HEADER MEMBRANE PROTEIN 11-MAY-20 6Z10 TITLE CRYSTAL STRUCTURE OF A HUMANIZED (K18E, K269N) RAT SUCCINATE RECEPTOR TITLE 2 SUCNR1 (GPR91) IN COMPLEX WITH A NANOBODY AND ANTAGONIST COMPND MOL_ID: 1; COMPND 2 MOLECULE: SUCCINATE RECEPTOR 1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: G-PROTEIN COUPLED RECEPTOR 91; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: NANOBODY6; COMPND 9 CHAIN: B; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 GENE: SUCNR1, GPR91; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 10 ORGANISM_TAXID: 30538; SOURCE 11 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS G PROTEIN-COUPLED RECEPTOR GPCR SUCCINATE RECEPTOR, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR M.HAFFKE,F.VILLARD REVDAT 2 23-SEP-20 6Z10 1 JRNL REVDAT 1 16-SEP-20 6Z10 0 JRNL AUTH J.VELCICKY,R.WILCKEN,S.COTESTA,P.JANSER,A.SCHLAPBACH, JRNL AUTH 2 T.WAGNER,P.PIECHON,F.VILLARD,R.BOUHELAL,F.PILLER, JRNL AUTH 3 S.HARLFINGER,R.STRINGER,D.FEHLMANN,K.KAUPMANN, JRNL AUTH 4 A.LITTLEWOOD-EVANS,M.HAFFKE,N.GOMMERMANN JRNL TITL DISCOVERY AND OPTIMIZATION OF NOVEL SUCNR1 INHIBITORS: JRNL TITL 2 DESIGN OF ZWITTERIONIC DERIVATIVES WITH A SALT BRIDGE FOR JRNL TITL 3 THE IMPROVEMENT OF ORAL EXPOSURE. JRNL REF J.MED.CHEM. V. 63 9856 2020 JRNL REFN ISSN 0022-2623 JRNL PMID 32856916 JRNL DOI 10.1021/ACS.JMEDCHEM.0C01020 REMARK 2 REMARK 2 RESOLUTION. 2.27 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.11.7 (19-MAR-2020) 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) : 2.27 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.12 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 77.3 REMARK 3 NUMBER OF REFLECTIONS : 25647 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.205 REMARK 3 R VALUE (WORKING SET) : 0.204 REMARK 3 FREE R VALUE : 0.223 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.160 REMARK 3 FREE R VALUE TEST SET COUNT : 1323 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.27 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.37 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 12.55 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 487 REMARK 3 BIN R VALUE (WORKING SET) : 0.2035 REMARK 3 BIN FREE R VALUE : 0.2071 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.07 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 26 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 : 3268 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 255 REMARK 3 SOLVENT ATOMS : 154 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 58.76 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.82 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.98840 REMARK 3 B22 (A**2) : -5.84560 REMARK 3 B33 (A**2) : 3.85730 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 4.72540 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.340 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.285 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.204 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.292 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.208 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 : 0.930 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3594 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 4820 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1278 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : 566 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3594 ; 10.000 ; 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 : 447 ; 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 : 2772 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 0.95 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.01 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 12.54 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|* } REMARK 3 ORIGIN FOR THE GROUP (A): -3.2191 23.0206 18.3267 REMARK 3 T TENSOR REMARK 3 T11: -0.0281 T22: -0.1399 REMARK 3 T33: -0.0125 T12: 0.0054 REMARK 3 T13: 0.0765 T23: 0.0101 REMARK 3 L TENSOR REMARK 3 L11: 0.5739 L22: 2.2281 REMARK 3 L33: 0.6897 L12: -0.3115 REMARK 3 L13: -0.0784 L23: 0.4213 REMARK 3 S TENSOR REMARK 3 S11: -0.0163 S12: 0.0241 S13: 0.0324 REMARK 3 S21: -0.2209 S22: 0.0178 S23: -0.0417 REMARK 3 S31: 0.0079 S32: 0.0514 S33: -0.0015 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { B|* } REMARK 3 ORIGIN FOR THE GROUP (A): 2.8018 63.9049 24.9163 REMARK 3 T TENSOR REMARK 3 T11: -0.0869 T22: -0.2516 REMARK 3 T33: 0.0080 T12: -0.0613 REMARK 3 T13: 0.0751 T23: 0.0410 REMARK 3 L TENSOR REMARK 3 L11: 2.8416 L22: 6.9541 REMARK 3 L33: 2.3300 L12: 0.0694 REMARK 3 L13: -0.9349 L23: 2.6162 REMARK 3 S TENSOR REMARK 3 S11: -0.0383 S12: 0.0264 S13: 0.1103 REMARK 3 S21: -0.2485 S22: 0.0081 S23: -0.0995 REMARK 3 S31: -0.1650 S32: 0.1253 S33: 0.0303 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6Z10 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-MAY-20. REMARK 100 THE DEPOSITION ID IS D_1292108668. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-FEB-20 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X10SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.999 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25647 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.269 REMARK 200 RESOLUTION RANGE LOW (A) : 63.120 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 90.6 REMARK 200 DATA REDUNDANCY : 5.400 REMARK 200 R MERGE (I) : 0.17200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.27 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44 REMARK 200 COMPLETENESS FOR SHELL (%) : 19.5 REMARK 200 DATA REDUNDANCY IN SHELL : 6.20 REMARK 200 R MERGE FOR SHELL (I) : 2.27400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.600 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: 6RNK REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 62.81 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.31 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM ADA PH 7.0, 28% (W/V) PEG MME REMARK 280 550, 0.55 M (NH4)2SO4, 200 MICROM RAW241, 2% (V/V) DMSO, LIPIDIC REMARK 280 CUBIC PHASE, TEMPERATURE 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 38.41950 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 75.50150 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 38.41950 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 75.50150 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1790 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18510 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 S SO4 A 414 LIES ON A SPECIAL POSITION. 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 ASP A -6 REMARK 465 TYR A -5 REMARK 465 LYS A -4 REMARK 465 ASP A -3 REMARK 465 ASP A -2 REMARK 465 ASP A -1 REMARK 465 ASP A 0 REMARK 465 LYS A 1 REMARK 465 ALA A 2 REMARK 465 GLN A 3 REMARK 465 ASN A 4 REMARK 465 LEU A 5 REMARK 465 SER A 6 REMARK 465 GLN A 215 REMARK 465 GLN A 216 REMARK 465 GLN A 217 REMARK 465 ALA A 218 REMARK 465 THR A 219 REMARK 465 VAL A 220 REMARK 465 LEU A 221 REMARK 465 SER A 222 REMARK 465 LEU A 223 REMARK 465 ASP A 257 REMARK 465 SER A 258 REMARK 465 TRP A 259 REMARK 465 PRO A 260 REMARK 465 GLN A 261 REMARK 465 LEU A 305 REMARK 465 ARG A 306 REMARK 465 GLN A 307 REMARK 465 TYR A 308 REMARK 465 PHE A 309 REMARK 465 LYS A 310 REMARK 465 SER A 311 REMARK 465 LEU A 312 REMARK 465 THR A 313 REMARK 465 SER A 314 REMARK 465 PHE A 315 REMARK 465 ARG A 316 REMARK 465 LEU A 317 REMARK 465 LEU A 318 REMARK 465 GLU A 319 REMARK 465 VAL A 320 REMARK 465 LEU A 321 REMARK 465 PHE A 322 REMARK 465 GLN A 323 REMARK 465 GLY A 324 REMARK 465 PRO A 325 REMARK 465 HIS A 326 REMARK 465 HIS A 327 REMARK 465 HIS A 328 REMARK 465 HIS A 329 REMARK 465 HIS A 330 REMARK 465 HIS A 331 REMARK 465 HIS A 332 REMARK 465 HIS A 333 REMARK 465 HIS A 334 REMARK 465 HIS A 335 REMARK 465 ASP B 1 REMARK 465 TYR B 2 REMARK 465 LYS B 3 REMARK 465 ASP B 4 REMARK 465 ASP B 5 REMARK 465 ASP B 6 REMARK 465 ASP B 7 REMARK 465 LYS B 8 REMARK 465 TYR B 35 REMARK 465 GLU B 138 REMARK 465 VAL B 139 REMARK 465 LEU B 140 REMARK 465 PHE B 141 REMARK 465 GLN B 142 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 SER A 214 OG REMARK 470 GLU B 9 CG CD OE1 OE2 REMARK 470 LEU B 137 CG CD1 CD2 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 CYS A 168 82.18 -156.65 REMARK 500 ARG B 111 -62.48 -90.71 REMARK 500 ASP B 115 73.42 -151.08 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 609 DISTANCE = 6.05 ANGSTROMS REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLC A 402 REMARK 610 OLC A 403 REMARK 610 OLC A 404 REMARK 610 OLC A 405 REMARK 610 OLC A 406 REMARK 610 OLC A 408 REMARK 610 OLC A 409 REMARK 610 OLC A 410 REMARK 610 OLC A 412 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue Q4T A 401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 402 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 403 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 404 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 405 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 406 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 407 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 408 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 409 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 410 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 411 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 412 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 413 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 414 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 415 DBREF 6Z10 A 2 317 UNP Q6IYF9 SUCR1_RAT 2 317 DBREF 6Z10 B 1 142 PDB 6Z10 6Z10 1 142 SEQADV 6Z10 ASP A -6 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 TYR A -5 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 LYS A -4 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 ASP A -3 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 ASP A -2 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 ASP A -1 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 ASP A 0 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 LYS A 1 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 GLU A 18 UNP Q6IYF9 LYS 18 ENGINEERED MUTATION SEQADV 6Z10 ASN A 269 UNP Q6IYF9 LYS 269 ENGINEERED MUTATION SEQADV 6Z10 LEU A 318 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 GLU A 319 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 VAL A 320 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 LEU A 321 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 PHE A 322 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 GLN A 323 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 GLY A 324 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 PRO A 325 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 HIS A 326 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 HIS A 327 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 HIS A 328 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 HIS A 329 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 HIS A 330 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 HIS A 331 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 HIS A 332 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 HIS A 333 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 HIS A 334 UNP Q6IYF9 EXPRESSION TAG SEQADV 6Z10 HIS A 335 UNP Q6IYF9 EXPRESSION TAG SEQRES 1 A 342 ASP TYR LYS ASP ASP ASP ASP LYS ALA GLN ASN LEU SER SEQRES 2 A 342 CYS GLU ASN TRP LEU ALA LEU GLU ASN ILE LEU GLU LYS SEQRES 3 A 342 TYR TYR LEU SER ALA PHE TYR GLY ILE GLU PHE ILE VAL SEQRES 4 A 342 GLY MET LEU GLY ASN PHE THR VAL VAL PHE GLY TYR LEU SEQRES 5 A 342 PHE CYS MET LYS ASN TRP ASN SER SER ASN VAL TYR LEU SEQRES 6 A 342 PHE ASN LEU SER ILE SER ASP LEU ALA PHE LEU CYS THR SEQRES 7 A 342 LEU PRO MET LEU ILE ARG SER TYR ALA THR GLY ASN TRP SEQRES 8 A 342 THR TYR GLY ASP VAL LEU CYS ILE SER ASN ARG TYR VAL SEQRES 9 A 342 LEU HIS ALA ASN LEU TYR THR SER ILE LEU PHE LEU THR SEQRES 10 A 342 PHE ILE SER ILE ASP ARG TYR LEU LEU MET LYS PHE PRO SEQRES 11 A 342 PHE ARG GLU HIS ILE LEU GLN LYS LYS GLU PHE ALA ILE SEQRES 12 A 342 LEU ILE SER LEU ALA VAL TRP VAL LEU VAL THR LEU GLU SEQRES 13 A 342 VAL LEU PRO MET LEU THR PHE ILE THR SER THR PRO ILE SEQRES 14 A 342 GLU LYS GLY ASP SER CYS VAL ASP TYR ALA SER SER GLY SEQRES 15 A 342 ASN PRO LYS TYR SER LEU ILE TYR SER LEU CYS LEU THR SEQRES 16 A 342 LEU LEU GLY PHE LEU ILE PRO LEU SER VAL MET CYS PHE SEQRES 17 A 342 PHE TYR TYR LYS MET VAL VAL PHE LEU LYS LYS ARG SER SEQRES 18 A 342 GLN GLN GLN ALA THR VAL LEU SER LEU ASN LYS PRO LEU SEQRES 19 A 342 ARG LEU VAL VAL LEU ALA VAL VAL ILE PHE SER VAL LEU SEQRES 20 A 342 PHE THR PRO TYR HIS ILE MET ARG ASN VAL ARG ILE ALA SEQRES 21 A 342 SER ARG LEU ASP SER TRP PRO GLN GLY CYS SER GLN LYS SEQRES 22 A 342 ALA ILE ASN CYS LEU TYR ILE LEU THR ARG PRO LEU ALA SEQRES 23 A 342 PHE LEU ASN SER ALA VAL ASN PRO ILE PHE TYR PHE LEU SEQRES 24 A 342 VAL GLY ASP HIS PHE ARG ASP MET LEU PHE SER LYS LEU SEQRES 25 A 342 ARG GLN TYR PHE LYS SER LEU THR SER PHE ARG LEU LEU SEQRES 26 A 342 GLU VAL LEU PHE GLN GLY PRO HIS HIS HIS HIS HIS HIS SEQRES 27 A 342 HIS HIS HIS HIS SEQRES 1 B 142 ASP TYR LYS ASP ASP ASP ASP LYS GLU VAL GLN LEU VAL SEQRES 2 B 142 GLU SER GLY GLY GLY LEU VAL GLN PRO GLY GLY SER LEU SEQRES 3 B 142 ARG LEU SER CYS GLU ALA SER GLY TYR THR LEU ALA ASN SEQRES 4 B 142 TYR ALA ILE GLY TRP PHE ARG GLN ALA PRO GLY LYS GLU SEQRES 5 B 142 ARG GLU GLY VAL SER CYS ILE SER SER GLY GLY SER THR SEQRES 6 B 142 VAL TYR SER GLU SER VAL LYS ASP ARG PHE THR ILE SER SEQRES 7 B 142 ARG ASP ASN ALA LYS LYS ILE VAL TYR LEU GLN MET ASN SEQRES 8 B 142 SER LEU GLN PRO GLU ASP THR ALA VAL TYR TYR CYS ALA SEQRES 9 B 142 ALA ASP PRO PHE GLY GLU ARG LEU CYS ILE ASP PRO ASN SEQRES 10 B 142 THR PHE ALA GLY TYR LEU GLU THR TRP GLY GLN GLY THR SEQRES 11 B 142 GLN VAL THR VAL SER SER LEU GLU VAL LEU PHE GLN HET Q4T A 401 36 HET OLC A 402 19 HET OLC A 403 19 HET OLC A 404 15 HET OLC A 405 21 HET OLC A 406 14 HET OLC A 407 25 HET OLC A 408 10 HET OLC A 409 12 HET OLC A 410 11 HET OLC A 411 25 HET OLC A 412 17 HET OLC A 413 25 HET SO4 A 414 5 HET CL A 415 1 HETNAM Q4T 2-[2-[[3-[4-CHLORANYL-2-FLUORANYL-5-[(3~{R})-PIPERIDIN- HETNAM 2 Q4T 3-YL]OXY-PHENYL]-2-FLUORANYL-PHENYL]CARBONYLAMINO]-5- HETNAM 3 Q4T FLUORANYL-PHENYL]ETHANOIC ACID HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM SO4 SULFATE ION HETNAM CL CHLORIDE ION HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 3 Q4T C26 H22 CL F3 N2 O4 FORMUL 4 OLC 12(C21 H40 O4) FORMUL 16 SO4 O4 S 2- FORMUL 17 CL CL 1- FORMUL 18 HOH *154(H2 O) HELIX 1 AA1 CYS A 7 TYR A 20 1 14 HELIX 2 AA2 TYR A 20 MET A 48 1 29 HELIX 3 AA3 ASN A 52 GLY A 82 1 31 HELIX 4 AA4 GLY A 87 PHE A 122 1 36 HELIX 5 AA5 HIS A 127 GLN A 130 5 4 HELIX 6 AA6 LYS A 131 THR A 160 1 30 HELIX 7 AA7 PRO A 161 GLY A 165 5 5 HELIX 8 AA8 ASN A 176 PHE A 192 1 17 HELIX 9 AA9 PHE A 192 SER A 214 1 23 HELIX 10 AB1 LYS A 225 SER A 254 1 30 HELIX 11 AB2 CYS A 263 LEU A 281 1 19 HELIX 12 AB3 LEU A 281 ASN A 286 1 6 HELIX 13 AB4 PRO A 287 LEU A 292 5 6 HELIX 14 AB5 HIS A 296 LYS A 304 1 9 HELIX 15 AB6 GLN B 94 THR B 98 5 5 HELIX 16 AB7 ARG B 111 ILE B 114 5 4 HELIX 17 AB8 ASP B 115 ALA B 120 1 6 HELIX 18 AB9 GLY B 121 LEU B 123 5 3 SHEET 1 AA1 4 GLN B 11 SER B 15 0 SHEET 2 AA1 4 LEU B 26 SER B 33 -1 O GLU B 31 N VAL B 13 SHEET 3 AA1 4 ILE B 85 MET B 90 -1 O MET B 90 N LEU B 26 SHEET 4 AA1 4 PHE B 75 ASP B 80 -1 N THR B 76 O GLN B 89 SHEET 1 AA2 6 LEU B 19 VAL B 20 0 SHEET 2 AA2 6 THR B 130 VAL B 134 1 O THR B 133 N VAL B 20 SHEET 3 AA2 6 ALA B 99 ASP B 106 -1 N TYR B 101 O THR B 130 SHEET 4 AA2 6 ALA B 41 GLN B 47 -1 N PHE B 45 O TYR B 102 SHEET 5 AA2 6 GLU B 54 ILE B 59 -1 O SER B 57 N TRP B 44 SHEET 6 AA2 6 THR B 65 TYR B 67 -1 O VAL B 66 N CYS B 58 SHEET 1 AA3 4 LEU B 19 VAL B 20 0 SHEET 2 AA3 4 THR B 130 VAL B 134 1 O THR B 133 N VAL B 20 SHEET 3 AA3 4 ALA B 99 ASP B 106 -1 N TYR B 101 O THR B 130 SHEET 4 AA3 4 THR B 125 TRP B 126 -1 O THR B 125 N ALA B 105 SSBOND 1 CYS A 7 CYS A 263 1555 1555 2.04 SSBOND 2 CYS A 91 CYS A 168 1555 1555 2.05 SSBOND 3 CYS B 30 CYS B 103 1555 1555 2.04 SSBOND 4 CYS B 58 CYS B 113 1555 1555 2.07 SITE 1 AC1 13 TYR A 26 LEU A 75 SER A 78 TYR A 79 SITE 2 AC1 13 TRP A 84 ASN A 94 ARG A 95 LEU A 98 SITE 3 AC1 13 CYS A 168 TYR A 244 ARG A 276 PHE A 280 SITE 4 AC1 13 HOH A 523 SITE 1 AC2 9 TYR A 57 PHE A 111 ASP A 115 LEU A 118 SITE 2 AC2 9 LEU A 129 PHE A 134 ILE A 138 OLC A 403 SITE 3 AC2 9 OLC A 407 SITE 1 AC3 8 TYR A 117 LEU A 118 LYS A 121 LEU A 137 SITE 2 AC3 8 PHE A 202 OLC A 402 OLC A 407 HOH A 527 SITE 1 AC4 6 PHE A 156 THR A 158 ASN A 176 TYR A 179 SITE 2 AC4 6 SER A 180 TYR A 183 SITE 1 AC5 6 LYS A 49 TRP A 51 ASN A 60 LYS A 132 SITE 2 AC5 6 TRP A 143 OLC A 408 SITE 1 AC6 5 ILE A 63 CYS A 70 SER A 93 ASN A 94 SITE 2 AC6 5 OLC A 413 SITE 1 AC7 8 VAL A 144 LEU A 145 ILE A 194 SER A 197 SITE 2 AC7 8 VAL A 198 TYR A 204 OLC A 402 OLC A 403 SITE 1 AC8 4 LEU A 45 MET A 48 TRP A 51 OLC A 405 SITE 1 AC9 5 LEU A 185 THR A 188 HIS A 245 ASN A 249 SITE 2 AC9 5 ALA A 253 SITE 1 AD1 4 LYS A 178 LEU A 181 ILE A 182 LEU A 185 SITE 1 AD2 7 TYR A 21 PHE A 25 MET A 247 ILE A 268 SITE 2 AD2 7 LEU A 271 THR A 275 OLC A 412 SITE 1 AD3 6 TRP A 10 TYR A 20 CYS A 263 ALA A 267 SITE 2 AD3 6 OLC A 411 HOH A 533 SITE 1 AD4 9 TYR A 86 GLY A 87 ASP A 88 VAL A 89 SITE 2 AD4 9 LEU A 90 TYR A 96 VAL A 97 OLC A 406 SITE 3 AD4 9 GLY B 17 SITE 1 AD5 3 HIS A 127 ILE A 128 LEU A 129 SITE 1 AD6 1 SER A 174 CRYST1 76.839 151.003 68.211 90.00 112.29 90.00 C 1 2 1 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 0.013014 0.000000 0.005335 0.00000 SCALE2 0.000000 0.006622 0.000000 0.00000 SCALE3 0.000000 0.000000 0.015844 0.00000 ATOM 1 N CYS A 7 -8.297 -7.465 2.989 1.00 83.54 N ANISOU 1 N CYS A 7 12577 8378 10785 117 205 -887 N ATOM 2 CA CYS A 7 -7.875 -6.087 2.736 1.00 83.94 C ANISOU 2 CA CYS A 7 12639 8524 10733 148 226 -841 C ATOM 3 C CYS A 7 -6.379 -5.925 2.976 1.00 83.11 C ANISOU 3 C CYS A 7 12549 8476 10554 206 396 -782 C ATOM 4 O CYS A 7 -5.943 -4.947 3.582 1.00 83.17 O ANISOU 4 O CYS A 7 12472 8569 10559 213 460 -712 O ATOM 5 CB CYS A 7 -8.686 -5.119 3.588 1.00 85.65 C ANISOU 5 CB CYS A 7 12698 8798 11047 99 179 -793 C ATOM 6 SG CYS A 7 -10.475 -5.289 3.382 1.00 92.24 S ANISOU 6 SG CYS A 7 13478 9562 12009 28 -17 -870 S ATOM 7 N GLU A 8 -5.601 -6.896 2.484 1.00 82.18 N ANISOU 7 N GLU A 8 12536 8305 10385 249 465 -817 N ATOM 8 CA GLU A 8 -4.145 -6.991 2.590 1.00 81.59 C ANISOU 8 CA GLU A 8 12479 8262 10259 312 625 -781 C ATOM 9 C GLU A 8 -3.437 -5.786 1.944 1.00 79.78 C ANISOU 