.76 C ANISOU 905 C GLN A 142 10307 9462 8256 9 30 -286 C ATOM 906 O GLN A 142 -2.082 -2.786 17.681 1.00 73.85 O ANISOU 906 O GLN A 142 10270 9483 8308 -111 91 -355 O ATOM 907 CB GLN A 142 -2.231 -0.703 15.506 1.00 71.65 C ANISOU 907 CB GLN A 142 9962 9389 7873 177 -67 -297 C ATOM 908 CG GLN A 142 -1.913 0.379 14.492 1.00 97.23 C ANISOU 908 CG GLN A 142 13256 12651 11037 322 -133 -225 C ATOM 909 CD GLN A 142 -2.923 0.290 13.381 1.00126.25 C ANISOU 909 CD GLN A 142 16793 16553 14623 404 -161 -326 C ATOM 910 OE1 GLN A 142 -2.773 -0.496 12.435 1.00126.72 O ANISOU 910 OE1 GLN A 142 16782 16683 14682 347 -156 -381 O ATOM 911 NE2 GLN A 142 -4.027 1.017 13.523 1.00117.89 N ANISOU 911 NE2 GLN A 142 15681 15630 13481 540 -191 -368 N ATOM 912 N SER A 143 -2.608 -0.908 18.844 1.00 70.65 N ANISOU 912 N SER A 143 9940 9059 7846 58 30 -278 N ATOM 913 CA SER A 143 -3.361 -1.579 19.899 1.00 70.82 C ANISOU 913 CA SER A 143 9922 9093 7893 -27 104 -350 C ATOM 914 C SER A 143 -4.512 -2.389 19.303 1.00 76.14 C ANISOU 914 C SER A 143 10428 9955 8545 -89 150 -501 C ATOM 915 O SER A 143 -5.088 -1.977 18.295 1.00 76.80 O ANISOU 915 O SER A 143 10410 10206 8563 -3 99 -554 O ATOM 916 CB SER A 143 -3.917 -0.557 20.888 1.00 73.49 C ANISOU 916 CB SER A 143 10299 9428 8195 68 87 -325 C ATOM 917 OG SER A 143 -4.883 -1.135 21.757 1.00 77.77 O ANISOU 917 OG SER A 143 10775 10028 8744 -1 163 -413 O ATOM 918 N LEU A 144 -4.856 -3.520 19.929 1.00 72.53 N ANISOU 918 N LEU A 144 9949 9476 8134 -238 251 -575 N ATOM 919 CA LEU A 144 -5.996 -4.311 19.470 1.00 73.50 C ANISOU 919 CA LEU A 144 9909 9780 8237 -333 312 -740 C ATOM 920 C LEU A 144 -7.266 -3.776 20.150 1.00 78.05 C ANISOU 920 C LEU A 144 10387 10505 8766 -286 326 -814 C ATOM 921 O LEU A 144 -8.370 -4.258 19.891 1.00 79.40 O ANISOU 921 O LEU A 144 10394 10867 8907 -357 374 -967 O ATOM 922 CB LEU A 144 -5.792 -5.825 19.722 1.00 73.35 C ANISOU 922 CB LEU A 144 9927 9659 8282 -531 437 -795 C ATOM 923 CG LEU A 144 -4.556 -6.474 19.071 1.00 75.60 C ANISOU 923 CG LEU A 144 10309 9805 8610 -569 435 -730 C ATOM 924 CD1 LEU A 144 -4.368 -7.878 19.573 1.00 75.02 C ANISOU 924 CD1 LEU A 144 10318 9597 8590 -735 571 -767 C ATOM 925 CD2 LEU A 144 -4.630 -6.440 17.555 1.00 76.24 C ANISOU 925 CD2 LEU A 144 10283 10031 8652 -538 375 -790 C ATOM 926 N LEU A 145 -7.100 -2.750 20.991 1.00 73.80 N ANISOU 926 N LEU A 145 9942 9888 8213 -167 283 -714 N ATOM 927 CA LEU A 145 -8.204 -2.123 21.698 1.00 75.02 C ANISOU 927 CA LEU A 145 10022 10165 8316 -94 292 -767 C ATOM 928 C LEU A 145 -8.750 -0.944 20.921 1.00 80.98 C ANISOU 928 C LEU A 145 10699 11095 8976 112 189 -774 C ATOM 929 O LEU A 145 -8.027 -0.295 20.163 1.00 79.94 O ANISOU 929 O LEU A 145 10643 10908 8822 220 107 -684 O ATOM 930 CB LEU A 145 -7.777 -1.632 23.104 1.00 74.16 C ANISOU 930 CB LEU A 145 10072 9874 8232 -66 307 -660 C ATOM 931 CG LEU A 145 -7.312 -2.663 24.140 1.00 77.92 C ANISOU 931 CG LEU A 145 10651 10176 8779 -227 411 -639 C ATOM 932 CD1 LEU A 145 -6.506 -1.991 25.236 1.00 77.34 C ANISOU 932 CD1 LEU A 145 10753 9916 8718 -161 382 -505 C ATOM 933 CD2 LEU A 145 -8.477 -3.464 24.706 1.00 78.17 C ANISOU 933 CD2 LEU A 145 10578 10314 8809 -354 534 -772 C ATOM 934 N THR A 146 -10.034 -0.660 21.138 1.00 78.54 N ANISOU 934 N THR A 146 10244 10997 8602 173 202 -881 N ATOM 935 CA THR A 146 -10.697 0.523 20.623 1.00 78.28 C ANISOU 935 CA THR A 146 10146 11138 8457 406 114 -887 C ATOM 936 C THR A 146 -10.523 1.550 21.716 1.00 80.86 C ANISOU 936 C THR A 146 10628 11322 8774 524 102 -778 C ATOM 937 O THR A 146 -10.310 1.164 22.871 1.00 81.00 O ANISOU 937 O THR A 146 10721 11198 8857 407 172 -755 O ATOM 938 CB THR A 146 -12.171 0.235 20.297 1.00 87.02 C ANISOU 938 CB THR A 146 10996 12578 9491 415 135 -1073 C ATOM 939 OG1 THR A 146 -12.890 0.005 21.510 1.00 89.49 O ANISOU 939 OG1 THR A 146 11262 12917 9822 337 223 -1135 O ATOM 940 CG2 THR A 146 -12.355 -0.917 19.328 1.00 84.31 C ANISOU 940 CG2 THR A 146 10499 12371 9164 252 164 -1205 C ATOM 941 N LYS A 147 -10.629 2.839 21.389 1.00 76.81 N ANISOU 941 N LYS A 147 10174 10838 8172 757 21 -714 N ATOM 942 CA LYS A 147 -10.516 3.915 22.371 1.00 76.04 C ANISOU 942 CA LYS A 147 10237 10605 8051 882 12 -621 C ATOM 943 C LYS A 147 -11.621 3.792 23.427 1.00 81.69 C ANISOU 943 C LYS A 147 10848 11444 8749 874 76 -714 C ATOM 944 O LYS A 147 -11.369 4.140 24.582 1.00 80.72 O ANISOU 944 O LYS A 147 10857 11161 8652 866 106 -651 O ATOM 945 CB LYS A 147 -10.534 5.290 21.696 1.00 78.70 C ANISOU 945 CB LYS A 147 10666 10957 8278 1142 -71 -547 C ATOM 946 CG LYS A 147 -9.231 5.601 20.973 1.00 81.71 C ANISOU 946 CG LYS A 147 11217 11142 8687 1135 -115 -423 C ATOM 947 CD LYS A 147 -9.326 6.864 20.166 1.00 89.06 C ANISOU 947 CD LYS A 147 12245 12095 9498 1385 -177 -359 C ATOM 948 CE LYS A 147 -8.504 6.723 18.923 1.00102.64 C ANISOU 948 CE LYS A 147 14004 13774 11222 1364 -213 -308 C ATOM 949 NZ LYS A 147 -8.491 7.977 18.132 1.00121.18 N ANISOU 949 NZ LYS A 147 16488 16108 13446 1607 -259 -227 N ATOM 950 N ASN A 148 -12.798 3.216 23.065 1.00 80.34 N ANISOU 950 N ASN A 148 10433 11558 8535 851 105 -872 N ATOM 951 CA ASN A 148 -13.880 2.982 24.028 1.00 81.90 C ANISOU 951 CA ASN A 148 10504 11897 8717 814 183 -979 C ATOM 952 C ASN A 148 -13.480 1.913 25.025 1.00 84.33 C ANISOU 952 C ASN A 148 10868 12035 9138 556 292 -980 C ATOM 953 O ASN A 148 -13.673 2.114 26.225 1.00 84.43 O ANISOU 953 O ASN A 148 10949 11972 9158 551 346 -959 O ATOM 954 CB ASN A 148 -15.198 2.598 23.346 1.00 89.48 C ANISOU 954 CB ASN A 148 11171 13227 9601 832 191 -1165 C ATOM 955 CG ASN A 148 -16.075 3.765 22.954 1.00124.74 C ANISOU 955 CG ASN A 148 15554 17922 13921 1137 113 -1190 C ATOM 956 OD1 ASN A 148 -16.228 4.744 23.696 1.00123.97 O ANISOU 956 OD1 ASN A 148 15569 17759 13776 1309 102 -1120 O ATOM 957 ND2 ASN A 148 -16.730 3.654 21.802 1.00118.74 N ANISOU 957 ND2 ASN A 148 14590 17452 13076 1218 60 -1302 N ATOM 958 N LYS A 149 -12.894 0.791 24.539 1.00 79.87 N ANISOU 958 N LYS A 149 10296 11400 8652 356 328 -999 N ATOM 959 CA LYS A 149 -12.429 -0.318 25.385 1.00 78.43 C ANISOU 959 CA LYS A 149 10195 11039 8568 122 439 -991 C ATOM 960 C LYS A 149 -11.322 0.170 26.323 1.00 80.72 C ANISOU 960 C LYS A 149 10732 11038 8898 157 420 -824 C ATOM 961 O LYS A 149 -11.412 -0.077 27.522 1.00 79.74 O ANISOU 961 O LYS A 149 10676 10824 8798 87 499 -813 O ATOM 962 CB LYS A 149 -11.966 -1.520 24.551 1.00 79.85 C ANISOU 962 CB LYS A 149 10339 11191 8808 -62 475 -1036 C ATOM 963 CG LYS A 149 -13.127 -2.334 24.010 1.00 94.64 C ANISOU 963 CG LYS A 149 11971 13331 10656 -185 544 -1235 C ATOM 964 CD LYS A 149 -12.723 -3.746 23.635 1.00107.83 C ANISOU 964 CD LYS A 149 13652 14917 12401 -425 634 -1290 C ATOM 965 CE LYS A 149 -13.666 -4.368 22.627 1.00120.02 C ANISOU 965 CE LYS A 149 14956 16741 13907 -523 660 -1487 C ATOM 966 NZ LYS A 149 -13.311 -3.990 21.231 1.00129.32 N ANISOU 966 NZ LYS A 149 16083 18009 15042 -400 532 -1474 N ATOM 967 N ALA A 150 -10.335 0.937 25.788 1.00 76.89 N ANISOU 967 N ALA A 150 10376 10428 8410 272 316 -703 N ATOM 968 CA ALA A 150 -9.240 1.546 26.559 1.00 75.30 C ANISOU 968 CA ALA A 150 10395 9978 8236 310 283 -557 C ATOM 969 C ALA A 150 -9.800 2.442 27.687 1.00 79.43 C ANISOU 969 C ALA A 150 10974 10497 8708 423 292 -544 C ATOM 970 O ALA A 150 -9.305 2.357 28.818 1.00 78.99 O ANISOU 970 O ALA A 150 11050 10278 8685 366 328 -485 O ATOM 971 CB ALA A 150 -8.313 2.345 25.646 1.00 75.02 C ANISOU 971 CB ALA A 150 10456 9860 8187 416 179 -459 C ATOM 972 N ARG A 151 -10.866 3.236 27.403 1.00 75.63 N ANISOU 972 N ARG A 151 10390 10208 8140 590 264 -605 N ATOM 973 CA ARG A 151 -11.516 4.081 28.414 1.00 75.66 C ANISOU 973 CA ARG A 151 10434 10230 8084 715 279 -605 C ATOM 974 C ARG A 151 -12.145 3.213 29.495 1.00 77.84 C ANISOU 974 C ARG A 151 10641 10546 8390 570 396 -681 C ATOM 975 O ARG A 151 -11.997 3.531 30.675 1.00 78.16 O ANISOU 975 O ARG A 151 10807 10462 8428 581 426 -632 O ATOM 976 CB ARG A 151 -12.578 5.010 27.803 1.00 78.73 C ANISOU 976 CB ARG A 151 10711 10844 8361 942 230 -663 C ATOM 977 CG ARG A 151 -12.020 6.162 26.985 1.00 93.36 C ANISOU 977 CG ARG A 151 12696 12620 10157 1132 130 -566 C ATOM 978 CD ARG A 151 -13.144 6.978 26.381 1.00107.38 C ANISOU 978 CD ARG A 151 14361 14634 11804 1381 90 -627 C ATOM 979 NE ARG A 151 -12.704 7.672 25.174 1.00116.19 N ANISOU 979 NE ARG A 151 15553 15730 12864 1530 8 -559 N ATOM 980 CZ ARG A 151 -13.306 7.587 23.993 1.00133.76 C ANISOU 980 CZ ARG A 151 17616 18189 15017 1633 -35 -628 C ATOM 981 NH1 ARG A 151 -14.408 6.860 23.851 1.00118.59 N ANISOU 981 NH1 ARG A 151 15429 16559 13071 1597 -6 -781 N ATOM 982 NH2 ARG A 151 -12.820 8.239 22.945 1.00126.31 N ANISOU 982 NH2 ARG A 151 16775 17199 14018 1771 -102 -551 N ATOM 983 N VAL A 152 -12.808 2.098 29.100 1.00 72.66 N ANISOU 983 N VAL A 152 9799 10053 7757 423 469 -804 N ATOM 984 CA VAL A 152 -13.440 1.167 30.042 1.00 72.29 C ANISOU 984 CA VAL A 152 9689 10042 7736 256 605 -887 C ATOM 985 C VAL A 152 -12.364 0.547 30.956 1.00 73.79 C ANISOU 985 C VAL A 152 10084 9952 8000 119 658 -784 C ATOM 986 O VAL A 152 -12.583 0.491 32.161 1.00 74.51 O ANISOU 986 O VAL A 152 10244 9981 8084 90 733 -775 O ATOM 987 CB VAL A 152 -14.326 0.086 29.352 1.00 77.04 C ANISOU 987 CB VAL A 152 10058 10867 8345 99 685 -1053 C ATOM 988 CG1 VAL A 152 -14.890 -0.911 30.374 1.00 77.26 C ANISOU 988 CG1 VAL A 152 10058 10893 8404 -102 851 -1132 C ATOM 989 CG2 VAL A 152 -15.472 0.735 28.571 1.00 78.12 C ANISOU 989 CG2 VAL A 152 9970 11324 8388 257 629 -1168 C ATOM 990 N ILE A 153 -11.191 0.170 30.412 1.00 68.10 N ANISOU 990 N ILE A 153 9466 9073 7337 61 612 -703 N ATOM 991 CA ILE A 153 -10.102 -0.405 31.208 1.00 66.96 C ANISOU 991 CA ILE A 153 9509 8686 7248 -38 648 -604 C ATOM 992 C ILE A 153 -9.522 0.643 32.194 1.00 71.60 C ANISOU 992 C ILE A 153 10269 9129 7807 86 588 -494 C ATOM 993 O ILE A 153 -9.315 0.310 33.365 1.00 72.28 O ANISOU 993 O ILE A 153 10464 9101 7897 32 654 -460 O ATOM 994 CB ILE A 153 -9.024 -1.046 30.307 1.00 69.17 C ANISOU 994 CB ILE A 153 9832 8864 7586 -113 612 -555 C ATOM 995 CG1 ILE A 153 -9.611 -2.303 29.635 1.00 69.98 C ANISOU 995 CG1 ILE A 153 9798 9074 7718 -277 708 -674 C ATOM 996 CG2 ILE A 153 -7.761 -1.431 31.117 1.00 69.44 C ANISOU 996 CG2 ILE A 153 10066 8661 7659 -161 621 -438 C ATOM 997 CD1 ILE A 153 -9.202 -2.550 28.237 1.00 72.42 C ANISOU 997 CD1 ILE A 153 10041 9427 8048 -290 647 -688 C ATOM 998 N ILE A 154 -9.313 1.901 31.755 1.00 67.95 N ANISOU 998 N ILE A 154 9839 8673 7305 249 475 -447 N ATOM 999 CA ILE A 154 -8.778 2.959 32.631 1.00 67.10 C ANISOU 999 CA ILE A 154 9901 8427 7165 355 422 -359 C ATOM 1000 C ILE A 154 -9.741 3.149 33.820 1.00 73.99 C ANISOU 1000 C ILE A 154 10768 9355 7991 389 497 -406 C ATOM 1001 O ILE A 154 -9.305 3.160 34.970 1.00 71.76 O ANISOU 1001 O ILE A 154 10620 8939 7705 365 523 -355 O ATOM 1002 CB ILE A 154 -8.470 4.282 31.854 1.00 68.80 C ANISOU 1002 CB ILE A 154 10169 8631 7341 516 310 -310 C ATOM 1003 CG1 ILE A 154 -7.303 4.060 30.859 1.00 68.44 C ANISOU 1003 CG1 ILE A 154 10161 8498 7346 461 247 -248 C ATOM 1004 CG2 ILE A 154 -8.112 5.420 32.797 1.00 66.31 C ANISOU 1004 CG2 ILE A 154 10029 8184 6982 616 274 -245 C ATOM 1005 CD1 ILE A 154 -7.312 5.024 29.623 1.00 70.12 C ANISOU 1005 CD1 ILE A 154 10364 8762 7516 598 164 -230 C ATOM 1006 N LEU A 155 -11.048 3.215 33.537 1.00 75.27 N ANISOU 1006 N LEU A 155 10760 9730 8111 439 537 -511 N ATOM 1007 CA LEU A 155 -12.092 3.339 34.550 1.00 77.37 C ANISOU 1007 CA LEU A 155 10981 10088 8326 469 620 -574 C ATOM 1008 C LEU A 155 -12.067 2.171 35.533 1.00 83.09 C ANISOU 1008 C LEU A 155 11741 10739 9090 287 747 -587 C ATOM 1009 O LEU A 155 -12.223 2.415 36.722 1.00 83.84 O ANISOU 1009 O LEU A 155 11928 10776 9152 312 794 -567 O ATOM 1010 CB LEU A 155 -13.458 3.425 33.879 1.00 79.31 C ANISOU 1010 CB LEU A 155 10996 10617 8522 534 642 -703 C ATOM 1011 CG LEU A 155 -14.206 4.673 34.243 1.00 87.09 C ANISOU 1011 CG LEU A 155 11980 11696 9414 754 610 -716 C ATOM 1012 CD1 LEU A 155 -14.083 5.750 33.133 1.00 87.46 C ANISOU 1012 CD1 LEU A 155 12035 11785 9408 957 486 -681 C ATOM 1013 CD2 LEU A 155 -15.646 4.343 34.609 1.00 93.89 C ANISOU 1013 CD2 LEU A 155 12636 12809 10229 743 711 -854 C ATOM 1014 N MET A 156 -11.830 0.920 35.047 1.00 80.63 N ANISOU 1014 N MET A 156 11380 10415 8841 112 808 -614 N ATOM 1015 CA MET A 156 -11.751 -0.291 35.867 1.00 81.51 C ANISOU 1015 CA MET A 156 11554 10432 8984 -62 944 -620 C ATOM 1016 C MET A 156 -10.544 -0.242 36.792 1.00 80.30 C ANISOU 1016 C MET A 156 11632 10042 8837 -48 916 -488 C ATOM 1017 O MET A 156 -10.698 -0.502 37.978 1.00 79.37 O ANISOU 1017 O MET A 156 11606 9859 8692 -78 1004 -474 O ATOM 1018 CB MET A 156 -11.734 -1.574 35.010 1.00 85.58 C ANISOU 1018 CB MET A 156 11985 10973 9558 -239 1014 -680 C ATOM 1019 CG MET A 156 -13.098 -1.961 34.467 1.00 93.54 C ANISOU 1019 CG MET A 156 12760 12230 10552 -317 1098 -844 C ATOM 1020 SD MET A 156 -14.481 -1.524 35.593 1.00103.11 S ANISOU 1020 SD MET A 156 13882 13602 11691 -279 1198 -932 S ATOM 1021 CE MET A 156 -14.414 -2.947 36.802 1.00100.32 C ANISOU 1021 CE MET A 156 13675 13077 11367 -510 1412 -927 C ATOM 1022 N VAL A 157 -9.360 0.140 36.266 1.00 74.29 N ANISOU 1022 N VAL A 157 10957 9167 8102 5 794 -398 N ATOM 1023 CA VAL A 157 -8.107 0.281 37.025 1.00 71.34 C ANISOU 1023 CA VAL A 157 10778 8601 7727 28 743 -284 C ATOM 1024 C VAL A 157 -8.344 1.234 38.182 1.00 73.91 C ANISOU 1024 C VAL A 157 11193 8902 7988 132 729 -263 C ATOM 1025 O VAL A 157 -8.086 0.849 39.313 1.00 73.74 O ANISOU 1025 O VAL A 157 11289 8786 7941 103 787 -227 O ATOM 1026 CB VAL A 157 -6.914 0.725 36.134 1.00 73.09 C ANISOU 1026 CB VAL A 157 11039 8752 7981 69 609 -213 C ATOM 1027 CG1 VAL A 157 -5.705 1.140 36.971 1.00 71.81 C ANISOU 1027 CG1 VAL A 157 11049 8434 7799 108 542 -116 C ATOM 1028 CG2 VAL A 157 -6.531 -0.376 35.147 1.00 72.53 C ANISOU 1028 CG2 VAL A 157 10908 8679 7969 -40 634 -223 C ATOM 1029 N TRP A 158 -8.918 2.418 37.919 1.00 70.72 N ANISOU 1029 N TRP A 158 10738 8588 7546 260 667 -292 N ATOM 1030 CA TRP A 158 -9.195 3.430 38.939 1.00 71.72 C ANISOU 1030 CA TRP A 158 10956 8691 7604 375 653 -281 C ATOM 1031 C TRP A 158 -10.270 2.992 39.949 1.00 77.85 C ANISOU 1031 C TRP A 158 11696 9543 8342 345 787 -343 C ATOM 1032 O TRP A 158 -10.051 3.174 41.145 1.00 77.52 O ANISOU 1032 O TRP A 158 11788 9409 8257 367 810 -305 O ATOM 1033 CB TRP A 158 -9.539 4.777 38.295 1.00 70.82 C ANISOU 1033 CB TRP A 158 10815 8642 7452 534 564 -294 C ATOM 1034 CG TRP A 158 -8.308 5.483 37.810 1.00 71.01 C ANISOU 1034 CG TRP A 158 10959 8531 7492 568 445 -214 C ATOM 1035 CD1 TRP A 158 -7.648 5.267 36.635 1.00 73.03 C ANISOU 1035 CD1 TRP A 158 11175 8775 7799 528 386 -188 C ATOM 1036 CD2 TRP A 158 -7.506 6.413 38.554 1.00 71.26 C ANISOU 1036 CD2 TRP A 158 11172 8416 7488 621 383 -155 C ATOM 1037 NE1 TRP A 158 -6.521 6.053 36.570 1.00 71.76 N ANISOU 1037 NE1 TRP A 158 11153 8475 7636 553 296 -117 N ATOM 1038 CE2 TRP A 158 -6.412 6.774 37.732 1.00 74.03 C ANISOU 1038 CE2 TRP A 158 11577 8680 7872 604 292 -101 C ATOM 1039 CE3 TRP A 158 -7.656 7.056 39.803 1.00 73.37 C ANISOU 1039 CE3 TRP A 158 11560 8626 7692 682 399 -153 C ATOM 1040 CZ2 TRP A 158 -5.476 7.744 38.116 1.00 73.27 C ANISOU 1040 CZ2 TRP A 158 11644 8446 7750 629 222 -54 C ATOM 1041 CZ3 TRP A 158 -6.732 8.020 40.178 1.00 74.48 C ANISOU 1041 CZ3 TRP A 158 11868 8627 7804 716 322 -107 C ATOM 1042 CH2 TRP A 158 -5.647 8.341 39.349 1.00 74.37 C ANISOU 1042 CH2 TRP A 158 11898 8531 7827 679 237 -62 C ATOM 1043 N ILE A 159 -11.377 2.373 39.499 1.00 77.24 N ANISOU 1043 N ILE A 159 11440 9634 8275 283 879 -441 N ATOM 1044 CA ILE A 159 -12.440 1.892 40.403 1.00 79.32 C ANISOU 1044 CA ILE A 159 11651 9984 8502 229 1026 -513 C ATOM 1045 C ILE A 159 -11.889 0.765 41.319 1.00 82.55 C ANISOU 1045 C ILE A 159 12200 10238 8927 89 1131 -462 C ATOM 1046 O ILE A 159 -12.070 0.821 42.544 1.00 83.02 O ANISOU 1046 O ILE A 159 12362 10247 8933 106 1199 -444 O ATOM 1047 CB ILE A 159 -13.722 1.439 39.622 1.00 84.00 C ANISOU 1047 CB ILE A 159 11997 10818 9102 168 1105 -649 C ATOM 1048 CG1 ILE A 159 -14.495 2.662 39.075 1.00 84.59 C ANISOU 1048 CG1 ILE A 159 11946 11074 9122 360 1020 -703 C ATOM 1049 CG2 ILE A 159 -14.646 0.561 40.510 1.00 86.74 C ANISOU 1049 CG2 ILE A 159 12296 11231 9431 34 1293 -728 C ATOM 1050 CD1 ILE A 159 -15.406 2.355 37.882 1.00 94.08 C ANISOU 1050 CD1 ILE A 159 12894 12524 10329 335 1032 -825 C ATOM 1051 N VAL A 160 -11.225 -0.236 40.722 1.00 77.38 N ANISOU 1051 N VAL A 160 11561 9507 8333 -31 1147 -437 N ATOM 1052 CA VAL A 160 -10.664 -1.358 41.470 1.00 77.27 C ANISOU 1052 CA VAL A 160 11695 9339 8323 -141 1249 -382 C ATOM 1053 C VAL A 160 -9.543 -0.856 42.424 1.00 80.08 C ANISOU 1053 C VAL A 160 12257 9532 8637 -40 1163 -265 C ATOM 1054 O VAL A 160 -9.607 -1.196 43.604 1.00 81.51 O ANISOU 1054 O VAL A 160 12560 9644 8765 -50 1254 -238 O ATOM 1055 CB VAL A 160 -10.217 -2.553 40.573 1.00 80.46 C ANISOU 1055 CB VAL A 160 12081 9696 8795 -278 1292 -385 C ATOM 1056 CG1 VAL A 160 -9.429 -3.579 41.372 1.00 80.40 C ANISOU 1056 CG1 VAL A 160 12274 9500 8775 -339 1378 -302 C ATOM 1057 CG2 VAL A 160 -11.426 -3.226 39.932 1.00 81.00 C ANISOU 1057 CG2 VAL A 160 11964 9924 8889 -415 1417 -521 C ATOM 1058 N ASER A 161 -8.562 -0.057 41.938 0.50 75.57 N ANISOU 1058 N ASER A 161 11722 8912 8081 49 999 -206 N ATOM 1059 N BSER A 161 -8.569 -0.045 41.937 0.50 74.34 N ANISOU 1059 N BSER A 161 11564 8756 7924 50 998 -206 N ATOM 1060 CA ASER A 161 -7.476 0.447 42.794 0.50 74.76 C ANISOU 1060 CA ASER A 161 11791 8681 7933 128 911 -116 C ATOM 1061 CA BSER A 161 -7.481 0.500 42.770 0.50 72.89 C ANISOU 1061 CA BSER A 161 11551 8447 7697 132 906 -117 C ATOM 1062 C ASER A 161 -8.020 1.381 43.903 0.50 79.49 C ANISOU 1062 C ASER A 161 12450 9297 8455 224 916 -131 C ATOM 1063 C BSER A 161 -8.035 1.366 43.908 0.50 78.70 C ANISOU 1063 C BSER A 161 12350 9199 8355 223 919 -131 C ATOM 1064 O ASER A 161 -7.476 1.377 45.007 0.50 79.05 O ANISOU 1064 O ASER A 161 12543 9151 8341 255 917 -78 O ATOM 1065 O BSER A 161 -7.499 1.333 45.018 0.50 78.31 O ANISOU 1065 O BSER A 161 12449 9058 8248 251 922 -79 O ATOM 1066 CB ASER A 161 -6.375 1.123 41.979 0.50 76.76 C ANISOU 1066 CB ASER A 161 12052 8893 8220 176 750 -70 C ATOM 1067 CB BSER A 161 -6.493 1.311 41.935 0.50 72.48 C ANISOU 1067 CB BSER A 161 11498 8364 7676 189 742 -78 C ATOM 1068 OG ASER A 161 -6.846 2.219 41.214 0.50 85.12 O ANISOU 1068 OG ASER A 161 13019 10036 9288 248 675 -111 O ATOM 1069 OG BSER A 161 -5.791 0.494 41.018 0.50 70.25 O ANISOU 1069 OG BSER A 161 11183 8053 7456 115 726 -52 O ATOM 1070 N GLY A 162 -9.125 2.084 43.624 1.00 76.73 N ANISOU 1070 N GLY A 162 11983 9075 8095 277 930 -205 N ATOM 1071 CA GLY A 162 -9.830 2.934 44.583 1.00 77.42 C ANISOU 1071 CA GLY A 162 12109 9199 8106 375 953 -233 C ATOM 1072 C GLY A 162 -10.499 2.110 45.671 1.00 85.41 C ANISOU 1072 C GLY A 162 13155 10220 9076 310 1116 -254 C ATOM 1073 O GLY A 162 -10.556 2.537 46.831 1.00 87.15 O ANISOU 1073 O GLY A 162 13491 10400 9222 376 1134 -236 O ATOM 1074 N LEU A 163 -10.977 0.900 45.317 1.00 82.96 N ANISOU 1074 N LEU A 163 12760 9954 8808 172 1243 -292 N ATOM 1075 CA LEU A 163 -11.582 -0.014 46.283 1.00 84.68 C ANISOU 1075 CA LEU A 163 13028 10161 8987 82 1425 -310 C ATOM 1076 C LEU A 163 -10.516 -0.641 47.178 1.00 88.55 C ANISOU 1076 C LEU A 163 13738 10468 9440 72 1440 -205 C ATOM 1077 O LEU A 163 -10.755 -0.795 48.375 1.00 91.06 O ANISOU 1077 O LEU A 163 14172 10745 9683 87 1534 -187 O ATOM 1078 CB LEU A 163 -12.396 -1.119 45.579 1.00 85.99 C ANISOU 1078 CB LEU A 163 13047 10418 9207 -84 1570 -395 C ATOM 1079 CG LEU A 163 -13.918 -0.934 45.423 1.00 92.44 C ANISOU 1079 CG LEU A 163 13659 11452 10013 -114 1668 -528 C ATOM 1080 CD1 LEU A 163 -14.408 0.476 45.839 1.00 92.74 C ANISOU 1080 CD1 LEU A 163 13663 11586 9988 69 1585 -548 C ATOM 1081 CD2 LEU A 163 -14.349 -1.255 44.007 1.00 95.00 C ANISOU 1081 CD2 LEU A 163 13772 11918 10406 -196 1656 -618 C ATOM 1082 N THR A 164 -9.351 -0.996 46.617 1.00 81.72 N ANISOU 1082 N THR A 164 12928 9505 8616 61 1349 -137 N ATOM 1083 CA THR A 164 -8.269 -1.622 47.381 1.00 80.62 C ANISOU 1083 CA THR A 164 12985 9216 8431 77 1350 -38 C ATOM 1084 C THR A 164 -7.456 -0.556 48.159 1.00 83.11 C ANISOU 1084 C THR A 164 13411 9489 8678 215 1204 14 C ATOM 1085 O THR A 164 -6.699 -0.926 49.064 1.00 83.21 O ANISOU 1085 O THR A 164 13585 9410 8620 256 1206 85 O ATOM 1086 CB THR A 164 -7.364 -2.505 46.483 1.00 83.41 C ANISOU 1086 CB THR A 164 13346 9498 8846 17 1323 6 C ATOM 1087 OG1 THR A 164 -6.530 -1.689 45.662 1.00 82.57 O ANISOU 1087 OG1 THR A 164 13180 9409 8784 78 1136 24 O ATOM 1088 CG2 THR A 164 -8.150 -3.461 45.616 1.00 79.40 C ANISOU 1088 CG2 THR A 164 12726 9036 8408 -130 1456 -63 C ATOM 1089 N SER A 165 -7.601 0.747 47.817 1.00 77.37 N ANISOU 1089 N SER A 165 12609 8827 7962 289 1084 -23 N ATOM 1090 CA SER A 165 -6.876 1.809 48.528 1.00 76.61 C ANISOU 1090 CA SER A 165 12622 8686 7800 397 957 8 C ATOM 1091 C SER A 165 -7.717 2.447 49.616 1.00 82.32 C ANISOU 1091 C SER A 165 13396 9441 8440 466 1015 -28 C ATOM 1092 O SER A 165 -7.195 2.698 50.696 1.00 81.94 O ANISOU 1092 O SER A 165 13492 9335 8307 525 986 6 O ATOM 1093 CB SER A 165 -6.391 2.908 47.580 1.00 78.00 C ANISOU 1093 CB SER A 165 12734 8878 8025 438 799 -5 C ATOM 1094 OG SER A 165 -5.534 2.390 46.577 1.00 81.37 O ANISOU 1094 OG SER A 165 13115 9279 8523 381 738 29 O ATOM 1095 N PHE A 166 -8.987 2.768 49.327 1.00 80.52 N ANISOU 1095 N PHE A 166 13044 9319 8229 469 1088 -103 N ATOM 1096 CA PHE A 166 -9.850 3.449 50.295 1.00 81.68 C ANISOU 1096 CA PHE A 166 13225 9513 8295 548 1144 -145 C ATOM 1097 C PHE A 166 -10.554 2.503 51.262 1.00 86.01 C ANISOU 1097 C PHE A 166 13818 10071 8791 491 1329 -150 C ATOM 1098 O PHE A 166 -10.777 2.910 52.398 1.00 87.02 O ANISOU 1098 O PHE A 166 14051 10187 8828 561 1362 -149 O ATOM 1099 CB PHE A 166 -10.898 4.318 49.581 1.00 84.04 C ANISOU 1099 CB PHE A 166 13370 9944 8618 609 1134 -226 C ATOM 1100 CG PHE A 166 -10.440 5.714 49.229 1.00 85.12 C ANISOU 1100 CG PHE A 166 13548 10049 8745 726 979 -223 C ATOM 1101 CD1 PHE A 166 -9.599 5.937 48.144 1.00 87.83 C ANISOU 1101 CD1 PHE A 166 13866 10349 9156 709 858 -194 C ATOM 1102 CD2 PHE A 166 -10.905 6.813 49.938 1.00 87.57 C ANISOU 1102 CD2 PHE A 166 13927 10370 8977 852 968 -254 C ATOM 1103 CE1 PHE A 166 -9.200 7.233 47.801 1.00 88.13 C ANISOU 1103 CE1 PHE A 166 13961 10343 9181 803 736 -194 C ATOM 1104 CE2 PHE A 166 -10.512 8.109 49.589 1.00 90.24 C ANISOU 1104 CE2 PHE A 166 14328 10657 9301 954 844 -255 C ATOM 1105 CZ PHE A 166 -9.657 8.308 48.528 1.00 87.29 C ANISOU 1105 CZ PHE A 166 13941 10230 8994 923 733 -224 C ATOM 1106 N LEU A 167 -10.926 1.276 50.851 1.00 82.51 N ANISOU 1106 N LEU A 167 13308 9646 8398 360 1459 -160 N ATOM 1107 CA LEU A 167 -11.628 0.391 51.792 1.00 84.28 C ANISOU 1107 CA LEU A 167 13594 9865 8565 291 1659 -168 C ATOM 1108 C LEU A 167 -10.726 -0.054 52.972 1.00 87.94 C ANISOU 1108 C LEU A 167 14295 10181 8936 331 1673 -70 C ATOM 1109 O LEU A 167 -11.145 0.201 54.097 1.00 87.46 O ANISOU 1109 O LEU A 167 14325 10124 8782 386 1742 -72 O ATOM 1110 CB LEU A 167 -12.299 -0.827 51.129 1.00 85.26 C ANISOU 1110 CB LEU A 167 13609 10031 8755 120 1821 -216 C ATOM 1111 CG LEU A 167 -13.737 -0.632 50.618 1.00 90.90 C ANISOU 1111 CG LEU A 167 14097 10941 9502 64 1912 -344 C ATOM 1112 CD1 LEU A 167 -14.234 -1.880 49.938 1.00 91.61 C ANISOU 1112 CD1 LEU A 167 14089 11064 9656 -130 2064 -400 C ATOM 1113 CD2 LEU A 167 -14.703 -0.274 51.758 1.00 94.43 C ANISOU 1113 CD2 LEU A 167 14560 11460 9858 107 2030 -387 C ATOM 1114 N PRO A 168 -9.487 -0.614 52.802 1.00 83.99 N ANISOU 1114 N PRO A 168 13899 9570 8445 330 1598 14 N ATOM 1115 CA PRO A 168 -8.693 -0.995 53.993 1.00 83.73 C ANISOU 1115 CA PRO A 168 14086 9429 8299 401 1608 101 C ATOM 1116 C PRO A 168 -8.346 0.170 54.921 1.00 86.33 C ANISOU 1116 C PRO A 168 14500 9767 8536 537 1488 105 C ATOM 1117 O PRO A 168 -8.074 -0.075 56.102 1.00 87.38 O ANISOU 1117 O PRO A 168 14802 9847 8551 600 1531 154 O ATOM 1118 CB PRO A 168 -7.420 -1.602 53.398 1.00 84.45 C ANISOU 1118 CB PRO A 168 14222 9440 8424 398 1514 173 C ATOM 1119 CG PRO A 168 -7.798 -2.024 52.040 1.00 87.95 C ANISOU 1119 CG PRO A 168 14501 9920 8995 281 1544 128 C ATOM 1120 CD PRO A 168 -8.797 -1.027 51.559 1.00 83.55 C ANISOU 1120 CD PRO A 168 13767 9491 8488 273 1518 31 C ATOM 1121 N ILE A 169 -8.393 1.429 54.425 1.00 80.79 N ANISOU 1121 N ILE A 169 13695 9128 7874 585 1348 51 N ATOM 1122 CA ILE A 169 -8.055 2.581 55.267 1.00 79.96 C ANISOU 1122 CA ILE A 169 13683 9019 7681 700 1239 42 C ATOM 1123 C ILE A 169 -9.319 3.145 55.973 1.00 87.50 C ANISOU 1123 C ILE A 169 14627 10040 8580 743 1345 -20 C ATOM 1124 O ILE A 169 -9.258 3.349 57.188 1.00 88.28 O ANISOU 1124 O ILE A 169 14868 10113 8562 814 1367 -6 O ATOM 1125 CB ILE A 169 -7.228 3.657 54.509 1.00 80.30 C ANISOU 1125 CB ILE A 169 13678 9059 7775 734 1038 26 C ATOM 1126 CG1 ILE A 169 -5.798 3.101 54.267 1.00 79.02 C ANISOU 1126 CG1 ILE A 169 13566 8838 7620 716 935 93 C ATOM 1127 CG2 ILE A 169 -7.167 4.999 55.291 1.00 80.08 C ANISOU 1127 CG2 ILE A 169 13736 9028 7661 834 952 -13 C ATOM 1128 CD1 ILE A 169 -5.065 3.679 53.175 1.00 85.59 C ANISOU 1128 CD1 ILE A 169 14313 9671 8536 693 789 83 C ATOM 1129 N GLN A 170 -10.448 3.353 55.257 1.00 85.41 N ANISOU 1129 N GLN A 170 14195 9874 8384 709 1412 -92 N ATOM 1130 CA GLN A 170 -11.671 3.888 55.884 1.00 86.66 C ANISOU 1130 CA GLN A 170 14322 10120 8485 762 1514 -158 C ATOM 1131 C GLN A 170 -12.275 2.889 56.877 1.00 93.03 C ANISOU 1131 C GLN A 170 15203 10924 9222 706 1717 -144 C ATOM 1132 O GLN A 170 -12.876 3.308 57.864 1.00 95.20 O ANISOU 1132 O GLN A 170 15538 11230 9403 774 1787 -170 O ATOM 1133 CB GLN A 170 -12.732 4.304 54.844 1.00 88.25 C ANISOU 1133 CB GLN A 170 14306 10460 8765 755 1534 -244 C ATOM 1134 CG GLN A 170 -12.288 5.315 53.763 1.00100.96 C ANISOU 1134 CG GLN A 170 15848 12075 10438 819 1356 -258 C ATOM 1135 CD GLN A 170 -11.575 6.552 54.253 1.00112.20 C ANISOU 1135 CD GLN A 170 17417 13415 11800 939 1215 -243 C ATOM 1136 OE1 GLN A 170 -12.099 7.329 55.057 1.00109.76 O ANISOU 1136 OE1 GLN A 170 17172 13126 11407 1041 1238 -278 O ATOM 1137 NE2 GLN A 170 -10.388 6.793 53.714 1.00 97.12 N ANISOU 1137 NE2 GLN A 170 15554 11416 9930 923 1069 -200 N ATOM 1138 N MET A 171 -12.085 1.581 56.629 1.00 90.02 N ANISOU 1138 N MET A 171 14836 10492 8877 586 1818 -102 N ATOM 1139 CA MET A 171 -12.544 0.477 57.473 1.00 91.99 C ANISOU 1139 CA MET A 171 15188 10704 9062 512 2030 -76 C ATOM 1140 C MET A 171 -11.562 0.215 58.631 1.00 93.89 C ANISOU 1140 C MET A 171 15679 10817 9179 597 2006 23 C ATOM 1141 O MET A 171 -11.838 -0.623 59.497 1.00 93.70 O ANISOU 1141 O MET A 171 15790 10740 9072 568 2179 61 O ATOM 1142 CB MET A 171 -12.709 -0.810 56.633 1.00 95.73 C ANISOU 1142 CB MET A 171 15593 11155 9623 345 2154 -75 C ATOM 1143 CG MET A 171 -13.859 -0.787 55.635 1.00101.40 C ANISOU 1143 CG MET A 171 16060 12027 10441 239 2224 -189 C ATOM 1144 SD MET A 171 -15.440 -0.288 56.365 1.00109.62 S ANISOU 1144 SD MET A 171 16998 13233 11418 248 2381 -294 S ATOM 1145 CE MET A 171 -15.896 -1.815 57.259 1.00108.43 C ANISOU 1145 CE MET A 171 16994 12998 11205 84 2681 -269 C ATOM 1146 N HIS A 172 -10.398 0.911 58.612 1.00 88.82 N ANISOU 1146 N HIS A 172 15096 10133 8520 699 1794 60 N ATOM 1147 CA HIS A 172 -9.297 0.849 59.590 1.00 88.45 C ANISOU 1147 CA HIS A 172 15252 10003 8351 801 1715 139 C ATOM 1148 C HIS A 172 -8.646 -0.564 59.687 1.00 91.26 C ANISOU 1148 C HIS A 172 15735 10260 8679 767 1797 234 C ATOM 1149 O HIS A 172 -7.968 -0.855 60.674 1.00 90.59 O ANISOU 1149 O HIS A 172 15837 10120 8463 863 1789 303 O ATOM 1150 CB HIS A 172 -9.741 1.349 60.985 1.00 90.44 C ANISOU 1150 CB HIS A 172 15633 10271 8460 895 1773 127 C ATOM 1151 CG HIS A 172 -10.299 2.742 61.002 1.00 93.74 C ANISOU 1151 CG HIS A 172 15965 10768 8884 956 1695 39 C ATOM 1152 ND1 HIS A 172 -11.133 3.163 62.016 1.00 96.53 N ANISOU 1152 ND1 HIS A 172 16377 11161 9138 1015 1795 3 N ATOM 1153 CD2 HIS A 172 -10.141 3.758 60.118 1.00 94.67 C ANISOU 1153 CD2 HIS A 172 15960 10922 9087 971 1542 -14 C ATOM 1154 CE1 HIS A 172 -11.450 4.411 61.725 1.00 95.79 C ANISOU 1154 CE1 HIS A 172 16199 11126 9072 1074 1697 -72 C ATOM 1155 NE2 HIS A 172 -10.878 4.813 60.588 1.00 94.82 N ANISOU 1155 NE2 HIS A 172 15973 10997 9058 1051 1546 -82 N ATOM 1156 N TRP A 173 -8.763 -1.388 58.622 1.00 87.28 N ANISOU 1156 N TRP A 173 15136 9735 8290 648 1860 236 N ATOM 1157 CA TRP A 173 -8.157 -2.717 58.529 1.00 87.38 C ANISOU 1157 CA TRP A 173 15270 9641 8288 616 1941 322 C ATOM 1158 C TRP A 173 -6.633 -2.650 58.561 1.00 87.02 C ANISOU 1158 C TRP A 173 15307 9559 8197 734 1749 394 C ATOM 1159 O TRP A 173 -5.985 -3.642 58.860 1.00 88.07 O ANISOU 1159 O TRP A 173 15594 9607 8262 777 1801 480 O ATOM 1160 CB TRP A 173 -8.582 -3.408 57.223 1.00 87.30 C ANISOU 1160 CB TRP A 173 15114 9631 8425 459 2020 286 C ATOM 1161 CG TRP A 173 -10.054 -3.670 57.049 1.00 90.83 C ANISOU 1161 CG TRP A 173 15452 10137 8922 316 2221 201 C ATOM 1162 CD1 TRP A 173 -11.013 -3.683 58.018 1.00 95.33 C ANISOU 1162 CD1 TRP A 173 16079 10731 9411 301 2388 174 C ATOM 1163 CD2 TRP A 173 -10.713 -4.045 55.831 1.00 91.29 C ANISOU 1163 CD2 TRP A 173 15321 10252 9114 159 2285 125 C ATOM 1164 NE1 TRP A 173 -12.234 -4.007 57.474 1.00 95.81 N ANISOU 1164 NE1 TRP A 173 15981 10873 9551 140 2551 79 N ATOM 1165 CE2 TRP A 173 -12.080 -4.238 56.136 1.00 96.68 C ANISOU 1165 CE2 TRP A 173 15937 11007 9790 50 2488 44 C ATOM 1166 CE3 TRP A 173 -10.282 -4.225 54.504 1.00 92.03 C ANISOU 1166 CE3 TRP A 173 15287 10354 9327 100 2190 111 C ATOM 1167 CZ2 TRP A 173 -13.024 -4.581 55.164 1.00 96.73 C ANISOU 1167 CZ2 TRP A 173 15740 11111 9901 -117 2589 -60 C ATOM 1168 CZ3 TRP A 173 -11.219 -4.574 53.539 1.00 94.13 C ANISOU 1168 CZ3 TRP A 173 15367 10703 9696 -59 2290 14 C ATOM 1169 CH2 TRP A 173 -12.571 -4.753 53.873 1.00 96.24 C ANISOU 1169 CH2 TRP A 173 15560 11056 9950 -167 2485 -74 C ATOM 1170 N TYR A 174 -6.062 -1.490 58.213 1.00 80.40 N ANISOU 1170 N TYR A 174 14366 8789 7393 785 1534 353 N ATOM 1171 CA TYR A 174 -4.619 -1.244 58.131 1.00 77.73 C ANISOU 1171 CA TYR A 174 14057 8454 7024 873 1335 393 C ATOM 1172 C TYR A 174 -3.971 -1.082 59.483 1.00 80.90 C ANISOU 1172 C TYR A 174 14632 8857 7248 1016 1282 433 C ATOM 1173 O TYR A 174 -2.764 -1.268 59.597 1.00 79.39 O ANISOU 1173 O TYR A 174 14494 8675 6997 1100 1159 478 O ATOM 1174 CB TYR A 174 -4.346 0.028 57.292 1.00 76.75 C ANISOU 1174 CB TYR A 174 13767 8399 6997 851 1147 320 C ATOM 1175 CG TYR A 174 -4.584 1.344 58.009 1.00 79.55 C ANISOU 1175 CG TYR A 174 14137 8801 7288 912 1069 257 C ATOM 1176 CD1 TYR A 174 -5.858 1.906 58.080 1.00 81.63 C ANISOU 1176 CD1 TYR A 174 14343 9095 7577 885 1161 193 C ATOM 1177 CD2 TYR A 174 -3.532 2.040 58.602 1.00 80.32 C ANISOU 1177 CD2 TYR A 174 14303 8921 7295 996 904 252 C ATOM 1178 CE1 TYR A 174 -6.073 3.134 58.710 1.00 81.16 C ANISOU 1178 CE1 TYR A 174 14313 9068 7456 952 1094 135 C ATOM 1179 CE2 TYR A 174 -3.737 3.264 59.238 1.00 80.62 C ANISOU 1179 CE2 TYR A 174 14370 8988 7273 1041 839 185 C ATOM 1180 CZ TYR A 174 -5.007 3.814 59.285 1.00 87.59 C ANISOU 1180 CZ TYR A 174 15215 9881 8185 1025 935 131 C ATOM 1181 OH TYR A 174 -5.198 5.024 59.936 1.00 89.55 O ANISOU 1181 OH TYR A 174 15513 10147 8366 1083 877 66 O ATOM 1182 N ARG A 175 -4.768 -0.683 60.488 1.00 78.20 N ANISOU 1182 N ARG A 175 14366 8527 6819 1049 1368 407 N ATOM 1183 CA ARG A 175 -4.328 -0.257 61.805 1.00 79.02 C ANISOU 1183 CA ARG A 175 14618 8654 6751 1183 1309 419 C ATOM 1184 C ARG A 175 -3.527 -1.269 62.611 1.00 85.21 C ANISOU 1184 C ARG A 175 15594 9397 7383 1301 1340 520 C ATOM 1185 O ARG A 175 -3.889 -2.440 62.752 1.00 85.46 O ANISOU 1185 O ARG A 175 15738 9346 7388 1289 1525 591 O ATOM 1186 CB ARG A 175 -5.501 0.242 62.644 1.00 77.86 C ANISOU 1186 CB ARG A 175 14514 8521 6547 1186 1430 372 C ATOM 1187 CG ARG A 175 -5.879 1.641 62.198 1.00 79.37 C ANISOU 1187 CG ARG A 175 14561 8777 6821 1155 1319 269 C ATOM 1188 CD ARG A 175 -6.854 2.319 63.103 1.00 85.19 C ANISOU 1188 CD ARG A 175 15345 9542 7480 1195 1402 217 C ATOM 1189 NE ARG A 175 -7.035 3.712 62.697 1.00 88.89 N ANISOU 1189 NE ARG A 175 15708 10056 8008 1196 1278 125 N ATOM 1190 CZ ARG A 175 -7.790 4.586 63.351 1.00104.25 C ANISOU 1190 CZ ARG A 175 17682 12033 9895 1248 1311 63 C ATOM 1191 NH1 ARG A 175 -8.450 4.217 64.441 1.00 88.48 N ANISOU 1191 NH1 ARG A 175 15798 10038 7783 1292 1462 79 N ATOM 1192 NH2 ARG A 175 -7.893 5.833 62.921 1.00100.72 N ANISOU 1192 NH2 ARG A 175 17163 11608 9498 1260 1202 -15 N ATOM 1193 N ALA A 176 -2.410 -0.748 63.153 1.00 83.28 N ANISOU 1193 N ALA A 176 15392 9221 7029 1419 1153 516 N ATOM 1194 CA ALA A 176 -1.485 -1.428 64.049 1.00 84.62 C ANISOU 1194 CA ALA A 176 15734 9401 7018 1580 1126 597 C ATOM 1195 C ALA A 176 -2.076 -1.390 65.450 1.00 91.14 C ANISOU 1195 C ALA A 176 16738 10217 7674 1670 1237 611 C ATOM 1196 O ALA A 176 -2.916 -0.524 65.753 1.00 90.26 O ANISOU 1196 O ALA A 176 16589 10124 7581 1619 1264 537 O ATOM 1197 CB ALA A 176 -0.120 -0.752 64.008 1.00 85.01 C ANISOU 1197 CB ALA A 176 15713 9566 7022 1652 872 557 C ATOM 1198 N THR A 177 -1.667 -2.342 66.295 1.00 90.10 N ANISOU 1198 N THR A 177 16809 10054 7370 1813 1310 710 N ATOM 1199 CA THR A 177 -2.206 -2.467 67.652 1.00 91.28 C ANISOU 1199 CA THR A 177 17158 10184 7341 1911 1439 742 C ATOM 1200 C THR A 177 -1.204 -2.065 68.746 1.00 94.14 C ANISOU 1200 C THR A 177 17623 10659 7488 2105 1271 741 C ATOM 1201 O THR A 177 -1.559 -2.135 69.927 1.00 95.55 O ANISOU 1201 O THR A 177 17976 10832 7496 2206 1362 767 O ATOM 1202 CB THR A 177 -2.727 -3.880 67.867 1.00105.96 C ANISOU 1202 CB THR A 177 19206 11903 9150 1921 1698 856 C ATOM 1203 OG1 THR A 177 -1.781 -4.804 67.318 1.00109.96 O ANISOU 1203 OG1 THR A 177 19750 12376 9654 1988 1661 937 O ATOM 1204 CG2 THR A 177 -4.100 -4.087 67.236 1.00105.28 C ANISOU 1204 CG2 THR A 177 19040 11731 9230 1715 1909 823 C ATOM 1205 N HIS A 178 0.020 -1.618 68.382 1.00 88.51 N ANISOU 1205 N HIS A 178 16795 10061 6775 2151 1032 700 N ATOM 1206 CA HIS A 178 0.951 -1.172 69.411 1.00 88.98 C ANISOU 1206 CA HIS A 178 16923 10258 6626 2318 865 673 C ATOM 1207 C HIS A 178 0.556 0.257 69.837 1.00 90.98 C ANISOU 1207 C HIS A 178 17110 10575 6885 2250 778 542 C ATOM 1208 O HIS A 178 -0.091 0.970 69.069 1.00 88.02 O ANISOU 1208 O HIS A 178 16593 10158 6693 2085 786 469 O ATOM 1209 CB HIS A 178 2.419 -1.328 69.020 1.00 89.92 C ANISOU 1209 CB HIS A 178 16956 10502 6709 2406 659 674 C ATOM 1210 CG HIS A 178 2.829 -0.575 67.811 1.00 91.97 C ANISOU 1210 CG HIS A 178 16972 10807 7166 2245 507 582 C ATOM 1211 ND1 HIS A 178 3.166 0.763 67.881 1.00 94.06 N ANISOU 1211 ND1 HIS A 178 17116 11178 7445 2176 330 447 N ATOM 1212 CD2 HIS A 178 3.012 -1.011 66.545 1.00 92.17 C ANISOU 1212 CD2 HIS A 178 16872 10783 7364 2151 510 609 C ATOM 1213 CE1 HIS A 178 3.527 1.106 66.651 1.00 91.69 C ANISOU 1213 CE1 HIS A 178 16627 10885 7327 2039 240 401 C ATOM 1214 NE2 HIS A 178 3.445 0.070 65.812 1.00 90.94 N ANISOU 1214 NE2 HIS A 178 16516 10704 7332 2024 339 496 N ATOM 1215 N AGLN A 179 0.883 0.629 71.084 0.50 89.91 N ANISOU 1215 N AGLN A 179 17094 10532 6536 2389 710 515 N ATOM 1216 N BGLN A 179 0.882 0.630 71.089 0.50 89.51 N ANISOU 1216 N BGLN A 179 17044 10482 6485 2390 710 514 N ATOM 1217 CA AGLN A 179 0.501 1.899 71.702 0.50 90.17 C ANISOU 1217 CA AGLN A 179 17116 10613 6531 2352 649 395 C ATOM 1218 CA BGLN A 179 0.513 1.906 71.705 0.50 89.56 C ANISOU 1218 CA BGLN A 179 17038 10537 6453 2353 647 394 C ATOM 1219 C AGLN A 179 1.075 3.114 70.973 0.50 93.05 C ANISOU 1219 C AGLN A 179 17285 11052 7019 2225 443 259 C ATOM 1220 C BGLN A 179 1.061 3.104 70.934 0.50 92.65 C ANISOU 1220 C BGLN A 179 17230 10997 6975 2221 445 260 C ATOM 1221 O AGLN A 179 0.372 4.117 70.882 0.50 92.61 O ANISOU 1221 O AGLN A 179 17185 10958 7045 2122 454 170 O ATOM 1222 O BGLN A 179 0.339 4.088 70.792 0.50 92.04 O ANISOU 1222 O BGLN A 179 17104 10879 6988 2113 461 173 O ATOM 1223 CB AGLN A 179 0.877 1.919 73.192 0.50 93.51 C ANISOU 1223 CB AGLN A 179 17718 11133 6678 2542 611 396 C ATOM 1224 CB BGLN A 179 0.964 1.960 73.175 0.50 92.64 C ANISOU 1224 CB BGLN A 179 17600 11034 6568 2543 594 390 C ATOM 1225 CG AGLN A 179 -0.309 1.637 74.146 0.50102.67 C ANISOU 1225 CG AGLN A 179 19069 12201 7740 2594 836 450 C ATOM 1226 CG BGLN A 179 0.354 3.106 73.991 0.50 94.31 C ANISOU 1226 CG BGLN A 179 17854 11265 6714 2521 586 281 C ATOM 1227 CD AGLN A 179 -0.892 0.224 74.162 0.50110.34 C ANISOU 1227 CD AGLN A 179 20188 13040 8696 2637 1080 605 C ATOM 1228 CD BGLN A 179 -1.065 2.879 74.469 0.50 93.99 C ANISOU 1228 CD BGLN A 179 17938 11104 6672 2509 832 330 C ATOM 1229 OE1AGLN A 179 -2.015 0.008 74.645 0.50100.99 O ANISOU 1229 OE1AGLN A 179 19117 11763 7492 2614 1294 639 O ATOM 1230 OE1BGLN A 179 -1.367 1.920 75.189 0.50 86.54 O ANISOU 1230 OE1BGLN A 179 17175 10117 5591 2627 990 440 O ATOM 1231 NE2AGLN A 179 -0.149 -0.780 73.687 0.50 99.26 N ANISOU 1231 NE2AGLN A 179 18801 11624 7289 2703 1067 700 N ATOM 1232 NE2BGLN A 179 -1.949 3.816 74.160 0.50 74.85 N ANISOU 1232 NE2BGLN A 179 15430 8632 4378 2380 869 242 N ATOM 1233 N GLU A 180 2.304 3.018 70.418 1.00 88.82 N ANISOU 1233 N GLU A 180 16636 10613 6497 2232 270 244 N ATOM 1234 CA GLU A 180 2.937 4.111 69.654 1.00 87.85 C ANISOU 1234 CA GLU A 180 16332 10555 6492 2093 87 117 C ATOM 1235 C GLU A 180 2.005 4.496 68.451 1.00 88.55 C ANISOU 1235 C GLU A 180 16307 10505 6833 1911 177 103 C ATOM 1236 O GLU A 180 1.677 5.673 68.293 1.00 86.92 O ANISOU 1236 O GLU A 180 16053 10279 6694 1810 133 -2 O ATOM 1237 CB GLU A 180 4.352 3.692 69.218 1.00 89.81 C ANISOU 1237 CB GLU A 180 16476 10937 6713 2136 -77 122 C ATOM 1238 CG GLU A 180 5.186 4.769 68.535 1.00103.32 C ANISOU 1238 CG GLU A 180 18007 12737 8515 1992 -268 -15 C ATOM 1239 CD GLU A 180 6.328 4.281 67.652 1.00133.57 C ANISOU 1239 CD GLU A 180 21686 16663 12400 1982 -383 2 C ATOM 1240 OE1 GLU A 180 6.665 5.002 66.685 1.00137.19 O ANISOU 1240 OE1 GLU A 180 21991 17124 13012 1816 -469 -79 O ATOM 1241 OE2 GLU A 180 6.892 3.193 67.921 1.00127.09 O ANISOU 1241 OE2 GLU A 180 20910 15914 11464 2147 -383 96 O ATOM 1242 N ALA A 181 1.463 3.476 67.733 1.00 84.02 N ANISOU 1242 N ALA A 181 15719 9832 6374 1888 325 212 N ATOM 1243 CA ALA A 181 0.475 3.618 66.657 1.00 81.92 C ANISOU 1243 CA ALA A 181 15351 9453 6322 1741 432 210 C ATOM 1244 C ALA A 181 -0.901 4.118 67.181 1.00 86.59 C ANISOU 1244 C ALA A 181 16010 9977 6912 1721 578 180 C ATOM 1245 O ALA A 181 -1.452 5.078 66.648 1.00 84.71 O ANISOU 1245 O ALA A 181 15684 9711 6790 1626 564 102 O ATOM 1246 CB ALA A 181 0.291 2.289 65.958 1.00 81.76 C ANISOU 1246 CB ALA A 181 15321 9361 6384 1733 560 325 C ATOM 1247 N ILE A 182 -1.446 3.452 68.218 1.00 85.93 N ANISOU 1247 N ILE A 182 16089 9872 6690 1822 725 245 N ATOM 1248 CA ILE A 182 -2.759 3.714 68.812 1.00 85.96 C ANISOU 1248 CA ILE A 182 16164 9825 6672 1818 891 229 C ATOM 1249 C ILE A 182 -2.850 5.153 69.295 1.00 91.31 C ANISOU 1249 C ILE A 182 16843 10545 7305 1819 787 107 C ATOM 1250 O ILE A 182 -3.843 5.814 68.976 1.00 91.20 O ANISOU 1250 O ILE A 182 16773 10492 7388 1753 859 53 O ATOM 1251 CB ILE A 182 -3.091 2.657 69.897 1.00 90.08 C ANISOU 1251 CB ILE A 182 16883 10320 7025 1933 1061 328 C ATOM 1252 CG1 ILE A 182 -3.763 1.439 69.216 1.00 88.79 C ANISOU 1252 CG1 ILE A 182 16708 10057 6971 1859 1264 422 C ATOM 1253 CG2 ILE A 182 -3.962 3.226 71.047 1.00 92.81 C ANISOU 1253 CG2 ILE A 182 17346 10671 7248 1988 1156 286 C ATOM 1254 CD1 ILE A 182 -3.846 0.196 70.007 1.00 94.40 C ANISOU 1254 CD1 ILE A 182 17622 10711 7536 1957 1433 539 C ATOM 1255 N ASN A 183 -1.795 5.664 69.974 1.00 89.15 N ANISOU 1255 N ASN A 183 16624 10358 6891 1890 614 53 N ATOM 1256 CA ASN A 183 -1.725 7.057 70.435 1.00 89.03 C ANISOU 1256 CA ASN A 183 16626 10377 6824 1878 504 -77 C ATOM 1257 C ASN A 183 -1.757 7.981 69.250 1.00 92.11 C ANISOU 1257 C ASN A 183 16868 10725 7403 1740 429 -154 C ATOM 1258 O ASN A 183 -2.462 8.976 69.290 1.00 92.81 O ANISOU 1258 O ASN A 183 16970 10770 7523 1711 454 -231 O ATOM 1259 CB ASN A 183 -0.466 7.334 71.268 1.00 87.78 C ANISOU 1259 CB ASN A 183 16529 10339 6484 1956 324 -133 C ATOM 1260 CG ASN A 183 -0.441 6.683 72.611 1.00103.25 C ANISOU 1260 CG ASN A 183 18661 12352 8216 2121 382 -77 C ATOM 1261 OD1 ASN A 183 -1.475 6.413 73.223 1.00103.42 O ANISOU 1261 OD1 ASN A 183 18794 12313 8186 2174 557 -30 O ATOM 1262 ND2 ASN A 183 0.754 6.430 73.105 1.00 93.35 N ANISOU 1262 ND2 ASN A 183 17431 11226 6811 2213 236 -83 N ATOM 1263 N CYS A 184 -1.011 7.637 68.190 1.00 87.94 N ANISOU 1263 N CYS A 184 16212 10207 6994 1667 344 -129 N ATOM 1264 CA CYS A 184 -0.953 8.408 66.967 1.00 86.73 C ANISOU 1264 CA CYS A 184 15923 10011 7018 1538 276 -187 C ATOM 1265 C CYS A 184 -2.333 8.465 66.294 1.00 90.12 C ANISOU 1265 C CYS A 184 