9 C GLU A 8 12310 8100 9903 349 684 -757 C ATOM 10 O GLU A 8 -2.365 -5.376 2.404 1.00 79.42 O ANISOU 10 O GLU A 8 12203 8113 9859 382 812 -704 O ATOM 11 CB GLU A 8 -3.662 -8.305 1.932 1.00 85.16 C ANISOU 11 CB GLU A 8 13055 8624 10676 350 665 -845 C ATOM 12 CG GLU A 8 -4.454 -9.560 2.299 1.00 92.33 C ANISOU 12 CG GLU A 8 13945 9441 11696 310 593 -886 C ATOM 13 CD GLU A 8 -5.775 -9.787 1.575 1.00101.16 C ANISOU 13 CD GLU A 8 15126 10491 12821 259 425 -964 C ATOM 14 OE1 GLU A 8 -5.814 -9.636 0.332 1.00103.45 O ANISOU 14 OE1 GLU A 8 15571 10754 12983 285 368 -1026 O ATOM 15 OE2 GLU A 8 -6.781 -10.090 2.259 1.00103.48 O ANISOU 15 OE2 GLU A 8 15313 10754 13249 195 349 -964 O ATOM 16 N ASN A 9 -4.038 -5.238 0.863 1.00 78.26 N ANISOU 16 N ASN A 9 12241 7891 9604 344 588 -800 N ATOM 17 CA ASN A 9 -3.507 -4.087 0.132 1.00 77.04 C ANISOU 17 CA ASN A 9 12174 7781 9315 376 637 -779 C ATOM 18 C ASN A 9 -3.621 -2.822 0.948 1.00 74.74 C ANISOU 18 C ASN A 9 11742 7582 9076 349 641 -703 C ATOM 19 O ASN A 9 -2.686 -2.027 0.975 1.00 74.77 O ANISOU 19 O ASN A 9 11734 7641 9035 375 759 -657 O ATOM 20 CB ASN A 9 -4.181 -3.910 -1.246 1.00 78.71 C ANISOU 20 CB ASN A 9 12582 7936 9388 385 517 -846 C ATOM 21 CG ASN A 9 -5.694 -3.804 -1.250 1.00 82.73 C ANISOU 21 CG ASN A 9 13060 8420 9955 336 310 -882 C ATOM 22 OD1 ASN A 9 -6.402 -4.351 -0.391 1.00 84.21 O ANISOU 22 OD1 ASN A 9 13104 8595 10296 287 249 -884 O ATOM 23 ND2 ASN A 9 -6.228 -3.120 -2.250 1.00 83.83 N ANISOU 23 ND2 ASN A 9 13339 8538 9974 349 196 -915 N ATOM 24 N TRP A 10 -4.758 -2.641 1.625 1.00 72.72 N ANISOU 24 N TRP A 10 11373 7337 8923 296 520 -694 N ATOM 25 CA TRP A 10 -4.997 -1.482 2.481 1.00 71.34 C ANISOU 25 CA TRP A 10 11058 7242 8806 268 514 -627 C ATOM 26 C TRP A 10 -4.154 -1.538 3.751 1.00 70.55 C ANISOU 26 C TRP A 10 10811 7197 8798 272 639 -563 C ATOM 27 O TRP A 10 -3.715 -0.498 4.242 1.00 70.62 O ANISOU 27 O TRP A 10 10745 7278 8810 275 694 -506 O ATOM 28 CB TRP A 10 -6.489 -1.332 2.784 1.00 70.82 C ANISOU 28 CB TRP A 10 10917 7160 8831 213 354 -646 C ATOM 29 CG TRP A 10 -7.282 -0.950 1.571 1.00 70.82 C ANISOU 29 CG TRP A 10 11051 7119 8738 217 211 -703 C ATOM 30 CD1 TRP A 10 -8.038 -1.775 0.792 1.00 71.62 C ANISOU 30 CD1 TRP A 10 11248 7135 8830 211 84 -787 C ATOM 31 CD2 TRP A 10 -7.322 0.341 0.944 1.00 70.60 C ANISOU 31 CD2 TRP A 10 11095 7126 8604 237 176 -683 C ATOM 32 NE1 TRP A 10 -8.573 -1.071 -0.264 1.00 71.85 N ANISOU 32 NE1 TRP A 10 11406 7145 8751 230 -41 -823 N ATOM 33 CE2 TRP A 10 -8.163 0.235 -0.183 1.00 71.34 C ANISOU 33 CE2 TRP A 10 11331 7152 8622 247 15 -756 C ATOM 34 CE3 TRP A 10 -6.754 1.586 1.246 1.00 70.89 C ANISOU 34 CE3 TRP A 10 11092 7238 8606 248 258 -613 C ATOM 35 CZ2 TRP A 10 -8.451 1.325 -1.003 1.00 71.68 C ANISOU 35 CZ2 TRP A 10 11486 7199 8549 272 -67 -755 C ATOM 36 CZ3 TRP A 10 -7.042 2.661 0.433 1.00 71.58 C ANISOU 36 CZ3 TRP A 10 11285 7329 8584 266 189 -610 C ATOM 37 CH2 TRP A 10 -7.869 2.523 -0.686 1.00 71.76 C ANISOU 37 CH2 TRP A 10 11460 7282 8523 282 29 -678 C ATOM 38 N LEU A 11 -3.856 -2.751 4.235 1.00 69.64 N ANISOU 38 N LEU A 11 10669 7041 8751 280 683 -574 N ATOM 39 CA LEU A 11 -2.980 -2.956 5.379 1.00 69.36 C ANISOU 39 CA LEU A 11 10518 7043 8791 298 790 -520 C ATOM 40 C LEU A 11 -1.525 -2.594 4.987 1.00 68.22 C ANISOU 40 C LEU A 11 10410 6934 8578 356 923 -507 C ATOM 41 O LEU A 11 -0.808 -2.007 5.786 1.00 68.48 O ANISOU 41 O LEU A 11 10338 7028 8653 370 992 -455 O ATOM 42 CB LEU A 11 -3.106 -4.409 5.871 1.00 69.99 C ANISOU 42 CB LEU A 11 10587 7055 8953 297 792 -540 C ATOM 43 CG LEU A 11 -2.347 -4.813 7.137 1.00 72.18 C ANISOU 43 CG LEU A 11 10761 7353 9312 322 877 -486 C ATOM 44 CD1 LEU A 11 -2.608 -3.855 8.299 1.00 72.75 C ANISOU 44 CD1 LEU A 11 10701 7498 9441 295 869 -419 C ATOM 45 CD2 LEU A 11 -2.715 -6.227 7.535 1.00 73.01 C ANISOU 45 CD2 LEU A 11 10877 7373 9490 314 864 -506 C ATOM 46 N ALA A 12 -1.121 -2.873 3.741 1.00 66.91 N ANISOU 46 N ALA A 12 10393 6723 8307 389 958 -557 N ATOM 47 CA ALA A 12 0.188 -2.498 3.219 1.00 65.93 C ANISOU 47 CA ALA A 12 10312 6619 8120 439 1099 -552 C ATOM 48 C ALA A 12 0.288 -0.961 3.161 1.00 65.38 C ANISOU 48 C ALA A 12 10214 6619 8009 424 1117 -507 C ATOM 49 O ALA A 12 1.336 -0.411 3.489 1.00 65.96 O ANISOU 49 O ALA A 12 10216 6738 8109 446 1231 -474 O ATOM 50 CB ALA A 12 0.384 -3.090 1.831 1.00 65.54 C ANISOU 50 CB ALA A 12 10454 6497 7952 472 1128 -619 C ATOM 51 N LEU A 13 -0.806 -0.271 2.768 1.00 63.96 N ANISOU 51 N LEU A 13 10083 6441 7777 387 999 -509 N ATOM 52 CA LEU A 13 -0.846 1.189 2.713 1.00 62.88 C ANISOU 52 CA LEU A 13 9929 6361 7602 372 1001 -467 C ATOM 53 C LEU A 13 -0.767 1.756 4.122 1.00 62.70 C ANISOU 53 C LEU A 13 9713 6410 7700 348 1008 -407 C ATOM 54 O LEU A 13 0.036 2.649 4.336 1.00 63.31 O ANISOU 54 O LEU A 13 9739 6536 7780 357 1097 -370 O ATOM 55 CB LEU A 13 -2.098 1.709 1.978 1.00 62.21 C ANISOU 55 CB LEU A 13 9943 6252 7440 347 853 -488 C ATOM 56 CG LEU A 13 -2.326 3.234 1.982 1.00 62.11 C ANISOU 56 CG LEU A 13 9912 6291 7395 330 832 -441 C ATOM 57 CD1 LEU A 13 -1.223 3.947 1.314 1.00 62.37 C ANISOU 57 CD1 LEU A 13 10032 6332 7333 360 975 -421 C ATOM 58 CD2 LEU A 13 -3.618 3.597 1.305 1.00 61.95 C ANISOU 58 CD2 LEU A 13 9984 6238 7316 315 663 -470 C ATOM 59 N GLU A 14 -1.544 1.215 5.094 1.00 61.72 N ANISOU 59 N GLU A 14 9487 6286 7676 319 925 -400 N ATOM 60 CA GLU A 14 -1.524 1.670 6.495 1.00 60.99 C ANISOU 60 CA GLU A 14 9230 6254 7688 301 930 -346 C ATOM 61 C GLU A 14 -0.113 1.587 7.061 1.00 60.31 C ANISOU 61 C GLU A 14 9074 6198 7641 342 1055 -322 C ATOM 62 O GLU A 14 0.338 2.540 7.681 1.00 60.47 O ANISOU 62 O GLU A 14 9004 6278 7693 340 1090 -282 O ATOM 63 CB GLU A 14 -2.443 0.808 7.388 1.00 63.11 C ANISOU 63 CB GLU A 14 9431 6496 8052 271 855 -347 C ATOM 64 CG GLU A 14 -3.926 1.122 7.370 1.00 68.65 C ANISOU 64 CG GLU A 14 10119 7185 8779 219 729 -358 C ATOM 65 CD GLU A 14 -4.804 0.158 8.154 1.00 76.91 C ANISOU 65 CD GLU A 14 11104 8188 9929 184 679 -366 C ATOM 66 OE1 GLU A 14 -4.447 -1.036 8.257 1.00 78.62 O ANISOU 66 OE1 GLU A 14 11348 8356 10169 201 716 -383 O ATOM 67 OE2 GLU A 14 -5.859 0.598 8.663 1.00 80.49 O ANISOU 67 OE2 GLU A 14 11483 8650 10447 140 609 -356 O ATOM 68 N ASN A 15 0.586 0.455 6.829 1.00 59.75 N ANISOU 68 N ASN A 15 9043 6082 7576 382 1116 -352 N ATOM 69 CA ASN A 15 1.936 0.228 7.336 1.00 59.96 C ANISOU 69 CA ASN A 15 8997 6126 7658 430 1223 -341 C ATOM 70 C ASN A 15 2.937 1.202 6.742 1.00 59.11 C ANISOU 70 C ASN A 15 8895 6050 7513 447 1329 -337 C ATOM 71 O ASN A 15 3.722 1.782 7.488 1.00 59.16 O ANISOU 71 O ASN A 15 8785 6104 7589 460 1378 -309 O ATOM 72 CB ASN A 15 2.380 -1.231 7.124 1.00 62.35 C ANISOU 72 CB ASN A 15 9351 6363 7977 472 1260 -380 C ATOM 73 CG ASN A 15 1.630 -2.255 7.961 1.00 67.63 C ANISOU 73 CG ASN A 15 9993 6994 8709 459 1180 -375 C ATOM 74 OD1 ASN A 15 1.099 -1.962 9.040 1.00 70.18 O ANISOU 74 OD1 ASN A 15 10228 7348 9089 430 1125 -333 O ATOM 75 ND2 ASN A 15 1.548 -3.484 7.475 1.00 68.71 N ANISOU 75 ND2 ASN A 15 10216 7056 8836 477 1180 -419 N ATOM 76 N ILE A 16 2.883 1.411 5.410 1.00 58.27 N ANISOU 76 N ILE A 16 8931 5911 7297 447 1362 -368 N ATOM 77 CA ILE A 16 3.745 2.345 4.679 1.00 58.02 C ANISOU 77 CA ILE A 16 8937 5893 7216 458 1481 -364 C ATOM 78 C ILE A 16 3.490 3.796 5.120 1.00 58.48 C ANISOU 78 C ILE A 16 8921 6012 7285 420 1453 -315 C ATOM 79 O ILE A 16 4.447 4.556 5.280 1.00 59.26 O ANISOU 79 O ILE A 16 8949 6143 7426 426 1553 -297 O ATOM 80 CB ILE A 16 3.628 2.139 3.135 1.00 58.11 C ANISOU 80 CB ILE A 16 9153 5841 7084 470 1517 -406 C ATOM 81 CG1 ILE A 16 4.491 0.955 2.678 1.00 59.40 C ANISOU 81 CG1 ILE A 16 9370 5949 7251 522 1619 -455 C ATOM 82 CG2 ILE A 16 4.038 3.363 2.357 1.00 58.46 C ANISOU 82 CG2 ILE A 16 9269 5895 7048 463 1609 -389 C ATOM 83 CD1 ILE A 16 4.037 0.275 1.359 1.00 60.46 C ANISOU 83 CD1 ILE A 16 9720 6007 7248 536 1604 -509 C ATOM 84 N LEU A 17 2.215 4.186 5.309 1.00 57.45 N ANISOU 84 N LEU A 17 8804 5896 7130 380 1319 -298 N ATOM 85 CA LEU A 17 1.882 5.542 5.730 1.00 56.87 C ANISOU 85 CA LEU A 17 8666 5874 7068 346 1284 -255 C ATOM 86 C LEU A 17 2.458 5.831 7.111 1.00 58.37 C ANISOU 86 C LEU A 17 8677 6121 7380 346 1305 -222 C ATOM 87 O LEU A 17 2.982 6.920 7.339 1.00 58.76 O ANISOU 87 O LEU A 17 8665 6209 7453 337 1354 -196 O ATOM 88 CB LEU A 17 0.359 5.783 5.738 1.00 55.37 C ANISOU 88 CB LEU A 17 8506 5681 6849 309 1131 -251 C ATOM 89 CG LEU A 17 -0.336 5.882 4.406 1.00 54.05 C ANISOU 89 CG LEU A 17 8516 5464 6557 308 1074 -280 C ATOM 90 CD1 LEU A 17 -1.807 6.111 4.592 1.00 53.24 C ANISOU 90 CD1 LEU A 17 8401 5360 6466 275 912 -282 C ATOM 91 CD2 LEU A 17 0.300 6.948 3.526 1.00 54.45 C ANISOU 91 CD2 LEU A 17 8663 5512 6512 318 1166 -264 C ATOM 92 N GLU A 18 2.381 4.854 8.032 1.00 58.82 N ANISOU 92 N GLU A 18 8660 6177 7513 360 1265 -225 N ATOM 93 CA GLU A 18 2.913 5.042 9.381 1.00 59.52 C ANISOU 93 CA GLU A 18 8599 6311 7704 370 1268 -196 C ATOM 94 C GLU A 18 4.426 5.064 9.395 1.00 60.32 C ANISOU 94 C GLU A 18 8640 6419 7860 411 1383 -208 C ATOM 95 O GLU A 18 5.021 5.984 9.952 1.00 61.02 O ANISOU 95 O GLU A 18 8630 6551 8004 408 1410 -189 O ATOM 96 CB GLU A 18 2.381 3.970 10.323 1.00 61.64 C ANISOU 96 CB GLU A 18 8831 6563 8024 376 1197 -192 C ATOM 97 CG GLU A 18 0.896 4.103 10.580 1.00 67.26 C ANISOU 97 CG GLU A 18 9559 7274 8723 328 1091 -178 C ATOM 98 CD GLU A 18 0.291 3.037 11.469 1.00 76.44 C ANISOU 98 CD GLU A 18 10699 8408 9938 326 1040 -173 C ATOM 99 OE1 GLU A 18 1.035 2.136 11.923 1.00 80.07 O ANISOU 99 OE1 GLU A 18 11140 8846 10436 368 1077 -176 O ATOM 100 OE2 GLU A 18 -0.936 3.104 11.707 1.00 78.14 O ANISOU 100 OE2 GLU A 18 10914 8614 10162 283 966 -166 O ATOM 101 N LYS A 19 5.051 4.087 8.740 1.00 60.15 N ANISOU 101 N LYS A 19 8674 6350 7829 450 1453 -245 N ATOM 102 CA LYS A 19 6.497 3.965 8.702 1.00 60.68 C ANISOU 102 CA LYS A 19 8676 6414 7967 495 1569 -267 C ATOM 103 C LYS A 19 7.208 5.078 7.915 1.00 60.98 C ANISOU 103 C LYS A 19 8721 6460 7988 480 1686 -270 C ATOM 104 O LYS A 19 8.248 5.561 8.362 1.00 61.46 O ANISOU 104 O LYS A 19 8661 6544 8149 494 1751 -272 O ATOM 105 CB LYS A 19 6.875 2.570 8.170 1.00 62.74 C ANISOU 105 CB LYS A 19 9003 6612 8221 542 1615 -309 C ATOM 106 CG LYS A 19 8.350 2.238 8.227 1.00 68.14 C ANISOU 106 CG LYS A 19 9604 7285 9003 599 1726 -339 C ATOM 107 CD LYS A 19 8.553 0.715 8.198 1.00 74.82 C ANISOU 107 CD LYS A 19 10487 8074 9868 652 1726 -373 C ATOM 108 CE LYS A 19 10.001 0.286 8.006 1.00 79.97 C ANISOU 108 CE LYS A 19 11072 8699 10615 716 1848 -415 C ATOM 109 NZ LYS A 19 10.871 0.644 9.166 1.00 83.15 N ANISOU 109 NZ LYS A 19 11294 9141 11160 748 1827 -405 N ATOM 110 N TYR A 20 6.664 5.485 6.755 1.00 60.46 N ANISOU 110 N TYR A 20 8801 6369 7801 453 1710 -271 N ATOM 111 CA TYR A 20 7.324 6.448 5.878 1.00 60.42 C ANISOU 111 CA TYR A 20 8840 6354 7762 440 1841 -271 C ATOM 112 C TYR A 20 6.673 7.830 5.770 1.00 59.13 C ANISOU 112 C TYR A 20 8705 6219 7543 390 1801 -231 C ATOM 113 O TYR A 20 7.395 8.828 5.816 1.00 59.58 O ANISOU 113 O TYR A 20 8699 6292 7649 374 1889 -217 O ATOM 114 CB TYR A 20 7.495 5.845 4.479 1.00 61.49 C ANISOU 114 CB TYR A 20 9151 6422 7790 462 1938 -308 C ATOM 115 CG TYR A 20 8.353 4.594 4.474 1.00 63.47 C ANISOU 115 CG TYR A 20 9372 6639 8107 517 2012 -353 C ATOM 116 CD1 TYR A 20 9.739 4.677 4.468 1.00 64.54 C ANISOU 116 CD1 TYR A 20 9409 6766 8346 545 2166 -375 C ATOM 117 CD2 TYR A 20 7.775 3.330 4.481 1.00 64.99 C ANISOU 117 CD2 TYR A 20 9624 6799 8268 540 1929 -377 C ATOM 118 CE1 TYR A 20 10.528 3.538 4.480 1.00 65.85 C ANISOU 118 CE1 TYR A 20 9539 6897 8584 602 2229 -419 C ATOM 119 CE2 TYR A 20 8.553 2.183 4.496 1.00 66.15 C ANISOU 119 CE2 TYR A 20 9745 6909 8478 594 1993 -417 C ATOM 120 CZ TYR A 20 9.932 2.291 4.484 1.00 67.61 C ANISOU 120 CZ TYR A 20 9835 7089 8764 628 2142 -438 C ATOM 121 OH TYR A 20 10.713 1.155 4.489 1.00 70.40 O ANISOU 121 OH TYR A 20 10157 7401 9190 689 2204 -483 O ATOM 122 N TYR A 21 5.349 7.911 5.603 1.00 57.44 N ANISOU 122 N TYR A 21 8583 6005 7239 366 1672 -216 N ATOM 123 CA TYR A 21 4.690 9.211 5.490 1.00 56.67 C ANISOU 123 CA TYR A 21 8514 5926 7090 326 1625 -179 C ATOM 124 C TYR A 21 4.744 9.993 6.809 1.00 55.65 C ANISOU 124 C TYR A 21 8212 5861 7073 304 1577 -148 C ATOM 125 O TYR A 21 5.161 11.139 6.795 1.00 55.10 O ANISOU 125 O TYR A 21 8110 5805 7020 283 1634 -127 O ATOM 126 CB TYR A 21 3.257 9.077 4.930 1.00 56.64 C ANISOU 126 CB TYR A 21 8646 5900 6975 313 1490 -181 C ATOM 127 CG TYR A 21 2.401 10.330 5.042 1.00 57.14 C ANISOU 127 CG TYR A 21 8716 5988 7009 278 1404 -144 C ATOM 128 CD1 TYR A 21 2.450 11.316 4.070 1.00 57.43 C ANISOU 128 CD1 TYR A 21 8878 5996 6946 271 1455 -128 C ATOM 129 CD2 TYR A 21 1.482 10.481 6.073 1.00 57.70 C ANISOU 129 CD2 TYR A 21 8681 6098 7143 256 1274 -127 C ATOM 130 CE1 TYR A 21 1.642 12.439 4.142 1.00 58.16 C ANISOU 130 CE1 TYR A 21 8984 6102 7011 246 1369 -95 C ATOM 131 CE2 TYR A 21 0.689 11.611 6.169 1.00 58.57 C ANISOU 131 CE2 TYR A 21 8793 6226 7234 230 1198 -98 C ATOM 132 CZ TYR A 21 0.769 12.592 5.199 1.00 59.23 C ANISOU 132 CZ TYR A 21 8997 6283 7224 226 1239 -83 C ATOM 133 OH TYR A 21 -0.032 13.711 5.274 1.00 60.05 O ANISOU 133 OH TYR A 21 9107 6397 7311 206 1156 -55 O ATOM 134 N LEU A 22 4.330 9.374 7.941 1.00 55.38 N ANISOU 134 N LEU A 22 8077 5855 7109 310 1477 -146 N ATOM 135 CA LEU A 22 4.331 10.011 9.264 1.00 55.08 C ANISOU 135 CA LEU A 22 7892 5872 7164 296 1423 -119 C ATOM 136 C LEU A 22 5.752 10.345 9.735 1.00 56.13 C ANISOU 136 C LEU A 22 7902 6023 7402 314 1519 -128 C ATOM 137 O LEU A 22 5.982 11.450 10.198 1.00 56.42 O ANISOU 137 O LEU A 22 7862 6090 7483 291 1523 -110 O ATOM 138 CB LEU A 22 3.564 9.172 10.315 1.00 54.48 C ANISOU 138 CB LEU A 22 7765 5811 7125 302 1310 -114 C ATOM 139 CG LEU A 22 2.046 8.985 10.096 1.00 54.64 C ANISOU 139 CG LEU A 22 7864 5816 7081 275 1201 -109 C ATOM 140 CD1 LEU A 22 1.402 8.275 11.252 1.00 54.10 C ANISOU 140 CD1 LEU A 22 7730 5757 7068 275 1120 -100 C ATOM 141 CD2 LEU A 22 1.335 10.311 9.893 1.00 55.02 C ANISOU 141 CD2 LEU A 22 7930 5883 7091 239 1158 -84 C ATOM 142 N SER A 23 6.719 9.428 9.547 1.00 56.77 N ANISOU 142 N SER A 23 7963 6079 7529 354 1598 -161 N ATOM 143 CA SER A 23 8.126 9.650 9.896 1.00 57.70 C ANISOU 143 CA SER A 23 7953 6204 7768 376 1689 -182 C ATOM 144 C SER A 23 8.717 10.874 9.202 1.00 58.44 C ANISOU 144 C SER A 23 8050 6288 7865 343 1807 -178 C ATOM 145 O SER A 23 9.389 11.677 9.852 1.00 59.32 O ANISOU 145 O SER A 23 8032 6425 8081 331 1824 -178 O ATOM 146 CB SER A 23 8.959 8.429 9.536 1.00 59.95 C ANISOU 146 CB SER A 23 8239 6450 8091 429 1765 -223 C ATOM 147 OG SER A 23 8.555 7.312 10.311 1.00 64.62 O ANISOU 147 OG SER A 23 8815 7042 8695 463 1661 -225 O ATOM 148 N ALA A 24 8.478 11.019 7.878 1.00 57.60 N ANISOU 148 N ALA A 24 8100 6139 7645 328 1889 -176 N ATOM 149 CA ALA A 24 8.977 12.146 7.090 1.00 56.54 C ANISOU 149 CA ALA A 24 8007 5982 7495 296 2018 -166 C ATOM 150 C ALA A 24 8.277 13.477 7.447 1.00 55.33 C ANISOU 150 C ALA A 24 7847 5858 7317 249 1944 -123 C ATOM 151 O ALA A 24 8.965 14.462 7.715 1.00 55.83 O ANISOU 151 O ALA A 24 7818 5928 7466 223 2009 -118 O ATOM 152 CB ALA A 24 8.835 11.848 5.602 1.00 56.60 C ANISOU 152 CB ALA A 24 8215 5928 7362 302 2115 -173 C ATOM 153 N PHE A 25 6.925 13.499 7.486 1.00 53.42 N ANISOU 153 N PHE A 25 7691 5630 6976 238 1806 -98 N ATOM 154 CA PHE A 25 6.149 14.696 7.797 1.00 51.93 C ANISOU 154 CA PHE A 25 7503 5465 6762 201 1727 -60 C ATOM 155 C PHE A 25 6.442 15.182 9.234 1.00 50.88 C ANISOU 155 C PHE A 25 7185 5386 6761 192 1670 -57 C ATOM 156 O PHE A 25 6.701 16.370 9.424 1.00 50.66 O ANISOU 156 O PHE A 25 7111 5365 6773 161 1698 -41 O ATOM 157 CB PHE A 25 4.646 14.441 7.550 1.00 51.27 C ANISOU 157 CB PHE A 25 7534 5380 6568 199 1587 -46 C ATOM 158 CG PHE A 25 3.800 15.609 7.059 1.00 51.17 C ANISOU 158 CG PHE A 25 7617 5356 6471 172 1540 -12 C ATOM 159 CD1 PHE A 25 4.011 16.894 7.532 1.00 51.57 C ANISOU 159 CD1 PHE A 25 7595 5425 6574 143 1557 13 C ATOM 160 CD2 PHE A 25 2.724 15.400 6.217 1.00 51.31 C ANISOU 160 CD2 PHE A 25 7789 5341 6366 179 1458 -11 C ATOM 161 CE1 PHE A 25 3.193 17.959 7.127 1.00 51.59 C ANISOU 161 CE1 PHE A 25 7687 5412 6504 124 1505 45 C ATOM 162 CE2 PHE A 25 1.914 16.464 5.815 1.00 51.52 C ANISOU 162 CE2 PHE A 25 7900 5353 6322 163 1395 18 C ATOM 163 CZ PHE A 25 2.145 17.733 6.286 1.00 51.03 C ANISOU 163 CZ PHE A 25 7769 5310 6312 137 1421 48 C ATOM 164 N TYR A 26 6.451 14.280 10.225 1.00 49.93 N ANISOU 164 N TYR A 26 6970 5295 6704 221 1593 -72 N ATOM 165 CA TYR A 26 6.794 14.664 11.592 1.00 49.71 C ANISOU 165 CA TYR A 26 6788 5312 6787 222 1535 -73 C ATOM 166 C TYR A 26 8.259 15.040 11.724 1.00 51.55 C ANISOU 166 C TYR A 26 6904 5539 7144 227 1638 -102 C ATOM 167 O TYR A 26 8.580 15.890 12.532 1.00 52.91 O ANISOU 167 O TYR A 26 6971 5737 7397 211 1609 -102 O ATOM 168 CB TYR A 26 6.384 13.605 12.647 1.00 48.57 C ANISOU 168 CB TYR A 26 6598 5193 6666 256 1425 -78 C ATOM 169 CG TYR A 26 4.885 13.545 12.893 1.00 47.02 C ANISOU 169 CG TYR A 26 6467 5007 6389 239 1314 -50 C ATOM 170 CD1 TYR A 26 4.153 14.701 13.160 1.00 46.38 C ANISOU 170 CD1 TYR A 26 6385 4948 6291 204 1264 -24 C ATOM 171 CD2 TYR A 26 4.202 12.335 12.860 1.00 46.32 C ANISOU 171 CD2 TYR A 26 6437 4903 6260 257 1264 -54 C ATOM 172 CE1 TYR A 26 2.776 14.658 13.340 1.00 46.35 C ANISOU 172 CE1 TYR A 26 6429 4949 6233 189 1169 -5 C ATOM 173 CE2 TYR A 26 2.826 12.282 13.029 1.00 46.60 C ANISOU 173 CE2 TYR A 26 6520 4941 6244 236 1172 -36 C ATOM 174 CZ TYR A 26 2.116 13.446 13.273 1.00 46.95 C ANISOU 174 CZ TYR A 26 6553 5007 6278 203 1125 -12 C ATOM 175 OH TYR A 26 0.755 13.380 13.424 1.00 47.40 O ANISOU 175 OH TYR A 26 6643 5062 6304 184 1039 -1 O ATOM 176 N GLY A 27 9.139 14.426 10.946 1.00 52.27 N ANISOU 176 N GLY A 27 7009 5593 7258 247 1757 -131 N ATOM 177 CA GLY A 27 10.564 14.745 10.966 1.00 53.30 C ANISOU 177 CA GLY A 27 7016 5708 7527 250 1872 -166 C ATOM 178 C GLY A 27 10.808 16.173 10.512 1.00 54.69 C ANISOU 178 C GLY A 27 7195 5866 7717 195 1961 -151 C ATOM 179 O GLY A 27 11.548 16.919 11.161 1.00 55.21 O ANISOU 179 O GLY A 27 7121 5942 7914 179 1972 -169 O ATOM 180 N ILE A 28 10.135 16.590 9.410 1.00 55.00 N ANISOU 180 N ILE A 28 7404 5874 7618 167 2014 -117 N ATOM 181 CA ILE A 28 10.218 17.948 8.853 1.00 55.19 C ANISOU 181 CA ILE A 28 7475 5869 7626 116 2102 -91 C ATOM 182 C ILE A 28 9.637 18.978 9.819 1.00 54.37 C ANISOU 182 C ILE A 28 7304 5806 7549 87 1980 -68 C ATOM 183 O ILE A 28 10.240 20.023 10.029 1.00 54.64 O ANISOU 183 O ILE A 28 7259 5829 7675 51 2037 -71 O ATOM 184 CB ILE A 28 9.554 17.991 7.452 1.00 56.45 C ANISOU 184 CB ILE A 28 7861 5979 7607 109 2163 -60 C ATOM 185 CG1 