16300 10353 7589 1495 431 -166 C ATOM 1266 O CYS A 184 -2.711 9.546 65.871 1.00 89.03 O ANISOU 1266 O CYS A 184 16133 10173 7521 1447 407 -243 O ATOM 1267 CB CYS A 184 0.109 7.858 66.021 1.00 86.24 C ANISOU 1267 CB CYS A 184 15739 9987 7040 1481 172 -151 C ATOM 1268 SG CYS A 184 0.254 8.771 64.466 1.00 88.43 S ANISOU 1268 SG CYS A 184 15861 10210 7528 1321 93 -214 S ATOM 1269 N TYR A 185 -3.091 7.339 66.214 1.00 87.10 N ANISOU 1269 N TYR A 185 15911 9947 7237 1515 596 -70 N ATOM 1270 CA TYR A 185 -4.435 7.344 65.596 1.00 85.90 C ANISOU 1270 CA TYR A 185 15682 9747 7208 1470 747 -65 C ATOM 1271 C TYR A 185 -5.389 8.283 66.353 1.00 89.27 C ANISOU 1271 C TYR A 185 16184 10169 7566 1525 812 -136 C ATOM 1272 O TYR A 185 -6.189 8.973 65.729 1.00 88.60 O ANISOU 1272 O TYR A 185 16022 10064 7578 1497 846 -185 O ATOM 1273 CB TYR A 185 -5.064 5.929 65.507 1.00 86.39 C ANISOU 1273 CB TYR A 185 15736 9792 7296 1461 928 34 C ATOM 1274 CG TYR A 185 -4.254 4.893 64.760 1.00 86.03 C ANISOU 1274 CG TYR A 185 15635 9736 7315 1420 894 110 C ATOM 1275 CD1 TYR A 185 -3.699 5.176 63.517 1.00 85.82 C ANISOU 1275 CD1 TYR A 185 15467 9710 7431 1337 777 90 C ATOM 1276 CD2 TYR A 185 -4.092 3.605 65.269 1.00 87.79 C ANISOU 1276 CD2 TYR A 185 15960 9942 7455 1469 997 207 C ATOM 1277 CE1 TYR A 185 -2.950 4.227 62.824 1.00 85.12 C ANISOU 1277 CE1 TYR A 185 15327 9615 7398 1307 749 157 C ATOM 1278 CE2 TYR A 185 -3.347 2.643 64.583 1.00 88.02 C ANISOU 1278 CE2 TYR A 185 15954 9954 7535 1448 973 279 C ATOM 1279 CZ TYR A 185 -2.785 2.959 63.355 1.00 92.91 C ANISOU 1279 CZ TYR A 185 16418 10585 8298 1366 846 251 C ATOM 1280 OH TYR A 185 -2.055 2.029 62.657 1.00 93.03 O ANISOU 1280 OH TYR A 185 16396 10588 8364 1351 824 317 O ATOM 1281 N ALA A 186 -5.283 8.313 67.685 1.00 86.04 N ANISOU 1281 N ALA A 186 15927 9784 6979 1617 825 -143 N ATOM 1282 CA ALA A 186 -6.100 9.161 68.550 1.00 86.73 C ANISOU 1282 CA ALA A 186 16108 9870 6975 1684 887 -210 C ATOM 1283 C ALA A 186 -5.647 10.628 68.514 1.00 91.25 C ANISOU 1283 C ALA A 186 16708 10424 7537 1676 736 -324 C ATOM 1284 O ALA A 186 -6.496 11.507 68.589 1.00 92.54 O ANISOU 1284 O ALA A 186 16893 10560 7707 1706 788 -387 O ATOM 1285 CB ALA A 186 -6.055 8.638 69.977 1.00 88.81 C ANISOU 1285 CB ALA A 186 16536 10165 7041 1787 951 -175 C ATOM 1286 N GLU A 187 -4.324 10.895 68.430 1.00 87.49 N ANISOU 1286 N GLU A 187 16240 9967 7036 1637 559 -357 N ATOM 1287 CA GLU A 187 -3.787 12.251 68.399 1.00 88.11 C ANISOU 1287 CA GLU A 187 16359 10018 7099 1598 424 -475 C ATOM 1288 C GLU A 187 -4.107 12.869 67.068 1.00 92.90 C ANISOU 1288 C GLU A 187 16860 10554 7885 1519 417 -497 C ATOM 1289 O GLU A 187 -3.519 12.505 66.056 1.00 92.62 O ANISOU 1289 O GLU A 187 16707 10520 7966 1436 355 -462 O ATOM 1290 CB GLU A 187 -2.268 12.295 68.688 1.00 90.18 C ANISOU 1290 CB GLU A 187 16639 10347 7278 1560 245 -517 C ATOM 1291 CG GLU A 187 -1.615 13.675 68.561 1.00103.95 C ANISOU 1291 CG GLU A 187 18419 12060 9017 1476 112 -653 C ATOM 1292 CD GLU A 187 -2.235 14.813 69.363 1.00132.74 C ANISOU 1292 CD GLU A 187 22218 15649 12568 1523 148 -753 C ATOM 1293 OE1 GLU A 187 -3.128 15.503 68.818 1.00131.66 O ANISOU 1293 OE1 GLU A 187 22089 15414 12522 1525 226 -771 O ATOM 1294 OE2 GLU A 187 -1.801 15.044 70.516 1.00123.00 O ANISOU 1294 OE2 GLU A 187 21099 14475 11161 1567 95 -819 O ATOM 1295 N GLU A 188 -5.037 13.826 67.082 1.00 91.21 N ANISOU 1295 N GLU A 188 16695 10281 7679 1560 481 -555 N ATOM 1296 CA GLU A 188 -5.528 14.574 65.929 1.00 90.06 C ANISOU 1296 CA GLU A 188 16482 10065 7673 1529 491 -580 C ATOM 1297 C GLU A 188 -4.397 15.147 65.065 1.00 93.33 C ANISOU 1297 C GLU A 188 16869 10432 8162 1412 343 -621 C ATOM 1298 O GLU A 188 -4.573 15.271 63.861 1.00 92.11 O ANISOU 1298 O GLU A 188 16615 10237 8144 1369 345 -599 O ATOM 1299 CB GLU A 188 -6.438 15.708 66.420 1.00 92.54 C ANISOU 1299 CB GLU A 188 16915 10324 7921 1623 555 -657 C ATOM 1300 CG GLU A 188 -7.453 16.177 65.395 1.00106.88 C ANISOU 1300 CG GLU A 188 18653 12103 9854 1663 630 -654 C ATOM 1301 CD GLU A 188 -8.479 15.172 64.902 1.00134.43 C ANISOU 1301 CD GLU A 188 21976 15674 13426 1691 760 -576 C ATOM 1302 OE1 GLU A 188 -8.783 14.202 65.636 1.00133.21 O ANISOU 1302 OE1 GLU A 188 21810 15590 13215 1708 847 -528 O ATOM 1303 OE2 GLU A 188 -9.016 15.388 63.791 1.00127.85 O ANISOU 1303 OE2 GLU A 188 21035 14836 12708 1697 782 -568 O ATOM 1304 N THR A 189 -3.249 15.492 65.681 1.00 91.09 N ANISOU 1304 N THR A 189 16666 10162 7781 1359 220 -687 N ATOM 1305 CA THR A 189 -2.085 16.083 65.017 1.00 90.15 C ANISOU 1305 CA THR A 189 16527 10013 7712 1227 84 -747 C ATOM 1306 C THR A 189 -1.053 15.031 64.618 1.00 93.03 C ANISOU 1306 C THR A 189 16758 10474 8116 1158 1 -686 C ATOM 1307 O THR A 189 0.047 15.382 64.193 1.00 94.70 O ANISOU 1307 O THR A 189 16935 10696 8350 1044 -118 -739 O ATOM 1308 CB THR A 189 -1.443 17.171 65.889 1.00 97.38 C ANISOU 1308 CB THR A 189 17601 10905 8495 1189 2 -882 C ATOM 1309 OG1 THR A 189 -0.948 16.583 67.090 1.00 97.63 O ANISOU 1309 OG1 THR A 189 17667 11055 8374 1234 -42 -890 O ATOM 1310 CG2 THR A 189 -2.392 18.333 66.184 1.00 95.57 C ANISOU 1310 CG2 THR A 189 17526 10556 8228 1258 83 -950 C ATOM 1311 N CYS A 190 -1.391 13.755 64.731 1.00 87.57 N ANISOU 1311 N CYS A 190 15994 9847 7430 1224 69 -579 N ATOM 1312 CA CYS A 190 -0.466 12.723 64.305 1.00 85.77 C ANISOU 1312 CA CYS A 190 15653 9699 7238 1181 3 -513 C ATOM 1313 C CYS A 190 -0.985 12.081 63.051 1.00 88.69 C ANISOU 1313 C CYS A 190 15888 10034 7776 1152 75 -425 C ATOM 1314 O CYS A 190 -2.144 11.649 63.011 1.00 89.08 O ANISOU 1314 O CYS A 190 15925 10061 7860 1212 212 -370 O ATOM 1315 CB CYS A 190 -0.223 11.684 65.390 1.00 86.39 C ANISOU 1315 CB CYS A 190 15776 9874 7173 1279 17 -457 C ATOM 1316 SG CYS A 190 1.118 10.524 64.997 1.00 89.84 S ANISOU 1316 SG CYS A 190 16100 10420 7615 1259 -86 -390 S ATOM 1317 N CYS A 191 -0.140 12.013 62.023 1.00 82.72 N ANISOU 1317 N CYS A 191 15025 9285 7121 1055 -13 -419 N ATOM 1318 CA CYS A 191 -0.531 11.318 60.811 1.00 81.28 C ANISOU 1318 CA CYS A 191 14711 9081 7091 1025 46 -337 C ATOM 1319 C CYS A 191 0.647 10.498 60.273 1.00 82.99 C ANISOU 1319 C CYS A 191 14824 9364 7343 970 -43 -294 C ATOM 1320 O CYS A 191 1.082 10.671 59.137 1.00 82.79 O ANISOU 1320 O CYS A 191 14701 9320 7433 882 -94 -295 O ATOM 1321 CB CYS A 191 -1.113 12.263 59.764 1.00 81.13 C ANISOU 1321 CB CYS A 191 14662 8974 7192 979 66 -371 C ATOM 1322 SG CYS A 191 -1.910 11.416 58.378 1.00 83.70 S ANISOU 1322 SG CYS A 191 14825 9293 7684 967 159 -282 S ATOM 1323 N ASP A 192 1.158 9.608 61.122 1.00 79.27 N ANISOU 1323 N ASP A 192 14384 8975 6759 1038 -58 -253 N ATOM 1324 CA ASP A 192 2.238 8.685 60.806 1.00 79.39 C ANISOU 1324 CA ASP A 192 14317 9071 6775 1032 -132 -203 C ATOM 1325 C ASP A 192 1.612 7.405 60.348 1.00 82.59 C ANISOU 1325 C ASP A 192 14683 9448 7251 1071 -5 -87 C ATOM 1326 O ASP A 192 0.759 6.848 61.043 1.00 82.19 O ANISOU 1326 O ASP A 192 14714 9373 7141 1148 120 -39 O ATOM 1327 CB ASP A 192 3.166 8.458 62.009 1.00 83.23 C ANISOU 1327 CB ASP A 192 14872 9674 7076 1111 -221 -226 C ATOM 1328 CG ASP A 192 3.950 9.675 62.430 1.00100.94 C ANISOU 1328 CG ASP A 192 17139 11970 9246 1045 -357 -361 C ATOM 1329 OD1 ASP A 192 4.224 10.542 61.559 1.00102.62 O ANISOU 1329 OD1 ASP A 192 17290 12138 9564 915 -410 -427 O ATOM 1330 OD2 ASP A 192 4.302 9.762 63.621 1.00110.51 O ANISOU 1330 OD2 ASP A 192 18436 13265 10287 1119 -406 -405 O ATOM 1331 N PHE A 193 1.975 6.976 59.143 1.00 79.70 N ANISOU 1331 N PHE A 193 14194 9076 7013 1004 -26 -50 N ATOM 1332 CA PHE A 193 1.388 5.795 58.536 1.00 78.97 C ANISOU 1332 CA PHE A 193 14057 8946 7004 1013 97 45 C ATOM 1333 C PHE A 193 1.905 4.519 59.202 1.00 84.18 C ANISOU 1333 C PHE A 193 14781 9649 7555 1114 124 127 C ATOM 1334 O PHE A 193 2.841 3.881 58.716 1.00 85.04 O ANISOU 1334 O PHE A 193 14830 9802 7677 1120 61 165 O ATOM 1335 CB PHE A 193 1.616 5.779 57.015 1.00 79.00 C ANISOU 1335 CB PHE A 193 13917 8930 7172 914 64 52 C ATOM 1336 CG PHE A 193 0.776 4.805 56.220 1.00 80.13 C ANISOU 1336 CG PHE A 193 14001 9024 7422 893 199 120 C ATOM 1337 CD1 PHE A 193 -0.560 4.584 56.541 1.00 83.41 C ANISOU 1337 CD1 PHE A 193 14454 9397 7840 911 352 131 C ATOM 1338 CD2 PHE A 193 1.304 4.148 55.113 1.00 82.07 C ANISOU 1338 CD2 PHE A 193 14143 9274 7766 843 177 161 C ATOM 1339 CE1 PHE A 193 -1.342 3.694 55.791 1.00 83.58 C ANISOU 1339 CE1 PHE A 193 14409 9388 7958 867 481 174 C ATOM 1340 CE2 PHE A 193 0.517 3.277 54.352 1.00 83.75 C ANISOU 1340 CE2 PHE A 193 14302 9443 8076 808 303 208 C ATOM 1341 CZ PHE A 193 -0.805 3.072 54.686 1.00 82.24 C ANISOU 1341 CZ PHE A 193 14144 9216 7886 812 453 208 C ATOM 1342 N PHE A 194 1.299 4.183 60.344 1.00 80.00 N ANISOU 1342 N PHE A 194 14385 9106 6905 1204 223 154 N ATOM 1343 CA PHE A 194 1.541 2.944 61.069 1.00 79.81 C ANISOU 1343 CA PHE A 194 14469 9095 6762 1320 292 246 C ATOM 1344 C PHE A 194 0.593 1.909 60.517 1.00 83.70 C ANISOU 1344 C PHE A 194 14963 9492 7347 1284 478 322 C ATOM 1345 O PHE A 194 -0.607 2.183 60.381 1.00 83.07 O ANISOU 1345 O PHE A 194 14868 9359 7337 1222 594 298 O ATOM 1346 CB PHE A 194 1.319 3.105 62.576 1.00 82.38 C ANISOU 1346 CB PHE A 194 14954 9445 6902 1431 321 238 C ATOM 1347 CG PHE A 194 2.317 3.965 63.304 1.00 84.72 C ANISOU 1347 CG PHE A 194 15267 9853 7069 1477 142 157 C ATOM 1348 CD1 PHE A 194 3.549 3.453 63.692 1.00 88.36 C ANISOU 1348 CD1 PHE A 194 15741 10426 7405 1578 31 180 C ATOM 1349 CD2 PHE A 194 2.003 5.276 63.658 1.00 86.52 C ANISOU 1349 CD2 PHE A 194 15506 10082 7286 1428 92 50 C ATOM 1350 CE1 PHE A 194 4.463 4.243 64.388 1.00 89.94 C ANISOU 1350 CE1 PHE A 194 15939 10757 7476 1609 -136 85 C ATOM 1351 CE2 PHE A 194 2.910 6.056 64.371 1.00 89.90 C ANISOU 1351 CE2 PHE A 194 15957 10613 7588 1451 -64 -40 C ATOM 1352 CZ PHE A 194 4.141 5.539 64.716 1.00 88.81 C ANISOU 1352 CZ PHE A 194 15806 10605 7331 1532 -180 -28 C ATOM 1353 N THR A 195 1.119 0.745 60.135 1.00 80.25 N ANISOU 1353 N THR A 195 14536 9040 6915 1317 509 405 N ATOM 1354 CA THR A 195 0.254 -0.315 59.633 1.00 80.02 C ANISOU 1354 CA THR A 195 14526 8913 6967 1267 700 469 C ATOM 1355 C THR A 195 0.538 -1.610 60.378 1.00 86.38 C ANISOU 1355 C THR A 195 15509 9677 7635 1390 805 573 C ATOM 1356 O THR A 195 1.553 -1.733 61.071 1.00 88.43 O ANISOU 1356 O THR A 195 15846 10005 7749 1529 702 602 O ATOM 1357 CB THR A 195 0.383 -0.507 58.101 1.00 84.79 C ANISOU 1357 CB THR A 195 14968 9498 7751 1153 676 463 C ATOM 1358 OG1 THR A 195 1.654 -1.075 57.785 1.00 90.11 O ANISOU 1358 OG1 THR A 195 15631 10209 8396 1216 575 510 O ATOM 1359 CG2 THR A 195 0.134 0.771 57.307 1.00 74.88 C ANISOU 1359 CG2 THR A 195 13557 8275 6620 1048 577 370 C ATOM 1360 N ASN A 196 -0.385 -2.564 60.275 1.00 82.24 N ANISOU 1360 N ASN A 196 15057 9044 7144 1342 1018 625 N ATOM 1361 CA ASN A 196 -0.161 -3.892 60.806 1.00 82.03 C ANISOU 1361 CA ASN A 196 15224 8942 7001 1446 1150 733 C ATOM 1362 C ASN A 196 0.569 -4.624 59.689 1.00 84.48 C ANISOU 1362 C ASN A 196 15468 9229 7402 1428 1114 773 C ATOM 1363 O ASN A 196 0.409 -4.268 58.516 1.00 85.33 O ANISOU 1363 O ASN A 196 15394 9348 7680 1293 1067 718 O ATOM 1364 CB ASN A 196 -1.453 -4.560 61.250 1.00 81.24 C ANISOU 1364 CB ASN A 196 15251 8729 6887 1385 1410 762 C ATOM 1365 CG ASN A 196 -2.487 -4.764 60.182 1.00 92.64 C ANISOU 1365 CG ASN A 196 16565 10119 8517 1189 1539 717 C ATOM 1366 OD1 ASN A 196 -2.284 -5.498 59.214 1.00 86.43 O ANISOU 1366 OD1 ASN A 196 15735 9279 7825 1125 1574 740 O ATOM 1367 ND2 ASN A 196 -3.668 -4.211 60.403 1.00 83.68 N ANISOU 1367 ND2 ASN A 196 15377 8999 7419 1098 1632 649 N ATOM 1368 N GLN A 197 1.431 -5.553 60.043 1.00 79.51 N ANISOU 1368 N GLN A 197 14980 8581 6648 1581 1118 864 N ATOM 1369 CA GLN A 197 2.285 -6.298 59.122 1.00 78.03 C ANISOU 1369 CA GLN A 197 14755 8382 6512 1609 1076 910 C ATOM 1370 C GLN A 197 1.510 -6.992 57.984 1.00 78.43 C ANISOU 1370 C GLN A 197 14759 8307 6733 1438 1237 911 C ATOM 1371 O GLN A 197 1.979 -6.942 56.860 1.00 76.87 O ANISOU 1371 O GLN A 197 14410 8140 6656 1377 1146 887 O ATOM 1372 CB GLN A 197 3.118 -7.307 59.915 1.00 81.34 C ANISOU 1372 CB GLN A 197 15390 8784 6732 1837 1105 1021 C ATOM 1373 CG GLN A 197 4.116 -6.614 60.842 1.00 99.31 C ANISOU 1373 CG GLN A 197 17661 11233 8841 2011 901 1003 C ATOM 1374 CD GLN A 197 4.647 -7.539 61.889 1.00129.09 C ANISOU 1374 CD GLN A 197 21678 14992 12380 2259 958 1112 C ATOM 1375 OE1 GLN A 197 5.561 -8.343 61.653 1.00128.10 O ANISOU 1375 OE1 GLN A 197 21604 14882 12186 2409 927 1183 O ATOM 1376 NE2 GLN A 197 4.082 -7.436 63.073 1.00126.56 N ANISOU 1376 NE2 GLN A 197 21518 14646 11922 2322 1044 1130 N ATOM 1377 N ALA A 198 0.333 -7.598 58.252 1.00 75.85 N ANISOU 1377 N ALA A 198 14551 7854 6414 1350 1473 927 N ATOM 1378 CA ALA A 198 -0.478 -8.273 57.232 1.00 75.25 C ANISOU 1378 CA ALA A 198 14429 7675 6490 1168 1639 908 C ATOM 1379 C ALA A 198 -1.006 -7.265 56.186 1.00 81.60 C ANISOU 1379 C ALA A 198 14959 8567 7480 997 1542 794 C ATOM 1380 O ALA A 198 -0.988 -7.594 55.002 1.00 82.21 O ANISOU 1380 O ALA A 198 14925 8624 7688 895 1546 773 O ATOM 1381 CB ALA A 198 -1.618 -9.033 57.870 1.00 76.92 C ANISOU 1381 CB ALA A 198 14818 7756 6653 1099 1913 932 C ATOM 1382 N TYR A 199 -1.398 -6.022 56.593 1.00 77.62 N ANISOU 1382 N TYR A 199 14354 8159 6978 982 1447 723 N ATOM 1383 CA TYR A 199 -1.812 -4.996 55.630 1.00 75.03 C ANISOU 1383 CA TYR A 199 13791 7913 6804 858 1345 624 C ATOM 1384 C TYR A 199 -0.599 -4.561 54.805 1.00 81.04 C ANISOU 1384 C TYR A 199 14428 8743 7619 893 1131 619 C ATOM 1385 O TYR A 199 -0.719 -4.489 53.592 1.00 82.18 O ANISOU 1385 O TYR A 199 14423 8898 7904 787 1105 581 O ATOM 1386 CB TYR A 199 -2.499 -3.778 56.279 1.00 74.41 C ANISOU 1386 CB TYR A 199 13663 7906 6702 854 1306 553 C ATOM 1387 CG TYR A 199 -2.635 -2.605 55.328 1.00 74.02 C ANISOU 1387 CG TYR A 199 13402 7939 6782 779 1165 466 C ATOM 1388 CD1 TYR A 199 -1.638 -1.637 55.236 1.00 75.51 C ANISOU 1388 CD1 TYR A 199 13534 8196 6961 837 952 445 C ATOM 1389 CD2 TYR A 199 -3.734 -2.486 54.484 1.00 74.45 C ANISOU 1389 CD2 TYR A 199 13317 8008 6962 650 1250 401 C ATOM 1390 CE1 TYR A 199 -1.713 -0.597 54.307 1.00 74.27 C ANISOU 1390 CE1 TYR A 199 13212 8090 6917 769 839 374 C ATOM 1391 CE2 TYR A 199 -3.818 -1.450 53.539 1.00 74.19 C ANISOU 1391 CE2 TYR A 199 13108 8046 7036 604 1123 332 C ATOM 1392 CZ TYR A 199 -2.802 -0.505 53.457 1.00 77.89 C ANISOU 1392 CZ TYR A 199 13550 8553 7493 666 923 325 C ATOM 1393 OH TYR A 199 -2.845 0.533 52.543 1.00 70.74 O ANISOU 1393 OH TYR A 199 12503 7695 6681 625 811 265 O ATOM 1394 N ALA A 200 0.554 -4.269 55.442 1.00 78.15 N ANISOU 1394 N ALA A 200 14117 8438 7139 1035 980 650 N ATOM 1395 CA ALA A 200 1.776 -3.839 54.745 1.00 76.79 C ANISOU 1395 CA ALA A 200 13822 8352 7004 1062 780 636 C ATOM 1396 C ALA A 200 2.222 -4.850 53.701 1.00 80.77 C ANISOU 1396 C ALA A 200 14298 8808 7582 1041 815 682 C ATOM 1397 O ALA A 200 2.633 -4.433 52.625 1.00 79.12 O ANISOU 1397 O ALA A 200 13929 8648 7487 972 708 644 O ATOM 1398 CB ALA A 200 2.900 -3.590 55.727 1.00 78.42 C ANISOU 1398 CB ALA A 200 14101 8646 7048 1223 642 658 C ATOM 1399 N ILE A 201 2.120 -6.163 53.991 1.00 78.62 N ANISOU 1399 N ILE A 201 14195 8432 7247 1098 976 763 N ATOM 1400 CA ILE A 201 2.477 -7.207 53.032 1.00 78.13 C ANISOU 1400 CA ILE A 201 14137 8303 7248 1081 1035 807 C ATOM 1401 C ILE A 201 1.384 -7.298 51.962 1.00 80.89 C ANISOU 1401 C ILE A 201 14374 8596 7766 879 1147 747 C ATOM 1402 O ILE A 201 1.698 -7.132 50.785 1.00 81.29 O ANISOU 1402 O ILE A 201 14270 8682 7933 810 1065 714 O ATOM 1403 CB ILE A 201 2.733 -8.577 53.709 1.00 83.28 C ANISOU 1403 CB ILE A 201 15039 8842 7763 1217 1184 914 C ATOM 1404 CG1 ILE A 201 3.953 -8.533 54.625 1.00 85.02 C ANISOU 1404 CG1 ILE A 201 15346 9153 7804 1447 1049 971 C ATOM 1405 CG2 ILE A 201 2.921 -9.660 52.664 1.00 85.31 C ANISOU 1405 CG2 ILE A 201 15316 9003 8095 1178 1274 948 C ATOM 1406 CD1 ILE A 201 3.946 -9.636 55.700 1.00 97.73 C ANISOU 1406 CD1 ILE A 201 17246 10653 9233 1611 1210 1078 C ATOM 1407 N ALA A 202 0.112 -7.557 52.365 1.00 76.81 N ANISOU 1407 N ALA A 202 13925 8006 7254 786 1334 726 N ATOM 1408 CA ALA A 202 -1.038 -7.705 51.457 1.00 75.45 C ANISOU 1408 CA ALA A 202 13639 7806 7221 594 1456 654 C ATOM 1409 C ALA A 202 -1.173 -6.542 50.475 1.00 76.87 C ANISOU 1409 C ALA A 202 13573 8103 7531 512 1301 567 C ATOM 1410 O ALA A 202 -1.185 -6.792 49.276 1.00 76.03 O ANISOU 1410 O ALA A 202 13352 7999 7536 422 1295 538 O ATOM 1411 CB ALA A 202 -2.330 -7.872 52.243 1.00 76.90 C ANISOU 1411 CB ALA A 202 13904 7945 7370 519 1650 628 C ATOM 1412 N SER A 203 -1.219 -5.283 50.964 1.00 73.78 N ANISOU 1412 N SER A 203 13118 7800 7115 552 1176 529 N ATOM 1413 CA SER A 203 -1.340 -4.103 50.096 1.00 72.85 C ANISOU 1413 CA SER A 203 12803 7776 7102 493 1038 453 C ATOM 1414 C SER A 203 -0.144 -3.953 49.129 1.00 76.65 C ANISOU 1414 C SER A 203 13192 8291 7638 511 878 468 C ATOM 1415 O SER A 203 -0.373 -3.618 47.975 1.00 75.90 O ANISOU 1415 O SER A 203 12950 8231 7658 426 840 421 O ATOM 1416 CB SER A 203 -1.517 -2.824 50.909 1.00 75.81 C ANISOU 1416 CB SER A 203 13172 8212 7420 546 947 415 C ATOM 1417 OG SER A 203 -0.355 -2.502 51.654 1.00 83.09 O ANISOU 1417 OG SER A 203 14174 9158 8239 664 815 454 O ATOM 1418 N SER A 204 1.108 -4.217 49.585 1.00 73.44 N ANISOU 1418 N SER A 204 12869 7890 7145 627 789 530 N ATOM 1419 CA SER A 204 2.331 -4.113 48.779 1.00 72.54 C ANISOU 1419 CA SER A 204 12668 7828 7067 653 642 542 C ATOM 1420 C SER A 204 2.352 -5.071 47.593 1.00 78.07 C ANISOU 1420 C SER A 204 13323 8480 7861 589 712 558 C ATOM 1421 O SER A 204 2.833 -4.716 46.508 1.00 76.44 O ANISOU 1421 O SER A 204 12981 8322 7743 544 613 534 O ATOM 1422 CB SER A 204 3.563 -4.398 49.629 1.00 76.60 C ANISOU 1422 CB SER A 204 13282 8378 7445 806 560 601 C ATOM 1423 OG SER A 204 3.977 -3.226 50.310 1.00 92.96 O ANISOU 1423 OG SER A 204 15326 10539 9455 843 419 559 O ATOM 1424 N ILE A 205 1.864 -6.300 47.811 1.00 75.66 N ANISOU 1424 N ILE A 205 13146 8072 7530 584 890 599 N ATOM 1425 CA ILE A 205 1.931 -7.320 46.790 1.00 74.24 C ANISOU 1425 CA ILE A 205 12956 7829 7421 529 971 613 C ATOM 1426 C ILE A 205 0.876 -7.081 45.717 1.00 79.16 C ANISOU 1426 C ILE A 205 13428 8467 8181 360 1022 530 C ATOM 1427 O ILE A 205 1.217 -7.081 44.536 1.00 77.45 O ANISOU 1427 O ILE A 205 13094 8280 8053 312 961 509 O ATOM 1428 CB ILE A 205 1.877 -8.717 47.437 1.00 77.20 C ANISOU 1428 CB ILE A 205 13554 8072 7705 587 1151 686 C ATOM 1429 CG1 ILE A 205 3.245 -8.989 48.099 1.00 77.30 C ANISOU 1429 CG1 ILE A 205 13678 8107 7587 790 1054 772 C ATOM 1430 CG2 ILE A 205 1.525 -9.801 46.405 1.00 76.39 C ANISOU 1430 CG2 ILE A 205 13462 7875 7687 479 1292 676 C ATOM 1431 CD1 ILE A 205 3.302 -10.077 48.986 1.00 89.95 C ANISOU 1431 CD1 ILE A 205 15521 9595 9061 901 1199 855 C ATOM 1432 N VAL A 206 -0.363 -6.829 46.114 1.00 78.03 N ANISOU 1432 N VAL A 206 13277 8324 8046 281 1124 478 N ATOM 1433 CA VAL A 206 -1.478 -6.639 45.187 1.00 77.85 C ANISOU 1433 CA VAL A 206 13102 8344 8133 135 1182 388 C ATOM 1434 C VAL A 206 -1.369 -5.285 44.465 1.00 78.49 C ANISOU 1434 C VAL A 206 13003 8539 8280 135 1006 338 C ATOM 1435 O VAL A 206 -1.723 -5.180 43.294 1.00 76.61 O ANISOU 1435 O VAL A 206 12625 8349 8135 54 992 285 O ATOM 1436 CB VAL A 206 -2.798 -6.789 45.990 1.00 84.31 C ANISOU 1436 CB VAL A 206 13968 9147 8918 68 1351 346 C ATOM 1437 CG1 VAL A 206 -4.023 -6.408 45.161 1.00 84.56 C ANISOU 1437 CG1 VAL A 206 13813 9274 9044 -63 1393 236 C ATOM 1438 CG2 VAL A 206 -2.934 -8.219 46.521 1.00 85.58 C ANISOU 1438 CG2 VAL A 206 14323 9172 9022 41 1555 392 C ATOM 1439 N SER A 207 -0.868 -4.266 45.155 1.00 74.34 N ANISOU 1439 N SER A 207 12495 8052 7698 226 878 355 N ATOM 1440 CA SER A 207 -0.773 -2.925 44.603 1.00 72.49 C ANISOU 1440 CA SER A 207 12133 7899 7511 228 730 311 C ATOM 1441 C SER A 207 0.491 -2.664 43.840 1.00 75.60 C ANISOU 1441 C SER A 207 12474 8314 7936 252 585 337 C ATOM 1442 O SER A 207 0.486 -1.757 42.992 1.00 76.68 O ANISOU 1442 O SER A 207 12498 8502 8134 223 495 299 O ATOM 1443 CB SER A 207 -0.855 -1.878 45.708 1.00 74.15 C ANISOU 1443 CB SER A 207 12399 8132 7644 298 671 302 C ATOM 1444 OG SER A 207 -2.144 -1.810 46.283 1.00 81.97 O ANISOU 1444 OG SER A 207 13402 9129 8614 274 791 261 O ATOM 1445 N PHE A 208 1.592 -3.350 44.179 1.00 68.49 N ANISOU 1445 N PHE A 208 11657 7386 6982 318 559 401 N ATOM 1446 CA PHE A 208 2.838 -2.977 43.548 1.00 66.66 C ANISOU 1446 CA PHE A 208 11358 7202 6770 343 414 416 C ATOM 1447 C PHE A 208 3.631 -4.145 42.983 1.00 70.69 C ANISOU 1447 C PHE A 208 11884 7686 7290 366 438 465 C ATOM 1448 O PHE A 208 4.056 -4.044 41.844 1.00 70.19 O ANISOU 1448 O PHE A 208 11714 7654 7301 324 380 453 O ATOM 1449 CB PHE A 208 3.705 -2.176 44.542 1.00 67.97 C ANISOU 1449 CB PHE A 208 11570 7414 6842 423 292 424 C ATOM 1450 CG PHE A 208 5.083 -1.815 44.031 1.00 68.46 C ANISOU 1450 CG PHE A 208 11558 7545 6908 438 148 428 C ATOM 1451 CD1 PHE A 208 5.277 -0.678 43.248 1.00 68.92 C ANISOU 1451 CD1 PHE A 208 11511 7644 7033 367 51 380 C ATOM 1452 CD2 PHE A 208 6.190 -2.603 44.346 1.00 69.97 C ANISOU 1452 CD2 PHE A 208 11790 7768 7029 530 116 478 C ATOM 1453 CE1 PHE A 208 6.549 -0.340 42.783 1.00 68.97 C ANISOU 1453 CE1 PHE A 208 11446 7719 7042 360 -67 376 C ATOM 1454 CE2 PHE A 208 7.459 -2.276 43.865 1.00 72.08 C ANISOU 1454 CE2 PHE A 208 11965 8126 7297 539 -13 471 C ATOM 1455 CZ PHE A 208 7.630 -1.143 43.091 1.00 69.43 C ANISOU 1455 CZ PHE A 208 11517 7828 7035 440 -100 416 C ATOM 1456 N TYR A 209 3.918 -5.186 43.776 1.00 68.41 N ANISOU 1456 N TYR A 209 11736 7343 6915 449 516 524 N ATOM 1457 CA TYR A 209 4.779 -6.281 43.335 1.00 68.28 C ANISOU 1457 CA TYR A 209 11760 7298 6887 507 536 579 C ATOM 1458 C TYR A 209 4.172 -7.133 42.224 1.00 72.64 C ANISOU 1458 C TYR A 209 12284 7782 7533 407 654 561 C ATOM 1459 O TYR A 209 4.884 -7.446 41.270 1.00 72.14 O ANISOU 1459 O TYR A 209 12158 7738 7515 410 609 571 O ATOM 1460 CB TYR A 209 5.215 -7.156 44.509 1.00 69.97 C ANISOU 1460 CB TYR A 209 12159 7463 6964 649 597 653 C ATOM 1461 CG TYR A 209 6.243 -6.485 45.390 1.00 72.25 C ANISOU 1461 CG TYR A 209 12449 7856 7145 772 446 669 C ATOM 1462 CD1 TYR A 209 7.527 -6.206 44.913 1.00 73.83 C ANISOU 1462 CD1 TYR A 209 12544 8166 7341 823 297 669 C ATOM 1463 CD2 TYR A 209 5.955 -6.167 46.716 1.00 73.83 C ANISOU 1463 CD2 TYR A 209 12754 8057 7240 835 456 676 C ATOM 1464 CE1 TYR A 209 8.494 -5.615 45.733 1.00 74.23 C ANISOU 1464 CE1 TYR A 209 12581 8339 7286 923 158 665 C ATOM 1465 CE2 TYR A 209 6.916 -5.579 47.546 1.00 75.29 C ANISOU 1465 CE2 TYR A 209 12937 8355 7315 945 314 677 C ATOM 1466 CZ TYR A 209 8.184 -5.306 47.048 1.00 79.39 C ANISOU 1466 CZ TYR A 209 13339 8995 7832 984 165 667 C ATOM 1467 OH TYR A 209 9.126 -4.705 47.848 1.00 76.84 O ANISOU 1467 OH TYR A 209 12991 8806 7397 1074 24 647 O ATOM 1468 N VAL A 210 2.878 -7.489 42.323 1.00 69.58 N ANISOU 1468 N VAL A 210 11934 7330 7175 313 805 526 N ATOM 1469 CA VAL A 210 2.211 -8.299 41.293 1.00 68.93 C ANISOU 1469 CA VAL A 210 11818 7197 7177 195 926 487 C ATOM 1470 C VAL A 210 2.237 -7.523 39.968 1.00 73.52 C ANISOU 1470 C VAL A 210 12200 7871 7862 123 813 430 C ATOM 1471 O VAL A 210 2.829 -8.066 39.044 1.00 74.09 O ANISOU 1471 O VAL A 210 12243 7935 7974 118 800 441 O ATOM 1472 CB VAL A 210 0.778 -8.787 41.683 1.00 71.95 C ANISOU 1472 CB VAL A 210 12256 7516 7564 85 1115 439 C ATOM 1473 CG1 VAL A 210 -0.017 -9.258 40.471 1.00 71.51 C ANISOU 1473 CG1 VAL A 210 12097 7464 7608 -69 1204 360 C ATOM 1474 CG2 VAL A 210 0.838 -9.878 42.737 1.00 72.10 C ANISOU 1474 CG2 VAL A 210 12507 7406 7482 144 1267 506 C ATOM 1475 N PRO A 211 1.718 -6.259 39.847 1.00 71.04 N ANISOU 1475 N PRO A 211 11765 7642 7583 88 727 378 N ATOM 1476 CA PRO A 211 1.745 -5.582 38.537 1.00 69.84 C ANISOU 1476 CA PRO A 211 11451 7567 7517 34 634 333 C ATOM 1477 C PRO A 211 3.152 -5.295 38.005 1.00 73.43 C ANISOU 1477 C PRO A 211 11867 8055 7977 92 497 376 C ATOM 1478 O PRO A 211 3.307 -5.300 36.788 1.00 72.29 O ANISOU 1478 O PRO A 211 11625 7942 7899 47 467 355 O ATOM 1479 CB PRO A 211 0.971 -4.281 38.793 1.00 70.87 C ANISOU 1479 CB PRO A 211 11513 7762 7650 25 582 285 C ATOM 1480 CG PRO A 211 1.028 -4.076 40.252 1.00 75.05 C ANISOU 1480 CG PRO A 211 12162 8262 8093 93 590 317 C ATOM 1481 CD PRO A 211 0.981 -5.435 40.836 1.00 72.04 C ANISOU 1481 CD PRO A 211 11911 7794 7668 99 729 355 C ATOM 1482 N LEU A 212 4.151 -5.029 38.896 1.00 70.46 N ANISOU 1482 N LEU A 212 11557 7689 7525 188 415 426 N ATOM 1483 CA LEU A 212 5.564 -4.778 38.554 1.00 70.08 C ANISOU 1483 CA LEU A 212 11463 7697 7466 242 288 457 C ATOM 1484 C LEU A 212 6.212 -6.000 37.900 1.00 74.87 C ANISOU 1484 C LEU A 212 12089 8276 8083 273 334 494 C ATOM 1485 O LEU A 212 6.897 -5.856 36.893 1.00 75.46 O ANISOU 1485 O LEU A 212 12067 8400 8204 256 265 490 O ATOM 1486 CB LEU A 212 6.372 -4.409 39.814 1.00 70.92 C ANISOU 1486 CB LEU A 212 11638 7838 7468 341 211 487 C ATOM 1487 CG LEU A 212 7.901 -4.335 39.663 1.00 75.63 C ANISOU 1487 CG LEU A 212 12185 8521 8029 407 91 511 C ATOM 1488 CD1 LEU A 212 8.314 -2.987 39.147 1.00 75.34 C ANISOU 1488 CD1 LEU A 212 12031 8561 8035 335 -32 464 C ATOM 1489 CD2 LEU A 212 8.595 -4.602 40.974 1.00 77.28 C ANISOU 1489 CD2 LEU A 212 12489 8763 8110 535 60 548 C ATOM 1490 N VAL A 213 6.044 -7.186 38.512 1.00 71.13 N ANISOU 1490 N VAL A 213 11755 7716 7555 325 455 533 N ATOM 1491 CA VAL A 213 6.619 -8.446 38.040 1.00 71.06 C ANISOU 1491 CA VAL A 213 11810 7653 7536 376 522 574 C ATOM 1492 C VAL A 213 6.033 -8.770 36.654 1.00 74.60 C ANISOU 1492 C VAL A 213 12174 8080 8092 253 580 523 C ATOM 1493 O VAL A 213 6.791 -9.154 35.762 1.00 75.20 O ANISOU 1493 O VAL A 213 12204 8174 8192 274 549 535 O ATOM 1494 CB VAL A 213 6.444 -9.609 39.076 1.00 74.78 C ANISOU 1494 CB VAL A 213 12491 8008 7913 460 663 630 C ATOM 1495 CG1 VAL A 213 6.770 -10.970 38.470 1.00 74.80 C ANISOU 1495 CG1 VAL A 213 12588 7918 7914 494 771 662 C ATOM 1496 CG2 VAL A 213 7.307 -9.369 40.305 1.00 74.90 C ANISOU 1496 CG2 VAL A 213 12579 8074 7804 619 581 686 C ATOM 1497 N ILE A 214 4.714 -8.562 36.467 1.00 69.22 N ANISOU 1497 N ILE A 214 11457 7381 7464 132 656 459 N ATOM 1498 CA ILE A 214 4.031 -8.815 35.193 1.00 68.40 C ANISOU 1498 CA ILE A 214 11258 7283 7449 12 707 393 C ATOM 1499 C ILE A 214 4.575 -7.845 34.106 1.00 73.80 C ANISOU 1499 C ILE A 214 11779 8073 8189 2 559 376 C ATOM 1500 O ILE A 214 4.947 -8.287 33.028 1.00 74.12 O ANISOU 1500 O ILE A 214 11770 8122 8272 -19 558 367 O ATOM 1501 CB ILE A 214 2.478 -8.754 35.375 1.00 70.70 C ANISOU 1501 CB ILE A 214 11529 7567 7765 -103 816 318 C ATOM 1502 CG1 ILE A 214 1.995 -9.985 36.195 1.00 70.91 C ANISOU 1502 CG1 ILE A 214 11732 7466 7743 -124 1002 330 C ATOM 1503 CG2 ILE A 214 1.745 -8.668 34.017 1.00 70.37 C ANISOU 1503 CG2 ILE A 214 11339 7592 7807 -218 826 230 C ATOM 1504 CD1 ILE A 214 0.647 -9.880 36.782 1.00 69.97 C ANISOU 1504 CD1 ILE A 214 11615 7348 7622 -217 1110 269 C ATOM 1505 N AMET A 215 4.638 -6.551 34.424 0.50 69.05 N ANISOU 1505 N AMET A 215 11115 7541 7581 19 447 372 N ATOM 1506 N BMET A 215 4.635 -6.544 34.421 0.50 72.46 N ANISOU 1506 N BMET A 215 11546 7973 8013 18 447 372 N ATOM 1507 CA AMET A 215 5.124 -5.471 33.573 0.50 66.83 C ANISOU 1507 CA AMET A 215 10711 7342 7339 7 319 360 C ATOM 1508 CA BMET A 215 5.118 -5.472 33.552 0.50 72.01 C ANISOU 1508 CA BMET A 215 11366 7999 7996 6 319 359 C ATOM 1509 C AMET A 215 6.566 -5.709 33.105 0.50 73.66 C ANISOU 1509 C AMET A 215 11556 8236 8197 60 247 405 C ATOM 1510 C BMET A 215 6.569 -5.715 33.097 0.50 75.94 C ANISOU 1510 C BMET A 215 11844 8524 8486 60 247 405 C ATOM 1511 O AMET A 215 6.843 -5.542 31.922 0.50 73.83 O ANISOU 1511 O AMET A 215 11486 8297 8269 24 210 390 O ATOM 1512 O BMET A 215 6.849 -5.568 31.912 0.50 76.04 O ANISOU 1512 O BMET A 215 11767 8576 8549 24 211 391 O ATOM 1513 CB AMET A 215 5.026 -4.158 34.356 0.50 67.62 C ANISOU 1513 CB AMET A 215 10810 7476 7408 26 237 356 C ATOM 1514 CB BMET A 215 4.991 -4.125 34.285 0.50 74.40 C ANISOU 1514 CB BMET A 215 11662 8337 8271 22 236 353 C ATOM 1515 CG AMET A 215 5.422 -2.933 33.587 0.50 68.58 C ANISOU 1515 CG AMET A 215 10840 7658 7561 5 126 342 C ATOM 1516 CG BMET A 215 5.504 -2.937 33.511 0.50 77.89 C ANISOU 1516 CG BMET A 215 12014 8838 8741 4 121 343 C ATOM 1517 SD AMET A 215 5.433 -1.498 34.682 0.50 70.67 S ANISOU 1517 SD AMET A 215 11147 7931 7773 29 47 335 S ATOM 1518 SD BMET A 215 6.939 -2.215 34.337 0.50 83.03 S ANISOU 1518 SD BMET A 215 12692 9524 9332 55 3 378 S ATOM 1519 CE AMET A 215 6.891 -1.860 35.727 0.50 67.42 C ANISOU 1519 CE AMET A 215 10795 7536 7285 97 -11 382 C ATOM 1520 CE BMET A 215 6.164 -1.068 35.344 0.50 79.98 C ANISOU 1520 CE BMET A 215 12358 9122 8910 54 -14 350 C ATOM 1521 N VAL A 216 7.468 -6.094 34.016 1.00 72.48 N ANISOU 1521 N VAL A 216 11484 8079 7977 154 227 457 N ATOM 1522 CA VAL A 216 8.887 -6.330 33.709 1.00 73.72 C ANISOU 1522 CA VAL A 216 11608 8293 8110 224 155 494 C ATOM 1523 C VAL A 216 9.045 -7.584 32.825 1.00 80.54 C ANISOU 1523 C VAL A 216 12491 9111 8999 236 237 507 C ATOM 1524 O VAL A 216 9.846 -7.577 31.893 1.00 80.56 O ANISOU 1524 O VAL A 216 12410 9172 9029 241 185 509 O ATOM 1525 CB VAL A 216 9.735 -6.392 35.016 1.00 78.36 C ANISOU 1525 CB VAL A 216 12267 8913 8595 342 107 537 C ATOM 1526 CG1 VAL A 216 11.088 -7.072 34.801 1.00 78.90 C ANISOU 1526 CG1 VAL A 216 12318 9043 8616 450 68 577 C ATOM 1527 CG2 VAL A 216 9.927 -4.993 35.603 1.00 77.46 C ANISOU 1527 CG2 VAL A 216 12101 8871 8460 314 -5 510 C ATOM 1528 N PHE A 217 8.247 -8.620 33.088 1.00 78.94 N ANISOU 1528 N PHE A 217 12402 8802 8790 229 375 507 N ATOM 1529 CA PHE A 217 8.270 -9.877 32.349 1.00 79.70 C ANISOU 1529 CA PHE A 217 12552 8826 8903 229 479 509 C ATOM 1530 C PHE A 217 7.684 -9.709 30.921 1.00 77.69 C ANISOU 1530 C PHE A 217 12179 8597 8741 105 487 443 C ATOM 1531 O PHE A 217 8.292 -10.178 29.950 1.00 76.61 O ANISOU 1531 O PHE A 217 12008 8474 8627 117 483 446 O ATOM 1532 CB PHE A 217 7.507 -10.947 33.151 1.00 84.51 C ANISOU 1532 CB PHE A 217 13339 9299 9470 232 641 519 C ATOM 1533 CG PHE A 217 7.287 -12.238 32.419 1.00 89.86 C ANISOU 1533 CG PHE A 217 14100 9874 10170 197 780 503 C ATOM 1534 CD1 PHE A 217 8.308 -13.180 32.315 1.00 96.43 C ANISOU 1534 CD1 PHE A 217 15029 10659 10949 325 806 562 C ATOM 1535 CD2 PHE A 217 6.062 -12.515 31.819 1.00 94.42 C ANISOU 1535 CD2 PHE A 217 14655 10408 10812 38 885 421 C ATOM 1536 CE1 PHE A 217 8.109 -14.378 31.619 1.00 98.88 C ANISOU 1536 CE1 PHE A 217 15437 10856 11275 290 944 543 C ATOM 1537 CE2 PHE A 217 5.863 -13.711 31.125 1.00 99.21 C ANISOU 1537 CE2 PHE A 217 15343 10916 11436 -15 1020 391 C ATOM 1538 CZ PHE A 217 6.889 -14.637 31.033 1.00 98.44 C ANISOU 1538 CZ PHE A 217 15366 10748 11289 110 1053 454 C ATOM 1539 N VAL A 218 6.506 -9.054 30.805 1.00 69.41 N ANISOU 1539 N VAL A 218 11070 7567 7736 0 499 383 N ATOM 1540 CA VAL A 218 5.799 -8.828 29.543 1.00 66.23 C ANISOU 1540 CA VAL A 218 10552 7211 7403 -103 503 313 C ATOM 1541 C VAL A 218 6.558 -7.813 28.662 1.00 69.58 C ANISOU 1541 C VAL A 218 10852 7733 7853 -88 367 323 C ATOM 1542 O VAL A 218 6.635 -8.014 27.449 1.00 70.44 O ANISOU 1542 O VAL A 218 10892 7872 8000 -123 366 296 O ATOM 1543 CB VAL A 218 4.332 -8.393 29.795 1.00 67.80 C ANISOU 1543 CB VAL A 218 10717 7425 7618 -189 551 244 C ATOM 1544 CG1 VAL A 218 3.680 -7.860 28.534 1.00 66.89 C ANISOU 1544 CG1 VAL A 218 10459 7401 7554 -260 517 174 C ATOM 1545 CG2 VAL A 218 3.507 -9.536 30.370 1.00 67.94 C ANISOU 1545 CG2 VAL A 218 10845 7348 7621 -245 715 214 C ATOM 1546 N TYR A 219 7.096 -6.729 29.247 1.00 64.16 N ANISOU 1546 N TYR A 219 10143 7093 7142 -46 262 356 N ATOM 1547 CA TYR A 219 7.784 -5.724 28.445 1.00 62.14 C ANISOU 1547 CA TYR A 219 9789 6916 6908 -54 154 361 C ATOM 1548 C TYR A 219 9.161 -6.173 27.992 1.00 68.72 C ANISOU 1548 C TYR A 219 10599 7780 7731 -3 117 401 C ATOM 1549 O TYR A 219 9.625 -5.698 26.960 1.00 69.70 O ANISOU 1549 O TYR A 219 10638 7960 7883 -31 67 396 O ATOM 1550 CB TYR A 219 7.870 -4.354 29.127 1.00 61.14 C ANISOU 1550 CB TYR A 219 9653 6819 6759 -51 67 368 C ATOM 1551 CG TYR A 219 7.649 -3.242 28.126 1.00 60.17 C ANISOU 1551 CG TYR A 219 9451 6740 6669 -98 12 344 C ATOM 1552 CD1 TYR A 219 6.406 -3.062 27.518 1.00 62.04 C ANISOU 1552 CD1 TYR A 219 9657 6985 6932 -131 50 298 C ATOM 1553 CD2 TYR A 219 8.700 -2.425 27.717 1.00 59.30 C ANISOU 1553 CD2 TYR A 219 9301 6674 6558 -107 -69 365 C ATOM 1554 CE1 TYR A 219 6.207 -2.070 26.562 1.00 62.31 C ANISOU 1554 CE1 TYR A 219 9636 7060 6979 -146 4 284 C ATOM 1555 CE2 TYR A 219 8.498 -1.394 26.800 1.00 58.96 C ANISOU 1555 CE2 TYR A 219 9218 6652 6534 -144 -103 352 C ATOM 1556 CZ TYR A 219 7.250 -1.223 26.225 1.00 65.12 C ANISOU 1556 CZ TYR A 219 9983 7430 7330 -150 -68 318 C ATOM 1557 OH TYR A 219 7.043 -0.237 25.298 1.00 65.55 O ANISOU 1557 OH TYR A 219 10015 7505 7387 -158 -99 312 O ATOM 1558 N SER A 220 9.810 -7.084 28.708 1.00 67.35 N ANISOU 1558 N SER A 220 10503 7578 7510 80 148 441 N ATOM 1559 CA SER A 220 11.087 -7.596 28.223 1.00 68.69 C ANISOU 1559 CA SER A 220 10642 7796 7663 147 119 473 C ATOM 1560 C SER A 220 10.817 -8.405 26.936 1.00 74.83 C ANISOU 1560 C SER A 220 11403 8543 8488 111 190 448 C ATOM 1561 O SER A 220 11.587 -8.296 25.972 1.00 75.37 O ANISOU 1561 O SER A 220 11388 8676 8573 113 148 451 O ATOM 1562 CB SER A 220 11.794 -8.426 29.289 1.00 71.79 C ANISOU 1562 CB SER A 220 11131 8170 7975 277 138 523 C ATOM 1563 OG SER A 220 10.874 -9.302 29.910 1.00 81.14 O ANISOU 1563 OG SER A 220 12454 9234 9142 286 256 526 O ATOM 1564 N ARG A 221 9.649 -9.096 26.883 1.00 70.87 N ANISOU 1564 N ARG A 221 10968 7951 8006 57 298 411 N ATOM 1565 CA ARG A 221 9.234 -9.845 25.712 1.00 71.60 C ANISOU 1565 CA ARG A 221 11047 8017 8139 1 372 366 C ATOM 1566 C ARG A 221 8.874 -8.921 24.568 1.00 75.28 C ANISOU 1566 C ARG A 221 11381 8567 8654 -77 309 323 C ATOM 1567 O ARG A 221 9.144 -9.276 23.428 1.00 75.24 O ANISOU 1567 O ARG A 221 11330 8587 8670 -91 318 305 O ATOM 1568 CB ARG A 221 8.085 -10.825 26.003 1.00 74.82 C ANISOU 1568 CB ARG A 221 11558 8320 8552 -59 513 321 C ATOM 1569 CG ARG A 221 8.558 -12.288 25.911 1.00 94.40 C ANISOU 1569 CG ARG A 221 14165 10698 11003 -5 622 340 C ATOM 1570 CD ARG A 221 8.743 -12.815 24.480 1.00106.66 C ANISOU 1570 CD ARG A 221 15670 12264 12590 -41 646 298 C ATOM 1571 NE ARG A 221 7.456 -13.038 23.822 1.00115.17 N ANISOU 1571 NE ARG A 221 16717 13330 13712 -187 723 199 N ATOM 1572 CZ ARG A 221 6.783 -14.183 23.853 1.00129.44 C ANISOU 1572 CZ ARG A 221 18639 15026 15516 -257 875 145 C ATOM 1573 NH1 ARG A 221 7.283 -15.241 24.480 1.00120.59 N ANISOU 1573 NH1 ARG A 221 17699 13771 14349 -180 974 195 N ATOM 1574 NH2 ARG A 221 5.608 -14.283 23.248 1.00115.39 N ANISOU 1574 NH2 ARG A 221 16799 13273 13773 -403 933 36 N ATOM 1575 N VAL A 222 8.294 -7.734 24.861 1.00 71.29 N ANISOU 1575 N VAL A 222 10827 8103 8156 -114 249 310 N ATOM 1576 CA VAL A 222 7.949 -6.713 23.860 1.00 69.64 C ANISOU 1576 CA VAL A 222 10516 7968 7974 -160 188 280 C ATOM 1577 C VAL A 222 9.242 -6.316 23.126 1.00 72.07 C ANISOU 1577 C VAL A 222 10768 8332 8283 -132 116 321 C ATOM 1578 O VAL A 222 9.277 -6.348 21.911 1.00 71.13 O ANISOU 1578 O VAL A 222 10592 8252 8183 -155 115 301 O ATOM 1579 CB VAL A 222 7.227 -5.506 24.531 1.00 72.58 C ANISOU 1579 CB VAL A 222 10882 8356 8337 -172 142 272 C ATOM 1580 CG1 VAL A 222 7.264 -4.257 23.653 1.00 71.75 C ANISOU 1580 CG1 VAL A 222 10708 8314 8240 -183 66 271 C ATOM 1581 CG2 VAL A 222 5.791 -5.864 24.891 1.00 72.41 C ANISOU 1581 CG2 VAL A 222 10877 8315 8320 -213 220 212 C ATOM 1582 N PHE A 223 10.306 -6.019 23.882 1.00 69.97 N ANISOU 1582 N PHE A 223 10515 8080 7989 -85 62 371 N ATOM 1583 CA PHE A 223 11.640 -5.684 23.400 1.00 70.33 C ANISOU 1583 CA PHE A 223 10499 8197 8027 -66 1 402 C ATOM 1584 C PHE A 223 12.277 -6.878 22.643 1.00 75.22 C ANISOU 1584 C PHE A 223 11109 8823 8647 -21 47 409 C ATOM 1585 O PHE A 223 12.932 -6.673 21.626 1.00 75.03 O ANISOU 1585 O PHE A 223 11014 8861 8635 -33 22 412 O ATOM 1586 CB PHE A 223 12.530 -5.233 24.577 1.00 72.38 C ANISOU 1586 CB PHE A 223 10768 8489 8244 -27 -61 433 C ATOM 1587 CG PHE A 223 12.299 -3.823 25.093 1.00 74.10 C ANISOU 1587 CG PHE A 223 10983 8714 8456 -81 -121 425 C ATOM 1588 CD1 PHE A 223 11.889 -2.806 24.238 1.00 77.83 C ANISOU 1588 CD1 PHE A 223 11425 9189 8955 -148 -139 409 C ATOM 1589 CD2 PHE A 223 12.565 -3.498 26.416 1.00 77.35 C ANISOU 1589 CD2 PHE A 223 11433 9130 8825 -55 -158 433 C ATOM 1590 CE1 PHE A 223 11.713 -1.500 24.706 1.00 79.52 C ANISOU 1590 CE1 PHE A 223 11665 9391 9157 -190 -183 402 C ATOM 1591 CE2 PHE A 223 12.395 -2.192 26.883 1.00 80.51 C ANISOU 1591 CE2 PHE A 223 11844 9529 9217 -110 -208 418 C ATOM 1592 CZ PHE A 223 11.980 -1.200 26.024 1.00 79.13 C ANISOU 1592 CZ PHE A 223 11654 9339 9072 -178 -216 404 C ATOM 1593 N GLN A 224 12.078 -8.113 23.127 1.00 72.90 N ANISOU 1593 N GLN A 224 10902 8460 8337 31 124 411 N ATOM 1594 CA GLN A 224 12.572 -9.319 22.445 1.00 73.30 C ANISOU 1594 CA GLN A 224 10976 8492 8383 83 186 414 C ATOM 1595 C GLN A 224 11.925 -9.441 21.046 1.00 77.54 C ANISOU 1595 C GLN A 224 11467 9031 8962 5 221 361 C ATOM 1596 O GLN A 224 12.629 -9.677 20.060 1.00 79.45 O ANISOU 1596 O GLN A 224 11661 9320 9208 24 215 364 O ATOM 1597 CB GLN A 224 12.245 -10.580 23.262 1.00 75.06 C ANISOU 1597 CB GLN A 224 11342 8603 8574 142 286 423 C ATOM 1598 CG GLN A 224 13.233 -10.950 24.340 1.00 98.67 C ANISOU 1598 CG GLN A 224 14392 11601 11496 277 268 484 C ATOM 1599 CD GLN A 224 12.646 -12.053 25.195 1.00135.03 C ANISOU 1599 CD GLN A 224 19171 16069 16065 323 384 495 C ATOM 1600 OE1 GLN A 224 12.156 -13.083 24.695 1.00134.11 O ANISOU 1600 OE1 GLN A 224 19144 15852 15961 300 499 468 O ATOM 1601 NE2 GLN A 224 12.644 -11.847 26.508 1.00131.49 N ANISOU 1601 NE2 GLN A 224 18785 15608 15567 379 366 530 N ATOM 1602 N GLU A 225 10.580 -9.271 20.987 1.00 70.49 N ANISOU 1602 N GLU A 225 10585 8105 8095 -77 255 308 N ATOM 1603 CA GLU A 225 9.741 -9.350 19.801 1.00 68.84 C ANISOU 1603 CA GLU A 225 10325 7918 7912 -150 284 241 C ATOM 1604 C GLU A 225 10.095 -8.262 18.768 1.00 72.50 C ANISOU 1604 C GLU A 225 10685 8478 8383 -162 200 250 C ATOM 1605 O GLU A 225 10.208 -8.572 17.596 1.00 71.38 O ANISOU 1605 O GLU A 225 10504 8371 8246 -174 214 224 O ATOM 1606 CB GLU A 225 8.247 -9.258 20.186 1.00 69.58 C ANISOU 1606 CB GLU A 225 10430 7989 8017 -222 327 177 C ATOM 1607 CG GLU A 225 7.654 -10.538 20.753 1.00 73.51 C ANISOU 1607 CG GLU A 225 11032 8386 8512 -253 450 139 C ATOM 1608 CD GLU A 225 7.927 -11.801 19.953 1.00 92.16 C ANISOU 1608 CD GLU A 225 13442 10700 10875 -262 536 106 C ATOM 1609 OE1 GLU A 225 8.312 -12.817 20.573 1.00 89.72 O ANISOU 1609 OE1 GLU A 225 13261 10283 10545 -218 619 134 O ATOM 1610 OE2 GLU A 225 7.808 -11.767 18.706 1.00 80.15 O ANISOU 1610 OE2 GLU A 225 11842 9244 9367 -299 522 58 O ATOM 1611 N ALA A 226 10.289 -7.010 19.193 1.00 69.99 N ANISOU 1611 N ALA A 226 10339 8194 8059 -161 123 286 N ATOM 1612 CA ALA A 226 10.634 -5.930 18.270 1.00 69.58 C ANISOU 1612 CA ALA A 226 10222 8211 8006 -177 61 301 C ATOM 1613 C ALA A 226 11.976 -6.226 17.559 1.00 74.84 C ANISOU 1613 C ALA A 226 10849 8920 8667 -152 52 333 C ATOM 1614 O ALA A 226 12.089 -6.009 16.356 1.00 76.29 O ANISOU 1614 O ALA A 226 10986 9150 8849 -167 49 325 O ATOM 1615 CB ALA A 226 10.699 -4.604 19.015 1.00 69.49 C ANISOU 1615 CB ALA A 226 10220 8200 7984 -187 -2 332 C ATOM 1616 N LYS A 227 12.963 -6.750 18.296 1.00 70.24 N ANISOU 1616 N LYS A 227 10281 8334 8072 -102 52 368 N ATOM 1617 CA LYS A 227 14.292 -7.080 17.784 1.00 70.38 C ANISOU 1617 CA LYS A 227 10249 8415 8077 -61 44 395 C ATOM 1618 C LYS A 227 14.170 -8.308 16.866 1.00 76.59 C ANISOU 1618 C LYS A 227 11054 9181 8868 -32 115 367 C ATOM 1619 O LYS A 227 14.647 -8.260 15.731 1.00 77.29 O ANISOU 1619 O LYS A 227 11086 9325 8956 -38 114 364 O ATOM 1620 CB LYS A 227 15.258 -7.321 18.962 1.00 72.91 C ANISOU 1620 CB LYS A 227 10578 8758 8367 8 19 431 C ATOM 1621 CG LYS A 227 16.729 -7.431 18.599 1.00 82.71 C ANISOU 1621 CG LYS A 227 11737 10107 9584 56 -6 453 C ATOM 1622 CD LYS A 227 17.559 -7.968 19.773 1.00 90.44 C ANISOU 1622 CD LYS A 227 12727 11123 10513 162 -25 479 C ATOM 1623 N ARG A 228 13.466 -9.371 17.338 1.00 72.94 N ANISOU 1623 N ARG A 228 10679 8629 8407 -13 185 340 N ATOM 1624 CA ARG A 228 13.213 -10.629 16.613 1.00 72.51 C ANISOU 1624 CA ARG A 228 10672 8524 8353 -2 272 299 C ATOM 1625 C ARG A 228 12.453 -10.405 15.280 1.00 73.09 C ANISOU 1625 C ARG A 228 10692 8635 8443 -79 279 239 C ATOM 1626 O ARG A 228 12.802 -11.034 14.281 1.00 74.78 O ANISOU 1626 O ARG A 228 10896 8865 8651 -64 314 217 O ATOM 1627 CB ARG A 228 12.415 -11.601 17.513 1.00 73.60 C ANISOU 1627 CB ARG A 228 10934 8544 8488 -3 359 274 C ATOM 1628 CG ARG A 228 12.180 -12.985 16.944 1.00 87.20 C ANISOU 1628 CG ARG A 228 12742 10185 10206 -3 470 226 C ATOM 1629 CD ARG A 228 11.133 -13.765 17.726 1.00106.07 C ANISOU 1629 CD ARG A 228 15254 12451 12598 -53 572 184 C ATOM 1630 NE ARG A 228 9.761 -13.368 17.397 1.00120.25 N ANISOU 1630 NE ARG A 228 16996 14271 14423 -184 581 99 N ATOM 1631 CZ ARG A 228 9.034 -13.893 16.413 1.00141.52 C ANISOU 1631 CZ ARG A 228 19673 16970 17128 -271 640 4 C ATOM 1632 NH1 ARG A 228 7.796 -13.468 16.196 1.00132.19 N ANISOU 1632 NH1 ARG A 228 18420 15844 15960 -376 636 -78 N ATOM 1633 NH2 ARG A 228 9.543 -14.838 15.631 1.00132.46 N ANISOU 1633 NH2 ARG A 228 18575 15785 15969 -249 701 -16 N ATOM 1634 N GLN A 229 11.445 -9.514 15.270 1.00 64.68 N ANISOU 1634 N GLN A 229 9592 7593 7390 -143 243 210 N ATOM 1635 CA GLN A 229 10.580 -9.263 14.124 1.00 62.87 C ANISOU 1635 CA GLN A 229 9310 7418 7158 -195 242 148 C ATOM 1636 C GLN A 229 11.158 -8.214 13.158 1.00 70.51 C ANISOU 1636 C GLN A 229 10207 8472 8110 -183 176 185 C ATOM 1637 O GLN A 229 10.496 -7.838 12.182 1.00 69.55 O ANISOU 1637 O GLN A 229 10045 8409 7971 -202 164 145 O ATOM 1638 CB GLN A 229 9.169 -8.890 14.574 1.00 62.96 C ANISOU 1638 CB GLN A 229 9318 7429 7174 -247 243 94 C ATOM 1639 CG GLN A 229 8.411 -10.078 15.168 1.00 65.32 C ANISOU 1639 CG GLN A 229 9684 7651 7485 -292 338 29 C ATOM 1640 CD GLN A 229 7.003 -9.724 15.569 1.00 82.30 C ANISOU 1640 CD GLN A 229 11807 9827 9636 -352 346 -36 C ATOM 1641 OE1 GLN A 229 6.253 -9.066 14.826 1.00 79.03 O ANISOU 1641 OE1 GLN A 229 11309 9513 9205 -367 304 -85 O ATOM 1642 NE2 GLN A 229 6.590 -10.202 16.735 1.00 71.09 N ANISOU 1642 NE2 GLN A 229 10459 8326 8227 -377 405 -44 N ATOM 1643 N LEU A 230 12.419 -7.790 13.381 1.00 69.95 N ANISOU 1643 N LEU A 230 10122 8418 8037 -150 142 256 N ATOM 1644 CA LEU A 230 13.084 -6.920 12.426 1.00 70.04 C ANISOU 1644 CA LEU A 230 10080 8501 8031 -154 105 289 C ATOM 1645 C LEU A 230 13.307 -7.722 11.134 1.00 77.58 C ANISOU 1645 C LEU A 230 11012 9493 8972 -138 146 257 C ATOM 1646 O LEU A 230 13.644 -8.915 11.159 1.00 79.00 O ANISOU 1646 O LEU A 230 11217 9643 9157 -106 198 238 O ATOM 1647 CB LEU A 230 14.392 -6.331 12.968 1.00 69.66 C ANISOU 1647 CB LEU A 230 10007 8479 7982 -146 69 353 C ATOM 1648 CG LEU A 230 14.242 -4.997 13.730 1.00 72.58 C ANISOU 1648 CG LEU A 230 10390 8836 8351 -187 17 382 C ATOM 1649 CD1 LEU A 230 15.411 -4.773 14.657 1.00 72.24 C ANISOU 1649 CD1 LEU A 230 10324 8819 8307 -187 -11 417 C ATOM 1650 CD2 LEU A 230 14.075 -3.799 12.764 1.00 70.16 C ANISOU 1650 CD2 LEU A 230 10081 8554 8022 -223 1 397 C ATOM 1651 N ASN A1002 12.973 -7.087 10.023 1.00 73.66 N ANISOU 1651 N ASN A1002 10487 9052 8449 -152 130 246 N ATOM 1652 CA ASN A1002 13.071 -7.654 8.704 1.00 72.78 C ANISOU 1652 CA ASN A1002 10352 8988 8312 -139 162 212 C ATOM 1653 C ASN A1002 13.716 -6.603 7.764 1.00 75.76 C ANISOU 1653 C ASN A1002 10699 9430 8655 -136 136 264 C ATOM 1654 O ASN A1002 14.049 -5.493 8.204 1.00 75.15 O ANISOU 1654 O ASN A1002 10629 9346 8577 -156 103 320 O ATOM 1655 CB ASN A1002 11.668 -8.104 8.232 1.00 71.18 C ANISOU 1655 CB ASN A1002 10152 8800 8095 -160 179 119 C ATOM 1656 CG ASN A1002 10.602 -7.028 8.252 1.00 87.34 C ANISOU 1656 CG ASN A1002 12185 10883 10117 -165 129 109 C ATOM 1657 OD1 ASN A1002 10.848 -5.853 7.971 1.00 86.47 O ANISOU 1657 OD1 ASN A1002 12076 10798 9979 -144 89 168 O ATOM 1658 ND2 ASN A1002 9.377 -7.411 8.561 1.00 77.58 N ANISOU 1658 ND2 ASN A1002 10941 9652 8882 -191 141 29 N ATOM 1659 N ILE A1003 13.872 -6.964 6.478 1.00 70.79 N ANISOU 1659 N ILE A1003 10050 8856 7992 -118 162 240 N ATOM 1660 CA ILE A1003 14.466 -6.152 5.429 1.00 70.59 C ANISOU 1660 CA ILE A1003 10010 8889 7922 -113 159 285 C ATOM 1661 C ILE A1003 13.681 -4.855 5.212 1.00 76.61 C ANISOU 1661 C ILE A1003 10806 9659 8645 -113 122 308 C ATOM 1662 O ILE A1003 14.303 -3.813 4.972 1.00 76.78 O ANISOU 1662 O ILE A1003 10850 9681 8643 -128 122 374 O ATOM 1663 CB ILE A1003 14.637 -6.971 4.091 1.00 72.74 C ANISOU 1663 CB ILE A1003 10261 9219 8156 -83 199 243 C ATOM 1664 CG1 ILE A1003 15.426 -6.179 3.025 1.00 72.49 C ANISOU 1664 CG1 ILE A1003 10220 9247 8075 -77 210 299 C ATOM 1665 CG2 ILE A1003 13.307 -7.517 3.523 1.00 70.80 C ANISOU 1665 CG2 ILE A1003 10020 8999 7882 -74 198 149 C ATOM 1666 CD1 ILE A1003 16.794 -5.665 3.453 1.00 73.18 C ANISOU 1666 CD1 ILE A1003 10282 9338 8186 -109 223 371 C ATOM 1667 N PHE A1004 12.337 -4.913 5.301 1.00 73.34 N ANISOU 1667 N PHE A1004 10399 9251 8216 -94 99 250 N ATOM 1668 CA PHE A1004 11.486 -3.736 5.081 1.00 73.33 C ANISOU 1668 CA PHE A1004 10434 9269 8161 -59 62 267 C ATOM 1669 C PHE A1004 11.729 -2.665 6.134 1.00 74.80 C ANISOU 1669 C PHE A1004 10671 9379 8370 -82 42 334 C ATOM 1670 O PHE A1004 11.862 -1.491 5.791 1.00 73.45 O ANISOU 1670 O PHE A1004 10561 9194 8153 -66 38 393 O ATOM 1671 CB PHE A1004 10.010 -4.128 5.026 1.00 75.28 C ANISOU 1671 CB PHE A1004 10650 9570 8384 -30 40 174 C ATOM 1672 CG PHE A1004 9.779 -5.164 3.958 1.00 76.94 C ANISOU 1672 CG PHE A1004 10811 9859 8564 -25 63 91 C ATOM 1673 CD1 PHE A1004 9.668 -4.795 2.622 1.00 79.91 C ANISOU 1673 CD1 PHE A1004 11184 10325 8853 35 54 90 C ATOM 1674 CD2 PHE A1004 9.736 -6.520 4.281 1.00 78.12 C ANISOU 1674 CD2 PHE A1004 10933 9984 8764 -77 103 17 C ATOM 1675 CE1 PHE A1004 9.505 -5.760 1.631 1.00 81.14 C ANISOU 1675 CE1 PHE A1004 11295 10558 8976 36 74 6 C ATOM 1676 CE2 PHE A1004 9.565 -7.484 3.289 1.00 80.82 C ANISOU 1676 CE2 PHE A1004 11245 10388 9077 -84 133 -68 C ATOM 1677 CZ PHE A1004 9.457 -7.099 1.973 1.00 80.03 C ANISOU 1677 CZ PHE A1004 11127 10389 8893 -30 114 -77 C ATOM 1678 N GLU A1005 11.871 -3.089 7.397 1.00 70.57 N ANISOU 1678 N GLU A1005 10124 8788 7900 -122 38 326 N ATOM 1679 CA GLU A1005 12.146 -2.187 8.503 1.00 69.52 C ANISOU 1679 CA GLU A1005 10036 8588 7791 -153 17 377 C ATOM 1680 C GLU A1005 13.589 -1.702 8.431 1.00 73.62 C ANISOU 1680 C GLU A1005 10557 9097 8316 -204 35 438 C ATOM 1681 O GLU A1005 13.814 -0.496 8.553 1.00 74.57 O ANISOU 1681 O GLU A1005 10738 9179 8415 -233 33 485 O ATOM 1682 CB GLU A1005 11.838 -2.858 9.825 1.00 69.74 C ANISOU 1682 CB GLU A1005 10052 8574 7873 -170 9 346 C ATOM 1683 CG GLU A1005 10.360 -3.121 9.993 1.00 70.71 C ANISOU 1683 CG GLU A1005 10170 8710 7985 -142 0 280 C ATOM 1684 CD GLU A1005 9.966 -3.543 11.393 1.00 87.87 C ANISOU 1684 CD GLU A1005 12354 10829 10204 -164 1 258 C ATOM 1685 OE1 GLU A1005 8.764 -3.411 11.715 1.00 67.14 O ANISOU 1685 OE1 GLU A1005 9728 8216 7567 -149 -7 213 O ATOM 1686 OE2 GLU A1005 10.842 -3.993 12.169 1.00 80.69 O ANISOU 1686 OE2 GLU A1005 11451 9875 9331 -187 12 285 O ATOM 1687 N MET A1006 14.547 -2.632 8.170 1.00 67.66 N ANISOU 1687 N MET A1006 9741 8384 7585 -215 61 432 N ATOM 1688 CA MET A1006 15.979 -2.355 7.981 1.00 66.34 C ANISOU 1688 CA MET A1006 9539 8247 7418 -263 84 473 C ATOM 1689 C MET A1006 16.208 -1.269 6.903 1.00 69.90 C ANISOU 1689 C MET A1006 10037 8706 7815 -287 112 516 C ATOM 1690 O MET A1006 16.942 -0.301 7.150 1.00 70.44 O ANISOU 1690 O MET A1006 10131 8755 7879 -361 128 554 O ATOM 1691 CB MET A1006 16.699 -3.648 7.579 1.00 67.92 C ANISOU 1691 CB MET A1006 9668 8507 7633 -232 112 450 C ATOM 1692 CG MET A1006 18.201 -3.536 7.515 1.00 70.53 C ANISOU 1692 CG MET A1006 9933 8901 7963 -269 134 479 C ATOM 1693 SD MET A1006 18.895 -4.929 6.602 1.00 73.32 S ANISOU 1693 SD MET A1006 10220 9331 8308 -201 178 454 S ATOM 1694 CE MET A1006 20.442 -5.057 7.411 1.00 70.43 C ANISOU 1694 CE MET A1006 9758 9047 7956 -212 176 470 C ATOM 1695 N LEU A1007 15.558 -1.415 5.728 1.00 64.96 N ANISOU 1695 N LEU A1007 9432 8109 7141 -228 125 504 N ATOM 1696 CA LEU A1007 15.689 -0.450 4.635 1.00 64.14 C ANISOU 1696 CA LEU A1007 9394 8008 6967 -227 159 550 C ATOM 1697 C LEU A1007 14.955 0.840 4.941 1.00 71.02 C ANISOU 1697 C LEU A1007 10380 8804 7802 -215 146 586 C ATOM 1698 O LEU A1007 15.439 1.896 4.540 1.00 73.62 O ANISOU 1698 O LEU A1007 10794 9091 8088 -253 190 642 O ATOM 1699 CB LEU A1007 15.221 -1.020 3.287 1.00 63.51 C ANISOU 1699 CB LEU A1007 9303 7998 6831 -149 171 524 C ATOM 1700 CG LEU A1007 16.170 -1.979 2.611 1.00 66.55 C ANISOU 1700 CG LEU A1007 9610 8451 7225 -159 209 508 C ATOM 1701 CD1 LEU A1007 15.493 -2.722 1.514 1.00 64.62 C ANISOU 1701 CD1 LEU A1007 9352 8269 6930 -84 209 457 C ATOM 1702 CD2 LEU A1007 17.452 -1.281 2.156 1.00 69.50 C ANISOU 1702 CD2 LEU A1007 9991 8836 7579 -227 267 568 C ATOM 1703 N ARG A1008 13.801 0.777 5.643 1.00 67.66 N ANISOU 1703 N ARG A1008 9967 8355 7386 -163 96 552 N ATOM 1704 CA ARG A1008 13.047 1.973 6.053 1.00 68.07 C ANISOU 1704 CA ARG A1008 10130 8335 7399 -131 82 582 C ATOM 1705 C ARG A1008 13.948 2.829 6.945 1.00 72.13 C ANISOU 1705 C ARG A1008 10696 8762 7946 -238 104 623 C ATOM 1706 O ARG A1008 13.935 4.052 6.840 1.00 73.02 O ANISOU 1706 O ARG A1008 10937 8797 8010 -248 135 671 O ATOM 1707 CB ARG A1008 11.732 1.586 6.787 1.00 68.55 C ANISOU 1707 CB ARG A1008 10162 8408 7474 -66 28 525 C ATOM 1708 CG ARG A1008 10.951 2.738 7.448 1.00 75.54 C ANISOU 1708 CG ARG A1008 11152 9223 8327 -22 10 549 C ATOM 1709 CD ARG A1008 10.610 3.858 6.472 1.00 82.93 C ANISOU 1709 CD ARG A1008 12212 10140 9156 67 33 603 C ATOM 1710 NE ARG A1008 9.845 4.947 7.082 1.00 83.78 N ANISOU 1710 NE ARG A1008 12437 10174 9222 132 21 627 N ATOM 1711 CZ ARG A1008 10.372 5.950 7.779 1.00 91.35 C ANISOU 1711 CZ ARG A1008 13514 11006 10190 66 53 675 C ATOM 1712 NH1 ARG A1008 11.679 5.981 8.031 1.00 72.78 N ANISOU 1712 NH1 ARG A1008 11155 8605 7893 -83 91 695 N ATOM 1713 NH2 ARG A1008 9.597 6.920 8.246 1.00 74.34 N ANISOU 1713 NH2 ARG A1008 11481 8780 7985 146 48 695 N ATOM 1714 N ILE A1009 14.740 2.172 7.798 1.00 68.05 N ANISOU 1714 N ILE A1009 10088 8264 7503 -316 93 599 N ATOM 1715 CA ILE A1009 15.709 2.817 8.672 1.00 68.26 C ANISOU 1715 CA ILE A1009 10128 8248 7560 -429 106 616 C ATOM 1716 C ILE A1009 16.836 3.451 7.822 1.00 75.90 C ANISOU 1716 C ILE A1009 11119 9223 8497 -518 176 653 C ATOM 1717 O ILE A1009 17.116 4.635 7.993 1.00 78.52 O ANISOU 1717 O ILE A1009 11557 9475 8804 -596 216 681 O ATOM 1718 CB ILE A1009 16.273 1.821 9.724 1.00 69.73 C ANISOU 1718 CB ILE A1009 10195 8485 7815 -459 70 576 C ATOM 1719 CG1 ILE A1009 15.203 1.411 10.751 1.00 69.06 C ANISOU 1719 CG1 ILE A1009 10118 8366 7756 -398 19 545 C ATOM 1720 CG2 ILE A1009 17.560 2.344 10.406 1.00 68.99 C ANISOU 1720 CG2 ILE A1009 10070 8404 7739 -582 83 578 C ATOM 1721 CD1 ILE A1009 15.489 0.070 11.488 1.00 67.94 C ANISOU 1721 CD1 ILE A1009 9877 8272 7663 -378 -4 510 C ATOM 1722 N ASP A1010 17.474 2.681 6.930 1.00 71.84 N ANISOU 1722 N ASP A1010 10516 8798 7981 -512 202 648 N ATOM 1723 CA ASP A1010 18.645 3.155 6.188 1.00 72.51 C ANISOU 1723 CA ASP A1010 10599 8912 8041 -608 276 675 C ATOM 1724 C ASP A1010 18.348 4.200 5.120 1.00 78.50 C ANISOU 1724 C ASP A1010 11510 9599 8718 -598 342 731 C ATOM 1725 O ASP A1010 19.144 5.128 4.953 1.00 79.04 O ANISOU 1725 O ASP A1010 11644 9624 8763 -716 418 759 O ATOM 1726 CB ASP A1010 19.398 1.975 5.566 1.00 73.69 C ANISOU 1726 CB ASP A1010 10608 9184 8207 -587 286 652 C ATOM 1727 CG ASP A1010 20.049 1.075 6.603 1.00 77.41 C ANISOU 1727 CG ASP A1010 10941 9728 8741 -602 243 609 C ATOM 1728 OD1 ASP A1010 20.340 1.559 7.708 1.00 77.75 O ANISOU 1728 OD1 ASP A1010 10980 9751 8811 -674 220 597 O ATOM 1729 OD2 ASP A1010 20.252 -0.113 6.310 1.00 79.32 O ANISOU 1729 OD2 ASP A1010 11093 10048 8998 -532 233 585 O ATOM 1730 N GLU A1011 17.227 4.046 4.396 1.00 75.04 N ANISOU 1730 N GLU A1011 11131 9154 8228 -458 320 743 N ATOM 1731 CA GLU A1011 16.832 4.930 3.306 1.00 74.68 C ANISOU 1731 CA GLU A1011 11237 9055 8082 -400 376 800 C ATOM 1732 C GLU A1011 15.953 6.087 3.771 1.00 79.93 C ANISOU 1732 C GLU A1011 12073 9595 8701 -353 373 833 C ATOM 1733 O GLU A1011 15.920 7.134 3.111 1.00 81.71 O ANISOU 1733 O GLU A1011 12469 9735 8840 -337 445 895 O ATOM 1734 CB GLU A1011 16.095 4.136 2.212 1.00 74.92 C ANISOU 1734 CB GLU A1011 11230 9177 8061 -255 348 785 C ATOM 1735 CG GLU A1011 16.888 2.999 1.599 1.00 77.49 C ANISOU 1735 CG GLU A1011 11413 9614 8415 -280 361 753 C ATOM 1736 CD GLU A1011 18.071 3.364 0.724 1.00 89.96 C ANISOU 1736 CD GLU A1011 13012 11208 9959 -363 457 796 C ATOM 1737 OE1 GLU A1011 18.315 4.570 0.502 1.00 85.24 O ANISOU 1737 OE1 GLU A1011 12557 10521 9308 -416 528 855 O ATOM 1738 OE2 GLU A1011 18.755 2.432 0.245 1.00 88.57 O ANISOU 1738 OE2 GLU A1011 12716 11131 9804 -374 470 768 O ATOM 1739 N GLY A1012 15.226 5.879 4.866 1.00 75.33 N ANISOU 1739 N GLY A1012 11456 8999 8166 -319 298 795 N ATOM 1740 CA GLY A1012 14.278 6.855 5.382 1.00 75.73 C ANISOU 1740 CA GLY A1012 11654 8948 8174 -249 286 817 C ATOM 1741 C GLY A1012 13.031 6.886 4.520 1.00 81.75 C ANISOU 1741 C GLY A1012 12469 9749 8841 -56 259 829 C ATOM 1742 O GLY A1012 12.837 6.006 3.673 1.00 79.76 O ANISOU 1742 O GLY A1012 12118 9614 8574 9 236 803 O ATOM 1743 N LEU A1013 12.167 7.886 4.738 1.00 82.00 N ANISOU 1743 N LEU A1013 12656 9696 8804 45 259 861 N ATOM 1744 CA LEU A1013 10.951 8.061 3.943 1.00 83.76 C ANISOU 1744 CA LEU A1013 12935 9977 8914 254 230 871 C ATOM 1745 C LEU A1013 10.772 9.516 3.610 1.00 91.38 C ANISOU 1745 C LEU A1013 14152 10803 9763 335 301 957 C ATOM 1746 O LEU A1013 10.888 10.378 4.477 1.00 92.89 O ANISOU 1746 O LEU A1013 14469 10855 9970 279 333 980 O ATOM 1747 CB LEU A1013 9.694 7.496 4.638 1.00 83.30 C ANISOU 1747 CB LEU A1013 12765 10008 8878 357 135 799 C ATOM 1748 CG LEU A1013 8.298 7.729 3.995 1.00 89.06 C ANISOU 1748 CG LEU A1013 13524 10832 9484 585 91 788 C ATOM 1749 CD1 LEU A1013 8.224 7.215 2.546 1.00 89.82 C ANISOU 1749 CD1 LEU A1013 13569 11059 9499 670 88 781 C ATOM 1750 CD2 LEU A1013 7.221 7.031 4.803 1.00 90.74 C ANISOU 1750 CD2 LEU A1013 13587 11148 9740 631 8 697 C ATOM 1751 N ARG A1014 10.551 9.786 2.334 1.00 89.39 N ANISOU 1751 N ARG A1014 13990 10585 9391 465 333 1005 N ATOM 1752 CA ARG A1014 10.299 11.120 1.816 1.00 91.28 C ANISOU 1752 CA ARG A1014 14498 10695 9490 587 410 1097 C ATOM 1753 C ARG A1014 9.213 10.977 0.772 1.00 95.96 C ANISOU 1753 C ARG A1014 15090 11429 9944 842 360 1100 C ATOM 1754 O ARG A1014 9.404 10.241 -0.186 1.00 95.35 O ANISOU 1754 O ARG A1014 14907 11478 9845 857 347 1081 O ATOM 1755 CB ARG A1014 11.579 11.776 1.252 1.00 92.83 C ANISOU 1755 CB ARG A1014 14849 10754 9666 437 547 1171 C ATOM 1756 CG ARG A1014 12.757 11.815 2.235 1.00104.88 C ANISOU 1756 CG ARG A1014 16330 12190 11328 164 591 1145 C ATOM 1757 CD ARG A1014 13.561 13.093 2.147 1.00124.97 C ANISOU 1757 CD ARG A1014 19129 14530 13825 40 739 1216 C ATOM 1758 NE ARG A1014 14.846 12.969 2.838 1.00135.03 N ANISOU 1758 NE ARG A1014 20308 15776 15220 -239 783 1173 N ATOM 1759 CZ ARG A1014 15.758 13.935 2.912 1.00148.52 C ANISOU 1759 CZ ARG A1014 22186 17330 16917 -423 916 1202 C ATOM 1760 NH1 ARG A1014 15.534 15.114 2.342 1.00132.52 N ANISOU 1760 NH1 ARG A1014 20461 15127 14762 -356 1033 1287 N ATOM 1761 NH2 ARG A1014 16.900 13.728 3.555 1.00136.29 N ANISOU 1761 NH2 ARG A1014 20506 15803 15473 -672 939 1143 N ATOM 1762 N LEU A1015 8.049 11.608 0.983 1.00 93.86 N ANISOU 1762 N LEU A1015 14918 11163 9580 1050 322 1110 N ATOM 1763 CA LEU A1015 6.940 11.519 0.031 1.00 95.18 C ANISOU 1763 CA LEU A1015 15070 11499 9596 1317 262 1101 C ATOM 1764 C LEU A1015 7.087 12.560 -1.132 1.00100.57 C ANISOU 1764 C LEU A1015 16026 12090 10096 1471 359 1219 C ATOM 1765 O LEU A1015 6.245 12.599 -2.043 1.00100.70 O ANISOU 1765 O LEU A1015 16057 12248 9958 1718 316 1224 O ATOM 1766 CB LEU A1015 5.584 11.654 0.750 1.00 95.69 C ANISOU 1766 CB LEU A1015 15085 11648 9627 1491 173 1047 C ATOM 1767 CG LEU A1015 5.166 10.505 1.697 1.00 99.44 C ANISOU 1767 CG LEU A1015 15280 12256 10247 1384 76 921 C ATOM 1768 CD1 LEU A1015 3.739 10.676 2.152 1.00100.36 C ANISOU 1768 CD1 LEU A1015 15344 12492 10295 1584 -2 867 C ATOM 1769 CD2 LEU A1015 5.286 9.148 1.039 1.00100.95 C ANISOU 1769 CD2 LEU A1015 15238 12633 10487 1315 26 837 C ATOM 1770 N LYS A1016 8.196 13.343 -1.120 1.00 97.09 N ANISOU 1770 N LYS A1016 15794 11425 9672 1316 493 1307 N ATOM 1771 CA LYS A1016 8.549 14.346 -2.132 1.00 98.40 C ANISOU 1771 CA LYS A1016 16252 11455 9680 1407 620 1427 C ATOM 1772 C LYS A1016 9.951 14.049 -2.694 1.00101.69 C ANISOU 1772 C LYS A1016 16654 11823 10162 1169 718 1450 C ATOM 1773 O LYS A1016 10.770 13.465 -1.990 1.00100.01 O ANISOU 1773 O LYS A1016 16276 11604 10119 916 712 1392 O ATOM 1774 CB LYS A1016 8.482 15.767 -1.536 1.00101.80 C ANISOU 1774 CB LYS A1016 17001 11631 10049 1444 720 1510 C ATOM 1775 N ILE A1017 10.220 14.439 -3.957 1.00 99.61 N ANISOU 1775 N ILE A1017 16557 11534 9754 1261 808 1534 N ATOM 1776 CA ILE A1017 11.502 14.209 -4.643 1.00 99.82 C ANISOU 1776 CA ILE A1017 16581 11529 9817 1059 914 1561 C ATOM 1777 C ILE A1017 12.672 14.895 -3.884 1.00105.13 C ANISOU 1777 C ILE A1017 17375 11976 10593 767 1048 1587 C ATOM 1778 O ILE A1017 12.527 16.018 -3.396 1.00106.52 O ANISOU 1778 O ILE A1017 17804 11949 10720 780 1128 1643 O ATOM 1779 CB ILE A1017 11.427 14.655 -6.144 1.00104.72 C ANISOU 1779 CB ILE A1017 17404 12152 10232 1249 996 1658 C ATOM 1780 CG1 ILE A1017 10.366 13.838 -6.922 1.00104.69 C ANISOU 1780 CG1 ILE A1017 17232 12416 10130 1511 851 1605 C ATOM 1781 CG2 ILE A1017 12.790 14.579 -6.853 1.00105.93 C ANISOU 1781 CG2 ILE A1017 17590 12249 10409 1034 1134 1696 C ATOM 1782 CD1 ILE A1017 10.045 14.356 -8.304 1.00111.85 C ANISOU 1782 CD1 ILE A1017 18348 13346 10803 1763 908 1699 C ATOM 1783 N TYR A1018 13.820 14.195 -3.790 1.00101.19 N ANISOU 1783 N TYR A1018 16689 11527 10231 507 1072 1536 N ATOM 1784 CA TYR A1018 15.045 14.666 -3.139 1.00101.49 C ANISOU 1784 CA TYR A1018 16776 11415 10372 204 1190 1533 C ATOM 1785 C TYR A1018 16.290 14.092 -3.824 1.00105.87 C ANISOU 1785 C TYR A1018 17203 12049 10975 14 1263 1520 C ATOM 1786 O TYR A1018 16.193 13.089 -4.526 1.00103.81 O ANISOU 1786 O TYR A1018 16759 11973 10711 98 1189 1491 O ATOM 1787 CB TYR A1018 15.047 14.310 -1.627 1.00101.06 C ANISOU 1787 CB TYR A1018 16541 11374 10481 69 1093 1440 C ATOM 1788 CG TYR A1018 15.193 12.838 -1.280 1.00100.00 C ANISOU 1788 CG TYR A1018 16052 11458 10486 12 957 1339 C ATOM 1789 CD1 TYR A1018 14.095 11.982 -1.305 1.00100.44 C ANISOU 1789 CD1 TYR A1018 15951 11674 10538 209 810 1292 C ATOM 1790 CD2 TYR A1018 16.410 12.322 -0.840 1.00100.10 C ANISOU 1790 CD2 TYR A1018 15890 11514 10629 -240 980 1283 C ATOM 1791 CE1 TYR A1018 14.216 10.634 -0.964 1.00 98.73 C ANISOU 1791 CE1 TYR A1018 15442 11628 10443 151 704 1199 C ATOM 1792 CE2 TYR A1018 16.543 10.976 -0.489 1.00 99.20 C ANISOU 1792 CE2 TYR A1018 15479 11582 10630 -270 864 1198 C ATOM 1793 CZ TYR A1018 15.440 10.135 -0.548 1.00105.40 C ANISOU 1793 CZ TYR A1018 16142 12494 11409 -77 733 1159 C ATOM 1794 OH TYR A1018 15.552 8.808 -0.191 1.00105.56 O ANISOU 1794 OH TYR A1018 15902 12667 11538 -111 637 1075 O ATOM 1795 N LYS A1019 17.459 14.714 -3.599 1.00105.24 N ANISOU 1795 N LYS A1019 17213 11838 10938 -249 1410 1531 N ATOM 1796 CA LYS A1019 18.732 14.217 -4.121 1.00106.30 C ANISOU 1796 CA LYS A1019 17206 12059 11125 -454 1488 1507 C ATOM 1797 C LYS A1019 19.352 13.281 -3.083 1.00111.31 C ANISOU 1797 C LYS A1019 17520 12831 11942 -634 1388 1393 C ATOM 1798 O LYS A1019 19.260 13.549 -1.880 1.00110.90 O ANISOU 1798 O LYS A1019 17451 12715 11969 -718 1346 1348 O ATOM 1799 CB LYS A1019 19.679 15.370 -4.474 1.00111.23 C ANISOU 1799 CB LYS A1019 18083 12492 11689 -653 1710 1568 C ATOM 1800 N ASP A1020 19.942 12.165 -3.530 1.00108.31 N ANISOU 1800 N ASP A1020 16894 12641 11619 -671 1348 1345 N ATOM 1801 CA ASP A1020 20.544 11.210 -2.600 1.00107.20 C ANISOU 1801 CA ASP A1020 16457 12640 11633 -806 1256 1244 C ATOM 1802 C ASP A1020 22.000 11.641 -2.274 1.00115.15 C ANISOU 1802 C ASP A1020 17427 13627 12697 -1104 1382 1212 C ATOM 1803 O ASP A1020 22.360 12.808 -2.501 1.00116.22 O ANISOU 1803 O ASP A1020 17792 13599 12766 -1223 1536 1261 O ATOM 1804 CB ASP A1020 20.450 9.760 -3.152 1.00107.07 C ANISOU 1804 CB ASP A1020 16202 12834 11648 -689 1152 1200 C ATOM 1805 CG ASP A1020 21.342 9.385 -4.329 1.00115.34 C ANISOU 1805 CG ASP A1020 17195 13976 12654 -736 1244 1216 C ATOM 1806 OD1 ASP A1020 21.961 10.300 -4.928 1.00118.03 O ANISOU 1806 OD1 ASP A1020 17707 14217 12920 -842 1402 1275 O ATOM 1807 OD2 ASP A1020 21.412 8.173 -4.661 1.00116.55 O ANISOU 1807 OD2 ASP A1020 17146 14294 12844 -668 1167 1168 O ATOM 1808 N THR A1021 22.823 10.702 -1.740 1.00113.03 N ANISOU 1808 N THR A1021 16873 13530 12544 -1220 1321 1125 N ATOM 1809 CA THR A1021 24.242 10.899 -1.394 1.00114.89 C ANISOU 1809 CA THR A1021 16997 13819 12837 -1492 1415 1068 C ATOM 1810 C THR A1021 25.034 11.424 -2.616 1.00121.60 C ANISOU 1810 C THR A1021 17957 14644 13601 -1598 1599 1118 C ATOM 1811 O THR A1021 25.836 12.351 -2.480 1.00122.75 O ANISOU 1811 O THR A1021 18198 14706 13737 -1831 1744 1108 O ATOM 1812 CB THR A1021 24.848 9.563 -0.890 1.00124.96 C ANISOU 1812 CB THR A1021 17937 15324 14220 -1505 1302 979 C ATOM 1813 OG1 THR A1021 23.969 8.946 0.058 1.00125.71 O ANISOU 1813 OG1 THR A1021 17952 15435 14377 -1368 1139 947 O ATOM 1814 CG2 THR A1021 26.246 9.729 -0.291 1.00124.96 C ANISOU 1814 CG2 THR A1021 17779 15419 14279 -1767 1367 900 C ATOM 1815 N GLU A1022 24.765 10.830 -3.802 1.00118.02 N ANISOU 1815 N GLU A1022 17498 14262 13080 -1429 1596 1167 N ATOM 1816 CA GLU A1022 25.404 11.110 -5.089 1.00119.26 C ANISOU 1816 CA GLU A1022 17747 14422 13146 -1480 1755 1220 C ATOM 1817 C GLU A1022 24.665 12.194 -5.913 1.00123.44 C ANISOU 1817 C GLU A1022 18635 14741 13525 -1372 1863 1336 C ATOM 1818 O GLU A1022 25.025 12.432 -7.074 1.00124.63 O ANISOU 1818 O GLU A1022 18899 14878 13576 -1372 1995 1397 O ATOM 1819 CB GLU A1022 25.509 9.816 -5.919 1.00119.72 C ANISOU 1819 CB GLU A1022 17604 14682 13204 -1340 1687 1204 C ATOM 1820 CG GLU A1022 25.775 8.551 -5.116 1.00127.93 C ANISOU 1820 CG GLU A1022 18328 15910 14371 -1329 1538 1105 C ATOM 1821 CD GLU A1022 26.817 7.622 -5.705 1.00150.58 C ANISOU 1821 CD GLU A1022 20974 18980 17261 -1370 1568 1061 C ATOM 1822 OE1 GLU A1022 26.801 7.401 -6.938 1.00150.77 O ANISOU 1822 OE1 GLU A1022 21051 19037 17200 -1278 1626 1107 O ATOM 1823 OE2 GLU A1022 27.643 7.099 -4.923 1.00143.92 O ANISOU 1823 OE2 GLU A1022 19901 18271 16512 -1480 1530 980 O ATOM 1824 N GLY A1023 23.660 12.834 -5.311 1.00118.09 N ANISOU 1824 N GLY A1023 18138 13906 12824 -1269 1811 1368 N ATOM 1825 CA GLY A1023 22.876 13.885 -5.958 1.00118.35 C ANISOU 1825 CA GLY A1023 18526 13736 12705 -1128 1902 1480 C ATOM 1826 C GLY A1023 21.898 13.427 -7.028 1.00119.21 C ANISOU 1826 C GLY A1023 18687 13910 12698 -819 1831 1543 C ATOM 1827 O GLY A1023 21.476 14.233 -7.864 1.00119.62 O ANISOU 1827 O GLY A1023 19028 13828 12594 -694 1933 1645 O ATOM 1828 N TYR A1024 21.523 12.130 -7.003 1.00112.39 N ANISOU 1828 N TYR A1024 17553 13251 11899 -691 1659 1478 N ATOM 1829 CA TYR A1024 20.569 11.528 -7.931 1.00110.76 C ANISOU 1829 CA TYR A1024 17342 13146 11594 -413 1567 1504 C ATOM 1830 C TYR A1024 19.150 11.677 -7.394 1.00110.34 C ANISOU 1830 C TYR A1024 17355 13057 11513 -198 1432 1507 C ATOM 1831 O TYR A1024 18.931 11.460 -6.199 1.00109.90 O ANISOU 1831 O TYR A1024 17178 13002 11576 -254 1336 1442 O ATOM 1832 CB TYR A1024 20.900 10.045 -8.163 1.00111.28 C ANISOU 1832 CB TYR A1024 17095 13443 11744 -406 1466 1420 C ATOM 1833 CG TYR A1024 22.227 9.784 -8.847 1.00115.87 C ANISOU 1833 CG TYR A1024 17592 14098 12334 -571 1590 1416 C ATOM 1834 CD1 TYR A1024 22.614 10.517 -9.969 1.00120.39 C ANISOU 1834 CD1 TYR A1024 18376 14595 12771 -581 1758 1504 C ATOM 1835 CD2 TYR A1024 23.052 8.742 -8.433 1.00116.12 C ANISOU 1835 CD2 TYR A1024 17334 14290 12497 -692 1540 1325 C ATOM 1836 CE1 TYR A1024 23.819 10.257 -10.624 1.00123.09 C ANISOU 1836 CE1 TYR A1024 18631 15021 13118 -733 1879 1495 C ATOM 1837 CE2 TYR A1024 24.258 8.469 -9.083 1.00118.41 C ANISOU 1837 CE2 TYR A1024 17529 14673 12788 -825 1652 1315 C ATOM 1838 CZ TYR A1024 24.638 9.231 -10.178 1.00129.79 C ANISOU 1838 CZ TYR A1024 19171 16042 14101 -853 1822 1397 C ATOM 1839 OH TYR A1024 25.829 8.971 -10.818 1.00132.45 O ANISOU 1839 OH TYR A1024 19407 16481 14437 -991 1942 1384 O ATOM 1840 N TYR A1025 18.184 12.040 -8.265 1.00103.91 N ANISOU 1840 N TYR A1025 16724 12224 10534 56 1425 1577 N ATOM 1841 CA TYR A1025 16.788 12.222 -7.866 1.00101.81 C ANISOU 1841 CA TYR A1025 16516 11951 10216 286 1302 1577 C ATOM 1842 C TYR A1025 16.175 10.909 -7.388 1.00101.04 C ANISOU 1842 C TYR A1025 16113 12055 10225 351 1111 1463 C ATOM 1843 O TYR A1025 16.208 9.891 -8.086 1.00100.70 O ANISOU 1843 O TYR A1025 15899 12183 10179 401 1056 1416 O ATOM 1844 CB TYR A1025 15.956 12.851 -8.978 1.00104.54 C ANISOU 1844 CB TYR A1025 17106 12270 10344 561 1335 1671 C ATOM 1845 CG TYR A1025 16.327 14.296 -9.226 1.00109.01 C ANISOU 1845 CG TYR A1025 18037 12586 10795 526 1528 1792 C ATOM 1846 CD1 TYR A1025 15.840 15.313 -8.408 1.00112.12 C ANISOU 1846 CD1 TYR A1025 18639 12791 11169 557 1555 1830 C ATOM 1847 CD2 TYR A1025 17.210 14.645 -10.245 1.00110.63 C ANISOU 1847 CD2 TYR A1025 18389 12732 10915 444 1699 1865 C ATOM 1848 CE1 TYR A1025 16.193 16.644 -8.620 1.00115.40 C ANISOU 1848 CE1 TYR A1025 19419 12951 11477 514 1750 1938 C ATOM 1849 CE2 TYR A1025 17.591 15.969 -10.449 1.00113.47 C ANISOU 1849 CE2 TYR A1025 19103 12840 11170 385 1900 1973 C ATOM 1850 CZ TYR A1025 17.070 16.967 -9.642 1.00122.80 C ANISOU 1850 CZ TYR A1025 20506 13822 12329 421 1927 2009 C ATOM 1851 OH TYR A1025 17.432 18.279 -9.840 1.00129.54 O ANISOU 1851 OH TYR A1025 21740 14404 13073 359 2140 2113 O ATOM 1852 N THR A1026 15.681 10.951 -6.148 1.00 93.16 N ANISOU 1852 N THR A1026 15056 11019 9321 329 1025 1416 N ATOM 1853 CA THR A1026 15.097 9.855 -5.396 1.00 89.94 C ANISOU 1853 CA THR A1026 14391 10756 9028 355 864 1310 C ATOM 1854 C THR A1026 13.725 10.275 -4.805 1.00 91.91 C ANISOU 1854 C THR A1026 14710 10983 9230 541 772 1304 C ATOM 1855 O THR A1026 13.432 11.464 -4.699 1.00 91.32 O ANISOU 1855 O THR A1026 14879 10753 9066 609 837 1382 O ATOM 1856 CB THR A1026 16.110 9.454 -4.291 1.00 91.36 C ANISOU 1856 CB THR A1026 14410 10915 9388 98 869 1252 C ATOM 1857 OG1 THR A1026 17.417 9.352 -4.859 1.00 90.52 O ANISOU 1857 OG1 THR A1026 14276 10818 9300 -67 979 1268 O ATOM 1858 CG2 THR A1026 15.759 8.150 -3.599 1.00 83.19 C ANISOU 1858 CG2 THR A1026 13109 10026 8475 101 728 1146 C ATOM 1859 N ILE A1027 12.893 9.283 -4.438 1.00 87.70 N ANISOU 1859 N ILE A1027 13965 10606 8750 622 629 1210 N ATOM 1860 CA ILE A1027 11.596 9.452 -3.769 1.00 87.34 C ANISOU 1860 CA ILE A1027 13916 10586 8683 777 529 1177 C ATOM 1861 C ILE A1027 11.316 8.208 -2.891 1.00 89.38 C ANISOU 1861 C ILE A1027 13903 10967 9091 701 413 1056 C ATOM 1862 O ILE A1027 11.917 7.152 -3.114 1.00 90.06 O ANISOU 1862 O ILE A1027 13818 11144 9255 596 401 1002 O ATOM 1863 CB ILE A1027 10.427 9.751 -4.760 1.00 91.22 C ANISOU 1863 CB ILE A1027 14498 11179 8984 1068 487 1199 C ATOM 1864 CG1 ILE A1027 9.219 10.381 -3.999 1.00 91.77 C ANISOU 1864 CG1 ILE A1027 14634 11228 9007 1232 422 1194 C ATOM 1865 CG2 ILE A1027 10.018 8.481 -5.546 1.00 90.52 C ANISOU 1865 CG2 ILE A1027 14187 11327 8878 1138 396 1104 C ATOM 1866 CD1 ILE A1027 8.477 11.419 -4.693 1.00104.52 C ANISOU 1866 CD1 ILE A1027 16479 12815 10417 1493 450 1277 C ATOM 1867 N GLY A1028 10.391 8.342 -1.940 1.00 82.86 N ANISOU 1867 N GLY A1028 13054 10140 8291 765 339 1018 N ATOM 1868 CA GLY A1028 9.958 7.261 -1.064 1.00 80.30 C ANISOU 1868 CA GLY A1028 12505 9916 8088 710 242 910 C ATOM 1869 C GLY A1028 11.059 6.717 -0.184 1.00 82.01 C ANISOU 1869 C GLY A1028 12620 10072 8468 480 264 886 C ATOM 1870 O GLY A1028 11.725 7.459 0.552 1.00 80.63 O ANISOU 1870 O GLY A1028 12543 9752 8341 362 319 932 O ATOM 1871 N ILE A1029 11.252 5.403 -0.266 1.00 77.71 N ANISOU 1871 N ILE A1029 11882 9645 8001 420 222 808 N ATOM 1872 CA ILE A1029 12.260 4.726 0.527 1.00 76.04 C ANISOU 1872 CA ILE A1029 11557 9405 7928 238 233 780 C ATOM 1873 C ILE A1029 13.351 4.285 -0.450 1.00 80.88 C ANISOU 1873 C ILE A1029 12134 10060 8536 172 295 797 C ATOM 1874 O ILE A1029 13.314 3.179 -1.020 1.00 79.35 O ANISOU 1874 O ILE A1029 11816 9981 8352 195 268 738 O ATOM 1875 CB ILE A1029 11.665 3.595 1.406 1.00 77.55 C ANISOU 1875 CB ILE A1029 11582 9668 8214 224 153 683 C ATOM 1876 CG1 ILE A1029 10.477 4.106 2.245 1.00 77.17 C ANISOU 1876 CG1 ILE A1029 11573 9596 8151 307 99 665 C ATOM 1877 CG2 ILE A1029 12.726 2.968 2.305 1.00 77.92 C ANISOU 1877 CG2 ILE A1029 11537 9680 8388 66 165 665 C ATOM 1878 CD1 ILE A1029 9.253 3.357 2.037 1.00 82.24 C ANISOU 1878 CD1 ILE A1029 12109 10375 8765 411 32 577 C ATOM 1879 N GLY A1030 14.265 5.230 -0.685 1.00 78.33 N ANISOU 1879 N GLY A1030 11937 9638 8186 93 387 876 N ATOM 1880 CA GLY A1030 15.435 5.066 -1.534 1.00 78.38 C ANISOU 1880 CA GLY A1030 11929 9669 8182 9 468 904 C ATOM 1881 C GLY A1030 15.151 4.619 -2.946 1.00 82.81 C ANISOU 1881 C GLY A1030 12485 10335 8644 130 473 902 C ATOM 1882 O GLY A1030 15.954 3.881 -3.522 1.00 83.88 O ANISOU 1882 O GLY A1030 12526 10544 8801 75 505 883 O ATOM 1883 N HIS A1031 14.016 5.062 -3.517 1.00 77.92 N ANISOU 1883 N HIS A1031 11965 9736 7906 305 441 918 N ATOM 1884 CA HIS A1031 13.668 4.741 -4.890 1.00 76.59 C ANISOU 1884 CA HIS A1031 11803 9679 7618 438 440 914 C ATOM 1885 C HIS A1031 14.264 5.781 -5.835 1.00 81.48 C ANISOU 1885 C HIS A1031 12619 10219 8120 455 556 1023 C ATOM 1886 O HIS A1031 13.717 6.876 -5.978 1.00 81.97 O ANISOU 1886 O HIS A1031 12872 10198 8076 564 582 1093 O ATOM 1887 CB HIS A1031 12.153 4.624 -5.100 1.00 76.72 C ANISOU 1887 CB HIS A1031 11804 9799 7547 633 341 863 C ATOM 1888 CG HIS A1031 11.821 4.214 -6.497 1.00 80.83 C ANISOU 1888 CG HIS A1031 12311 10462 7940 764 331 841 C ATOM 1889 ND1 HIS A1031 11.721 2.881 -6.849 1.00 81.92 N ANISOU 1889 ND1 HIS A1031 12269 10741 8115 746 280 734 N ATOM 1890 CD2 HIS A1031 11.676 4.972 -7.609 1.00 84.24 C ANISOU 1890 CD2 HIS A1031 12900 10903 8205 907 375 915 C ATOM 1891 CE1 HIS A1031 11.489 2.868 -8.148 1.00 82.75 C ANISOU 1891 CE1 HIS A1031 12413 10950 8078 873 286 736 C ATOM 1892 NE2 HIS A1031 11.445 4.104 -8.648 1.00 84.55 N ANISOU 1892 NE2 HIS A1031 12841 11109 8176 981 340 847 N ATOM 1893 N LEU A1032 15.373 5.425 -6.495 1.00 78.57 N ANISOU 1893 N LEU A1032 12214 9875 7765 355 633 1037 N ATOM 1894 CA LEU A1032 16.029 6.275 -7.484 1.00 80.35 C ANISOU 1894 CA LEU A1032 12616 10035 7879 350 761 1134 C ATOM 1895 C LEU A1032 15.113 6.415 -8.701 1.00 85.63 C ANISOU 1895 C LEU A1032 13384 10784 8370 580 739 1157 C ATOM 1896 O LEU A1032 14.657 5.409 -9.246 1.00 85.01 O ANISOU 1896 O LEU A1032 13165 10865 8271 668 661 1080 O ATOM 1897 CB LEU A1032 17.389 5.677 -7.880 1.00 80.67 C ANISOU 1897 CB LEU A1032 12549 10123 7980 193 840 1123 C ATOM 1898 CG LEU A1032 18.201 6.482 -8.875 1.00 88.38 C ANISOU 1898 CG LEU A1032 13691 11036 8852 152 992 1216 C ATOM 1899 CD1 LEU A1032 19.639 6.583 -8.441 1.00 89.45 C ANISOU 1899 CD1 LEU A1032 13765 11132 9091 -89 1093 1218 C ATOM 1900 CD2 LEU A1032 18.131 5.868 -10.241 1.00 93.64 C ANISOU 1900 CD2 LEU A1032 14334 11831 9412 274 998 1210 C ATOM 1901 N LEU A1033 14.839 7.659 -9.106 1.00 83.27 N ANISOU 1901 N LEU A1033 13333 10373 7933 682 811 1260 N ATOM 1902 CA LEU A1033 13.977 7.962 -10.243 1.00 84.03 C ANISOU 1902 CA LEU A1033 13553 10542 7832 930 796 1297 C ATOM 1903 C LEU A1033 14.773 8.053 -11.558 1.00 92.98 C ANISOU 1903 C LEU A1033 14783 11688 8857 930 913 1361 C ATOM 1904 O LEU A1033 14.272 7.632 -12.612 1.00 92.60 O ANISOU 1904 O LEU A1033 14716 11786 8681 1100 870 1341 O ATOM 1905 CB LEU A1033 13.229 9.280 -9.998 1.00 84.42 C ANISOU 1905 CB LEU A1033 13850 10458 7768 1077 819 1384 C ATOM 1906 CG LEU A1033 12.131 9.227 -8.963 1.00 87.34 C ANISOU 1906 CG LEU A1033 14139 10858 8187 1159 691 1321 C ATOM 1907 CD1 LEU A1033 11.814 10.615 -8.406 1.00 87.46 C ANISOU 1907 CD1 LEU A1033 14413 10679 8141 1223 752 1415 C ATOM 1908 CD2 LEU A1033 10.913 8.498 -9.494 1.00 89.65 C ANISOU 1908 CD2 LEU A1033 14291 11381 8391 1375 552 1233 C ATOM 1909 N THR A1034 15.993 8.645 -11.498 1.00 92.21 N ANISOU 1909 N THR A1034 14792 11443 8801 736 1065 1433 N ATOM 1910 CA THR A1034 16.856 8.865 -12.662 1.00 94.13 C ANISOU 1910 CA THR A1034 15145 11673 8945 705 1206 1503 C ATOM 1911 C THR A1034 18.223 9.403 -12.244 1.00100.50 C ANISOU 1911 C THR A1034 16004 12335 9847 430 1364 1545 C ATOM 1912 O THR A1034 18.344 10.098 -11.233 1.00100.09 O ANISOU 1912 O THR A1034 16023 12138 9870 313 1393 1561 O ATOM 1913 CB THR A1034 16.175 9.835 -13.696 1.00100.54 C ANISOU 1913 CB THR A1034 16247 12434 9519 948 1265 1613 C ATOM 1914 OG1 THR A1034 16.931 9.870 -14.910 1.00101.87 O ANISOU 1914 OG1 THR A1034 16504 12619 9582 936 1392 1671 O ATOM 1915 CG2 THR A1034 15.943 11.257 -13.154 1.00 97.46 C ANISOU 1915 CG2 THR A1034 16142 11816 9074 967 1351 1714 C ATOM 1916 N LYS A1035 19.241 9.119 -13.061 1.00 99.74 N ANISOU 1916 N LYS A1035 15876 12286 9734 329 1471 1559 N ATOM 1917 CA LYS A1035 20.582 9.651 -12.862 1.00101.43 C ANISOU 1917 CA LYS A1035 16133 12394 10011 66 1639 1592 C ATOM 1918 C LYS A1035 20.682 11.022 -13.593 1.00110.10 C ANISOU 1918 C LYS A1035 17587 13307 10938 93 1823 1727 C ATOM 1919 O LYS A1035 21.621 11.786 -13.342 1.00111.97 O ANISOU 1919 O LYS A1035 17932 13406 11207 -133 1986 1763 O ATOM 1920 CB LYS A1035 21.652 8.650 -13.332 1.00103.55 C ANISOU 1920 CB LYS A1035 16179 12819 10346 -57 1671 1534 C ATOM 1921 CG LYS A1035 21.876 7.482 -12.371 1.00114.86 C ANISOU 1921 CG LYS A1035 17298 14379 11964 -143 1538 1412 C ATOM 1922 CD LYS A1035 22.514 6.293 -13.099 1.00125.78 C ANISOU 1922 CD LYS A1035 18481 15944 13365 -144 1532 1354 C ATOM 1923 CE LYS A1035 22.387 4.981 -12.355 1.00130.12 C ANISOU 1923 CE LYS A1035 18762 16622 14056 -137 1381 1239 C ATOM 1924 NZ LYS A1035 22.537 3.812 -13.270 1.00135.02 N ANISOU 1924 NZ LYS A1035 19251 17404 14647 -48 1354 1185 N ATOM 1925 N SER A1036 19.675 11.341 -14.455 1.00107.58 N ANISOU 1925 N SER A1036 17456 12987 10431 372 1797 1794 N ATOM 1926 CA SER A1036 19.560 12.600 -15.202 1.00110.01 C ANISOU 1926 CA SER A1036 18137 13118 10545 469 1959 1933 C ATOM 1927 C SER A1036 19.492 13.804 -14.248 1.00115.82 C ANISOU 1927 C SER A1036 19095 13608 11304 374 2040 1985 C ATOM 1928 O SER A1036 18.784 13.736 -13.237 1.00114.10 O ANISOU 1928 O SER A1036 18796 13386 11170 419 1905 1934 O ATOM 1929 CB SER A1036 18.331 12.587 -16.110 1.00113.75 C ANISOU 1929 CB SER A1036 18725 13678 10817 829 1869 1975 C ATOM 1930 OG SER A1036 18.190 13.789 -16.850 1.00124.16 O ANISOU 1930 OG SER A1036 20425 14823 11926 959 2026 2118 O ATOM 1931 N PRO A1037 20.200 14.921 -14.553 1.00114.94 N ANISOU 1931 N PRO A1037 19276 13281 11113 241 2269 2084 N ATOM 1932 CA PRO A1037 20.168 16.073 -13.645 1.00115.48 C ANISOU 1932 CA PRO A1037 19575 13099 11201 133 2360 2124 C ATOM 1933 C PRO A1037 18.981 16.993 -13.930 1.00120.10 C ANISOU 1933 C PRO A1037 20500 13544 11590 447 2363 2233 C ATOM 1934 O PRO A1037 19.079 18.211 -13.770 1.00122.95 O ANISOU 1934 O PRO A1037 21200 13642 11873 401 2530 2320 O ATOM 1935 CB PRO A1037 21.518 16.760 -13.903 1.00119.13 C ANISOU 1935 CB PRO A1037 20186 13410 11667 -176 2618 2163 C ATOM 1936 CG PRO A1037 22.113 16.091 -15.120 1.00124.15 C ANISOU 1936 CG PRO A1037 20722 14207 12242 -167 2671 2173 C ATOM 1937 CD PRO A1037 21.082 15.189 -15.703 1.00118.46 C ANISOU 1937 CD PRO A1037 19866 13694 11449 162 2469 2157 C ATOM 1938 N SER A1038 17.851 16.407 -14.334 1.00113.90 N ANISOU 1938 N SER A1038 19622 12938 10719 769 2181 2219 N ATOM 1939 CA SER A1038 16.649 17.156 -14.666 1.00114.11 C ANISOU 1939 CA SER A1038 19926 12891 10540 1116 2156 2311 C ATOM 1940 C SER A1038 15.508 16.740 -13.764 1.00113.90 C ANISOU 1940 C SER A1038 19712 12984 10583 1275 1930 2227 C ATOM 1941 O SER A1038 15.206 15.550 -13.672 1.00111.76 O ANISOU 1941 O SER A1038 19098 12959 10407 1300 1749 2114 O ATOM 1942 CB SER A1038 16.286 16.952 -16.136 1.00117.95 C ANISOU 1942 CB SER A1038 20498 13508 10810 1388 2158 2375 C ATOM 1943 OG SER A1038 14.944 17.314 -16.425 1.00124.60 O ANISOU 1943 OG SER A1038 21487 14393 11461 1777 2057 2423 O ATOM 1944 N LEU A1039 14.872 17.726 -13.106 1.00109.87 N ANISOU 1944 N LEU A1039 19437 12290 10018 1381 1951 2280 N ATOM 1945 CA LEU A1039 13.728 17.520 -12.217 1.00108.07 C ANISOU 1945 CA LEU A1039 19076 12152 9835 1547 1759 2212 C ATOM 1946 C LEU A1039 12.492 17.078 -13.026 1.00111.56 C ANISOU 1946 C LEU A1039 19451 12833 10104 1934 1601 2204 C ATOM 1947 O LEU A1039 11.673 16.297 -12.525 1.00109.12 O ANISOU 1947 O LEU A1039 18864 12728 9868 2023 1403 2094 O ATOM 1948 CB LEU A1039 13.445 18.801 -11.417 1.00109.30 C ANISOU 1948 CB LEU A1039 19546 12031 9952 1569 1853 2282 C ATOM 1949 CG LEU A1039 12.296 18.761 -10.423 1.00113.03 C ANISOU 1949 CG LEU A1039 19919 12566 10463 1736 1681 2222 C ATOM 1950 CD1 LEU A1039 12.598 17.836 -9.260 1.00110.94 C ANISOU 1950 CD1 LEU A1039 19285 12408 10460 1475 1556 2079 C ATOM 1951 CD2 LEU A1039 11.973 20.139 -9.933 1.00117.64 C ANISOU 1951 CD2 LEU A1039 20885 12865 10947 1825 1800 2316 C ATOM 1952 N ASN A1040 12.384 17.562 -14.285 1.00110.07 N ANISOU 1952 N ASN A1040 19513 12627 9681 2152 1696 2315 N ATOM 1953 CA ASN A1040 11.320 17.204 -15.225 1.00110.28 C ANISOU 1953 CA ASN A1040 19496 12898 9509 2524 1563 2310 C ATOM 1954 C ASN A1040 11.436 15.712 -15.561 1.00109.73 C ANISOU 1954 C ASN A1040 19017 13126 9549 2438 1415 2171 C ATOM 1955 O ASN A1040 10.436 14.989 -15.474 1.00108.22 O ANISOU 1955 O ASN A1040 18585 13182 9351 2608 1219 2065 O ATOM 1956 CB ASN A1040 11.393 18.071 -16.495 1.00116.91 C ANISOU 1956 CB ASN A1040 20716 13630 10074 2745 1723 2468 C ATOM 1957 CG ASN A1040 11.305 19.561 -16.259 1.00150.24 C ANISOU 1957 CG ASN A1040 25392 17529 14165 2841 1896 2615 C ATOM 1958 OD1 ASN A1040 11.934 20.124 -15.349 1.00142.84 O ANISOU 1958 OD1 ASN A1040 24565 16339 13368 2575 2015 2630 O ATOM 1959 ND2 ASN A1040 10.564 20.244 -17.118 1.00149.09 N ANISOU 1959 ND2 ASN A1040 25536 17378 13732 3227 1927 2728 N ATOM 1960 N ALA A1041 12.681 15.249 -15.876 1.00103.79 N ANISOU 1960 N ALA A1041 18184 12345 8907 2155 1518 2162 N ATOM 1961 CA ALA A1041 13.016 13.854 -16.175 1.00101.26 C ANISOU 1961 CA ALA A1041 17508 12263 8703 2036 1414 2037 C ATOM 1962 C ALA A1041 12.620 12.958 -15.003 1.00104.20 C ANISOU 1962 C ALA A1041 17545 12757 9290 1925 1237 1889 C ATOM 1963 O ALA A1041 12.007 11.918 -15.230 1.00103.48 O ANISOU 1963 O ALA A1041 17195 12913 9209 2018 1078 1775 O ATOM 1964 CB ALA A1041 14.503 13.718 -16.466 1.00101.64 C ANISOU 1964 CB ALA A1041 17557 12215 8846 1734 1579 2063 C ATOM 1965 N ALA A1042 12.918 13.404 -13.751 1.00 99.99 N ANISOU 1965 N ALA A1042 17035 12044 8914 1733 1272 1889 N ATOM 1966 CA ALA A1042 12.602 12.739 -12.482 1.00 97.29 C ANISOU 1966 CA ALA A1042 16426 11767 8773 1616 1131 1768 C ATOM 1967 C ALA A1042 11.096 12.708 -12.220 1.00101.11 C ANISOU 1967 C ALA A1042 16858 12386 9175 1894 969 1720 C ATOM 1968 O ALA A1042 10.611 11.728 -11.658 1.00 97.91 O ANISOU 1968 O ALA A1042 16163 12148 8888 1862 819 1591 O ATOM 1969 CB ALA A1042 13.306 13.443 -11.342 1.00 97.53 C ANISOU 1969 CB ALA A1042 16556 11558 8944 1372 1231 1799 C ATOM 1970 N LYS A1043 10.359 13.774 -12.631 1.00100.82 N ANISOU 1970 N LYS A1043 17103 12279 8927 2170 1005 1821 N ATOM 1971 CA LYS A1043 8.904 13.855 -12.482 1.00101.33 C ANISOU 1971 CA LYS A1043 17128 12495 8878 2471 858 1780 C ATOM 1972 C LYS A1043 8.206 12.973 -13.525 1.00107.63 C ANISOU 1972 C LYS A1043 17736 13606 9551 2675 729 1698 C ATOM 1973 O LYS A1043 7.143 12.417 -13.241 1.00107.20 O ANISOU 1973 O LYS A1043 17466 13769 9494 2806 566 1584 O ATOM 1974 CB LYS A1043 8.414 15.298 -12.589 1.00105.60 C ANISOU 1974 CB LYS A1043 18047 12856 9221 2718 949 1920 C ATOM 1975 CG LYS A1043 8.366 16.023 -11.255 1.00116.93 C ANISOU 1975 CG LYS A1043 19587 14074 10765 2618 983 1939 C ATOM 1976 CD LYS A1043 7.583 17.325 -11.366 1.00126.65 C ANISOU 1976 CD LYS A1043 21169 15174 11777 2934 1039 2056 C ATOM 1977 CE LYS A1043 7.601 18.135 -10.093 1.00129.98 C ANISOU 1977 CE LYS A1043 21740 15352 12295 2832 1096 2082 C ATOM 1978 NZ LYS A1043 6.682 19.303 -10.173 1.00134.96 N ANISOU 1978 NZ LYS A1043 22693 15882 12702 3185 1131 2183 N ATOM 1979 N SER A1044 8.801 12.837 -14.726 1.00105.64 N ANISOU 1979 N SER A1044 17559 13387 9194 2692 806 1747 N ATOM 1980 CA SER A1044 8.246 11.986 -15.782 1.00106.06 C ANISOU 1980 CA SER A1044 17439 13736 9122 2865 693 1663 C ATOM 1981 C SER A1044 8.292 10.535 -15.316 1.00107.67 C ANISOU 1981 C SER A1044 17258 14117 9535 2655 570 1486 C ATOM 1982 O SER A1044 7.248 9.878 -15.235 1.00106.92 O ANISOU 1982 O SER A1044 16944 14261 9419 2777 411 1356 O ATOM 1983 CB SER A1044 9.018 12.166 -17.084 1.00110.80 C ANISOU 1983 CB SER A1044 18216 14302 9580 2894 822 1759 C ATOM 1984 OG SER A1044 9.092 13.538 -17.423 1.00125.36 O ANISOU 1984 OG SER A1044 20454 15933 11244 3054 968 1934 O ATOM 1985 N GLU A1045 9.507 10.085 -14.913 1.00101.84 N ANISOU 1985 N GLU A1045 16446 13250 9000 2334 652 1480 N ATOM 1986 CA GLU A1045 9.812 8.760 -14.395 1.00 98.68 C ANISOU 1986 CA GLU A1045 15729 12956 8811 2108 573 1337 C ATOM 1987 C GLU A1045 8.930 8.448 -13.208 