ILE A 28 10.406 17.203 6.457 1.00 58.42 C ANISOU 185 CG1 ILE A 28 8172 6177 7848 131 2330 -89 C ATOM 186 CG2 ILE A 28 9.354 19.426 6.954 1.00 56.67 C ANISOU 186 CG2 ILE A 28 7970 5975 7588 61 2216 -20 C ATOM 187 CD1 ILE A 28 9.673 16.782 5.222 1.00 60.76 C ANISOU 187 CD1 ILE A 28 8702 6429 7953 146 2348 -72 C ATOM 188 N GLU A 29 8.497 18.655 10.447 1.00 53.36 N ANISOU 188 N GLU A 29 7202 5720 7353 103 1818 -49 N ATOM 189 CA GLU A 29 7.858 19.512 11.447 1.00 52.55 C ANISOU 189 CA GLU A 29 7040 5656 7272 83 1699 -31 C ATOM 190 C GLU A 29 8.756 19.674 12.676 1.00 52.28 C ANISOU 190 C GLU A 29 6820 5652 7392 90 1669 -65 C ATOM 191 O GLU A 29 8.811 20.758 13.239 1.00 51.84 O ANISOU 191 O GLU A 29 6701 5606 7390 61 1643 -62 O ATOM 192 CB GLU A 29 6.504 18.926 11.874 1.00 52.94 C ANISOU 192 CB GLU A 29 7145 5738 7232 103 1551 -11 C ATOM 193 CG GLU A 29 5.433 19.075 10.814 1.00 53.60 C ANISOU 193 CG GLU A 29 7399 5793 7176 92 1536 19 C ATOM 194 CD GLU A 29 4.094 18.453 11.162 1.00 54.32 C ANISOU 194 CD GLU A 29 7531 5907 7203 107 1398 29 C ATOM 195 OE1 GLU A 29 3.944 17.951 12.297 1.00 53.52 O ANISOU 195 OE1 GLU A 29 7334 5843 7158 122 1322 20 O ATOM 196 OE2 GLU A 29 3.179 18.494 10.310 1.00 54.34 O ANISOU 196 OE2 GLU A 29 7663 5883 7101 103 1363 45 O ATOM 197 N PHE A 30 9.445 18.597 13.099 1.00 52.11 N ANISOU 197 N PHE A 30 6717 5641 7441 134 1663 -101 N ATOM 198 CA PHE A 30 10.366 18.654 14.227 1.00 52.71 C ANISOU 198 CA PHE A 30 6623 5738 7664 153 1619 -141 C ATOM 199 C PHE A 30 11.499 19.639 13.929 1.00 54.15 C ANISOU 199 C PHE A 30 6712 5888 7974 115 1737 -169 C ATOM 200 O PHE A 30 11.823 20.442 14.786 1.00 55.31 O ANISOU 200 O PHE A 30 6752 6049 8216 100 1682 -187 O ATOM 201 CB PHE A 30 10.963 17.271 14.532 1.00 52.35 C ANISOU 201 CB PHE A 30 6525 5695 7669 213 1602 -175 C ATOM 202 CG PHE A 30 11.983 17.280 15.652 1.00 52.39 C ANISOU 202 CG PHE A 30 6360 5715 7831 245 1542 -223 C ATOM 203 CD1 PHE A 30 13.339 17.327 15.380 1.00 52.88 C ANISOU 203 CD1 PHE A 30 6302 5746 8044 251 1641 -275 C ATOM 204 CD2 PHE A 30 11.582 17.286 16.974 1.00 52.68 C ANISOU 204 CD2 PHE A 30 6359 5790 7866 270 1388 -221 C ATOM 205 CE1 PHE A 30 14.266 17.374 16.412 1.00 53.29 C ANISOU 205 CE1 PHE A 30 6191 5807 8251 283 1565 -327 C ATOM 206 CE2 PHE A 30 12.514 17.284 18.001 1.00 52.98 C ANISOU 206 CE2 PHE A 30 6258 5836 8037 308 1314 -269 C ATOM 207 CZ PHE A 30 13.846 17.341 17.715 1.00 52.79 C ANISOU 207 CZ PHE A 30 6107 5782 8169 315 1393 -324 C ATOM 208 N ILE A 31 12.098 19.584 12.733 1.00 53.98 N ANISOU 208 N ILE A 31 6735 5817 7959 99 1903 -174 N ATOM 209 CA ILE A 31 13.192 20.488 12.375 1.00 54.26 C ANISOU 209 CA ILE A 31 6682 5808 8126 56 2044 -201 C ATOM 210 C ILE A 31 12.745 21.960 12.277 1.00 55.07 C ANISOU 210 C ILE A 31 6829 5896 8199 -5 2055 -166 C ATOM 211 O ILE A 31 13.315 22.812 12.958 1.00 55.60 O ANISOU 211 O ILE A 31 6764 5962 8398 -33 2039 -193 O ATOM 212 CB ILE A 31 13.903 19.998 11.074 1.00 53.89 C ANISOU 212 CB ILE A 31 6692 5702 8081 56 2243 -213 C ATOM 213 CG1 ILE A 31 14.547 18.611 11.270 1.00 53.76 C ANISOU 213 CG1 ILE A 31 6599 5694 8135 120 2238 -259 C ATOM 214 CG2 ILE A 31 14.919 21.032 10.580 1.00 54.01 C ANISOU 214 CG2 ILE A 31 6638 5658 8223 0 2420 -232 C ATOM 215 CD1 ILE A 31 14.897 17.927 9.978 1.00 54.41 C ANISOU 215 CD1 ILE A 31 6784 5723 8165 132 2411 -265 C ATOM 216 N VAL A 32 11.736 22.252 11.419 1.00 55.13 N ANISOU 216 N VAL A 32 7023 5888 8037 -24 2075 -109 N ATOM 217 CA VAL A 32 11.175 23.591 11.173 1.00 55.22 C ANISOU 217 CA VAL A 32 7110 5876 7994 -73 2084 -68 C ATOM 218 C VAL A 32 10.567 24.212 12.446 1.00 55.69 C ANISOU 218 C VAL A 32 7093 5986 8080 -76 1915 -66 C ATOM 219 O VAL A 32 10.779 25.397 12.729 1.00 55.87 O ANISOU 219 O VAL A 32 7066 5991 8172 -118 1928 -67 O ATOM 220 CB VAL A 32 10.168 23.560 9.990 1.00 55.07 C ANISOU 220 CB VAL A 32 7317 5828 7778 -73 2111 -13 C ATOM 221 CG1 VAL A 32 9.452 24.895 9.831 1.00 54.93 C ANISOU 221 CG1 VAL A 32 7384 5789 7698 -111 2087 32 C ATOM 222 CG2 VAL A 32 10.861 23.154 8.688 1.00 54.90 C ANISOU 222 CG2 VAL A 32 7393 5744 7725 -74 2302 -15 C ATOM 223 N GLY A 33 9.887 23.382 13.231 1.00 55.60 N ANISOU 223 N GLY A 33 7071 6032 8023 -32 1768 -68 N ATOM 224 CA GLY A 33 9.253 23.778 14.481 1.00 56.02 C ANISOU 224 CA GLY A 33 7068 6132 8085 -25 1613 -68 C ATOM 225 C GLY A 33 10.239 24.136 15.569 1.00 56.67 C ANISOU 225 C GLY A 33 6976 6226 8328 -25 1576 -120 C ATOM 226 O GLY A 33 10.060 25.150 16.243 1.00 57.01 O ANISOU 226 O GLY A 33 6979 6276 8406 -49 1516 -122 O ATOM 227 N MET A 34 11.279 23.313 15.768 1.00 56.72 N ANISOU 227 N MET A 34 6878 6233 8439 6 1600 -167 N ATOM 228 CA MET A 34 12.289 23.595 16.788 1.00 57.58 C ANISOU 228 CA MET A 34 6813 6348 8715 14 1548 -227 C ATOM 229 C MET A 34 13.078 24.877 16.463 1.00 59.05 C ANISOU 229 C MET A 34 6925 6486 9026 -49 1651 -249 C ATOM 230 O MET A 34 13.254 25.720 17.341 1.00 58.99 O ANISOU 230 O MET A 34 6831 6484 9099 -66 1572 -277 O ATOM 231 CB MET A 34 13.241 22.403 16.981 1.00 57.91 C ANISOU 231 CB MET A 34 6759 6393 8852 69 1548 -275 C ATOM 232 CG MET A 34 12.632 21.247 17.747 1.00 59.60 C ANISOU 232 CG MET A 34 7012 6651 8981 136 1411 -266 C ATOM 233 SD MET A 34 12.456 21.631 19.500 1.00 65.92 S ANISOU 233 SD MET A 34 7743 7493 9810 166 1214 -289 S ATOM 234 CE MET A 34 12.009 20.064 20.145 1.00 59.21 C ANISOU 234 CE MET A 34 6949 6673 8876 247 1108 -277 C ATOM 235 N LEU A 35 13.542 25.036 15.200 1.00 59.82 N ANISOU 235 N LEU A 35 7064 6528 9137 -87 1835 -237 N ATOM 236 CA LEU A 35 14.293 26.224 14.796 1.00 60.37 C ANISOU 236 CA LEU A 35 7074 6537 9327 -154 1963 -253 C ATOM 237 C LEU A 35 13.443 27.468 14.928 1.00 59.72 C ANISOU 237 C LEU A 35 7072 6448 9171 -197 1920 -211 C ATOM 238 O LEU A 35 13.897 28.469 15.480 1.00 60.51 O ANISOU 238 O LEU A 35 7071 6527 9393 -235 1905 -243 O ATOM 239 CB LEU A 35 14.817 26.090 13.354 1.00 61.69 C ANISOU 239 CB LEU A 35 7312 6640 9490 -182 2185 -237 C ATOM 240 CG LEU A 35 15.929 25.058 13.127 1.00 64.80 C ANISOU 240 CG LEU A 35 7598 7019 10003 -150 2272 -292 C ATOM 241 CD1 LEU A 35 16.216 24.878 11.625 1.00 65.48 C ANISOU 241 CD1 LEU A 35 7804 7041 10036 -172 2500 -266 C ATOM 242 CD2 LEU A 35 17.223 25.466 13.850 1.00 65.78 C ANISOU 242 CD2 LEU A 35 7485 7123 10385 -166 2277 -374 C ATOM 243 N GLY A 36 12.212 27.398 14.446 1.00 58.35 N ANISOU 243 N GLY A 36 7074 6289 8808 -187 1891 -146 N ATOM 244 CA GLY A 36 11.304 28.531 14.519 1.00 57.95 C ANISOU 244 CA GLY A 36 7108 6230 8680 -218 1844 -104 C ATOM 245 C GLY A 36 10.931 28.940 15.931 1.00 57.46 C ANISOU 245 C GLY A 36 6963 6216 8654 -204 1672 -129 C ATOM 246 O GLY A 36 10.969 30.121 16.269 1.00 57.58 O ANISOU 246 O GLY A 36 6947 6205 8724 -244 1662 -135 O ATOM 247 N ASN A 37 10.568 27.973 16.764 1.00 57.16 N ANISOU 247 N ASN A 37 6899 6240 8580 -147 1543 -142 N ATOM 248 CA ASN A 37 10.157 28.253 18.125 1.00 57.57 C ANISOU 248 CA ASN A 37 6897 6334 8641 -126 1384 -163 C ATOM 249 C ASN A 37 11.303 28.666 19.024 1.00 58.17 C ANISOU 249 C ASN A 37 6808 6403 8892 -132 1346 -235 C ATOM 250 O ASN A 37 11.084 29.538 19.840 1.00 58.77 O ANISOU 250 O ASN A 37 6857 6482 8990 -144 1262 -251 O ATOM 251 CB ASN A 37 9.347 27.110 18.718 1.00 58.34 C ANISOU 251 CB ASN A 37 7041 6489 8635 -64 1271 -149 C ATOM 252 CG ASN A 37 7.935 27.144 18.203 1.00 60.27 C ANISOU 252 CG ASN A 37 7432 6742 8725 -66 1258 -88 C ATOM 253 OD1 ASN A 37 7.117 27.939 18.663 1.00 61.32 O ANISOU 253 OD1 ASN A 37 7598 6882 8818 -76 1194 -71 O ATOM 254 ND2 ASN A 37 7.631 26.325 17.206 1.00 60.49 N ANISOU 254 ND2 ASN A 37 7550 6762 8670 -56 1317 -58 N ATOM 255 N PHE A 38 12.510 28.109 18.875 1.00 58.52 N ANISOU 255 N PHE A 38 6739 6431 9066 -124 1401 -284 N ATOM 256 CA PHE A 38 13.638 28.513 19.721 1.00 59.39 C ANISOU 256 CA PHE A 38 6676 6526 9363 -128 1349 -364 C ATOM 257 C PHE A 38 14.075 29.947 19.405 1.00 58.12 C ANISOU 257 C PHE A 38 6469 6305 9309 -206 1437 -378 C ATOM 258 O PHE A 38 14.382 30.705 20.325 1.00 57.91 O ANISOU 258 O PHE A 38 6353 6272 9377 -217 1343 -428 O ATOM 259 CB PHE A 38 14.807 27.495 19.698 1.00 61.02 C ANISOU 259 CB PHE A 38 6757 6727 9699 -90 1373 -420 C ATOM 260 CG PHE A 38 14.603 26.403 20.740 1.00 63.88 C ANISOU 260 CG PHE A 38 7114 7146 10012 -5 1207 -436 C ATOM 261 CD1 PHE A 38 14.466 26.718 22.088 1.00 65.81 C ANISOU 261 CD1 PHE A 38 7326 7417 10262 26 1033 -469 C ATOM 262 CD2 PHE A 38 14.477 25.077 20.367 1.00 65.29 C ANISOU 262 CD2 PHE A 38 7342 7344 10120 45 1227 -414 C ATOM 263 CE1 PHE A 38 14.250 25.722 23.041 1.00 66.70 C ANISOU 263 CE1 PHE A 38 7460 7572 10310 107 889 -476 C ATOM 264 CE2 PHE A 38 14.256 24.084 21.323 1.00 66.43 C ANISOU 264 CE2 PHE A 38 7497 7530 10212 122 1081 -423 C ATOM 265 CZ PHE A 38 14.157 24.412 22.653 1.00 66.47 C ANISOU 265 CZ PHE A 38 7476 7559 10222 153 916 -452 C ATOM 266 N THR A 39 14.009 30.347 18.119 1.00 56.68 N ANISOU 266 N THR A 39 6368 6071 9095 -258 1612 -331 N ATOM 267 CA THR A 39 14.325 31.700 17.673 1.00 55.16 C ANISOU 267 CA THR A 39 6166 5809 8985 -336 1720 -329 C ATOM 268 C THR A 39 13.342 32.745 18.263 1.00 54.13 C ANISOU 268 C THR A 39 6108 5686 8771 -350 1615 -303 C ATOM 269 O THR A 39 13.788 33.782 18.757 1.00 54.39 O ANISOU 269 O THR A 39 6055 5682 8926 -392 1597 -344 O ATOM 270 CB THR A 39 14.345 31.754 16.133 1.00 55.63 C ANISOU 270 CB THR A 39 6343 5810 8985 -375 1930 -272 C ATOM 271 OG1 THR A 39 15.272 30.798 15.645 1.00 55.73 O ANISOU 271 OG1 THR A 39 6284 5812 9079 -359 2033 -303 O ATOM 272 CG2 THR A 39 14.700 33.139 15.591 1.00 55.75 C ANISOU 272 CG2 THR A 39 6365 5737 9081 -458 2066 -263 C ATOM 273 N VAL A 40 12.026 32.482 18.223 1.00 53.07 N ANISOU 273 N VAL A 40 6124 5596 8445 -315 1547 -240 N ATOM 274 CA VAL A 40 11.042 33.433 18.757 1.00 53.07 C ANISOU 274 CA VAL A 40 6191 5602 8370 -321 1455 -217 C ATOM 275 C VAL A 40 11.022 33.444 20.303 1.00 54.26 C ANISOU 275 C VAL A 40 6254 5801 8563 -284 1278 -273 C ATOM 276 O VAL A 40 10.815 34.494 20.895 1.00 53.99 O ANISOU 276 O VAL A 40 6209 5749 8557 -306 1223 -290 O ATOM 277 CB VAL A 40 9.631 33.271 18.150 1.00 52.20 C ANISOU 277 CB VAL A 40 6259 5509 8063 -300 1446 -137 C ATOM 278 CG1 VAL A 40 9.649 33.520 16.647 1.00 51.97 C ANISOU 278 CG1 VAL A 40 6344 5417 7984 -337 1609 -83 C ATOM 279 CG2 VAL A 40 9.037 31.912 18.478 1.00 52.31 C ANISOU 279 CG2 VAL A 40 6304 5595 7978 -234 1358 -127 C ATOM 280 N VAL A 41 11.293 32.304 20.945 1.00 55.79 N ANISOU 280 N VAL A 41 6390 6046 8762 -227 1193 -305 N ATOM 281 CA VAL A 41 11.369 32.193 22.406 1.00 57.36 C ANISOU 281 CA VAL A 41 6522 6283 8988 -181 1026 -360 C ATOM 282 C VAL A 41 12.602 32.942 22.902 1.00 60.34 C ANISOU 282 C VAL A 41 6746 6619 9563 -213 1006 -444 C ATOM 283 O VAL A 41 12.470 33.777 23.791 1.00 60.71 O ANISOU 283 O VAL A 41 6775 6660 9633 -218 908 -479 O ATOM 284 CB VAL A 41 11.323 30.719 22.905 1.00 56.63 C ANISOU 284 CB VAL A 41 6432 6248 8838 -106 945 -365 C ATOM 285 CG1 VAL A 41 11.797 30.591 24.346 1.00 56.68 C ANISOU 285 CG1 VAL A 41 6358 6275 8902 -56 783 -434 C ATOM 286 CG2 VAL A 41 9.929 30.160 22.777 1.00 56.84 C ANISOU 286 CG2 VAL A 41 6605 6314 8678 -76 926 -294 C ATOM 287 N PHE A 42 13.782 32.703 22.300 1.00 62.42 N ANISOU 287 N PHE A 42 6896 6845 9977 -238 1105 -480 N ATOM 288 CA PHE A 42 14.987 33.432 22.713 1.00 64.80 C ANISOU 288 CA PHE A 42 7030 7097 10495 -276 1092 -568 C ATOM 289 C PHE A 42 14.896 34.914 22.333 1.00 65.01 C ANISOU 289 C PHE A 42 7073 7057 10569 -359 1176 -558 C ATOM 290 O PHE A 42 15.357 35.753 23.098 1.00 65.41 O ANISOU 290 O PHE A 42 7033 7080 10742 -381 1096 -625 O ATOM 291 CB PHE A 42 16.295 32.755 22.254 1.00 66.67 C ANISOU 291 CB PHE A 42 7120 7307 10906 -278 1174 -620 C ATOM 292 CG PHE A 42 16.556 31.416 22.933 1.00 69.46 C ANISOU 292 CG PHE A 42 7428 7715 11248 -188 1048 -653 C ATOM 293 CD1 PHE A 42 17.218 30.397 22.266 1.00 71.51 C ANISOU 293 CD1 PHE A 42 7634 7971 11567 -166 1140 -659 C ATOM 294 CD2 PHE A 42 16.059 31.149 24.205 1.00 71.02 C ANISOU 294 CD2 PHE A 42 7663 7963 11357 -120 848 -670 C ATOM 295 CE1 PHE A 42 17.403 29.149 22.871 1.00 72.70 C ANISOU 295 CE1 PHE A 42 7758 8166 11699 -78 1022 -683 C ATOM 296 CE2 PHE A 42 16.231 29.901 24.797 1.00 72.18 C ANISOU 296 CE2 PHE A 42 7798 8153 11475 -33 738 -689 C ATOM 297 CZ PHE A 42 16.904 28.911 24.129 1.00 72.40 C ANISOU 297 CZ PHE A 42 7763 8175 11569 -12 821 -695 C ATOM 298 N GLY A 43 14.193 35.237 21.250 1.00 64.60 N ANISOU 298 N GLY A 43 7156 6982 10407 -395 1312 -474 N ATOM 299 CA GLY A 43 13.924 36.618 20.868 1.00 64.36 C ANISOU 299 CA GLY A 43 7178 6887 10389 -464 1386 -449 C ATOM 300 C GLY A 43 13.119 37.342 21.939 1.00 64.22 C ANISOU 300 C GLY A 43 7203 6891 10305 -445 1231 -460 C ATOM 301 O GLY A 43 13.385 38.506 22.229 1.00 64.56 O ANISOU 301 O GLY A 43 7204 6879 10446 -495 1227 -494 O ATOM 302 N TYR A 44 12.147 36.660 22.572 1.00 63.32 N ANISOU 302 N TYR A 44 7173 6854 10033 -375 1107 -434 N ATOM 303 CA TYR A 44 11.367 37.252 23.652 1.00 62.79 C ANISOU 303 CA TYR A 44 7150 6809 9898 -349 967 -448 C ATOM 304 C TYR A 44 12.172 37.325 24.947 1.00 65.04 C ANISOU 304 C TYR A 44 7309 7100 10301 -326 823 -547 C ATOM 305 O TYR A 44 12.121 38.334 25.648 1.00 65.10 O ANISOU 305 O TYR A 44 7305 7081 10350 -344 753 -589 O ATOM 306 CB TYR A 44 10.070 36.480 23.870 1.00 61.11 C ANISOU 306 CB TYR A 44 7065 6666 9489 -285 904 -389 C ATOM 307 CG TYR A 44 8.891 37.070 23.130 1.00 59.84 C ANISOU 307 CG TYR A 44 7041 6487 9207 -303 967 -310 C ATOM 308 CD1 TYR A 44 9.063 37.728 21.917 1.00 59.39 C ANISOU 308 CD1 TYR A 44 7022 6366 9180 -363 1109 -270 C ATOM 309 CD2 TYR A 44 7.599 36.957 23.633 1.00 59.35 C ANISOU 309 CD2 TYR A 44 7077 6469 9006 -258 888 -277 C ATOM 310 CE1 TYR A 44 7.988 38.292 21.246 1.00 59.48 C ANISOU 310 CE1 TYR A 44 7167 6354 9078 -370 1147 -201 C ATOM 311 CE2 TYR A 44 6.510 37.481 22.946 1.00 59.29 C ANISOU 311 CE2 TYR A 44 7183 6442 8903 -268 931 -212 C ATOM 312 CZ TYR A 44 6.711 38.160 21.759 1.00 59.83 C ANISOU 312 CZ TYR A 44 7292 6445 8997 -321 1051 -174 C ATOM 313 OH TYR A 44 5.655 38.684 21.061 1.00 60.63 O ANISOU 313 OH TYR A 44 7514 6520 9002 -322 1079 -111 O ATOM 314 N LEU A 45 12.927 36.266 25.260 1.00 66.70 N ANISOU 314 N LEU A 45 7432 7342 10568 -283 773 -590 N ATOM 315 CA LEU A 45 13.745 36.220 26.468 1.00 68.82 C ANISOU 315 CA LEU A 45 7586 7615 10947 -248 616 -689 C ATOM 316 C LEU A 45 14.873 37.255 26.454 1.00 72.00 C ANISOU 316 C LEU A 45 7841 7941 11576 -318 638 -770 C ATOM 317 O LEU A 45 15.310 37.680 27.521 1.00 72.51 O ANISOU 317 O LEU A 45 7837 7994 11720 -301 491 -855 O ATOM 318 CB LEU A 45 14.322 34.810 26.700 1.00 68.41 C ANISOU 318 CB LEU A 45 7477 7606 10911 -181 558 -713 C ATOM 319 CG LEU A 45 13.324 33.680 26.941 1.00 68.92 C ANISOU 319 CG LEU A 45 7674 7741 10773 -107 512 -648 C ATOM 320 CD1 LEU A 45 14.027 32.335 27.059 1.00 68.79 C ANISOU 320 CD1 LEU A 45 7593 7750 10794 -45 470 -674 C ATOM 321 CD2 LEU A 45 12.452 33.959 28.140 1.00 69.48 C ANISOU 321 CD2 LEU A 45 7844 7841 10714 -61 373 -652 C ATOM 322 N PHE A 46 15.333 37.683 25.263 1.00 74.06 N ANISOU 322 N PHE A 46 8059 8142 11938 -396 823 -746 N ATOM 323 CA PHE A 46 16.423 38.661 25.168 1.00 76.38 C ANISOU 323 CA PHE A 46 8203 8350 12466 -473 872 -822 C ATOM 324 C PHE A 46 16.057 40.031 24.557 1.00 77.00 C ANISOU 324 C PHE A 46 8347 8356 12555 -558 995 -782 C ATOM 325 O PHE A 46 16.885 40.931 24.634 1.00 77.65 O ANISOU 325 O PHE A 46 8311 8360 12831 -625 1022 -849 O ATOM 326 CB PHE A 46 17.625 38.067 24.422 1.00 77.58 C ANISOU 326 CB PHE A 46 8207 8470 12799 -499 992 -855 C ATOM 327 CG PHE A 46 18.247 36.932 25.200 1.00 80.07 C ANISOU 327 CG PHE A 46 8421 8838 13165 -416 842 -922 C ATOM 328 CD1 PHE A 46 18.246 35.644 24.697 1.00 81.58 C ANISOU 328 CD1 PHE A 46 8635 9074 13288 -366 895 -881 C ATOM 329 CD2 PHE A 46 18.719 37.129 26.488 1.00 81.65 C ANISOU 329 CD2 PHE A 46 8530 9041 13452 -377 632 -1022 C ATOM 330 CE1 PHE A 46 18.772 34.591 25.435 1.00 82.62 C ANISOU 330 CE1 PHE A 46 8688 9248 13455 -282 750 -937 C ATOM 331 CE2 PHE A 46 19.239 36.074 27.227 1.00 82.59 C ANISOU 331 CE2 PHE A 46 8579 9203 13596 -288 479 -1078 C ATOM 332 CZ PHE A 46 19.258 34.813 26.697 1.00 82.54 C ANISOU 332 CZ PHE A 46 8591 9239 13532 -241 541 -1033 C ATOM 333 N CYS A 47 14.855 40.214 23.975 1.00 76.68 N ANISOU 333 N CYS A 47 8486 8330 12318 -556 1062 -680 N ATOM 334 CA CYS A 47 14.491 41.501 23.363 1.00 76.82 C ANISOU 334 CA CYS A 47 8580 8271 12337 -629 1173 -637 C ATOM 335 C CYS A 47 13.295 42.181 24.010 1.00 76.89 C ANISOU 335 C CYS A 47 8715 8299 12201 -601 1066 -611 C ATOM 336 O CYS A 47 13.234 43.410 24.016 1.00 77.50 O ANISOU 336 O CYS A 47 8808 8306 12333 -654 1091 -619 O ATOM 337 CB CYS A 47 14.286 41.372 21.854 1.00 77.38 C ANISOU 337 CB CYS A 47 8752 8309 12342 -664 1380 -542 C ATOM 338 SG CYS A 47 15.673 40.626 20.972 1.00 80.48 S ANISOU 338 SG CYS A 47 9010 8666 12904 -701 1548 -569 S ATOM 339 N MET A 48 12.301 41.410 24.454 1.00 76.38 N ANISOU 339 N MET A 48 8746 8321 11953 -521 965 -574 N ATOM 340 CA MET A 48 11.108 41.997 25.054 1.00 76.19 C ANISOU 340 CA MET A 48 8839 8315 11794 -491 878 -550 C ATOM 341 C MET A 48 11.344 42.330 26.520 1.00 76.40 C ANISOU 341 C MET A 48 8805 8353 11870 -461 705 -644 C ATOM 342 O MET A 48 11.684 41.446 27.310 1.00 77.10 O ANISOU 342 O MET A 48 8842 8497 11956 -405 593 -691 O ATOM 343 CB MET A 48 9.876 41.095 24.863 1.00 76.28 C ANISOU 343 CB MET A 48 8982 8401 11600 -426 864 -469 C ATOM 344 CG MET A 48 9.512 40.866 23.410 1.00 77.87 C ANISOU 344 CG MET A 48 9270 8584 11732 -449 1015 -379 C ATOM 345 SD MET A 48 9.157 42.359 22.464 1.00 79.64 S ANISOU 345 SD MET A 48 9585 8707 11966 -518 1136 -326 S ATOM 346 CE MET A 48 8.702 41.718 20.976 1.00 71.70 C ANISOU 346 CE MET A 48 8700 7701 10840 -514 1265 -228 C ATOM 347 N LYS A 49 11.189 43.612 26.889 1.00 75.75 N ANISOU 347 N LYS A 49 8738 8212 11831 -496 681 -673 N ATOM 348 CA LYS A 49 11.372 44.028 28.281 1.00 75.42 C ANISOU 348 CA LYS A 49 8658 8172 11825 -467 514 -767 C ATOM 349 C LYS A 49 10.023 44.201 29.008 1.00 73.68 C ANISOU 349 C LYS A 49 8582 7993 11422 -407 435 -737 C ATOM 350 O LYS A 49 9.892 43.805 30.168 1.00 73.96 O ANISOU 350 O LYS A 49 8633 8074 11395 -342 296 -786 O ATOM 351 CB LYS A 49 12.224 45.306 28.369 1.00 78.30 C ANISOU 351 CB LYS A 49 8931 8438 12383 -546 525 -841 C ATOM 352 CG LYS A 49 13.277 45.261 29.484 1.00 83.97 C ANISOU 352 CG LYS A 49 9511 9148 13245 -533 369 -969 C ATOM 353 CD LYS A 49 13.437 46.602 30.235 1.00 89.59 C ANISOU 353 CD LYS A 49 10204 9785 14051 -569 288 -1052 C ATOM 354 CE LYS A 49 14.051 47.729 29.425 1.00 93.56 C ANISOU 354 CE LYS A 49 10632 10176 14739 -679 424 -1062 C ATOM 355 NZ LYS A 49 13.736 