1.00101.09 C ANISOU 1987 C GLU A1045 15861 13318 9232 2098 445 1235 C ATOM 1988 O GLU A1045 8.484 7.308 -13.087 1.00100.35 O ANISOU 1988 O GLU A1045 15505 13412 9213 2059 330 1089 O ATOM 1989 CB GLU A1045 11.298 8.646 -14.016 1.00 99.04 C ANISOU 1989 CB GLU A1045 15777 12820 9032 1798 702 1378 C ATOM 1990 CG GLU A1045 12.252 8.574 -15.202 1.00111.73 C ANISOU 1990 CG GLU A1045 17468 14424 10559 1760 820 1438 C ATOM 1991 CD GLU A1045 12.076 7.424 -16.179 1.00140.70 C ANISOU 1991 CD GLU A1045 20953 18332 14174 1827 743 1336 C ATOM 1992 OE1 GLU A1045 12.184 7.671 -17.402 1.00144.63 O ANISOU 1992 OE1 GLU A1045 21585 18879 14489 1965 802 1397 O ATOM 1993 OE2 GLU A1045 11.836 6.280 -15.729 1.00138.49 O ANISOU 1993 OE2 GLU A1045 20409 18183 14026 1741 631 1195 O ATOM 1994 N LEU A1046 8.636 9.460 -12.357 1.00 97.79 N ANISOU 1994 N LEU A1046 15600 12737 8818 2138 471 1308 N ATOM 1995 CA LEU A1046 7.752 9.298 -11.202 1.00 96.71 C ANISOU 1995 CA LEU A1046 15324 12647 8776 2147 360 1222 C ATOM 1996 C LEU A1046 6.317 9.035 -11.667 1.00104.63 C ANISOU 1996 C LEU A1046 16213 13919 9622 2422 218 1131 C ATOM 1997 O LEU A1046 5.723 8.040 -11.243 1.00103.78 O ANISOU 1997 O LEU A1046 15838 13986 9607 2367 103 981 O ATOM 1998 CB LEU A1046 7.811 10.512 -10.255 1.00 96.52 C ANISOU 1998 CB LEU A1046 15520 12379 8774 2137 432 1326 C ATOM 1999 CG LEU A1046 7.012 10.424 -8.937 1.00 99.57 C ANISOU 1999 CG LEU A1046 15779 12782 9270 2125 335 1248 C ATOM 2000 CD1 LEU A1046 7.396 9.205 -8.119 1.00 97.53 C ANISOU 2000 CD1 LEU A1046 15240 12574 9242 1863 278 1126 C ATOM 2001 CD2 LEU A1046 7.222 11.651 -8.101 1.00101.42 C ANISOU 2001 CD2 LEU A1046 16259 12757 9518 2102 425 1354 C ATOM 2002 N ASP A1047 5.792 9.889 -12.577 1.00104.41 N ANISOU 2002 N ASP A1047 16387 13935 9349 2716 234 1216 N ATOM 2003 CA ASP A1047 4.445 9.778 -13.136 1.00105.89 C ANISOU 2003 CA ASP A1047 16480 14406 9347 3016 102 1136 C ATOM 2004 C ASP A1047 4.251 8.451 -13.881 1.00110.42 C ANISOU 2004 C ASP A1047 16780 15256 9920 2977 7 979 C ATOM 2005 O ASP A1047 3.174 7.866 -13.780 1.00110.47 O ANISOU 2005 O ASP A1047 16562 15516 9896 3068 -128 831 O ATOM 2006 CB ASP A1047 4.137 10.970 -14.048 1.00110.30 C ANISOU 2006 CB ASP A1047 17344 14937 9629 3343 158 1278 C ATOM 2007 CG ASP A1047 3.761 12.246 -13.307 1.00122.50 C ANISOU 2007 CG ASP A1047 19134 16291 11120 3485 207 1391 C ATOM 2008 OD1 ASP A1047 4.346 12.510 -12.239 1.00121.67 O ANISOU 2008 OD1 ASP A1047 19080 15948 11201 3257 276 1426 O ATOM 2009 OD2 ASP A1047 2.920 13.003 -13.824 1.00132.40 O ANISOU 2009 OD2 ASP A1047 20541 17630 12133 3832 181 1446 O ATOM 2010 N LYS A1048 5.294 7.949 -14.570 1.00107.10 N ANISOU 2010 N LYS A1048 16367 14786 9540 2823 82 1000 N ATOM 2011 CA LYS A1048 5.238 6.657 -15.265 1.00107.12 C ANISOU 2011 CA LYS A1048 16131 15018 9553 2760 10 851 C ATOM 2012 C LYS A1048 5.158 5.505 -14.239 1.00111.17 C ANISOU 2012 C LYS A1048 16365 15569 10304 2509 -57 696 C ATOM 2013 O LYS A1048 4.271 4.656 -14.342 1.00111.61 O ANISOU 2013 O LYS A1048 16195 15868 10342 2541 -172 528 O ATOM 2014 CB LYS A1048 6.451 6.459 -16.202 1.00109.32 C ANISOU 2014 CB LYS A1048 16507 15212 9819 2658 124 922 C ATOM 2015 CG LYS A1048 6.508 7.417 -17.381 1.00128.20 C ANISOU 2015 CG LYS A1048 19164 17592 11955 2907 195 1061 C ATOM 2016 N ALA A1049 6.069 5.504 -13.239 1.00106.48 N ANISOU 2016 N ALA A1049 15797 14738 9924 2263 21 749 N ATOM 2017 CA ALA A1049 6.164 4.492 -12.192 1.00104.63 C ANISOU 2017 CA ALA A1049 15347 14493 9916 2026 -19 632 C ATOM 2018 C ALA A1049 4.878 4.377 -11.362 1.00110.39 C ANISOU 2018 C ALA A1049 15933 15348 10661 2094 -131 523 C ATOM 2019 O ALA A1049 4.408 3.260 -11.141 1.00109.38 O ANISOU 2019 O ALA A1049 15578 15369 10611 1998 -202 362 O ATOM 2020 CB ALA A1049 7.340 4.798 -11.284 1.00103.95 C ANISOU 2020 CB ALA A1049 15351 14135 10009 1805 85 733 C ATOM 2021 N ILE A1050 4.306 5.520 -10.924 1.00109.19 N ANISOU 2021 N ILE A1050 15921 15137 10428 2258 -137 607 N ATOM 2022 CA ILE A1050 3.095 5.572 -10.092 1.00109.61 C ANISOU 2022 CA ILE A1050 15855 15305 10485 2342 -232 518 C ATOM 2023 C ILE A1050 1.846 5.275 -10.941 1.00118.60 C ANISOU 2023 C ILE A1050 16852 16779 11433 2569 -347 390 C ATOM 2024 O ILE A1050 0.947 4.573 -10.470 1.00118.84 O ANISOU 2024 O ILE A1050 16653 16992 11508 2534 -436 230 O ATOM 2025 CB ILE A1050 2.992 6.941 -9.342 1.00112.59 C ANISOU 2025 CB ILE A1050 16453 15489 10835 2448 -187 657 C ATOM 2026 CG1 ILE A1050 4.208 7.200 -8.411 1.00110.90 C ANISOU 2026 CG1 ILE A1050 16353 14967 10816 2196 -80 756 C ATOM 2027 CG2 ILE A1050 1.667 7.118 -8.592 1.00113.61 C ANISOU 2027 CG2 ILE A1050 16473 15759 10933 2584 -285 573 C ATOM 2028 CD1 ILE A1050 4.454 6.222 -7.263 1.00110.65 C ANISOU 2028 CD1 ILE A1050 16123 14900 11019 1932 -104 657 C ATOM 2029 N GLY A1051 1.809 5.806 -12.163 1.00118.48 N ANISOU 2029 N GLY A1051 16969 16845 11202 2792 -339 457 N ATOM 2030 CA GLY A1051 0.694 5.633 -13.088 1.00120.84 C ANISOU 2030 CA GLY A1051 17149 17481 11284 3039 -449 345 C ATOM 2031 C GLY A1051 -0.366 6.717 -12.986 1.00129.02 C ANISOU 2031 C GLY A1051 18273 18616 12133 3360 -504 390 C ATOM 2032 O GLY A1051 -1.542 6.440 -13.238 1.00130.50 O ANISOU 2032 O GLY A1051 18270 19122 12194 3525 -623 245 O ATOM 2033 N ARG A1052 0.042 7.963 -12.612 1.00126.77 N ANISOU 2033 N ARG A1052 18280 18063 11822 3451 -412 583 N ATOM 2034 CA ARG A1052 -0.820 9.153 -12.465 1.00128.61 C ANISOU 2034 CA ARG A1052 18669 18323 11873 3774 -435 661 C ATOM 2035 C ARG A1052 0.014 10.459 -12.403 1.00134.84 C ANISOU 2035 C ARG A1052 19852 18757 12624 3831 -286 895 C ATOM 2036 O ARG A1052 1.237 10.399 -12.231 1.00133.51 O ANISOU 2036 O ARG A1052 19791 18327 12609 3572 -172 977 O ATOM 2037 CB ARG A1052 -1.728 9.048 -11.214 1.00125.79 C ANISOU 2037 CB ARG A1052 18133 18043 11619 3747 -512 556 C ATOM 2038 CG ARG A1052 -0.999 9.247 -9.893 1.00131.30 C ANISOU 2038 CG ARG A1052 18916 18414 12558 3486 -425 628 C ATOM 2039 CD ARG A1052 -1.932 9.603 -8.758 1.00136.40 C ANISOU 2039 CD ARG A1052 19494 19098 13236 3560 -479 582 C ATOM 2040 NE ARG A1052 -1.201 9.799 -7.506 1.00138.71 N ANISOU 2040 NE ARG A1052 19875 19081 13749 3311 -397 650 N ATOM 2041 CZ ARG A1052 -0.735 10.968 -7.079 1.00153.91 C ANISOU 2041 CZ ARG A1052 22097 20720 15661 3360 -299 814 C ATOM 2042 NH1 ARG A1052 -0.921 12.069 -7.796 1.00141.16 N ANISOU 2042 NH1 ARG A1052 20747 19065 13823 3656 -259 941 N ATOM 2043 NH2 ARG A1052 -0.084 11.047 -5.926 1.00140.77 N ANISOU 2043 NH2 ARG A1052 20479 18808 14200 3115 -237 848 N ATOM 2044 N ASN A1053 -0.666 11.630 -12.505 1.00133.68 N ANISOU 2044 N ASN A1053 19918 18605 12268 4168 -283 994 N ATOM 2045 CA ASN A1053 -0.055 12.963 -12.413 1.00134.46 C ANISOU 2045 CA ASN A1053 20421 18363 12303 4251 -133 1209 C ATOM 2046 C ASN A1053 0.262 13.238 -10.936 1.00136.02 C ANISOU 2046 C ASN A1053 20652 18304 12727 4023 -81 1231 C ATOM 2047 O ASN A1053 -0.652 13.526 -10.158 1.00136.22 O ANISOU 2047 O ASN A1053 20618 18401 12740 4151 -149 1185 O ATOM 2048 CB ASN A1053 -0.979 14.050 -13.017 1.00139.37 C ANISOU 2048 CB ASN A1053 21263 19080 12611 4717 -151 1297 C ATOM 2049 CG ASN A1053 -1.564 13.700 -14.367 1.00168.44 C ANISOU 2049 CG ASN A1053 24850 23100 16049 4986 -243 1238 C ATOM 2050 OD1 ASN A1053 -2.511 12.913 -14.472 1.00163.14 O ANISOU 2050 OD1 ASN A1053 23849 22794 15343 5060 -401 1055 O ATOM 2051 ND2 ASN A1053 -1.025 14.286 -15.429 1.00162.66 N ANISOU 2051 ND2 ASN A1053 24406 22260 15136 5134 -142 1385 N ATOM 2052 N THR A1054 1.545 13.097 -10.542 1.00130.12 N ANISOU 2052 N THR A1054 19974 17284 12181 3683 33 1287 N ATOM 2053 CA THR A1054 1.979 13.231 -9.143 1.00127.81 C ANISOU 2053 CA THR A1054 19686 16762 12114 3429 78 1292 C ATOM 2054 C THR A1054 2.412 14.652 -8.750 1.00132.26 C ANISOU 2054 C THR A1054 20637 16988 12630 3476 223 1464 C ATOM 2055 O THR A1054 2.187 15.049 -7.600 1.00130.75 O ANISOU 2055 O THR A1054 20473 16675 12531 3426 225 1460 O ATOM 2056 CB THR A1054 3.129 12.251 -8.817 1.00129.17 C ANISOU 2056 CB THR A1054 19695 16850 12536 3031 113 1240 C ATOM 2057 OG1 THR A1054 4.295 12.590 -9.565 1.00125.53 O ANISOU 2057 OG1 THR A1054 19441 16207 12048 2936 250 1359 O ATOM 2058 CG2 THR A1054 2.751 10.786 -9.023 1.00126.06 C ANISOU 2058 CG2 THR A1054 18935 16744 12219 2942 -14 1062 C ATOM 2059 N ASN A1055 3.068 15.387 -9.684 1.00130.24 N ANISOU 2059 N ASN A1055 20683 16569 12231 3551 356 1609 N ATOM 2060 CA ASN A1055 3.650 16.732 -9.509 1.00131.44 C ANISOU 2060 CA ASN A1055 21248 16368 12325 3562 533 1778 C ATOM 2061 C ASN A1055 4.792 16.682 -8.451 1.00132.64 C ANISOU 2061 C ASN A1055 21397 16262 12739 3147 626 1777 C ATOM 2062 O ASN A1055 5.020 17.644 -7.709 1.00132.71 O ANISOU 2062 O ASN A1055 21650 16006 12770 3099 728 1854 O ATOM 2063 CB ASN A1055 2.580 17.808 -9.171 1.00135.11 C ANISOU 2063 CB ASN A1055 21928 16797 12613 3907 522 1838 C ATOM 2064 CG ASN A1055 2.951 19.224 -9.582 1.00160.15 C ANISOU 2064 CG ASN A1055 25587 19656 15605 4055 710 2029 C ATOM 2065 OD1 ASN A1055 3.236 19.517 -10.756 1.00155.46 O ANISOU 2065 OD1 ASN A1055 25189 19043 14835 4191 791 2125 O ATOM 2066 ND2 ASN A1055 2.910 20.145 -8.629 1.00151.54 N ANISOU 2066 ND2 ASN A1055 24721 18313 14544 4045 789 2086 N ATOM 2067 N GLY A1056 5.509 15.556 -8.435 1.00126.52 N ANISOU 2067 N GLY A1056 20351 15576 12147 2863 592 1687 N ATOM 2068 CA GLY A1056 6.631 15.300 -7.536 1.00124.05 C ANISOU 2068 CA GLY A1056 19972 15086 12074 2479 658 1666 C ATOM 2069 C GLY A1056 6.263 14.906 -6.119 1.00124.86 C ANISOU 2069 C GLY A1056 19873 15210 12358 2354 563 1564 C ATOM 2070 O GLY A1056 7.139 14.853 -5.251 1.00123.20 O ANISOU 2070 O GLY A1056 19640 14843 12329 2064 617 1554 O ATOM 2071 N VAL A1057 4.967 14.640 -5.870 1.00120.49 N ANISOU 2071 N VAL A1057 19170 14863 11749 2572 423 1485 N ATOM 2072 CA VAL A1057 4.443 14.278 -4.550 1.00118.52 C ANISOU 2072 CA VAL A1057 18732 14653 11646 2489 332 1386 C ATOM 2073 C VAL A1057 3.714 12.936 -4.647 1.00120.44 C ANISOU 2073 C VAL A1057 18607 15215 11940 2503 177 1230 C ATOM 2074 O VAL A1057 2.884 12.753 -5.538 1.00121.00 O ANISOU 2074 O VAL A1057 18614 15511 11849 2745 104 1196 O ATOM 2075 CB VAL A1057 3.508 15.388 -3.968 1.00123.81 C ANISOU 2075 CB VAL A1057 19599 15243 12201 2732 333 1435 C ATOM 2076 CG1 VAL A1057 3.024 15.031 -2.562 1.00122.14 C ANISOU 2076 CG1 VAL A1057 19200 15063 12144 2631 251 1335 C ATOM 2077 CG2 VAL A1057 4.178 16.764 -3.970 1.00125.01 C ANISOU 2077 CG2 VAL A1057 20160 15061 12279 2732 505 1589 C ATOM 2078 N ILE A1058 4.011 12.008 -3.716 1.00114.74 N ANISOU 2078 N ILE A1058 17651 14512 11432 2246 132 1131 N ATOM 2079 CA ILE A1058 3.369 10.689 -3.653 1.00113.04 C ANISOU 2079 CA ILE A1058 17103 14562 11287 2212 7 975 C ATOM 2080 C ILE A1058 2.791 10.448 -2.245 1.00114.93 C ANISOU 2080 C ILE A1058 17204 14808 11655 2136 -52 893 C ATOM 2081 O ILE A1058 3.139 11.168 -1.308 1.00113.39 O ANISOU 2081 O ILE A1058 17156 14402 11526 2060 4 956 O ATOM 2082 CB ILE A1058 4.313 9.533 -4.098 1.00114.97 C ANISOU 2082 CB ILE A1058 17185 14847 11651 1981 18 924 C ATOM 2083 CG1 ILE A1058 5.593 9.450 -3.229 1.00113.72 C ANISOU 2083 CG1 ILE A1058 17055 14466 11688 1682 97 961 C ATOM 2084 CG2 ILE A1058 4.636 9.638 -5.592 1.00117.36 C ANISOU 2084 CG2 ILE A1058 17583 15207 11802 2094 57 980 C ATOM 2085 CD1 ILE A1058 6.212 8.128 -3.171 1.00115.70 C ANISOU 2085 CD1 ILE A1058 17084 14790 12087 1469 75 874 C ATOM 2086 N THR A1059 1.905 9.443 -2.108 1.00111.40 N ANISOU 2086 N THR A1059 16484 14606 11238 2150 -159 747 N ATOM 2087 CA THR A1059 1.283 9.076 -0.830 1.00110.54 C ANISOU 2087 CA THR A1059 16224 14532 11245 2074 -211 657 C ATOM 2088 C THR A1059 2.112 7.988 -0.134 1.00113.04 C ANISOU 2088 C THR A1059 16390 14780 11778 1763 -198 599 C ATOM 2089 O THR A1059 3.046 7.452 -0.734 1.00113.41 O ANISOU 2089 O THR A1059 16423 14794 11873 1631 -161 614 O ATOM 2090 CB THR A1059 -0.174 8.606 -1.036 1.00119.80 C ANISOU 2090 CB THR A1059 17184 16013 12321 2251 -319 521 C ATOM 2091 OG1 THR A1059 -0.190 7.370 -1.751 1.00117.82 O ANISOU 2091 OG1 THR A1059 16717 15953 12095 2159 -362 405 O ATOM 2092 CG2 THR A1059 -1.049 9.647 -1.738 1.00121.01 C ANISOU 2092 CG2 THR A1059 17468 16272 12238 2601 -345 571 C ATOM 2093 N LYS A1060 1.759 7.652 1.117 1.00107.58 N ANISOU 2093 N LYS A1060 15593 14075 11207 1661 -225 534 N ATOM 2094 CA LYS A1060 2.422 6.603 1.895 1.00105.24 C ANISOU 2094 CA LYS A1060 15162 13722 11101 1397 -215 478 C ATOM 2095 C LYS A1060 2.164 5.247 1.226 1.00107.97 C ANISOU 2095 C LYS A1060 15289 14268 11465 1340 -257 354 C ATOM 2096 O LYS A1060 3.073 4.418 1.135 1.00106.26 O ANISOU 2096 O LYS A1060 15021 14000 11353 1163 -227 343 O ATOM 2097 CB LYS A1060 1.925 6.611 3.358 1.00106.41 C ANISOU 2097 CB LYS A1060 15261 13826 11342 1340 -234 437 C ATOM 2098 CG LYS A1060 3.009 6.321 4.382 1.00108.69 C ANISOU 2098 CG LYS A1060 15571 13927 11800 1106 -188 467 C ATOM 2099 N ASP A1061 0.929 5.057 0.717 1.00105.35 N ANISOU 2099 N ASP A1061 14836 14174 11020 1499 -325 256 N ATOM 2100 CA ASP A1061 0.483 3.865 -0.009 1.00105.42 C ANISOU 2100 CA ASP A1061 14639 14401 11014 1463 -367 115 C ATOM 2101 C ASP A1061 1.358 3.649 -1.277 1.00107.77 C ANISOU 2101 C ASP A1061 14993 14691 11265 1454 -338 161 C ATOM 2102 O ASP A1061 1.760 2.514 -1.562 1.00107.90 O ANISOU 2102 O ASP A1061 14895 14746 11358 1303 -328 85 O ATOM 2103 CB ASP A1061 -1.019 4.023 -0.375 1.00109.15 C ANISOU 2103 CB ASP A1061 14989 15147 11335 1671 -446 10 C ATOM 2104 CG ASP A1061 -1.550 3.073 -1.440 1.00119.98 C ANISOU 2104 CG ASP A1061 16176 16781 12631 1685 -495 -135 C ATOM 2105 N GLU A1062 1.668 4.750 -2.002 1.00101.52 N ANISOU 2105 N GLU A1062 14394 13835 10344 1615 -312 288 N ATOM 2106 CA GLU A1062 2.457 4.750 -3.230 1.00100.45 C ANISOU 2106 CA GLU A1062 14341 13687 10138 1634 -274 348 C ATOM 2107 C GLU A1062 3.936 4.467 -2.949 1.00100.96 C ANISOU 2107 C GLU A1062 14469 13538 10352 1408 -191 421 C ATOM 2108 O GLU A1062 4.544 3.682 -3.683 1.00 99.61 O ANISOU 2108 O GLU A1062 14238 13408 10201 1324 -172 392 O ATOM 2109 CB GLU A1062 2.281 6.077 -3.977 1.00103.32 C ANISOU 2109 CB GLU A1062 14918 14029 10311 1882 -256 469 C ATOM 2110 CG GLU A1062 0.912 6.204 -4.626 1.00111.67 C ANISOU 2110 CG GLU A1062 15890 15358 11180 2142 -346 388 C ATOM 2111 CD GLU A1062 0.503 7.577 -5.124 1.00126.52 C ANISOU 2111 CD GLU A1062 17990 17224 12856 2437 -337 505 C ATOM 2112 OE1 GLU A1062 -0.393 7.634 -5.995 1.00122.66 O ANISOU 2112 OE1 GLU A1062 17443 16980 12182 2672 -406 450 O ATOM 2113 OE2 GLU A1062 1.043 8.591 -4.628 1.00113.37 O ANISOU 2113 OE2 GLU A1062 16559 15310 11208 2440 -259 644 O ATOM 2114 N ALA A1063 4.502 5.091 -1.887 1.00 96.12 N ANISOU 2114 N ALA A1063 13968 12716 9837 1313 -144 505 N ATOM 2115 CA ALA A1063 5.883 4.876 -1.419 1.00 94.64 C ANISOU 2115 CA ALA A1063 13818 12347 9793 1096 -73 561 C ATOM 2116 C ALA A1063 6.097 3.422 -0.963 1.00 97.91 C ANISOU 2116 C ALA A1063 14034 12816 10351 922 -94 452 C ATOM 2117 O ALA A1063 7.147 2.843 -1.244 1.00 96.90 O ANISOU 2117 O ALA A1063 13884 12642 10290 797 -50 465 O ATOM 2118 CB ALA A1063 6.207 5.822 -0.273 1.00 94.73 C ANISOU 2118 CB ALA A1063 13964 12162 9865 1041 -35 641 C ATOM 2119 N GLU A1064 5.094 2.846 -0.260 1.00 94.14 N ANISOU 2119 N GLU A1064 13420 12435 9913 922 -153 344 N ATOM 2120 CA GLU A1064 5.105 1.474 0.232 1.00 92.60 C ANISOU 2120 CA GLU A1064 13062 12282 9840 771 -163 235 C ATOM 2121 C GLU A1064 5.036 0.497 -0.940 1.00 94.50 C ANISOU 2121 C GLU A1064 13201 12672 10034 772 -172 147 C ATOM 2122 O GLU A1064 5.721 -0.526 -0.909 1.00 93.17 O ANISOU 2122 O GLU A1064 12972 12469 9957 636 -140 110 O ATOM 2123 CB GLU A1064 3.930 1.247 1.198 1.00 94.39 C ANISOU 2123 CB GLU A1064 13189 12578 10096 779 -209 142 C ATOM 2124 CG GLU A1064 4.168 0.163 2.242 1.00110.63 C ANISOU 2124 CG GLU A1064 15155 14574 12305 599 -189 78 C ATOM 2125 CD GLU A1064 3.376 -1.133 2.137 1.00143.69 C ANISOU 2125 CD GLU A1064 19178 18904 16512 536 -202 -80 C ATOM 2126 OE1 GLU A1064 3.792 -2.129 2.775 1.00135.30 O ANISOU 2126 OE1 GLU A1064 18076 17767 15564 388 -164 -118 O ATOM 2127 OE2 GLU A1064 2.326 -1.149 1.453 1.00146.72 O ANISOU 2127 OE2 GLU A1064 19477 19478 16791 634 -247 -171 O ATOM 2128 N LYS A1065 4.223 0.819 -1.976 1.00 91.04 N ANISOU 2128 N LYS A1065 12750 12400 9441 939 -214 113 N ATOM 2129 CA LYS A1065 4.050 -0.017 -3.163 1.00 91.27 C ANISOU 2129 CA LYS A1065 12684 12594 9399 957 -231 19 C ATOM 2130 C LYS A1065 5.374 -0.113 -3.960 1.00 93.66 C ANISOU 2130 C LYS A1065 13074 12805 9709 907 -167 104 C ATOM 2131 O LYS A1065 5.789 -1.228 -4.296 1.00 93.39 O ANISOU 2131 O LYS A1065 12958 12798 9728 801 -147 32 O ATOM 2132 CB LYS A1065 2.899 0.507 -4.040 1.00 96.06 C ANISOU 2132 CB LYS A1065 13264 13415 9818 1172 -298 -28 C ATOM 2133 CG LYS A1065 2.522 -0.432 -5.190 1.00118.47 C ANISOU 2133 CG LYS A1065 15975 16464 12576 1185 -329 -163 C ATOM 2134 CD LYS A1065 1.786 0.298 -6.313 1.00134.81 C ANISOU 2134 CD LYS A1065 18067 18728 14427 1432 -386 -162 C ATOM 2135 CE LYS A1065 1.847 -0.441 -7.635 1.00151.60 C ANISOU 2135 CE LYS A1065 20125 21017 16461 1448 -399 -250 C ATOM 2136 NZ LYS A1065 0.992 -1.659 -7.650 1.00163.52 N ANISOU 2136 NZ LYS A1065 21415 22724 17990 1347 -443 -466 N ATOM 2137 N LEU A1066 6.035 1.046 -4.231 1.00 88.37 N ANISOU 2137 N LEU A1066 12576 12019 8982 978 -126 253 N ATOM 2138 CA LEU A1066 7.321 1.128 -4.936 1.00 87.01 C ANISOU 2138 CA LEU A1066 12494 11757 8810 926 -52 343 C ATOM 2139 C LEU A1066 8.402 0.358 -4.188 1.00 86.88 C ANISOU 2139 C LEU A1066 12426 11620 8964 725 -4 343 C ATOM 2140 O LEU A1066 9.169 -0.376 -4.804 1.00 86.59 O ANISOU 2140 O LEU A1066 12353 11599 8948 661 33 327 O ATOM 2141 CB LEU A1066 7.772 2.590 -5.081 1.00 87.60 C ANISOU 2141 CB LEU A1066 12775 11699 8808 1005 1 498 C ATOM 2142 CG LEU A1066 7.366 3.362 -6.320 1.00 92.95 C ANISOU 2142 CG LEU A1066 13571 12459 9288 1210 3 551 C ATOM 2143 CD1 LEU A1066 7.757 4.805 -6.174 1.00 93.12 C ANISOU 2143 CD1 LEU A1066 13824 12305 9253 1265 73 702 C ATOM 2144 CD2 LEU A1066 8.032 2.806 -7.551 1.00 95.97 C ANISOU 2144 CD2 LEU A1066 13940 12907 9617 1198 40 546 C ATOM 2145 N PHE A1067 8.459 0.539 -2.863 1.00 80.21 N ANISOU 2145 N PHE A1067 11583 10663 8230 641 -6 361 N ATOM 2146 CA PHE A1067 9.396 -0.123 -1.971 1.00 78.60 C ANISOU 2146 CA PHE A1067 11331 10355 8177 476 28 362 C ATOM 2147 C PHE A1067 9.275 -1.652 -2.083 1.00 85.89 C ANISOU 2147 C PHE A1067 12117 11359 9157 411 18 241 C ATOM 2148 O PHE A1067 10.304 -2.319 -2.210 1.00 86.27 O ANISOU 2148 O PHE A1067 12144 11368 9265 328 64 249 O ATOM 2149 CB PHE A1067 9.173 0.355 -0.543 1.00 78.95 C ANISOU 2149 CB PHE A1067 11399 10298 8302 431 11 384 C ATOM 2150 CG PHE A1067 10.127 -0.169 0.503 1.00 78.74 C ANISOU 2150 CG PHE A1067 11336 10169 8414 284 39 395 C ATOM 2151 CD1 PHE A1067 11.502 -0.016 0.355 1.00 81.02 C ANISOU 2151 CD1 PHE A1067 11660 10389 8736 204 97 466 C ATOM 2152 CD2 PHE A1067 9.649 -0.750 1.669 1.00 78.37 C ANISOU 2152 CD2 PHE A1067 11221 10101 8453 232 10 334 C ATOM 2153 CE1 PHE A1067 12.377 -0.476 1.334 1.00 80.66 C ANISOU 2153 CE1 PHE A1067 11569 10278 8802 91 114 470 C ATOM 2154 CE2 PHE A1067 10.526 -1.217 2.643 1.00 80.10 C ANISOU 2154 CE2 PHE A1067 11418 10235 8782 122 33 349 C ATOM 2155 CZ PHE A1067 11.883 -1.067 2.476 1.00 78.47 C ANISOU 2155 CZ PHE A1067 11234 9979 8600 60 79 415 C ATOM 2156 N ASN A1068 8.033 -2.194 -2.142 1.00 83.53 N ANISOU 2156 N ASN A1068 11730 11181 8825 452 -34 123 N ATOM 2157 CA ASN A1068 7.784 -3.636 -2.308 1.00 82.93 C ANISOU 2157 CA ASN A1068 11543 11177 8790 379 -30 -9 C ATOM 2158 C ASN A1068 8.326 -4.135 -3.649 1.00 86.40 C ANISOU 2158 C ASN A1068 11978 11685 9165 400 -2 -28 C ATOM 2159 O ASN A1068 8.900 -5.215 -3.702 1.00 85.30 O ANISOU 2159 O ASN A1068 11803 11518 9089 315 39 -75 O ATOM 2160 CB ASN A1068 6.293 -3.969 -2.168 1.00 84.55 C ANISOU 2160 CB ASN A1068 11651 11517 8957 407 -83 -143 C ATOM 2161 CG ASN A1068 5.731 -3.729 -0.784 1.00111.43 C ANISOU 2161 CG ASN A1068 15042 14859 12436 369 -100 -146 C ATOM 2162 OD1 ASN A1068 6.371 -3.975 0.244 1.00105.60 O ANISOU 2162 OD1 ASN A1068 14332 13978 11812 273 -65 -103 O ATOM 2163 ND2 ASN A1068 4.508 -3.237 -0.726 1.00108.18 N ANISOU 2163 ND2 ASN A1068 14585 14568 11951 456 -154 -200 N ATOM 2164 N GLN A1069 8.176 -3.335 -4.717 1.00 84.68 N ANISOU 2164 N GLN A1069 11813 11550 8813 524 -19 16 N ATOM 2165 CA GLN A1069 8.676 -3.662 -6.052 1.00 85.05 C ANISOU 2165 CA GLN A1069 11870 11668 8778 561 8 9 C ATOM 2166 C GLN A1069 10.198 -3.724 -6.041 1.00 89.02 C ANISOU 2166 C GLN A1069 12427 12043 9352 482 86 107 C ATOM 2167 O GLN A1069 10.774 -4.690 -6.537 1.00 90.51 O ANISOU 2167 O GLN A1069 12577 12250 9562 435 123 60 O ATOM 2168 CB GLN A1069 8.211 -2.626 -7.085 1.00 87.66 C ANISOU 2168 CB GLN A1069 12272 12099 8938 730 -20 58 C ATOM 2169 CG GLN A1069 6.730 -2.650 -7.455 1.00106.25 C ANISOU 2169 CG GLN A1069 14545 14648 11177 844 -103 -58 C ATOM 2170 CD GLN A1069 6.396 -1.569 -8.467 1.00120.79 C ANISOU 2170 CD GLN A1069 16481 16581 12833 1043 -127 12 C ATOM 2171 OE1 GLN A1069 7.256 -1.089 -9.226 1.00111.75 O ANISOU 2171 OE1 GLN A1069 15453 15379 11629 1084 -72 120 O ATOM 2172 NE2 GLN A1069 5.131 -1.156 -8.501 1.00112.45 N ANISOU 2172 NE2 GLN A1069 15380 15675 11670 1181 -205 -47 N ATOM 2173 N ASP A1070 10.838 -2.696 -5.455 1.00 83.62 N ANISOU 2173 N ASP A1070 11832 11238 8701 467 113 235 N ATOM 2174 CA ASP A1070 12.282 -2.534 -5.336 1.00 82.64 C ANISOU 2174 CA ASP A1070 11749 11010 8639 384 185 329 C ATOM 2175 C ASP A1070 12.926 -3.634 -4.482 1.00 84.00 C ANISOU 2175 C ASP A1070 11839 11130 8949 271 204 284 C ATOM 2176 O ASP A1070 13.983 -4.156 -4.857 1.00 81.77 O ANISOU 2176 O ASP A1070 11535 10843 8689 231 258 299 O ATOM 2177 CB ASP A1070 12.590 -1.156 -4.738 1.00 84.47 C ANISOU 2177 CB ASP A1070 12090 11131 8875 376 205 447 C ATOM 2178 CG ASP A1070 12.595 -0.026 -5.742 1.00 93.02 C ANISOU 2178 CG ASP A1070 13306 12219 9820 473 238 535 C ATOM 2179 OD1 ASP A1070 11.964 -0.175 -6.814 1.00 93.89 O ANISOU 2179 OD1 ASP A1070 13419 12446 9811 590 215 497 O ATOM 2180 OD2 ASP A1070 13.232 1.003 -5.461 1.00100.89 O ANISOU 2180 OD2 ASP A1070 14412 13104 10819 432 293 637 O ATOM 2181 N VAL A1071 12.284 -3.995 -3.349 1.00 80.95 N ANISOU 2181 N VAL A1071 11409 10708 8641 232 165 231 N ATOM 2182 CA VAL A1071 12.797 -5.057 -2.478 1.00 80.36 C ANISOU 2182 CA VAL A1071 11278 10574 8681 147 185 193 C ATOM 2183 C VAL A1071 12.686 -6.381 -3.225 1.00 85.46 C ANISOU 2183 C VAL A1071 11873 11285 9311 148 206 89 C ATOM 2184 O VAL A1071 13.656 -7.136 -3.243 1.00 86.35 O ANISOU 2184 O VAL A1071 11972 11366 9469 117 256 93 O ATOM 2185 CB VAL A1071 12.152 -5.113 -1.076 1.00 83.44 C ANISOU 2185 CB VAL A1071 11652 10900 9150 106 150 168 C ATOM 2186 CG1 VAL A1071 12.646 -6.335 -0.292 1.00 83.10 C ANISOU 2186 CG1 VAL A1071 11573 10799 9204 41 182 127 C ATOM 2187 CG2 VAL A1071 12.441 -3.835 -0.288 1.00 82.65 C ANISOU 2187 CG2 VAL A1071 11611 10722 9069 94 139 270 C ATOM 2188 N ASP A1072 11.559 -6.613 -3.923 1.00 81.45 N ANISOU 2188 N ASP A1072 11340 10879 8727 192 172 -6 N ATOM 2189 CA ASP A1072 11.358 -7.830 -4.701 1.00 81.06 C ANISOU 2189 CA ASP A1072 11251 10897 8651 181 194 -124 C ATOM 2190 C ASP A1072 12.335 -7.897 -5.885 1.00 83.37 C ANISOU 2190 C ASP A1072 11567 11225 8883 220 239 -84 C ATOM 2191 O ASP A1072 12.809 -8.984 -6.210 1.00 83.00 O ANISOU 2191 O ASP A1072 11507 11171 8856 194 287 -141 O ATOM 2192 CB ASP A1072 9.902 -7.952 -5.175 1.00 84.20 C ANISOU 2192 CB ASP A1072 11598 11425 8968 210 141 -249 C ATOM 2193 CG ASP A1072 9.491 -9.352 -5.609 1.00102.91 C ANISOU 2193 CG ASP A1072 13921 13844 11334 151 169 -407 C ATOM 2194 OD1 ASP A1072 10.030 -10.341 -5.039 1.00104.76 O ANISOU 2194 OD1 ASP A1072 14175 13969 11661 73 229 -430 O ATOM 2195 OD2 ASP A1072 8.612 -9.465 -6.496 1.00111.90 O ANISOU 2195 OD2 ASP A1072 15012 15133 12372 184 134 -514 O ATOM 2196 N ALA A1073 12.668 -6.752 -6.499 1.00 78.89 N ANISOU 2196 N ALA A1073 11049 10687 8241 284 236 17 N ATOM 2197 CA ALA A1073 13.623 -6.726 -7.604 1.00 79.15 C ANISOU 2197 CA ALA A1073 11108 10753 8211 316 290 64 C ATOM 2198 C ALA A1073 15.055 -7.048 -7.101 1.00 83.36 C ANISOU 2198 C ALA A1073 11633 11201 8839 252 356 129 C ATOM 2199 O ALA A1073 15.801 -7.753 -7.796 1.00 83.76 O ANISOU 2199 O ALA A1073 11670 11282 8875 260 408 110 O ATOM 2200 CB ALA A1073 13.592 -5.378 -8.289 1.00 80.22 C ANISOU 2200 CB ALA A1073 11320 10921 8239 394 286 162 C ATOM 2201 N ALA A1074 15.410 -6.552 -5.879 1.00 77.41 N ANISOU 2201 N ALA A1074 10882 10356 8176 198 350 196 N ATOM 2202 CA ALA A1074 16.707 -6.769 -5.225 1.00 75.85 C ANISOU 2202 CA ALA A1074 10656 10103 8063 143 397 250 C ATOM 2203 C ALA A1074 16.925 -8.247 -4.946 1.00 79.74 C ANISOU 2203 C ALA A1074 11106 10581 8612 139 419 170 C ATOM 2204 O ALA A1074 18.000 -8.755 -5.248 1.00 79.86 O ANISOU 2204 O ALA A1074 11096 10613 8634 149 473 185 O ATOM 2205 CB ALA A1074 16.797 -5.970 -3.935 1.00 75.58 C ANISOU 2205 CB ALA A1074 10630 9989 8099 90 370 313 C ATOM 2206 N VAL A1075 15.893 -8.944 -4.427 1.00 76.41 N ANISOU 2206 N VAL A1075 10683 10128 8220 128 386 80 N ATOM 2207 CA VAL A1075 15.927 -10.379 -4.110 1.00 76.91 C ANISOU 2207 CA VAL A1075 10744 10148 8331 118 422 -3 C ATOM 2208 C VAL A1075 16.014 -11.205 -5.422 1.00 85.54 C ANISOU 2208 C VAL A1075 11843 11304 9353 154 465 -78 C ATOM 2209 O VAL A1075 16.819 -12.140 -5.512 1.00 86.52 O ANISOU 2209 O VAL A1075 11976 11401 9496 176 524 -93 O ATOM 2210 CB VAL A1075 14.715 -10.803 -3.237 1.00 78.87 C ANISOU 2210 CB VAL A1075 11002 10343 8622 74 391 -84 C ATOM 2211 CG1 VAL A1075 14.730 -12.293 -2.960 1.00 78.64 C ANISOU 2211 CG1 VAL A1075 11004 10246 8631 56 450 -170 C ATOM 2212 CG2 VAL A1075 14.688 -10.028 -1.930 1.00 77.64 C ANISOU 2212 CG2 VAL A1075 10845 10123 8531 46 353 -10 C ATOM 2213 N ARG A1076 15.219 -10.834 -6.439 1.00 83.13 N ANISOU 2213 N ARG A1076 11538 11090 8957 174 434 -124 N ATOM 2214 CA ARG A1076 15.217 -11.540 -7.716 1.00 84.37 C ANISOU 2214 CA ARG A1076 11701 11321 9033 207 468 -204 C ATOM 2215 C ARG A1076 16.573 -11.361 -8.421 1.00 89.52 C ANISOU 2215 C ARG A1076 12356 12001 9655 254 523 -119 C ATOM 2216 O ARG A1076 17.111 -12.316 -8.985 1.00 89.73 O ANISOU 2216 O ARG A1076 12392 12035 9666 278 581 -167 O ATOM 2217 CB ARG A1076 14.054 -11.070 -8.597 1.00 86.26 C ANISOU 2217 CB ARG A1076 11930 11678 9166 234 411 -269 C ATOM 2218 CG ARG A1076 12.678 -11.621 -8.169 1.00 98.65 C ANISOU 2218 CG ARG A1076 13471 13262 10747 179 372 -407 C ATOM 2219 CD ARG A1076 11.514 -10.836 -8.773 1.00113.64 C ANISOU 2219 CD ARG A1076 15335 15302 12540 225 294 -450 C ATOM 2220 NE ARG A1076 11.564 -10.831 -10.239 1.00132.61 N ANISOU 2220 NE ARG A1076 17741 17831 14812 297 295 -484 N ATOM 2221 CZ ARG A1076 11.866 -9.773 -10.988 1.00152.16 C ANISOU 2221 CZ ARG A1076 20248 20370 17195 393 278 -380 C ATOM 2222 NH1 ARG A1076 12.123 -8.599 -10.420 1.00133.89 N ANISOU 2222 NH1 ARG A1076 17970 17998 14903 420 262 -241 N ATOM 2223 NH2 ARG A1076 11.905 -9.877 -12.311 1.00148.36 N ANISOU 2223 NH2 ARG A1076 19777 20004 16589 460 284 -418 N ATOM 2224 N GLY A1077 17.137 -10.162 -8.312 1.00 85.73 N ANISOU 2224 N GLY A1077 11873 11529 9172 259 516 3 N ATOM 2225 CA GLY A1077 18.443 -9.846 -8.868 1.00 85.33 C ANISOU 2225 CA GLY A1077 11812 11511 9096 279 577 87 C ATOM 2226 C GLY A1077 19.532 -10.691 -8.243 1.00 87.29 C ANISOU 2226 C GLY A1077 12023 11720 9423 277 628 94 C ATOM 2227 O GLY A1077 20.454 -11.127 -8.942 1.00 88.41 O ANISOU 2227 O GLY A1077 12148 11912 9533 316 690 99 O ATOM 2228 N ILE A1078 19.397 -10.974 -6.926 1.00 80.03 N ANISOU 2228 N ILE A1078 11094 10718 8596 246 602 91 N ATOM 2229 CA ILE A1078 20.334 -11.816 -6.178 1.00 78.53 C ANISOU 2229 CA ILE A1078 10878 10490 8470 270 641 97 C ATOM 2230 C ILE A1078 20.282 -13.262 -6.732 1.00 82.97 C ANISOU 2230 C ILE A1078 11482 11035 9009 326 693 0 C ATOM 2231 O ILE A1078 21.331 -13.836 -7.045 1.00 81.97 O ANISOU 2231 O ILE A1078 11336 10939 8868 390 753 11 O ATOM 2232 CB ILE A1078 20.072 -11.756 -4.641 1.00 79.41 C ANISOU 2232 CB ILE A1078 10988 10514 8669 236 599 115 C ATOM 2233 CG1 ILE A1078 20.565 -10.422 -4.056 1.00 78.60 C ANISOU 2233 CG1 ILE A1078 10840 10433 8592 185 568 214 C ATOM 2234 CG2 ILE A1078 20.764 -12.897 -3.944 1.00 79.81 C ANISOU 2234 CG2 ILE A1078 11042 10519 8764 293 639 100 C ATOM 2235 CD1 ILE A1078 19.959 -9.993 -2.705 1.00 78.38 C ANISOU 2235 CD1 ILE A1078 10824 10327 8629 138 509 230 C ATOM 2236 N LEU A1079 19.059 -13.820 -6.869 1.00 80.61 N ANISOU 2236 N LEU A1079 11237 10693 8698 298 676 -102 N ATOM 2237 CA LEU A1079 18.819 -15.184 -7.367 1.00 81.21 C ANISOU 2237 CA LEU A1079 11375 10733 8750 322 732 -215 C ATOM 2238 C LEU A1079 19.197 -15.315 -8.870 1.00 88.58 C ANISOU 2238 C LEU A1079 12306 11764 9588 369 770 -243 C ATOM 2239 O LEU A1079 19.651 -16.384 -9.292 1.00 88.84 O ANISOU 2239 O LEU A1079 12383 11774 9600 420 840 -299 O ATOM 2240 CB LEU A1079 17.356 -15.625 -7.109 1.00 80.11 C ANISOU 2240 CB LEU A1079 11278 10540 8619 246 707 -332 C ATOM 2241 CG LEU A1079 16.883 -15.592 -5.639 1.00 81.83 C ANISOU 2241 CG LEU A1079 11511 10657 8926 196 682 -315 C ATOM 2242 CD1 LEU A1079 15.376 -15.622 -5.533 1.00 80.86 C ANISOU 2242 CD1 LEU A1079 11394 10533 8798 109 645 -421 C ATOM 2243 CD2 LEU A1079 17.501 -16.704 -4.817 1.00 82.24 C ANISOU 2243 CD2 LEU A1079 11634 10586 9030 235 753 -315 C ATOM 2244 N ARG A1080 19.060 -14.220 -9.650 1.00 86.41 N ANISOU 2244 N ARG A1080 11994 11590 9249 364 732 -198 N ATOM 2245 CA ARG A1080 19.411 -14.184 -11.078 1.00 87.65 C ANISOU 2245 CA ARG A1080 12153 11848 9302 413 767 -210 C ATOM 2246 C ARG A1080 20.954 -14.236 -11.232 1.00 91.13 C ANISOU 2246 C ARG A1080 12558 12318 9748 470 837 -127 C ATOM 2247 O ARG A1080 21.461 -15.014 -12.033 1.00 91.64 O ANISOU 2247 O ARG A1080 12642 12414 9763 529 900 -171 O ATOM 2248 CB ARG A1080 18.802 -12.918 -11.744 1.00 89.70 C ANISOU 2248 CB ARG A1080 12403 12195 9483 406 711 -169 C ATOM 2249 CG ARG A1080 19.027 -12.763 -13.247 1.00105.09 C ANISOU 2249 CG ARG A1080 14368 14254 11306 463 742 -176 C ATOM 2250 CD ARG A1080 18.334 -11.526 -13.811 1.00123.09 C ANISOU 2250 CD ARG A1080 16665 16609 13496 479 687 -130 C ATOM 2251 NE ARG A1080 18.852 -11.163 -15.137 1.00140.11 N ANISOU 2251 NE ARG A1080 18847 18859 15530 542 734 -92 N ATOM 2252 CZ ARG A1080 18.427 -10.129 -15.864 1.00158.25 C ANISOU 2252 CZ ARG A1080 21186 21225 17716 587 709 -41 C ATOM 2253 NH1 ARG A1080 17.458 -9.341 -15.410 1.00148.76 N ANISOU 2253 NH1 ARG A1080 20000 20016 16507 586 633 -24 N ATOM 2254 NH2 ARG A1080 18.966 -9.877 -17.051 1.00143.79 N ANISOU 2254 NH2 ARG A1080 19392 19471 15772 645 765 -3 N ATOM 2255 N ASN A1081 21.685 -13.440 -10.434 1.00 86.48 N ANISOU 2255 N ASN A1081 11913 11727 9217 450 829 -18 N ATOM 2256 CA ASN A1081 23.143 -13.364 -10.467 1.00 86.09 C ANISOU 2256 CA ASN A1081 11799 11737 9173 488 890 54 C ATOM 2257 C ASN A1081 23.812 -14.649 -9.912 1.00 91.19 C ANISOU 2257 C ASN A1081 12444 12342 9861 566 935 17 C ATOM 2258 O ASN A1081 23.521 -15.086 -8.792 1.00 90.10 O ANISOU 2258 O ASN A1081 12329 12112 9794 563 909 4 O ATOM 2259 CB ASN A1081 23.601 -12.144 -9.699 1.00 81.02 C ANISOU 2259 CB ASN A1081 11095 11109 8578 421 864 158 C ATOM 2260 CG ASN A1081 24.990 -11.703 -10.038 1.00 90.24 C ANISOU 2260 CG ASN A1081 12181 12381 9725 425 929 226 C ATOM 2261 OD1 ASN A1081 25.973 -12.318 -9.632 1.00 83.56 O ANISOU 2261 OD1 ASN A1081 11266 11574 8907 477 966 227 O ATOM 2262 ND2 ASN A1081 25.096 -10.588 -10.743 1.00 80.37 N ANISOU 2262 ND2 ASN A1081 10937 11182 8420 370 950 285 N ATOM 2263 N ALA A1082 24.717 -15.246 -10.720 1.00 88.89 N ANISOU 2263 N ALA A1082 12137 12120 9516 649 1011 5 N ATOM 2264 CA ALA A1082 25.444 -16.477 -10.383 1.00 88.67 C ANISOU 2264 CA ALA A1082 12123 12065 9502 760 1068 -26 C ATOM 2265 C ALA A1082 26.507 -16.241 -9.317 1.00 91.16 C ANISOU 2265 C ALA A1082 12338 12426 9872 796 1065 51 C ATOM 2266 O ALA A1082 26.898 -17.199 -8.653 1.00 92.71 O ANISOU 2266 O ALA A1082 12560 12576 10089 897 1090 34 O ATOM 2267 CB ALA A1082 26.080 -17.077 -11.626 1.00 90.60 C ANISOU 2267 CB ALA A1082 12377 12385 9662 847 1149 -62 C ATOM 2268 N LYS A1083 26.972 -14.991 -9.141 1.00 85.18 N ANISOU 2268 N LYS A1083 11476 11759 9130 716 1039 131 N ATOM 2269 CA LYS A1083 27.957 -14.666 -8.107 1.00 84.64 C ANISOU 2269 CA LYS A1083 11292 11760 9108 727 1027 189 C ATOM 2270 C LYS A1083 27.269 -14.446 -6.744 1.00 86.59 C ANISOU 2270 C LYS A1083 11568 11901 9433 675 949 202 C ATOM 2271 O LYS A1083 27.858 -14.783 -5.716 1.00 85.74 O ANISOU 2271 O LYS A1083 11412 11807 9357 739 937 218 O ATOM 2272 CB LYS A1083 28.799 -13.430 -8.487 1.00 87.40 C ANISOU 2272 CB LYS A1083 11519 12252 9437 638 1049 253 C ATOM 2273 CG LYS A1083 29.732 -13.650 -9.687 1.00106.00 C ANISOU 2273 CG LYS A1083 13820 14741 11716 695 1140 248 C ATOM 2274 CD LYS A1083 30.797 -12.544 -9.891 1.00115.77 C ANISOU 2274 CD LYS A1083 14917 16134 12936 601 1184 305 C ATOM 2275 CE LYS A1083 31.840 -12.415 -8.787 1.00127.52 C ANISOU 2275 CE LYS A1083 16248 17735 14467 605 1172 322 C ATOM 2276 NZ LYS A1083 32.541 -13.694 -8.479 1.00136.70 N ANISOU 2276 NZ LYS A1083 17362 18963 15617 793 1190 284 N ATOM 2277 N LEU A1084 26.024 -13.906 -6.736 1.00 82.11 N ANISOU 2277 N LEU A1084 11077 11236 8883 575 897 192 N ATOM 2278 CA LEU A1084 25.294 -13.583 -5.500 1.00 80.74 C ANISOU 2278 CA LEU A1084 10931 10967 8779 517 826 204 C ATOM 2279 C LEU A1084 24.461 -14.749 -4.907 1.00 83.30 C ANISOU 2279 C LEU A1084 11367 11152 9133 567 821 139 C ATOM 2280 O LEU A1084 24.409 -14.877 -3.683 1.00 83.39 O ANISOU 2280 O LEU A1084 11384 11104 9195 577 790 156 O ATOM 2281 CB LEU A1084 24.388 -12.343 -5.694 1.00 79.91 C ANISOU 2281 CB LEU A1084 10849 10839 8676 394 775 229 C ATOM 2282 CG LEU A1084 25.073 -11.031 -6.138 1.00 84.53 C ANISOU 2282 CG LEU A1084 11363 11520 9233 318 790 301 C ATOM 2283 CD1 LEU A1084 24.076 -9.904 -6.260 1.00 83.42 C ANISOU 2283 CD1 LEU A1084 11284 11327 9083 229 746 327 C ATOM 2284 CD2 LEU A1084 26.171 -10.620 -5.184 1.00 87.20 C ANISOU 2284 CD2 LEU A1084 11591 11927 9615 292 789 348 C ATOM 2285 N LYS A1085 23.792 -15.547 -5.749 1.00 79.27 N ANISOU 2285 N LYS A1085 10947 10587 8583 587 857 60 N ATOM 2286 CA LYS A1085 22.934 -16.695 -5.384 1.00 79.13 C ANISOU 2286 CA LYS A1085 11054 10429 8582 605 877 -23 C ATOM 2287 C LYS A1085 23.632 -17.715 -4.391 1.00 84.48 C ANISOU 2287 C LYS A1085 11776 11040 9284 724 921 -9 C ATOM 2288 O LYS A1085 22.999 -18.042 -3.364 1.00 83.13 O ANISOU 2288 O LYS A1085 11678 10749 9158 704 907 -22 O ATOM 2289 CB LYS A1085 22.487 -17.407 -6.680 1.00 81.78 C ANISOU 2289 CB LYS A1085 11461 10760 8853 613 929 -117 C ATOM 2290 CG LYS A1085 21.355 -18.422 -6.572 1.00 84.72 C ANISOU 2290 CG LYS A1085 11962 10996 9232 575 956 -231 C ATOM 2291 CD LYS A1085 21.146 -19.025 -7.965 1.00 92.64 C ANISOU 2291 CD LYS A1085 13013 12029 10157 584 1007 -327 C ATOM 2292 CE LYS A1085 20.677 -20.451 -7.996 1.00112.20 C ANISOU 2292 CE LYS A1085 15637 14370 12623 591 1088 -445 C ATOM 2293 NZ LYS A1085 21.693 -21.388 -7.441 1.00132.43 N ANISOU 2293 NZ LYS A1085 18273 16851 15194 728 1168 -409 N ATOM 2294 N PRO A1086 24.900 -18.211 -4.629 1.00 81.70 N ANISOU 2294 N PRO A1086 11384 10764 8893 859 974 17 N ATOM 2295 CA PRO A1086 25.516 -19.142 -3.664 1.00 81.97 C ANISOU 2295 CA PRO A1086 11470 10743 8932 1003 1010 35 C ATOM 2296 C PRO A1086 25.780 -18.493 -2.306 1.00 85.32 C ANISOU 2296 C PRO A1086 11819 11193 9405 995 941 107 C ATOM 2297 O PRO A1086 25.605 -19.149 -1.273 1.00 85.56 O ANISOU 2297 O PRO A1086 11942 11115 9452 1061 950 111 O ATOM 2298 CB PRO A1086 26.828 -19.553 -4.341 1.00 84.98 C ANISOU 2298 CB PRO A1086 11788 11252 9250 1150 1069 50 C ATOM 2299 CG PRO A1086 26.702 -19.146 -5.757 1.00 89.60 C ANISOU 2299 CG PRO A1086 12336 11911 9797 1077 1085 19 C ATOM 2300 CD PRO A1086 25.827 -17.945 -5.747 1.00 84.14 C ANISOU 2300 CD PRO A1086 11602 11223 9146 900 1008 34 C ATOM 2301 N VAL A1087 26.164 -17.195 -2.301 1.00 80.39 N ANISOU 2301 N VAL A1087 11042 10705 8799 906 878 161 N ATOM 2302 CA VAL A1087 26.404 -16.446 -1.061 1.00 78.70 C ANISOU 2302 CA VAL A1087 10747 10528 8627 873 809 218 C ATOM 2303 C VAL A1087 25.078 -16.328 -0.274 1.00 81.05 C ANISOU 2303 C VAL A1087 11150 10666 8979 778 766 202 C ATOM 2304 O VAL A1087 25.069 -16.612 0.917 1.00 80.97 O ANISOU 2304 O VAL A1087 11175 10599 8991 828 747 223 O ATOM 2305 CB VAL A1087 27.067 -15.055 -1.276 1.00 80.63 C ANISOU 2305 CB VAL A1087 10825 10935 8876 771 768 266 C ATOM 2306 CG1 VAL A1087 27.572 -14.483 0.048 1.00 79.61 C ANISOU 2306 CG1 VAL A1087 10605 10867 8777 762 707 310 C ATOM 2307 CG2 VAL A1087 28.201 -15.135 -2.282 1.00 81.27 C ANISOU 2307 CG2 VAL A1087 10805 11174 8900 832 825 268 C ATOM 2308 N TYR A1088 23.977 -15.951 -0.953 1.00 76.43 N ANISOU 2308 N TYR A1088 10612 10023 8404 656 755 163 N ATOM 2309 CA TYR A1088 22.631 -15.760 -0.399 1.00 75.53 C ANISOU 2309 CA TYR A1088 10576 9789 8334 556 717 134 C ATOM 2310 C TYR A1088 22.078 -17.062 0.227 1.00 80.49 C ANISOU 2310 C TYR A1088 11351 10259 8971 610 771 82 C ATOM 2311 O TYR A1088 21.487 -17.024 1.311 1.00 77.58 O ANISOU 2311 O TYR A1088 11029 9804 8643 576 746 90 O ATOM 2312 CB TYR A1088 21.716 -15.255 -1.525 1.00 76.91 C ANISOU 2312 CB TYR A1088 10758 9978 8489 454 705 88 C ATOM 2313 CG TYR A1088 20.337 -14.810 -1.096 1.00 78.83 C ANISOU 2313 CG TYR A1088 11040 10146 8764 349 656 56 C ATOM 2314 CD1 TYR A1088 20.155 -13.635 -0.369 1.00 79.94 C ANISOU 2314 CD1 TYR A1088 11129 10306 8940 285 586 115 C ATOM 2315 CD2 TYR A1088 19.204 -15.505 -1.502 1.00 80.46 C ANISOU 2315 CD2 TYR A1088 11331 10282 8960 307 681 -43 C ATOM 2316 CE1 TYR A1088 18.884 -13.213 0.019 1.00 80.68 C ANISOU 2316 CE1 TYR A1088 11254 10344 9056 205 542 85 C ATOM 2317 CE2 TYR A1088 17.928 -15.098 -1.117 1.00 81.53 C ANISOU 2317 CE2 TYR A1088 11481 10378 9119 214 637 -82 C ATOM 2318 CZ TYR A1088 17.771 -13.947 -0.360 1.00 89.94 C ANISOU 2318 CZ TYR A1088 12493 11462 10217 173 566 -13 C ATOM 2319 OH TYR A1088 16.510 -13.539 0.003 1.00 91.58 O ANISOU 2319 OH TYR A1088 12711 11643 10440 97 523 -53 O ATOM 2320 N ASP A1089 22.338 -18.219 -0.437 1.00 80.70 N ANISOU 2320 N ASP A1089 11462 10245 8955 698 855 32 N ATOM 2321 CA ASP A1089 21.943 -19.560 0.023 1.00 80.95 C ANISOU 2321 CA ASP A1089 11667 10108 8982 756 936 -19 C ATOM 2322 C ASP A1089 22.693 -19.995 1.279 1.00 84.93 C ANISOU 2322 C ASP A1089 12208 10576 9486 896 948 48 C ATOM 2323 O ASP A1089 22.117 -20.704 2.095 1.00 86.23 O ANISOU 2323 O ASP A1089 12517 10584 9662 905 992 30 O ATOM 2324 CB ASP A1089 22.170 -20.607 -1.074 1.00 83.53 C ANISOU 2324 CB ASP A1089 12081 10404 9253 823 1030 -88 C ATOM 2325 CG ASP A1089 21.249 -20.502 -2.275 1.00 88.86 C ANISOU 2325 CG ASP A1089 12760 11089 9912 695 1034 -183 C ATOM 2326 OD1 ASP A1089 20.260 -19.729 -2.207 1.00 87.85 O ANISOU 2326 OD1 ASP A1089 12586 10976 9816 557 969 -204 O ATOM 2327 OD2 ASP A1089 21.513 -21.194 -3.280 1.00 92.72 O ANISOU 2327 OD2 ASP A1089 13299 11581 10349 744 1101 -239 O ATOM 2328 N SER A1090 23.967 -19.602 1.434 1.00 80.27 N ANISOU 2328 N SER A1090 11491 10137 8873 1007 914 121 N ATOM 2329 CA SER A1090 24.755 -19.983 2.604 1.00 79.95 C ANISOU 2329 CA SER A1090 11463 10102 8812 1164 912 182 C ATOM 2330 C SER A1090 24.418 -19.117 3.820 1.00 83.74 C ANISOU 2330 C SER A1090 11890 10589 9340 1087 826 227 C ATOM 2331 O SER A1090 24.657 -19.531 4.958 1.00 86.71 O ANISOU 2331 O SER A1090 12326 10920 9701 1196 828 265 O ATOM 2332 CB SER A1090 26.243 -19.899 2.295 1.00 83.78 C ANISOU 2332 CB SER A1090 11807 10783 9244 1311 906 224 C ATOM 2333 OG SER A1090 26.683 -18.555 2.302 1.00 95.48 O ANISOU 2333 OG SER A1090 13086 12440 10751 1210 818 261 O ATOM 2334 N LEU A1091 23.837 -17.939 3.598 1.00 76.89 N ANISOU 2334 N LEU A1091 10926 9768 8520 911 756 225 N ATOM 2335 CA LEU A1091 23.541 -17.006 4.686 1.00 75.08 C ANISOU 2335 CA LEU A1091 10642 9550 8334 832 674 265 C ATOM 2336 C LEU A1091 22.259 -17.317 5.477 1.00 79.34 C ANISOU 2336 C LEU A1091 11323 9912 8910 764 687 237 C ATOM 2337 O LEU A1091 21.308 -17.880 4.952 1.00 81.04 O ANISOU 2337 O LEU A1091 11646 10013 9134 700 742 171 O ATOM 2338 CB LEU A1091 23.439 -15.571 4.128 1.00 73.37 C ANISOU 2338 CB LEU A1091 10288 9444 8145 681 606 276 C ATOM 2339 CG LEU A1091 24.709 -14.932 3.578 1.00 77.23 C ANISOU 2339 CG LEU A1091 10616 10122 8607 701 589 310 C ATOM 2340 CD1 LEU A1091 24.412 -13.555 3.024 1.00 76.79 C ANISOU 2340 CD1 LEU A1091 10481 10123 8573 539 545 321 C ATOM 2341 CD2 LEU A1091 25.821 -14.854 4.630 1.00 78.72 C ANISOU 2341 CD2 LEU A1091 10709 10424 8775 799 554 353 C ATOM 2342 N ASP A1092 22.232 -16.895 6.732 1.00 74.30 N ANISOU 2342 N ASP A1092 10674 9266 8290 766 635 281 N ATOM 2343 CA ASP A1092 21.068 -16.966 7.611 1.00 73.31 C ANISOU 2343 CA ASP A1092 10657 8998 8201 690 638 264 C ATOM 2344 C ASP A1092 20.103 -15.794 7.281 1.00 77.23 C ANISOU 2344 C ASP A1092 11082 9517 8746 509 575 241 C ATOM 2345 O ASP A1092 20.446 -14.901 6.501 1.00 75.69 O ANISOU 2345 O ASP A1092 10768 9439 8551 457 530 252 O ATOM 2346 CB ASP A1092 21.514 -16.926 9.075 1.00 74.60 C ANISOU 2346 CB ASP A1092 10831 9162 8350 781 603 325 C ATOM 2347 CG ASP A1092 22.534 -15.840 9.338 1.00 80.81 C ANISOU 2347 CG ASP A1092 11436 10137 9131 790 508 374 C ATOM 2348 OD1 ASP A1092 23.738 -16.099 9.120 1.00 80.62 O ANISOU 2348 OD1 ASP A1092 11336 10238 9060 916 511 396 O ATOM 2349 OD2 ASP A1092 22.121 -14.708 9.685 1.00 85.57 O ANISOU 2349 OD2 ASP A1092 11970 10770 9774 663 438 383 O ATOM 2350 N ALA A1093 18.904 -15.815 7.865 1.00 74.87 N ANISOU 2350 N ALA A1093 10862 9106 8478 423 582 208 N ATOM 2351 CA ALA A1093 17.842 -14.846 7.610 1.00 74.12 C ANISOU 2351 CA ALA A1093 10718 9026 8417 279 531 178 C ATOM 2352 C ALA A1093 18.299 -13.395 7.788 1.00 77.60 C ANISOU 2352 C ALA A1093 11033 9581 8869 242 436 238 C ATOM 2353 O ALA A1093 18.031 -12.568 6.904 1.00 76.75 O ANISOU 2353 O ALA A1093 10863 9538 8761 171 404 229 O ATOM 2354 CB ALA A1093 16.663 -15.130 8.524 1.00 74.70 C ANISOU 2354 CB ALA A1093 10886 8978 8518 217 554 142 C ATOM 2355 N VAL A1094 18.996 -13.092 8.919 1.00 73.35 N ANISOU 2355 N VAL A1094 10470 9069 8333 292 397 297 N ATOM 2356 CA VAL A1094 19.483 -11.741 9.249 1.00 71.99 C ANISOU 2356 CA VAL A1094 10190 8993 8170 242 317 344 C ATOM 2357 C VAL A1094 20.571 -11.308 8.229 1.00 77.03 C ANISOU 2357 C VAL A1094 10719 9765 8784 247 313 362 C ATOM 2358 O VAL A1094 20.478 -10.219 7.666 1.00 77.02 O ANISOU 2358 O VAL A1094 10665 9811 8788 155 284 372 O ATOM 2359 CB VAL A1094 19.978 -11.642 10.721 1.00 75.24 C ANISOU 2359 CB VAL A1094 10598 9411 8577 294 279 385 C ATOM 2360 CG1 VAL A1094 20.249 -10.201 11.116 1.00 74.41 C ANISOU 2360 CG1 VAL A1094 10404 9384 8486 207 203 412 C ATOM 2361 CG2 VAL A1094 18.963 -12.257 11.686 1.00 74.55 C ANISOU 2361 CG2 VAL A1094 10637 9184 8504 303 306 369 C ATOM 2362 N ARG A1095 21.542 -12.192 7.937 1.00 73.55 N ANISOU 2362 N ARG A1095 10259 9376 8310 359 354 366 N ATOM 2363 CA ARG A1095 22.638 -11.921 7.008 1.00 72.87 C ANISOU 2363 CA ARG A1095 10064 9429 8196 373 363 378 C ATOM 2364 C ARG A1095 22.164 -11.801 5.564 1.00 76.85 C ANISOU 2364 C ARG A1095 10580 9927 8693 314 397 349 C ATOM 2365 O ARG A1095 22.765 -11.040 4.800 1.00 76.58 O ANISOU 2365 O ARG A1095 10460 9994 8642 266 394 367 O ATOM 2366 CB ARG A1095 23.741 -12.960 7.145 1.00 69.85 C ANISOU 2366 CB ARG A1095 9659 9112 7770 534 399 385 C ATOM 2367 CG ARG A1095 24.579 -12.656 8.374 1.00 76.39 C ANISOU 2367 CG ARG A1095 10408 10035 8582 587 345 418 C ATOM 2368 CD ARG A1095 25.696 -13.626 8.516 1.00 81.45 C ANISOU 2368 CD ARG A1095 11014 10768 9163 774 373 427 C ATOM 2369 NE ARG A1095 26.506 -13.379 9.704 1.00 83.11 N ANISOU 2369 NE ARG A1095 11136 11100 9343 844 313 449 N ATOM 2370 CZ ARG A1095 26.488 -14.137 10.795 1.00 89.00 C ANISOU 2370 CZ ARG A1095 11968 11794 10055 987 309 467 C ATOM 2371 NH1 ARG A1095 25.680 -15.185 10.868 1.00 72.33 N ANISOU 2371 NH1 ARG A1095 10047 9491 7943 1059 375 467 N ATOM 2372 NH2 ARG A1095 27.284 -13.855 11.822 1.00 63.35 N ANISOU 2372 NH2 ARG A1095 8620 8688 6764 1058 245 481 N ATOM 2373 N ARG A1096 21.063 -12.490 5.201 1.00 72.52 N ANISOU 2373 N ARG A1096 10137 9265 8150 306 431 299 N ATOM 2374 CA ARG A1096 20.460 -12.381 3.867 1.00 70.88 C ANISOU 2374 CA ARG A1096 9942 9063 7926 253 452 259 C ATOM 2375 C ARG A1096 19.896 -10.979 3.679 1.00 72.89 C ANISOU 2375 C ARG A1096 10164 9344 8189 147 397 280 C ATOM 2376 O ARG A1096 20.021 -10.412 2.597 1.00 74.36 O ANISOU 2376 O ARG A1096 10318 9594 8343 118 403 287 O ATOM 2377 CB ARG A1096 19.359 -13.422 3.682 1.00 71.54 C ANISOU 2377 CB ARG A1096 10137 9035 8012 252 498 182 C ATOM 2378 CG ARG A1096 19.866 -14.765 3.184 1.00 88.55 C ANISOU 2378 CG ARG A1096 12348 11162 10135 349 578 147 C ATOM 2379 CD ARG A1096 18.722 -15.684 2.810 1.00102.96 C ANISOU 2379 CD ARG A1096 14283 12879 11956 307 634 52 C ATOM 2380 NE ARG A1096 18.467 -16.672 3.855 1.00118.75 N ANISOU 2380 NE ARG A1096 16403 14743 13974 344 687 36 N ATOM 2381 CZ ARG A1096 18.815 -17.952 3.775 1.00140.57 C ANISOU 2381 CZ ARG A1096 19277 17421 16710 432 778 8 C ATOM 2382 NH1 ARG A1096 19.462 -18.407 2.706 1.00124.66 N ANISOU 2382 NH1 ARG A1096 17256 15455 14654 495 820 -11 N ATOM 2383 NH2 ARG A1096 18.564 -18.778 4.782 1.00134.90 N ANISOU 2383 NH2 ARG A1096 18692 16564 16001 467 836 5 N ATOM 2384 N ALA A1097 19.306 -10.410 4.749 1.00 66.96 N ANISOU 2384 N ALA A1097 9432 8539 7472 100 350 295 N ATOM 2385 CA ALA A1097 18.735 -9.068 4.752 1.00 65.20 C ANISOU 2385 CA ALA A1097 9200 8320 7252 17 301 319 C ATOM 2386 C ALA A1097 19.856 -8.028 4.527 1.00 67.38 C ANISOU 2386 C ALA A1097 9404 8685 7514 -20 293 378 C ATOM 2387 O ALA A1097 19.672 -7.096 3.745 1.00 67.21 O ANISOU 2387 O ALA A1097 9388 8684 7464 -70 292 398 O ATOM 2388 CB ALA A1097 17.997 -8.811 6.073 1.00 65.07 C ANISOU 2388 CB ALA A1097 9223 8227 7273 -10 261 321 C ATOM 2389 N ALA A1098 21.030 -8.223 5.172 1.00 63.07 N ANISOU 2389 N ALA A1098 8791 8197 6977 8 294 402 N ATOM 2390 CA ALA A1098 22.186 -7.341 5.012 1.00 62.83 C ANISOU 2390 CA ALA A1098 8671 8270 6931 -47 298 438 C ATOM 2391 C ALA A1098 22.657 -7.388 3.562 1.00 66.07 C ANISOU 2391 C ALA A1098 9054 8750 7301 -42 353 439 C ATOM 2392 O ALA A1098 22.900 -6.327 2.997 1.00 67.05 O ANISOU 2392 O ALA A1098 9167 8905 7404 -126 368 467 O ATOM 2393 CB ALA A1098 23.305 -7.724 5.971 1.00 63.95 C ANISOU 2393 CB ALA A1098 8726 8494 7077 1 284 443 C ATOM 2394 N LEU A1099 22.638 -8.584 2.916 1.00 61.37 N ANISOU 2394 N LEU A1099 8473 8158 6687 51 390 406 N ATOM 2395 CA LEU A1099 23.006 -8.723 1.496 1.00 60.84 C ANISOU 2395 CA LEU A1099 8388 8154 6573 66 444 400 C ATOM 2396 C LEU A1099 21.926 -8.109 0.592 1.00 64.51 C ANISOU 2396 C LEU A1099 8931 8570 7011 18 441 395 C ATOM 2397 O LEU A1099 22.291 -7.509 -0.417 1.00 63.87 O ANISOU 2397 O LEU A1099 8838 8546 6885 -11 476 419 O ATOM 2398 CB LEU A1099 23.304 -10.181 1.100 1.00 60.83 C ANISOU 2398 CB LEU A1099 8393 8165 6553 185 489 359 C ATOM 2399 CG LEU A1099 23.877 -10.390 -0.316 1.00 66.36 C ANISOU 2399 CG LEU A1099 9065 8949 7200 213 549 351 C ATOM 2400 CD1 LEU A1099 25.299 -9.850 -0.444 1.00 66.89 C ANISOU 2400 CD1 LEU A1099 9007 9159 7249 194 576 389 C ATOM 2401 CD2 LEU A1099 23.782 -11.830 -0.738 1.00 69.16 C ANISOU 2401 CD2 LEU A1099 9472 9271 7535 324 594 298 C ATOM 2402 N ILE A1100 20.611 -8.229 0.948 1.00 61.91 N ANISOU 2402 N ILE A1100 8677 8148 6698 17 402 363 N ATOM 2403 CA ILE A1100 19.517 -7.603 0.160 1.00 61.68 C ANISOU 2403 CA ILE A1100 8708 8099 6629 -7 387 352 C ATOM 2404 C ILE A1100 19.701 -6.070 0.202 1.00 63.05 C ANISOU 2404 C ILE A1100 8894 8275 6787 -76 375 421 C ATOM 2405 O ILE A1100 19.679 -5.426 -0.827 1.00 61.11 O ANISOU 2405 O ILE A1100 8679 8059 6481 -82 400 447 O ATOM 2406 CB ILE A1100 18.064 -8.028 0.609 1.00 64.17 C ANISOU 2406 CB ILE A1100 9077 8343 6962 1 348 291 C ATOM 2407 CG1 ILE A1100 17.829 -9.552 0.392 1.00 64.28 C ANISOU 2407 CG1 ILE A1100 9105 8338 6981 48 383 211 C ATOM 2408 CG2 ILE A1100 16.978 -7.186 -0.154 1.00 63.13 C ANISOU 2408 CG2 ILE A1100 8987 8228 6773 -5 319 283 C ATOM 2409 CD1 ILE A1100 16.782 -10.181 1.260 1.00 65.45 C ANISOU 2409 CD1 ILE A1100 9296 8405 7168 33 369 150 C ATOM 2410 N ASN A1101 19.924 -5.522 1.401 1.00 61.16 N ANISOU 2410 N ASN A1101 8643 8000 6595 -127 345 450 N ATOM 2411 CA ASN A1101 20.153 -4.114 1.660 1.00 62.03 C ANISOU 2411 CA ASN A1101 8780 8090 6698 -208 343 506 C ATOM 2412 C ASN A1101 21.232 -3.525 0.704 1.00 70.80 C ANISOU 2412 C ASN A1101 9867 9269 7764 -258 412 546 C ATOM 2413 O ASN A1101 21.013 -2.469 0.093 1.00 72.14 O ANISOU 2413 O ASN A1101 10116 9409 7884 -296 439 587 O ATOM 2414 CB ASN A1101 20.577 -3.961 3.116 1.00 58.84 C ANISOU 2414 CB ASN A1101 8337 7666 6353 -253 310 511 C ATOM 2415 CG ASN A1101 20.616 -2.544 3.605 1.00 76.26 C ANISOU 2415 CG ASN A1101 10592 9827 8558 -349 304 552 C ATOM 2416 OD1 ASN A1101 21.255 -1.651 3.009 1.00 72.08 O ANISOU 2416 OD1 ASN A1101 10076 9316 7994 -422 355 587 O ATOM 2417 ND2 ASN A1101 19.951 -2.324 4.725 1.00 61.33 N ANISOU 2417 ND2 ASN A1101 8736 7866 6702 -354 251 544 N ATOM 2418 N MET A1102 22.375 -4.237 0.562 1.00 68.20 N ANISOU 2418 N MET A1102 9435 9033 7443 -248 447 533 N ATOM 2419 CA MET A1102 23.507 -3.850 -0.282 1.00 68.40 C ANISOU 2419 CA MET A1102 9410 9148 7430 -298 521 558 C ATOM 2420 C MET A1102 23.099 -3.749 -1.759 1.00 73.60 C ANISOU 2420 C MET A1102 10142 9808 8014 -261 566 572 C ATOM 2421 O MET A1102 23.379 -2.734 -2.391 1.00 75.46 O ANISOU 2421 O MET A1102 10429 10041 8202 -328 623 618 O ATOM 2422 CB MET A1102 24.656 -4.848 -0.098 1.00 70.44 C ANISOU 2422 CB MET A1102 9534 9523 7706 -255 539 529 C ATOM 2423 CG MET A1102 25.490 -4.588 1.136 1.00 73.15 C ANISOU 2423 CG MET A1102 9781 9922 8092 -313 514 524 C ATOM 2424 SD MET A1102 26.930 -5.675 1.217 1.00 76.84 S ANISOU 2424 SD MET A1102 10077 10566 8552 -231 539 492 S ATOM 2425 CE MET A1102 27.991 -4.917 0.018 1.00 74.13 C ANISOU 2425 CE MET A1102 9666 10343 8158 -335 639 508 C ATOM 2426 N VAL A1103 22.421 -4.795 -2.292 1.00 67.66 N ANISOU 2426 N VAL A1103 9405 9057 7247 -156 547 527 N ATOM 2427 CA VAL A1103 21.916 -4.906 -3.665 1.00 66.17 C ANISOU 2427 CA VAL A1103 9276 8886 6979 -99 574 520 C ATOM 2428 C VAL A1103 20.870 -3.820 -3.925 1.00 72.63 C ANISOU 2428 C VAL A1103 10211 9638 7747 -104 551 554 C ATOM 2429 O VAL A1103 20.826 -3.250 -5.007 1.00 75.27 O ANISOU 2429 O VAL A1103 10611 9991 7997 -89 594 588 O ATOM 2430 CB VAL A1103 21.348 -6.334 -3.895 1.00 68.41 C ANISOU 2430 CB VAL A1103 9546 9178 7267 -4 551 441 C ATOM 2431 CG1 VAL A1103 20.555 -6.436 -5.206 1.00 68.09 C ANISOU 2431 CG1 VAL A1103 9569 9163 7140 54 558 413 C ATOM 2432 CG2 VAL A1103 22.474 -7.365 -3.859 1.00 68.11 C ANISOU 2432 CG2 VAL A1103 9420 9206 7253 32 593 419 C ATOM 2433 N PHE A1104 20.020 -3.541 -2.944 1.00 68.66 N ANISOU 2433 N PHE A1104 9740 9061 7285 -111 486 546 N ATOM 2434 CA PHE A1104 19.019 -2.493 -3.034 1.00 67.84 C ANISOU 2434 CA PHE A1104 9746 8897 7132 -96 460 578 C ATOM 2435 C PHE A1104 19.719 -1.112 -3.203 1.00 74.25 C ANISOU 2435 C PHE A1104 10634 9670 7909 -177 526 663 C ATOM 2436 O PHE A1104 19.264 -0.266 -3.991 1.00 74.47 O ANISOU 2436 O PHE A1104 10779 9670 7846 -139 552 710 O ATOM 2437 CB PHE A1104 18.156 -2.537 -1.770 1.00 67.96 C ANISOU 2437 CB PHE A1104 9762 8848 7211 -97 386 549 C ATOM 2438 CG PHE A1104 17.063 -1.506 -1.685 1.00 69.44 C ANISOU 2438 CG PHE A1104 10054 8979 7351 -63 352 575 C ATOM 2439 CD1 PHE A1104 17.344 -0.200 -1.294 1.00 71.71 C ANISOU 2439 CD1 PHE A1104 10429 9190 7629 -121 378 647 C ATOM 2440 CD2 PHE A1104 15.741 -1.849 -1.953 1.00 72.48 C ANISOU 2440 CD2 PHE A1104 10449 9393 7696 28 297 519 C ATOM 2441 CE1 PHE A1104 16.329 0.747 -1.200 1.00 73.41 C ANISOU 2441 CE1 PHE A1104 10757 9345 7790 -66 351 674 C ATOM 2442 CE2 PHE A1104 14.719 -0.904 -1.827 1.00 75.47 C ANISOU 2442 CE2 PHE A1104 10914 9740 8022 84 261 541 C ATOM 2443 CZ PHE A1104 15.022 0.388 -1.461 1.00 73.53 C ANISOU 2443 CZ PHE A1104 10770 9404 7762 49 289 624 C ATOM 2444 N GLN A1105 20.834 -0.902 -2.475 1.00 71.21 N ANISOU 2444 N GLN A1105 10186 9286 7585 -287 558 679 N ATOM 2445 CA GLN A1105 21.561 0.358 -2.522 1.00 71.67 C ANISOU 2445 CA GLN A1105 10310 9303 7619 -401 634 741 C ATOM 2446 C GLN A1105 22.460 0.496 -3.741 1.00 77.48 C ANISOU 2446 C GLN A1105 11046 10103 8289 -432 736 771 C ATOM 2447 O GLN A1105 22.467 1.562 -4.346 1.00 78.54 O ANISOU 2447 O GLN A1105 11313 10176 8351 -468 808 832 O ATOM 2448 CB GLN A1105 22.404 0.517 -1.256 1.00 72.92 C ANISOU 2448 CB GLN A1105 10380 9466 7861 -521 627 725 C ATOM 2449 CG GLN A1105 23.091 1.884 -1.136 1.00 77.78 C ANISOU 2449 CG GLN A1105 11069 10027 8457 -674 709 770 C ATOM 2450 CD GLN A1105 24.145 1.928 -0.069 1.00 86.10 C ANISOU 2450 CD GLN A1105 11995 11138 9581 -805 709 734 C ATOM 2451 OE1 GLN A1105 24.366 0.969 0.674 1.00 88.13 O ANISOU 2451 OE1 GLN A1105 12116 11473 9897 -762 641 685 O ATOM 2452 NE2 GLN A1105 24.833 3.043 0.025 1.00 71.29 N ANISOU 2452 NE2 GLN A1105 10167 9230 7690 -966 791 752 N ATOM 2453 N MET A1106 23.244 -0.540 -4.079 1.00 75.03 N ANISOU 2453 N MET A1106 10601 9908 7999 -415 752 732 N ATOM 2454 CA MET A1106 24.258 -0.477 -5.138 1.00 76.13 C ANISOU 2454 CA MET A1106 10714 10129 8084 -454 856 753 C ATOM 2455 C MET A1106 23.941 -1.265 -6.394 1.00 78.26 C ANISOU 2455 C MET A1106 10993 10457 8283 -329 866 739 C ATOM 2456 O MET A1106 24.630 -1.098 -7.401 1.00 79.87 O ANISOU 2456 O MET A1106 11205 10718 8423 -348 959 765 O ATOM 2457 CB MET A1106 25.586 -1.009 -4.591 1.00 79.57 C ANISOU 2457 CB MET A1106 10970 10681 8583 -528 880 716 C ATOM 2458 CG MET A1106 26.235 -0.115 -3.555 1.00 84.87 C ANISOU 2458 CG MET A1106 11609 11335 9303 -686 897 721 C ATOM 2459 SD MET A1106 27.555 -1.040 -2.726 1.00 90.88 S ANISOU 2459 SD MET A1106 12125 12272 10131 -709 878 654 S ATOM 2460 CE MET A1106 26.619 -1.905 -1.511 1.00 86.26 C ANISOU 2460 CE MET A1106 11532 11628 9616 -589 741 619 C ATOM 2461 N GLY A1107 22.954 -2.142 -6.327 1.00 72.32 N ANISOU 2461 N GLY A1107 10237 9700 7542 -212 780 688 N ATOM 2462 CA GLY A1107 22.583 -3.000 -7.444 1.00 71.94 C ANISOU 2462 CA GLY A1107 10192 9712 7429 -100 780 651 C ATOM 2463 C GLY A1107 23.379 -4.285 -7.439 1.00 77.35 C ANISOU 2463 C GLY A1107 10746 10485 8157 -72 792 594 C ATOM 2464 O GLY A1107 24.467 -4.348 -6.860 1.00 78.15 O ANISOU 2464 O GLY A1107 10748 10631 8314 -137 824 599 O ATOM 2465 N GLU A1108 22.823 -5.319 -8.073 1.00 74.06 N ANISOU 2465 N GLU A1108 10331 10099 7710 30 768 531 N ATOM 2466 CA GLU A1108 23.371 -6.669 -8.221 1.00 74.42 C ANISOU 2466 CA GLU A1108 10291 10206 7777 88 785 469 C ATOM 2467 C GLU A1108 24.819 -6.658 -8.750 1.00 79.22 C ANISOU 2467 C GLU A1108 10822 10915 8364 64 879 499 C ATOM 2468 O GLU A1108 25.679 -7.364 -8.235 1.00 78.39 O ANISOU 2468 O GLU A1108 10614 10862 8309 79 893 475 O ATOM 2469 CB GLU A1108 22.490 -7.487 -9.193 1.00 76.09 C ANISOU 2469 CB GLU A1108 10554 10433 7922 182 768 399 C ATOM 2470 CG GLU A1108 21.001 -7.517 -8.871 1.00 91.10 C ANISOU 2470 CG GLU A1108 12515 12274 9826 203 682 351 C ATOM 2471 CD GLU A1108 20.106 -6.353 -9.275 1.00117.50 C ANISOU 2471 CD GLU A1108 15946 15604 13095 210 651 392 C ATOM 2472 OE1 GLU A1108 20.632 -5.317 -9.736 1.00115.53 O ANISOU 2472 OE1 GLU A1108 15742 15360 12792 184 704 478 O ATOM 2473 OE2 GLU A1108 18.872 -6.462 -9.090 1.00115.94 O ANISOU 2473 OE2 GLU A1108 15776 15390 12888 242 580 338 O ATOM 2474 N THR A1109 25.066 -5.881 -9.799 1.00 78.03 N ANISOU 2474 N THR A1109 10724 10797 8128 39 948 548 N ATOM 2475 CA THR A1109 26.366 -5.786 -10.457 1.00 79.30 C ANISOU 2475 CA THR A1109 10817 11062 8253 5 1053 574 C ATOM 2476 C THR A1109 27.375 -5.150 -9.474 1.00 84.00 C ANISOU 2476 C THR A1109 11314 11685 8917 -120 1080 604 C ATOM 2477 O THR A1109 28.503 -5.632 -9.386 1.00 85.09 O ANISOU 2477 O THR A1109 11319 11938 9074 -124 1126 583 O ATOM 2478 CB THR A1109 26.184 -5.060 -11.814 1.00 86.00 C ANISOU 2478 CB THR A1109 11778 11917 8981 10 1122 622 C ATOM 2479 OG1 THR A1109 25.963 -6.050 -12.829 1.00 84.40 O ANISOU 2479 OG1 THR A1109 11583 11772 8713 127 1128 568 O ATOM 2480 CG2 THR A1109 27.359 -4.137 -12.198 1.00 84.89 C ANISOU 2480 CG2 THR A1109 11618 11830 8807 -106 1247 687 C ATOM 2481 N GLY A1110 26.947 -4.120 -8.737 1.00 79.04 N ANISOU 2481 N GLY A1110 10748 10964 8320 -212 1050 643 N ATOM 2482 CA GLY A1110 27.784 -3.435 -7.761 1.00 78.66 C ANISOU 2482 CA GLY A1110 10619 10937 8332 -348 1070 659 C ATOM 2483 C GLY A1110 28.313 -4.363 -6.685 1.00 82.02 C ANISOU 2483 C GLY A1110 10891 11434 8839 -311 1012 604 C ATOM 2484 O GLY A1110 29.529 -4.473 -6.509 1.00 83.39 O ANISOU 2484 O GLY A1110 10920 11740 9024 -355 1060 587 O ATOM 2485 N VAL A1111 27.398 -5.089 -6.010 1.00 76.11 N ANISOU 2485 N VAL A1111 10174 10609 8136 -217 913 572 N ATOM 2486 CA VAL A1111 27.695 -6.017 -4.913 1.00 75.34 C ANISOU 2486 CA VAL A1111 9975 10545 8106 -155 854 528 C ATOM 2487 C VAL A1111 28.542 -7.212 -5.412 1.00 80.87 C ANISOU 2487 C VAL A1111 10577 11367 8782 -41 896 490 C ATOM 2488 O VAL A1111 29.455 -7.637 -4.707 1.00 81.35 O ANISOU 2488 O VAL A1111 10509 11530 8870 -13 892 470 O ATOM 2489 CB VAL A1111 26.396 -6.460 -4.176 1.00 76.59 C ANISOU 2489 CB VAL A1111 10222 10571 8308 -94 760 506 C ATOM 2490 CG1 VAL A1111 26.680 -7.509 -3.110 1.00 75.54 C ANISOU 2490 CG1 VAL A1111 10016 10457 8229 -12 715 468 C ATOM 2491 CG2 VAL A1111 25.707 -5.255 -3.545 1.00 75.44 C ANISOU 2491 CG2 VAL A1111 10155 10325 8184 -196 721 543 C ATOM 2492 N ALA A1112 28.289 -7.700 -6.639 1.00 78.01 N ANISOU 2492 N ALA A1112 10273 11007 8359 31 939 479 N ATOM 2493 CA ALA A1112 29.015 -8.818 -7.251 1.00 77.90 C ANISOU 2493 CA ALA A1112 10193 11094 8312 149 988 441 C ATOM 2494 C ALA A1112 30.499 -8.492 -7.460 1.00 83.46 C ANISOU 2494 C ALA A1112 10744 11974 8993 103 1067 454 C ATOM 2495 O ALA A1112 31.290 -9.404 -7.691 1.00 85.32 O ANISOU 2495 O ALA A1112 10891 12320 9206 212 1103 422 O ATOM 2496 CB ALA A1112 28.369 -9.197 -8.568 1.00 78.50 C ANISOU 2496 CB ALA A1112 10374 11135 8317 209 1019 424 C ATOM 2497 N GLY A1113 30.862 -7.213 -7.331 1.00 79.06 N ANISOU 2497 N GLY A1113 10158 11442 8438 -59 1099 493 N ATOM 2498 CA GLY A1113 32.237 -6.746 -7.447 1.00 79.86 C ANISOU 2498 CA GLY A1113 10104 11717 8521 -149 1182 493 C ATOM 2499 C GLY A1113 33.052 -7.019 -6.200 1.00 84.16 C ANISOU 2499 C GLY A1113 10479 12382 9116 -139 1136 457 C ATOM 2500 O GLY A1113 34.282 -6.984 -6.246 1.00 86.10 O ANISOU 2500 O GLY A1113 10552 12822 9340 -169 1195 432 O ATOM 2501 N PHE A1114 32.372 -7.283 -5.072 1.00 79.20 N ANISOU 2501 N PHE A1114 9893 11652 8545 -95 1033 450 N ATOM 2502 CA PHE A1114 32.991 -7.588 -3.782 1.00 79.31 C ANISOU 2502 CA PHE A1114 9770 11766 8597 -59 973 418 C ATOM 2503 C PHE A1114 33.360 -9.076 -3.742 1.00 86.93 C ANISOU 2503 C PHE A1114 10684 12804 9541 168 962 386 C ATOM 2504 O PHE A1114 32.830 -9.828 -2.917 1.00 86.94 O ANISOU 2504 O PHE A1114 10745 12717 9571 286 890 378 O ATOM 2505 CB PHE A1114 32.047 -7.224 -2.620 1.00 78.85 C ANISOU 2505 CB PHE A1114 9804 11555 8600 -101 877 431 C ATOM 2506 CG PHE A1114 31.757 -5.762 -2.415 1.00 79.85 C ANISOU 2506 CG PHE A1114 9983 11609 8746 -308 884 459 C ATOM 2507 CD1 PHE A1114 32.499 -5.010 -1.515 1.00 84.02 C ANISOU 2507 CD1 PHE A1114 10392 12237 9296 -439 875 437 C ATOM 2508 CD2 PHE A1114 30.684 -5.154 -3.050 1.00 81.17 C ANISOU 2508 CD2 PHE A1114 10332 11604 8905 -361 896 501 C ATOM 2509 CE1 PHE A1114 32.197 -3.662 -1.284 1.00 84.62 C ANISOU 2509 CE1 PHE A1114 10545 12219 9388 -633 891 459 C ATOM 2510 CE2 PHE A1114 30.378 -3.810 -2.814 1.00 83.86 C ANISOU 2510 CE2 PHE A1114 10750 11857 9256 -529 908 532 C ATOM 2511 CZ PHE A1114 31.138 -3.073 -1.935 1.00 82.52 C ANISOU 2511 CZ PHE A1114 10479 11764 9112 -670 911 512 C ATOM 2512 N THR A1115 34.263 -9.494 -4.646 1.00 85.41 N ANISOU 2512 N THR A1115 10397 12765 9292 231 1042 369 N ATOM 2513 CA THR A1115 34.712 -10.874 -4.835 1.00 86.26 C ANISOU 2513 CA THR A1115 10470 12946 9361 458 1057 339 C ATOM 2514 C THR A1115 35.243 -11.518 -3.534 1.00 90.25 C ANISOU 2514 C THR A1115 10872 13543 9875 596 990 316 C ATOM 2515 O THR A1115 34.791 -12.620 -3.193 1.00 89.47 O ANISOU 2515 O THR A1115 10879 13339 9775 776 959 312 O ATOM 2516 CB THR A1115 35.745 -10.913 -5.967 1.00 96.59 C ANISOU 2516 CB THR A1115 11660 14438 10602 468 1162 325 C ATOM 2517 OG1 THR A1115 35.044 -10.649 -7.180 1.00 94.99 O ANISOU 2517 OG1 THR A1115 11604 14112 10376 406 1215 349 O ATOM 2518 CG2 THR A1115 36.476 -12.263 -6.073 1.00 97.44 C ANISOU 2518 CG2 THR A1115 11698 14667 10658 715 1185 290 C ATOM 2519 N ASN A1116 36.186 -10.853 -2.825 1.00 87.23 N ANISOU 2519 N ASN A1116 10294 13355 9492 513 974 297 N ATOM 2520 CA ASN A1116 36.745 -11.404 -1.588 1.00 87.28 C ANISOU 2520 CA ASN A1116 10189 13483 9489 657 904 272 C ATOM 2521 C ASN A1116 35.668 -11.478 -0.513 1.00 87.90 C ANISOU 2521 C ASN A1116 10423 13352 9624 667 812 297 C ATOM 2522 O ASN A1116 35.422 -12.567 -0.005 1.00 88.47 O ANISOU 2522 O ASN A1116 10577 13354 9682 871 780 300 O ATOM 2523 CB ASN A1116 37.962 -10.604 -1.095 1.00 91.76 C ANISOU 2523 CB ASN A1116 10497 14331 10037 544 903 229 C ATOM 2524 CG ASN A1116 39.159 -10.549 -2.036 1.00124.07 C ANISOU 2524 CG ASN A1116 14397 18675 14068 533 1001 192 C ATOM 2525 OD1 ASN A1116 39.171 -11.115 -3.140 1.00115.22 O ANISOU 2525 OD1 ASN A1116 13335 17530 12912 622 1075 204 O ATOM 2526 ND2 ASN A1116 40.212 -9.855 -1.603 1.00120.13 N ANISOU 2526 ND2 ASN A1116 13656 18438 13549 413 1006 137 N ATOM 2527 N SER A1117 34.976 -10.352 -0.226 1.00 81.05 N ANISOU 2527 N SER A1117 9617 12367 8814 452 781 315 N ATOM 2528 CA SER A1117 33.922 -10.266 0.790 1.00 78.28 C ANISOU 2528 CA SER A1117 9402 11823 8515 437 698 336 C ATOM 2529 C SER A1117 32.860 -11.321 0.598 1.00 80.20 C ANISOU 2529 C SER A1117 9849 11854 8769 578 694 353 C ATOM 2530 O SER A1117 32.491 -11.956 1.569 1.00 80.00 O ANISOU 2530 O SER A1117 9891 11751 8755 692 641 356 O ATOM 2531 CB SER A1117 33.258 -8.895 0.793 1.00 80.13 C ANISOU 2531 CB SER A1117 9701 11945 8798 194 689 356 C ATOM 2532 OG SER A1117 34.189 -7.851 1.006 1.00 91.34 O ANISOU 2532 OG SER A1117 10955 13539 10212 27 706 331 O ATOM 2533 N LEU A1118 32.379 -11.531 -0.636 1.00 76.43 N ANISOU 2533 N LEU A1118 9473 11286 8281 570 754 358 N ATOM 2534 CA LEU A1118 31.335 -12.526 -0.905 1.00 75.84 C ANISOU 2534 CA LEU A1118 9587 11015 8212 676 759 353 C ATOM 2535 C LEU A1118 31.872 -13.945 -0.656 1.00 82.48 C ANISOU 2535 C LEU A1118 10436 11893 9009 915 781 335 C ATOM 2536 O LEU A1118 31.194 -14.762 -0.026 1.00 80.87 O ANISOU 2536 O LEU A1118 10370 11537 8818 1013 762 332 O ATOM 2537 CB LEU A1118 30.770 -12.374 -2.333 1.00 75.03 C ANISOU 2537 CB LEU A1118 9573 10843 8093 610 815 350 C ATOM 2538 CG LEU A1118 29.905 -11.136 -2.599 1.00 77.30 C ANISOU 2538 CG LEU A1118 9923 11037 8410 419 794 375 C ATOM 2539 CD1 LEU A1118 29.769 -10.896 -4.062 1.00 77.05 C ANISOU 2539 CD1 LEU A1118 9932 11011 8332 378 859 377 C ATOM 2540 CD2 LEU A1118 28.526 -11.260 -1.954 1.00 76.95 C ANISOU 2540 CD2 LEU A1118 10026 10800 8413 405 731 372 C ATOM 2541 N ARG A1119 33.125 -14.194 -1.069 1.00 82.90 N ANISOU 2541 N ARG A1119 10340 12153 9005 1009 826 322 N ATOM 2542 CA ARG A1119 33.782 -15.480 -0.874 1.00 85.17 C ANISOU 2542 CA ARG A1119 10626 12502 9234 1263 854 308 C ATOM 2543 C ARG A1119 33.892 -15.808 0.640 1.00 91.98 C ANISOU 2543 C ARG A1119 11484 13367 10096 1378 784 321 C ATOM 2544 O ARG A1119 33.550 -16.920 1.044 1.00 92.76 O ANISOU 2544 O ARG A1119 11736 13334 10173 1556 797 325 O ATOM 2545 CB ARG A1119 35.159 -15.489 -1.570 1.00 86.50 C ANISOU 2545 CB ARG A1119 10597 12933 9335 1332 911 289 C ATOM 2546 CG ARG A1119 36.000 -16.744 -1.314 1.00103.79 C ANISOU 2546 CG ARG A1119 12761 15228 11447 1626 937 277 C ATOM 2547 CD ARG A1119 37.201 -16.881 -2.240 1.00124.84 C ANISOU 2547 CD ARG A1119 15256 18136 14042 1706 1009 251 C ATOM 2548 NE ARG A1119 37.977 -15.643 -2.364 1.00139.31 N ANISOU 2548 NE ARG A1119 16849 20201 15883 1513 1004 238 N ATOM 2549 CZ ARG A1119 38.179 -14.997 -3.510 1.00155.69 C ANISOU 2549 CZ ARG A1119 18864 22335 17954 1358 1073 230 C ATOM 2550 NH1 ARG A1119 38.885 -13.876 -3.529 1.00147.63 N ANISOU 2550 NH1 ARG A1119 17642 21511 16940 1168 1083 215 N ATOM 2551 NH2 ARG A1119 37.683 -15.475 -4.647 1.00138.62 N ANISOU 2551 NH2 ARG A1119 16851 20039 15778 1386 1141 234 N ATOM 2552 N MET A1120 34.297 -14.840 1.473 1.00 89.16 N ANISOU 2552 N MET A1120 10976 13142 9759 1269 718 325 N ATOM 2553 CA MET A1120 34.446 -15.109 2.904 1.00 89.26 C ANISOU 2553 CA MET A1120 10976 13182 9759 1384 647 334 C ATOM 2554 C MET A1120 33.133 -15.106 3.669 1.00 88.36 C ANISOU 2554 C MET A1120 11058 12809 9705 1323 603 358 C ATOM 2555 O MET A1120 33.066 -15.759 4.700 1.00 87.31 O ANISOU 2555 O MET A1120 10995 12631 9547 1476 572 372 O ATOM 2556 CB MET A1120 35.440 -14.171 3.538 1.00 93.15 C ANISOU 2556 CB MET A1120 11222 13935 10235 1303 591 312 C ATOM 2557 CG MET A1120 36.835 -14.483 3.087 1.00 99.91 C ANISOU 2557 CG MET A1120 11869 15081 11010 1433 630 279 C ATOM 2558 SD MET A1120 37.965 -13.234 3.647 1.00106.99 S ANISOU 2558 SD MET A1120 12453 16306 11893 1266 580 227 S ATOM 2559 CE MET A1120 37.103 -11.695 3.081 1.00102.11 C ANISOU 2559 CE MET A1120 11903 15518 11378 878 600 238 C ATOM 2560 N LEU A1121 32.083 -14.439 3.156 1.00 83.01 N ANISOU 2560 N LEU A1121 10478 11966 9095 1120 607 363 N ATOM 2561 CA LEU A1121 30.747 -14.484 3.757 1.00 80.77 C ANISOU 2561 CA LEU A1121 10378 11444 8866 1061 576 376 C ATOM 2562 C LEU A1121 30.199 -15.898 3.603 1.00 86.39 C ANISOU 2562 C LEU A1121 11284 11983 9556 1226 634 369 C ATOM 2563 O LEU A1121 29.543 -16.426 4.494 1.00 86.01 O ANISOU 2563 O LEU A1121 11374 11787 9520 1283 621 378 O ATOM 2564 CB LEU A1121 29.801 -13.482 3.079 1.00 78.75 C ANISOU 2564 CB LEU A1121 10169 11083 8669 835 572 376 C ATOM 2565 CG LEU A1121 29.866 -12.031 3.483 1.00 81.84 C ANISOU 2565 CG LEU A1121 10461 11538 9096 644 519 388 C ATOM 2566 CD1 LEU A1121 28.919 -11.220 2.625 1.00 80.89 C ANISOU 2566 CD1 LEU A1121 10423 11302 9011 475 534 395 C ATOM 2567 CD2 LEU A1121 29.560 -11.833 4.963 1.00 82.08 C ANISOU 2567 CD2 LEU A1121 10511 11524 9151 643 445 399 C ATOM 2568 N GLN A1122 30.497 -16.509 2.455 1.00 85.84 N ANISOU 2568 N GLN A1122 11232 11933 9450 1296 707 348 N ATOM 2569 CA GLN A1122 30.116 -17.871 2.110 1.00 86.93 C ANISOU 2569 CA GLN A1122 11556 11915 9557 1446 783 328 C ATOM 2570 C GLN A1122 30.829 -18.865 3.043 1.00 91.99 C ANISOU 2570 C GLN A1122 12233 12588 10134 1699 795 348 C ATOM 2571 O GLN A1122 30.205 -19.827 3.496 1.00 92.34 O ANISOU 2571 O GLN A1122 12482 12434 10168 1795 837 348 O ATOM 2572 CB GLN A1122 30.453 -18.140 0.638 1.00 88.89 C ANISOU 2572 CB GLN A1122 11785 12217 9771 1460 855 298 C ATOM 2573 CG GLN A1122 30.035 -19.515 0.151 1.00110.47 C ANISOU 2573 CG GLN A1122 14723 14781 12469 1590 944 262 C ATOM 2574 CD GLN A1122 29.424 -19.462 -1.219 1.00131.35 C ANISOU 2574 CD GLN A1122 17420 17367 15121 1473 989 216 C ATOM 2575 OE1 GLN A1122 29.789 -18.637 -2.067 1.00124.81 O ANISOU 2575 OE1 GLN A1122 16457 16676 14288 1377 980 219 O ATOM 2576 NE2 GLN A1122 28.490 -20.367 -1.468 1.00127.18 N ANISOU 2576 NE2 GLN A1122 17095 16634 14593 1479 1045 166 N ATOM 2577 N GLN A1123 32.115 -18.591 3.363 1.00 88.13 N ANISOU 2577 N GLN A1123 11542 12350 9593 1803 761 363 N ATOM 2578 CA GLN A1123 32.962 -19.414 4.238 1.00 88.63 C ANISOU 2578 CA GLN A1123 11599 12506 9572 2075 759 384 C ATOM 2579 C GLN A1123 32.746 -19.062 5.738 1.00 91.58 C ANISOU 2579 C GLN A1123 11973 12868 9956 2074 674 413 C ATOM 2580 O GLN A1123 33.449 -19.580 6.616 1.00 91.68 O ANISOU 2580 O GLN A1123 11963 12983 9889 2298 653 434 O ATOM 2581 CB GLN A1123 34.435 -19.269 3.829 1.00 91.08 C ANISOU 2581 CB GLN A1123 11666 13131 9811 2188 758 371 C ATOM 2582 CG GLN A1123 34.738 -19.883 2.456 1.00100.62 C ANISOU 2582 CG GLN A1123 12902 14346 10984 2259 854 346 C ATOM 2583 CD GLN A1123 36.084 -19.495 1.897 1.00116.19 C ANISOU 2583 CD GLN A1123 14605 16639 12901 2302 859 324 C ATOM 2584 OE1 GLN A1123 36.914 -18.864 2.559 1.00110.39 O ANISOU 2584 OE1 GLN A1123 13650 16150 12143 2300 793 320 O ATOM 2585 NE2 GLN A1123 36.329 -19.867 0.651 1.00108.64 N ANISOU 2585 NE2 GLN A1123 13659 15701 11919 2333 942 302 N ATOM 2586 N LYS A1124 31.736 -18.201 6.009 1.00 86.04 N ANISOU 2586 N LYS A1124 11307 12041 9344 1834 628 414 N ATOM 2587 CA LYS A1124 31.287 -17.748 7.324 1.00 85.29 C ANISOU 2587 CA LYS A1124 11234 11897 9274 1784 553 437 C ATOM 2588 C LYS A1124 32.431 -17.039 8.112 1.00 91.08 C ANISOU 2588 C LYS A1124 11726 12917 9963 1820 466 437 C ATOM 2589 O LYS A1124 32.483 -17.094 9.351 1.00 92.93 O ANISOU 2589 O LYS A1124 11975 13170 10166 1908 409 456 O ATOM 2590 CB LYS A1124 30.659 -18.924 8.120 1.00 88.19 C ANISOU 2590 CB LYS A1124 11854 12045 9611 1953 598 463 C ATOM 2591 CG LYS A1124 29.585 -19.671 7.324 1.00101.17 C ANISOU 2591 CG LYS A1124 13723 13424 11292 1899 696 441 C ATOM 2592 CD LYS A1124 28.710 -20.584 8.165 1.00106.14 C ANISOU 2592 CD LYS A1124 14613 13802 11914 1973 749 457 C ATOM 2593 CE LYS A1124 27.548 -21.118 7.352 1.00114.84 C ANISOU 2593 CE LYS A1124 15905 14665 13064 1849 839 410 C ATOM 2594 NZ LYS A1124 26.528 -20.070 7.053 1.00118.73 N ANISOU 2594 NZ LYS A1124 16340 15120 13653 1570 788 380 N ATOM 2595 N ARG A1125 33.307 -16.325 7.388 1.00 86.07 N ANISOU 2595 N ARG A1125 10870 12510 9325 1733 457 407 N ATOM 2596 CA ARG A1125 34.443 -15.596 7.962 1.00 86.20 C ANISOU 2596 CA ARG A1125 10626 12828 9298 1727 386 382 C ATOM 2597 C ARG A1125 34.071 -14.109 8.069 1.00 88.35 C ANISOU 2597 C ARG A1125 10812 13104 9652 1416 336 364 C ATOM 2598 O ARG A1125 34.648 -13.240 7.402 1.00 88.10 O ANISOU 2598 O ARG A1125 10610 13228 9635 1253 347 332 O ATOM 2599 CB ARG A1125 35.698 -15.838 7.117 1.00 85.30 C ANISOU 2599 CB ARG A1125 10324 12970 9117 1833 428 351 C ATOM 2600 CG ARG A1125 36.026 -17.317 6.993 1.00 87.62 C ANISOU 2600 CG ARG A1125 10731 13240 9323 2158 487 371 C ATOM 2601 CD ARG A1125 36.898 -17.628 5.814 1.00 78.87 C ANISOU 2601 CD ARG A1125 9504 12296 8168 2235 557 344 C ATOM 2602 NE ARG A1125 38.186 -16.951 5.901 1.00 86.06 N ANISOU 2602 NE ARG A1125 10095 13575 9029 2217 515 297 N ATOM 2603 CZ ARG A1125 39.197 -17.177 5.074 1.00109.85 C ANISOU 2603 CZ ARG A1125 12943 16813 11980 2309 567 265 C ATOM 2604 NH1 ARG A1125 40.334 -16.509 5.208 1.00 99.83 N ANISOU 2604 NH1 ARG A1125 11368 15894 10668 2263 532 209 N ATOM 2605 NH2 ARG A1125 39.085 -18.084 4.111 1.00102.01 N ANISOU 2605 NH2 ARG A1125 12088 15705 10965 2444 659 280 N ATOM 2606 N TRP A1126 33.088 -13.845 8.942 1.00 82.82 N ANISOU 2606 N TRP A1126 10248 12221 8999 1342 290 386 N ATOM 2607 CA TRP A1126 32.447 -12.563 9.175 1.00 80.91 C ANISOU 2607 CA TRP A1126 9999 11909 8835 1077 248 380 C ATOM 2608 C TRP A1126 33.415 -11.409 9.444 1.00 87.37 C ANISOU 2608 C TRP A1126 10577 12979 9640 930 200 334 C ATOM 2609 O TRP A1126 33.289 -10.369 8.789 1.00 87.37 O ANISOU 2609 O TRP A1126 10537 12968 9692 699 222 320 O ATOM 2610 CB TRP A1126 31.429 -12.666 10.309 1.00 78.02 C ANISOU 2610 CB TRP A1126 9799 11350 8495 1088 203 408 C ATOM 2611 CG TRP A1126 30.605 -13.922 10.301 1.00 78.26 C ANISOU 2611 CG TRP A1126 10059 11155 8520 1245 257 440 C ATOM 2612 CD1 TRP A1126 30.495 -14.829 11.315 1.00 81.35 C ANISOU 2612 CD1 TRP A1126 10568 11480 8861 1442 250 467 C ATOM 2613 CD2 TRP A1126 29.794 -14.422 9.225 1.00 77.26 C ANISOU 2613 CD2 TRP A1126 10080 10841 8434 1211 335 443 C ATOM 2614 NE1 TRP A1126 29.683 -15.870 10.935 1.00 80.12 N ANISOU 2614 NE1 TRP A1126 10632 11095 8715 1520 332 484 N ATOM 2615 CE2 TRP A1126 29.232 -15.647 9.660 1.00 80.71 C ANISOU 2615 CE2 TRP A1126 10721 11100 8847 1376 381 463 C ATOM 2616 CE3 TRP A1126 29.477 -13.950 7.940 1.00 78.05 C ANISOU 2616 CE3 TRP A1126 10169 10908 8580 1057 376 426 C ATOM 2617 CZ2 TRP A1126 28.351 -16.393 8.868 1.00 79.16 C ANISOU 2617 CZ2 TRP A1126 10702 10698 8676 1367 463 453 C ATOM 2618 CZ3 TRP A1126 28.638 -14.713 7.137 1.00 79.22 C ANISOU 2618 CZ3 TRP A1126 10483 10874 8745 1074 446 420 C ATOM 2619 CH2 TRP A1126 28.094 -15.926 7.599 1.00 79.91 C ANISOU 2619 CH2 TRP A1126 10758 10793 8813 1219 489 426 C ATOM 2620 N ASP A1127 34.375 -11.575 10.361 1.00 85.74 N ANISOU 2620 N ASP A1127 10217 13001 9358 1059 141 306 N ATOM 2621 CA ASP A1127 35.292 -10.482 10.700 1.00 86.66 C ANISOU 2621 CA ASP A1127 10095 13374 9459 899 96 241 C ATOM 2622 C ASP A1127 36.252 -10.176 9.557 1.00 91.49 C ANISOU 2622 C ASP A1127 10520 14185 10055 816 161 200 C ATOM 2623 O ASP A1127 36.592 -9.013 9.353 1.00 91.69 O ANISOU 2623 O ASP A1127 10424 14306 10109 566 171 154 O ATOM 2624 CB ASP A1127 36.052 -10.772 12.002 1.00 89.94 C ANISOU 2624 CB ASP A1127 10380 14010 9784 1069 8 209 C ATOM 2625 CG ASP A1127 35.238 -10.657 13.286 1.00 98.56 C ANISOU 2625 CG ASP A1127 11612 14950 10887 1078 -64 234 C ATOM 2626 OD1 ASP A1127 33.982 -10.615 13.203 1.00 95.39 O ANISOU 2626 OD1 ASP A1127 11434 14247 10564 1000 -40 285 O ATOM 2627 OD2 ASP A1127 35.852 -10.647 14.376 1.00107.82 O ANISOU 2627 OD2 ASP A1127 12665 16318 11982 1176 -144 199 O ATOM 2628 N GLU A1128 36.641 -11.202 8.782 1.00 88.71 N ANISOU 2628 N GLU A1128 10170 13878 9659 1014 218 216 N ATOM 2629 CA GLU A1128 37.519 -11.043 7.620 1.00 89.16 C ANISOU 2629 CA GLU A1128 10064 14118 9695 960 293 181 C ATOM 2630 C GLU A1128 36.734 -10.400 6.482 1.00 91.13 C ANISOU 2630 C GLU A1128 10443 14155 10027 736 367 209 C ATOM 2631 O GLU A1128 37.298 -9.601 5.732 1.00 92.26 O ANISOU 2631 O GLU A1128 10457 14422 10177 552 422 176 O ATOM 2632 CB GLU A1128 38.115 -12.385 7.181 1.00 91.58 C ANISOU 2632 CB GLU A1128 10354 14521 9921 1266 332 191 C ATOM 2633 CG GLU A1128 39.014 -13.035 8.216 1.00102.30 C ANISOU 2633 CG GLU A1128 11573 16125 11171 1527 264 165 C ATOM 2634 CD GLU A1128 39.500 -14.408 7.798 1.00123.73 C ANISOU 2634 CD GLU A1128 14318 18895 13797 1860 312 187 C ATOM 2635 OE1 GLU A1128 38.839 -15.409 8.160 1.00117.32 O ANISOU 2635 OE1 GLU A1128 13743 17865 12969 2068 317 245 O ATOM 2636 OE2 GLU A1128 40.536 -14.481 7.098 1.00117.10 O ANISOU 2636 OE2 GLU A1128 13278 18313 12903 1909 355 142 O ATOM 2637 N ALA A1129 35.424 -10.738 6.366 1.00 83.92 N ANISOU 2637 N ALA A1129 9786 12931 9169 752 372 267 N ATOM 2638 CA ALA A1129 34.512 -10.161 5.374 1.00 81.16 C ANISOU 2638 CA ALA A1129 9578 12373 8885 569 427 295 C ATOM 2639 C ALA A1129 34.336 -8.674 5.678 1.00 83.26 C ANISOU 2639 C ALA A1129 9810 12626 9198 295 406 281 C ATOM 2640 O ALA A1129 34.536 -7.837 4.785 1.00 82.48 O ANISOU 2640 O ALA A1129 9676 12552 9112 114 470 275 O ATOM 2641 CB ALA A1129 33.165 -10.884 5.396 1.00 79.90 C ANISOU 2641 CB ALA A1129 9671 11925 8762 655 423 340 C ATOM 2642 N ALA A1130 34.059 -8.354 6.976 1.00 77.98 N ANISOU 2642 N ALA A1130 9154 11931 8544 273 323 274 N ATOM 2643 CA ALA A1130 33.867 -7.007 7.508 1.00 77.14 C ANISOU 2643 CA ALA A1130 9035 11799 8476 35 295 255 C ATOM 2644 C ALA A1130 35.086 -6.093 7.283 1.00 83.84 C ANISOU 2644 C ALA A1130 9664 12895 9298 -145 332 190 C ATOM 2645 O ALA A1130 34.908 -4.894 7.037 1.00 84.33 O ANISOU 2645 O ALA A1130 9757 12890 9393 -388 369 182 O ATOM 2646 CB ALA A1130 33.557 -7.079 8.979 1.00 77.44 C ANISOU 2646 CB ALA A1130 9100 11811 8513 95 200 250 C ATOM 2647 N VAL A1131 36.310 -6.645 7.363 1.00 81.40 N ANISOU 2647 N VAL A1131 9137 12869 8921 -27 328 139 N ATOM 2648 CA VAL A1131 37.522 -5.856 7.147 1.00 83.35 C ANISOU 2648 CA VAL A1131 9146 13387 9137 -203 370 59 C ATOM 2649 C VAL A1131 37.543 -5.381 5.675 1.00 90.02 C ANISOU 2649 C VAL A1131 10030 14171 10001 -355 494 80 C ATOM 2650 O VAL A1131 37.699 -4.184 5.422 1.00 89.82 O ANISOU 2650 O VAL A1131 9989 14141 9997 -623 552 53 O ATOM 2651 CB VAL A1131 38.809 -6.635 7.567 1.00 88.19 C ANISOU 2651 CB VAL A1131 9499 14349 9659 -9 333 -6 C ATOM 2652 CG1 VAL A1131 40.057 -6.112 6.858 1.00 89.86 C ANISOU 2652 CG1 VAL A1131 9461 14849 9833 -159 413 -86 C ATOM 2653 CG2 VAL A1131 39.008 -6.578 9.073 1.00 88.02 C ANISOU 2653 CG2 VAL A1131 9392 14447 9604 44 218 -53 C ATOM 2654 N ASN A1132 37.320 -6.312 4.729 1.00 89.11 N ANISOU 2654 N ASN A1132 9995 13988 9876 -183 538 130 N ATOM 2655 CA ASN A1132 37.352 -6.050 3.287 1.00 90.58 C ANISOU 2655 CA ASN A1132 10223 14130 10063 -278 652 153 C ATOM 2656 C ASN A1132 36.232 -5.103 2.821 1.00 95.24 C ANISOU 2656 C ASN A1132 11040 14437 10709 -465 688 209 C ATOM 2657 O ASN A1132 36.474 -4.255 1.943 1.00 95.53 O ANISOU 2657 O ASN A1132 11081 14475 10741 -653 787 210 O ATOM 2658 CB ASN A1132 37.320 -7.354 2.505 1.00 91.30 C ANISOU 2658 CB ASN A1132 10357 14211 10121 -29 679 185 C ATOM 2659 CG ASN A1132 38.690 -7.965 2.426 1.00122.19 C ANISOU 2659 CG ASN A1132 14021 18445 13961 103 700 128 C ATOM 2660 OD1 ASN A1132 39.022 -8.886 3.173 1.00122.62 O ANISOU 2660 OD1 ASN A1132 14010 18608 13974 335 633 113 O ATOM 2661 ND2 ASN A1132 39.550 -7.398 1.588 1.00115.58 N ANISOU 2661 ND2 ASN A1132 13036 17783 13098 -44 795 90 N ATOM 2662 N LEU A1133 35.035 -5.224 3.437 1.00 90.25 N ANISOU 2662 N LEU A1133 10596 13574 10121 -410 614 253 N ATOM 2663 CA LEU A1133 33.878 -4.375 3.153 1.00 88.29 C ANISOU 2663 CA LEU A1133 10561 13067 9916 -546 630 304 C ATOM 2664 C LEU A1133 34.155 -2.919 3.590 1.00 93.48 C ANISOU 2664 C LEU A1133 11194 13738 10588 -809 653 275 C ATOM 2665 O LEU A1133 33.638 -2.003 2.951 1.00 92.87 O ANISOU 2665 O LEU A1133 11261 13506 10520 -957 718 311 O ATOM 2666 CB LEU A1133 32.599 -4.926 3.827 1.00 85.83 C ANISOU 2666 CB LEU A1133 10423 12545 9642 -415 543 342 C ATOM 2667 CG LEU A1133 32.016 -6.193 3.191 1.00 88.39 C ANISOU 2667 CG LEU A1133 10845 12781 9959 -209 547 372 C ATOM 2668 CD1 LEU A1133 31.267 -7.022 4.190 1.00 86.45 C ANISOU 2668 CD1 LEU A1133 10686 12424 9735 -59 466 380 C ATOM 2669 CD2 LEU A1133 31.135 -5.867 2.014 1.00 90.36 C ANISOU 2669 CD2 LEU A1133 11254 12865 10213 -265 602 412 C ATOM 2670 N ALA A1134 34.983 -2.705 4.646 1.00 91.02 N ANISOU 2670 N ALA A1134 10705 13611 10266 -864 605 204 N ATOM 2671 CA ALA A1134 35.316 -1.355 5.106 1.00 92.16 C ANISOU 2671 CA ALA A1134 10821 13778 10420 -1132 634 157 C ATOM 2672 C ALA A1134 36.317 -0.692 4.155 1.00101.76 C ANISOU 2672 C ALA A1134 11925 15135 11603 -1325 766 119 C ATOM 2673 O ALA A1134 36.272 0.532 3.970 1.00103.15 O ANISOU 2673 O ALA A1134 12188 15218 11788 -1570 846 113 O ATOM 2674 CB ALA A1134 35.870 -1.392 6.509 1.00 93.25 C ANISOU 2674 CB ALA A1134 10798 14087 10547 -1126 539 81 C ATOM 2675 N LYS A1135 37.199 -1.504 3.525 1.00 99.84 N ANISOU 2675 N LYS A1135 11507 15108 11318 -1213 801 95 N ATOM 2676 CA LYS A1135 38.204 -1.032 2.563 1.00101.46 C ANISOU 2676 CA LYS A1135 11586 15477 11486 -1376 936 56 C ATOM 2677 C LYS A1135 37.560 -0.934 1.169 1.00104.82 C ANISOU 2677 C LYS A1135 12217 15701 11910 -1374 1034 146 C ATOM 2678 O LYS A1135 38.062 -1.515 0.194 1.00106.31 O ANISOU 2678 O LYS A1135 12332 16001 12061 -1290 1101 152 O ATOM 2679 CB LYS A1135 39.449 -1.952 2.557 1.00105.36 C ANISOU 2679 CB LYS A1135 11788 16317 11927 -1238 926 -15 C ATOM 2680 CG LYS A1135 40.320 -1.872 3.812 1.00114.07 C ANISOU 2680 CG LYS A1135 12645 17689 13007 -1271 847 -124 C ATOM 2681 CD LYS A1135 41.278 -3.051 3.866 1.00122.17 C ANISOU 2681 CD LYS A1135 13424 19025 13969 -1025 807 -171 C ATOM 2682 CE LYS A1135 42.134 -3.069 5.107 1.00131.87 C ANISOU 2682 CE LYS A1135 14397 20554 15154 -1011 714 -280 C ATOM 2683 NZ LYS A1135 43.073 -4.226 5.107 1.00139.71 N ANISOU 2683 NZ LYS A1135 15156 21860 16068 -737 679 -320 N ATOM 2684 N SER A1136 36.433 -0.195 1.087 1.00 98.13 N ANISOU 2684 N SER A1136 11627 14564 11092 -1452 1041 213 N ATOM 2685 CA SER A1136 35.671 0.005 -0.144 1.00 96.30 C ANISOU 2685 CA SER A1136 11613 14130 10846 -1439 1119 300 C ATOM 2686 C SER A1136 35.139 1.447 -0.250 1.00100.24 C ANISOU 2686 C SER A1136 12320 14417 11348 -1660 1194 336 C ATOM 2687 O SER A1136 35.047 2.145 0.766 1.00 99.65 O ANISOU 2687 O SER A1136 12262 14298 11303 -1786 1156 303 O ATOM 2688 CB SER A1136 34.515 -0.988 -0.203 1.00 96.22 C ANISOU 2688 CB SER A1136 11739 13966 10856 -1186 1021 361 C ATOM 2689 OG SER A1136 33.465 -0.626 0.679 1.00101.96 O ANISOU 2689 OG SER A1136 12613 14501 11625 -1186 934 385 O ATOM 2690 N ARG A1137 34.750 1.875 -1.475 1.00 97.12 N ANISOU 2690 N ARG A1137 12103 13885 10915 -1690 1300 407 N ATOM 2691 CA ARG A1137 34.169 3.204 -1.720 1.00 97.30 C ANISOU 2691 CA ARG A1137 12368 13681 10919 -1857 1385 460 C ATOM 2692 C ARG A1137 32.835 3.336 -0.984 1.00 99.37 C ANISOU 2692 C ARG A1137 12811 13728 11219 -1758 1269 503 C ATOM 2693 O ARG A1137 32.548 4.398 -0.426 1.00100.82 O ANISOU 2693 O ARG A1137 13122 13774 11411 -1906 1290 506 O ATOM 2694 CB ARG A1137 33.975 3.460 -3.222 1.00 98.14 C ANISOU 2694 CB ARG A1137 12633 13697 10958 -1847 1511 536 C ATOM 2695 CG ARG A1137 34.389 4.860 -3.660 1.00114.49 C ANISOU 2695 CG ARG A1137 14836 15680 12984 -2110 1685 551 C ATOM 2696 CD ARG A1137 35.825 4.899 -4.168 1.00128.93 C ANISOU 2696 CD ARG A1137 16466 17736 14784 -2275 1820 487 C ATOM 2697 NE ARG A1137 36.210 6.232 -4.637 1.00139.90 N ANISOU 2697 NE ARG A1137 18005 19023 16126 -2545 2011 500 N ATOM 2698 CZ ARG A1137 37.421 6.549 -5.085 1.00157.49 C ANISOU 2698 CZ ARG A1137 20097 21419 18322 -2753 2165 441 C ATOM 2699 NH1 ARG A1137 37.681 7.783 -5.495 1.00148.58 N ANISOU 2699 NH1 ARG A1137 19143 20161 17148 -3008 2353 456 N ATOM 2700 NH2 ARG A1137 38.384 5.635 -5.126 1.00143.31 N ANISOU 2700 NH2 ARG A1137 17994 19922 16535 -2705 2141 364 N ATOM 2701 N TRP A1138 32.054 2.229 -0.946 1.00 91.35 N ANISOU 2701 N TRP A1138 11798 12688 10222 -1514 1152 528 N ATOM 2702 CA TRP A1138 30.758 2.092 -0.277 1.00 87.50 C ANISOU 2702 CA TRP A1138 11447 12031 9769 -1392 1035 559 C ATOM 2703 C TRP A1138 30.820 2.529 1.185 1.00 91.89 C ANISOU 2703 C TRP A1138 11958 12581 10374 -1485 965 511 C ATOM 2704 O TRP A1138 29.939 3.267 1.643 1.00 90.33 O ANISOU 2704 O TRP A1138 11933 12201 10187 -1517 940 541 O ATOM 2705 CB TRP A1138 30.274 0.631 -0.366 1.00 83.06 C ANISOU 2705 CB TRP A1138 10827 