49.069 30.016 1.00 95.56 N ANISOU 355 NZ LYS A 49 10927 10360 15021 -706 366 -1109 N ATOM 356 N ASN A 50 9.024 44.779 28.325 1.00 71.69 N ANISOU 356 N ASN A 50 8436 7718 11083 -424 525 -658 N ATOM 357 CA ASN A 50 7.708 44.969 28.929 1.00 70.38 C ANISOU 357 CA ASN A 50 8393 7585 10764 -368 467 -631 C ATOM 358 C ASN A 50 6.633 44.266 28.095 1.00 67.73 C ANISOU 358 C ASN A 50 8153 7294 10286 -339 545 -527 C ATOM 359 O ASN A 50 6.312 44.708 26.990 1.00 69.02 O ANISOU 359 O ASN A 50 8363 7416 10446 -377 652 -462 O ATOM 360 CB ASN A 50 7.402 46.459 29.174 1.00 72.30 C ANISOU 360 CB ASN A 50 8672 7752 11047 -401 462 -656 C ATOM 361 CG ASN A 50 7.134 47.293 27.939 1.00 77.02 C ANISOU 361 CG ASN A 50 9314 8277 11671 -460 598 -587 C ATOM 362 OD1 ASN A 50 7.917 47.329 26.966 1.00 78.46 O ANISOU 362 OD1 ASN A 50 9445 8415 11951 -521 704 -566 O ATOM 363 ND2 ASN A 50 6.009 47.992 27.966 1.00 78.16 N ANISOU 363 ND2 ASN A 50 9564 8404 11729 -438 599 -549 N ATOM 364 N TRP A 51 6.106 43.142 28.601 1.00 63.55 N ANISOU 364 N TRP A 51 7658 6845 9643 -272 489 -513 N ATOM 365 CA TRP A 51 5.147 42.337 27.849 1.00 59.76 C ANISOU 365 CA TRP A 51 7253 6409 9044 -246 550 -426 C ATOM 366 C TRP A 51 3.708 42.822 27.893 1.00 57.16 C ANISOU 366 C TRP A 51 7027 6079 8613 -218 551 -382 C ATOM 367 O TRP A 51 3.218 43.214 28.941 1.00 57.82 O ANISOU 367 O TRP A 51 7140 6167 8662 -184 481 -420 O ATOM 368 CB TRP A 51 5.175 40.892 28.348 1.00 58.83 C ANISOU 368 CB TRP A 51 7127 6368 8858 -189 498 -428 C ATOM 369 CG TRP A 51 6.442 40.145 28.069 1.00 58.03 C ANISOU 369 CG TRP A 51 6928 6275 8845 -204 508 -455 C ATOM 370 CD1 TRP A 51 7.701 40.661 27.965 1.00 58.45 C ANISOU 370 CD1 TRP A 51 6876 6280 9054 -254 517 -512 C ATOM 371 CD2 TRP A 51 6.576 38.731 27.943 1.00 57.38 C ANISOU 371 CD2 TRP A 51 6838 6249 8715 -167 506 -434 C ATOM 372 NE1 TRP A 51 8.600 39.660 27.718 1.00 58.52 N ANISOU 372 NE1 TRP A 51 6806 6312 9118 -247 527 -527 N ATOM 373 CE2 TRP A 51 7.939 38.457 27.733 1.00 58.23 C ANISOU 373 CE2 TRP A 51 6831 6340 8952 -191 515 -479 C ATOM 374 CE3 TRP A 51 5.670 37.669 27.947 1.00 57.50 C ANISOU 374 CE3 TRP A 51 6927 6321 8602 -117 505 -382 C ATOM 375 CZ2 TRP A 51 8.414 37.163 27.533 1.00 58.49 C ANISOU 375 CZ2 TRP A 51 6829 6413 8982 -161 519 -473 C ATOM 376 CZ3 TRP A 51 6.151 36.390 27.801 1.00 58.06 C ANISOU 376 CZ3 TRP A 51 6967 6428 8664 -91 504 -376 C ATOM 377 CH2 TRP A 51 7.509 36.150 27.600 1.00 58.28 C ANISOU 377 CH2 TRP A 51 6887 6441 8815 -109 509 -421 C ATOM 378 N ASN A 52 3.005 42.727 26.773 1.00 54.21 N ANISOU 378 N ASN A 52 6711 5697 8188 -226 628 -305 N ATOM 379 CA ASN A 52 1.586 43.018 26.709 1.00 51.88 C ANISOU 379 CA ASN A 52 6502 5404 7807 -192 624 -263 C ATOM 380 C ASN A 52 0.782 41.670 26.641 1.00 49.95 C ANISOU 380 C ASN A 52 6287 5232 7461 -143 617 -222 C ATOM 381 O ASN A 52 1.369 40.594 26.784 1.00 49.57 O ANISOU 381 O ASN A 52 6200 5229 7406 -134 608 -231 O ATOM 382 CB ASN A 52 1.258 44.022 25.561 1.00 51.74 C ANISOU 382 CB ASN A 52 6538 5313 7807 -227 693 -212 C ATOM 383 CG ASN A 52 1.430 43.537 24.147 1.00 52.41 C ANISOU 383 CG ASN A 52 6655 5387 7873 -250 775 -147 C ATOM 384 OD1 ASN A 52 1.359 42.346 23.846 1.00 53.92 O ANISOU 384 OD1 ASN A 52 6844 5633 8011 -230 782 -123 O ATOM 385 ND2 ASN A 52 1.621 44.457 23.233 1.00 51.35 N ANISOU 385 ND2 ASN A 52 6566 5174 7772 -292 843 -115 N ATOM 386 N SER A 53 -0.541 41.736 26.446 1.00 48.67 N ANISOU 386 N SER A 53 6186 5073 7233 -113 617 -183 N ATOM 387 CA SER A 53 -1.397 40.558 26.344 1.00 47.87 C ANISOU 387 CA SER A 53 6108 5027 7055 -74 614 -149 C ATOM 388 C SER A 53 -0.990 39.635 25.201 1.00 47.80 C ANISOU 388 C SER A 53 6099 5032 7031 -91 659 -105 C ATOM 389 O SER A 53 -0.798 38.442 25.429 1.00 48.36 O ANISOU 389 O SER A 53 6149 5153 7071 -73 651 -107 O ATOM 390 CB SER A 53 -2.855 40.975 26.206 1.00 47.61 C ANISOU 390 CB SER A 53 6124 4978 6988 -44 607 -121 C ATOM 391 OG SER A 53 -3.220 41.842 27.267 1.00 48.66 O ANISOU 391 OG SER A 53 6261 5094 7136 -25 576 -165 O ATOM 392 N SER A 54 -0.797 40.191 23.994 1.00 47.13 N ANISOU 392 N SER A 54 6047 4896 6964 -125 711 -68 N ATOM 393 CA SER A 54 -0.384 39.448 22.808 1.00 46.74 C ANISOU 393 CA SER A 54 6018 4847 6893 -142 768 -27 C ATOM 394 C SER A 54 0.977 38.744 22.996 1.00 46.87 C ANISOU 394 C SER A 54 5962 4888 6959 -163 794 -59 C ATOM 395 O SER A 54 1.140 37.620 22.531 1.00 47.82 O ANISOU 395 O SER A 54 6083 5041 7045 -154 815 -41 O ATOM 396 CB SER A 54 -0.352 40.364 21.595 1.00 47.41 C ANISOU 396 CB SER A 54 6172 4859 6983 -174 826 15 C ATOM 397 OG SER A 54 -1.663 40.659 21.148 1.00 49.05 O ANISOU 397 OG SER A 54 6456 5049 7132 -141 792 53 O ATOM 398 N ASN A 55 1.927 39.372 23.711 1.00 45.85 N ANISOU 398 N ASN A 55 5765 4741 6916 -188 783 -113 N ATOM 399 CA ASN A 55 3.221 38.764 23.990 1.00 45.46 C ANISOU 399 CA ASN A 55 5629 4710 6935 -201 789 -155 C ATOM 400 C ASN A 55 3.051 37.537 24.837 1.00 45.64 C ANISOU 400 C ASN A 55 5632 4802 6906 -150 722 -172 C ATOM 401 O ASN A 55 3.656 36.509 24.536 1.00 46.46 O ANISOU 401 O ASN A 55 5705 4933 7016 -143 743 -171 O ATOM 402 CB ASN A 55 4.151 39.731 24.726 1.00 45.76 C ANISOU 402 CB ASN A 55 5592 4710 7085 -232 763 -221 C ATOM 403 CG ASN A 55 4.522 40.962 23.974 1.00 47.17 C ANISOU 403 CG ASN A 55 5779 4807 7336 -292 839 -210 C ATOM 404 OD1 ASN A 55 4.632 42.010 24.569 1.00 48.08 O ANISOU 404 OD1 ASN A 55 5877 4883 7509 -310 806 -249 O ATOM 405 ND2 ASN A 55 4.751 40.875 22.673 1.00 47.89 N ANISOU 405 ND2 ASN A 55 5907 4863 7425 -324 945 -159 N ATOM 406 N VAL A 56 2.222 37.641 25.895 1.00 44.93 N ANISOU 406 N VAL A 56 5569 4737 6766 -111 651 -189 N ATOM 407 CA VAL A 56 1.919 36.550 26.815 1.00 44.48 C ANISOU 407 CA VAL A 56 5518 4737 6647 -59 594 -201 C ATOM 408 C VAL A 56 1.306 35.379 26.047 1.00 44.52 C ANISOU 408 C VAL A 56 5561 4772 6584 -43 632 -146 C ATOM 409 O VAL A 56 1.759 34.246 26.208 1.00 45.53 O ANISOU 409 O VAL A 56 5668 4932 6698 -22 623 -151 O ATOM 410 CB VAL A 56 1.017 37.025 28.001 1.00 44.64 C ANISOU 410 CB VAL A 56 5579 4762 6618 -23 538 -222 C ATOM 411 CG1 VAL A 56 0.466 35.841 28.793 1.00 44.99 C ANISOU 411 CG1 VAL A 56 5658 4855 6580 29 509 -217 C ATOM 412 CG2 VAL A 56 1.777 37.979 28.926 1.00 44.40 C ANISOU 412 CG2 VAL A 56 5516 4705 6649 -30 481 -291 C ATOM 413 N TYR A 57 0.325 35.646 25.179 1.00 43.47 N ANISOU 413 N TYR A 57 5482 4622 6413 -52 668 -98 N ATOM 414 CA TYR A 57 -0.331 34.584 24.420 1.00 43.05 C ANISOU 414 CA TYR A 57 5467 4591 6300 -38 691 -54 C ATOM 415 C TYR A 57 0.601 33.923 23.434 1.00 44.22 C ANISOU 415 C TYR A 57 5602 4735 6463 -59 744 -40 C ATOM 416 O TYR A 57 0.530 32.704 23.250 1.00 45.11 O ANISOU 416 O TYR A 57 5723 4879 6539 -39 747 -27 O ATOM 417 CB TYR A 57 -1.573 35.093 23.684 1.00 42.44 C ANISOU 417 CB TYR A 57 5449 4487 6188 -38 697 -14 C ATOM 418 CG TYR A 57 -2.625 35.688 24.582 1.00 42.53 C ANISOU 418 CG TYR A 57 5470 4499 6193 -14 657 -28 C ATOM 419 CD1 TYR A 57 -2.906 35.129 25.821 1.00 43.49 C ANISOU 419 CD1 TYR A 57 5575 4655 6293 18 629 -54 C ATOM 420 CD2 TYR A 57 -3.342 36.815 24.197 1.00 42.97 C ANISOU 420 CD2 TYR A 57 5556 4511 6261 -18 653 -15 C ATOM 421 CE1 TYR A 57 -3.879 35.669 26.652 1.00 44.04 C ANISOU 421 CE1 TYR A 57 5659 4719 6356 41 611 -69 C ATOM 422 CE2 TYR A 57 -4.312 37.366 25.022 1.00 43.70 C ANISOU 422 CE2 TYR A 57 5649 4599 6356 7 625 -32 C ATOM 423 CZ TYR A 57 -4.591 36.776 26.240 1.00 44.98 C ANISOU 423 CZ TYR A 57 5794 4798 6499 35 610 -60 C ATOM 424 OH TYR A 57 -5.536 37.318 27.070 1.00 47.55 O ANISOU 424 OH TYR A 57 6125 5114 6827 61 600 -79 O ATOM 425 N LEU A 58 1.458 34.714 22.771 1.00 44.13 N ANISOU 425 N LEU A 58 5575 4681 6510 -99 795 -43 N ATOM 426 CA LEU A 58 2.404 34.180 21.794 1.00 43.85 C ANISOU 426 CA LEU A 58 5529 4634 6499 -122 869 -33 C ATOM 427 C LEU A 58 3.450 33.319 22.491 1.00 44.57 C ANISOU 427 C LEU A 58 5535 4758 6641 -106 850 -77 C ATOM 428 O LEU A 58 3.836 32.292 21.944 1.00 44.66 O ANISOU 428 O LEU A 58 5544 4783 6641 -98 886 -67 O ATOM 429 CB LEU A 58 3.088 35.308 21.006 1.00 43.42 C ANISOU 429 CB LEU A 58 5478 4514 6505 -173 947 -27 C ATOM 430 CG LEU A 58 2.249 35.952 19.918 1.00 44.22 C ANISOU 430 CG LEU A 58 5689 4570 6543 -184 983 28 C ATOM 431 CD1 LEU A 58 2.817 37.308 19.505 1.00 44.63 C ANISOU 431 CD1 LEU A 58 5750 4548 6659 -233 1048 30 C ATOM 432 CD2 LEU A 58 2.048 35.014 18.747 1.00 44.06 C ANISOU 432 CD2 LEU A 58 5743 4551 6447 -174 1030 69 C ATOM 433 N PHE A 59 3.908 33.719 23.693 1.00 45.07 N ANISOU 433 N PHE A 59 5535 4829 6760 -97 785 -129 N ATOM 434 CA PHE A 59 4.889 32.929 24.430 1.00 46.12 C ANISOU 434 CA PHE A 59 5592 4989 6943 -71 741 -176 C ATOM 435 C PHE A 59 4.310 31.586 24.865 1.00 46.02 C ANISOU 435 C PHE A 59 5618 5024 6843 -18 699 -158 C ATOM 436 O PHE A 59 4.988 30.573 24.777 1.00 46.29 O ANISOU 436 O PHE A 59 5619 5075 6896 2 704 -168 O ATOM 437 CB PHE A 59 5.426 33.685 25.642 1.00 46.61 C ANISOU 437 CB PHE A 59 5595 5043 7071 -66 660 -239 C ATOM 438 CG PHE A 59 6.738 33.109 26.140 1.00 47.88 C ANISOU 438 CG PHE A 59 5659 5211 7321 -48 617 -297 C ATOM 439 CD1 PHE A 59 7.926 33.360 25.468 1.00 48.48 C ANISOU 439 CD1 PHE A 59 5643 5251 7526 -90 679 -325 C ATOM 440 CD2 PHE A 59 6.787 32.356 27.303 1.00 48.87 C ANISOU 440 CD2 PHE A 59 5788 5371 7408 13 513 -327 C ATOM 441 CE1 PHE A 59 9.137 32.891 25.965 1.00 49.22 C ANISOU 441 CE1 PHE A 59 5630 5347 7725 -70 628 -389 C ATOM 442 CE2 PHE A 59 7.994 31.845 27.771 1.00 49.31 C ANISOU 442 CE2 PHE A 59 5756 5428 7550 40 454 -384 C ATOM 443 CZ PHE A 59 9.161 32.133 27.111 1.00 49.26 C ANISOU 443 CZ PHE A 59 5640 5389 7689 -1 506 -419 C ATOM 444 N ASN A 60 3.040 31.574 25.262 1.00 45.67 N ANISOU 444 N ASN A 60 5643 4997 6714 2 669 -132 N ATOM 445 CA ASN A 60 2.319 30.361 25.633 1.00 45.65 C ANISOU 445 CA ASN A 60 5685 5028 6631 44 646 -110 C ATOM 446 C ASN A 60 2.137 29.447 24.436 1.00 45.04 C ANISOU 446 C ASN A 60 5635 4953 6525 36 705 -70 C ATOM 447 O ASN A 60 2.311 28.247 24.554 1.00 45.51 O ANISOU 447 O ASN A 60 5698 5033 6562 65 699 -67 O ATOM 448 CB ASN A 60 0.970 30.724 26.215 1.00 47.02 C ANISOU 448 CB ASN A 60 5916 5207 6744 57 623 -93 C ATOM 449 CG ASN A 60 1.036 30.919 27.688 1.00 51.20 C ANISOU 449 CG ASN A 60 6448 5746 7259 91 558 -132 C ATOM 450 OD1 ASN A 60 0.964 29.963 28.466 1.00 52.81 O ANISOU 450 OD1 ASN A 60 6679 5971 7416 132 529 -134 O ATOM 451 ND2 ASN A 60 1.213 32.162 28.098 1.00 52.25 N ANISOU 451 ND2 ASN A 60 6565 5858 7431 76 535 -163 N ATOM 452 N LEU A 61 1.830 30.013 23.276 1.00 44.37 N ANISOU 452 N LEU A 61 5582 4842 6437 1 760 -40 N ATOM 453 CA LEU A 61 1.674 29.278 22.030 1.00 44.65 C ANISOU 453 CA LEU A 61 5661 4870 6436 -7 814 -6 C ATOM 454 C LEU A 61 2.996 28.543 21.690 1.00 46.53 C ANISOU 454 C LEU A 61 5850 5107 6721 -6 858 -26 C ATOM 455 O LEU A 61 2.959 27.389 21.266 1.00 47.17 O ANISOU 455 O LEU A 61 5954 5200 6767 13 874 -14 O ATOM 456 CB LEU A 61 1.322 30.283 20.935 1.00 43.89 C ANISOU 456 CB LEU A 61 5616 4731 6329 -41 859 22 C ATOM 457 CG LEU A 61 1.118 29.770 19.528 1.00 43.90 C ANISOU 457 CG LEU A 61 5691 4712 6277 -48 912 57 C ATOM 458 CD1 LEU A 61 -0.181 28.976 19.416 1.00 43.77 C ANISOU 458 CD1 LEU A 61 5728 4714 6190 -22 862 78 C ATOM 459 CD2 LEU A 61 1.199 30.925 18.499 1.00 43.45 C ANISOU 459 CD2 LEU A 61 5691 4600 6216 -82 967 81 C ATOM 460 N SER A 62 4.156 29.188 21.939 1.00 46.63 N ANISOU 460 N SER A 62 5786 5104 6827 -24 873 -64 N ATOM 461 CA SER A 62 5.459 28.582 21.700 1.00 46.99 C ANISOU 461 CA SER A 62 5763 5146 6947 -21 914 -93 C ATOM 462 C SER A 62 5.760 27.483 22.686 1.00 47.07 C ANISOU 462 C SER A 62 5735 5190 6958 32 840 -120 C ATOM 463 O SER A 62 6.319 26.482 22.281 1.00 46.98 O ANISOU 463 O SER A 62 5707 5182 6960 51 871 -124 O ATOM 464 CB SER A 62 6.560 29.626 21.753 1.00 48.60 C ANISOU 464 CB SER A 62 5880 5315 7271 -58 945 -133 C ATOM 465 OG SER A 62 6.432 30.465 20.626 1.00 51.72 O ANISOU 465 OG SER A 62 6325 5665 7661 -107 1040 -101 O ATOM 466 N ILE A 63 5.392 27.639 23.967 1.00 47.51 N ANISOU 466 N ILE A 63 5790 5268 6994 61 746 -137 N ATOM 467 CA ILE A 63 5.581 26.571 24.955 1.00 48.83 C ANISOU 467 CA ILE A 63 5953 5461 7141 119 672 -155 C ATOM 468 C ILE A 63 4.709 25.338 24.576 1.00 49.10 C ANISOU 468 C ILE A 63 6064 5510 7083 140 694 -109 C ATOM 469 O ILE A 63 5.159 24.196 24.666 1.00 48.78 O ANISOU 469 O ILE A 63 6017 5475 7043 177 685 -115 O ATOM 470 CB ILE A 63 5.269 27.071 26.383 1.00 50.23 C ANISOU 470 CB ILE A 63 6143 5649 7293 147 576 -179 C ATOM 471 CG1 ILE A 63 6.232 28.218 26.811 1.00 51.69 C ANISOU 471 CG1 ILE A 63 6246 5814 7580 129 537 -237 C ATOM 472 CG2 ILE A 63 5.265 25.913 27.395 1.00 50.91 C ANISOU 472 CG2 ILE A 63 6264 5753 7326 213 505 -185 C ATOM 473 CD1 ILE A 63 7.777 27.988 26.506 1.00 53.53 C ANISOU 473 CD1 ILE A 63 6364 6030 7944 128 542 -286 C ATOM 474 N SER A 64 3.481 25.594 24.101 1.00 48.95 N ANISOU 474 N SER A 64 6114 5489 6996 117 721 -68 N ATOM 475 CA SER A 64 2.554 24.568 23.631 1.00 48.96 C ANISOU 475 CA SER A 64 6182 5495 6926 125 741 -31 C ATOM 476 C SER A 64 3.179 23.842 22.421 1.00 49.65 C ANISOU 476 C SER A 64 6267 5569 7027 118 805 -25 C ATOM 477 O SER A 64 3.116 22.618 22.364 1.00 50.61 O ANISOU 477 O SER A 64 6413 5696 7121 145 805 -18 O ATOM 478 CB SER A 64 1.222 25.215 23.248 1.00 48.54 C ANISOU 478 CB SER A 64 6181 5435 6827 98 750 0 C ATOM 479 OG SER A 64 0.290 24.295 22.716 1.00 49.30 O ANISOU 479 OG SER A 64 6332 5530 6872 102 761 28 O ATOM 480 N ASP A 65 3.774 24.589 21.462 1.00 48.98 N ANISOU 480 N ASP A 65 6163 5462 6984 82 869 -29 N ATOM 481 CA ASP A 65 4.404 24.026 20.267 1.00 48.82 C ANISOU 481 CA ASP A 65 6154 5422 6973 74 950 -26 C ATOM 482 C ASP A 65 5.602 23.188 20.677 1.00 49.11 C ANISOU 482 C ASP A 65 6116 5465 7080 108 948 -62 C ATOM 483 O ASP A 65 5.767 22.076 20.187 1.00 49.66 O ANISOU 483 O ASP A 65 6208 5530 7129 129 978 -59 O ATOM 484 CB ASP A 65 4.878 25.136 19.286 1.00 50.04 C ANISOU 484 CB ASP A 65 6309 5541 7162 27 1033 -22 C ATOM 485 CG ASP A 65 3.799 25.902 18.554 1.00 54.87 C ANISOU 485 CG ASP A 65 7014 6134 7702 -1 1043 17 C ATOM 486 OD1 ASP A 65 2.656 25.441 18.540 1.00 55.54 O ANISOU 486 OD1 ASP A 65 7160 6231 7713 14 994 40 O ATOM 487 OD2 ASP A 65 4.104 26.978 17.999 1.00 58.24 O ANISOU 487 OD2 ASP A 65 7450 6526 8152 -36 1098 23 O ATOM 488 N LEU A 66 6.441 23.715 21.565 1.00 49.04 N ANISOU 488 N LEU A 66 6018 5461 7155 116 906 -102 N ATOM 489 CA LEU A 66 7.662 23.048 21.996 1.00 49.83 C ANISOU 489 CA LEU A 66 6031 5561 7342 154 887 -147 C ATOM 490 C LEU A 66 7.385 21.753 22.743 1.00 50.53 C ANISOU 490 C LEU A 66 6153 5668 7377 215 816 -141 C ATOM 491 O LEU A 66 8.165 20.807 22.623 1.00 51.48 O ANISOU 491 O LEU A 66 6238 5781 7540 251 825 -161 O ATOM 492 CB LEU A 66 8.559 23.995 22.823 1.00 50.01 C ANISOU 492 CB LEU A 66 5949 5578 7474 151 835 -199 C ATOM 493 CG LEU A 66 9.321 25.066 22.027 1.00 51.08 C ANISOU 493 CG LEU A 66 6018 5679 7712 92 928 -219 C ATOM 494 CD1 LEU A 66 9.836 26.162 22.938 1.00 51.34 C ANISOU 494 CD1 LEU A 66 5967 5705 7837 80 859 -267 C ATOM 495 CD2 LEU A 66 10.448 24.460 21.222 1.00 51.56 C ANISOU 495 CD2 LEU A 66 6009 5714 7866 94 1021 -245 C ATOM 496 N ALA A 67 6.271 21.685 23.482 1.00 49.88 N ANISOU 496 N ALA A 67 6143 5603 7205 226 755 -113 N ATOM 497 CA ALA A 67 5.874 20.482 24.205 1.00 49.92 C ANISOU 497 CA ALA A 67 6200 5616 7149 278 703 -99 C ATOM 498 C ALA A 67 5.579 19.383 23.175 1.00 50.28 C ANISOU 498 C ALA A 67 6296 5650 7158 277 768 -73 C ATOM 499 O ALA A 67 6.101 18.264 23.304 1.00 50.73 O ANISOU 499 O ALA A 67 6348 5698 7227 321 757 -83 O ATOM 500 CB ALA A 67 4.642 20.765 25.074 1.00 49.74 C ANISOU 500 CB ALA A 67 6250 5606 7045 278 658 -72 C ATOM 501 N PHE A 68 4.825 19.732 22.106 1.00 49.70 N ANISOU 501 N PHE A 68 6269 5570 7044 229 830 -46 N ATOM 502 CA PHE A 68 4.514 18.805 21.028 1.00 49.96 C ANISOU 502 CA PHE A 68 6360 5587 7037 224 886 -27 C ATOM 503 C PHE A 68 5.795 18.355 20.313 1.00 50.32 C ANISOU 503 C PHE A 68 6358 5615 7146 238 948 -56 C ATOM 504 O PHE A 68 5.956 17.171 20.050 1.00 50.32 O ANISOU 504 O PHE A 68 6382 5603 7134 268 962 -57 O ATOM 505 CB PHE A 68 3.494 19.428 20.050 1.00 50.11 C ANISOU 505 CB PHE A 68 6444 5597 7000 176 920 1 C ATOM 506 CG PHE A 68 3.591 18.947 18.615 1.00 51.33 C ANISOU 506 CG PHE A 68 6652 5725 7125 163 992 6 C ATOM 507 CD1 PHE A 68 3.167 17.679 18.261 1.00 52.06 C ANISOU 507 CD1 PHE A 68 6801 5805 7173 182 990 13 C ATOM 508 CD2 PHE A 68 4.146 19.752 17.630 1.00 52.44 C ANISOU 508 CD2 PHE A 68 6796 5846 7281 134 1066 3 C ATOM 509 CE1 PHE A 68 3.286 17.232 16.952 1.00 52.72 C ANISOU 509 CE1 PHE A 68 6947 5861 7222 175 1053 11 C ATOM 510 CE2 PHE A 68 4.268 19.297 16.319 1.00 52.95 C ANISOU 510 CE2 PHE A 68 6933 5882 7305 128 1140 7 C ATOM 511 CZ PHE A 68 3.823 18.049 15.988 1.00 52.60 C ANISOU 511 CZ PHE A 68 6947 5828 7210 150 1127 9 C ATOM 512 N LEU A 69 6.687 19.302 19.965 1.00 50.40 N ANISOU 512 N LEU A 69 6300 5618 7232 213 996 -80 N ATOM 513 CA LEU A 69 7.921 19.003 19.233 1.00 50.08 C ANISOU 513 CA LEU A 69 6203 5554 7271 220 1079 -111 C ATOM 514 C LEU A 69 8.846 18.071 20.002 1.00 50.92 C ANISOU 514 C LEU A 69 6234 5662 7451 282 1030 -148 C ATOM 515 O LEU A 69 9.528 17.249 19.400 1.00 51.11 O ANISOU 515 O LEU A 69 6241 5666 7512 305 1090 -166 O ATOM 516 CB LEU A 69 8.635 20.292 18.814 1.00 49.65 C ANISOU 516 CB LEU A 69 6085 5483 7297 174 1148 -129 C ATOM 517 CG LEU A 69 7.863 21.202 17.871 1.00 50.24 C ANISOU 517 CG LEU A 69 6247 5542 7299 119 1208 -91 C ATOM 518 CD1 LEU A 69 8.334 22.608 17.979 1.00 50.46 C ANISOU 518 CD1 LEU A 69 6214 5556 7402 77 1235 -105 C ATOM 519 CD2 LEU A 69 7.966 20.727 16.478 1.00 51.06 C ANISOU 519 CD2 LEU A 69 6428 5613 7359 109 1320 -79 C ATOM 520 N CYS A 70 8.816 18.139 21.327 1.00 51.47 N ANISOU 520 N CYS A 70 6272 5752 7531 314 919 -158 N ATOM 521 CA CYS A 70 9.611 17.267 22.183 1.00 52.58 C ANISOU 521 CA CYS A 70 6360 5890 7728 385 844 -190 C ATOM 522 C CYS A 70 9.128 15.810 22.183 1.00 53.50 C ANISOU 522 C CYS A 70 6561 5997 7769 428 832 -164 C ATOM 523 O CYS A 70 9.919 14.926 22.470 1.00 54.24 O ANISOU 523 O CYS A 70 6617 6076 7915 488 803 -190 O ATOM 524 CB CYS A 70 9.698 17.835 23.594 1.00 53.41 C ANISOU 524 CB CYS A 70 6434 6012 7849 411 722 -209 C ATOM 525 SG CYS A 70 10.729 19.319 23.717 1.00 57.63 S ANISOU 525 SG CYS A 70 6831 6542 8524 376 718 -266 S ATOM 526 N THR A 71 7.853 15.552 21.834 1.00 53.39 N ANISOU 526 N THR A 71 6655 5986 7644 399 854 -117 N ATOM 527 CA THR A 71 7.312 14.190 21.748 1.00 53.40 C ANISOU 527 CA THR A 71 6738 5970 7580 429 852 -93 C ATOM 528 C THR A 71 7.681 13.498 20.443 1.00 53.05 C ANISOU 528 C THR A 71 6708 5901 7549 424 945 -103 C ATOM 529 O THR A 71 7.645 