11509 9222 -1148 938 559 C ATOM 2706 CG TRP A1138 29.081 0.316 0.487 1.00 80.57 C ANISOU 2706 CG TRP A1138 10603 11062 8949 -1033 818 570 C ATOM 2707 CD1 TRP A1138 27.858 0.921 0.450 1.00 82.15 C ANISOU 2707 CD1 TRP A1138 11001 11070 9143 -1017 798 617 C ATOM 2708 CD2 TRP A1138 28.986 -0.720 1.465 1.00 79.03 C ANISOU 2708 CD2 TRP A1138 10307 10922 8799 -906 712 533 C ATOM 2709 NE1 TRP A1138 27.011 0.334 1.359 1.00 79.32 N ANISOU 2709 NE1 TRP A1138 10655 10653 8829 -905 686 604 N ATOM 2710 CE2 TRP A1138 27.669 -0.694 1.979 1.00 80.45 C ANISOU 2710 CE2 TRP A1138 10629 10934 9004 -837 636 556 C ATOM 2711 CE3 TRP A1138 29.876 -1.699 1.932 1.00 80.42 C ANISOU 2711 CE3 TRP A1138 10294 11276 8985 -827 678 483 C ATOM 2712 CZ2 TRP A1138 27.222 -1.602 2.938 1.00 78.21 C ANISOU 2712 CZ2 TRP A1138 10312 10643 8761 -715 540 533 C ATOM 2713 CZ3 TRP A1138 29.430 -2.594 2.890 1.00 80.63 C ANISOU 2713 CZ3 TRP A1138 10304 11285 9045 -686 579 468 C ATOM 2714 CH2 TRP A1138 28.122 -2.529 3.394 1.00 79.48 C ANISOU 2714 CH2 TRP A1138 10311 10959 8930 -643 516 493 C ATOM 2715 N TYR A1139 31.844 2.062 1.913 1.00 90.62 N ANISOU 2715 N TYR A1139 11567 12629 10234 -1512 929 434 N ATOM 2716 CA TYR A1139 31.999 2.421 3.313 1.00 91.44 C ANISOU 2716 CA TYR A1139 11609 12762 10373 -1594 857 377 C ATOM 2717 C TYR A1139 32.300 3.926 3.447 1.00 96.51 C ANISOU 2717 C TYR A1139 12338 13329 11003 -1867 955 355 C ATOM 2718 O TYR A1139 31.710 4.575 4.297 1.00 94.93 O ANISOU 2718 O TYR A1139 12252 12992 10824 -1924 913 353 O ATOM 2719 CB TYR A1139 33.076 1.561 4.003 1.00 94.21 C ANISOU 2719 CB TYR A1139 11685 13384 10728 -1539 796 296 C ATOM 2720 CG TYR A1139 33.237 1.887 5.473 1.00 97.56 C ANISOU 2720 CG TYR A1139 12038 13858 11174 -1607 712 231 C ATOM 2721 CD1 TYR A1139 32.398 1.320 6.430 1.00 98.30 C ANISOU 2721 CD1 TYR A1139 12187 13865 11297 -1445 588 250 C ATOM 2722 CD2 TYR A1139 34.191 2.805 5.904 1.00100.53 C ANISOU 2722 CD2 TYR A1139 12300 14361 11537 -1847 763 146 C ATOM 2723 CE1 TYR A1139 32.509 1.654 7.779 1.00 99.91 C ANISOU 2723 CE1 TYR A1139 12340 14109 11513 -1503 511 193 C ATOM 2724 CE2 TYR A1139 34.305 3.154 7.248 1.00101.98 C ANISOU 2724 CE2 TYR A1139 12426 14591 11732 -1917 683 78 C ATOM 2725 CZ TYR A1139 33.469 2.568 8.184 1.00109.70 C ANISOU 2725 CZ TYR A1139 13463 15483 12734 -1734 554 106 C ATOM 2726 OH TYR A1139 33.605 2.893 9.511 1.00114.70 O ANISOU 2726 OH TYR A1139 14039 16172 13370 -1793 475 38 O ATOM 2727 N ASN A1140 33.174 4.475 2.590 1.00 95.56 N ANISOU 2727 N ASN A1140 12182 13282 10845 -2036 1096 340 N ATOM 2728 CA ASN A1140 33.548 5.892 2.603 1.00 96.98 C ANISOU 2728 CA ASN A1140 12462 13382 11006 -2319 1221 314 C ATOM 2729 C ASN A1140 32.366 6.815 2.221 1.00 98.92 C ANISOU 2729 C ASN A1140 13042 13311 11231 -2325 1272 410 C ATOM 2730 O ASN A1140 32.169 7.845 2.870 1.00 99.60 O ANISOU 2730 O ASN A1140 13259 13262 11321 -2480 1300 392 O ATOM 2731 CB ASN A1140 34.742 6.128 1.688 1.00100.88 C ANISOU 2731 CB ASN A1140 12838 14034 11457 -2486 1374 276 C ATOM 2732 CG ASN A1140 36.020 5.566 2.264 1.00133.35 C ANISOU 2732 CG ASN A1140 16611 18477 15578 -2537 1338 157 C ATOM 2733 OD1 ASN A1140 36.357 4.390 2.082 1.00124.40 O ANISOU 2733 OD1 ASN A1140 15295 17528 14442 -2343 1271 149 O ATOM 2734 ND2 ASN A1140 36.739 6.387 3.018 1.00131.69 N ANISOU 2734 ND2 ASN A1140 16312 18355 15370 -2790 1377 54 N ATOM 2735 N GLN A1141 31.568 6.420 1.216 1.00 93.07 N ANISOU 2735 N GLN A1141 12437 12462 10461 -2142 1276 504 N ATOM 2736 CA GLN A1141 30.396 7.151 0.728 1.00 92.55 C ANISOU 2736 CA GLN A1141 12675 12131 10358 -2087 1311 600 C ATOM 2737 C GLN A1141 29.271 7.185 1.798 1.00 96.43 C ANISOU 2737 C GLN A1141 13262 12489 10890 -1978 1178 610 C ATOM 2738 O GLN A1141 28.803 8.274 2.148 1.00 96.84 O ANISOU 2738 O GLN A1141 13513 12356 10925 -2070 1219 632 O ATOM 2739 CB GLN A1141 29.891 6.496 -0.576 1.00 93.35 C ANISOU 2739 CB GLN A1141 12838 12218 10411 -1892 1323 677 C ATOM 2740 CG GLN A1141 29.227 7.441 -1.577 1.00116.84 C ANISOU 2740 CG GLN A1141 16105 14986 13304 -1889 1435 773 C ATOM 2741 CD GLN A1141 30.021 7.602 -2.860 1.00144.12 C ANISOU 2741 CD GLN A1141 19569 18499 16690 -1968 1591 799 C ATOM 2742 OE1 GLN A1141 30.622 6.654 -3.392 1.00139.31 O ANISOU 2742 OE1 GLN A1141 18772 18075 16085 -1907 1584 773 O ATOM 2743 NE2 GLN A1141 30.000 8.807 -3.418 1.00139.42 N ANISOU 2743 NE2 GLN A1141 19214 17736 16022 -2094 1744 856 N ATOM 2744 N THR A1142 28.859 6.005 2.325 1.00 91.40 N ANISOU 2744 N THR A1142 12490 11938 10299 -1786 1030 594 N ATOM 2745 CA THR A1142 27.794 5.897 3.327 1.00 90.33 C ANISOU 2745 CA THR A1142 12426 11695 10202 -1675 907 600 C ATOM 2746 C THR A1142 28.318 5.170 4.597 1.00 95.60 C ANISOU 2746 C THR A1142 12875 12521 10927 -1667 798 519 C ATOM 2747 O THR A1142 27.949 4.016 4.834 1.00 94.62 O ANISOU 2747 O THR A1142 12663 12458 10830 -1484 698 518 O ATOM 2748 CB THR A1142 26.571 5.205 2.715 1.00 97.02 C ANISOU 2748 CB THR A1142 13366 12464 11035 -1441 845 663 C ATOM 2749 OG1 THR A1142 26.999 4.037 2.012 1.00 97.13 O ANISOU 2749 OG1 THR A1142 13228 12628 11047 -1336 834 653 O ATOM 2750 CG2 THR A1142 25.796 6.117 1.787 1.00 95.49 C ANISOU 2750 CG2 THR A1142 13420 12092 10769 -1422 924 743 C ATOM 2751 N PRO A1143 29.123 5.855 5.456 1.00 93.12 N ANISOU 2751 N PRO A1143 12488 12268 10624 -1862 818 448 N ATOM 2752 CA PRO A1143 29.732 5.167 6.614 1.00 92.07 C ANISOU 2752 CA PRO A1143 12135 12321 10526 -1842 715 367 C ATOM 2753 C PRO A1143 28.797 4.665 7.700 1.00 93.15 C ANISOU 2753 C PRO A1143 12306 12389 10699 -1687 581 374 C ATOM 2754 O PRO A1143 29.111 3.636 8.278 1.00 92.46 O ANISOU 2754 O PRO A1143 12054 12451 10628 -1568 494 341 O ATOM 2755 CB PRO A1143 30.679 6.216 7.204 1.00 95.69 C ANISOU 2755 CB PRO A1143 12539 12844 10976 -2109 778 282 C ATOM 2756 CG PRO A1143 30.910 7.193 6.127 1.00101.85 C ANISOU 2756 CG PRO A1143 13459 13522 11717 -2278 939 313 C ATOM 2757 CD PRO A1143 29.659 7.226 5.314 1.00 96.34 C ANISOU 2757 CD PRO A1143 12998 12604 11003 -2118 950 427 C ATOM 2758 N ASN A1144 27.715 5.386 8.030 1.00 88.66 N ANISOU 2758 N ASN A1144 11945 11608 10135 -1686 569 414 N ATOM 2759 CA ASN A1144 26.811 4.977 9.118 1.00 86.77 C ANISOU 2759 CA ASN A1144 11739 11305 9927 -1556 452 416 C ATOM 2760 C ASN A1144 25.970 3.792 8.694 1.00 87.94 C ANISOU 2760 C ASN A1144 11892 11435 10088 -1327 394 465 C ATOM 2761 O ASN A1144 25.766 2.880 9.490 1.00 88.22 O ANISOU 2761 O ASN A1144 11848 11523 10148 -1205 304 447 O ATOM 2762 CB ASN A1144 25.926 6.145 9.599 1.00 86.40 C ANISOU 2762 CB ASN A1144 11909 11047 9874 -1623 464 436 C ATOM 2763 CG ASN A1144 26.741 7.364 9.961 1.00116.99 C ANISOU 2763 CG ASN A1144 15807 14913 13730 -1872 541 379 C ATOM 2764 OD1 ASN A1144 27.570 7.335 10.877 1.00114.11 O ANISOU 2764 OD1 ASN A1144 15290 14692 13377 -1971 503 294 O ATOM 2765 ND2 ASN A1144 26.602 8.427 9.181 1.00112.98 N ANISOU 2765 ND2 ASN A1144 15489 14252 13186 -1982 660 419 N ATOM 2766 N ARG A1145 25.506 3.798 7.438 1.00 81.97 N ANISOU 2766 N ARG A1145 11233 10606 9307 -1274 452 522 N ATOM 2767 CA ARG A1145 24.710 2.732 6.862 1.00 79.62 C ANISOU 2767 CA ARG A1145 10945 10296 9013 -1082 412 555 C ATOM 2768 C ARG A1145 25.589 1.514 6.595 1.00 81.71 C ANISOU 2768 C ARG A1145 11024 10738 9284 -1010 403 527 C ATOM 2769 O ARG A1145 25.149 0.393 6.858 1.00 81.45 O ANISOU 2769 O ARG A1145 10954 10720 9271 -860 340 522 O ATOM 2770 CB ARG A1145 24.048 3.215 5.571 1.00 80.28 C ANISOU 2770 CB ARG A1145 11181 10271 9049 -1055 479 615 C ATOM 2771 CG ARG A1145 23.054 2.219 5.020 1.00 81.73 C ANISOU 2771 CG ARG A1145 11385 10438 9229 -871 433 633 C ATOM 2772 CD ARG A1145 23.155 2.097 3.534 1.00 74.80 C ANISOU 2772 CD ARG A1145 10535 9586 8300 -836 501 665 C ATOM 2773 NE ARG A1145 22.117 1.202 3.035 1.00 77.33 N ANISOU 2773 NE ARG A1145 10878 9893 8611 -674 454 666 N ATOM 2774 CZ ARG A1145 21.068 1.590 2.325 1.00 82.62 C ANISOU 2774 CZ ARG A1145 11680 10483 9229 -601 458 698 C ATOM 2775 NH1 ARG A1145 20.915 2.867 1.997 1.00 70.79 N ANISOU 2775 NH1 ARG A1145 10327 8892 7678 -656 513 747 N ATOM 2776 NH2 ARG A1145 20.173 0.704 1.918 1.00 70.24 N ANISOU 2776 NH2 ARG A1145 10104 8932 7652 -471 412 676 N ATOM 2777 N ALA A1146 26.830 1.734 6.085 1.00 76.08 N ANISOU 2777 N ALA A1146 10202 10157 8550 -1119 474 504 N ATOM 2778 CA ALA A1146 27.774 0.653 5.824 1.00 75.04 C ANISOU 2778 CA ALA A1146 9885 10212 8413 -1044 472 474 C ATOM 2779 C ALA A1146 28.174 -0.021 7.118 1.00 79.66 C ANISOU 2779 C ALA A1146 10337 10908 9020 -979 383 425 C ATOM 2780 O ALA A1146 28.277 -1.245 7.135 1.00 80.18 O ANISOU 2780 O ALA A1146 10329 11048 9086 -815 346 421 O ATOM 2781 CB ALA A1146 29.000 1.166 5.102 1.00 76.94 C ANISOU 2781 CB ALA A1146 10027 10583 8622 -1189 571 451 C ATOM 2782 N LYS A1147 28.354 0.769 8.207 1.00 75.95 N ANISOU 2782 N LYS A1147 9857 10439 8560 -1097 351 389 N ATOM 2783 CA LYS A1147 28.699 0.278 9.541 1.00 76.11 C ANISOU 2783 CA LYS A1147 9765 10565 8588 -1038 261 342 C ATOM 2784 C LYS A1147 27.606 -0.678 10.054 1.00 76.76 C ANISOU 2784 C LYS A1147 9937 10534 8692 -845 187 377 C ATOM 2785 O LYS A1147 27.938 -1.759 10.540 1.00 76.98 O ANISOU 2785 O LYS A1147 9874 10664 8711 -698 139 363 O ATOM 2786 CB LYS A1147 28.885 1.450 10.513 1.00 80.59 C ANISOU 2786 CB LYS A1147 10345 11119 9156 -1217 247 295 C ATOM 2787 CG LYS A1147 29.681 1.134 11.786 1.00103.90 C ANISOU 2787 CG LYS A1147 13127 14258 12091 -1200 166 223 C ATOM 2788 CD LYS A1147 31.083 1.773 11.769 1.00122.54 C ANISOU 2788 CD LYS A1147 15304 16835 14419 -1389 211 136 C ATOM 2789 CE LYS A1147 31.119 3.296 11.790 1.00135.63 C ANISOU 2789 CE LYS A1147 17056 18396 16081 -1658 282 103 C ATOM 2790 NZ LYS A1147 30.638 3.856 13.080 1.00146.65 N ANISOU 2790 NZ LYS A1147 18526 19709 17483 -1705 213 72 N ATOM 2791 N ARG A1148 26.318 -0.303 9.897 1.00 70.19 N ANISOU 2791 N ARG A1148 9287 9500 7882 -839 187 421 N ATOM 2792 CA ARG A1148 25.188 -1.129 10.337 1.00 68.48 C ANISOU 2792 CA ARG A1148 9159 9174 7688 -687 133 445 C ATOM 2793 C ARG A1148 25.101 -2.426 9.533 1.00 71.51 C ANISOU 2793 C ARG A1148 9521 9584 8067 -537 151 459 C ATOM 2794 O ARG A1148 24.961 -3.493 10.121 1.00 71.90 O ANISOU 2794 O ARG A1148 9556 9643 8121 -403 113 452 O ATOM 2795 CB ARG A1148 23.863 -0.365 10.265 1.00 65.85 C ANISOU 2795 CB ARG A1148 9001 8650 7368 -719 134 477 C ATOM 2796 CG ARG A1148 23.688 0.695 11.339 1.00 61.60 C ANISOU 2796 CG ARG A1148 8518 8050 6836 -824 104 462 C ATOM 2797 CD ARG A1148 22.274 1.282 11.347 1.00 67.95 C ANISOU 2797 CD ARG A1148 9496 8674 7647 -808 99 495 C ATOM 2798 NE ARG A1148 21.924 1.930 10.075 1.00 71.41 N ANISOU 2798 NE ARG A1148 10032 9042 8060 -839 165 533 N ATOM 2799 CZ ARG A1148 22.297 3.155 9.724 1.00 84.68 C ANISOU 2799 CZ ARG A1148 11782 10677 9714 -974 227 544 C ATOM 2800 NH1 ARG A1148 23.003 3.909 10.556 1.00 84.32 N ANISOU 2800 NH1 ARG A1148 11714 10652 9671 -1112 231 508 N ATOM 2801 NH2 ARG A1148 21.956 3.641 8.543 1.00 75.78 N ANISOU 2801 NH2 ARG A1148 10759 9485 8550 -973 291 588 N ATOM 2802 N VAL A1149 25.257 -2.349 8.209 1.00 67.62 N ANISOU 2802 N VAL A1149 9034 9103 7558 -558 215 475 N ATOM 2803 CA VAL A1149 25.230 -3.538 7.351 1.00 66.57 C ANISOU 2803 CA VAL A1149 8884 8997 7414 -427 241 479 C ATOM 2804 C VAL A1149 26.426 -4.481 7.715 1.00 71.74 C ANISOU 2804 C VAL A1149 9387 9822 8051 -334 232 451 C ATOM 2805 O VAL A1149 26.202 -5.675 7.975 1.00 70.00 O ANISOU 2805 O VAL A1149 9183 9586 7829 -183 215 449 O ATOM 2806 CB VAL A1149 25.199 -3.137 5.861 1.00 69.37 C ANISOU 2806 CB VAL A1149 9276 9339 7741 -474 312 502 C ATOM 2807 CG1 VAL A1149 25.349 -4.354 4.953 1.00 69.10 C ANISOU 2807 CG1 VAL A1149 9211 9355 7688 -347 343 494 C ATOM 2808 CG2 VAL A1149 23.907 -2.403 5.546 1.00 68.00 C ANISOU 2808 CG2 VAL A1149 9261 9009 7569 -505 310 530 C ATOM 2809 N ILE A1150 27.659 -3.919 7.813 1.00 70.34 N ANISOU 2809 N ILE A1150 9068 9806 7851 -426 247 426 N ATOM 2810 CA ILE A1150 28.883 -4.658 8.171 1.00 71.90 C ANISOU 2810 CA ILE A1150 9095 10208 8016 -335 235 392 C ATOM 2811 C ILE A1150 28.731 -5.298 9.566 1.00 76.82 C ANISOU 2811 C ILE A1150 9718 10833 8638 -211 155 382 C ATOM 2812 O ILE A1150 29.091 -6.461 9.731 1.00 77.40 O ANISOU 2812 O ILE A1150 9752 10973 8681 -31 146 381 O ATOM 2813 CB ILE A1150 30.159 -3.763 8.065 1.00 76.29 C ANISOU 2813 CB ILE A1150 9485 10955 8548 -492 267 349 C ATOM 2814 CG1 ILE A1150 30.487 -3.446 6.581 1.00 76.77 C ANISOU 2814 CG1 ILE A1150 9539 11036 8594 -572 365 362 C ATOM 2815 CG2 ILE A1150 31.366 -4.403 8.768 1.00 76.94 C ANISOU 2815 CG2 ILE A1150 9367 11280 8586 -392 227 298 C ATOM 2816 CD1 ILE A1150 31.374 -2.243 6.352 1.00 83.27 C ANISOU 2816 CD1 ILE A1150 10270 11967 9403 -794 426 327 C ATOM 2817 N THR A1151 28.152 -4.574 10.543 1.00 73.62 N ANISOU 2817 N THR A1151 9378 10340 8256 -293 105 380 N ATOM 2818 CA THR A1151 27.937 -5.120 11.892 1.00 72.70 C ANISOU 2818 CA THR A1151 9279 10213 8130 -179 34 376 C ATOM 2819 C THR A1151 26.940 -6.279 11.816 1.00 75.12 C ANISOU 2819 C THR A1151 9728 10363 8451 -21 44 412 C ATOM 2820 O THR A1151 27.219 -7.311 12.421 1.00 75.14 O ANISOU 2820 O THR A1151 9721 10409 8421 147 25 414 O ATOM 2821 CB THR A1151 27.533 -4.016 12.873 1.00 72.63 C ANISOU 2821 CB THR A1151 9313 10144 8141 -315 -13 362 C ATOM 2822 OG1 THR A1151 28.694 -3.213 13.056 1.00 80.28 O ANISOU 2822 OG1 THR A1151 10125 11297 9082 -444 -17 308 O ATOM 2823 CG2 THR A1151 27.099 -4.548 14.219 1.00 63.51 C ANISOU 2823 CG2 THR A1151 8210 8947 6975 -198 -79 366 C ATOM 2824 N THR A1152 25.822 -6.136 11.039 1.00 69.51 N ANISOU 2824 N THR A1152 9150 9483 7779 -69 80 435 N ATOM 2825 CA THR A1152 24.830 -7.205 10.879 1.00 68.52 C ANISOU 2825 CA THR A1152 9152 9215 7667 46 100 450 C ATOM 2826 C THR A1152 25.534 -8.470 10.330 1.00 76.11 C ANISOU 2826 C THR A1152 10073 10253 8593 199 142 446 C ATOM 2827 O THR A1152 25.293 -9.560 10.844 1.00 77.05 O ANISOU 2827 O THR A1152 10265 10312 8697 339 149 451 O ATOM 2828 CB THR A1152 23.664 -6.754 10.002 1.00 70.16 C ANISOU 2828 CB THR A1152 9466 9286 7906 -38 128 457 C ATOM 2829 OG1 THR A1152 23.178 -5.494 10.451 1.00 68.03 O ANISOU 2829 OG1 THR A1152 9230 8962 7656 -165 96 464 O ATOM 2830 CG2 THR A1152 22.534 -7.756 9.965 1.00 61.92 C ANISOU 2830 CG2 THR A1152 8543 8106 6877 44 147 451 C ATOM 2831 N PHE A1153 26.448 -8.318 9.349 1.00 73.32 N ANISOU 2831 N PHE A1153 9612 10029 8217 178 178 438 N ATOM 2832 CA PHE A1153 27.212 -9.451 8.815 1.00 73.52 C ANISOU 2832 CA PHE A1153 9590 10144 8201 333 220 432 C ATOM 2833 C PHE A1153 28.140 -10.027 9.882 1.00 80.59 C ANISOU 2833 C PHE A1153 10402 11174 9047 480 182 427 C ATOM 2834 O PHE A1153 28.211 -11.243 10.018 1.00 81.26 O ANISOU 2834 O PHE A1153 10548 11231 9097 664 207 436 O ATOM 2835 CB PHE A1153 28.028 -9.050 7.576 1.00 75.08 C ANISOU 2835 CB PHE A1153 9676 10470 8379 269 269 423 C ATOM 2836 CG PHE A1153 27.267 -8.928 6.282 1.00 75.15 C ANISOU 2836 CG PHE A1153 9777 10369 8406 204 321 430 C ATOM 2837 CD1 PHE A1153 26.442 -9.959 5.839 1.00 76.70 C ANISOU 2837 CD1 PHE A1153 10101 10436 8606 300 352 425 C ATOM 2838 CD2 PHE A1153 27.440 -7.819 5.457 1.00 76.48 C ANISOU 2838 CD2 PHE A1153 9907 10576 8577 52 349 436 C ATOM 2839 CE1 PHE A1153 25.788 -9.870 4.600 1.00 76.68 C ANISOU 2839 CE1 PHE A1153 10166 10365 8605 249 394 419 C ATOM 2840 CE2 PHE A1153 26.775 -7.727 4.228 1.00 77.58 C ANISOU 2840 CE2 PHE A1153 10132 10632 8714 18 395 445 C ATOM 2841 CZ PHE A1153 25.955 -8.753 3.808 1.00 74.68 C ANISOU 2841 CZ PHE A1153 9870 10160 8346 120 410 433 C ATOM 2842 N ARG A1154 28.826 -9.160 10.652 1.00 78.91 N ANISOU 2842 N ARG A1154 10059 11103 8821 403 126 409 N ATOM 2843 CA ARG A1154 29.749 -9.565 11.721 1.00 80.38 C ANISOU 2843 CA ARG A1154 10139 11457 8944 542 75 395 C ATOM 2844 C ARG A1154 29.043 -10.372 12.815 1.00 85.10 C ANISOU 2844 C ARG A1154 10888 11918 9529 689 48 423 C ATOM 2845 O ARG A1154 29.481 -11.472 13.136 1.00 86.56 O ANISOU 2845 O ARG A1154 11090 12147 9651 906 58 436 O ATOM 2846 CB ARG A1154 30.416 -8.330 12.358 1.00 80.83 C ANISOU 2846 CB ARG A1154 10039 11677 8994 385 17 353 C ATOM 2847 CG ARG A1154 31.888 -8.143 12.019 1.00 92.29 C ANISOU 2847 CG ARG A1154 11257 13417 10393 380 22 304 C ATOM 2848 CD ARG A1154 32.739 -7.814 13.237 1.00100.71 C ANISOU 2848 CD ARG A1154 12163 14701 11400 396 -59 252 C ATOM 2849 NE ARG A1154 32.236 -6.666 13.992 1.00112.30 N ANISOU 2849 NE ARG A1154 13669 16094 12908 198 -104 232 N ATOM 2850 CZ ARG A1154 32.300 -6.550 15.314 1.00131.45 C ANISOU 2850 CZ ARG A1154 16072 18577 15296 239 -184 209 C ATOM 2851 NH1 ARG A1154 32.848 -7.514 16.047 1.00120.29 N ANISOU 2851 NH1 ARG A1154 14601 17305 13800 481 -232 209 N ATOM 2852 NH2 ARG A1154 31.814 -5.473 15.916 1.00122.37 N ANISOU 2852 NH2 ARG A1154 14968 17344 14183 51 -215 188 N ATOM 2853 N THR A1155 27.956 -9.819 13.379 1.00 80.50 N ANISOU 2853 N THR A1155 10422 11168 8998 577 24 435 N ATOM 2854 CA THR A1155 27.206 -10.376 14.500 1.00 79.81 C ANISOU 2854 CA THR A1155 10477 10944 8901 674 4 459 C ATOM 2855 C THR A1155 26.182 -11.453 14.093 1.00 84.46 C ANISOU 2855 C THR A1155 11261 11317 9513 752 78 483 C ATOM 2856 O THR A1155 26.086 -12.483 14.758 1.00 85.80 O ANISOU 2856 O THR A1155 11539 11422 9640 920 100 505 O ATOM 2857 CB THR A1155 26.475 -9.252 15.258 1.00 85.21 C ANISOU 2857 CB THR A1155 11194 11553 9630 509 -48 453 C ATOM 2858 OG1 THR A1155 25.409 -8.749 14.445 1.00 89.31 O ANISOU 2858 OG1 THR A1155 11803 11912 10219 363 -11 457 O ATOM 2859 CG2 THR A1155 27.396 -8.116 15.680 1.00 79.91 C ANISOU 2859 CG2 THR A1155 10350 11073 8939 395 -111 414 C ATOM 2860 N GLY A1156 25.384 -11.178 13.071 1.00 79.63 N ANISOU 2860 N GLY A1156 10703 10593 8960 625 119 474 N ATOM 2861 CA GLY A1156 24.316 -12.075 12.650 1.00 78.66 C ANISOU 2861 CA GLY A1156 10748 10277 8861 655 188 474 C ATOM 2862 C GLY A1156 23.052 -11.765 13.420 1.00 81.21 C ANISOU 2862 C GLY A1156 11186 10445 9226 570 173 475 C ATOM 2863 O GLY A1156 22.111 -12.563 13.425 1.00 80.08 O ANISOU 2863 O GLY A1156 11187 10145 9096 593 231 466 O ATOM 2864 N THR A1157 23.046 -10.606 14.110 1.00 77.60 N ANISOU 2864 N THR A1157 10664 10036 8783 469 103 478 N ATOM 2865 CA THR A1157 21.941 -10.121 14.950 1.00 76.96 C ANISOU 2865 CA THR A1157 10671 9834 8735 390 79 479 C ATOM 2866 C THR A1157 21.411 -8.784 14.406 1.00 83.22 C ANISOU 2866 C THR A1157 11427 10618 9574 215 51 467 C ATOM 2867 O THR A1157 21.983 -8.237 13.457 1.00 84.24 O ANISOU 2867 O THR A1157 11469 10833 9705 154 54 463 O ATOM 2868 CB THR A1157 22.386 -9.969 16.425 1.00 81.35 C ANISOU 2868 CB THR A1157 11212 10445 9253 453 21 495 C ATOM 2869 OG1 THR A1157 23.131 -8.764 16.576 1.00 81.69 O ANISOU 2869 OG1 THR A1157 11116 10630 9291 356 -46 482 O ATOM 2870 CG2 THR A1157 23.185 -11.169 16.958 1.00 80.08 C ANISOU 2870 CG2 THR A1157 11072 10335 9020 660 39 516 C ATOM 2871 N TRP A1158 20.352 -8.237 15.029 1.00 79.19 N ANISOU 2871 N TRP A1158 10991 10006 9093 144 31 464 N ATOM 2872 CA TRP A1158 19.769 -6.961 14.617 1.00 77.86 C ANISOU 2872 CA TRP A1158 10815 9814 8954 8 9 458 C ATOM 2873 C TRP A1158 20.244 -5.816 15.502 1.00 83.58 C ANISOU 2873 C TRP A1158 11493 10593 9670 -63 -52 463 C ATOM 2874 O TRP A1158 19.723 -4.705 15.392 1.00 83.91 O ANISOU 2874 O TRP A1158 11561 10592 9731 -167 -66 462 O ATOM 2875 CB TRP A1158 18.247 -7.058 14.665 1.00 75.11 C ANISOU 2875 CB TRP A1158 10572 9332 8634 -19 29 442 C ATOM 2876 CG TRP A1158 17.664 -7.885 13.561 1.00 75.72 C ANISOU 2876 CG TRP A1158 10683 9368 8718 1 88 416 C ATOM 2877 CD1 TRP A1158 17.063 -9.100 13.683 1.00 78.49 C ANISOU 2877 CD1 TRP A1158 11113 9639 9072 55 143 390 C ATOM 2878 CD2 TRP A1158 17.583 -7.533 12.170 1.00 75.61 C ANISOU 2878 CD2 TRP A1158 10636 9388 8704 -43 103 405 C ATOM 2879 NE1 TRP A1158 16.576 -9.513 12.466 1.00 78.28 N ANISOU 2879 NE1 TRP A1158 11094 9600 9049 35 186 353 N ATOM 2880 CE2 TRP A1158 16.893 -8.577 11.514 1.00 79.58 C ANISOU 2880 CE2 TRP A1158 11188 9841 9209 -14 157 364 C ATOM 2881 CE3 TRP A1158 18.025 -6.431 11.409 1.00 76.78 C ANISOU 2881 CE3 TRP A1158 10730 9600 8843 -109 84 424 C ATOM 2882 CZ2 TRP A1158 16.668 -8.574 10.129 1.00 78.66 C ANISOU 2882 CZ2 TRP A1158 11053 9755 9081 -35 180 339 C ATOM 2883 CZ3 TRP A1158 17.763 -6.409 10.045 1.00 78.12 C ANISOU 2883 CZ3 TRP A1158 10897 9786 8999 -121 113 411 C ATOM 2884 CH2 TRP A1158 17.089 -7.469 9.419 1.00 78.72 C ANISOU 2884 CH2 TRP A1158 11007 9829 9072 -80 154 368 C ATOM 2885 N ASP A1159 21.267 -6.068 16.337 1.00 81.53 N ANISOU 2885 N ASP A1159 11165 10437 9375 -2 -84 464 N ATOM 2886 CA ASP A1159 21.789 -5.135 17.338 1.00 82.74 C ANISOU 2886 CA ASP A1159 11267 10661 9509 -64 -145 452 C ATOM 2887 C ASP A1159 22.176 -3.755 16.792 1.00 85.35 C ANISOU 2887 C ASP A1159 11541 11037 9853 -227 -152 435 C ATOM 2888 O ASP A1159 22.134 -2.801 17.559 1.00 85.51 O ANISOU 2888 O ASP A1159 11572 11049 9869 -314 -188 419 O ATOM 2889 CB ASP A1159 22.970 -5.752 18.118 1.00 86.91 C ANISOU 2889 CB ASP A1159 11702 11342 9979 49 -180 444 C ATOM 2890 CG ASP A1159 22.615 -6.996 18.941 1.00103.76 C ANISOU 2890 CG ASP A1159 13929 13413 12082 220 -170 468 C ATOM 2891 OD1 ASP A1159 21.433 -7.122 19.371 1.00102.93 O ANISOU 2891 OD1 ASP A1159 13954 13152 12003 213 -151 480 O ATOM 2892 OD2 ASP A1159 23.503 -7.858 19.127 1.00114.58 O ANISOU 2892 OD2 ASP A1159 15249 14889 13396 366 -172 475 O ATOM 2893 N ALA A1160 22.506 -3.625 15.494 1.00 81.70 N ANISOU 2893 N ALA A1160 11037 10606 9398 -272 -108 439 N ATOM 2894 CA ALA A1160 22.845 -2.323 14.892 1.00 80.52 C ANISOU 2894 CA ALA A1160 10864 10475 9253 -431 -90 431 C ATOM 2895 C ALA A1160 21.574 -1.516 14.552 1.00 81.82 C ANISOU 2895 C ALA A1160 11169 10476 9443 -492 -73 451 C ATOM 2896 O ALA A1160 21.628 -0.289 14.496 1.00 80.61 O ANISOU 2896 O ALA A1160 11051 10292 9287 -616 -63 448 O ATOM 2897 CB ALA A1160 23.693 -2.519 13.647 1.00 81.47 C ANISOU 2897 CB ALA A1160 10896 10695 9362 -444 -40 431 C ATOM 2898 N TYR A1161 20.435 -2.207 14.374 1.00 78.35 N ANISOU 2898 N TYR A1161 10811 9937 9020 -403 -65 466 N ATOM 2899 CA TYR A1161 19.148 -1.614 14.003 1.00 78.73 C ANISOU 2899 CA TYR A1161 10971 9862 9080 -425 -54 478 C ATOM 2900 C TYR A1161 18.198 -1.519 15.204 1.00 85.16 C ANISOU 2900 C TYR A1161 11860 10592 9906 -401 -89 471 C ATOM 2901 O TYR A1161 17.037 -1.088 15.074 1.00 84.14 O ANISOU 2901 O TYR A1161 11815 10374 9781 -399 -86 474 O ATOM 2902 CB TYR A1161 18.518 -2.410 12.844 1.00 79.05 C ANISOU 2902 CB TYR A1161 11030 9883 9124 -358 -17 480 C ATOM 2903 CG TYR A1161 19.300 -2.234 11.566 1.00 79.47 C ANISOU 2903 CG TYR A1161 11034 10004 9159 -391 24 492 C ATOM 2904 CD1 TYR A1161 20.387 -3.056 11.271 1.00 81.67 C ANISOU 2904 CD1 TYR A1161 11213 10387 9430 -354 41 485 C ATOM 2905 CD2 TYR A1161 19.008 -1.197 10.686 1.00 79.91 C ANISOU 2905 CD2 TYR A1161 11147 10022 9192 -451 51 513 C ATOM 2906 CE1 TYR A1161 21.161 -2.851 10.128 1.00 82.67 C ANISOU 2906 CE1 TYR A1161 11288 10588 9536 -390 85 494 C ATOM 2907 CE2 TYR A1161 19.767 -0.992 9.533 1.00 81.21 C ANISOU 2907 CE2 TYR A1161 11277 10247 9333 -487 99 528 C ATOM 2908 CZ TYR A1161 20.831 -1.833 9.251 1.00 85.99 C ANISOU 2908 CZ TYR A1161 11771 10962 9938 -463 117 516 C ATOM 2909 OH TYR A1161 21.569 -1.645 8.114 1.00 85.01 O ANISOU 2909 OH TYR A1161 11609 10904 9788 -500 171 528 O ATOM 2910 N LYS A 263 18.735 -1.889 16.385 1.00 82.12 N ANISOU 2910 N LYS A 263 11438 10250 9515 -375 -124 460 N ATOM 2911 CA LYS A 263 18.105 -1.798 17.699 1.00 80.89 C ANISOU 2911 CA LYS A 263 11342 10034 9359 -354 -158 453 C ATOM 2912 C LYS A 263 17.727 -0.331 17.953 1.00 80.64 C ANISOU 2912 C LYS A 263 11376 9940 9324 -453 -172 450 C ATOM 2913 O LYS A 263 18.591 0.551 17.842 1.00 80.28 O ANISOU 2913 O LYS A 263 11299 9939 9265 -551 -174 441 O ATOM 2914 CB LYS A 263 19.113 -2.301 18.752 1.00 84.48 C ANISOU 2914 CB LYS A 263 11727 10585 9787 -309 -196 442 C ATOM 2915 CG LYS A 263 18.534 -2.775 20.072 1.00101.75 C ANISOU 2915 CG LYS A 263 13977 12720 11962 -236 -218 442 C ATOM 2916 CD LYS A 263 19.651 -2.975 21.102 1.00116.18 C ANISOU 2916 CD LYS A 263 15734 14669 13742 -192 -267 430 C ATOM 2917 CE LYS A 263 20.426 -4.264 20.903 1.00134.80 C ANISOU 2917 CE LYS A 263 18032 17114 16071 -62 -253 443 C ATOM 2918 NZ LYS A 263 21.798 -4.179 21.472 1.00148.76 N ANISOU 2918 NZ LYS A 263 19677 19063 17783 -36 -307 420 N ATOM 2919 N PHE A 264 16.423 -0.077 18.205 1.00 73.77 N ANISOU 2919 N PHE A 264 10600 8967 8462 -429 -170 452 N ATOM 2920 CA PHE A 264 15.792 1.230 18.503 1.00 72.59 C ANISOU 2920 CA PHE A 264 10544 8734 8302 -484 -177 453 C ATOM 2921 C PHE A 264 16.106 2.292 17.472 1.00 76.63 C ANISOU 2921 C PHE A 264 11089 9227 8798 -561 -145 469 C ATOM 2922 O PHE A 264 16.371 3.436 17.824 1.00 76.44 O ANISOU 2922 O PHE A 264 11127 9161 8757 -646 -143 464 O ATOM 2923 CB PHE A 264 16.140 1.740 19.925 1.00 73.75 C ANISOU 2923 CB PHE A 264 10709 8879 8435 -524 -217 433 C ATOM 2924 CG PHE A 264 15.811 0.723 20.991 1.00 73.31 C ANISOU 2924 CG PHE A 264 10643 8831 8380 -436 -240 425 C ATOM 2925 CD1 PHE A 264 14.502 0.286 21.176 1.00 74.77 C ANISOU 2925 CD1 PHE A 264 10889 8944 8577 -368 -222 428 C ATOM 2926 CD2 PHE A 264 16.819 0.140 21.745 1.00 74.35 C ANISOU 2926 CD2 PHE A 264 10703 9055 8492 -414 -271 415 C ATOM 2927 CE1 PHE A 264 14.204 -0.690 22.117 1.00 75.65 C ANISOU 2927 CE1 PHE A 264 11009 9050 8686 -298 -222 424 C ATOM 2928 CE2 PHE A 264 16.523 -0.828 22.694 1.00 77.74 C ANISOU 2928 CE2 PHE A 264 11149 9480 8909 -317 -280 419 C ATOM 2929 CZ PHE A 264 15.215 -1.233 22.883 1.00 76.07 C ANISOU 2929 CZ PHE A 264 11018 9171 8714 -267 -249 426 C ATOM 2930 N CYS A 265 15.987 1.923 16.196 1.00 75.05 N ANISOU 2930 N CYS A 265 10870 9047 8599 -530 -112 486 N ATOM 2931 CA CYS A 265 16.237 2.824 15.080 1.00 76.21 C ANISOU 2931 CA CYS A 265 11062 9173 8720 -584 -70 510 C ATOM 2932 C CYS A 265 14.929 3.256 14.426 1.00 76.29 C ANISOU 2932 C CYS A 265 11172 9110 8704 -511 -56 529 C ATOM 2933 O CYS A 265 14.796 4.428 14.075 1.00 76.55 O ANISOU 2933 O CYS A 265 11313 9072 8700 -541 -27 554 O ATOM 2934 CB CYS A 265 17.197 2.190 14.083 1.00 77.92 C ANISOU 2934 CB CYS A 265 11182 9483 8940 -599 -42 516 C ATOM 2935 SG CYS A 265 18.940 2.365 14.550 1.00 83.70 S ANISOU 2935 SG CYS A 265 11806 10322 9674 -717 -41 492 S ATOM 2936 N LEU A 266 13.945 2.339 14.337 1.00 68.81 N ANISOU 2936 N LEU A 266 10195 8182 7769 -414 -72 512 N ATOM 2937 CA LEU A 266 12.605 2.601 13.813 1.00 67.20 C ANISOU 2937 CA LEU A 266 10049 7950 7531 -328 -71 510 C ATOM 2938 C LEU A 266 11.833 3.537 14.771 1.00 70.43 C ANISOU 2938 C LEU A 266 10555 8281 7923 -311 -89 510 C ATOM 2939 O LEU A 266 12.111 3.497 15.980 1.00 71.28 O ANISOU 2939 O LEU A 266 10658 8367 8060 -353 -110 497 O ATOM 2940 CB LEU A 266 11.892 1.256 13.673 1.00 66.52 C ANISOU 2940 CB LEU A 266 9883 7923 7468 -265 -79 468 C ATOM 2941 CG LEU A 266 10.822 1.155 12.608 1.00 71.12 C ANISOU 2941 CG LEU A 266 10465 8546 8011 -186 -73 448 C ATOM 2942 CD1 LEU A 266 11.427 1.221 11.182 1.00 69.99 C ANISOU 2942 CD1 LEU A 266 10313 8445 7835 -186 -46 473 C ATOM 2943 CD2 LEU A 266 9.992 -0.117 12.817 1.00 73.21 C ANISOU 2943 CD2 LEU A 266 10657 8856 8302 -157 -73 383 C ATOM 2944 N LYS A 267 10.886 4.379 14.256 1.00 64.62 N ANISOU 2944 N LYS A 267 9911 7509 7133 -236 -80 526 N ATOM 2945 CA LYS A 267 10.123 5.333 15.100 1.00 64.14 C ANISOU 2945 CA LYS A 267 9955 7371 7044 -199 -91 528 C ATOM 2946 C LYS A 267 9.263 4.598 16.135 1.00 68.12 C ANISOU 2946 C LYS A 267 10398 7904 7580 -160 -122 481 C ATOM 2947 O LYS A 267 9.250 4.972 17.304 1.00 68.06 O ANISOU 2947 O LYS A 267 10434 7842 7583 -186 -135 474 O ATOM 2948 CB LYS A 267 9.250 6.288 14.274 1.00 66.24 C ANISOU 2948 CB LYS A 267 10330 7608 7229 -89 -73 555 C ATOM 2949 N GLU A 268 8.635 3.497 15.719 1.00 65.33 N ANISOU 2949 N GLU A 268 9944 7636 7241 -113 -127 442 N ATOM 2950 CA GLU A 268 7.796 2.657 16.567 1.00 64.73 C ANISOU 2950 CA GLU A 268 9809 7591 7194 -93 -135 391 C ATOM 2951 C GLU A 268 8.618 1.960 17.637 1.00 69.11 C ANISOU 2951 C GLU A 268 10337 8120 7803 -166 -137 390 C ATOM 2952 O GLU A 268 8.101 1.782 18.735 1.00 70.69 O ANISOU 2952 O GLU A 268 10548 8299 8014 -159 -141 368 O ATOM 2953 CB GLU A 268 7.011 1.635 15.744 1.00 65.66 C ANISOU 2953 CB GLU A 268 9832 7806 7311 -53 -124 338 C ATOM 2954 CG GLU A 268 6.043 2.284 14.764 1.00 74.08 C ANISOU 2954 CG GLU A 268 10909 8933 8306 47 -133 327 C ATOM 2955 CD GLU A 268 6.619 2.746 13.436 1.00 90.41 C ANISOU 2955 CD GLU A 268 13009 11013 10330 69 -128 370 C ATOM 2956 OE1 GLU A 268 7.838 2.558 13.196 1.00 76.92 O ANISOU 2956 OE1 GLU A 268 11303 9270 8654 -8 -113 406 O ATOM 2957 OE2 GLU A 268 5.839 3.310 12.635 1.00 79.68 O ANISOU 2957 OE2 GLU A 268 11672 9707 8896 174 -137 367 O ATOM 2958 N HIS A 269 9.895 1.634 17.360 1.00 63.45 N ANISOU 2958 N HIS A 269 9588 7412 7107 -225 -134 414 N ATOM 2959 CA HIS A 269 10.769 1.001 18.349 1.00 62.86 C ANISOU 2959 CA HIS A 269 9483 7335 7065 -269 -143 415 C ATOM 2960 C HIS A 269 11.279 2.045 19.366 1.00 67.57 C ANISOU 2960 C HIS A 269 10144 7881 7648 -316 -169 430 C ATOM 2961 O HIS A 269 11.505 1.707 20.534 1.00 67.10 O ANISOU 2961 O HIS A 269 10080 7816 7597 -323 -186 420 O ATOM 2962 CB HIS A 269 11.933 0.251 17.672 1.00 63.58 C ANISOU 2962 CB HIS A 269 9504 7481 7174 -295 -132 426 C ATOM 2963 CG HIS A 269 11.496 -0.978 16.922 1.00 66.73 C ANISOU 2963 CG HIS A 269 9850 7918 7586 -255 -102 400 C ATOM 2964 ND1 HIS A 269 12.369 -2.019 16.689 1.00 68.64 N ANISOU 2964 ND1 HIS A 269 10038 8196 7845 -252 -85 402 N ATOM 2965 CD2 HIS A 269 10.288 -1.297 16.387 1.00 67.82 C ANISOU 2965 CD2 HIS A 269 9982 8068 7717 -218 -84 363 C ATOM 2966 CE1 HIS A 269 11.681 -2.917 16.006 1.00 67.53 C ANISOU 2966 CE1 HIS A 269 9879 8070 7711 -224 -50 367 C ATOM 2967 NE2 HIS A 269 10.422 -2.532 15.816 1.00 67.38 N ANISOU 2967 NE2 HIS A 269 9878 8045 7678 -212 -51 336 N ATOM 2968 N LYS A 270 11.433 3.310 18.928 1.00 64.22 N ANISOU 2968 N LYS A 270 9791 7414 7195 -347 -165 451 N ATOM 2969 CA LYS A 270 11.842 4.409 19.800 1.00 64.54 C ANISOU 2969 CA LYS A 270 9912 7392 7217 -408 -177 453 C ATOM 2970 C LYS A 270 10.664 4.738 20.736 1.00 69.14 C ANISOU 2970 C LYS A 270 10564 7921 7784 -346 -188 437 C ATOM 2971 O LYS A 270 10.883 5.066 21.902 1.00 68.37 O ANISOU 2971 O LYS A 270 10503 7794 7682 -379 -208 422 O ATOM 2972 CB LYS A 270 12.280 5.633 18.989 1.00 66.61 C ANISOU 2972 CB LYS A 270 10260 7601 7447 -464 -147 479 C ATOM 2973 CG LYS A 270 13.634 5.469 18.325 1.00 79.48 C ANISOU 2973 CG LYS A 270 11822 9288 9090 -557 -130 486 C ATOM 2974 CD LYS A 270 14.027 6.745 17.579 1.00 86.77 C ANISOU 2974 CD LYS A 270 12855 10138 9975 -630 -79 511 C ATOM 2975 CE LYS A 270 15.364 6.641 16.884 1.00 98.32 C ANISOU 2975 CE LYS A 270 14244 11667 11447 -737 -49 513 C ATOM 2976 NZ LYS A 270 16.504 6.705 17.838 1.00108.08 N ANISOU 2976 NZ LYS A 270 15410 12957 12698 -860 -69 469 N ATOM 2977 N ALA A 271 9.411 4.584 20.221 1.00 64.51 N ANISOU 2977 N ALA A 271 9982 7345 7185 -252 -176 431 N ATOM 2978 CA ALA A 271 8.179 4.769 20.978 1.00 63.01 C ANISOU 2978 CA ALA A 271 9831 7134 6978 -180 -179 408 C ATOM 2979 C ALA A 271 8.116 3.710 22.080 1.00 67.21 C ANISOU 2979 C ALA A 271 10303 7690 7542 -191 -185 381 C ATOM 2980 O ALA A 271 7.829 4.039 23.228 1.00 69.65 O ANISOU 2980 O ALA A 271 10664 7961 7840 -185 -194 370 O ATOM 2981 CB ALA A 271 6.985 4.662 20.051 1.00 63.40 C ANISOU 2981 CB ALA A 271 9854 7234 7001 -82 -166 394 C ATOM 2982 N LEU A 272 8.478 2.459 21.750 1.00 61.80 N ANISOU 2982 N LEU A 272 9529 7061 6892 -205 -174 375 N ATOM 2983 CA LEU A 272 8.558 1.349 22.688 1.00 60.62 C ANISOU 2983 CA LEU A 272 9347 6921 6764 -207 -165 360 C ATOM 2984 C LEU A 272 9.666 1.601 23.731 1.00 67.98 C ANISOU 2984 C LEU A 272 10305 7837 7688 -247 -198 377 C ATOM 2985 O LEU A 272 9.454 1.354 24.928 1.00 68.85 O ANISOU 2985 O LEU A 272 10444 7928 7786 -230 -201 368 O ATOM 2986 CB LEU A 272 8.804 0.031 21.944 1.00 59.59 C ANISOU 2986 CB LEU A 272 9141 6837 6662 -207 -135 353 C ATOM 2987 CG LEU A 272 7.633 -0.517 21.135 1.00 62.68 C ANISOU 2987 CG LEU A 272 9492 7264 7059 -180 -98 312 C ATOM 2988 CD1 LEU A 272 8.070 -1.717 20.287 1.00 61.07 C ANISOU 2988 CD1 LEU A 272 9231 7094 6879 -193 -66 302 C ATOM 2989 CD2 LEU A 272 6.483 -0.891 22.041 1.00 65.28 C ANISOU 2989 CD2 LEU A 272 9835 7582 7386 -164 -65 272 C ATOM 2990 N LYS A 273 10.832 2.121 23.290 1.00 65.00 N ANISOU 2990 N LYS A 273 9913 7477 7307 -304 -221 394 N ATOM 2991 CA LYS A 273 11.912 2.431 24.219 1.00 65.65 C ANISOU 2991 CA LYS A 273 9997 7576 7373 -353 -258 391 C ATOM 2992 C LYS A 273 11.421 3.504 25.243 1.00 70.20 C ANISOU 2992 C LYS A 273 10669 8085 7917 -366 -274 375 C ATOM 2993 O LYS A 273 11.646 3.334 26.446 1.00 69.14 O ANISOU 2993 O LYS A 273 10546 7960 7762 -360 -299 361 O ATOM 2994 CB LYS A 273 13.182 2.882 23.470 1.00 68.30 C ANISOU 2994 CB LYS A 273 10287 7958 7708 -434 -268 397 C ATOM 2995 CG LYS A 273 14.315 3.342 24.398 1.00 74.35 C ANISOU 2995 CG LYS A 273 11035 8769 8448 -505 -309 373 C ATOM 2996 CD LYS A 273 15.655 3.244 23.731 1.00 79.10 C ANISOU 2996 CD LYS A 273 11538 9465 9051 -571 -314 368 C ATOM 2997 CE LYS A 273 16.690 4.049 24.457 1.00 91.10 C ANISOU 2997 CE LYS A 273 13039 11038 10538 -677 -347 324 C ATOM 2998 NZ LYS A 273 18.020 3.938 23.806 1.00106.84 N ANISOU 2998 NZ LYS A 273 14912 13151 12530 -749 -347 307 N ATOM 2999 N THR A 274 10.687 4.549 24.764 1.00 67.35 N ANISOU 2999 N THR A 274 10388 7657 7545 -364 -257 378 N ATOM 3000 CA THR A 274 10.158 5.633 25.611 1.00 67.91 C ANISOU 3000 CA THR A 274 10571 7650 7581 -362 -262 363 C ATOM 3001 C THR A 274 9.264 5.056 26.723 1.00 71.61 C ANISOU 3001 C THR A 274 11046 8119 8043 -292 -262 347 C ATOM 3002 O THR A 274 9.480 5.375 27.901 1.00 70.86 O ANISOU 3002 O THR A 274 10997 8005 7921 -309 -284 329 O ATOM 3003 CB THR A 274 9.426 6.705 24.784 1.00 67.56 C ANISOU 3003 CB THR A 274 10621 7535 7513 -330 -232 377 C ATOM 3004 OG1 THR A 274 10.346 7.208 23.821 1.00 68.43 O ANISOU 3004 OG1 THR A 274 10741 7636 7623 -407 -219 395 O ATOM 3005 CG2 THR A 274 8.924 7.881 25.649 1.00 62.30 C ANISOU 3005 CG2 THR A 274 10093 6775 6802 -318 -229 362 C ATOM 3006 N LEU A 275 8.319 4.169 26.349 1.00 66.45 N ANISOU 3006 N LEU A 275 10343 7495 7411 -224 -232 347 N ATOM 3007 CA LEU A 275 7.416 3.535 27.304 1.00 65.37 C ANISOU 3007 CA LEU A 275 10209 7360 7268 -172 -211 329 C ATOM 3008 C LEU A 275 8.183 2.711 28.328 1.00 69.32 C ANISOU 3008 C LEU A 275 10695 7879 7764 -186 -224 333 C ATOM 3009 O LEU A 275 7.803 2.736 29.485 1.00 70.63 O ANISOU 3009 O LEU A 275 10911 8023 7902 -161 -221 322 O ATOM 3010 CB LEU A 275 6.358 2.675 26.609 1.00 64.74 C ANISOU 3010 CB LEU A 275 10066 7321 7212 -128 -165 312 C ATOM 3011 CG LEU A 275 5.422 3.378 25.633 1.00 68.70 C ANISOU 3011 CG LEU A 275 10567 7837 7699 -81 -156 300 C ATOM 3012 CD1 LEU A 275 4.430 2.402 25.074 1.00 68.52 C ANISOU 3012 CD1 LEU A 275 10456 7884 7693 -54 -115 262 C ATOM 3013 CD2 LEU A 275 4.692 4.524 26.296 1.00 71.80 C ANISOU 3013 CD2 LEU A 275 11047 8185 8047 -29 -162 291 C ATOM 3014 N GLY A 276 9.278 2.059 27.922 1.00 65.66 N ANISOU 3014 N GLY A 276 10169 7462 7316 -212 -239 350 N ATOM 3015 CA GLY A 276 10.133 1.270 28.813 1.00 65.02 C ANISOU 3015 CA GLY A 276 10073 7418 7213 -196 -257 359 C ATOM 3016 C GLY A 276 10.925 2.133 29.786 1.00 69.08 C ANISOU 3016 C GLY A 276 10618 7946 7682 -231 -315 343 C ATOM 3017 O GLY A 276 11.325 1.658 30.847 1.00 68.90 O ANISOU 3017 O GLY A 276 10605 7955 7619 -194 -335 343 O ATOM 3018 N ILE A 277 11.191 3.406 29.418 1.00 66.70 N ANISOU 3018 N ILE A 277 10342 7622 7379 -305 -339 326 N ATOM 3019 CA ILE A 277 11.907 4.374 30.260 1.00 67.27 C ANISOU 3019 CA ILE A 277 10452 7701 7408 -370 -385 292 C ATOM 3020 C ILE A 277 10.934 4.834 31.382 1.00 72.10 C ANISOU 3020 C ILE A 277 11166 8243 7984 -329 -378 276 C ATOM 3021 O ILE A 277 11.340 4.856 32.550 1.00 72.75 O ANISOU 3021 O ILE A 277 11268 8356 8018 -326 -414 252 O ATOM 3022 CB ILE A 277 12.531 5.544 29.428 1.00 70.12 C ANISOU 3022 CB ILE A 277 10827 8040 7776 -482 -388 275 C ATOM 3023 CG1 ILE A 277 13.679 4.999 28.518 1.00 70.50 C ANISOU 3023 CG1 ILE A 277 10755 8184 7847 -525 -397 285 C ATOM 3024 CG2 ILE A 277 13.065 6.641 30.354 1.00 70.99 C ANISOU 3024 CG2 ILE A 277 11001 8135 7839 -569 -420 223 C ATOM 3025 CD1 ILE A 277 14.094 5.825 27.312 1.00 73.50 C ANISOU 3025 CD1 ILE A 277 11143 8538 8248 -620 -369 287 C ATOM 3026 N ILE A 278 9.642 5.110 31.025 1.00 67.40 N ANISOU 3026 N ILE A 278 10626 7575 7407 -283 -333 286 N ATOM 3027 CA ILE A 278 8.533 5.482 31.919 1.00 67.07 C ANISOU 3027 CA ILE A 278 10671 7477 7336 -227 -312 271 C ATOM 3028 C ILE A 278 8.400 4.408 33.006 1.00 70.71 C ANISOU 3028 C ILE A 278 11118 7973 7774 -171 -305 276 C ATOM 3029 O ILE A 278 8.324 4.710 34.205 1.00 72.41 O ANISOU 3029 O ILE A 278 11398 8176 7940 -156 -320 257 O ATOM 3030 CB ILE A 278 7.198 5.658 31.111 1.00 70.31 C ANISOU 3030 CB ILE A 278 11094 7852 7768 -167 -263 279 C ATOM 3031 CG1 ILE A 278 7.291 6.729 29.984 1.00 71.15 C ANISOU 3031 CG1 ILE A 278 11240 7915 7879 -193 -262 286 C ATOM 3032 CG2 ILE A 278 6.009 5.931 32.022 1.00 70.92 C ANISOU 3032 CG2 ILE A 278 11237 7897 7812 -98 -235 259 C ATOM 3033 CD1 ILE A 278 7.200 8.171 30.467 1.00 87.05 C ANISOU 3033 CD1 ILE A 278 13392 9837 9845 -206 -265 267 C ATOM 3034 N MET A 279 8.419 3.154 32.575 1.00 65.47 N ANISOU 3034 N MET A 279 10385 7349 7141 -142 -276 302 N ATOM 3035 CA MET A 279 8.331 1.958 33.424 1.00 64.14 C ANISOU 3035 CA MET A 279 10223 7198 6950 -83 -247 318 C ATOM 3036 C MET A 279 9.581 1.732 34.292 1.00 69.17 C ANISOU 3036 C MET A 279 10857 7893 7531 -71 -305 322 C ATOM 3037 O MET A 279 9.460 1.272 35.428 1.00 70.15 O ANISOU 3037 O MET A 279 11035 8018 7601 -11 -295 329 O ATOM 3038 CB MET A 279 8.117 0.731 32.532 1.00 64.98 C ANISOU 3038 CB MET A 279 10271 7315 7103 -67 -191 339 C ATOM 3039 CG MET A 279 6.784 0.708 31.907 1.00 66.95 C ANISOU 3039 CG MET A 279 10510 7537 7389 -68 -130 321 C ATOM 3040 SD MET A 279 6.785 -0.548 30.661 1.00 69.74 S ANISOU 3040 SD MET A 279 10788 7914 7796 -79 -78 328 S ATOM 3041 CE MET A 279 5.145 -0.390 30.098 1.00 66.59 C ANISOU 3041 CE MET A 279 10362 7518 7422 -85 -19 283 C ATOM 3042 N GLY A 280 10.762 1.973 33.734 1.00 65.50 N ANISOU 3042 N GLY A 280 10323 7493 7072 -119 -360 317 N ATOM 3043 CA GLY A 280 12.007 1.773 34.463 1.00 67.02 C ANISOU 3043 CA GLY A 280 10481 7781 7203 -102 -424 307 C ATOM 3044 C GLY A 280 12.254 2.837 35.519 1.00 71.56 C ANISOU 3044 C GLY A 280 11105 8369 7717 -142 -479 258 C ATOM 3045 O GLY A 280 12.745 2.535 36.614 1.00 71.36 O ANISOU 3045 O GLY A 280 11089 8410 7615 -86 -518 249 O ATOM 3046 N THR A 281 11.901 4.092 35.189 1.00 68.22 N ANISOU 3046 N THR A 281 10724 7879 7318 -231 -479 226 N ATOM 3047 CA THR A 281 12.039 5.246 36.081 1.00 69.31 C ANISOU 3047 CA THR A 281 10932 8001 7402 -288 -517 169 C ATOM 3048 C THR A 281 11.077 5.061 37.284 1.00 74.16 C ANISOU 3048 C THR A 281 11642 8567 7969 -199 -494 174 C ATOM 3049 O THR A 281 11.529 5.170 38.432 1.00 75.75 O ANISOU 3049 O THR A 281 11867 8821 8093 -184 -540 142 O ATOM 3050 CB THR A 281 11.847 6.546 35.291 1.00 74.12 C ANISOU 3050 CB THR A 281 11593 8523 8048 -392 -499 144 C ATOM 3051 OG1 THR A 281 12.908 6.632 34.340 1.00 74.49 O ANISOU 3051 OG1 THR A 281 11549 8631 8123 -481 -517 135 O ATOM 3052 CG2 THR A 281 11.900 7.764 36.155 1.00 74.39 C ANISOU 3052 CG2 THR A 281 11727 8510 8027 -457 -521 81 C ATOM 3053 N PHE A 282 9.801 4.679 37.025 1.00 68.33 N ANISOU 3053 N PHE A 282 10942 7750 7269 -138 -421 211 N ATOM 3054 CA PHE A 282 8.819 4.420 38.080 1.00 67.39 C ANISOU 3054 CA PHE A 282 10905 7591 7110 -60 -380 217 C ATOM 3055 C PHE A 282 9.359 3.366 39.049 1.00 74.06 C ANISOU 3055 C PHE A 282 11747 8503 7890 15 -393 239 C ATOM 3056 O PHE A 282 9.350 3.593 40.256 1.00 76.63 O ANISOU 3056 O PHE A 282 12140 8838 8137 50 -413 219 O ATOM 3057 CB PHE A 282 7.482 3.970 37.478 1.00 67.23 C ANISOU 3057 CB PHE A 282 10886 7513 7145 -21 -294 244 C ATOM 3058 CG PHE A 282 6.377 3.758 38.486 1.00 67.52 C ANISOU 3058 CG PHE A 282 10997 7514 7145 43 -235 242 C ATOM 3059 CD1 PHE A 282 6.208 2.523 39.112 1.00 70.30 C ANISOU 3059 CD1 PHE A 282 11363 7878 7471 101 -183 273 C ATOM 3060 CD2 PHE A 282 5.479 4.777 38.780 1.00 68.43 C ANISOU 3060 CD2 PHE A 282 11177 7578 7245 52 -218 210 C ATOM 3061 CE1 PHE A 282 5.188 2.329 40.046 1.00 71.41 C ANISOU 3061 CE1 PHE A 282 11575 7985 7573 148 -114 270 C ATOM 3062 CE2 PHE A 282 4.445 4.579 39.696 1.00 71.57 C ANISOU 3062 CE2 PHE A 282 11632 7956 7606 111 -157 204 C ATOM 3063 CZ PHE A 282 4.303 3.356 40.322 1.00 70.90 C ANISOU 3063 CZ PHE A 282 11553 7888 7498 149 -103 233 C ATOM 3064 N THR A 283 9.858 2.238 38.512 1.00 69.39 N ANISOU 3064 N THR A 283 11090 7957 7320 51 -381 280 N ATOM 3065 CA THR A 283 10.438 1.120 39.256 1.00 68.62 C ANISOU 3065 CA THR A 283 11001 7919 7153 150 -384 314 C ATOM 3066 C THR A 283 11.642 1.599 40.084 1.00 72.49 C ANISOU 3066 C THR A 283 11465 8524 7552 156 -488 274 C ATOM 3067 O THR A 283 11.655 1.372 41.272 1.00 71.01 O ANISOU 3067 O THR A 283 11345 8363 7273 237 -499 276 O ATOM 3068 CB THR A 283 10.802 -0.024 38.289 1.00 70.36 C ANISOU 3068 CB THR A 283 11159 8156 7419 182 -349 360 C ATOM 3069 OG1 THR A 283 9.609 -0.453 37.631 1.00 69.78 O ANISOU 3069 OG1 THR A 283 11109 7987 7418 164 -251 378 O ATOM 3070 CG2 THR A 283 11.467 -1.218 38.988 1.00 66.07 C ANISOU 3070 CG2 THR A 283 10645 7666 6792 311 -345 403 C ATOM 3071 N LEU A 284 12.618 2.283 39.484 1.00 71.26 N ANISOU 3071 N LEU A 284 11215 8445 7414 66 -560 230 N ATOM 3072 CA LEU A 284 13.789 2.740 40.231 1.00 72.66 C ANISOU 3072 CA LEU A 284 11343 8761 7503 50 -659 170 C ATOM 3073 C LEU A 284 13.413 3.693 41.354 1.00 74.63 C ANISOU 3073 C LEU A 284 11685 8982 7689 21 -683 115 C ATOM 3074 O LEU A 284 14.014 3.618 42.416 1.00 74.98 O ANISOU 3074 O LEU A 284 11729 9133 7626 76 -745 83 O ATOM 3075 CB LEU A 284 14.816 3.407 39.299 1.00 73.96 C ANISOU 3075 CB LEU A 284 11387 9006 7707 -80 -711 119 C ATOM 3076 CG LEU A 284 15.708 2.419 38.544 1.00 80.90 C ANISOU 3076 CG LEU A 284 12145 9994 8600 -27 -723 154 C ATOM 3077 CD1 LEU A 284 16.089 2.959 37.184 1.00 81.42 C ANISOU 3077 CD1 LEU A 284 12128 10055 8754 -161 -715 135 C ATOM 3078 CD2 LEU A 284 16.955 2.059 39.362 1.00 86.37 C ANISOU 3078 CD2 LEU A 284 12751 10890 9176 49 -813 117 C ATOM 3079 N CYS A 285 12.423 4.573 41.123 1.00 68.90 N ANISOU 3079 N CYS A 285 11040 8120 7019 -51 -635 101 N ATOM 3080 CA CYS A 285 11.962 5.559 42.094 1.00 67.99 C ANISOU 3080 CA CYS A 285 11029 7955 6849 -78 -646 47 C ATOM 3081 C CYS A 285 11.117 4.939 43.196 1.00 71.17 C ANISOU 3081 C CYS A 285 11528 8324 7190 50 -603 84 C ATOM 3082 O CYS A 285 11.148 5.461 44.290 1.00 71.10 O ANISOU 3082 O CYS A 285 11585 8334 7095 60 -637 37 O ATOM 3083 CB CYS A 285 11.193 6.678 41.396 1.00 67.42 C ANISOU 3083 CB CYS A 285 11020 7747 6848 -171 -601 28 C ATOM 3084 SG CYS A 285 12.213 7.743 40.349 1.00 71.66 S ANISOU 3084 SG CYS A 285 11499 8299 7431 -347 -638 -32 S ATOM 3085 N TRP A 286 10.313 3.889 42.916 1.00 69.33 N ANISOU 3085 N TRP A 286 11313 8033 6997 134 -518 161 N ATOM 3086 CA TRP A 286 9.409 3.318 43.921 1.00 69.76 C ANISOU 3086 CA TRP A 286 11470 8039 6996 237 -452 195 C ATOM 3087 C TRP A 286 9.912 2.055 44.578 1.00 76.69 C ANISOU 3087 C TRP A 286 12363 8983 7791 362 -447 247 C ATOM 3088 O TRP A 286 9.500 1.781 45.702 1.00 78.73 O ANISOU 3088 O TRP A 286 12721 9228 7963 446 -415 262 O ATOM 3089 CB TRP A 286 8.026 3.044 43.318 1.00 67.59 C ANISOU 3089 CB TRP A 286 11223 7652 6806 235 -339 231 C ATOM 3090 CG TRP A 286 7.153 4.263 43.283 1.00 68.57 C ANISOU 3090 CG TRP A 286 11394 7703 6956 182 -324 185 C ATOM 3091 CD1 TRP A 286 6.780 4.965 42.180 1.00 70.83 C ANISOU 3091 CD1 TRP A 286 11644 7942 7325 116 -315 170 C ATOM 3092 CD2 TRP A 286 6.637 4.988 44.411 1.00 69.53 C ANISOU 3092 CD2 TRP A 286 11617 7795 7005 207 -321 148 C ATOM 3093 NE1 TRP A 286 5.982 6.022 42.540 1.00 70.08 N ANISOU 3093 NE1 TRP A 286 11629 7784 7213 113 -298 132 N ATOM 3094 CE2 TRP A 286 5.902 6.079 43.905 1.00 72.43 C ANISOU 3094 CE2 TRP A 286 12010 8091 7420 162 -303 114 C ATOM 3095 CE3 TRP A 286 6.709 4.812 45.807 1.00 71.75 C ANISOU 3095 CE3 TRP A 286 11979 8105 7176 277 -329 142 C ATOM 3096 CZ2 TRP A 286 5.270 7.008 44.739 1.00 72.21 C ANISOU 3096 CZ2 TRP A 286 12086 8014 7337 182 -292 71 C ATOM 3097 CZ3 TRP A 286 6.080 5.734 46.626 1.00 73.27 C ANISOU 3097 CZ3 TRP A 286 12266 8254 7317 284 -321 96 C ATOM 3098 CH2 TRP A 286 5.391 6.827 46.090 1.00 73.38 C ANISOU 3098 CH2 TRP A 286 12303 8192 7384 235 -302 59 C ATOM 3099 N LEU A 287 10.766 1.267 43.899 1.00 73.77 N ANISOU 3099 N LEU A 287 11909 8680 7439 389 -469 280 N ATOM 3100 CA LEU A 287 11.273 -0.005 44.423 1.00 74.54 C ANISOU 3100 CA LEU A 287 12038 8832 7451 536 -455 340 C ATOM 3101 C LEU A 287 12.058 0.181 45.736 1.00 78.97 C ANISOU 3101 C LEU A 287 12626 9518 7861 625 -544 310 C ATOM 3102 O LEU A 287 11.770 -0.585 46.659 1.00 78.47 O ANISOU 3102 O LEU A 287 12677 9435 7704 758 -493 361 O ATOM 3103 CB LEU A 287 12.103 -0.770 43.377 1.00 75.11 C ANISOU 3103 CB LEU A 287 12010 8960 7567 555 -467 372 C ATOM 3104 CG LEU A 287 12.415 -2.254 43.634 1.00 82.05 C ANISOU 3104 CG LEU A 287 12950 9849 8378 720 -415 451 C ATOM 3105 CD1 LEU A 287 11.152 -3.065 43.998 1.00 82.40 C ANISOU 3105 CD1 LEU A 287 13148 9732 8426 764 -265 511 C ATOM 3106 CD2 LEU A 287 13.107 -2.859 42.432 1.00 85.68 C ANISOU 3106 CD2 LEU A 287 13309 10347 8900 721 -419 473 C ATOM 3107 N PRO A 288 12.964 1.200 45.915 1.00 75.75 N ANISOU 3107 N PRO A 288 12130 9237 7416 551 -666 222 N ATOM 3108 CA PRO A 288 13.646 1.339 47.222 1.00 76.03 C ANISOU 3108 CA PRO A 288 12186 9410 7292 640 -753 180 C ATOM 3109 C PRO A 288 12.653 1.431 48.382 1.00 79.19 C ANISOU 3109 C PRO A 288 12746 9720 7623 700 -695 195 C ATOM 3110 O PRO A 288 12.801 0.684 49.338 1.00 80.00 O ANISOU 3110 O PRO A 288 12927 9872 7598 859 -690 237 O ATOM 3111 CB PRO A 288 14.461 2.628 47.065 1.00 77.78 C ANISOU 3111 CB PRO A 288 12295 9740 7519 484 -864 61 C ATOM 3112 CG PRO A 288 14.685 2.760 45.607 1.00 80.47 C ANISOU 3112 CG PRO A 288 12529 10050 7994 366 -849 64 C ATOM 3113 CD PRO A 288 13.443 2.229 44.963 1.00 75.03 C ANISOU 3113 CD PRO A 288 11922 9174 7413 382 -724 151 C ATOM 3114 N PHE A 289 11.594 2.264 48.253 1.00 74.07 N ANISOU 3114 N PHE A 289 12156 8934 7055 590 -639 169 N ATOM 3115 CA PHE A 289 10.561 2.435 49.277 1.00 72.68 C ANISOU 3115 CA PHE A 289 12122 8670 6822 635 -574 176 C ATOM 3116 C PHE A 289 9.891 1.105 49.574 1.00 76.96 C ANISOU 3116 C PHE A 289 12766 9137 7339 766 -453 279 C ATOM 3117 O PHE A 289 9.951 0.646 50.706 1.00 79.77 O ANISOU 3117 O PHE A 289 13221 9527 7561 894 -445 306 O ATOM 3118 CB PHE A 289 9.521 3.505 48.853 1.00 72.70 C ANISOU 3118 CB PHE A 289 12152 8543 6927 508 -526 135 C ATOM 3119 CG PHE A 289 8.321 3.642 49.767 1.00 72.80 C ANISOU 3119 CG PHE A 289 12299 8464 6897 556 -441 145 C ATOM 3120 CD1 PHE A 289 8.413 4.352 50.960 1.00 75.40 C ANISOU 3120 CD1 PHE A 289 12705 8832 7111 578 -490 85 C ATOM 3121 CD2 PHE A 289 7.100 3.061 49.433 1.00 73.69 C ANISOU 3121 CD2 PHE A 289 12454 8465 7081 571 -307 203 C ATOM 3122 CE1 PHE A 289 7.305 4.474 51.808 1.00 76.60 C ANISOU 3122 CE1 PHE A 289 12981 8905 7220 628 -406 93 C ATOM 3123 CE2 PHE A 289 5.990 3.179 50.282 1.00 76.70 C ANISOU 3123 CE2 PHE A 289 12945 8779 7419 611 -220 205 C ATOM 3124 CZ PHE A 289 6.101 3.886 51.465 1.00 75.69 C ANISOU 3124 CZ PHE A 289 12898 8683 7176 645 -269 155 C ATOM 3125 N PHE A 290 9.312 0.454 48.564 1.00 73.27 N ANISOU 3125 N PHE A 290 12280 8572 6988 734 -357 334 N ATOM 3126 CA PHE A 290 8.618 -0.827 48.744 1.00 71.91 C ANISOU 3126 CA PHE A 290 12214 8308 6803 824 -218 421 C ATOM 3127 C PHE A 290 9.521 -1.973 49.279 1.00 78.40 C ANISOU 3127 C PHE A 290 13091 9197 7499 994 -227 487 C ATOM 3128 O PHE A 290 9.021 -2.792 50.045 1.00 78.99 O ANISOU 3128 O PHE A 290 13315 9203 7494 1097 -122 550 O ATOM 3129 CB PHE A 290 7.914 -1.238 47.452 1.00 70.90 C ANISOU 3129 CB PHE A 290 12034 8081 6824 733 -123 444 C ATOM 3130 CG PHE A 290 6.610 -0.494 47.277 1.00 70.13 C ANISOU 3130 CG PHE A 290 11941 7898 6806 631 -58 404 C ATOM 3131 CD1 PHE A 290 5.456 -0.908 47.939 1.00 71.70 C ANISOU 3131 CD1 PHE A 290 12249 8016 6979 655 74 426 C ATOM 3132 CD2 PHE A 290 6.527 0.616 46.439 1.00 70.12 C ANISOU 3132 CD2 PHE A 290 11841 7904 6898 520 -120 345 C ATOM 3133 CE1 PHE A 290 4.248 -0.215 47.773 1.00 70.90 C ANISOU 3133 CE1 PHE A 290 12132 7865 6942 577 131 382 C ATOM 3134 CE2 PHE A 290 5.314 1.298 46.269 1.00 70.99 C ANISOU 3134 CE2 PHE A 290 11959 7949 7066 460 -61 311 C ATOM 3135 CZ PHE A 290 4.190 0.881 46.945 1.00 68.06 C ANISOU 3135 CZ PHE A 290 11672 7520 6666 493 59 327 C ATOM 3136 N ILE A 291 10.820 -2.021 48.923 1.00 76.43 N ANISOU 3136 N ILE A 291 12733 9086 7221 1033 -345 473 N ATOM 3137 CA ILE A 291 11.715 -3.075 49.415 1.00 78.16 C ANISOU 3137 CA ILE A 291 13000 9390 7306 1226 -362 534 C ATOM 3138 C ILE A 291 11.952 -2.882 50.928 1.00 85.57 C ANISOU 3138 C ILE A 291 14034 10417 8063 1355 -415 523 C ATOM 3139 O ILE A 291 11.711 -3.803 51.707 1.00 84.78 O ANISOU 3139 O ILE A 291 14096 10265 7850 1513 -328 602 O ATOM 3140 CB ILE A 291 13.047 -3.170 48.607 1.00 81.08 C ANISOU 3140 CB ILE A 291 13206 9914 7688 1243 -476 513 C ATOM 3141 CG1 ILE A 291 12.814 -3.904 47.284 1.00 80.52 C ANISOU 3141 CG1 ILE A 291 13104 9738 7751 1195 -387 563 C ATOM 3142 CG2 ILE A 291 14.163 -3.870 49.430 1.00 83.73 C ANISOU 3142 CG2 ILE A 291 13565 10414 7836 1471 -548 544 C ATOM 3143 CD1 ILE A 291 14.075 -4.060 46.363 1.00 93.84 C ANISOU 3143 CD1 ILE A 291 14627 11568 9459 1210 -481 547 C ATOM 3144 N VAL A 292 12.390 -1.673 51.327 1.00 85.99 N ANISOU 3144 N VAL A 292 13997 10593 8084 1280 -546 421 N ATOM 3145 CA VAL A 292 12.685 -1.270 52.714 1.00 88.14 C ANISOU 3145 CA VAL A 292 14330 10976 8183 1375 -622 380 C ATOM 3146 C VAL A 292 11.406 -1.391 53.569 1.00 94.07 C ANISOU 3146 C VAL A 292 15271 11570 8901 1404 -491 425 C ATOM 3147 O VAL A 292 11.473 -1.802 54.723 1.00 94.66 O ANISOU 3147 O VAL A 292 15472 11684 8811 1565 -481 459 O ATOM 3148 CB VAL A 292 13.304 0.150 52.718 1.00 92.03 C ANISOU 3148 CB VAL A 292 14680 11602 8686 1227 -770 242 C ATOM 3149 CG1 VAL A 292 13.342 0.764 54.111 1.00 93.03 C ANISOU 3149 CG1 VAL A 292 14880 11812 8656 1278 -833 178 C ATOM 3150 CG2 VAL A 292 14.707 0.113 52.115 1.00 92.40 C ANISOU 3150 CG2 VAL A 292 14542 11846 8720 1228 -895 196 C ATOM 3151 N ASN A 293 10.249 -1.136 52.966 1.00 91.06 N ANISOU 3151 N ASN A 293 14910 11020 8669 1264 -382 429 N ATOM 3152 CA ASN A 293 8.966 -1.287 53.634 1.00 91.03 C ANISOU 3152 CA ASN A 293 15061 10875 8651 1273 -241 465 C ATOM 3153 C ASN A 293 8.697 -2.779 53.975 1.00 94.14 C ANISOU 3153 C ASN A 293 15613 11183 8972 1421 -97 583 C ATOM 3154 O ASN A 293 8.339 -3.059 55.107 1.00 94.67 O ANISOU 3154 O ASN A 293 15836 11225 8908 1529 -35 619 O ATOM 3155 CB ASN A 293 7.871 -0.713 52.741 1.00 92.87 C ANISOU 3155 CB ASN A 293 15243 10983 9062 1095 -166 435 C ATOM 3156 CG ASN A 293 6.521 -0.683 53.379 1.00123.17 C ANISOU 3156 CG ASN A 293 19202 14704 12891 1084 -29 447 C ATOM 3157 OD1 ASN A 293 6.200 0.206 54.178 1.00115.36 O ANISOU 3157 OD1 ASN A 293 18254 13732 11845 1075 -60 392 O ATOM 3158 ND2 ASN A 293 5.704 -1.662 53.026 1.00117.40 N ANISOU 3158 ND2 ASN A 293 18532 13859 12217 1078 131 513 N ATOM 3159 N ILE A 294 8.914 -3.721 53.024 1.00 90.71 N ANISOU 3159 N ILE A 294 15155 10700 8611 1431 -41 643 N ATOM 3160 CA ILE A 294 8.649 -5.162 53.221 1.00 91.54 C ANISOU 3160 CA ILE A 294 15433 10692 8656 1555 117 753 C ATOM 3161 C ILE A 294 9.719 -5.830 54.149 1.00 97.04 C ANISOU 3161 C ILE A 294 16232 11498 9143 1804 59 812 C ATOM 3162 O ILE A 294 9.377 -6.739 54.912 1.00 95.95 O ANISOU 3162 O ILE A 294 16303 11266 8888 1940 190 898 O ATOM 3163 CB ILE A 294 8.469 -5.912 51.849 1.00 93.70 C ANISOU 3163 CB ILE A 294 15657 10865 9080 1471 205 784 C ATOM 3164 CG1 ILE A 294 7.575 -7.149 51.984 1.00 94.97 C ANISOU 3164 CG1 ILE A 294 16014 10839 9231 1496 430 867 C ATOM 3165 CG2 ILE A 294 9.779 -6.254 51.114 1.00 93.71 C ANISOU 3165 CG2 ILE A 294 15548 10978 9078 1547 93 795 C ATOM 3166 CD1 ILE A 294 6.103 -6.866 51.814 1.00103.07 C ANISOU 3166 CD1 ILE A 294 17046 11745 10370 1316 564 829 C ATOM 3167 N VAL A 295 10.979 -5.335 54.097 1.00 95.18 N ANISOU 3167 N VAL A 295 15846 11467 8852 1861 -133 758 N ATOM 3168 CA VAL A 295 12.133 -5.767 54.886 1.00 97.07 C ANISOU 3168 CA VAL A 295 16119 11877 8886 2100 -233 786 C ATOM 3169 C VAL A 295 11.906 -5.413 56.345 1.00106.65 C ANISOU 3169 C VAL A 295 17457 13135 9929 2198 -248 776 C ATOM 3170 O VAL A 295 12.197 -6.219 57.223 1.00108.64 O ANISOU 3170 O VAL A 295 17872 13411 9994 2428 -214 855 O ATOM 3171 CB VAL A 295 13.438 -5.132 54.332 1.00100.19 C ANISOU 3171 CB VAL A 295 16271 12505 9293 2077 -436 697 C ATOM 3172 CG1 VAL A 295 14.527 -4.996 55.397 1.00101.75 C ANISOU 3172 CG1 VAL A 295 16445 12949 9268 2272 -588 663 C ATOM 3173 CG2 VAL A 295 13.951 -5.907 53.129 1.00 99.40 C ANISOU 3173 CG2 VAL A 295 16095 12391 9280 2094 -414 743 C ATOM 3174 N HIS A 296 11.359 -4.229 56.609 1.00106.15 N ANISOU 3174 N HIS A 296 17336 13074 9923 2035 -291 683 N ATOM 3175 CA HIS A 296 11.123 -3.792 57.972 1.00108.85 C ANISOU 3175 CA HIS A 296 17789 13462 10108 2113 -310 660 C ATOM 3176 C HIS A 296 9.849 -4.393 58.580 1.00114.04 C ANISOU 3176 C HIS A 296 18677 13913 10741 2141 -101 746 C ATOM 3177 O HIS A 296 9.594 -4.185 59.769 1.00116.21 O ANISOU 3177 O HIS A 296 19075 14210 10869 2229 -91 745 O ATOM 3178 CB HIS A 296 11.140 -2.271 58.065 1.00110.09 C ANISOU 3178 CB HIS A 296 17806 13709 10316 1941 -440 519 C ATOM 3179 CG HIS A 296 12.510 -1.702 57.830 1.00115.07 C ANISOU 3179 CG HIS A 296 18238 14575 10907 1934 -644 422 C ATOM 3180 ND1 HIS A 296 13.614 -2.154 58.529 1.00119.29 N ANISOU 3180 ND1 HIS A 296 18766 15319 11241 2147 -752 427 N ATOM 3181 CD2 HIS A 296 12.905 -0.716 56.997 1.00116.66 C ANISOU 3181 CD2 HIS A 296 18248 14838 11239 1738 -746 315 C ATOM 3182 CE1 HIS A 296 14.643 -1.469 58.064 1.00119.04 C ANISOU 3182 CE1 HIS A 296 18517 15481 11232 2061 -916 316 C ATOM 3183 NE2 HIS A 296 14.263 -0.573 57.162 1.00117.76 N ANISOU 3183 NE2 HIS A 296 18249 15229 11267 1807 -913 246 N ATOM 3184 N VAL A 297 9.100 -5.192 57.802 1.00108.92 N ANISOU 3184 N VAL A 297 18089 13075 10220 2072 71 818 N ATOM 3185 CA VAL A 297 7.916 -5.910 58.273 1.00108.71 C ANISOU 3185 CA VAL A 297 18276 12852 10176 2078 295 897 C ATOM 3186 C VAL A 297 8.407 -7.268 58.821 1.00115.73 C ANISOU 3186 C VAL A 297 19376 13706 10889 2324 382 1023 C ATOM 3187 O VAL A 297 7.958 -7.695 59.890 1.00116.35 O ANISOU 3187 O VAL A 297 19670 13715 10820 2439 497 1086 O ATOM 3188 CB VAL A 297 6.823 -6.031 57.172 1.00110.14 C ANISOU 3188 CB VAL A 297 18405 12864 10577 1859 439 888 C ATOM 3189 CG1 VAL A 297 5.760 -7.048 57.543 1.00110.38 C ANISOU 3189 CG1 VAL A 297 18655 12702 10584 1864 690 971 C ATOM 3190 CG2 VAL A 297 6.176 -4.684 56.893 1.00108.35 C ANISOU 3190 CG2 VAL A 297 18026 12663 10481 1665 377 778 C ATOM 3191 N ILE A 298 9.370 -7.906 58.111 1.00113.85 N ANISOU 3191 N ILE A 298 19083 13522 10652 2418 324 1060 N ATOM 3192 CA ILE A 298 9.997 -9.173 58.498 1.00116.05 C ANISOU 3192 CA ILE A 298 19555 13780 10757 2681 389 1179 C ATOM 3193 C ILE A 298 10.895 -8.909 59.710 1.00123.88 C ANISOU 3193 C ILE A 298 20580 14984 11507 2920 238 1175 C ATOM 3194 O ILE A 298 10.590 -9.370 60.809 1.00125.27 O ANISOU 3194 O ILE A 298 20989 15103 11507 3079 337 1248 O ATOM 3195 CB ILE A 298 10.793 -9.855 57.333 1.00118.71 C ANISOU 3195 CB ILE A 298 19804 14131 11167 2719 361 1209 C ATOM 3196 CG1 ILE A 298 10.164 -9.627 55.928 1.00117.14 C ANISOU 3196 CG1 ILE A 298 19452 13822 11235 2440 412 1156 C ATOM 3197 CG2 ILE A 298 11.025 -11.344 57.599 1.00121.39 C ANISOU 3197 CG2 ILE A 298 20412 14350 11361 2961 513 1350 C ATOM 3198 CD1 ILE A 298 8.714 -10.201 55.630 1.00126.59 C ANISOU 3198 CD1 ILE A 298 20796 14752 12552 2272 667 1191 C ATOM 3199 N GLN A 299 11.966 -8.121 59.507 1.00121.96 N ANISOU 3199 N GLN A 299 20098 14991 11252 2930 2 1078 N ATOM 3200 CA GLN A 299 12.962 -7.762 60.519 1.00124.22 C ANISOU 3200 CA GLN A 299 20350 15536 11313 3134 -178 1039 C ATOM 3201 C GLN A 299 12.380 -7.034 61.711 1.00131.02 C ANISOU 3201 C GLN A 299 21294 16412 12074 3117 -183 995 C ATOM 3202 O GLN A 299 12.890 -7.238 62.807 1.00133.93 O ANISOU 3202 O GLN A 299 21769 16914 12203 3355 -240 1020 O ATOM 3203 CB GLN A 299 14.074 -6.896 59.921 1.00125.14 C ANISOU 3203 CB GLN A 299 20156 15911 11481 3059 -414 910 C ATOM 3204 CG GLN A 299 15.070 -7.680 59.078 1.00141.70 C ANISOU 3204 CG GLN A 299 22167 18095 13578 3186 -458 952 C ATOM 3205 CD GLN A 299 16.260 -6.854 58.654 1.00161.12 C ANISOU 3205 CD GLN A 299 24321 20848 16050 3132 -689 819 C ATOM 3206 OE1 GLN A 299 16.274 -5.617 58.751 1.00155.45 O ANISOU 3206 OE1 GLN A 299 23443 20231 15389 2939 -805 685 O ATOM 3207 NE2 GLN A 299 17.289 -7.530 58.159 1.00153.00 N ANISOU 3207 NE2 GLN A 299 23210 19958 14965 3299 -751 849 N ATOM 3208 N ASP A 300 11.356 -6.164 61.505 1.00126.86 N ANISOU 3208 N ASP A 300 20717 15767 11717 2854 -133 925 N ATOM 3209 CA ASP A 300 10.665 -5.343 62.520 1.00127.45 C ANISOU 3209 CA ASP A 300 20858 15837 11729 2801 -127 869 C ATOM 3210 C ASP A 300 11.449 -4.036 62.832 1.00132.78 C ANISOU 3210 C ASP A 300 21332 16759 12360 2746 -365 714 C ATOM 3211 O ASP A 300 10.812 -2.992 62.968 1.00130.99 O ANISOU 3211 O ASP A 300 21060 16497 12215 2566 -377 623 O ATOM 3212 CB ASP A 300 10.348 -6.148 63.818 1.00131.19 C ANISOU 3212 CB ASP A 300 21623 16251 11972 3037 0 979 C ATOM 3213 CG ASP A 300 9.543 -5.435 64.901 1.00141.49 C ANISOU 3213 CG ASP A 300 23026 17532 13203 2997 36 936 C ATOM 3214 OD1 ASP A 300 8.398 -5.017 64.617 1.00140.51 O ANISOU 3214 OD1 ASP A 300 22902 17246 13241 2786 155 910 O ATOM 3215 OD2 ASP A 300 10.020 -5.383 66.060 1.00148.37 O ANISOU 3215 OD2 ASP A 300 23989 18544 13839 3196 -40 936 O ATOM 3216 N ASN A 301 12.806 -4.076 62.913 1.00132.51 N ANISOU 3216 N ASN A 301 21175 16976 12199 2890 -547 674 N ATOM 3217 CA ASN A 301 13.620 -2.901 63.279 1.00134.63 C ANISOU 3217 CA ASN A 301 21253 17497 12401 2831 -766 512 C ATOM 3218 C ASN A 301 14.556 -2.360 62.160 1.00141.18 C ANISOU 3218 C ASN A 301 21801 18475 13365 2680 -916 408 C ATOM 3219 O ASN A 301 14.828 -3.059 61.173 1.00140.65 O ANISOU 3219 O ASN A 301 21679 18364 13397 2692 -878 474 O ATOM 3220 CB ASN A 301 14.460 -3.203 64.546 1.00138.98 C ANISOU 3220 CB ASN A 301 21873 18284 12648 3119 -875 512 C ATOM 3221 CG ASN A 301 15.880 -3.721 64.337 1.00163.49 C ANISOU 3221 CG ASN A 301 24837 21652 15628 3312 -1024 505 C ATOM 3222 OD1 ASN A 301 16.197 -4.449 63.380 1.00159.07 O ANISOU 3222 OD1 ASN A 301 24230 21050 15161 3342 -986 575 O ATOM 3223 ND2 ASN A 301 16.769 -3.373 65.255 1.00154.30 N ANISOU 3223 ND2 ASN A 301 23604 20783 14240 3459 -1198 414 N ATOM 3224 N LEU A 302 15.096 -1.117 62.408 1.00139.27 N ANISOU 3224 N LEU A 302 21395 18420 13103 2546 -1084 239 N ATOM 3225 CA LEU A 302 16.028 -0.264 61.638 1.00138.97 C ANISOU 3225 CA LEU A 302 21089 18558 13155 2366 -1243 95 C ATOM 3226 C LEU A 302 15.258 0.502 60.497 1.00140.93 C ANISOU 3226 C LEU A 302 21275 18590 13681 2061 -1168 61 C ATOM 3227 O LEU A 302 15.870 1.159 59.638 1.00139.55 O ANISOU 3227 O LEU A 302 20906 18498 13620 1883 -1257 -36 O ATOM 3228 CB LEU A 302 17.298 -1.040 61.155 1.00139.85 C ANISOU 3228 CB LEU A 302 21053 18887 13198 2523 -1339 115 C ATOM 3229 CG LEU A 302 17.602 -1.269 59.676 1.00142.38 C ANISOU 3229 CG LEU A 302 21221 19160 13716 2402 -1322 135 C ATOM 3230 CD1 LEU A 302 18.839 -0.504 59.248 1.00143.09 C ANISOU 3230 CD1 LEU A 302 21031 19528 13808 2281 -1504 -25 C ATOM 3231 CD2 LEU A 302 17.772 -2.733 59.379 1.00144.28 C ANISOU 3231 CD2 LEU A 302 21554 19355 13909 2645 -1237 294 C ATOM 3232 N ILE A 303 13.900 0.514 60.598 1.00136.87 N ANISOU 3232 N ILE A 303 20932 17817 13255 2002 -1007 129 N ATOM 3233 CA ILE A 303 12.977 1.193 59.681 1.00134.50 C ANISOU 3233 CA ILE A 303 20608 17311 13187 1761 -922 109 C ATOM 3234 C ILE A 303 13.208 2.686 59.652 1.00135.68 C ANISOU 3234 C ILE A 303 20649 17524 13380 1553 -1031 -54 C ATOM 3235 O ILE A 303 13.234 3.266 58.567 1.00135.60 O ANISOU 3235 O ILE A 303 20523 17457 13542 1363 -1039 -100 O ATOM 3236 CB ILE A 303 11.499 0.898 60.030 1.00137.12 C ANISOU 3236 CB ILE A 303 21138 17404 13557 1773 -735 200 C ATOM 3237 N ARG A 304 13.336 3.300 60.841 1.00129.49 N ANISOU 3237 N ARG A 304 19921 16843 12435 1590 -1103 -141 N ATOM 3238 CA ARG A 304 13.512 4.729 61.085 1.00128.20 C ANISOU 3238 CA ARG A 304 19704 16731 12273 1406 -1194 -308 C ATOM 3239 C ARG A 304 12.277 5.508 60.589 1.00127.00 C ANISOU 3239 C ARG A 304 19631 16325 12298 1234 -1076 -310 C ATOM 3240 O ARG A 304 11.204 4.921 60.440 1.00125.83 O ANISOU 3240 O ARG A 304 19594 15996 12220 1288 -929 -191 O ATOM 3241 CB ARG A 304 14.834 5.268 60.487 1.00129.15 C ANISOU 3241 CB ARG A 304 19604 17056 12411 1277 -1348 -437 C ATOM 3242 CG ARG A 304 15.632 6.229 61.402 1.00143.59 C ANISOU 3242 CG ARG A 304 21376 19100 14082 1215 -1496 -620 C ATOM 3243 CD ARG A 304 15.137 6.353 62.845 1.00157.69 C ANISOU 3243 CD ARG A 304 23332 20895 15687 1344 -1490 -635 C ATOM 3244 NE ARG A 304 14.511 7.651 63.118 1.00166.14 N ANISOU 3244 NE ARG A 304 24486 21836 16802 1157 -1466 -747 N ATOM 3245 CZ ARG A 304 13.484 7.837 63.947 1.00176.09 C ANISOU 3245 CZ ARG A 304 25938 22958 18011 1219 -1379 -717 C ATOM 3246 NH1 ARG A 304 12.933 6.806 64.575 1.00158.70 N ANISOU 3246 NH1 ARG A 304 23866 20718 15716 1445 -1298 -576 N ATOM 3247 NH2 ARG A 304 12.989 9.053 64.137 1.00161.99 N ANISOU 3247 NH2 ARG A 304 24225 21061 16264 1056 -1362 -826 N ATOM 3248 N LYS A 305 12.409 6.826 60.407 1.00120.57 N ANISOU 3248 N LYS A 305 18771 15503 11538 1035 -1134 -449 N ATOM 3249 CA LYS A 305 11.342 7.716 59.953 1.00117.55 C ANISOU 3249 CA LYS A 305 18465 14899 11300 887 -1038 -466 C ATOM 3250 C LYS A 305 11.879 8.563 58.816 1.00118.45 C ANISOU 3250 C LYS A 305 18451 15000 11554 672 -1088 -552 C ATOM 3251 O LYS A 305 11.221 8.740 57.790 1.00116.27 O ANISOU 3251 O LYS A 305 18175 14556 11446 585 -1002 -503 O ATOM 3252 CB LYS A 305 10.861 8.599 61.118 1.00120.10 C ANISOU 3252 CB LYS A 305 18927 15196 11509 884 -1039 -555 C ATOM 3253 CG LYS A 305 9.351 8.662 61.270 1.00119.20 C ANISOU 3253 CG LYS A 305 18967 14869 11455 919 -884 -481 C ATOM 3254 CD LYS A 305 8.928 9.971 61.901 1.00119.02 C ANISOU 3254 CD LYS A 305 19052 14781 11390 835 -888 -601 C ATOM 3255 CE LYS A 305 7.443 10.044 62.060 1.00113.03 C ANISOU 3255 CE LYS A 305 18428 13837 10681 885 -736 -534 C ATOM 3256 NZ LYS A 305 6.980 11.450 62.103 1.00115.17 N ANISOU 3256 NZ LYS A 305 18782 13996 10981 769 -724 -643 N ATOM 3257 N GLU A 306 13.118 9.049 59.009 1.00115.02 N ANISOU 3257 N GLU A 306 17903 14761 11037 589 -1226 -683 N ATOM 3258 CA GLU A 306 13.889 9.866 58.076 1.00113.83 C ANISOU 3258 CA GLU A 306 17624 14642 10983 370 -1284 -789 C ATOM 3259 C GLU A 306 14.202 9.073 56.815 1.00111.96 C ANISOU 3259 C GLU A 306 17255 14408 10877 372 -1263 -692 C ATOM 3260 O GLU A 306 14.293 9.678 55.755 1.00111.55 O ANISOU 3260 O GLU A 306 17148 14271 10963 199 -1243 -722 O ATOM 3261 CB GLU A 306 15.195 10.410 58.719 1.00117.77 C ANISOU 3261 CB GLU A 306 18015 15396 11337 289 -1435 -964 C ATOM 3262 CG GLU A 306 15.558 9.860 60.100 1.00133.59 C ANISOU 3262 CG GLU A 306 20038 17605 13117 484 -1517 -982 C ATOM 3263 CD GLU A 306 16.962 9.303 60.293 1.00158.93 C ANISOU 3263 CD GLU A 306 23052 21139 16195 555 -1661 -1041 C ATOM 3264 OE1 GLU A 306 17.603 8.898 59.294 1.00149.54 O ANISOU 3264 OE1 GLU A 306 21704 20018 15095 516 -1681 -1014 O ATOM 3265 OE2 GLU A 306 17.392 9.203 61.466 1.00155.11 O ANISOU 3265 OE2 GLU A 306 22575 20853 15508 675 -1752 -1108 O ATOM 3266 N VAL A 307 14.330 7.733 56.908 1.00104.80 N ANISOU 3266 N VAL A 307 16317 13580 9923 571 -1257 -572 N ATOM 3267 CA VAL A 307 14.605 6.878 55.742 1.00101.81 C ANISOU 3267 CA VAL A 307 15826 13197 9658 593 -1230 -475 C ATOM 3268 C VAL A 307 13.285 6.620 54.996 1.00 99.10 C ANISOU 3268 C VAL A 307 15582 12596 9474 588 -1079 -355 C ATOM 3269 O VAL A 307 13.230 6.874 53.802 1.00 97.95 O ANISOU 3269 O VAL A 307 15369 12367 9481 463 -1048 -346 O ATOM 3270 CB VAL A 307 15.363 5.570 56.110 1.00106.75 C ANISOU 3270 CB VAL A 307 16390 14013 10159 812 -1282 -404 C ATOM 3271 CG1 VAL A 307 15.536 4.657 54.901 1.00104.93 C ANISOU 3271 CG1 VAL A 307 16070 13749 10048 843 -1236 -299 C ATOM 3272 CG2 VAL A 307 16.728 5.886 56.722 1.00108.84 C ANISOU 3272 CG2 VAL A 307 16515 14575 10265 812 -1445 -541 C ATOM 3273 N TYR A 308 12.231 6.167 55.695 1.00 92.64 N ANISOU 3273 N TYR A 308 14917 11666 8616 715 -984 -274 N ATOM 3274 CA TYR A 308 10.897 5.897 55.146 1.00 90.08 C ANISOU 3274 CA TYR A 308 14679 11128 8421 716 -836 -177 C ATOM 3275 C TYR A 308 10.371 7.103 54.349 1.00 92.33 C ANISOU 3275 C TYR A 308 14960 11277 8842 534 -809 -238 C ATOM 3276 O TYR A 308 10.015 6.930 53.179 1.00 90.67 O ANISOU 3276 O TYR A 308 14700 10975 8777 478 -750 -186 O ATOM 3277 CB TYR A 308 9.922 5.517 56.279 1.00 91.49 C ANISOU 3277 CB TYR A 308 15022 11237 8502 852 -748 -123 C ATOM 3278 CG TYR A 308 8.575 4.995 55.819 1.00 91.50 C ANISOU 3278 CG TYR A 308 15094 11058 8614 869 -586 -24 C ATOM 3279 CD1 TYR A 308 8.376 3.640 55.582 1.00 93.39 C ANISOU 3279 CD1 TYR A 308 15350 11269 8866 973 -500 93 C ATOM 3280 CD2 TYR A 308 7.479 5.847 55.692 1.00 91.45 C ANISOU 3280 CD2 TYR A 308 15146 10917 8684 788 -514 -54 C ATOM 3281 CE1 TYR A 308 7.134 3.149 55.185 1.00 94.11 C ANISOU 3281 CE1 TYR A 308 15495 11211 9053 966 -345 164 C ATOM 3282 CE2 TYR A 308 6.230 5.368 55.302 1.00 91.25 C ANISOU 3282 CE2 TYR A 308 15161 10763 8749 804 -370 20 C ATOM 3283 CZ TYR A 308 6.063 4.017 55.048 1.00 99.78 C ANISOU 3283 CZ TYR A 308 16240 11826 9847 879 -285 123 C ATOM 3284 OH TYR A 308 4.842 3.526 54.656 1.00101.18 O ANISOU 3284 OH TYR A 308 16443 11890 10109 871 -137 179 O ATOM 3285 N ILE A 309 10.387 8.317 54.955 1.00 89.56 N ANISOU 3285 N ILE A 309 14672 10920 8438 449 -852 -352 N ATOM 3286 CA ILE A 309 9.942 9.569 54.322 1.00 89.08 C ANISOU 3286 CA ILE A 309 14647 10720 8478 293 -823 -416 C ATOM 3287 C ILE A 309 10.802 9.866 53.073 1.00 90.24 C ANISOU 3287 C ILE A 309 14662 10896 8730 146 -870 -447 C ATOM 3288 O ILE A 309 10.234 10.081 52.010 1.00 89.02 O ANISOU 3288 O ILE A 309 14505 10610 8707 89 -802 -405 O ATOM 3289 CB ILE A 309 9.911 10.770 55.323 1.00 94.25 C ANISOU 3289 CB ILE A 309 15417 11363 9031 236 -858 -540 C ATOM 3290 CG1 ILE A 309 8.772 10.581 56.362 1.00 95.50 C ANISOU 3290 CG1 ILE A 309 15722 11449 9113 377 -778 -497 C ATOM 3291 CG2 ILE A 309 9.768 12.135 54.590 1.00 94.26 C ANISOU 3291 CG2 ILE A 309 15465 11227 9124 61 -837 -620 C ATOM 3292 CD1 ILE A 309 8.677 11.645 57.490 1.00105.97 C ANISOU 3292 CD1 ILE A 309 17179 12767 10320 351 -806 -614 C ATOM 3293 N LEU A 310 12.143 9.843 53.195 1.00 86.66 N ANISOU 3293 N LEU A 310 14092 10625 8210 92 -983 -521 N ATOM 3294 CA LEU A 310 13.083 10.098 52.102 1.00 86.38 C ANISOU 3294 CA LEU A 310 13918 10646 8256 -54 -1027 -563 C ATOM 3295 C LEU A 310 12.815 9.197 50.876 1.00 88.82 C ANISOU 3295 C LEU A 310 14151 10898 8697 -10 -966 -437 C ATOM 3296 O LEU A 310 12.732 9.701 49.753 1.00 88.90 O ANISOU 3296 O LEU A 310 14138 10812 8827 -130 -930 -437 O ATOM 3297 CB LEU A 310 14.527 9.893 52.601 1.00 88.41 C ANISOU 3297 CB LEU A 310 14035 11163 8395 -68 -1158 -652 C ATOM 3298 CG LEU A 310 15.635 9.908 51.540 1.00 94.36 C ANISOU 3298 CG LEU A 310 14609 12028 9215 -197 -1207 -691 C ATOM 3299 CD1 LEU A 310 15.924 11.333 51.043 1.00 95.08 C ANISOU 3299 CD1 LEU A 310 14719 12044 9363 -451 -1201 -817 C ATOM 3300 CD2 LEU A 310 16.880 9.229 52.057 1.00 99.94 C ANISOU 3300 CD2 LEU A 310 15156 13023 9793 -118 -1325 -737 C ATOM 3301 N LEU A 311 12.675 7.874 51.092 1.00 83.61 N ANISOU 3301 N LEU A 311 13470 10291 8007 164 -947 -332 N ATOM 3302 CA LEU A 311 12.423 6.906 50.020 1.00 80.76 C ANISOU 3302 CA LEU A 311 13049 9880 7757 212 -884 -220 C ATOM 3303 C LEU A 311 11.033 7.106 49.448 1.00 80.72 C ANISOU 3303 C LEU A 311 13134 9670 7866 197 -766 -162 C ATOM 3304 O LEU A 311 10.840 6.893 48.263 1.00 80.66 O ANISOU 3304 O LEU A 311 13070 9602 7977 154 -722 -115 O ATOM 3305 CB LEU A 311 12.619 5.456 50.503 1.00 81.02 C ANISOU 3305 CB LEU A 311 13072 10002 7711 404 -879 -130 C ATOM 3306 CG LEU A 311 13.977 5.107 51.167 1.00 86.89 C ANISOU 3306 CG LEU A 311 13722 10982 8310 478 -1001 -178 C ATOM 3307 CD1 LEU A 311 13.986 3.687 51.622 1.00 87.24 C ANISOU 3307 CD1 LEU A 311 13806 11071 8271 696 -970 -70 C ATOM 3308 CD2 LEU A 311 15.167 5.338 50.231 1.00 88.45 C ANISOU 3308 CD2 LEU A 311 13740 11312 8557 364 -1081 -238 C ATOM 3309 N ASN A 312 10.082 7.575 50.265 1.00 75.56 N ANISOU 3309 N ASN A 312 12614 8926 7170 231 -717 -175 N ATOM 3310 CA ASN A 312 8.729 7.864 49.811 1.00 73.10 C ANISOU 3310 CA ASN A 312 12377 8450 6948 229 -610 -136 C ATOM 3311 C ASN A 312 8.768 9.084 48.920 1.00 77.02 C ANISOU 3311 C ASN A 312 12872 8865 7526 87 -619 -195 C ATOM 3312 O ASN A 312 8.057 9.126 47.909 1.00 76.57 O ANISOU 3312 O ASN A 312 12804 8713 7575 73 -552 -150 O ATOM 3313 CB ASN A 312 7.780 8.077 50.998 1.00 68.75 C ANISOU 3313 CB ASN A 312 11963 7844 6314 311 -558 -143 C ATOM 3314 CG ASN A 312 6.319 7.870 50.670 1.00 83.62 C ANISOU 3314 CG ASN A 312 13894 9608 8270 360 -433 -84 C ATOM 3315 OD1 ASN A 312 5.493 7.720 51.562 1.00 69.57 O ANISOU 3315 OD1 ASN A 312 12204 7799 6429 442 -370 -70 O ATOM 3316 ND2 ASN A 312 5.958 7.827 49.387 1.00 78.81 N ANISOU 3316 ND2 ASN A 312 13216 8942 7786 312 -393 -51 N ATOM 3317 N TRP A 313 9.657 10.044 49.250 1.00 73.86 N ANISOU 3317 N TRP A 313 12481 8510 7070 -21 -698 -299 N ATOM 3318 CA TRP A 313 9.839 11.262 48.456 1.00 74.04 C ANISOU 3318 CA TRP A 313 12531 8444 7156 -172 -696 -362 C ATOM 3319 C TRP A 313 10.595 10.978 47.151 1.00 75.12 C ANISOU 3319 C TRP A 313 12534 8622 7386 -257 -714 -337 C ATOM 3320 O TRP A 313 10.382 11.708 46.197 1.00 74.04 O ANISOU 3320 O TRP A 313 12430 8375 7327 -341 -673 -341 O ATOM 3321 CB TRP A 313 10.485 12.381 49.275 1.00 74.70 C ANISOU 3321 CB TRP A 313 12688 8550 7146 -283 -754 -493 C ATOM 3322 CG TRP A 313 9.434 13.151 50.004 1.00 76.25 C ANISOU 3322 CG TRP A 313 13059 8613 7298 -235 -697 -518 C ATOM 3323 CD1 TRP A 313 8.753 12.753 51.119 1.00 79.31 C ANISOU 3323 CD1 TRP A 313 13515 9016 7605 -100 -679 -496 C ATOM 3324 CD2 TRP A 313 8.808 14.364 49.561 1.00 76.11 C ANISOU 3324 CD2 TRP A 313 13181 8417 7322 -296 -633 -549 C ATOM 3325 NE1 TRP A 313 7.770 13.666 51.423 1.00 79.15 N ANISOU 3325 NE1 TRP A 313 13651 8850 7572 -78 -613 -522 N ATOM 3326 CE2 TRP A 313 7.782 14.666 50.484 1.00 80.52 C ANISOU 3326 CE2 TRP A 313 13876 8901 7817 -188 -585 -553 C ATOM 3327 CE3 TRP A 313 9.043 15.248 48.494 1.00 76.77 C ANISOU 3327 CE3 TRP A 313 13300 8392 7476 -425 -604 -574 C ATOM 3328 CZ2 TRP A 313 6.987 15.808 50.365 1.00 80.09 C ANISOU 3328 CZ2 TRP A 313 13987 8675 7767 -190 -515 -582 C ATOM 3329 CZ3 TRP A 313 8.261 16.380 48.382 1.00 78.29 C ANISOU 3329 CZ3 TRP A 313 13675 8403 7671 -426 -531 -597 C ATOM 3330 CH2 TRP A 313 7.254 16.657 49.312 1.00 79.50 C ANISOU 3330 CH2 TRP A 313 13957 8492 7759 -304 -491 -603 C ATOM 3331 N ILE A 314 11.410 9.899 47.083 1.00 71.85 N ANISOU 3331 N ILE A 314 11983 8359 6959 -214 -766 -304 N ATOM 3332 CA ILE A 314 12.058 9.441 45.842 1.00 71.94 C ANISOU 3332 CA ILE A 314 11860 8417 7056 -266 -774 -268 C ATOM 3333 C ILE A 314 10.932 9.054 44.889 1.00 73.80 C ANISOU 3333 C ILE A 314 12119 8521 7400 -208 -680 -171 C ATOM 3334 O ILE A 314 10.936 9.460 43.725 1.00 72.81 O ANISOU 3334 O ILE A 314 11970 8332 7362 -289 -653 -162 O ATOM 3335 CB ILE A 314 13.059 8.248 46.049 1.00 76.31 C ANISOU 3335 CB ILE A 314 12275 9162 7558 -188 -841 -244 C ATOM 3336 CG1 ILE A 314 14.206 8.556 47.080 1.00 78.91 C ANISOU 3336 CG1 ILE A 314 12554 9674 7756 -222 -950 -352 C ATOM 3337 CG2 ILE A 314 13.619 7.742 44.726 1.00 75.80 C ANISOU 3337 CG2 ILE A 314 12079 9134 7586 -228 -837 -201 C ATOM 3338 CD1 ILE A 314 15.143 9.682 46.782 1.00 85.45 C ANISOU 3338 CD1 ILE A 314 13328 10554 8584 -427 -1000 -477 C ATOM 3339 N GLY A 315 9.948 8.325 45.425 1.00 70.23 N ANISOU 3339 N GLY A 315 11719 8032 6931 -73 -625 -108 N ATOM 3340 CA GLY A 315 8.751 7.918 44.694 1.00 69.02 C ANISOU 3340 CA GLY A 315 11581 7779 6865 -17 -531 -34 C ATOM 3341 C GLY A 315 7.934 9.112 44.218 1.00 72.07 C ANISOU 3341 C GLY A 315 12053 8035 7294 -63 -487 -60 C ATOM 3342 O GLY A 315 7.530 9.167 43.049 1.00 69.64 O ANISOU 3342 O GLY A 315 11712 7674 7072 -80 -447 -27 O ATOM 3343 N TYR A 316 7.702 10.096 45.125 1.00 69.03 N ANISOU 3343 N TYR A 316 11789 7601 6840 -74 -494 -123 N ATOM 3344 CA TYR A 316 6.955 11.328 44.838 1.00 68.16 C ANISOU 3344 CA TYR A 316 11795 7358 6745 -95 -449 -153 C ATOM 3345 C TYR A 316 7.534 12.112 43.657 1.00 72.44 C ANISOU 3345 C TYR A 316 12333 7846 7347 -213 -457 -172 C ATOM 3346 O TYR A 316 6.815 12.465 42.727 1.00 71.38 O ANISOU 3346 O TYR A 316 12228 7624 7268 -186 -402 -137 O ATOM 3347 CB TYR A 316 6.947 12.226 46.074 1.00 70.01 C ANISOU 3347 CB TYR A 316 12163 7558 6879 -105 -467 -232 C ATOM 3348 CG TYR A 316 5.995 11.816 47.174 1.00 71.26 C ANISOU 3348 CG TYR A 316 12378 7722 6975 24 -427 -214 C ATOM 3349 CD1 TYR A 316 4.975 10.894 46.939 1.00 72.42 C ANISOU 3349 CD1 TYR A 316 12476 7875 7166 130 -356 -137 C ATOM 3350 CD2 TYR A 316 6.069 12.400 48.434 1.00 72.86 C ANISOU 3350 CD2 TYR A 316 12689 7922 7073 30 -450 -282 C ATOM 3351 CE1 TYR A 316 4.074 10.544 47.945 1.00 73.80 C ANISOU 3351 CE1 TYR A 316 12706 8053 7282 234 -302 -125 C ATOM 3352 CE2 TYR A 316 5.168 12.069 49.439 1.00 73.55 C ANISOU 3352 CE2 TYR A 316 12838 8011 7098 149 -403 -265 C ATOM 3353 CZ TYR A 316 4.175 11.140 49.193 1.00 77.54 C ANISOU 3353 CZ TYR A 316 13291 8521 7649 249 -326 -185 C ATOM 3354 OH TYR A 316 3.296 10.841 50.195 1.00 73.11 O ANISOU 3354 OH TYR A 316 12792 7963 7024 351 -266 -174 O ATOM 3355 N VAL A 317 8.843 12.358 43.688 1.00 71.20 N ANISOU 3355 N VAL A 317 12132 7752 7168 -341 -522 -229 N ATOM 3356 CA VAL A 317 9.602 13.112 42.697 1.00 71.64 C ANISOU 3356 CA VAL A 317 12187 7768 7267 -485 -525 -260 C ATOM 3357 C VAL A 317 9.445 12.454 41.287 1.00 76.86 C ANISOU 3357 C VAL A 317 12744 8432 8026 -458 -495 -175 C ATOM 3358 O VAL A 317 9.658 13.132 40.270 1.00 77.65 O ANISOU 3358 O VAL A 317 12877 8459 8170 -540 -466 -176 O ATOM 3359 CB VAL A 317 11.059 13.204 43.243 1.00 76.72 C ANISOU 3359 CB VAL A 317 12757 8539 7854 -620 -608 -350 C ATOM 3360 CG1 VAL A 317 12.135 12.808 42.241 1.00 76.56 C ANISOU 3360 CG1 VAL A 317 12585 8616 7888 -717 -636 -343 C ATOM 3361 CG2 VAL A 317 11.330 14.565 43.860 1.00 77.85 C ANISOU 3361 CG2 VAL A 317 13046 8603 7931 -744 -606 -462 C ATOM 3362 N ASN A 318 8.984 11.170 41.234 1.00 72.55 N ANISOU 3362 N ASN A 318 12098 7959 7509 -341 -488 -103 N ATOM 3363 CA ASN A 318 8.732 10.454 39.983 1.00 70.93 C ANISOU 3363 CA ASN A 318 11798 7763 7390 -309 -457 -31 C ATOM 3364 C ASN A 318 7.544 11.057 39.220 1.00 75.52 C ANISOU 3364 C ASN A 318 12460 8227 8008 -252 -387 -2 C ATOM 3365 O ASN A 318 7.544 10.994 37.995 1.00 76.90 O ANISOU 3365 O ASN A 318 12588 8389 8242 -266 -367 34 O ATOM 3366 CB ASN A 318 8.511 8.958 40.187 1.00 67.45 C ANISOU 3366 CB ASN A 318 11255 7411 6961 -211 -452 25 C ATOM 3367 CG ASN A 318 8.311 8.234 38.869 1.00 82.96 C ANISOU 3367 CG ASN A 318 13125 9385 9010 -195 -419 84 C ATOM 3368 OD1 ASN A 318 9.263 8.014 38.123 1.00 78.37 O ANISOU 3368 OD1 ASN A 318 12458 8857 8461 -260 -449 90 O ATOM 3369 ND2 ASN A 318 7.062 7.971 38.486 1.00 66.25 N ANISOU 3369 ND2 ASN A 318 11019 7223 6928 -116 -354 119 N ATOM 3370 N SER A 319 6.556 11.646 39.912 1.00 70.73 N ANISOU 3370 N SER A 319 11969 7547 7357 -177 -352 -18 N ATOM 3371 CA SER A 319 5.411 12.282 39.259 1.00 70.07 C ANISOU 3371 CA SER A 319 11962 7373 7288 -94 -291 3 C ATOM 3372 C SER A 319 5.834 13.476 38.384 1.00 75.34 C ANISOU 3372 C SER A 319 12732 7934 7960 -168 -278 -10 C ATOM 3373 O SER A 319 5.091 13.874 37.487 1.00 74.54 O ANISOU 3373 O SER A 319 12673 7775 7875 -93 -233 24 O ATOM 3374 CB SER A 319 4.401 12.745 40.295 1.00 73.68 C ANISOU 3374 CB SER A 319 12527 7784 7682 4 -258 -22 C ATOM 3375 OG SER A 319 3.674 11.637 40.781 1.00 83.00 O ANISOU 3375 OG SER A 319 13619 9049 8868 90 -236 5 O ATOM 3376 N GLY A 320 7.010 14.033 38.656 1.00 73.39 N ANISOU 3376 N GLY A 320 12526 7667 7690 -314 -312 -63 N ATOM 3377 CA GLY A 320 7.535 15.148 37.885 1.00 74.66 C ANISOU 3377 CA GLY A 320 12800 7716 7851 -418 -282 -83 C ATOM 3378 C GLY A 320 8.343 14.735 36.672 1.00 79.90 C ANISOU 3378 C GLY A 320 13350 8431 8579 -503 -290 -50 C ATOM 3379 O GLY A 320 8.573 15.556 35.783 1.00 80.37 O ANISOU 3379 O GLY A 320 13504 8391 8644 -565 -246 -44 O ATOM 3380 N PHE A 321 8.742 13.450 36.603 1.00 77.28 N ANISOU 3380 N PHE A 321 12828 8247 8288 -497 -337 -24 N ATOM 3381 CA PHE A 321 9.621 12.911 35.562 1.00 77.31 C ANISOU 3381 CA PHE A 321 12703 8324 8346 -575 -352 2 C ATOM 3382 C PHE A 321 8.948 12.603 34.234 1.00 80.05 C ANISOU 3382 C PHE A 321 13018 8651 8747 -491 -310 75 C ATOM 3383 O PHE A 321 9.539 12.935 33.207 1.00 77.83 O ANISOU 3383 O PHE A 321 12737 8346 8490 -570 -291 87 O ATOM 3384 CB PHE A 321 10.360 11.646 36.050 1.00 78.91 C ANISOU 3384 CB PHE A 321 12730 8692 8558 -581 -416 -1 C ATOM 3385 CG PHE A 321 11.400 11.861 37.135 1.00 81.93 C ANISOU 3385 CG PHE A 321 13097 9149 8882 -682 -475 -81 C ATOM 3386 CD1 PHE A 321 11.751 13.142 37.550 1.00 86.64 C ANISOU 3386 CD1 PHE A 321 13824 9665 9432 -802 -466 -159 C ATOM 3387 CD2 PHE A 321 12.037 10.782 37.730 1.00 84.56 C ANISOU 3387 CD2 PHE A 321 13294 9639 9197 -652 -537 -84 C ATOM 3388 CE1 PHE A 321 12.674 13.331 38.579 1.00 88.94 C ANISOU 3388 CE1 PHE A 321 14087 10048 9659 -900 -525 -250 C ATOM 3389 CE2 PHE A 321 12.981 10.975 38.740 1.00 88.51 C ANISOU 3389 CE2 PHE A 321 13765 10238 9625 -726 -601 -165 C ATOM 3390 CZ PHE A 321 13.294 12.246 39.154 1.00 87.72 C ANISOU 3390 CZ PHE A 321 13774 10074 9481 -857 -598 -254 C ATOM 3391 N ASN A 322 7.753 11.962 34.222 1.00 78.54 N ANISOU 3391 N ASN A 322 12792 8481 8568 -341 -294 115 N ATOM 3392 CA ASN A 322 7.116 11.559 32.945 1.00 78.57 C ANISOU 3392 CA ASN A 322 12738 8501 8616 -262 -263 171 C ATOM 3393 C ASN A 322 6.976 12.677 31.924 1.00 79.86 C ANISOU 3393 C ASN A 322 13024 8555 8763 -260 -219 189 C ATOM 3394 O ASN A 322 7.335 12.415 30.782 1.00 78.89 O ANISOU 3394 O ASN A 322 12840 8459 8676 -285 -211 222 O ATOM 3395 CB ASN A 322 5.769 10.877 33.124 1.00 83.52 C ANISOU 3395 CB ASN A 322 13315 9172 9247 -118 -242 189 C ATOM 3396 CG ASN A 322 5.883 9.481 33.639 1.00 94.39 C ANISOU 3396 CG ASN A 322 14559 10655 10652 -116 -261 193 C ATOM 3397 OD1 ASN A 322 6.889 9.101 34.253 1.00 77.34 O ANISOU 3397 OD1 ASN A 322 12363 8534 8488 -190 -300 179 O ATOM 3398 ND2 ASN A 322 4.799 8.741 33.506 1.00 88.98 N ANISOU 3398 ND2 ASN A 322 13809 10016 9983 -24 -227 206 N ATOM 3399 N PRO A 323 6.546 13.915 32.269 1.00 77.08 N ANISOU 3399 N PRO A 323 12859 8074 8353 -230 -184 170 N ATOM 3400 CA PRO A 323 6.465 14.964 31.238 1.00 77.40 C ANISOU 3400 CA PRO A 323 13047 7995 8368 -215 -129 198 C ATOM 3401 C PRO A 323 7.787 15.172 30.484 1.00 81.47 C ANISOU 3401 C PRO A 323 13557 8490 8909 -388 -119 198 C ATOM 3402 O PRO A 323 7.747 15.295 29.258 1.00 82.20 O ANISOU 3402 O PRO A 323 13664 8560 9008 -359 -86 246 O ATOM 3403 CB PRO A 323 6.046 16.192 32.037 1.00 79.89 C ANISOU 3403 CB PRO A 323 13578 8166 8610 -182 -91 165 C ATOM 3404 CG PRO A 323 5.279 15.616 33.181 1.00 83.34 C ANISOU 3404 CG PRO A 323 13947 8680 9039 -91 -123 142 C ATOM 3405 CD PRO A 323 6.055 14.426 33.568 1.00 78.23 C ANISOU 3405 CD PRO A 323 13110 8167 8445 -190 -182 128 C ATOM 3406 N LEU A 324 8.942 15.110 31.178 1.00 77.79 N ANISOU 3406 N LEU A 324 13047 8057 8453 -558 -151 142 N ATOM 3407 CA LEU A 324 10.262 15.237 30.549 1.00 78.72 C ANISOU 3407 CA LEU A 324 13127 8191 8594 -738 -142 125 C ATOM 3408 C LEU A 324 10.566 14.086 29.590 1.00 81.38 C ANISOU 3408 C LEU A 324 13269 8662 8992 -720 -168 173 C ATOM 3409 O LEU A 324 11.193 14.311 28.553 1.00 81.25 O ANISOU 3409 O LEU A 324 13254 8628 8989 -800 -132 192 O ATOM 3410 CB LEU A 324 11.376 15.322 31.597 1.00 79.85 C ANISOU 3410 CB LEU A 324 13226 8389 8723 -909 -184 38 C ATOM 3411 CG LEU A 324 11.583 16.697 32.181 1.00 87.05 C ANISOU 3411 CG LEU A 324 14349 9149 9576 -1021 -135 -30 C ATOM 3412 CD1 LEU A 324 12.048 16.616 33.613 1.00 87.84 C ANISOU 3412 CD1 LEU A 324 14406 9325 9644 -1096 -197 -119 C ATOM 3413 CD2 LEU A 324 12.511 17.533 31.311 1.00 92.24 C ANISOU 3413 CD2 LEU A 324 15094 9721 10231 -1205 -63 -50 C ATOM 3414 N ILE A 325 10.129 12.862 29.936 1.00 76.81 N ANISOU 3414 N ILE A 325 12535 8205 8444 -619 -220 189 N ATOM 3415 CA ILE A 325 10.345 11.659 29.130 1.00 75.54 C ANISOU 3415 CA ILE A 325 12199 8166 8338 -592 -241 228 C ATOM 3416 C ILE A 325 9.493 11.743 27.836 1.00 83.92 C ANISOU 3416 C ILE A 325 13292 9188 9405 -485 -197 286 C ATOM 3417 O ILE A 325 9.917 11.223 26.797 1.00 85.03 O ANISOU 3417 O ILE A 325 13342 9387 9579 -505 -192 315 O ATOM 3418 CB ILE A 325 10.078 10.360 29.954 1.00 76.00 C ANISOU 3418 CB ILE A 325 12122 8339 8415 -518 -290 225 C ATOM 3419 CG1 ILE A 325 10.938 10.333 31.236 1.00 76.07 C ANISOU 3419 CG1 ILE A 325 12110 8399 8396 -601 -338 169 C ATOM 3420 CG2 ILE A 325 10.341 9.102 29.122 1.00 73.88 C ANISOU 3420 CG2 ILE A 325 11695 8177 8198 -494 -300 260 C ATOM 3421 CD1 ILE A 325 10.366 9.526 32.387 1.00 78.94 C ANISOU 3421 CD1 ILE A 325 12438 8812 8743 -504 -366 166 C ATOM 3422 N TYR A 326 8.337 12.443 27.877 1.00 81.06 N ANISOU 3422 N TYR A 326 13059 8738 9000 -364 -166 300 N ATOM 3423 CA TYR A 326 7.462 12.581 26.712 1.00 80.60 C ANISOU 3423 CA TYR A 326 13031 8668 8928 -235 -133 348 C ATOM 3424 C TYR A 326 8.068 13.495 25.669 1.00 85.48 C ANISOU 3424 C TYR A 326 13770 9188 9519 -296 -81 377 C ATOM 3425 O TYR A 326 7.629 13.481 24.532 1.00 84.72 O