12.264 20.391 1.00 53.36 O ANISOU 529 O THR A 71 6790 5917 7566 462 943 -99 O ATOM 530 CB THR A 71 5.763 14.167 21.807 1.00 54.55 C ANISOU 530 CB THR A 71 6983 6121 7622 393 842 -47 C ATOM 531 OG1 THR A 71 5.200 14.615 20.565 1.00 55.68 O ANISOU 531 OG1 THR A 71 7161 6261 7734 337 910 -35 O ATOM 532 CG2 THR A 71 5.196 14.931 22.973 1.00 54.72 C ANISOU 532 CG2 THR A 71 7009 6164 7619 389 774 -34 C ATOM 533 N LEU A 72 7.921 14.284 19.363 1.00 52.12 N ANISOU 533 N LEU A 72 6573 5780 7450 377 1033 -111 N ATOM 534 CA LEU A 72 8.141 13.742 18.021 1.00 51.06 C ANISOU 534 CA LEU A 72 6482 5617 7302 368 1135 -117 C ATOM 535 C LEU A 72 9.254 12.702 17.908 1.00 51.01 C ANISOU 535 C LEU A 72 6425 5585 7370 424 1167 -154 C ATOM 536 O LEU A 72 8.952 11.687 17.301 1.00 51.71 O ANISOU 536 O LEU A 72 6590 5649 7407 438 1199 -148 O ATOM 537 CB LEU A 72 8.287 14.824 16.961 1.00 50.22 C ANISOU 537 CB LEU A 72 6382 5503 7197 312 1231 -117 C ATOM 538 CG LEU A 72 7.017 15.653 16.721 1.00 50.46 C ANISOU 538 CG LEU A 72 6494 5545 7134 262 1207 -77 C ATOM 539 CD1 LEU A 72 7.223 16.658 15.587 1.00 51.34 C ANISOU 539 CD1 LEU A 72 6634 5636 7235 215 1305 -73 C ATOM 540 CD2 LEU A 72 5.782 14.785 16.480 1.00 49.68 C ANISOU 540 CD2 LEU A 72 6503 5439 6934 264 1166 -51 C ATOM 541 N PRO A 73 10.453 12.791 18.523 1.00 50.34 N ANISOU 541 N PRO A 73 6219 5501 7407 464 1146 -195 N ATOM 542 CA PRO A 73 11.408 11.670 18.398 1.00 50.12 C ANISOU 542 CA PRO A 73 6147 5443 7453 527 1169 -231 C ATOM 543 C PRO A 73 10.831 10.326 18.880 1.00 50.78 C ANISOU 543 C PRO A 73 6315 5513 7465 577 1099 -209 C ATOM 544 O PRO A 73 11.105 9.321 18.260 1.00 51.78 O ANISOU 544 O PRO A 73 6471 5607 7596 607 1152 -222 O ATOM 545 CB PRO A 73 12.629 12.150 19.187 1.00 50.51 C ANISOU 545 CB PRO A 73 6043 5497 7651 561 1121 -281 C ATOM 546 CG PRO A 73 12.513 13.649 19.157 1.00 51.04 C ANISOU 546 CG PRO A 73 6072 5586 7734 494 1140 -278 C ATOM 547 CD PRO A 73 11.044 13.910 19.284 1.00 49.69 C ANISOU 547 CD PRO A 73 6028 5439 7414 455 1100 -219 C ATOM 548 N MET A 74 9.977 10.310 19.922 1.00 50.43 N ANISOU 548 N MET A 74 6321 5487 7352 583 994 -174 N ATOM 549 CA MET A 74 9.328 9.102 20.439 1.00 49.99 C ANISOU 549 CA MET A 74 6357 5410 7227 621 939 -146 C ATOM 550 C MET A 74 8.265 8.614 19.460 1.00 50.67 C ANISOU 550 C MET A 74 6554 5479 7220 576 1001 -119 C ATOM 551 O MET A 74 8.140 7.418 19.242 1.00 51.70 O ANISOU 551 O MET A 74 6742 5572 7327 605 1010 -117 O ATOM 552 CB MET A 74 8.651 9.369 21.807 1.00 49.90 C ANISOU 552 CB MET A 74 6379 5417 7164 630 834 -115 C ATOM 553 CG MET A 74 9.564 9.168 22.995 1.00 51.88 C ANISOU 553 CG MET A 74 6575 5662 7474 709 734 -138 C ATOM 554 SD MET A 74 8.833 9.516 24.613 1.00 54.55 S ANISOU 554 SD MET A 74 6981 6014 7732 726 620 -103 S ATOM 555 CE MET A 74 8.575 11.276 24.470 1.00 53.24 C ANISOU 555 CE MET A 74 6752 5897 7580 650 637 -111 C ATOM 556 N LEU A 75 7.461 9.520 18.912 1.00 50.30 N ANISOU 556 N LEU A 75 6539 5454 7120 507 1031 -100 N ATOM 557 CA LEU A 75 6.391 9.158 17.988 1.00 49.95 C ANISOU 557 CA LEU A 75 6598 5391 6991 465 1066 -80 C ATOM 558 C LEU A 75 6.962 8.649 16.660 1.00 50.84 C ANISOU 558 C LEU A 75 6737 5471 7107 470 1161 -109 C ATOM 559 O LEU A 75 6.479 7.628 16.158 1.00 51.85 O ANISOU 559 O LEU A 75 6948 5565 7187 476 1171 -108 O ATOM 560 CB LEU A 75 5.432 10.351 17.787 1.00 48.87 C ANISOU 560 CB LEU A 75 6482 5281 6804 400 1058 -56 C ATOM 561 CG LEU A 75 4.159 10.387 18.635 1.00 48.51 C ANISOU 561 CG LEU A 75 6475 5246 6712 380 986 -22 C ATOM 562 CD1 LEU A 75 4.411 10.058 20.086 1.00 48.14 C ANISOU 562 CD1 LEU A 75 6399 5205 6689 426 923 -14 C ATOM 563 CD2 LEU A 75 3.473 11.713 18.506 1.00 48.83 C ANISOU 563 CD2 LEU A 75 6509 5314 6729 328 978 -8 C ATOM 564 N ILE A 76 8.010 9.316 16.115 1.00 50.22 N ANISOU 564 N ILE A 76 6592 5398 7091 468 1236 -137 N ATOM 565 CA ILE A 76 8.682 8.902 14.884 1.00 50.51 C ANISOU 565 CA ILE A 76 6655 5400 7137 477 1349 -167 C ATOM 566 C ILE A 76 9.354 7.529 15.089 1.00 52.25 C ANISOU 566 C ILE A 76 6860 5587 7408 546 1349 -194 C ATOM 567 O ILE A 76 9.213 6.648 14.242 1.00 52.92 O ANISOU 567 O ILE A 76 7029 5633 7447 556 1400 -206 O ATOM 568 CB ILE A 76 9.688 9.968 14.391 1.00 50.48 C ANISOU 568 CB ILE A 76 6572 5401 7206 457 1445 -191 C ATOM 569 CG1 ILE A 76 9.010 11.337 14.144 1.00 51.42 C ANISOU 569 CG1 ILE A 76 6722 5544 7272 391 1447 -161 C ATOM 570 CG2 ILE A 76 10.372 9.493 13.124 1.00 50.50 C ANISOU 570 CG2 ILE A 76 6613 5359 7214 468 1582 -222 C ATOM 571 CD1 ILE A 76 10.027 12.539 14.099 1.00 52.70 C ANISOU 571 CD1 ILE A 76 6778 5713 7534 368 1519 -181 C ATOM 572 N ARG A 77 10.037 7.318 16.231 1.00 52.85 N ANISOU 572 N ARG A 77 6839 5671 7571 599 1281 -205 N ATOM 573 CA ARG A 77 10.665 6.033 16.521 1.00 54.26 C ANISOU 573 CA ARG A 77 7004 5813 7800 674 1265 -228 C ATOM 574 C ARG A 77 9.605 4.914 16.625 1.00 54.19 C ANISOU 574 C ARG A 77 7119 5775 7695 680 1218 -198 C ATOM 575 O ARG A 77 9.818 3.832 16.101 1.00 54.71 O ANISOU 575 O ARG A 77 7231 5795 7761 714 1256 -217 O ATOM 576 CB ARG A 77 11.539 6.114 17.794 1.00 57.51 C ANISOU 576 CB ARG A 77 7298 6237 8316 735 1175 -246 C ATOM 577 CG ARG A 77 12.544 4.970 17.942 1.00 64.69 C ANISOU 577 CG ARG A 77 8163 7104 9314 824 1169 -284 C ATOM 578 CD ARG A 77 12.270 4.080 19.147 1.00 71.23 C ANISOU 578 CD ARG A 77 9035 7913 10115 887 1043 -259 C ATOM 579 NE ARG A 77 12.613 2.670 18.926 1.00 77.22 N ANISOU 579 NE ARG A 77 9835 8614 10892 955 1056 -274 N ATOM 580 CZ ARG A 77 13.788 2.126 19.227 1.00 81.01 C ANISOU 580 CZ ARG A 77 10227 9065 11488 1042 1030 -318 C ATOM 581 NH1 ARG A 77 14.001 0.833 19.014 1.00 81.49 N ANISOU 581 NH1 ARG A 77 10337 9067 11557 1103 1043 -329 N ATOM 582 NH2 ARG A 77 14.759 2.869 19.748 1.00 80.96 N ANISOU 582 NH2 ARG A 77 10080 9081 11600 1071 985 -355 N ATOM 583 N SER A 78 8.454 5.186 17.245 1.00 53.66 N ANISOU 583 N SER A 78 7105 5728 7556 642 1145 -155 N ATOM 584 CA SER A 78 7.384 4.194 17.369 1.00 53.74 C ANISOU 584 CA SER A 78 7221 5704 7493 635 1109 -127 C ATOM 585 C SER A 78 6.775 3.838 16.024 1.00 54.30 C ANISOU 585 C SER A 78 7384 5747 7501 594 1172 -139 C ATOM 586 O SER A 78 6.622 2.662 15.742 1.00 54.58 O ANISOU 586 O SER A 78 7485 5733 7520 617 1180 -148 O ATOM 587 CB SER A 78 6.312 4.663 18.341 1.00 54.09 C ANISOU 587 CB SER A 78 7288 5774 7491 600 1035 -83 C ATOM 588 OG SER A 78 6.925 5.013 19.565 1.00 55.88 O ANISOU 588 OG SER A 78 7447 6023 7763 644 972 -78 O ATOM 589 N TYR A 79 6.465 4.828 15.183 1.00 54.60 N ANISOU 589 N TYR A 79 7435 5809 7500 539 1213 -140 N ATOM 590 CA TYR A 79 5.910 4.589 13.853 1.00 55.14 C ANISOU 590 CA TYR A 79 7608 5849 7495 506 1261 -155 C ATOM 591 C TYR A 79 6.919 3.893 12.941 1.00 56.94 C ANISOU 591 C TYR A 79 7855 6036 7743 548 1356 -198 C ATOM 592 O TYR A 79 6.542 2.999 12.194 1.00 57.44 O ANISOU 592 O TYR A 79 8018 6053 7756 551 1373 -216 O ATOM 593 CB TYR A 79 5.429 5.897 13.226 1.00 54.21 C ANISOU 593 CB TYR A 79 7509 5762 7328 448 1276 -143 C ATOM 594 CG TYR A 79 4.063 6.316 13.710 1.00 54.04 C ANISOU 594 CG TYR A 79 7509 5758 7264 401 1187 -110 C ATOM 595 CD1 TYR A 79 2.981 5.444 13.636 1.00 54.00 C ANISOU 595 CD1 TYR A 79 7578 5718 7222 385 1136 -108 C ATOM 596 CD2 TYR A 79 3.835 7.606 14.185 1.00 54.44 C ANISOU 596 CD2 TYR A 79 7505 5856 7324 370 1161 -86 C ATOM 597 CE1 TYR A 79 1.714 5.838 14.030 1.00 54.66 C ANISOU 597 CE1 TYR A 79 7668 5812 7287 340 1066 -84 C ATOM 598 CE2 TYR A 79 2.574 8.001 14.613 1.00 54.78 C ANISOU 598 CE2 TYR A 79 7562 5912 7339 330 1088 -60 C ATOM 599 CZ TYR A 79 1.514 7.117 14.514 1.00 55.65 C ANISOU 599 CZ TYR A 79 7736 5987 7421 315 1044 -60 C ATOM 600 OH TYR A 79 0.249 7.483 14.879 1.00 57.36 O ANISOU 600 OH TYR A 79 7955 6210 7629 274 982 -42 O ATOM 601 N ALA A 80 8.201 4.254 13.034 1.00 57.82 N ANISOU 601 N ALA A 80 7869 6160 7939 582 1417 -219 N ATOM 602 CA ALA A 80 9.246 3.613 12.234 1.00 59.05 C ANISOU 602 CA ALA A 80 8025 6275 8135 627 1523 -265 C ATOM 603 C ALA A 80 9.452 2.135 12.590 1.00 60.23 C ANISOU 603 C ALA A 80 8192 6378 8315 690 1493 -281 C ATOM 604 O ALA A 80 9.814 1.347 11.719 1.00 60.91 O ANISOU 604 O ALA A 80 8337 6416 8391 718 1569 -316 O ATOM 605 CB ALA A 80 10.559 4.376 12.356 1.00 59.13 C ANISOU 605 CB ALA A 80 7901 6305 8259 646 1593 -289 C ATOM 606 N THR A 81 9.231 1.749 13.856 1.00 60.67 N ANISOU 606 N THR A 81 8210 6441 8402 717 1388 -255 N ATOM 607 CA THR A 81 9.379 0.348 14.301 1.00 61.37 C ANISOU 607 CA THR A 81 8326 6477 8515 780 1352 -261 C ATOM 608 C THR A 81 8.028 -0.435 14.299 1.00 61.90 C ANISOU 608 C THR A 81 8517 6509 8493 745 1299 -235 C ATOM 609 O THR A 81 8.030 -1.645 14.415 1.00 62.47 O ANISOU 609 O THR A 81 8638 6524 8572 786 1287 -242 O ATOM 610 CB THR A 81 10.110 0.260 15.672 1.00 62.85 C ANISOU 610 CB THR A 81 8412 6675 8792 845 1274 -253 C ATOM 611 OG1 THR A 81 9.285 0.787 16.715 1.00 64.22 O ANISOU 611 OG1 THR A 81 8590 6884 8926 813 1180 -204 O ATOM 612 CG2 THR A 81 11.475 0.977 15.673 1.00 63.27 C ANISOU 612 CG2 THR A 81 8324 6755 8961 880 1317 -292 C ATOM 613 N GLY A 82 6.900 0.257 14.210 1.00 61.82 N ANISOU 613 N GLY A 82 8547 6527 8414 672 1266 -207 N ATOM 614 CA GLY A 82 5.588 -0.373 14.158 1.00 62.04 C ANISOU 614 CA GLY A 82 8672 6519 8380 630 1218 -190 C ATOM 615 C GLY A 82 4.885 -0.607 15.476 1.00 62.62 C ANISOU 615 C GLY A 82 8738 6591 8463 625 1140 -145 C ATOM 616 O GLY A 82 3.729 -1.053 15.488 1.00 63.12 O ANISOU 616 O GLY A 82 8867 6621 8494 581 1109 -131 O ATOM 617 N ASN A 83 5.556 -0.322 16.599 1.00 62.32 N ANISOU 617 N ASN A 83 8626 6581 8473 669 1108 -124 N ATOM 618 CA ASN A 83 4.952 -0.574 17.902 1.00 62.45 C ANISOU 618 CA ASN A 83 8657 6587 8484 672 1044 -78 C ATOM 619 C ASN A 83 5.312 0.449 18.977 1.00 61.38 C ANISOU 619 C ASN A 83 8444 6509 8367 688 998 -54 C ATOM 620 O ASN A 83 6.297 1.200 18.870 1.00 61.68 O ANISOU 620 O ASN A 83 8398 6590 8449 712 1008 -78 O ATOM 621 CB ASN A 83 5.262 -2.002 18.381 1.00 65.12 C ANISOU 621 CB ASN A 83 9049 6851 8842 736 1032 -74 C ATOM 622 CG ASN A 83 6.714 -2.398 18.292 1.00 70.60 C ANISOU 622 CG ASN A 83 9692 7533 9598 824 1046 -107 C ATOM 623 OD1 ASN A 83 7.630 -1.546 18.282 1.00 72.93 O ANISOU 623 OD1 ASN A 83 9891 7880 9939 847 1051 -128 O ATOM 624 ND2 ASN A 83 6.954 -3.711 18.208 1.00 70.85 N ANISOU 624 ND2 ASN A 83 9783 7491 9645 875 1055 -118 N ATOM 625 N TRP A 84 4.480 0.469 20.022 1.00 59.53 N ANISOU 625 N TRP A 84 8245 6270 8103 670 954 -10 N ATOM 626 CA TRP A 84 4.681 1.340 21.149 1.00 58.03 C ANISOU 626 CA TRP A 84 8008 6124 7915 687 904 13 C ATOM 627 C TRP A 84 5.480 0.552 22.159 1.00 57.47 C ANISOU 627 C TRP A 84 7957 6016 7864 778 856 23 C ATOM 628 O TRP A 84 5.069 -0.538 22.537 1.00 58.07 O ANISOU 628 O TRP A 84 8121 6028 7917 797 854 48 O ATOM 629 CB TRP A 84 3.333 1.771 21.744 1.00 56.96 C ANISOU 629 CB TRP A 84 7913 5996 7732 624 893 53 C ATOM 630 CG TRP A 84 3.504 2.667 22.918 1.00 56.23 C ANISOU 630 CG TRP A 84 7790 5946 7631 643 846 75 C ATOM 631 CD1 TRP A 84 3.305 2.344 24.224 1.00 56.98 C ANISOU 631 CD1 TRP A 84 7944 6013 7693 679 810 112 C ATOM 632 CD2 TRP A 84 4.039 4.001 22.908 1.00 55.53 C ANISOU 632 CD2 TRP A 84 7612 5925 7563 636 826 56 C ATOM 633 NE1 TRP A 84 3.635 3.414 25.028 1.00 56.90 N ANISOU 633 NE1 TRP A 84 7892 6053 7676 695 763 115 N ATOM 634 CE2 TRP A 84 4.107 4.434 24.246 1.00 56.07 C ANISOU 634 CE2 TRP A 84 7688 6006 7610 668 770 79 C ATOM 635 CE3 TRP A 84 4.489 4.862 21.900 1.00 55.39 C ANISOU 635 CE3 TRP A 84 7519 5950 7577 607 856 22 C ATOM 636 CZ2 TRP A 84 4.530 5.709 24.591 1.00 56.20 C ANISOU 636 CZ2 TRP A 84 7631 6079 7643 665 735 65 C ATOM 637 CZ3 TRP A 84 4.960 6.106 22.254 1.00 55.78 C ANISOU 637 CZ3 TRP A 84 7492 6051 7649 603 831 12 C ATOM 638 CH2 TRP A 84 4.970 6.521 23.584 1.00 55.87 C ANISOU 638 CH2 TRP A 84 7505 6078 7647 631 766 31 C ATOM 639 N THR A 85 6.666 1.042 22.524 1.00 56.19 N ANISOU 639 N THR A 85 7713 5885 7752 838 815 -1 N ATOM 640 CA THR A 85 7.530 0.339 23.476 1.00 55.38 C ANISOU 640 CA THR A 85 7624 5744 7675 939 746 2 C ATOM 641 C THR A 85 7.939 1.204 24.649 1.00 53.85 C ANISOU 641 C THR A 85 7392 5588 7481 975 659 8 C ATOM 642 O THR A 85 8.687 0.721 25.485 1.00 53.88 O ANISOU 642 O THR A 85 7409 5560 7502 1067 581 6 O ATOM 643 CB THR A 85 8.835 -0.162 22.789 1.00 57.15 C ANISOU 643 CB THR A 85 7776 5949 7988 1005 760 -52 C ATOM 644 OG1 THR A 85 9.608 0.955 22.312 1.00 58.99 O ANISOU 644 OG1 THR A 85 7879 6242 8291 991 777 -96 O ATOM 645 CG2 THR A 85 8.575 -1.132 21.665 1.00 57.12 C ANISOU 645 CG2 THR A 85 7825 5899 7981 986 841 -66 C ATOM 646 N TYR A 86 7.506 2.471 24.709 1.00 52.73 N ANISOU 646 N TYR A 86 7206 5507 7322 912 663 11 N ATOM 647 CA TYR A 86 7.923 3.397 25.750 1.00 52.07 C ANISOU 647 CA TYR A 86 7083 5461 7242 942 580 8 C ATOM 648 C TYR A 86 7.240 3.233 27.112 1.00 52.79 C ANISOU 648 C TYR A 86 7291 5526 7240 966 525 58 C ATOM 649 O TYR A 86 7.748 3.797 28.080 1.00 53.10 O ANISOU 649 O TYR A 86 7319 5581 7275 1015 437 50 O ATOM 650 CB TYR A 86 7.795 4.835 25.277 1.00 50.83 C ANISOU 650 CB TYR A 86 6836 5372 7107 869 608 -12 C ATOM 651 CG TYR A 86 8.807 5.204 24.227 1.00 50.40 C ANISOU 651 CG TYR A 86 6658 5338 7152 865 651 -66 C ATOM 652 CD1 TYR A 86 10.081 5.616 24.580 1.00 50.86 C ANISOU 652 CD1 TYR A 86 6608 5410 7306 922 591 -113 C ATOM 653 CD2 TYR A 86 8.492 5.144 22.875 1.00 50.74 C ANISOU 653 CD2 TYR A 86 6699 5384 7197 805 753 -74 C ATOM 654 CE1 TYR A 86 11.018 5.955 23.616 1.00 51.49 C ANISOU 654 CE1 TYR A 86 6570 5502 7493 913 652 -165 C ATOM 655 CE2 TYR A 86 9.427 5.461 21.901 1.00 50.87 C ANISOU 655 CE2 TYR A 86 6619 5410 7297 802 813 -122 C ATOM 656 CZ TYR A 86 10.689 5.870 22.277 1.00 52.05 C ANISOU 656 CZ TYR A 86 6652 5571 7552 853 772 -166 C ATOM 657 OH TYR A 86 11.621 6.225 21.340 1.00 54.25 O ANISOU 657 OH TYR A 86 6829 5854 7929 845 851 -214 O ATOM 658 N GLY A 87 6.140 2.477 27.197 1.00 52.52 N ANISOU 658 N GLY A 87 7371 5447 7138 933 578 106 N ATOM 659 CA GLY A 87 5.480 2.271 28.481 1.00 52.71 C ANISOU 659 CA GLY A 87 7520 5435 7073 953 552 157 C ATOM 660 C GLY A 87 4.242 3.102 28.739 1.00 52.72 C ANISOU 660 C GLY A 87 7545 5465 7022 869 602 185 C ATOM 661 O GLY A 87 3.874 3.934 27.911 1.00 53.39 O ANISOU 661 O GLY A 87 7545 5601 7139 794 643 165 O ATOM 662 N ASP A 88 3.600 2.898 29.908 1.00 52.05 N ANISOU 662 N ASP A 88 7583 5340 6855 885 601 233 N ATOM 663 CA ASP A 88 2.349 3.555 30.272 1.00 52.20 C ANISOU 663 CA ASP A 88 7635 5370 6827 812 663 262 C ATOM 664 C ASP A 88 2.452 5.060 30.612 1.00 51.58 C ANISOU 664 C ASP A 88 7490 5365 6745 796 623 239 C ATOM 665 O ASP A 88 1.617 5.823 30.139 1.00 51.43 O ANISOU 665 O ASP A 88 7417 5381 6742 714 678 236 O ATOM 666 CB ASP A 88 1.609 2.809 31.386 1.00 54.35 C ANISOU 666 CB ASP A 88 8071 5565 7014 832 702 320 C ATOM 667 CG ASP A 88 2.409 2.466 32.618 1.00 61.99 C ANISOU 667 CG ASP A 88 9151 6494 7909 943 614 338 C ATOM 668 OD1 ASP A 88 3.507 3.036 32.790 1.00 64.34 O ANISOU 668 OD1 ASP A 88 9386 6835 8225 1005 505 298 O ATOM 669 OD2 ASP A 88 1.929 1.628 33.427 1.00 64.86 O ANISOU 669 OD2 ASP A 88 9670 6777 8198 970 653 391 O ATOM 670 N VAL A 89 3.450 5.489 31.395 1.00 50.89 N ANISOU 670 N VAL A 89 7401 5294 6641 873 521 219 N ATOM 671 CA VAL A 89 3.614 6.908 31.766 1.00 50.62 C ANISOU 671 CA VAL A 89 7306 5321 6608 861 474 191 C ATOM 672 C VAL A 89 3.780 7.776 30.509 1.00 50.10 C ANISOU 672 C VAL A 89 7084 5319 6633 792 501 150 C ATOM 673 O VAL A 89 3.126 8.821 30.385 1.00 50.20 O ANISOU 673 O VAL A 89 7059 5371 6644 729 533 148 O ATOM 674 CB VAL A 89 4.792 7.113 32.789 1.00 51.15 C ANISOU 674 CB VAL A 89 7394 5385 6656 965 337 165 C ATOM 675 CG1 VAL A 89 5.066 8.584 33.063 1.00 51.99 C ANISOU 675 CG1 VAL A 89 7420 5551 6782 949 281 124 C ATOM 676 CG2 VAL A 89 4.545 6.369 34.095 1.00 50.99 C ANISOU 676 CG2 VAL A 89 7559 5296 6519 1036 310 211 C ATOM 677 N LEU A 90 4.629 7.318 29.568 1.00 49.55 N ANISOU 677 N LEU A 90 6935 5251 6639 807 495 119 N ATOM 678 CA LEU A 90 4.901 8.032 28.327 1.00 50.15 C ANISOU 678 CA LEU A 90 6885 5376 6795 750 532 83 C ATOM 679 C LEU A 90 3.741 7.951 27.324 1.00 51.53 C ANISOU 679 C LEU A 90 7069 5551 6961 663 630 103 C ATOM 680 O LEU A 90 3.620 8.826 26.471 1.00 52.68 O ANISOU 680 O LEU A 90 7140 5736 7140 606 661 84 O ATOM 681 CB LEU A 90 6.239 7.607 27.702 1.00 49.83 C ANISOU 681 CB LEU A 90 6760 5331 6840 799 506 39 C ATOM 682 CG LEU A 90 7.471 8.103 28.461 1.00 49.74 C ANISOU 682 CG LEU A 90 6686 5334 6880 871 398 -3 C ATOM 683 CD1 LEU A 90 8.732 7.447 27.956 1.00 49.13 C ANISOU 683 CD1 LEU A 90 6530 5238 6900 931 375 -46 C ATOM 684 CD2 LEU A 90 7.557 9.623 28.456 1.00 49.62 C ANISOU 684 CD2 LEU A 90 6583 5373 6897 823 387 -31 C ATOM 685 N CYS A 91 2.860 6.964 27.455 1.00 51.51 N ANISOU 685 N CYS A 91 7159 5499 6915 652 673 140 N ATOM 686 CA CYS A 91 1.663 6.879 26.634 1.00 52.35 C ANISOU 686 CA CYS A 91 7271 5598 7020 571 747 153 C ATOM 687 C CYS A 91 0.730 8.041 27.030 1.00 52.44 C ANISOU 687 C CYS A 91 7272 5643 7012 518 760 164 C ATOM 688 O CYS A 91 0.238 8.758 26.168 1.00 53.63 O ANISOU 688 O CYS A 91 7365 5823 7188 457 785 151 O ATOM 689 CB CYS A 91 0.963 5.535 26.830 1.00 54.19 C ANISOU 689 CB CYS A 91 7602 5760 7229 571 788 186 C ATOM 690 SG CYS A 91 -0.652 5.430 26.005 1.00 62.22 S ANISOU 690 SG CYS A 91 8621 6757 8262 470 863 194 S ATOM 691 N ILE A 92 0.485 8.218 28.330 1.00 51.03 N ANISOU 691 N ILE A 92 7156 5453 6782 545 744 188 N ATOM 692 CA ILE A 92 -0.405 9.241 28.822 1.00 50.76 C ANISOU 692 CA ILE A 92 7119 5440 6726 503 765 198 C ATOM 693 C ILE A 92 0.154 10.639 28.585 1.00 51.07 C ANISOU 693 C ILE A 92 7068 5543 6794 494 721 164 C ATOM 694 O ILE A 92 -0.581 11.513 28.129 1.00 50.91 O ANISOU 694 O ILE A 92 7002 5549 6793 435 749 159 O ATOM 695 CB ILE A 92 -0.747 8.978 30.319 1.00 51.41 C ANISOU 695 CB ILE A 92 7316 5484 6734 543 770 232 C ATOM 696 CG1 ILE A 92 -1.409 7.602 30.493 1.00 52.94 C ANISOU 696 CG1 ILE A 92 7604 5603 6909 539 835 270 C ATOM 697 CG2 ILE A 92 -1.639 10.095 30.915 1.00 51.32 C ANISOU 697 CG2 ILE A 92 7306 5493 6701 505 800 237 C ATOM 698 CD1 ILE A 92 -1.510 7.207 31.972 1.00 55.67 C ANISOU 698 CD1 ILE A 92 8090 5898 7165 594 844 309 C ATOM 699 N SER A 93 1.460 10.853 28.862 1.00 50.79 N ANISOU 699 N SER A 93 7000 5526 6771 552 649 137 N ATOM 700 CA SER A 93 2.056 12.173 28.675 1.00 50.36 C ANISOU 700 CA SER A 93 6856 5523 6757 539 611 101 C ATOM 701 C SER A 93 2.073 12.587 27.214 1.00 49.28 C ANISOU 701 C SER A 93 6635 5411 6680 482 655 83 C ATOM 702 O SER A 93 1.675 13.719 26.921 1.00 49.02 O ANISOU 702 O SER A 93 6560 5406 6658 435 668 76 O ATOM 703 CB SER A 93 3.433 12.281 29.333 1.00 51.88 C ANISOU 703 CB SER A 93 7022 5721 6970 613 520 68 C ATOM 704 OG SER A 93 4.405 11.455 28.722 1.00 54.78 O ANISOU 704 OG SER A 93 7348 6075 7392 649 507 49 O ATOM 705 N ASN A 94 2.403 11.651 26.292 1.00 48.44 N ANISOU 705 N ASN A 94 6522 5285 6599 485 683 79 N ATOM 706 CA ASN A 94 2.376 11.939 24.851 1.00 48.24 C ANISOU 706 CA ASN A 94 6447 5272 6609 435 732 65 C ATOM 707 C ASN A 94 0.963 12.148 24.337 1.00 46.57 C ANISOU 707 C ASN A 94 6266 5057 6372 371 772 86 C ATOM 708 O ASN A 94 0.753 13.085 23.574 1.00 46.10 O ANISOU 708 O ASN A 94 6170 5020 6327 329 786 76 O ATOM 709 CB ASN A 94 3.039 10.842 24.026 1.00 50.80 C ANISOU 709 CB ASN A 94 6772 5571 6959 460 757 51 C ATOM 710 CG ASN A 94 4.541 10.825 24.085 1.00 57.01 C ANISOU 710 CG ASN A 94 7492 6363 7805 513 730 16 C ATOM 711 OD1 ASN A 94 5.186 11.760 24.529 1.00 59.42 O ANISOU 711 OD1 ASN A 94 7734 6696 8148 523 693 -6 O ATOM 712 ND2 ASN A 94 5.139 9.751 23.646 1.00 59.33 N ANISOU 712 ND2 ASN A 94 7793 6628 8123 551 747 4 N ATOM 713 N ARG A 95 -0.010 11.283 24.745 1.00 45.37 N ANISOU 713 N ARG A 95 6179 4869 6190 365 788 112 N ATOM 714 CA ARG A 95 -1.409 11.424 24.323 1.00 44.55 C ANISOU 714 CA ARG A 95 6089 4754 6084 305 818 124 C ATOM 715 C ARG A 95 -1.987 12.759 24.810 1.00 44.70 C ANISOU 715 C ARG A 95 6078 4803 6102 279 809 126 C ATOM 716 O ARG A 95 -2.739 13.401 24.077 1.00 44.52 O ANISOU 716 O ARG A 95 6031 4789 6097 233 816 121 O ATOM 717 CB ARG A 95 -2.264 10.259 24.837 1.00 44.41 C ANISOU 717 CB ARG A 95 6136 4684 6054 303 847 148 C ATOM 718 CG ARG A 95 -2.033 8.951 24.110 1.00 44.29 C ANISOU 718 CG ARG A 95 6153 4629 6048 312 861 142 C ATOM 719 CD ARG A 95 -2.788 8.843 22.793 1.00 45.49 C ANISOU 719 CD ARG A 95 6294 4768 6223 258 873 124 C ATOM 720 NE ARG A 95 -2.445 7.574 22.141 1.00 46.78 N ANISOU 720 NE ARG A 95 6497 4889 6389 273 884 114 N ATOM 721 CZ ARG A 95 -2.607 7.306 20.843 1.00 46.17 C ANISOU 721 CZ ARG A 95 6426 4798 6318 249 884 88 C ATOM 722 NH1 ARG A 95 -2.239 6.121 20.348 1.00 44.66 N ANISOU 722 NH1 ARG A 95 6278 4565 6126 269 897 75 N ATOM 723 NH2 ARG A 95 -3.145 8.213 20.031 1.00 42.77 N ANISOU 723 NH2 ARG A 95 5971 4391 5888 209 867 72 N ATOM 724 N TYR A 96 -1.599 13.192 26.021 1.00 44.96 N ANISOU 724 N TYR A 96 6119 4849 6113 314 786 131 N ATOM 725 CA TYR A 96 -2.017 14.473 26.564 1.00 46.17 C ANISOU 725 CA TYR A 96 6250 5029 6263 297 777 128 C ATOM 726 C TYR A 96 -1.456 15.612 25.708 1.00 47.40 C ANISOU 726 C TYR A 96 6337 5220 6451 276 758 104 C ATOM 727 O TYR A 96 -2.221 16.406 25.184 1.00 47.73 O ANISOU 727 O TYR A 96 6357 5270 6507 234 769 104 O ATOM 728 CB TYR A 96 -1.605 14.640 28.060 1.00 46.25 C ANISOU 728 CB TYR A 96 6303 5039 6232 347 748 132 C ATOM 729 CG TYR A 96 -1.771 16.057 28.577 1.00 46.98 C ANISOU 729 CG TYR A 96 6370 5160 6322 337 730 119 C ATOM 730 CD1 TYR A 96 -3.026 16.573 28.857 1.00 48.39 C ANISOU 730 CD1 TYR A 96 6559 5331 6496 302 771 130 C ATOM 731 CD2 TYR A 96 -0.681 16.895 28.728 1.00 47.70 C ANISOU 731 CD2 TYR A 96 6415 5280 6429 359 673 89 C ATOM 732 CE1 TYR A 96 -3.193 17.892 29.267 1.00 49.32 C ANISOU 732 CE1 TYR A 96 6653 5471 6615 293 757 115 C ATOM 733 CE2 TYR A 96 -0.835 18.217 29.131 1.00 49.00 C ANISOU 733 CE2 TYR A 96 6556 5465 6596 345 656 73 C ATOM 734 CZ TYR A 96 -2.094 18.718 29.385 1.00 50.25 C ANISOU 734 CZ TYR A 96 6735 5616 6740 314 698 87 C ATOM 735 OH TYR A 96 -2.248 20.008 29.843 1.00 52.54 O ANISOU 735 OH TYR A 96 7009 5922 7033 306 682 69 O ATOM 736 N VAL A 97 -0.133 15.684 25.564 1.00 47.86 N ANISOU 736 N VAL A 97 6361 5294 6529 306 733 83 N ATOM 737 CA VAL A 97 0.538 16.777 24.864 1.00 48.70 C ANISOU 737 CA VAL A 97 6404 5426 6675 286 729 60 C ATOM 738 C VAL A 97 0.047 16.976 23.418 1.00 49.65 C ANISOU 738 C VAL A 97 6522 5540 6801 238 769 64 C ATOM 739 O VAL A 97 -0.070 18.121 22.977 1.00 50.27 O ANISOU 739 O VAL A 97 6576 5631 6893 208 773 60 O ATOM 740 CB VAL A 97 2.073 16.588 24.946 1.00 49.27 C ANISOU 740 CB VAL A 97 6430 5503 6788 327 706 31 C ATOM 741 CG1 VAL A 97 2.803 17.481 23.964 1.00 49.59 C ANISOU 741 CG1 VAL A 97 6405 5555 6883 297 734 9 C ATOM 742 CG2 VAL A 97 2.573 16.834 26.363 1.00 49.65 C ANISOU 742 CG2 VAL A 97 6476 5557 6831 374 640 18 C ATOM 743 N LEU A 98 -0.235 15.880 22.683 1.00 49.28 N ANISOU 743 N LEU A 98 6512 5471 6742 235 793 71 N ATOM 744 CA LEU A 98 -0.689 16.002 21.300 1.00 48.74 C ANISOU 744 CA LEU A 98 6462 5390 6665 199 817 71 C ATOM 745 C LEU A 98 -2.051 16.691 21.215 1.00 49.34 C ANISOU 745 C LEU A 98 6548 5464 6734 162 800 82 C ATOM 746 O LEU A 98 -2.170 17.679 20.497 1.00 50.12 O ANISOU 746 O LEU A 98 6642 5568 6832 139 799 80 O ATOM 747 CB LEU A 98 -0.648 14.672 20.549 1.00 47.69 C ANISOU 747 CB LEU A 98 6373 5229 6520 208 837 68 C ATOM 748 CG LEU A 98 0.678 14.291 19.826 1.00 48.45 C ANISOU 748 CG LEU A 98 6460 5321 6629 231 874 48 C ATOM 749 CD1 LEU A 98 0.813 14.948 18.493 1.00 48.40 C ANISOU 749 CD1 LEU A 98 6472 5310 6609 203 911 41 C ATOM 750 CD2 LEU A 98 1.910 14.481 20.675 1.00 48.99 C ANISOU 750 CD2 LEU A 98 6467 5408 6741 270 866 34 C ATOM 751 N HIS A 99 -3.037 16.249 22.000 1.00 48.85 N ANISOU 751 N HIS A 99 6498 5390 6672 160 791 94 N ATOM 752 CA HIS A 99 -4.342 16.909 22.021 1.00 48.76 C ANISOU 752 CA HIS A 99 6479 5374 6676 128 778 98 C ATOM 753 C HIS A 99 -4.244 18.307 22.639 1.00 48.21 C ANISOU 753 C HIS A 99 6374 5329 6613 128 767 97 C ATOM 754 O HIS A 99 -4.880 19.233 22.139 1.00 48.46 O ANISOU 754 O HIS A 99 6394 5361 6658 105 751 95 O ATOM 755 CB HIS A 99 -5.379 16.066 22.782 1.00 49.58 C ANISOU 755 CB HIS A 99 6595 5450 6795 123 792 107 C ATOM 756 CG HIS A 99 -6.271 15.243 21.900 1.00 51.68 C ANISOU 756 CG HIS A 99 6875 5679 7082 96 786 99 C ATOM 757 ND1 HIS A 99 -5.763 14.222 21.112 1.00 52.98 N ANISOU 757 ND1 HIS A 99 7075 5825 7229 104 788 92 N ATOM 758 CD2 HIS A 99 -7.617 15.290 21.739 1.00 52.58 C ANISOU 758 CD2 HIS A 99 6968 5767 7243 65 775 91 C ATOM 759 CE1 HIS A 99 -6.806 13.695 20.490 1.00 53.22 C ANISOU 759 CE1 HIS A 99 7112 5819 7289 75 770 79 C ATOM 760 NE2 HIS A 99 -7.939 14.312 20.822 1.00 53.39 N ANISOU 760 NE2 HIS A 99 7095 5835 7357 51 758 76 N ATOM 761 N ALA A 100 -3.465 18.468 23.716 1.00 47.42 N ANISOU 761 N ALA A 100 6265 5247 6505 156 767 96 N ATOM 762 CA ALA A 100 -3.354 19.762 24.381 1.00 47.27 C ANISOU 762 CA ALA A 100 6219 5248 6493 157 751 88 C ATOM 763 C ALA A 100 -2.739 20.825 23.476 1.00 47.59 C ANISOU 763 C ALA A 100 6232 5300 6551 139 745 78 C ATOM 764 O ALA A 100 -3.241 21.944 23.432 1.00 47.57 O ANISOU 764 O ALA A 100 6216 5298 6560 120 736 77 O ATOM 765 CB ALA A 100 -2.607 19.647 25.699 1.00 47.10 C ANISOU 765 CB ALA A 100 6206 5238 6454 197 737 82 C ATOM 766 N ASN A 101 -1.728 20.459 22.684 1.00 47.81 N ANISOU 766 N ASN A 101 6255 5327 6582 142 760 72 N ATOM 767 CA ASN A 101 -1.129 21.409 21.747 1.00 48.43 C ANISOU 767 CA ASN A 101 6319 5404 6677 121 778 65 C ATOM 768 C ASN A 101 -2.134 21.851 20.662 1.00 48.49 C ANISOU 768 C ASN A 101 6367 5392 6664 92 777 80 C ATOM 769 O ASN A 101 -2.132 23.007 20.256 1.00 49.63 O ANISOU 769 O ASN A 101 6511 5531 6815 74 778 82 O ATOM 770 CB ASN A 101 0.181 20.859 21.132 1.00 49.33 C ANISOU 770 CB ASN A 101 6421 5515 6807 132 814 53 C ATOM 771 CG ASN A 101 0.693 21.656 19.957 1.00 52.27 C ANISOU 771 CG ASN A 101 6799 5872 7189 104 860 52 C ATOM 772 OD1 ASN A 101 0.744 21.182 18.839 1.00 53.70 O ANISOU 772 OD1 ASN A 101 7026 6034 7342 98 897 58 O ATOM 773 ND2 ASN A 101 1.017 22.906 20.164 1.00 53.37 N ANISOU 773 ND2 ASN A 101 6905 6013 7361 86 862 46 N ATOM 774 N LEU A 102 -2.969 20.938 20.201 1.00 47.33 N ANISOU 774 N LEU A 102 6256 5230 6496 91 767 87 N ATOM 775 CA LEU A 102 -3.923 21.211 19.161 1.00 47.28 C ANISOU 775 CA LEU A 102 6291 5200 6473 72 744 93 C ATOM 776 C LEU A 102 -4.961 22.256 19.607 1.00 48.11 C ANISOU 776 C LEU A 102 6374 5304 6603 63 708 96 C ATOM 777 O LEU A 102 -5.149 23.272 18.926 1.00 48.64 O ANISOU 777 O LEU A 102 6461 5356 6662 53 693 101 O ATOM 778 CB LEU A 102 -4.577 19.886 18.785 1.00 47.63 C ANISOU 778 CB LEU A 102 6366 5225 6506 74 731 89 C ATOM 779 CG LEU A 102 -5.236 19.777 17.419 1.00 50.04 C ANISOU 779 CG LEU A 102 6732 5498 6782 64 698 85 C ATOM 780 CD1 LEU A 102 -4.189 19.639 16.324 1.00 50.62 C ANISOU 780 CD1 LEU A 102 6866 5561 6806 69 738 85 C ATOM 781 CD2 LEU A 102 -6.125 18.558 17.364 1.00 50.66 C ANISOU 781 CD2 LEU A 102 6818 5554 6875 61 670 73 C ATOM 782 N TYR A 103 -5.585 22.044 20.786 1.00 47.45 N ANISOU 782 N TYR A 103 6254 5230 6547 69 703 92 N ATOM 783 CA TYR A 103 -6.653 22.894 21.282 1.00 46.49 C ANISOU 783 CA TYR A 103 6105 5103 6458 63 681 90 C ATOM 784 C TYR A 103 -6.174 24.141 22.055 1.00 46.79 C ANISOU 784 C TYR A 103 6117 5157 6503 68 688 87 C ATOM 785 O TYR A 103 -6.908 25.124 22.074 1.00 46.86 O ANISOU 785 O TYR A 103 6114 5155 6536 63 667 84 O ATOM 786 CB TYR A 103 -7.647 22.060 22.073 1.00 45.75 C ANISOU 786 CB TYR A 103 5990 5000 6395 63 691 86 C ATOM 787 CG TYR A 103 -8.289 21.027 21.172 1.00 46.47 C ANISOU 787 CG TYR A 103 6098 5063 6495 52 671 81 C ATOM 788 CD1 TYR A 103 -8.094 19.665 21.388 1.00 47.31 C ANISOU 788 CD1 TYR A 103 6221 5162 6594 54 698 83 C ATOM 789 CD2 TYR A 103 -8.946 21.406 20.009 1.00 46.93 C ANISOU 789 CD2 TYR A 103 6169 5098 6563 43 616 73 C ATOM 790 CE1 TYR A 103 -8.618 18.711 20.518 1.00 47.79 C ANISOU 790 CE1 TYR A 103 6300 5192 6665 41 675 73 C ATOM 791 CE2 TYR A 103 -9.511 20.462 19.154 1.00 47.58 C ANISOU 791 CE2 TYR A 103 6273 5151 6653 34 582 60 C ATOM 792 CZ TYR A 103 -9.343 19.115 19.410 1.00 48.46 C ANISOU 792 CZ TYR A 103 6392 5255 6764 31 614 58 C ATOM 793 OH TYR A 103 -9.891 18.195 18.550 1.00 49.87 O ANISOU 793 OH TYR A 103 6594 5400 6955 21 576 40 O ATOM 794 N THR A 104 -4.958 24.138 22.659 1.00 46.65 N ANISOU 794 N THR A 104 6091 5161 6474 79 708 82 N ATOM 795 CA THR A 104 -4.438 25.364 23.300 1.00 46.40 C ANISOU 795 CA THR A 104 6036 5139 6456 80 703 71 C ATOM 796 C THR A 104 -4.012 26.329 22.187 1.00 46.56 C ANISOU 796 C THR A 104 6066 5143 6482 59 706 76 C ATOM 797 O THR A 104 -4.239 27.516 22.326 1.00 47.52 O ANISOU 797 O THR A 104 6179 5254 6621 52 694 73 O ATOM 798 CB THR A 104 -3.227 25.128 24.256 1.00 46.82 C ANISOU 798 CB THR A 104 6071 5212 6506 101 706 54 C ATOM 799 OG1 THR A 104 -2.257 24.323 23.618 1.00 48.00 O ANISOU 799 OG1 THR A 104 6221 5365 6654 104 721 54 O ATOM 800 CG2 THR A 104 -3.600 24.482 25.551 1.00 46.91 C ANISOU 800 CG2 THR A 104 6096 5231 6497 128 702 51 C ATOM 801 N SER A 105 -3.423 25.831 21.080 1.00 45.82 N ANISOU 801 N SER A 105 6000 5040 6370 51 727 85 N ATOM 802 CA SER A 105 -2.968 26.693 20.001 1.00 45.66 C ANISOU 802 CA SER A 105 6010 4995 6345 32 749 94 C ATOM 803 C SER A 105 -4.063 27.542 19.380 1.00 44.98 C ANISOU 803 C SER A 105 5963 4879 6247 26 714 109 C ATOM 804 O SER A 105 -3.859 28.744 19.232 1.00 45.49 O ANISOU 804 O SER A 105 6035 4924 6324 14 721 114 O ATOM 805 CB SER A 105 -2.224 25.906 18.933 1.00 47.52 C ANISOU 805 CB SER A 105 6283 5220 6552 28 791 100 C ATOM 806 OG SER A 105 -3.115 25.058 18.234 1.00 51.12 O ANISOU 806 OG SER A 105 6791 5665 6969 35 765 110 O ATOM 807 N ILE A 106 -5.215 26.960 19.042 1.00 44.01 N ANISOU 807 N ILE A 106 5862 4748 6110 35 673 113 N ATOM 808 CA ILE A 106 -6.305 27.735 18.449 1.00 44.11 C ANISOU 808 CA ILE A 106 5906 4729 6124 39 621 121 C ATOM 809 C ILE A 106 -6.865 28.746 19.468 1.00 45.23 C ANISOU 809 C ILE A 106 5996 4874 6315 43 604 111 C ATOM 810 O ILE A 106 -7.204 29.872 19.075 1.00 46.24 O ANISOU 810 O ILE A 106 6147 4972 6449 45 580 119 O ATOM 811 CB ILE A 106 -7.383 26.838 17.781 1.00 43.65 C ANISOU 811 CB ILE A 106 5874 4655 6057 48 568 117 C ATOM 812 CG1 ILE A 106 -8.411 27.660 16.962 1.00 43.58 C ANISOU 812 CG1 ILE A 106 5906 4604 6048 61 495 121 C ATOM 813 CG2 ILE A 106 -8.055 25.903 18.775 1.00 43.61 C ANISOU 813 CG2 ILE A 106 5804 4671 6097 51 565 100 C ATOM 814 CD1 ILE A 106 -9.225 26.749 15.983 1.00 44.76 C ANISOU 814 CD1 ILE A 106 6100 4728 6180 71 428 111 C ATOM 815 N LEU A 107 -6.880 28.387 20.784 1.00 44.75 N ANISOU 815 N LEU A 107 5877 4844 6282 48 622 95 N ATOM 816 CA LEU A 107 -7.346 29.267 21.859 1.00 44.94 C ANISOU 816 CA LEU A 107 5861 4870 6343 56 618 80 C ATOM 817 C LEU A 107 -6.431 30.463 22.111 1.00 46.26 C ANISOU 817 C LEU A 107 6028 5033 6515 47 633 76 C ATOM 818 O LEU A 107 -6.915 31.587 22.301 1.00 46.79 O ANISOU 818 O LEU A 107 6091 5079 6608 51 616 71 O ATOM 819 CB LEU A 107 -7.557 28.508 23.155 1.00 44.72 C ANISOU 819 CB LEU A 107 5800 4868 6324 67 642 66 C ATOM 820 CG LEU A 107 -8.896 27.876 23.337 1.00 45.39 C ANISOU 820 CG LEU A 107 5863 4942 6442 72 637 62 C ATOM 821 CD1 LEU A 107 -8.919 27.160 24.611 1.00 45.91 C ANISOU 821 CD1 LEU A 107 5918 5024 6503 82 681 54 C ATOM 822 CD2 LEU A 107 -10.014 28.911 23.310 1.00 45.82 C ANISOU 822 CD2 LEU A 107 5892 4969 6549 79 610 51 C ATOM 823 N PHE A 108 -5.114 30.254 22.070 1.00 46.54 N ANISOU 823 N PHE A 108 6063 5081 6537 36 663 74 N ATOM 824 CA PHE A 108 -4.165 31.369 22.192 1.00 46.82 C ANISOU 824 CA PHE A 108 6089 5104 6595 20 680 65 C ATOM 825 C PHE A 108 -4.332 32.315 21.016 1.00 47.31 C ANISOU 825 C PHE A 108 6201 5121 6653 4 682 88 C ATOM 826 O PHE A 108 -4.346 33.515 21.246 1.00 48.17 O ANISOU 826 O PHE A 108 6308 5205 6789 -2 678 83 O ATOM 827 CB PHE A 108 -2.707 30.890 22.356 1.00 46.40 C ANISOU 827 CB PHE A 108 6008 5069 6552 11 711 51 C ATOM 828 CG PHE A 108 -2.477 30.365 23.753 1.00 46.23 C ANISOU 828 CG PHE A 108 5949 5081 6536 34 690 23 C ATOM 829 CD1 PHE A 108 -2.797 31.133 24.857 1.00 46.81 C ANISOU 829 CD1 PHE A 108 6009 5155 6621 45 664 0 C ATOM 830 CD2 PHE A 108 -1.976 29.093 23.959 1.00 46.64 C ANISOU 830 CD2 PHE A 108 5993 5158 6571 50 695 20 C ATOM 831 CE1 PHE A 108 -2.633 30.630 26.138 1.00 47.64 C ANISOU 831 CE1 PHE A 108 6107 5283 6710 74 643 -23 C ATOM 832 CE2 PHE A 108 -1.802 28.594 25.244 1.00 47.26 C ANISOU 832 CE2 PHE A 108 6059 5259 6640 80 669 -1 C ATOM 833 CZ PHE A 108 -2.140 29.360 26.326 1.00 47.10 C ANISOU 833 CZ PHE A 108 6039 5238 6620 92 644 -22 C ATOM 834 N LEU A 109 -4.599 31.794 19.794 1.00 46.94 N ANISOU 834 N LEU A 109 6212 5057 6566 4 683 114 N ATOM 835 CA LEU A 109 -4.827 32.662 18.622 1.00 46.85 C ANISOU 835 CA LEU A 109 6277 4993 6530 -1 679 141 C ATOM 836 C LEU A 109 -6.177 33.386 18.668 1.00 46.72 C ANISOU 836 C LEU A 109 6271 4952 6528 22 612 143 C ATOM 837 O LEU A 109 -6.311 34.481 18.128 1.00 46.48 O ANISOU 837 O LEU A 109 6292 4875 6494 22 602 160 O ATOM 838 CB LEU A 109 -4.648 31.926 17.287 1.00 46.60 C ANISOU 838 CB LEU A 109 6326 4945 6437 -2 696 164 C ATOM 839 CG LEU A 109 -3.325 32.150 16.564 1.00 47.07 C ANISOU 839 CG LEU A 109 6427 4979 6480 -29 782 178 C ATOM 840 CD1 LEU A 109 -3.057 33.655 16.304 1.00 47.06 C ANISOU 840 CD1 LEU A 109 6462 4923 6494 -47 810 194 C ATOM 841 CD2 LEU A 109 -2.200 31.507 17.297 1.00 47.65 C ANISOU 841 CD2 LEU A 109 6416 5092 6596 -43 833 152 C ATOM 842 N THR A 110 -7.166 32.779 19.318 1.00 46.38 N ANISOU 842 N THR A 110 6179 4936 6509 42 571 125 N ATOM 843 CA THR A 110 -8.478 33.392 19.491 1.00 46.18 C ANISOU 843 CA THR A 110 6138 4887 6521 66 513 118 C ATOM 844 C THR A 110 -8.341 34.576 20.454 1.00 46.58 C ANISOU 844 C THR A 110 6153 4931 6613 65 529 102 C ATOM 845 O THR A 110 -8.882 35.634 20.187 1.00 47.48 O ANISOU 845 O THR A 110 6290 5004 6747 79 496 107 O ATOM 846 CB THR A 110 -9.458 32.354 20.061 1.00 46.22 C ANISOU 846 CB THR A 110 6084 4920 6559 80 492 97 C ATOM 847 OG1 THR A 110 -9.501 31.215 19.188 1.00 46.60 O ANISOU 847 OG1 THR A 110 6165 4970 6572 78 475 106 O ATOM 848 CG2 THR A 110 -10.835 32.934 20.313 1.00 45.47 C ANISOU 848 CG2 THR A 110 5950 4799 6528 105 442 80 C ATOM 849 N PHE A 111 -7.590 34.413 21.556 1.00 46.22 N ANISOU 849 N PHE A 111 6062 4922 6578 53 572 81 N ATOM 850 CA PHE A 111 -7.406 35.487 22.530 1.00 45.74 C ANISOU 850 CA PHE A 111 5976 4853 6550 53 581 58 C ATOM 851 C PHE A 111 -6.514 36.590 21.985 1.00 45.39 C ANISOU 851 C PHE A 111 5968 4770 6509 29 598 70 C ATOM 852 O PHE A 111 -6.795 37.750 22.251 1.00 45.65 O ANISOU 852 O PHE A 111 6005 4768 6573 34 585 61 O ATOM 853 CB PHE A 111 -6.951 34.947 23.894 1.00 45.81 C ANISOU 853 CB PHE A 111 5940 4905 6559 56 605 28 C ATOM 854 CG PHE A 111 -8.108 34.280 24.617 1.00 46.40 C ANISOU 854 CG PHE A 111 5988 4997 6643 81 603 17 C ATOM 855 CD1 PHE A 111 -9.216 35.016 25.022 1.00 46.90 C ANISOU 855 CD1 PHE A 111 6036 5037 6748 101 592 2 C ATOM 856 CD2 PHE A 111 -8.113 32.915 24.840 1.00 47.02 C ANISOU 856 CD2 PHE A 111 6058 5108 6698 83 620 20 C ATOM 857 CE1 PHE A 111 -10.305 34.396 25.626 1.00 47.25 C ANISOU 857 CE1 PHE A 111 6047 5088 6816 120 609 -10 C ATOM 858 CE2 PHE A 111 -9.205 32.295 25.450 1.00 47.35 C ANISOU 858 CE2 PHE A 111 6077 5155 6758 100 634 12 C ATOM 859 CZ PHE A 111 -10.287 33.041 25.848 1.00 47.16 C ANISOU 859 CZ PHE A 111 6030 5107 6783 116 634 -4 C ATOM 860 N ILE A 112 -5.527 36.259 21.116 1.00 45.36 N ANISOU 860 N ILE A 112 5996 4761 6479 4 633 90 N ATOM 861 CA ILE A 112 -4.686 37.265 20.443 1.00 45.34 C ANISOU 861 CA ILE A 112 6036 4708 6485 -26 671 106 C ATOM 862 C ILE A 112 -5.608 38.123 19.555 1.00 46.09 C ANISOU 862 C ILE A 112 6207 4744 6563 -8 636 137 C ATOM 863 O ILE A 112 -5.558 39.339 19.654 1.00 46.63 O ANISOU 863 O ILE A 112 6292 4765 6660 -14 638 137 O ATOM 864 CB ILE A 112 -3.501 36.650 19.619 1.00 45.10 C ANISOU 864 CB ILE A 112 6027 4677 6432 -56 735 122 C ATOM 865 CG1 ILE A 112 -2.469 35.952 20.516 1.00 45.46 C ANISOU 865 CG1 ILE A 112 5991 4771 6512 -68 759 86 C ATOM 866 CG2 ILE A 112 -2.793 37.680 18.749 1.00 45.17 C ANISOU 866 CG2 ILE A 112 6095 4618 6448 -88 793 146 C ATOM 867 CD1 ILE A 112 -1.598 34.908 19.768 1.00 45.38 C ANISOU 867 CD1 ILE A 112 5988 4775 6481 -81 812 97 C ATOM 868 N SER A 113 -6.522 37.493 18.793 1.00 45.70 N ANISOU 868 N SER A 113 6199 4692 6472 20 590 157 N ATOM 869 CA SER A 113 -7.477 38.184 17.930 1.00 46.06 C ANISOU 869 CA SER A 113 6320 4680 6500 50 531 182 C ATOM 870 C SER A 113 -8.386 39.169 18.703 1.00 46.79 C ANISOU 870 C SER A 113 6371 4753 6654 76 484 161 C ATOM 871 O SER A 113 -8.632 40.278 18.218 1.00 47.17 O ANISOU 871 O SER A 113 6481 4737 6704 89 461 180 O ATOM 872 CB SER A 113 -8.319 37.173 17.166 1.00 46.73 C ANISOU 872 CB SER A 113 6436 4774 6545 78 471 191 C ATOM 873 OG SER A 113 -7.454 36.351 16.404 1.00 49.57 O ANISOU 873 OG SER A 113 6847 5143 6843 56 520 209 O ATOM 874 N ILE A 114 -8.893 38.765 19.890 1.00 46.10 N ANISOU 874 N ILE A 114 6190 4714 6614 88 476 123 N ATOM 875 CA ILE A 114 -9.706 39.653 20.723 1.00 45.52 C ANISOU 875 CA ILE A 114 6073 4622 6600 113 450 96 C ATOM 876 C ILE A 114 -8.819 40.807 21.244 1.00 46.56 C ANISOU 876 C ILE A 114 6213 4728 6751 89 491 86 C ATOM 877 O ILE A 114 -9.275 41.946 21.325 1.00 47.32 O ANISOU 877 O ILE A 114 6326 4774 