ANISOU 3425 O TYR A 326 13678 9103 9409 -204 -59 422 O ATOM 3426 CB TYR A 326 6.062 13.056 27.125 1.00 82.37 C ANISOU 3426 CB TYR A 326 13346 8853 9100 -68 -118 347 C ATOM 3427 CG TYR A 326 5.377 12.046 28.015 1.00 83.96 C ANISOU 3427 CG TYR A 326 13414 9159 9326 -11 -153 320 C ATOM 3428 CD1 TYR A 326 5.476 10.682 27.757 1.00 84.55 C ANISOU 3428 CD1 TYR A 326 13304 9360 9459 -28 -178 321 C ATOM 3429 CD2 TYR A 326 4.671 12.447 29.142 1.00 86.12 C ANISOU 3429 CD2 TYR A 326 13763 9397 9562 53 -150 291 C ATOM 3430 CE1 TYR A 326 4.866 9.743 28.581 1.00 84.17 C ANISOU 3430 CE1 TYR A 326 13160 9390 9430 11 -190 297 C ATOM 3431 CE2 TYR A 326 4.090 11.513 29.999 1.00 87.24 C ANISOU 3431 CE2 TYR A 326 13795 9630 9723 91 -167 266 C ATOM 3432 CZ TYR A 326 4.205 10.159 29.718 1.00 92.23 C ANISOU 3432 CZ TYR A 326 14254 10376 10412 64 -183 271 C ATOM 3433 OH TYR A 326 3.635 9.218 30.527 1.00 91.31 O ANISOU 3433 OH TYR A 326 14052 10332 10310 91 -181 250 O ATOM 3434 N CYS A 327 9.121 14.234 26.029 1.00 83.59 N ANISOU 3434 N CYS A 327 13622 8865 9271 -461 -58 347 N ATOM 3435 CA CYS A 327 9.817 15.112 25.106 1.00 84.02 C ANISOU 3435 CA CYS A 327 13805 8816 9301 -557 11 368 C ATOM 3436 C CYS A 327 10.602 14.294 24.086 1.00 87.69 C ANISOU 3436 C CYS A 327 14110 9393 9816 -624 2 392 C ATOM 3437 O CYS A 327 10.939 14.814 23.022 1.00 88.85 O ANISOU 3437 O CYS A 327 14343 9476 9941 -658 64 428 O ATOM 3438 CB CYS A 327 10.703 16.091 25.860 1.00 85.49 C ANISOU 3438 CB CYS A 327 14125 8894 9465 -741 46 309 C ATOM 3439 SG CYS A 327 9.778 17.427 26.658 1.00 90.51 S ANISOU 3439 SG CYS A 327 15038 9333 10018 -653 96 295 S ATOM 3440 N ARG A 328 10.815 12.994 24.374 1.00 82.40 N ANISOU 3440 N ARG A 328 13222 8882 9204 -624 -67 376 N ATOM 3441 CA ARG A 328 11.464 12.052 23.468 1.00 81.51 C ANISOU 3441 CA ARG A 328 12946 8887 9137 -659 -80 396 C ATOM 3442 C ARG A 328 10.613 11.871 22.208 1.00 85.48 C ANISOU 3442 C ARG A 328 13458 9393 9625 -516 -56 454 C ATOM 3443 O ARG A 328 11.160 11.769 21.111 1.00 86.69 O ANISOU 3443 O ARG A 328 13584 9569 9784 -554 -27 483 O ATOM 3444 CB ARG A 328 11.679 10.708 24.160 1.00 78.59 C ANISOU 3444 CB ARG A 328 12381 8663 8817 -650 -150 370 C ATOM 3445 CG ARG A 328 12.851 10.702 25.126 1.00 79.60 C ANISOU 3445 CG ARG A 328 12452 8841 8952 -794 -182 313 C ATOM 3446 CD ARG A 328 13.042 9.340 25.745 1.00 77.83 C ANISOU 3446 CD ARG A 328 12057 8756 8760 -749 -245 301 C ATOM 3447 NE ARG A 328 12.728 8.279 24.791 1.00 80.47 N ANISOU 3447 NE ARG A 328 12289 9157 9130 -661 -242 344 N ATOM 3448 CZ ARG A 328 13.628 7.613 24.075 1.00 91.39 C ANISOU 3448 CZ ARG A 328 13553 10632 10539 -704 -244 352 C ATOM 3449 NH1 ARG A 328 14.929 7.871 24.218 1.00 67.33 N ANISOU 3449 NH1 ARG A 328 10453 7643 7485 -834 -252 318 N ATOM 3450 NH2 ARG A 328 13.239 6.677 23.218 1.00 76.32 N ANISOU 3450 NH2 ARG A 328 11570 8770 8658 -621 -236 385 N ATOM 3451 N SER A 329 9.275 11.868 22.374 1.00 80.01 N ANISOU 3451 N SER A 329 12802 8693 8906 -349 -68 465 N ATOM 3452 CA SER A 329 8.316 11.760 21.283 1.00 79.13 C ANISOU 3452 CA SER A 329 12693 8610 8762 -192 -55 505 C ATOM 3453 C SER A 329 8.256 13.085 20.504 1.00 85.26 C ANISOU 3453 C SER A 329 13683 9249 9461 -155 14 550 C ATOM 3454 O SER A 329 8.023 14.148 21.107 1.00 86.78 O ANISOU 3454 O SER A 329 14058 9311 9605 -141 47 547 O ATOM 3455 CB SER A 329 6.936 11.378 21.813 1.00 81.71 C ANISOU 3455 CB SER A 329 12975 8996 9077 -37 -87 485 C ATOM 3456 OG SER A 329 5.981 11.351 20.763 1.00 95.42 O ANISOU 3456 OG SER A 329 14702 10786 10767 119 -80 508 O ATOM 3457 N PRO A 330 8.480 13.057 19.168 1.00 81.34 N ANISOU 3457 N PRO A 330 13191 8772 8945 -134 45 594 N ATOM 3458 CA PRO A 330 8.419 14.312 18.387 1.00 81.61 C ANISOU 3458 CA PRO A 330 13456 8662 8890 -83 125 648 C ATOM 3459 C PRO A 330 7.004 14.892 18.358 1.00 84.77 C ANISOU 3459 C PRO A 330 13975 9032 9203 152 126 670 C ATOM 3460 O PRO A 330 6.843 16.109 18.281 1.00 84.85 O ANISOU 3460 O PRO A 330 14226 8882 9130 207 193 705 O ATOM 3461 CB PRO A 330 8.883 13.888 16.988 1.00 83.00 C ANISOU 3461 CB PRO A 330 13570 8903 9063 -92 145 688 C ATOM 3462 CG PRO A 330 9.514 12.534 17.170 1.00 86.43 C ANISOU 3462 CG PRO A 330 13753 9489 9596 -200 85 647 C ATOM 3463 CD PRO A 330 8.781 11.902 18.296 1.00 81.53 C ANISOU 3463 CD PRO A 330 13027 8936 9013 -145 18 599 C ATOM 3464 N ASP A 331 5.985 14.014 18.467 1.00 80.36 N ANISOU 3464 N ASP A 331 13246 8629 8657 287 58 643 N ATOM 3465 CA ASP A 331 4.572 14.385 18.489 1.00 80.75 C ANISOU 3465 CA ASP A 331 13347 8710 8626 519 45 645 C ATOM 3466 C ASP A 331 4.231 15.192 19.752 1.00 83.86 C ANISOU 3466 C ASP A 331 13880 8987 8997 538 60 625 C ATOM 3467 O ASP A 331 3.462 16.162 19.677 1.00 84.65 O ANISOU 3467 O ASP A 331 14157 9009 8996 712 94 652 O ATOM 3468 CB ASP A 331 3.709 13.123 18.402 1.00 81.89 C ANISOU 3468 CB ASP A 331 13242 9068 8805 599 -24 597 C ATOM 3469 CG ASP A 331 3.695 12.475 17.034 1.00 95.21 C ANISOU 3469 CG ASP A 331 14818 10877 10479 643 -36 611 C ATOM 3470 OD1 ASP A 331 3.524 13.206 16.029 1.00 96.79 O ANISOU 3470 OD1 ASP A 331 15149 11042 10584 765 -3 664 O ATOM 3471 OD2 ASP A 331 3.812 11.233 16.968 1.00102.92 O ANISOU 3471 OD2 ASP A 331 15589 11983 11532 566 -75 568 O ATOM 3472 N PHE A 332 4.826 14.794 20.901 1.00 77.25 N ANISOU 3472 N PHE A 332 12970 8140 8242 370 36 577 N ATOM 3473 CA PHE A 332 4.665 15.457 22.186 1.00 76.61 C ANISOU 3473 CA PHE A 332 13006 7954 8147 354 45 547 C ATOM 3474 C PHE A 332 5.483 16.740 22.215 1.00 83.43 C ANISOU 3474 C PHE A 332 14125 8606 8968 251 123 569 C ATOM 3475 O PHE A 332 4.941 17.785 22.602 1.00 84.61 O ANISOU 3475 O PHE A 332 14484 8624 9040 352 167 577 O ATOM 3476 CB PHE A 332 5.060 14.536 23.337 1.00 76.61 C ANISOU 3476 CB PHE A 332 12840 8032 8237 218 -9 489 C ATOM 3477 CG PHE A 332 3.921 13.754 23.929 1.00 76.85 C ANISOU 3477 CG PHE A 332 12726 8195 8279 337 -54 454 C ATOM 3478 CD1 PHE A 332 2.923 14.390 24.658 1.00 80.30 C ANISOU 3478 CD1 PHE A 332 13259 8596 8656 473 -43 438 C ATOM 3479 CD2 PHE A 332 3.854 12.380 23.782 1.00 78.90 C ANISOU 3479 CD2 PHE A 332 12762 8612 8606 307 -95 432 C ATOM 3480 CE1 PHE A 332 1.873 13.665 25.221 1.00 81.22 C ANISOU 3480 CE1 PHE A 332 13232 8845 8781 567 -73 397 C ATOM 3481 CE2 PHE A 332 2.803 11.649 24.349 1.00 81.76 C ANISOU 3481 CE2 PHE A 332 12999 9088 8978 392 -118 391 C ATOM 3482 CZ PHE A 332 1.825 12.295 25.073 1.00 80.45 C ANISOU 3482 CZ PHE A 332 12914 8898 8754 515 -106 372 C ATOM 3483 N ARG A 333 6.769 16.681 21.755 1.00 79.18 N ANISOU 3483 N ARG A 333 13577 8035 8474 52 150 575 N ATOM 3484 CA ARG A 333 7.666 17.839 21.636 1.00 79.62 C ANISOU 3484 CA ARG A 333 13863 7896 8492 -90 241 586 C ATOM 3485 C ARG A 333 6.985 18.981 20.840 1.00 85.06 C ANISOU 3485 C ARG A 333 14824 8433 9063 89 326 654 C ATOM 3486 O ARG A 333 7.073 20.136 21.246 1.00 88.53 O ANISOU 3486 O ARG A 333 15520 8675 9442 63 404 653 O ATOM 3487 CB ARG A 333 8.970 17.424 20.942 1.00 78.99 C ANISOU 3487 CB ARG A 333 13685 7859 8470 -292 259 587 C ATOM 3488 CG ARG A 333 10.234 17.843 21.668 1.00 87.98 C ANISOU 3488 CG ARG A 333 14861 8926 9643 -558 291 525 C ATOM 3489 CD ARG A 333 11.494 17.536 20.876 1.00 98.07 C ANISOU 3489 CD ARG A 333 16045 10256 10962 -745 321 525 C ATOM 3490 NE ARG A 333 11.664 16.100 20.647 1.00112.95 N ANISOU 3490 NE ARG A 333 17640 12356 12921 -727 231 521 N ATOM 3491 CZ ARG A 333 11.716 15.522 19.451 1.00135.89 C ANISOU 3491 CZ ARG A 333 20456 15342 15834 -673 235 570 C ATOM 3492 NH1 ARG A 333 11.650 16.258 18.346 1.00126.17 N ANISOU 3492 NH1 ARG A 333 19397 14004 14537 -631 322 631 N ATOM 3493 NH2 ARG A 333 11.850 14.206 19.349 1.00128.36 N ANISOU 3493 NH2 ARG A 333 19257 14568 14945 -657 159 558 N ATOM 3494 N ILE A 334 6.260 18.649 19.747 1.00 78.74 N ANISOU 3494 N ILE A 334 13973 7727 8218 286 311 710 N ATOM 3495 CA ILE A 334 5.545 19.617 18.915 1.00 78.84 C ANISOU 3495 CA ILE A 334 14225 7630 8099 504 381 782 C ATOM 3496 C ILE A 334 4.351 20.193 19.686 1.00 80.14 C ANISOU 3496 C ILE A 334 14502 7757 8191 718 372 772 C ATOM 3497 O ILE A 334 4.127 21.408 19.629 1.00 82.77 O ANISOU 3497 O ILE A 334 15136 7895 8418 818 460 812 O ATOM 3498 CB ILE A 334 5.131 19.003 17.536 1.00 81.65 C ANISOU 3498 CB ILE A 334 14463 8139 8421 658 352 831 C ATOM 3499 CG1 ILE A 334 6.340 19.013 16.573 1.00 82.30 C ANISOU 3499 CG1 ILE A 334 14580 8167 8524 481 416 869 C ATOM 3500 CG2 ILE A 334 3.916 19.733 16.890 1.00 82.95 C ANISOU 3500 CG2 ILE A 334 14799 8285 8434 984 377 891 C ATOM 3501 CD1 ILE A 334 6.310 17.907 15.497 1.00 92.76 C ANISOU 3501 CD1 ILE A 334 15673 9695 9875 525 358 881 C ATOM 3502 N ALA A 335 3.581 19.338 20.380 1.00 71.71 N ANISOU 3502 N ALA A 335 13206 6869 7170 792 276 719 N ATOM 3503 CA ALA A 335 2.415 19.792 21.142 1.00 71.04 C ANISOU 3503 CA ALA A 335 13193 6782 7019 996 265 701 C ATOM 3504 C ALA A 335 2.838 20.793 22.267 1.00 77.23 C ANISOU 3504 C ALA A 335 14210 7344 7790 885 327 675 C ATOM 3505 O ALA A 335 2.244 21.866 22.409 1.00 77.06 O ANISOU 3505 O ALA A 335 14441 7178 7660 1053 389 700 O ATOM 3506 CB ALA A 335 1.699 18.597 21.726 1.00 69.46 C ANISOU 3506 CB ALA A 335 12691 6814 6887 1031 167 639 C ATOM 3507 N PHE A 336 3.912 20.447 23.008 1.00 73.89 N ANISOU 3507 N PHE A 336 13709 6896 7470 606 313 621 N ATOM 3508 CA PHE A 336 4.453 21.241 24.098 1.00 73.89 C ANISOU 3508 CA PHE A 336 13886 6720 7468 456 359 574 C ATOM 3509 C PHE A 336 4.892 22.596 23.613 1.00 82.65 C ANISOU 3509 C PHE A 336 15341 7571 8490 426 487 614 C ATOM 3510 O PHE A 336 4.487 23.581 24.230 1.00 85.89 O ANISOU 3510 O PHE A 336 15994 7814 8824 503 546 605 O ATOM 3511 CB PHE A 336 5.610 20.524 24.816 1.00 73.92 C ANISOU 3511 CB PHE A 336 13708 6791 7587 167 311 506 C ATOM 3512 CG PHE A 336 5.293 19.222 25.520 1.00 72.39 C ANISOU 3512 CG PHE A 336 13217 6814 7475 174 202 463 C ATOM 3513 CD1 PHE A 336 3.986 18.898 25.872 1.00 73.88 C ANISOU 3513 CD1 PHE A 336 13332 7103 7636 391 160 462 C ATOM 3514 CD2 PHE A 336 6.310 18.345 25.880 1.00 73.48 C ANISOU 3514 CD2 PHE A 336 13158 7053 7706 -36 149 421 C ATOM 3515 CE1 PHE A 336 3.697 17.697 26.525 1.00 73.46 C ANISOU 3515 CE1 PHE A 336 13027 7231 7654 380 81 422 C ATOM 3516 CE2 PHE A 336 6.022 17.141 26.529 1.00 74.40 C ANISOU 3516 CE2 PHE A 336 13034 7347 7886 -20 65 390 C ATOM 3517 CZ PHE A 336 4.716 16.823 26.841 1.00 71.91 C ANISOU 3517 CZ PHE A 336 12664 7110 7547 178 37 391 C ATOM 3518 N AGLN A 337 5.686 22.681 22.512 0.50 79.45 N ANISOU 3518 N AGLN A 337 14980 7119 8087 321 543 660 N ATOM 3519 N BGLN A 337 5.665 22.664 22.508 0.50 79.33 N ANISOU 3519 N BGLN A 337 14961 7108 8072 326 541 660 N ATOM 3520 CA AGLN A 337 6.148 23.975 21.972 0.50 81.17 C ANISOU 3520 CA AGLN A 337 15553 7070 8215 275 690 703 C ATOM 3521 CA BGLN A 337 6.135 23.924 21.908 0.50 80.97 C ANISOU 3521 CA BGLN A 337 15517 7056 8192 282 687 706 C ATOM 3522 C AGLN A 337 4.956 24.844 21.522 0.50 85.01 C ANISOU 3522 C AGLN A 337 16300 7445 8554 612 748 779 C ATOM 3523 C BGLN A 337 4.957 24.823 21.531 0.50 84.93 C ANISOU 3523 C BGLN A 337 16283 7439 8546 610 746 778 C ATOM 3524 O AGLN A 337 5.019 26.065 21.655 0.50 86.65 O ANISOU 3524 O AGLN A 337 16857 7395 8672 621 870 796 O ATOM 3525 O BGLN A 337 5.031 26.038 21.711 0.50 86.57 O ANISOU 3525 O BGLN A 337 16837 7390 8666 613 866 791 O ATOM 3526 CB AGLN A 337 7.198 23.817 20.839 0.50 82.84 C ANISOU 3526 CB AGLN A 337 15745 7274 8455 102 744 739 C ATOM 3527 CB BGLN A 337 7.005 23.654 20.665 0.50 82.38 C ANISOU 3527 CB BGLN A 337 15652 7257 8394 157 728 752 C ATOM 3528 CG AGLN A 337 6.697 23.222 19.524 0.50 97.02 C ANISOU 3528 CG AGLN A 337 17428 9214 10221 301 711 820 C ATOM 3529 CG BGLN A 337 8.346 23.011 20.984 0.50 94.14 C ANISOU 3529 CG BGLN A 337 16934 8828 10006 -179 699 680 C ATOM 3530 CD AGLN A 337 7.761 23.169 18.459 0.50110.63 C ANISOU 3530 CD AGLN A 337 19163 10909 11963 127 780 855 C ATOM 3531 CD BGLN A 337 9.198 22.791 19.766 0.50115.06 C ANISOU 3531 CD BGLN A 337 19546 11500 12672 -296 749 722 C ATOM 3532 OE1AGLN A 337 8.498 22.183 18.332 0.50105.33 O ANISOU 3532 OE1AGLN A 337 18221 10404 11397 -44 716 820 O ATOM 3533 OE1BGLN A 337 9.762 23.732 19.195 0.50113.94 O ANISOU 3533 OE1BGLN A 337 19663 11159 12469 -396 887 753 O ATOM 3534 NE2AGLN A 337 7.840 24.218 17.647 0.50 97.86 N ANISOU 3534 NE2AGLN A 337 17869 9081 10234 181 918 928 N ATOM 3535 NE2BGLN A 337 9.335 21.539 19.358 0.50103.99 N ANISOU 3535 NE2BGLN A 337 17831 10332 11349 -297 650 722 N ATOM 3536 N GLU A 338 3.864 24.210 21.049 1.00 79.86 N ANISOU 3536 N GLU A 338 15478 6995 7872 888 663 816 N ATOM 3537 CA GLU A 338 2.641 24.895 20.638 1.00 80.96 C ANISOU 3537 CA GLU A 338 15804 7096 7861 1248 694 879 C ATOM 3538 C GLU A 338 1.889 25.457 21.858 1.00 85.20 C ANISOU 3538 C GLU A 338 16454 7562 8355 1366 694 835 C ATOM 3539 O GLU A 338 1.548 26.637 21.864 1.00 86.81 O ANISOU 3539 O GLU A 338 17002 7551 8433 1519 797 875 O ATOM 3540 CB GLU A 338 1.741 23.934 19.830 1.00 81.44 C ANISOU 3540 CB GLU A 338 15590 7444 7909 1477 589 903 C ATOM 3541 CG GLU A 338 0.495 24.590 19.248 1.00 96.05 C ANISOU 3541 CG GLU A 338 17601 9306 9587 1873 610 967 C ATOM 3542 CD GLU A 338 0.752 25.647 18.194 1.00122.75 C ANISOU 3542 CD GLU A 338 21338 12470 12831 1982 738 1069 C ATOM 3543 OE1 GLU A 338 1.625 25.419 17.323 1.00104.53 O ANISOU 3543 OE1 GLU A 338 19020 10138 10558 1821 772 1104 O ATOM 3544 OE2 GLU A 338 0.091 26.711 18.253 1.00121.88 O ANISOU 3544 OE2 GLU A 338 21529 12207 12574 2232 813 1115 O ATOM 3545 N LEU A 339 1.634 24.613 22.879 1.00 80.86 N ANISOU 3545 N LEU A 339 15633 7188 7902 1302 589 755 N ATOM 3546 CA LEU A 339 0.921 25.008 24.100 1.00 81.25 C ANISOU 3546 CA LEU A 339 15750 7201 7919 1403 581 706 C ATOM 3547 C LEU A 339 1.683 26.054 24.918 1.00 87.05 C ANISOU 3547 C LEU A 339 16783 7651 8640 1213 680 670 C ATOM 3548 O LEU A 339 1.058 26.938 25.501 1.00 87.29 O ANISOU 3548 O LEU A 339 17048 7542 8576 1371 735 666 O ATOM 3549 CB LEU A 339 0.624 23.798 24.982 1.00 78.75 C ANISOU 3549 CB LEU A 339 15079 7130 7714 1339 458 630 C ATOM 3550 CG LEU A 339 -0.321 22.751 24.413 1.00 82.10 C ANISOU 3550 CG LEU A 339 15202 7844 8148 1523 365 637 C ATOM 3551 CD1 LEU A 339 -0.524 21.649 25.403 1.00 80.01 C ANISOU 3551 CD1 LEU A 339 14643 7767 7989 1425 276 560 C ATOM 3552 CD2 LEU A 339 -1.664 23.346 24.019 1.00 85.63 C ANISOU 3552 CD2 LEU A 339 15752 8335 8447 1895 382 674 C ATOM 3553 N LEU A 340 3.026 25.961 24.933 1.00 84.55 N ANISOU 3553 N LEU A 340 16458 7255 8410 876 708 638 N ATOM 3554 CA LEU A 340 3.913 26.875 25.650 1.00 85.76 C ANISOU 3554 CA LEU A 340 16861 7162 8560 634 803 582 C ATOM 3555 C LEU A 340 4.208 28.102 24.805 1.00 91.03 C ANISOU 3555 C LEU A 340 17923 7546 9119 652 965 647 C ATOM 3556 O LEU A 340 4.906 28.999 25.280 1.00 92.27 O ANISOU 3556 O LEU A 340 18339 7464 9255 450 1073 599 O ATOM 3557 CB LEU A 340 5.225 26.172 26.096 1.00 84.65 C ANISOU 3557 CB LEU A 340 16499 7107 8555 262 753 501 C ATOM 3558 CG LEU A 340 5.070 25.053 27.146 1.00 87.27 C ANISOU 3558 CG LEU A 340 16498 7676 8984 219 611 430 C ATOM 3559 CD1 LEU A 340 6.403 24.477 27.533 1.00 86.84 C ANISOU 3559 CD1 LEU A 340 16261 7698 9036 -114 571 356 C ATOM 3560 CD2 LEU A 340 4.353 25.545 28.378 1.00 89.63 C ANISOU 3560 CD2 LEU A 340 16912 7911 9233 323 609 380 C ATOM 3561 N CYS A 341 3.637 28.144 23.567 1.00 87.63 N ANISOU 3561 N CYS A 341 17546 7143 8609 900 987 752 N ATOM 3562 CA ACYS A 341 3.757 29.243 22.605 0.50 90.33 C ANISOU 3562 CA ACYS A 341 18272 7226 8822 985 1145 839 C ATOM 3563 CA BCYS A 341 3.774 29.231 22.580 0.50 89.42 C ANISOU 3563 CA BCYS A 341 18155 7113 8708 982 1145 840 C ATOM 3564 C CYS A 341 5.258 29.609 22.410 1.00 95.06 C ANISOU 3564 C CYS A 341 18997 7646 9477 590 1256 807 C ATOM 3565 O CYS A 341 5.635 30.795 22.430 1.00 96.69 O ANISOU 3565 O CYS A 341 19594 7542 9601 506 1421 811 O ATOM 3566 CB ACYS A 341 2.915 30.448 23.039 0.50 93.09 C ANISOU 3566 CB ACYS A 341 18999 7349 9022 1236 1241 863 C ATOM 3567 CB BCYS A 341 2.914 30.440 22.954 0.50 91.37 C ANISOU 3567 CB BCYS A 341 18781 7133 8801 1243 1243 869 C ATOM 3568 SG ACYS A 341 1.486 30.039 24.094 0.50 96.07 S ANISOU 3568 SG ACYS A 341 19181 7936 9384 1534 1107 821 S ATOM 3569 SG BCYS A 341 2.959 31.795 21.749 0.50 97.83 S ANISOU 3569 SG BCYS A 341 20119 7616 9436 1401 1452 994 S ATOM 3570 N LEU A 342 6.113 28.570 22.244 1.00 89.68 N ANISOU 3570 N LEU A 342 17978 7164 8931 343 1172 766 N ATOM 3571 CA LEU A 342 7.556 28.706 22.061 1.00 99.74 C ANISOU 3571 CA LEU A 342 19277 8348 10272 -39 1253 719 C ATOM 3572 C LEU A 342 7.919 29.138 20.624 1.00139.22 C ANISOU 3572 C LEU A 342 24475 13222 15201 -25 1381 819 C ATOM 3573 O LEU A 342 7.749 28.388 19.660 1.00109.72 O ANISOU 3573 O LEU A 342 20547 9665 11478 95 1318 886 O ATOM 3574 CB LEU A 342 8.266 27.394 22.427 1.00 97.03 C ANISOU 3574 CB LEU A 342 18492 8289 10086 -259 1108 643 C ATOM 3575 CG LEU A 342 8.500 27.109 23.900 1.00100.23 C ANISOU 3575 CG LEU A 342 18745 8769 10567 -419 1024 522 C ATOM 3576 CD1 LEU A 342 9.239 25.803 24.065 1.00 97.87 C ANISOU 3576 CD1 LEU A 342 18036 8746 10403 -600 895 468 C ATOM 3577 CD2 LEU A 342 9.304 28.232 24.569 1.00105.04 C ANISOU 3577 CD2 LEU A 342 19636 9128 11147 -688 1153 436 C TER 3578 LEU A 342 HETATM 3579 C1 JTZ A1201 2.778 8.429 53.520 1.00 66.95 C HETATM 3580 N1 JTZ A1201 2.598 7.082 51.526 1.00 72.75 N HETATM 3581 O1 JTZ A1201 3.514 6.690 48.903 1.00 67.74 O HETATM 3582 C2 JTZ A1201 2.152 7.149 52.964 1.00 68.38 C HETATM 3583 O2 JTZ A1201 2.587 3.269 49.412 1.00 78.08 O HETATM 3584 C3 JTZ A1201 0.615 7.151 53.042 1.00 65.88 C HETATM 3585 C4 JTZ A1201 2.104 5.913 50.712 1.00 74.42 C HETATM 3586 C5 JTZ A1201 3.136 5.537 49.645 1.00 73.45 C HETATM 3587 C6 JTZ A1201 2.493 4.516 48.720 1.00 76.54 C HETATM 3588 C7 JTZ A1201 1.711 2.207 49.117 1.00 81.83 C HETATM 3589 C8 JTZ A1201 1.123 1.947 47.848 1.00 80.60 C HETATM 3590 C9 JTZ A1201 0.348 0.799 47.658 1.00 80.91 C HETATM 3591 C10 JTZ A1201 0.110 -0.075 48.724 1.00 82.04 C HETATM 3592 C11 JTZ A1201 0.680 0.177 49.984 1.00 83.41 C HETATM 3593 C12 JTZ A1201 1.507 1.302 50.200 1.00 83.81 C HETATM 3594 C13 JTZ A1201 2.060 1.579 51.589 1.00 85.61 C HETATM 3595 C14 JTZ A1201 3.062 0.605 52.118 1.00 90.04 C HETATM 3596 C15 JTZ A1201 2.738 -0.356 52.991 1.00 92.00 C HETATM 3597 C1 CLR A1202 -11.268 9.973 30.300 1.00104.68 C HETATM 3598 C2 CLR A1202 -11.095 9.880 28.772 1.00103.78 C HETATM 3599 C3 CLR A1202 -9.640 9.724 28.322 1.00102.62 C HETATM 3600 C4 CLR A1202 -9.034 8.502 29.000 1.00100.63 C HETATM 3601 C5 CLR A1202 -9.133 8.704 30.498 1.00101.46 C HETATM 3602 C6 CLR A1202 -7.969 8.691 31.181 1.00101.12 C HETATM 3603 C7 CLR A1202 -7.844 9.248 32.582 1.00102.65 C HETATM 3604 C8 CLR A1202 -9.118 8.954 33.379 1.00104.28 C HETATM 3605 C9 CLR A1202 -10.311 9.547 32.592 1.00106.07 C HETATM 3606 C10 CLR A1202 -10.501 8.943 31.166 1.00104.27 C HETATM 3607 C11 CLR A1202 -11.607 9.529 33.450 1.00107.84 C HETATM 3608 C12 CLR A1202 -11.451 10.058 34.891 1.00107.26 C HETATM 3609 C13 CLR A1202 -10.321 9.373 35.679 1.00106.68 C HETATM 3610 C14 CLR A1202 -9.077 9.547 34.795 1.00104.75 C HETATM 3611 C15 CLR A1202 -7.917 9.168 35.700 1.00105.39 C HETATM 3612 C16 CLR A1202 -8.347 9.750 37.046 1.00106.52 C HETATM 3613 C17 CLR A1202 -9.823 10.169 36.922 1.00108.40 C HETATM 3614 C18 CLR A1202 -10.707 7.902 35.990 1.00105.29 C HETATM 3615 C19 CLR A1202 -11.288 7.619 31.207 1.00103.72 C HETATM 3616 C20 CLR A1202 -10.590 10.111 38.272 1.00110.90 C HETATM 3617 C21 CLR A1202 -12.054 10.561 38.212 1.00110.73 C HETATM 3618 C22 CLR A1202 -9.912 10.979 39.341 1.00112.23 C HETATM 3619 C23 CLR A1202 -9.737 10.254 40.675 1.00113.19 C HETATM 3620 C24 CLR A1202 -10.178 11.159 41.819 1.00113.93 C HETATM 3621 C25 CLR A1202 -9.857 10.550 43.178 1.00114.36 C HETATM 3622 C26 CLR A1202 -9.036 11.511 44.038 1.00113.94 C HETATM 3623 C27 CLR A1202 -11.138 10.123 43.885 1.00114.48 C HETATM 3624 O1 CLR A1202 -9.589 9.554 26.901 1.00104.57 O HETATM 3625 C1 OLB A1203 -9.232 21.321 26.221 1.00133.43 C HETATM 3626 C2 OLB A1203 -9.367 20.195 27.233 1.00129.89 C HETATM 3627 C3 OLB A1203 -9.087 20.647 28.666 1.00125.73 C HETATM 3628 C4 OLB A1203 -7.943 19.863 29.298 1.00121.45 C HETATM 3629 C5 OLB A1203 -8.200 19.630 30.785 1.00117.44 C HETATM 3630 O19 OLB A1203 -8.224 22.022 26.177 1.00134.19 O HETATM 3631 O20 OLB A1203 -10.227 21.551 25.355 1.00135.54 O HETATM 3632 C21 OLB A1203 -10.099 21.213 23.968 1.00136.70 C HETATM 3633 C22 OLB A1203 -11.464 21.157 23.287 1.00136.80 C HETATM 3634 O23 OLB A1203 -11.324 21.521 21.908 1.00136.21 O HETATM 3635 C24 OLB A1203 -12.061 19.757 23.400 1.00137.06 C HETATM 3636 O25 OLB A1203 -11.379 18.844 22.528 1.00137.47 O HETATM 3637 C6 OLB A1203 -7.252 20.453 31.647 1.00114.40 C HETATM 3638 C7 OLB A1203 -6.395 19.542 32.512 1.00113.18 C HETATM 3639 C8 OLB A1203 -6.193 20.112 33.913 1.00112.30 C HETATM 3640 C9 OLB A1203 -7.236 19.559 34.868 1.00109.54 C HETATM 3641 C10 OLB A1203 -7.391 19.964 36.135 1.00107.34 C HETATM 3642 C11 OLB A1203 -6.552 21.029 36.811 1.00105.66 C HETATM 3643 C1 OLB A1204 -8.128 20.169 52.353 1.00114.43 C HETATM 3644 C2 OLB A1204 -8.876 20.035 51.036 1.00113.69 C HETATM 3645 C3 OLB A1204 -7.945 19.983 49.821 1.00112.28 C HETATM 3646 C4 OLB A1204 -8.398 18.954 48.786 1.00111.05 C HETATM 3647 C5 OLB A1204 -7.471 18.953 47.573 1.00109.92 C HETATM 3648 O19 OLB A1204 -7.158 20.908 52.451 1.00116.48 O HETATM 3649 O20 OLB A1204 -8.548 19.502 53.433 1.00112.88 O HETATM 3650 C21 OLB A1204 -7.913 19.657 54.704 1.00114.06 C HETATM 3651 C22 OLB A1204 -8.869 20.351 55.663 1.00114.96 C HETATM 3652 O23 OLB A1204 -10.018 19.513 55.844 1.00116.01 O HETATM 3653 C24 OLB A1204 -8.144 20.616 56.983 1.00113.84 C HETATM 3654 O25 OLB A1204 -9.044 20.717 58.096 1.00112.34 O HETATM 3655 C1 OLB A1205 -5.128 -5.132 27.484 1.00106.48 C HETATM 3656 C2 OLB A1205 -5.936 -5.792 28.592 1.00103.50 C HETATM 3657 C3 OLB A1205 -5.444 -5.446 29.997 1.00100.63 C HETATM 3658 C4 OLB A1205 -5.233 -6.694 30.841 1.00 97.93 C HETATM 3659 C5 OLB A1205 -4.826 -6.306 32.256 1.00 97.57 C HETATM 3660 O19 OLB A1205 -4.176 -4.396 27.721 1.00107.69 O HETATM 3661 O20 OLB A1205 -5.462 -5.327 26.202 1.00107.27 O HETATM 3662 C21 OLB A1205 -4.990 -6.440 25.434 1.00106.31 C HETATM 3663 C22 OLB A1205 -5.854 -6.584 24.186 1.00106.47 C HETATM 3664 O23 OLB A1205 -5.044 -6.445 23.016 1.00108.28 O HETATM 3665 C24 OLB A1205 -6.564 -7.932 24.153 1.00105.28 C HETATM 3666 O25 OLB A1205 -7.673 -7.864 23.243 1.00104.11 O HETATM 3667 C6 OLB A1205 -3.538 -7.013 32.658 1.00 97.85 C HETATM 3668 C7 OLB A1205 -3.644 -7.583 34.067 1.00 98.85 C HETATM 3669 C8 OLB A1205 -3.142 -9.022 34.141 1.00 99.43 C HETATM 3670 C1 OLB A1206 14.824 1.648 31.665 1.00117.66 C HETATM 3671 C2 OLB A1206 14.834 2.950 32.448 1.00114.97 C HETATM 3672 C3 OLB A1206 16.239 3.340 32.908 1.00112.53 C HETATM 3673 C4 OLB A1206 16.558 4.790 32.559 1.00111.18 C HETATM 3674 C5 OLB A1206 16.495 5.690 33.792 1.00110.33 C HETATM 3675 O19 OLB A1206 15.072 0.587 32.232 1.00119.21 O HETATM 3676 O20 OLB A1206 14.525 1.680 30.355 1.00117.65 O HETATM 3677 C21 OLB A1206 14.447 0.535 29.497 1.00116.23 C HETATM 3678 C22 OLB A1206 15.702 0.459 28.635 1.00115.65 C HETATM 3679 O23 OLB A1206 16.020 -0.911 28.373 1.00116.26 O HETATM 3680 C24 OLB A1206 15.481 1.177 27.309 1.00115.12 C HETATM 3681 O25 OLB A1206 16.680 1.103 26.520 1.00114.49 O HETATM 3682 C6 OLB A1206 17.417 6.897 33.652 1.00108.90 C HETATM 3683 C1 OLB A1207 6.231 32.282 32.145 1.00121.03 C HETATM 3684 C2 OLB A1207 5.410 32.390 33.425 1.00115.32 C HETATM 3685 C3 OLB A1207 6.227 32.805 34.649 1.00109.58 C HETATM 3686 C4 OLB A1207 5.462 32.554 35.939 1.00105.34 C HETATM 3687 C5 OLB A1207 6.459 32.269 37.048 1.00104.34 C HETATM 3688 O19 OLB A1207 7.459 32.342 32.134 1.00123.09 O HETATM 3689 O20 OLB A1207 5.600 32.113 30.978 1.00122.24 O HETATM 3690 C21 OLB A1207 5.517 30.818 30.377 1.00121.41 C HETATM 3691 C22 OLB A1207 6.237 30.858 29.038 1.00120.48 C HETATM 3692 O23 OLB A1207 7.099 29.721 28.881 1.00118.80 O HETATM 3693 C24 OLB A1207 5.180 30.883 27.947 1.00120.64 C HETATM 3694 O25 OLB A1207 5.821 31.149 26.697 1.00121.50 O HETATM 3695 C6 OLB A1207 6.134 30.965 37.762 1.00104.26 C HETATM 3696 C1 OLB A1208 10.075 21.290 25.601 1.00124.44 C HETATM 3697 C2 OLB A1208 9.271 22.122 26.585 1.00118.76 C HETATM 3698 C3 OLB A1208 9.351 21.597 28.021 1.00113.76 C HETATM 3699 C4 OLB A1208 8.094 20.831 28.414 1.00109.02 C HETATM 3700 C5 OLB A1208 8.377 19.890 29.572 1.00105.43 C HETATM 3701 O19 OLB A1208 10.932 20.496 25.989 1.00126.30 O HETATM 3702 O20 OLB A1208 9.837 21.427 24.285 1.00126.87 O HETATM 3703 C21 OLB A1208 10.872 21.347 23.296 1.00129.87 C HETATM 3704 C22 OLB A1208 11.329 22.744 22.879 1.00133.31 C HETATM 3705 O23 OLB A1208 11.775 23.500 24.015 1.00135.08 O HETATM 3706 C24 OLB A1208 12.412 22.669 21.803 1.00133.31 C HETATM 3707 O25 OLB A1208 12.590 23.963 21.206 1.00133.24 O HETATM 3708 C6 OLB A1208 7.640 20.329 30.826 1.00105.18 C HETATM 3709 C10 OLC A1209 -6.018 -3.053 40.884 1.00 94.33 C HETATM 3710 C9 OLC A1209 -6.211 -3.120 39.556 1.00 96.86 C HETATM 3711 C11 OLC A1209 -5.699 -4.217 41.795 1.00 91.56 C HETATM 3712 C8 OLC A1209 -6.118 -4.373 38.706 1.00 97.80 C HETATM 3713 C7 OLC A1209 -7.254 -4.416 37.692 1.00 98.11 C HETATM 3714 C6 OLC A1209 -6.772 -4.937 36.341 1.00 98.89 C HETATM 3715 C5 OLC A1209 -7.400 -4.136 35.205 1.00100.36 C HETATM 3716 C4 OLC A1209 -8.147 -5.033 34.224 1.00103.43 C HETATM 3717 C3 OLC A1209 -9.652 -4.745 34.216 1.00105.02 C HETATM 3718 C2 OLC A1209 -10.179 -4.492 32.802 1.00104.71 C HETATM 3719 C1 OLB A1210 7.308 26.683 59.853 1.00122.10 C HETATM 3720 C2 OLB A1210 6.809 26.114 58.549 1.00116.91 C HETATM 3721 C3 OLB A1210 6.344 27.230 57.619 1.00114.08 C HETATM 3722 C4 OLB A1210 4.828 27.239 57.424 1.00113.55 C HETATM 3723 C5 OLB A1210 4.303 26.181 56.449 1.00112.99 C HETATM 3724 O19 OLB A1210 8.237 27.481 59.865 1.00122.96 O HETATM 3725 O20 OLB A1210 6.725 26.319 61.002 1.00126.60 O HETATM 3726 C21 OLB A1210 7.359 25.458 61.962 1.00127.94 C HETATM 3727 C22 OLB A1210 6.951 25.825 63.394 1.00128.65 C HETATM 3728 O23 OLB A1210 6.721 27.238 63.544 1.00128.57 O HETATM 3729 C24 OLB A1210 5.723 25.023 63.828 1.00128.04 C HETATM 3730 O25 OLB A1210 5.151 25.581 65.023 1.00126.92 O HETATM 3731 C6 OLB A1210 4.338 26.649 54.996 1.00112.24 C HETATM 3732 C7 OLB A1210 5.227 25.749 54.138 1.00111.65 C HETATM 3733 C8 OLB A1210 4.438 24.710 53.343 1.00111.51 C HETATM 3734 C9 OLB A1210 5.161 24.372 52.055 1.00109.97 C HETATM 3735 C10 OLB A1210 4.495 23.839 51.028 1.00108.23 C HETATM 3736 C11 OLB A1210 5.217 23.508 49.743 1.00107.25 C HETATM 3737 S SO4 A1211 -1.879 2.953 19.572 1.00 77.47 S HETATM 3738 O1 SO4 A1211 -0.900 3.804 18.925 1.00 78.86 O HETATM 3739 O2 SO4 A1211 -3.240 3.209 19.033 1.00 77.27 O HETATM 3740 O3 SO4 A1211 -1.475 1.570 19.387 1.00 74.47 O HETATM 3741 O4 SO4 A1211 -1.900 3.258 21.003 1.00 79.68 O HETATM 3742 S SO4 A1212 16.609 6.581 21.267 1.00141.21 S HETATM 3743 O1 SO4 A1212 16.429 7.849 20.542 1.00141.12 O HETATM 3744 O2 SO4 A1212 17.614 5.741 20.597 1.00140.90 O HETATM 3745 O3 SO4 A1212 15.336 5.856 21.313 1.00140.95 O HETATM 3746 O4 SO4 A1212 17.060 6.881 22.628 1.00141.40 O HETATM 3747 S SO4 A1213 36.502 -7.188 -2.099 1.00165.54 S HETATM 3748 O1 SO4 A1213 35.987 -5.964 -2.724 1.00166.31 O HETATM 3749 O2 SO4 A1213 37.105 -8.057 -3.114 1.00164.66 O HETATM 3750 O3 SO4 A1213 35.409 -7.899 -1.464 1.00164.82 O HETATM 3751 O4 SO4 A1213 37.497 -6.820 -1.089 1.00165.59 O HETATM 3752 S SO4 A1214 25.247 7.887 5.796 1.00184.85 S HETATM 3753 O1 SO4 A1214 24.136 7.245 5.095 1.00185.20 O HETATM 3754 O2 SO4 A1214 25.930 8.808 4.884 1.00184.93 O HETATM 3755 O3 SO4 A1214 24.745 8.627 6.955 1.00184.85 O HETATM 3756 O4 SO4 A1214 26.176 6.862 6.246 1.00184.18 O HETATM 3757 C9 OLC A1215 -8.421 16.887 39.231 1.00108.46 C HETATM 3758 C8 OLC A1215 -8.495 15.734 38.253 1.00108.81 C HETATM 3759 C24 OLC A1215 -10.130 12.659 25.507 1.00128.41 C HETATM 3760 C7 OLC A1215 -8.258 16.237 36.834 1.00109.25 C HETATM 3761 C6 OLC A1215 -8.185 15.078 35.849 1.00110.32 C HETATM 3762 C5 OLC A1215 -9.394 15.048 34.912 1.00112.02 C HETATM 3763 C4 OLC A1215 -9.028 15.481 33.492 1.00113.12 C HETATM 3764 C3 OLC A1215 -8.795 14.283 32.581 1.00115.23 C HETATM 3765 C2 OLC A1215 -9.806 14.239 31.434 1.00118.43 C HETATM 3766 C21 OLC A1215 -9.441 13.503 27.747 1.00126.95 C HETATM 3767 C1 OLC A1215 -9.133 14.176 30.075 1.00121.96 C HETATM 3768 C22 OLC A1215 -10.504 13.595 26.654 1.00128.12 C HETATM 3769 O19 OLC A1215 -7.915 14.178 29.977 1.00122.76 O HETATM 3770 O25 OLC A1215 -11.076 12.796 24.437 1.00128.56 O HETATM 3771 O23 OLC A1215 -11.786 13.227 27.183 1.00128.61 O HETATM 3772 O20 OLC A1215 -9.879 14.136 28.961 1.00124.94 O HETATM 3773 C10 OLC A1216 1.956 25.666 37.101 1.00102.52 C HETATM 3774 C9 OLC A1216 0.899 25.275 36.383 1.00102.22 C HETATM 3775 C11 OLC A1216 2.767 26.918 36.853 1.00104.94 C HETATM 3776 C8 OLC A1216 0.322 26.019 35.199 1.00103.54 C HETATM 3777 C24 OLC A1216 -6.318 26.393 24.706 1.00124.35 C HETATM 3778 C12 OLC A1216 4.253 26.635 37.077 1.00107.58 C HETATM 3779 C7 OLC A1216 0.250 25.090 33.985 1.00104.55 C HETATM 3780 C13 OLC A1216 5.123 27.623 36.300 1.00109.25 C HETATM 3781 C6 OLC A1216 -0.170 25.841 32.723 1.00104.26 C HETATM 3782 C14 OLC A1216 6.611 27.426 36.577 1.00110.02 C HETATM 3783 C5 OLC A1216 0.759 25.584 31.537 1.00104.99 C HETATM 3784 C4 OLC A1216 0.032 24.856 30.406 1.00107.63 C HETATM 3785 C3 OLC A1216 -0.527 25.803 29.346 1.00111.27 C HETATM 3786 C2 OLC A1216 -1.689 25.174 28.572 1.00115.88 C HETATM 3787 C21 OLC A1216 -4.222 26.325 26.063 1.00124.73 C HETATM 3788 C1 OLC A1216 -2.307 26.128 27.560 1.00121.12 C HETATM 3789 C22 OLC A1216 -5.749 26.411 26.129 1.00125.05 C HETATM 3790 O19 OLC A1216 -1.603 26.906 26.920 1.00122.70 O HETATM 3791 O25 OLC A1216 -7.745 26.216 24.701 1.00122.97 O HETATM 3792 O23 OLC A1216 -6.280 25.322 26.902 1.00125.05 O HETATM 3793 O20 OLC A1216 -3.636 26.120 27.361 1.00123.74 O HETATM 3794 C1 OLA A1217 13.012 14.582 56.511 1.00122.40 C HETATM 3795 O1 OLA A1217 14.216 14.447 56.830 1.00122.98 O HETATM 3796 O2 OLA A1217 12.127 14.294 57.351 1.00121.66 O HETATM 3797 C2 OLA A1217 12.628 15.101 55.140 1.00122.20 C HETATM 3798 C3 OLA A1217 12.985 14.111 54.026 1.00120.05 C HETATM 3799 C4 OLA A1217 12.196 14.406 52.753 1.00118.20 C HETATM 3800 C5 OLA A1217 12.935 15.362 51.819 1.00117.26 C HETATM 3801 C6 OLA A1217 12.052 15.780 50.645 1.00117.35 C HETATM 3802 C7 OLA A1217 12.885 16.273 49.462 1.00116.84 C HETATM 3803 C8 OLA A1217 12.938 15.224 48.351 1.00115.73 C HETATM 3804 C9 OLA A1217 13.938 15.641 47.291 1.00113.70 C HETATM 3805 C10 OLA A1217 14.909 14.857 46.802 1.00112.09 C HETATM 3806 C11 OLA A1217 15.191 13.428 47.226 1.00110.22 C HETATM 3807 C12 OLA A1217 16.625 13.061 46.850 1.00109.18 C HETATM 3808 C1 OLA A1218 -6.335 24.684 30.069 1.00118.71 C HETATM 3809 O1 OLA A1218 -5.545 23.879 29.528 1.00120.24 O HETATM 3810 O2 OLA A1218 -7.471 24.830 29.558 1.00119.34 O HETATM 3811 C2 OLA A1218 -5.909 25.472 31.294 1.00115.27 C HETATM 3812 C3 OLA A1218 -6.414 24.835 32.585 1.00111.45 C HETATM 3813 C4 OLA A1218 -5.689 25.376 33.813 1.00108.77 C HETATM 3814 C5 OLA A1218 -5.403 24.242 34.789 1.00108.13 C HETATM 3815 C6 OLA A1218 -4.474 24.655 35.927 1.00108.22 C HETATM 3816 C7 OLA A1218 -5.192 24.599 37.280 1.00108.54 C HETATM 3817 C8 OLA A1218 -4.488 23.716 38.311 1.00108.29 C HETATM 3818 C9 OLA A1218 -3.452 24.507 39.095 1.00109.55 C HETATM 3819 C10 OLA A1218 -3.603 25.048 40.319 1.00109.51 C HETATM 3820 C11 OLA A1218 -4.857 24.990 41.172 1.00108.72 C HETATM 3821 C12 OLA A1218 -4.958 26.244 42.039 1.00107.80 C HETATM 3822 C1 OLA A1219 6.139 -14.032 27.694 1.00115.95 C HETATM 3823 O1 OLA A1219 6.903 -14.900 27.208 1.00117.35 O HETATM 3824 O2 OLA A1219 6.659 -13.026 28.242 1.00117.78 O HETATM 3825 C2 OLA A1219 4.635 -14.228 27.628 1.00109.71 C HETATM 3826 C3 OLA A1219 3.886 -12.976 28.056 1.00103.49 C HETATM 3827 C4 OLA A1219 2.500 -12.989 27.442 1.00100.32 C HETATM 3828 C5 OLA A1219 1.627 -11.899 28.042 1.00 98.27 C HETATM 3829 C6 OLA A1219 0.785 -12.503 29.149 1.00 98.02 C HETATM 3830 C7 OLA A1219 -0.497 -11.727 29.381 1.00 98.62 C HETATM 3831 C8 OLA A1219 -0.772 -11.713 30.878 1.00 99.43 C HETATM 3832 C1 OLA A1220 13.869 -4.684 29.999 1.00122.40 C HETATM 3833 O1 OLA A1220 14.749 -3.999 29.424 1.00122.45 O HETATM 3834 O2 OLA A1220 14.214 -5.780 30.512 1.00123.90 O HETATM 3835 C2 OLA A1220 12.425 -4.203 30.039 1.00118.97 C HETATM 3836 C3 OLA A1220 11.847 -4.232 31.454 1.00114.68 C HETATM 3837 C4 OLA A1220 10.791 -3.152 31.682 1.00111.00 C HETATM 3838 C5 OLA A1220 11.367 -1.953 32.429 1.00108.83 C HETATM 3839 C6 OLA A1220 11.333 -2.118 33.949 1.00106.96 C HETATM 3840 C7 OLA A1220 12.698 -1.872 34.592 1.00105.24 C HETATM 3841 C8 OLA A1220 13.304 -3.147 35.162 1.00105.31 C HETATM 3842 C9 OLA A1220 13.934 -2.863 36.512 1.00105.73 C HETATM 3843 C10 OLA A1220 13.936 -3.705 37.563 1.00105.08 C HETATM 3844 C11 OLA A1220 13.310 -5.087 37.600 1.00103.59 C HETATM 3845 O HOH A1301 -4.328 10.755 64.286 1.00 66.50 O HETATM 3846 O HOH A1302 2.722 11.638 34.053 1.00 59.77 O HETATM 3847 O HOH A1303 -11.569 7.491 61.094 1.00 94.45 O HETATM 3848 O HOH A1304 10.103 -5.313 14.764 1.00 72.48 O HETATM 3849 O HOH A1305 3.154 7.825 39.157 1.00 63.52 O HETATM 3850 O HOH A1306 1.692 10.325 31.958 1.00 69.74 O HETATM 3851 O HOH A1307 -5.264 0.763 51.431 1.00 72.39 O HETATM 3852 O HOH A1308 22.606 -5.643 13.293 1.00 75.11 O HETATM 3853 O HOH A1309 11.928 4.899 46.848 1.00 64.92 O HETATM 3854 O HOH A1310 14.459 -0.371 15.149 1.00 64.59 O HETATM 3855 O HOH A1311 21.237 -14.795 12.230 1.00 81.10 O HETATM 3856 O HOH A1312 -4.423 -0.353 46.701 1.00 81.94 O HETATM 3857 O HOH A1313 -9.905 17.163 57.763 1.00 86.72 O HETATM 3858 O HOH A1314 11.588 2.127 -2.815 1.00 66.51 O HETATM 3859 O HOH A1315 0.451 19.826 59.086 1.00 95.55 O HETATM 3860 O HOH A1316 5.693 10.955 36.014 1.00 91.42 O HETATM 3861 O HOH A1317 14.663 -2.146 18.242 1.00 88.48 O HETATM 3862 O HOH A1318 6.312 -1.722 3.712 1.00 86.04 O HETATM 3863 O HOH A1319 -3.148 -4.426 22.050 1.00 53.62 O HETATM 3864 O HOH A1320 -11.154 9.591 56.271 1.00112.21 O HETATM 3865 O HOH A1321 9.154 8.314 21.589 1.00 70.49 O HETATM 3866 O HOH A1322 9.467 3.986 -2.213 1.00 69.29 O HETATM 3867 O HOH A1323 2.614 12.673 62.332 1.00 80.20 O HETATM 3868 O HOH A1324 8.570 7.148 35.567 1.00 64.28 O HETATM 3869 O HOH A1325 11.102 -11.975 61.970 1.00 87.37 O HETATM 3870 O HOH A1326 -12.923 6.304 59.073 1.00 78.67 O HETATM 3871 O HOH A1327 1.162 -6.856 62.837 1.00 91.20 O HETATM 3872 O HOH A1328 22.283 -9.652 -11.587 1.00 81.67 O HETATM 3873 O HOH A1329 19.645 3.633 -2.460 1.00105.46 O HETATM 3874 O HOH A1330 7.974 -9.202 63.473 1.00108.57 O HETATM 3875 O HOH A1331 -7.875 21.808 19.197 1.00 83.93 O HETATM 3876 O HOH A1332 16.541 0.978 -5.324 1.00 68.53 O HETATM 3877 O HOH A1333 18.203 -3.559 -7.055 1.00 85.39 O HETATM 3878 O HOH A1334 -0.300 -7.227 65.162 1.00 92.05 O HETATM 3879 O HOH A1335 10.527 30.745 28.369 1.00 93.83 O HETATM 3880 O HOH A1336 -13.710 8.663 62.301 1.00134.09 O CONECT 616 1322 CONECT 1268 1316 CONECT 1316 1268 CONECT 1322 616 CONECT 3579 3582 CONECT 3580 3582 3585 CONECT 3581 3586 CONECT 3582 3579 3580 3584 CONECT 3583 3587 3588 CONECT 3584 3582 CONECT 3585 3580 3586 CONECT 3586 3581 3585 3587 CONECT 3587 3583 3586 CONECT 3588 3583 3589 3593 CONECT 3589 3588 3590 CONECT 3590 3589 3591 CONECT 3591 3590 3592 CONECT 3592 3591 3593 CONECT 3593 3588 3592 3594 CONECT 3594 3593 3595 CONECT 3595 3594 3596 CONECT 3596 3595 CONECT 3597 3598 3606 CONECT 3598 3597 3599 CONECT 3599 3598 3600 3624 CONECT 3600 3599 3601 CONECT 3601 3600 3602 3606 CONECT 3602 3601 3603 CONECT 3603 3602 3604 CONECT 3604 3603 3605 3610 CONECT 3605 3604 3606 3607 CONECT 3606 3597 3601 3605 3615 CONECT 3607 3605 3608 CONECT 3608 3607 3609 CONECT 3609 3608 3610 3613 3614 CONECT 3610 3604 3609 3611 CONECT 3611 3610 3612 CONECT 3612 3611 3613 CONECT 3613 3609 3612 3616 CONECT 3614 3609 CONECT 3615 3606 CONECT 3616 3613 3617 3618 CONECT 3617 3616 CONECT 3618 3616 3619 CONECT 3619 3618 3620 CONECT 3620 3619 3621 CONECT 3621 3620 3622 3623 CONECT 3622 3621 CONECT 3623 3621 CONECT 3624 3599 CONECT 3625 3626 3630 3631 CONECT 3626 3625 3627 CONECT 3627 3626 3628 CONECT 3628 3627 3629 CONECT 3629 3628 3637 CONECT 3630 3625 CONECT 3631 3625 3632 CONECT 3632 3631 3633 CONECT 3633 3632 3634 3635 CONECT 3634 3633 CONECT 3635 3633 3636 CONECT 3636 3635 CONECT 3637 3629 3638 CONECT 3638 3637 3639 CONECT 3639 3638 3640 CONECT 3640 3639 3641 CONECT 3641 3640 3642 CONECT 3642 3641 CONECT 3643 3644 3648 3649 CONECT 3644 3643 3645 CONECT 3645 3644 3646 CONECT 3646 3645 3647 CONECT 3647 3646 CONECT 3648 3643 CONECT 3649 3643 3650 CONECT 3650 3649 3651 CONECT 3651 3650 3652 3653 CONECT 3652 3651 CONECT 3653 3651 3654 CONECT 3654 3653 CONECT 3655 3656 3660 3661 CONECT 3656 3655 3657 CONECT 3657 3656 3658 CONECT 3658 3657 3659 CONECT 3659 3658 3667 CONECT 3660 3655 CONECT 3661 3655 3662 CONECT 3662 3661 3663 CONECT 3663 3662 3664 3665 CONECT 3664 3663 CONECT 3665 3663 3666 CONECT 3666 3665 CONECT 3667 3659 3668 CONECT 3668 3667 3669 CONECT 3669 3668 CONECT 3670 3671 3675 3676 CONECT 3671 3670 3672 CONECT 3672 3671 3673 CONECT 3673 3672 3674 CONECT 3674 3673 3682 CONECT 3675 3670 CONECT 3676 3670 3677 CONECT 3677 3676 3678 CONECT 3678 3677 3679 3680 CONECT 3679 3678 CONECT 3680 3678 3681 CONECT 3681 3680 CONECT 3682 3674 CONECT 3683 3684 3688 3689 CONECT 3684 3683 3685 CONECT 3685 3684 3686 CONECT 3686 3685 3687 CONECT 3687 3686 3695 CONECT 3688 3683 CONECT 3689 3683 3690 CONECT 3690 3689 3691 CONECT 3691 3690 3692 3693 CONECT 3692 3691 CONECT 3693 3691 3694 CONECT 3694 3693 CONECT 3695 3687 CONECT 3696 3697 3701 3702 CONECT 3697 3696 3698 CONECT 3698 3697 3699 CONECT 3699 3698 3700 CONECT 3700 3699 3708 CONECT 3701 3696 CONECT 3702 3696 3703 CONECT 3703 3702 3704 CONECT 3704 3703 3705 3706 CONECT 3705 3704 CONECT 3706 3704 3707 CONECT 3707 3706 CONECT 3708 3700 CONECT 3709 3710 3711 CONECT 3710 3709 3712 CONECT 3711 3709 CONECT 3712 3710 3713 CONECT 3713 3712 3714 CONECT 3714 3713 3715 CONECT 3715 3714 3716 CONECT 3716 3715 3717 CONECT 3717 3716 3718 CONECT 3718 3717 CONECT 3719 3720 3724 3725 CONECT 3720 3719 3721 CONECT 3721 3720 3722 CONECT 3722 3721 3723 CONECT 3723 3722 3731 CONECT 3724 3719 CONECT 3725 3719 3726 CONECT 3726 3725 3727 CONECT 3727 3726 3728 3729 CONECT 3728 3727 CONECT 3729 3727 3730 CONECT 3730 3729 CONECT 3731 3723 3732 CONECT 3732 3731 3733 CONECT 3733 3732 3734 CONECT 3734 3733 3735 CONECT 3735 3734 3736 CONECT 3736 3735 CONECT 3737 3738 3739 3740 3741 CONECT 3738 3737 CONECT 3739 3737 CONECT 3740 3737 CONECT 3741 3737 CONECT 3742 3743 3744 3745 3746 CONECT 3743 3742 CONECT 3744 3742 CONECT 3745 3742 CONECT 3746 3742 CONECT 3747 3748 3749 3750 3751 CONECT 3748 3747 CONECT 3749 3747 CONECT 3750 3747 CONECT 3751 3747 CONECT 3752 3753 3754 3755 3756 CONECT 3753 3752 CONECT 3754 3752 CONECT 3755 3752 CONECT 3756 3752 CONECT 3757 3758 CONECT 3758 3757 3760 CONECT 3759 3768 3770 CONECT 3760 3758 3761 CONECT 3761 3760 3762 CONECT 3762 3761 3763 CONECT 3763 3762 3764 CONECT 3764 3763 3765 CONECT 3765 3764 3767 CONECT 3766 3768 3772 CONECT 3767 3765 3769 3772 CONECT 3768 3759 3766 3771 CONECT 3769 3767 CONECT 3770 3759 CONECT 3771 3768 CONECT 3772 3766 3767 CONECT 3773 3774 3775 CONECT 3774 3773 3776 CONECT 3775 3773 3778 CONECT 3776 3774 3779 CONECT 3777 3789 3791 CONECT 3778 3775 3780 CONECT 3779 3776 3781 CONECT 3780 3778 3782 CONECT 3781 3779 3783 CONECT 3782 3780 CONECT 3783 3781 3784 CONECT 3784 3783 3785 CONECT 3785 3784 3786 CONECT 3786 3785 3788 CONECT 3787 3789 3793 CONECT 3788 3786 3790 3793 CONECT 3789 3777 3787 3792 CONECT 3790 3788 CONECT 3791 3777 CONECT 3792 3789 CONECT 3793 3787 3788 CONECT 3794 3795 3796 3797 CONECT 3795 3794 CONECT 3796 3794 CONECT 3797 3794 3798 CONECT 3798 3797 3799 CONECT 3799 3798 3800 CONECT 3800 3799 3801 CONECT 3801 3800 3802 CONECT 3802 3801 3803 CONECT 3803 3802 3804 CONECT 3804 3803 3805 CONECT 3805 3804 3806 CONECT 3806 3805 3807 CONECT 3807 3806 CONECT 3808 3809 3810 3811 CONECT 3809 3808 CONECT 3810 3808 CONECT 3811 3808 3812 CONECT 3812 3811 3813 CONECT 3813 3812 3814 CONECT 3814 3813 3815 CONECT 3815 3814 3816 CONECT 3816 3815 3817 CONECT 3817 3816 3818 CONECT 3818 3817 3819 CONECT 3819 3818 3820 CONECT 3820 3819 3821 CONECT 3821 3820 CONECT 3822 3823 3824 3825 CONECT 3823 3822 CONECT 3824 3822 CONECT 3825 3822 3826 CONECT 3826 3825 3827 CONECT 3827 3826 3828 CONECT 3828 3827 3829 CONECT 3829 3828 3830 CONECT 3830 3829 3831 CONECT 3831 3830 CONECT 3832 3833 3834 3835 CONECT 3833 3832 CONECT 3834 3832 CONECT 3835 3832 3836 CONECT 3836 3835 3837 CONECT 3837 3836 3838 CONECT 3838 3837 3839 CONECT 3839 3838 3840 CONECT 3840 3839 3841 CONECT 3841 3840 3842 CONECT 3842 3841 3843 CONECT 3843 3842 3844 CONECT 3844 3843 MASTER 444 0 20 23 3 0 29 6 3828 1 270 39 END