6881 107 469 82 O ATOM 878 CB ILE A 114 -10.370 38.861 21.885 1.00 44.86 C ANISOU 878 CB ILE A 114 5901 4592 6553 128 456 58 C ATOM 879 CG1 ILE A 114 -11.223 37.675 21.359 1.00 44.24 C ANISOU 879 CG1 ILE A 114 5805 4532 6473 144 420 63 C ATOM 880 CG2 ILE A 114 -11.161 39.788 22.823 1.00 44.93 C ANISOU 880 CG2 ILE A 114 5867 4579 6624 155 450 25 C ATOM 881 CD1 ILE A 114 -11.712 36.753 22.428 1.00 44.61 C ANISOU 881 CD1 ILE A 114 5776 4624 6551 147 450 34 C ATOM 882 N ASP A 115 -7.543 40.526 21.550 1.00 46.63 N ANISOU 882 N ASP A 115 6208 4764 6746 48 547 79 N ATOM 883 CA ASP A 115 -6.610 41.543 22.011 1.00 47.21 C ANISOU 883 CA ASP A 115 6278 4808 6850 18 581 62 C ATOM 884 C ASP A 115 -6.372 42.592 20.934 1.00 48.22 C ANISOU 884 C ASP A 115 6489 4857 6976 4 594 99 C ATOM 885 O ASP A 115 -6.326 43.785 21.253 1.00 48.72 O ANISOU 885 O ASP A 115 6562 4869 7079 -1 595 87 O ATOM 886 CB ASP A 115 -5.268 40.933 22.454 1.00 47.87 C ANISOU 886 CB ASP A 115 6319 4932 6936 -20 627 42 C ATOM 887 CG ASP A 115 -4.387 41.975 23.116 1.00 51.95 C ANISOU 887 CG ASP A 115 6814 5419 7507 -49 646 7 C ATOM 888 OD1 ASP A 115 -4.835 42.576 24.114 1.00 52.93 O ANISOU 888 OD1 ASP A 115 6916 5540 7656 -30 617 -29 O ATOM 889 OD2 ASP A 115 -3.263 42.227 22.602 1.00 53.27 O ANISOU 889 OD2 ASP A 115 6987 5557 7697 -93 693 14 O ATOM 890 N ARG A 116 -6.195 42.150 19.664 1.00 47.81 N ANISOU 890 N ARG A 116 6508 4786 6870 -3 608 145 N ATOM 891 CA ARG A 116 -5.973 43.048 18.538 1.00 47.40 C ANISOU 891 CA ARG A 116 6564 4651 6795 -13 630 189 C ATOM 892 C ARG A 116 -7.205 43.893 18.293 1.00 48.74 C ANISOU 892 C ARG A 116 6784 4767 6969 37 555 202 C ATOM 893 O ARG A 116 -7.065 45.077 18.009 1.00 49.95 O ANISOU 893 O ARG A 116 6999 4844 7136 31 568 220 O ATOM 894 CB ARG A 116 -5.536 42.318 17.259 1.00 47.24 C ANISOU 894 CB ARG A 116 6629 4621 6701 -25 668 233 C ATOM 895 CG ARG A 116 -4.410 41.280 17.398 1.00 49.21 C ANISOU 895 CG ARG A 116 6822 4926 6949 -64 739 218 C ATOM 896 CD ARG A 116 -3.225 41.700 18.248 1.00 52.00 C ANISOU 896 CD ARG A 116 7093 5285 7379 -113 802 182 C ATOM 897 NE ARG A 116 -2.544 42.896 17.733 1.00 54.44 N ANISOU 897 NE ARG A 116 7460 5507 7717 -152 870 202 N ATOM 898 CZ ARG A 116 -1.607 43.566 18.398 1.00 55.62 C ANISOU 898 CZ ARG A 116 7542 5637 7952 -197 915 167 C ATOM 899 NH1 ARG A 116 -1.221 43.161 19.599 1.00 54.88 N ANISOU 899 NH1 ARG A 116 7331 5607 7913 -202 888 109 N ATOM 900 NH2 ARG A 116 -1.041 44.638 17.862 1.00 55.93 N ANISOU 900 NH2 ARG A 116 7639 5589 8025 -237 985 188 N ATOM 901 N TYR A 117 -8.399 43.331 18.473 1.00 49.16 N ANISOU 901 N TYR A 117 6801 4853 7023 86 478 189 N ATOM 902 CA TYR A 117 -9.647 44.064 18.341 1.00 50.68 C ANISOU 902 CA TYR A 117 7015 4998 7243 141 395 190 C ATOM 903 C TYR A 117 -9.781 45.137 19.439 1.00 51.46 C ANISOU 903 C TYR A 117 7059 5077 7416 145 404 153 C ATOM 904 O TYR A 117 -10.130 46.279 19.124 1.00 52.55 O ANISOU 904 O TYR A 117 7257 5139 7572 168 376 167 O ATOM 905 CB TYR A 117 -10.856 43.104 18.361 1.00 51.34 C ANISOU 905 CB TYR A 117 7044 5124 7338 186 319 171 C ATOM 906 CG TYR A 117 -12.185 43.816 18.453 1.00 53.07 C ANISOU 906 CG TYR A 117 7245 5299 7619 246 234 155 C ATOM 907 CD1 TYR A 117 -12.703 44.499 17.365 1.00 54.60 C ANISOU 907 CD1 TYR A 117 7542 5413 7790 289 157 189 C ATOM 908 CD2 TYR A 117 -12.890 43.864 19.646 1.00 54.54 C ANISOU 908 CD2 TYR A 117 7319 5516 7888 264 234 106 C ATOM 909 CE1 TYR A 117 -13.897 45.201 17.457 1.00 56.17 C ANISOU 909 CE1 TYR A 117 7717 5567 8060 351 71 170 C ATOM 910 CE2 TYR A 117 -14.110 44.519 19.737 1.00 56.00 C ANISOU 910 CE2 TYR A 117 7475 5656 8146 322 165 85 C ATOM 911 CZ TYR A 117 -14.623 45.171 18.630 1.00 57.99 C ANISOU 911 CZ TYR A 117 7815 5832 8387 367 76 115 C ATOM 912 OH TYR A 117 -15.813 45.873 18.715 1.00 61.67 O ANISOU 912 OH TYR A 117 8246 6247 8938 431 -2 91 O ATOM 913 N LEU A 118 -9.556 44.780 20.722 1.00 50.58 N ANISOU 913 N LEU A 118 6848 5028 7341 128 437 105 N ATOM 914 CA LEU A 118 -9.671 45.764 21.802 1.00 49.81 C ANISOU 914 CA LEU A 118 6711 4911 7304 135 445 63 C ATOM 915 C LEU A 118 -8.607 46.871 21.678 1.00 49.64 C ANISOU 915 C LEU A 118 6740 4828 7294 92 489 71 C ATOM 916 O LEU A 118 -8.880 48.022 21.980 1.00 49.50 O ANISOU 916 O LEU A 118 6738 4751 7318 106 477 57 O ATOM 917 CB LEU A 118 -9.629 45.076 23.171 1.00 49.69 C ANISOU 917 CB LEU A 118 6605 4971 7305 131 470 11 C ATOM 918 CG LEU A 118 -10.849 44.199 23.473 1.00 50.75 C ANISOU 918 CG LEU A 118 6683 5147 7453 173 441 -3 C ATOM 919 CD1 LEU A 118 -10.625 43.334 24.696 1.00 50.92 C ANISOU 919 CD1 LEU A 118 6642 5238 7466 163 483 -41 C ATOM 920 CD2 LEU A 118 -12.093 45.036 23.651 1.00 51.11 C ANISOU 920 CD2 LEU A 118 6714 5145 7562 226 401 -21 C ATOM 921 N LEU A 119 -7.411 46.528 21.208 1.00 49.68 N ANISOU 921 N LEU A 119 6767 4839 7270 38 545 91 N ATOM 922 CA LEU A 119 -6.327 47.487 20.996 1.00 50.00 C ANISOU 922 CA LEU A 119 6847 4815 7338 -13 602 98 C ATOM 923 C LEU A 119 -6.642 48.452 19.840 1.00 51.67 C ANISOU 923 C LEU A 119 7178 4924 7529 0 598 154 C ATOM 924 O LEU A 119 -6.181 49.597 19.826 1.00 52.41 O ANISOU 924 O LEU A 119 7310 4940 7662 -27 631 156 O ATOM 925 CB LEU A 119 -5.026 46.740 20.708 1.00 49.06 C ANISOU 925 CB LEU A 119 6709 4727 7205 -70 672 104 C ATOM 926 CG LEU A 119 -3.770 47.578 20.719 1.00 48.48 C ANISOU 926 CG LEU A 119 6635 4595 7189 -134 743 93 C ATOM 927 CD1 LEU A 119 -3.504 48.115 22.085 1.00 47.68 C ANISOU 927 CD1 LEU A 119 6453 4505 7159 -144 721 23 C ATOM 928 CD2 LEU A 119 -2.601 46.768 20.217 1.00 49.54 C ANISOU 928 CD2 LEU A 119 6752 4754 7319 -183 817 104 C ATOM 929 N MET A 120 -7.396 47.985 18.860 1.00 52.16 N ANISOU 929 N MET A 120 7308 4980 7529 41 554 198 N ATOM 930 CA MET A 120 -7.833 48.797 17.744 1.00 53.49 C ANISOU 930 CA MET A 120 7611 5051 7661 71 527 253 C ATOM 931 C MET A 120 -8.789 49.902 18.256 1.00 53.52 C ANISOU 931 C MET A 120 7609 5003 7724 121 461 232 C ATOM 932 O MET A 120 -8.716 51.035 17.801 1.00 54.64 O ANISOU 932 O MET A 120 7845 5047 7871 124 469 261 O ATOM 933 CB MET A 120 -8.525 47.861 16.743 1.00 55.57 C ANISOU 933 CB MET A 120 7935 5334 7846 114 467 288 C ATOM 934 CG MET A 120 -9.265 48.541 15.649 1.00 60.61 C ANISOU 934 CG MET A 120 8714 5878 8436 169 399 338 C ATOM 935 SD MET A 120 -10.237 47.306 14.772 1.00 72.54 S ANISOU 935 SD MET A 120 10258 7429 9876 229 293 351 S ATOM 936 CE MET A 120 -9.036 46.640 13.732 1.00 67.50 C ANISOU 936 CE MET A 120 9731 6784 9130 176 392 399 C ATOM 937 N LYS A 121 -9.644 49.584 19.228 1.00 52.58 N ANISOU 937 N LYS A 121 7382 4944 7652 159 408 180 N ATOM 938 CA LYS A 121 -10.606 50.521 19.797 1.00 51.83 C ANISOU 938 CA LYS A 121 7265 4806 7621 212 354 151 C ATOM 939 C LYS A 121 -10.020 51.358 20.919 1.00 50.98 C ANISOU 939 C LYS A 121 7112 4685 7575 178 405 103 C ATOM 940 O LYS A 121 -10.442 52.488 21.107 1.00 51.31 O ANISOU 940 O LYS A 121 7182 4653 7662 206 383 93 O ATOM 941 CB LYS A 121 -11.812 49.749 20.355 1.00 53.46 C ANISOU 941 CB LYS A 121 7372 5078 7860 266 293 112 C ATOM 942 CG LYS A 121 -12.694 49.140 19.295 1.00 58.30 C ANISOU 942 CG LYS A 121 8023 5685 8442 316 209 145 C ATOM 943 CD LYS A 121 -13.747 48.260 19.918 1.00 64.64 C ANISOU 943 CD LYS A 121 8706 6556 9297 353 169 100 C ATOM 944 CE LYS A 121 -14.801 49.014 20.678 1.00 69.10 C ANISOU 944 CE LYS A 121 9203 7091 9959 408 137 54 C ATOM 945 NZ LYS A 121 -15.599 48.081 21.510 1.00 72.76 N ANISOU 945 NZ LYS A 121 9539 7627 10480 423 145 5 N ATOM 946 N PHE A 122 -9.152 50.767 21.738 1.00 50.06 N ANISOU 946 N PHE A 122 6920 4638 7462 126 460 66 N ATOM 947 CA PHE A 122 -8.569 51.387 22.923 1.00 49.51 C ANISOU 947 CA PHE A 122 6800 4566 7445 96 493 7 C ATOM 948 C PHE A 122 -7.056 51.135 22.886 1.00 50.25 C ANISOU 948 C PHE A 122 6883 4674 7535 18 559 5 C ATOM 949 O PHE A 122 -6.547 50.200 23.532 1.00 50.75 O ANISOU 949 O PHE A 122 6875 4820 7589 -3 572 -27 O ATOM 950 CB PHE A 122 -9.163 50.775 24.208 1.00 48.75 C ANISOU 950 CB PHE A 122 6610 4550 7363 128 476 -54 C ATOM 951 CG PHE A 122 -10.669 50.622 24.197 1.00 49.05 C ANISOU 951 CG PHE A 122 6627 4592 7416 202 425 -56 C ATOM 952 CD1 PHE A 122 -11.493 51.728 24.263 1.00 49.47 C ANISOU 952 CD1 PHE A 122 6702 4572 7522 250 393 -67 C ATOM 953 CD2 PHE A 122 -11.259 49.374 24.063 1.00 49.51 C ANISOU 953 CD2 PHE A 122 6641 4722 7450 222 409 -47 C ATOM 954 CE1 PHE A 122 -12.868 51.587 24.201 1.00 49.69 C ANISOU 954 CE1 PHE A 122 6696 4599 7585 319 344 -73 C ATOM 955 CE2 PHE A 122 -12.634 49.237 24.040 1.00 49.62 C ANISOU 955 CE2 PHE A 122 6619 4733 7501 285 363 -55 C ATOM 956 CZ PHE A 122 -13.426 50.343 24.106 1.00 49.36 C ANISOU 956 CZ PHE A 122 6597 4628 7528 334 330 -70 C ATOM 957 N PRO A 123 -6.319 51.972 22.124 1.00 49.11 N ANISOU 957 N PRO A 123 6811 4442 7406 -26 604 39 N ATOM 958 CA PRO A 123 -4.870 51.745 21.987 1.00 48.57 C ANISOU 958 CA PRO A 123 6721 4376 7356 -104 678 36 C ATOM 959 C PRO A 123 -4.062 51.835 23.291 1.00 48.63 C ANISOU 959 C PRO A 123 6632 4417 7430 -141 682 -45 C ATOM 960 O PRO A 123 -2.986 51.235 23.421 1.00 48.36 O ANISOU 960 O PRO A 123 6540 4419 7414 -190 718 -65 O ATOM 961 CB PRO A 123 -4.438 52.815 20.962 1.00 48.88 C ANISOU 961 CB PRO A 123 6868 4295 7411 -139 735 88 C ATOM 962 CG PRO A 123 -5.697 53.243 20.270 1.00 49.15 C ANISOU 962 CG PRO A 123 7000 4278 7397 -68 677 137 C ATOM 963 CD PRO A 123 -6.786 53.092 21.283 1.00 47.77 C ANISOU 963 CD PRO A 123 6751 4162 7239 -4 594 86 C ATOM 964 N PHE A 124 -4.583 52.586 24.263 1.00 48.72 N ANISOU 964 N PHE A 124 6626 4409 7475 -111 638 -96 N ATOM 965 CA PHE A 124 -3.877 52.844 25.517 1.00 48.56 C ANISOU 965 CA PHE A 124 6538 4404 7510 -138 626 -179 C ATOM 966 C PHE A 124 -4.059 51.737 26.569 1.00 47.69 C ANISOU 966 C PHE A 124 6359 4402 7357 -105 587 -225 C ATOM 967 O PHE A 124 -3.437 51.822 27.631 1.00 47.81 O ANISOU 967 O PHE A 124 6330 4434 7402 -120 564 -295 O ATOM 968 CB PHE A 124 -4.232 54.254 26.067 1.00 48.50 C ANISOU 968 CB PHE A 124 6561 4310 7556 -125 605 -217 C ATOM 969 CG PHE A 124 -3.640 55.364 25.208 1.00 48.61 C ANISOU 969 CG PHE A 124 6636 4206 7627 -179 656 -184 C ATOM 970 CD1 PHE A 124 -4.267 55.776 24.037 1.00 48.54 C ANISOU 970 CD1 PHE A 124 6724 4130 7588 -156 674 -105 C ATOM 971 CD2 PHE A 124 -2.399 55.910 25.507 1.00 49.22 C ANISOU 971 CD2 PHE A 124 6676 4234 7791 -253 689 -230 C ATOM 972 CE1 PHE A 124 -3.680 56.740 23.210 1.00 48.65 C ANISOU 972 CE1 PHE A 124 6812 4027 7644 -206 736 -66 C ATOM 973 CE2 PHE A 124 -1.831 56.890 24.682 1.00 49.02 C ANISOU 973 CE2 PHE A 124 6708 4091 7826 -310 755 -196 C ATOM 974 CZ PHE A 124 -2.477 57.301 23.548 1.00 48.04 C ANISOU 974 CZ PHE A 124 6695 3899 7658 -286 785 -110 C ATOM 975 N ARG A 125 -4.847 50.667 26.248 1.00 46.17 N ANISOU 975 N ARG A 125 6166 4279 7098 -63 578 -186 N ATOM 976 CA ARG A 125 -5.058 49.498 27.099 1.00 44.67 C ANISOU 976 CA ARG A 125 5926 4185 6861 -34 556 -215 C ATOM 977 C ARG A 125 -5.579 49.831 28.502 1.00 45.62 C ANISOU 977 C ARG A 125 6035 4316 6980 7 526 -282 C ATOM 978 O ARG A 125 -5.076 49.284 29.488 1.00 47.08 O ANISOU 978 O ARG A 125 6191 4552 7144 7 509 -331 O ATOM 979 CB ARG A 125 -3.789 48.630 27.175 1.00 42.70 C ANISOU 979 CB ARG A 125 5628 3985 6612 -79 570 -228 C ATOM 980 CG ARG A 125 -3.271 48.104 25.845 1.00 40.82 C ANISOU 980 CG ARG A 125 5400 3745 6365 -115 616 -165 C ATOM 981 CD ARG A 125 -2.157 47.115 26.136 1.00 42.54 C ANISOU 981 CD ARG A 125 5555 4021 6589 -144 624 -190 C ATOM 982 NE ARG A 125 -1.750 46.367 24.950 1.00 43.73 N ANISOU 982 NE ARG A 125 5714 4182 6718 -168 675 -134 N ATOM 983 CZ ARG A 125 -2.295 45.223 24.563 1.00 44.60 C ANISOU 983 CZ ARG A 125 5835 4352 6761 -138 672 -98 C ATOM 984 NH1 ARG A 125 -1.888 44.634 23.451 1.00 43.83 N ANISOU 984 NH1 ARG A 125 5759 4254 6642 -160 721 -51 N ATOM 985 NH2 ARG A 125 -3.254 44.656 25.288 1.00 44.44 N ANISOU 985 NH2 ARG A 125 5807 4385 6695 -87 627 -111 N ATOM 986 N GLU A 126 -6.597 50.675 28.594 1.00 44.84 N ANISOU 986 N GLU A 126 5969 4170 6900 47 518 -285 N ATOM 987 CA GLU A 126 -7.129 51.040 29.893 1.00 46.40 C ANISOU 987 CA GLU A 126 6166 4368 7094 88 504 -350 C ATOM 988 C GLU A 126 -7.970 49.966 30.525 1.00 48.11 C ANISOU 988 C GLU A 126 6362 4659 7257 136 514 -357 C ATOM 989 O GLU A 126 -8.067 49.926 31.754 1.00 49.68 O ANISOU 989 O GLU A 126 6570 4878 7430 161 516 -414 O ATOM 990 CB GLU A 126 -7.919 52.345 29.826 1.00 49.00 C ANISOU 990 CB GLU A 126 6532 4614 7472 119 500 -358 C ATOM 991 CG GLU A 126 -7.058 53.530 29.436 1.00 53.87 C ANISOU 991 CG GLU A 126 7178 5142 8146 69 498 -364 C ATOM 992 CD GLU A 126 -7.305 53.939 28.005 1.00 60.06 C ANISOU 992 CD GLU A 126 8004 5866 8950 61 508 -287 C ATOM 993 OE1 GLU A 126 -7.308 55.158 27.754 1.00 59.15 O ANISOU 993 OE1 GLU A 126 7935 5657 8885 55 508 -287 O ATOM 994 OE2 GLU A 126 -7.542 53.058 27.145 1.00 64.66 O ANISOU 994 OE2 GLU A 126 8584 6490 9494 66 513 -228 O ATOM 995 N HIS A 127 -8.618 49.121 29.715 1.00 47.36 N ANISOU 995 N HIS A 127 6250 4599 7146 150 524 -301 N ATOM 996 CA HIS A 127 -9.507 48.094 30.226 1.00 47.22 C ANISOU 996 CA HIS A 127 6206 4641 7094 190 544 -304 C ATOM 997 C HIS A 127 -8.768 46.962 30.936 1.00 48.11 C ANISOU 997 C HIS A 127 6310 4825 7145 175 552 -320 C ATOM 998 O HIS A 127 -7.660 46.589 30.525 1.00 48.56 O ANISOU 998 O HIS A 127 6359 4901 7190 133 538 -306 O ATOM 999 CB HIS A 127 -10.344 47.542 29.073 1.00 47.61 C ANISOU 999 CB HIS A 127 6236 4698 7156 205 538 -245 C ATOM 1000 CG HIS A 127 -11.252 48.564 28.470 1.00 49.77 C ANISOU 1000 CG HIS A 127 6522 4900 7488 237 516 -232 C ATOM 1001 ND1 HIS A 127 -12.555 48.719 28.906 1.00 51.49 N ANISOU 1001 ND1 HIS A 127 6710 5104 7749 293 524 -257 N ATOM 1002 CD2 HIS A 127 -11.002 49.485 27.518 1.00 50.97 C ANISOU 1002 CD2 HIS A 127 6717 4985 7665 225 487 -199 C ATOM 1003 CE1 HIS A 127 -13.057 49.707 28.195 1.00 51.69 C ANISOU 1003 CE1 HIS A 127 6755 5058 7827 317 488 -240 C ATOM 1004 NE2 HIS A 127 -12.159 50.204 27.352 1.00 51.96 N ANISOU 1004 NE2 HIS A 127 6842 5055 7844 278 464 -203 N ATOM 1005 N ILE A 128 -9.393 46.390 31.987 1.00 47.77 N ANISOU 1005 N ILE A 128 6270 4816 7064 213 582 -350 N ATOM 1006 CA ILE A 128 -8.871 45.237 32.727 1.00 47.86 C ANISOU 1006 CA ILE A 128 6291 4890 7006 213 591 -361 C ATOM 1007 C ILE A 128 -8.604 44.065 31.755 1.00 47.92 C ANISOU 1007 C ILE A 128 6264 4943 7001 187 588 -304 C ATOM 1008 O ILE A 128 -7.532 43.463 31.831 1.00 48.41 O ANISOU 1008 O ILE A 128 6326 5038 7032 163 568 -305 O ATOM 1009 CB ILE A 128 -9.820 44.813 33.891 1.00 48.12 C ANISOU 1009 CB ILE A 128 6349 4937 6998 262 645 -390 C ATOM 1010 CG1 ILE A 128 -10.006 45.964 34.905 1.00 48.84 C ANISOU 1010 CG1 ILE A 128 6488 4979 7089 290 652 -454 C ATOM 1011 CG2 ILE A 128 -9.335 43.538 34.574 1.00 47.93 C ANISOU 1011 CG2 ILE A 128 6350 4969 6892 266 657 -390 C ATOM 1012 CD1 ILE A 128 -11.235 45.855 35.743 1.00 50.07 C ANISOU 1012 CD1 ILE A 128 6665 5128 7233 339 728 -476 C ATOM 1013 N LEU A 129 -9.528 43.810 30.785 1.00 46.91 N ANISOU 1013 N LEU A 129 6107 4810 6905 194 600 -259 N ATOM 1014 CA LEU A 129 -9.381 42.766 29.759 1.00 46.39 C ANISOU 1014 CA LEU A 129 6020 4779 6828 172 594 -207 C ATOM 1015 C LEU A 129 -8.070 42.924 28.940 1.00 46.56 C ANISOU 1015 C LEU A 129 6049 4795 6848 126 569 -187 C ATOM 1016 O LEU A 129 -7.596 41.951 28.359 1.00 47.15 O ANISOU 1016 O LEU A 129 6114 4906 6897 106 572 -157 O ATOM 1017 CB LEU A 129 -10.567 42.813 28.757 1.00 46.31 C ANISOU 1017 CB LEU A 129 5987 4744 6863 190 586 -173 C ATOM 1018 CG LEU A 129 -11.958 42.260 29.132 1.00 46.64 C ANISOU 1018 CG LEU A 129 5991 4794 6934 227 616 -181 C ATOM 1019 CD1 LEU A 129 -12.838 42.152 27.905 1.00 45.82 C ANISOU 1019 CD1 LEU A 129 5859 4669 6881 238 577 -148 C ATOM 1020 CD2 LEU A 129 -11.871 40.914 29.695 1.00 47.70 C ANISOU 1020 CD2 LEU A 129 6118 4983 7023 223 654 -180 C ATOM 1021 N GLN A 130 -7.513 44.158 28.858 1.00 46.26 N ANISOU 1021 N GLN A 130 6027 4704 6844 106 554 -203 N ATOM 1022 CA GLN A 130 -6.295 44.513 28.089 1.00 45.22 C ANISOU 1022 CA GLN A 130 5899 4549 6733 56 550 -188 C ATOM 1023 C GLN A 130 -5.017 44.509 28.906 1.00 44.56 C ANISOU 1023 C GLN A 130 5797 4480 6655 31 538 -237 C ATOM 1024 O GLN A 130 -3.979 44.816 28.353 1.00 44.11 O ANISOU 1024 O GLN A 130 5727 4398 6635 -14 543 -233 O ATOM 1025 CB GLN A 130 -6.451 45.896 27.439 1.00 45.26 C ANISOU 1025 CB GLN A 130 5935 4473 6786 46 547 -176 C ATOM 1026 CG GLN A 130 -7.668 46.043 26.535 1.00 45.58 C ANISOU 1026 CG GLN A 130 6001 4487 6830 78 538 -131 C ATOM 1027 CD GLN A 130 -7.698 47.435 25.959 1.00 47.72 C ANISOU 1027 CD GLN A 130 6319 4670 7143 72 531 -118 C ATOM 1028 OE1 GLN A 130 -8.229 48.362 26.563 1.00 47.68 O ANISOU 1028 OE1 GLN A 130 6319 4625 7172 98 519 -150 O ATOM 1029 NE2 GLN A 130 -7.090 47.632 24.790 1.00 48.73 N ANISOU 1029 NE2 GLN A 130 6489 4759 7266 37 546 -70 N ATOM 1030 N LYS A 131 -5.082 44.188 30.211 1.00 44.68 N ANISOU 1030 N LYS A 131 5814 4527 6635 61 520 -285 N ATOM 1031 CA LYS A 131 -3.908 44.159 31.072 1.00 45.38 C ANISOU 1031 CA LYS A 131 5892 4626 6725 49 483 -340 C ATOM 1032 C LYS A 131 -3.109 42.865 30.939 1.00 47.10 C ANISOU 1032 C LYS A 131 6079 4898 6917 40 476 -327 C ATOM 1033 O LYS A 131 -3.688 41.798 30.708 1.00 47.13 O ANISOU 1033 O LYS A 131 6088 4945 6873 60 500 -288 O ATOM 1034 CB LYS A 131 -4.298 44.390 32.531 1.00 46.13 C ANISOU 1034 CB LYS A 131 6028 4723 6778 93 461 -398 C ATOM 1035 CG LYS A 131 -5.047 45.679 32.773 1.00 49.04 C ANISOU 1035 CG LYS A 131 6425 5033 7175 107 470 -420 C ATOM 1036 CD LYS A 131 -4.296 46.950 32.341 1.00 52.35 C ANISOU 1036 CD LYS A 131 6830 5385 7674 62 448 -441 C ATOM 1037 CE LYS A 131 -5.117 48.170 32.709 1.00 56.68 C ANISOU 1037 CE LYS A 131 7417 5874 8245 87 454 -468 C ATOM 1038 NZ LYS A 131 -4.524 49.451 32.220 1.00 59.26 N ANISOU 1038 NZ LYS A 131 7740 6123 8654 42 443 -481 N ATOM 1039 N LYS A 132 -1.767 42.968 31.088 1.00 48.22 N ANISOU 1039 N LYS A 132 6184 5033 7103 10 442 -365 N ATOM 1040 CA LYS A 132 -0.826 41.848 31.005 1.00 49.09 C ANISOU 1040 CA LYS A 132 6255 5188 7210 4 427 -364 C ATOM 1041 C LYS A 132 -1.177 40.783 32.030 1.00 49.83 C ANISOU 1041 C LYS A 132 6386 5333 7214 59 399 -375 C ATOM 1042 O LYS A 132 -1.212 39.609 31.680 1.00 50.84 O ANISOU 1042 O LYS A 132 6507 5502 7308 69 419 -338 O ATOM 1043 CB LYS A 132 0.608 42.327 31.241 1.00 51.33 C ANISOU 1043 CB LYS A 132 6482 5444 7577 -30 381 -423 C ATOM 1044 CG LYS A 132 1.634 41.212 31.076 1.00 56.62 C ANISOU 1044 CG LYS A 132 7097 6152 8265 -34 365 -426 C ATOM 1045 CD LYS A 132 2.465 41.015 32.326 1.00 62.34 C ANISOU 1045 CD LYS A 132 7807 6887 8993 -3 266 -503 C ATOM 1046 CE LYS A 132 3.667 41.907 32.371 1.00 67.15 C ANISOU 1046 CE LYS A 132 8340 7445 9729 -47 224 -569 C ATOM 1047 NZ LYS A 132 4.499 41.619 33.568 1.00 70.77 N ANISOU 1047 NZ LYS A 132 8782 7913 10193 -9 104 -650 N ATOM 1048 N GLU A 133 -1.496 41.193 33.275 1.00 49.26 N ANISOU 1048 N GLU A 133 6365 5252 7099 97 362 -424 N ATOM 1049 CA GLU A 133 -1.865 40.313 34.386 1.00 49.00 C ANISOU 1049 CA GLU A 133 6396 5253 6968 154 346 -436 C ATOM 1050 C GLU A 133 -3.152 39.525 34.091 1.00 48.14 C ANISOU 1050 C GLU A 133 6314 5170 6807 173 423 -375 C ATOM 1051 O GLU A 133 -3.275 38.367 34.487 1.00 48.29 O ANISOU 1051 O GLU A 133 6365 5223 6761 202 431 -359 O ATOM 1052 CB GLU A 133 -1.981 41.108 35.707 1.00 52.12 C ANISOU 1052 CB GLU A 133 6861 5620 7324 189 302 -503 C ATOM 1053 CG GLU A 133 -0.863 42.123 35.943 1.00 60.44 C ANISOU 1053 CG GLU A 133 7881 6633 8451 164 223 -572 C ATOM 1054 CD GLU A 133 -1.109 43.523 35.390 1.00 72.24 C ANISOU 1054 CD GLU A 133 9349 8072 10027 123 249 -578 C ATOM 1055 OE1 GLU A 133 -0.246 44.027 34.635 1.00 74.90 O ANISOU 1055 OE1 GLU A 133 9613 8381 10463 68 239 -584 O ATOM 1056 OE2 GLU A 133 -2.165 44.119 35.715 1.00 76.25 O ANISOU 1056 OE2 GLU A 133 9910 8557 10503 146 287 -579 O ATOM 1057 N PHE A 134 -4.091 40.138 33.371 1.00 47.24 N ANISOU 1057 N PHE A 134 6186 5034 6730 157 473 -345 N ATOM 1058 CA PHE A 134 -5.323 39.463 32.989 1.00 46.81 C ANISOU 1058 CA PHE A 134 6136 4995 6653 171 536 -295 C ATOM 1059 C PHE A 134 -5.016 38.412 31.908 1.00 47.27 C ANISOU 1059 C PHE A 134 6155 5085 6720 146 546 -245 C ATOM 1060 O PHE A 134 -5.629 37.348 31.916 1.00 47.71 O ANISOU 1060 O PHE A 134 6220 5167 6740 163 579 -216 O ATOM 1061 CB PHE A 134 -6.342 40.487 32.475 1.00 46.33 C ANISOU 1061 CB PHE A 134 6064 4895 6643 166 565 -285 C ATOM 1062 CG PHE A 134 -7.735 39.928 32.358 1.00 46.67 C ANISOU 1062 CG PHE A 134 6105 4945 6681 189 620 -255 C ATOM 1063 CD1 PHE A 134 -8.580 39.891 33.460 1.00 47.58 C ANISOU 1063 CD1 PHE A 134 6258 5055 6765 228 665 -281 C ATOM 1064 CD2 PHE A 134 -8.203 39.432 31.151 1.00 46.98 C ANISOU 1064 CD2 PHE A 134 6106 4993 6752 172 631 -206 C ATOM 1065 CE1 PHE A 134 -9.858 39.361 33.357 1.00 47.97 C ANISOU 1065 CE1 PHE A 134 6288 5105 6832 244 726 -259 C ATOM 1066 CE2 PHE A 134 -9.478 38.887 31.056 1.00 47.59 C ANISOU 1066 CE2 PHE A 134 6166 5072 6844 191 672 -188 C ATOM 1067 CZ PHE A 134 -10.289 38.839 32.160 1.00 47.69 C ANISOU 1067 CZ PHE A 134 6199 5078 6843 224 723 -215 C ATOM 1068 N ALA A 135 -4.065 38.705 30.970 1.00 47.24 N ANISOU 1068 N ALA A 135 6110 5072 6767 106 526 -236 N ATOM 1069 CA ALA A 135 -3.641 37.782 29.905 1.00 46.82 C ANISOU 1069 CA ALA A 135 6027 5041 6719 84 541 -194 C ATOM 1070 C ALA A 135 -2.964 36.578 30.504 1.00 47.47 C ANISOU 1070 C ALA A 135 6112 5165 6761 104 522 -205 C ATOM 1071 O ALA A 135 -3.131 35.483 29.977 1.00 47.97 O ANISOU 1071 O ALA A 135 6172 5254 6802 105 545 -168 O ATOM 1072 CB ALA A 135 -2.706 38.467 28.937 1.00 46.50 C ANISOU 1072 CB ALA A 135 5954 4972 6743 38 542 -190 C ATOM 1073 N ILE A 136 -2.210 36.755 31.611 1.00 47.42 N ANISOU 1073 N ILE A 136 6117 5159 6743 124 471 -256 N ATOM 1074 CA ILE A 136 -1.589 35.636 32.318 1.00 47.93 C ANISOU 1074 CA ILE A 136 6197 5253 6759 156 436 -269 C ATOM 1075 C ILE A 136 -2.670 34.740 32.926 1.00 48.09 C ANISOU 1075 C ILE A 136 6284 5292 6698 195 474 -243 C ATOM 1076 O ILE A 136 -2.560 33.512 32.860 1.00 48.90 O ANISOU 1076 O ILE A 136 6396 5419 6765 209 483 -217 O ATOM 1077 CB ILE A 136 -0.570 36.123 33.367 1.00 48.78 C ANISOU 1077 CB ILE A 136 6310 5349 6873 176 352 -338 C ATOM 1078 CG1 ILE A 136 0.618 36.821 32.686 1.00 49.67 C ANISOU 1078 CG1 ILE A 136 6337 5440 7094 129 325 -366 C ATOM 1079 CG2 ILE A 136 -0.077 34.959 34.230 1.00 49.50 C ANISOU 1079 CG2 ILE A 136 6443 5466 6899 226 303 -350 C ATOM 1080 CD1 ILE A 136 1.407 37.701 33.621 1.00 50.86 C ANISOU 1080 CD1 ILE A 136 6484 5563 7280 137 240 -443 C ATOM 1081 N LEU A 137 -3.736 35.346 33.469 1.00 47.61 N ANISOU 1081 N LEU A 137 6264 5212 6613 210 507 -249 N ATOM 1082 CA LEU A 137 -4.870 34.623 34.026 1.00 47.75 C ANISOU 1082 CA LEU A 137 6336 5235 6572 239 568 -227 C ATOM 1083 C LEU A 137 -5.592 33.845 32.920 1.00 48.78 C ANISOU 1083 C LEU A 137 6424 5378 6732 215 620 -173 C ATOM 1084 O LEU A 137 -5.877 32.671 33.092 1.00 49.36 O ANISOU 1084 O LEU A 137 6522 5465 6766 228 651 -148 O ATOM 1085 CB LEU A 137 -5.823 35.605 34.716 1.00 47.69 C ANISOU 1085 CB LEU A 137 6364 5198 6559 255 602 -251 C ATOM 1086 CG LEU A 137 -7.105 35.010 35.246 1.00 49.02 C ANISOU 1086 CG LEU A 137 6576 5360 6691 279 689 -232 C ATOM 1087 CD1 LEU A 137 -6.816 34.013 36.357 1.00 49.83 C ANISOU 1087 CD1 LEU A 137 6771 5471 6693 319 697 -235 C ATOM 1088 CD2 LEU A 137 -8.063 36.087 35.699 1.00 48.88 C ANISOU 1088 CD2 LEU A 137 6571 5308 6694 291 733 -258 C ATOM 1089 N ILE A 138 -5.856 34.481 31.773 1.00 49.24 N ANISOU 1089 N ILE A 138 6428 5425 6857 181 623 -156 N ATOM 1090 CA ILE A 138 -6.490 33.836 30.612 1.00 49.79 C ANISOU 1090 CA ILE A 138 6465 5500 6954 160 651 -112 C ATOM 1091 C ILE A 138 -5.626 32.684 30.070 1.00 51.00 C ANISOU 1091 C ILE A 138 6609 5680 7090 151 638 -90 C ATOM 1092 O ILE A 138 -6.181 31.656 29.677 1.00 52.44 O ANISOU 1092 O ILE A 138 6791 5871 7263 150 666 -62 O ATOM 1093 CB ILE A 138 -6.810 34.888 29.516 1.00 49.78 C ANISOU 1093 CB ILE A 138 6430 5472 7013 135 640 -101 C ATOM 1094 CG1 ILE A 138 -7.935 35.844 29.976 1.00 50.15 C ANISOU 1094 CG1 ILE A 138 6480 5488 7087 152 658 -119 C ATOM 1095 CG2 ILE A 138 -7.112 34.256 28.157 1.00 49.70 C ANISOU 1095 CG2 ILE A 138 6401 5465 7020 115 643 -60 C ATOM 1096 CD1 ILE A 138 -9.227 35.189 30.220 1.00 51.14 C ANISOU 1096 CD1 ILE A 138 6598 5612 7221 169 705 -109 C ATOM 1097 N SER A 139 -4.278 32.823 30.078 1.00 49.99 N ANISOU 1097 N SER A 139 6468 5560 6966 144 598 -109 N ATOM 1098 CA SER A 139 -3.376 31.768 29.624 1.00 49.29 C ANISOU 1098 CA SER A 139 6364 5493 6871 141 589 -97 C ATOM 1099 C SER A 139 -3.479 30.561 30.546 1.00 49.16 C ANISOU 1099 C SER A 139 6392 5493 6793 179 592 -93 C ATOM 1100 O SER A 139 -3.590 29.432 30.073 1.00 48.89 O ANISOU 1100 O SER A 139 6359 5469 6745 178 614 -65 O ATOM 1101 CB SER A 139 -1.945 32.282 29.559 1.00 50.13 C ANISOU 1101 CB SER A 139 6433 5597 7019 128 548 -129 C ATOM 1102 OG SER A 139 -1.867 33.337 28.613 1.00 52.51 O ANISOU 1102 OG SER A 139 6704 5872 7375 89 564 -123 O ATOM 1103 N LEU A 140 -3.517 30.801 31.860 1.00 49.14 N ANISOU 1103 N LEU A 140 6439 5486 6747 213 574 -122 N ATOM 1104 CA LEU A 140 -3.682 29.729 32.833 1.00 49.83 C ANISOU 1104 CA LEU A 140 6596 5578 6761 254 584 -115 C ATOM 1105 C LEU A 140 -5.077 29.072 32.641 1.00 49.44 C ANISOU 1105 C LEU A 140 6563 5520 6703 246 666 -77 C ATOM 1106 O LEU A 140 -5.163 27.844 32.652 1.00 50.18 O ANISOU 1106 O LEU A 140 6683 5617 6768 256 690 -51 O ATOM 1107 CB LEU A 140 -3.508 30.281 34.260 1.00 51.06 C ANISOU 1107 CB LEU A 140 6822 5719 6858 295 550 -156 C ATOM 1108 CG LEU A 140 -3.881 29.317 35.404 1.00 53.46 C ANISOU 1108 CG LEU A 140 7234 6014 7064 344 578 -144 C ATOM 1109 CD1 LEU A 140 -3.009 28.035 35.368 1.00 54.00 C ANISOU 1109 CD1 LEU A 140 7319 6094 7105 369 538 -129 C ATOM 1110 CD2 LEU A 140 -3.859 30.027 36.778 1.00 53.78 C ANISOU 1110 CD2 LEU A 140 7366 6033 7034 386 551 -187 C ATOM 1111 N ALA A 141 -6.138 29.877 32.387 1.00 47.90 N ANISOU 1111 N ALA A 141 6343 5309 6547 226 705 -76 N ATOM 1112 CA ALA A 141 -7.474 29.377 32.081 1.00 47.50 C ANISOU 1112 CA ALA A 141 6280 5245 6522 214 774 -50 C ATOM 1113 C ALA A 141 -7.478 28.480 30.823 1.00 47.96 C ANISOU 1113 C ALA A 141 6295 5313 6614 186 770 -19 C ATOM 1114 O ALA A 141 -8.060 27.394 30.857 1.00 48.42 O ANISOU 1114 O ALA A 141 6366 5364 6667 186 813 1 O ATOM 1115 CB ALA A 141 -8.440 30.531 31.906 1.00 47.31 C ANISOU 1115 CB ALA A 141 6220 5200 6555 203 793 -64 C ATOM 1116 N VAL A 142 -6.807 28.909 29.729 1.00 47.68 N ANISOU 1116 N VAL A 142 6219 5288 6610 164 724 -17 N ATOM 1117 CA VAL A 142 -6.657 28.110 28.505 1.00 47.57 C ANISOU 1117 CA VAL A 142 6181 5280 6612 142 717 8 C ATOM 1118 C VAL A 142 -6.023 26.722 28.819 1.00 47.26 C ANISOU 1118 C VAL A 142 6172 5254 6530 159 724 19 C ATOM 1119 O VAL A 142 -6.565 25.692 28.408 1.00 48.02 O ANISOU 1119 O VAL A 142 6271 5343 6630 151 749 39 O ATOM 1120 CB VAL A 142 -5.849 28.872 27.416 1.00 48.01 C ANISOU 1120 CB VAL A 142 6210 5337 6693 120 682 7 C ATOM 1121 CG1 VAL A 142 -5.440 27.948 26.270 1.00 48.04 C ANISOU 1121 CG1 VAL A 142 6212 5347 6695 105 683 28 C ATOM 1122 CG2 VAL A 142 -6.638 30.057 26.881 1.00 48.32 C ANISOU 1122 CG2 VAL A 142 6233 5353 6772 106 675 7 C ATOM 1123 N TRP A 143 -4.912 26.695 29.570 1.00 45.94 N ANISOU 1123 N TRP A 143 6027 5100 6329 185 694 2 N ATOM 1124 CA TRP A 143 -4.277 25.431 29.929 1.00 45.77 C ANISOU 1124 CA TRP A 143 6039 5084 6268 211 689 11 C ATOM 1125 C TRP A 143 -5.192 24.523 30.772 1.00 46.02 C ANISOU 1125 C TRP A 143 6132 5097 6258 229 740 30 C ATOM 1126 O TRP A 143 -5.242 23.329 30.533 1.00 45.41 O ANISOU 1126 O TRP A 143 6071 5012 6169 232 761 51 O ATOM 1127 CB TRP A 143 -2.933 25.671 30.624 1.00 45.24 C ANISOU 1127 CB TRP A 143 5978 5027 6182 243 628 -19 C ATOM 1128 CG TRP A 143 -1.848 26.083 29.679 1.00 44.97 C ANISOU 1128 CG TRP A 143 5877 5004 6205 221 597 -34 C ATOM 1129 CD1 TRP A 143 -1.314 27.325 29.533 1.00 45.62 C ANISOU 1129 CD1 TRP A 143 5917 5085 6331 203 570 -62 C ATOM 1130 CD2 TRP A 143 -1.144 25.234 28.764 1.00 44.99 C ANISOU 1130 CD2 TRP A 143 5851 5013 6230 215 602 -24 C ATOM 1131 NE1 TRP A 143 -0.323 27.307 28.584 1.00 45.77 N ANISOU 1131 NE1 TRP A 143 5880 5107 6403 182 568 -68 N ATOM 1132 CE2 TRP A 143 -0.187 26.032 28.104 1.00 45.34 C ANISOU 1132 CE2 TRP A 143 5834 5059 6334 192 588 -46 C ATOM 1133 CE3 TRP A 143 -1.194 23.860 28.472 1.00 45.38 C ANISOU 1133 CE3 TRP A 143 5923 5061 6258 228 622 0 C ATOM 1134 CZ2 TRP A 143 0.691 25.513 27.152 1.00 45.33 C ANISOU 1134 CZ2 TRP A 143 5793 5058 6370 182 604 -45 C ATOM 1135 CZ3 TRP A 143 -0.343 23.358 27.501 1.00 45.61 C ANISOU 1135 CZ3 TRP A 143 5915 5094 6321 221 628 -1 C ATOM 1136 CH2 TRP A 143 0.589 24.183 26.861 1.00 45.31 C ANISOU 1136 CH2 TRP A 143 5816 5058 6340 199 623 -24 C ATOM 1137 N VAL A 144 -5.922 25.093 31.741 1.00 46.76 N ANISOU 1137 N VAL A 144 6261 5175 6329 241 771 20 N ATOM 1138 CA VAL A 144 -6.849 24.334 32.584 1.00 47.56 C ANISOU 1138 CA VAL A 144 6426 5250 6396 255 845 38 C ATOM 1139 C VAL A 144 -8.056 23.789 31.754 1.00 48.12 C ANISOU 1139 C VAL A 144 6447 5302 6534 214 905 59 C ATOM 1140 O VAL A 144 -8.368 22.612 31.819 1.00 48.31 O ANISOU 1140 O VAL A 144 6500 5307 6550 212 949 81 O ATOM 1141 CB VAL A 144 -7.320 25.165 33.815 1.00 48.00 C ANISOU 1141 CB VAL A 144 6538 5289 6412 278 878 18 C ATOM 1142 CG1 VAL A 144 -8.449 24.443 34.555 1.00 48.50 C ANISOU 1142 CG1 VAL A 144 6660 5312 6454 282 986 39 C ATOM 1143 CG2 VAL A 144 -6.159 25.455 34.762 1.00 48.06 C ANISOU 1143 CG2 VAL A 144 6614 5304 6342 326 808 -6 C ATOM 1144 N LEU A 145 -8.699 24.642 30.951 1.00 48.11 N ANISOU 1144 N LEU A 145 6374 5303 6603 184 897 48 N ATOM 1145 CA LEU A 145 -9.812 24.260 30.099 1.00 48.38 C ANISOU 1145 CA LEU A 145 6352 5318 6713 150 925 56 C ATOM 1146 C LEU A 145 -9.427 23.112 29.163 1.00 48.10 C ANISOU 1146 C LEU A 145 6310 5285 6679 136 902 73 C ATOM 1147 O LEU A 145 -10.145 22.123 29.101 1.00 48.47 O ANISOU 1147 O LEU A 145 6356 5306 6755 121 946 84 O ATOM 1148 CB LEU A 145 -10.280 25.501 29.288 1.00 49.21 C ANISOU 1148 CB LEU A 145 6391 5425 6881 133 886 39 C ATOM 1149 CG LEU A 145 -11.192 25.261 28.053 1.00 51.41 C ANISOU 1149 CG LEU A 145 6608 5687 7239 104 865 40 C ATOM 1150 CD1 LEU A 145 -12.561 24.766 28.465 1.00 52.04 C ANISOU 1150 CD1 LEU A 145 6654 5730 7389 92 932 33 C ATOM 1151 CD2 LEU A 145 -11.357 26.524 27.234 1.00 51.94 C ANISOU 1151 CD2 LEU A 145 6638 5755 7344 100 806 28 C ATOM 1152 N VAL A 146 -8.289 23.237 28.456 1.00 47.78 N ANISOU 1152 N VAL A 146 6267 5272 6615 139 841 73 N ATOM 1153 CA VAL A 146 -7.835 22.238 27.492 1.00 47.67 C ANISOU 1153 CA VAL A 146 6252 5261 6600 129 821 85 C ATOM 1154 C VAL A 146 -7.423 20.953 28.169 1.00 47.86 C ANISOU 1154 C VAL A 146 6330 5275 6581 151 849 100 C ATOM 1155 O VAL A 146 -7.748 19.879 27.660 1.00 48.30 O ANISOU 1155 O VAL A 146 6389 5311 6653 137 866 111 O ATOM 1156 CB VAL A 146 -6.755 22.770 26.533 1.00 47.57 C ANISOU 1156 CB VAL A 146 6222 5271 6580 126 770 80 C ATOM 1157 CG1 VAL A 146 -6.234 21.660 25.626 1.00 47.20 C ANISOU 1157 CG1 VAL A 146 6186 5223 6525 122 764 89 C ATOM 1158 CG2 VAL A 146 -7.293 23.941 25.714 1.00 47.61 C ANISOU 1158 CG2 VAL A 146 6193 5273 6625 104 745 73 C ATOM 1159 N THR A 147 -6.821 21.035 29.377 1.00 47.22 N ANISOU 1159 N THR A 147 6299 5198 6443 188 852 100 N ATOM 1160 CA THR A 147 -6.485 19.842 30.167 1.00 46.81 C ANISOU 1160 CA THR A 147 6320 5128 6338 219 875 118 C ATOM 1161 C THR A 147 -7.770 19.090 30.488 1.00 47.61 C ANISOU 1161 C THR A 147 6444 5186 6460 199 959 136 C ATOM 1162 O THR A 147 -7.819 17.877 30.313 1.00 49.02 O ANISOU 1162 O THR A 147 6649 5339 6637 196 983 154 O ATOM 1163 CB THR A 147 -5.687 20.234 31.415 1.00 47.36 C ANISOU 1163 CB THR A 147 6451 5205 6338 269 846 108 C ATOM 1164 OG1 THR A 147 -4.419 20.724 30.974 1.00 48.68 O ANISOU 1164 OG1 THR A 147 6577 5405 6513 282 768 86 O ATOM 1165 CG2 THR A 147 -5.453 19.073 32.361 1.00 47.60 C ANISOU 1165 CG2 THR A 147 6582 5205 6299 311 868 130 C ATOM 1166 N LEU A 148 -8.841 19.818 30.842 1.00 46.78 N ANISOU 1166 N LEU A 148 6316 5068 6390 180 1007 127 N ATOM 1167 CA LEU A 148 -10.139 19.236 31.121 1.00 47.14 C ANISOU 1167 CA LEU A 148 6360 5066 6484 153 1099 136 C ATOM 1168 C LEU A 148 -10.813 18.654 29.872 1.00 47.74 C ANISOU 1168 C LEU A 148 6362 5127 6651 108 1089 132 C ATOM 1169 O LEU A 148 -11.448 17.604 29.970 1.00 48.13 O ANISOU 1169 O LEU A 148 6422 5132 6733 88 1151 143 O ATOM 1170 CB LEU A 148 -11.061 20.256 31.801 1.00 47.40 C ANISOU 1170 CB LEU A 148 6376 5088 6547 149 1154 120 C ATOM 1171 CG LEU A 148 -10.663 20.709 33.199 1.00 47.96 C ANISOU 1171 CG LEU A 148 6543 5157 6523 193 1183 122 C ATOM 1172 CD1 LEU A 148 -11.581 21.816 33.694 1.00 48.13 C ANISOU 1172 CD1 LEU A 148 6538 5167 6583 188 1237 99 C ATOM 1173 CD2 LEU A 148 -10.637 19.555 34.162 1.00 47.92 C ANISOU 1173 CD2 LEU A 148 6651 5108 6447 216 1258 152 C ATOM 1174 N GLU A 149 -10.677 19.301 28.709 1.00 47.75 N ANISOU 1174 N GLU A 149 6297 5157 6688 93 1012 114 N ATOM 1175 CA GLU A 149 -11.268 18.788 27.459 1.00 48.28 C ANISOU 1175 CA GLU A 149 6310 5208 6827 58 982 104 C ATOM 1176 C GLU A 149 -10.672 17.434 27.041 1.00 49.51 C ANISOU 1176 C GLU A 149 6507 5352 6953 59 976 118 C ATOM 1177 O GLU A 149 -11.348 16.609 26.450 1.00 49.71 O ANISOU 1177 O GLU A 149 6510 5342 7036 30 983 112 O ATOM 1178 CB GLU A 149 -11.018 19.782 26.315 1.00 48.90 C ANISOU 1178 CB GLU A 149 6345 5316 6917 54 897 88 C ATOM 1179 CG GLU A 149 -11.892 21.019 26.325 1.00 49.81 C ANISOU 1179 CG GLU A 149 6406 5430 7092 47 887 69 C ATOM 1180 CD GLU A 149 -11.510 22.078 25.307 1.00 52.96 C ANISOU 1180 CD GLU A 149 6788 5852 7483 50 806 61 C ATOM 1181 OE1 GLU A 149 -10.454 21.936 24.654 1.00 53.52 O ANISOU 1181 OE1 GLU A 149 6893 5944 7499 56 770 71 O ATOM 1182 OE2 GLU A 149 -12.258 23.070 25.174 1.00 55.21 O ANISOU 1182 OE2 GLU A 149 7029 6127 7820 48 786 46 O ATOM 1183 N VAL A 150 -9.385 17.247 27.323 1.00 50.09 N ANISOU 1183 N VAL A 150 6635 5451 6945 95 956 132 N ATOM 1184 CA VAL A 150 -8.532 16.109 26.997 1.00 50.45 C ANISOU 1184 CA VAL A 150 6723 5492 6955 110 943 144 C ATOM 1185 C VAL A 150 -8.627 14.970 28.040 1.00 52.05 C ANISOU 1185 C VAL A 150 6996 5651 7128 126 1009 169 C ATOM 1186 O VAL A 150 -8.374 13.809 27.704 1.00 52.62 O ANISOU 1186 O VAL A 150 7099 5698 7197 128 1013 178 O ATOM 1187 CB VAL A 150 -7.107 16.703 26.878 1.00 50.27 C ANISOU 1187 CB VAL A 150 6707 5515 6878 145 887 139 C ATOM 1188 CG1 VAL A 150 -6.018 15.671 27.078 1.00 51.07 C ANISOU 1188 CG1 VAL A 150 6859 5612 6934 182 879 150 C ATOM 1189 CG2 VAL A 150 -6.935 17.438 25.556 1.00 50.05 C ANISOU 1189 CG2 VAL A 150 6630 5511 6875 124 838 122 C ATOM 1190 N LEU A 151 -9.005 15.302 29.295 1.00 52.23 N ANISOU 1190 N LEU A 151 7058 5661 7126 140 1064 180 N ATOM 1191 CA LEU A 151 -9.110 14.354 30.404 1.00 53.10 C ANISOU 1191 CA LEU A 151 7262 5723 7191 160 1138 209 C ATOM 1192 C LEU A 151 -10.025 13.134 30.142 1.00 52.61 C ANISOU 1192 C LEU A 151 7200 5596 7192 119 1208 220 C ATOM 1193 O LEU A 151 -9.598 12.034 30.518 1.00 53.18 O ANISOU 1193 O LEU A 151 7355 5633 7220 142 1232 246 O ATOM 1194 CB LEU A 151 -9.533 15.086 31.681 1.00 54.67 C ANISOU 1194 CB LEU A 151 7506 5913 7353 177 1197 215 C ATOM 1195 CG LEU A 151 -8.666 14.880 32.916 1.00 57.25 C ANISOU 1195 CG LEU A 151 7958 6232 7562 241 1195 236 C ATOM 1196 CD1 LEU A 151 -7.231 15.340 32.652 1.00 58.18 C ANISOU 1196 CD1 LEU A 151 8066 6407 7635 285 1075 219 C ATOM 1197 CD2 LEU A 151 -9.275 15.621 34.128 1.00 57.90 C ANISOU 1197 CD2 LEU A 151 8098 6297 7606 253 1268 238 C ATOM 1198 N PRO A 152 -11.224 13.226 29.486 1.00 50.97 N ANISOU 1198 N PRO A 152 6905 5367 7094 62 1233 198 N ATOM 1199 CA PRO A 152 -11.989 12.002 29.221 1.00 50.30 C ANISOU 1199 CA PRO A 152 6816 5215 7081 21 1291 201 C ATOM 1200 C PRO A 152 -11.224 11.017 28.335 1.00 49.52 C ANISOU 1200 C PRO A 152 6739 5114 6961 30 1230 201 C ATOM 1201 O PRO A 152 -11.380 9.808 28.515 1.00 49.00 O ANISOU 1201 O PRO A 152 6723 4988 6906 20 1282 218 O ATOM 1202 CB PRO A 152 -13.272 12.512 28.559 1.00 50.88 C ANISOU 1202 CB PRO A 152 6771 5277 7285 -33 1290 163 C ATOM 1203 CG PRO A 152 -13.340 13.925 28.917 1.00 51.32 C ANISOU 1203 CG PRO A 152 6794 5377 7327 -17 1276 153 C ATOM 1204 CD PRO A 152 -11.943 14.398 28.965 1.00 49.94 C ANISOU 1204 CD PRO A 152 6675 5263 7035 35 1204 166 C ATOM 1205 N MET A 153 -10.388 11.521 27.389 1.00 49.15 N ANISOU 1205 N MET A 153 6662 5125 6886 48 1129 183 N ATOM 1206 CA MET A 153 -9.576 10.635 26.556 1.00 49.15 C ANISOU 1206 CA MET A 153 6689 5123 6861 62 1081 180 C ATOM 1207 C MET A 153 -8.566 9.878 27.446 1.00 48.75 C ANISOU 1207 C MET A 153 6736 5060 6728 117 1102 214 C ATOM 1208 O MET A 153 -8.408 8.679 27.291 1.00 49.46 O ANISOU 1208 O MET A 153 6871 5104 6818 120 1119 224 O ATOM 1209 CB MET A 153 -8.846 11.418 25.460 1.00 50.29 C ANISOU 1209 CB MET A 153 6793 5328 6987 73 993 157 C ATOM 1210 CG MET A 153 -7.688 10.647 24.856 1.00 53.29 C ANISOU 1210 CG MET A 153 7212 5713 7322 104 959 157 C ATOM 1211 SD MET A 153 -6.540 11.592 23.874 1.00 60.60 S ANISOU 1211 SD MET A 153 8108 6703 8212 127 891 137 S ATOM 1212 CE MET A 153 -5.862 12.649 25.065 1.00 59.78 C ANISOU 1212 CE MET A 153 8002 6644 8069 163 889 151 C ATOM 1213 N LEU A 154 -7.901 10.574 28.371 1.00 48.04 N ANISOU 1213 N LEU A 154 6680 5004 6568 162 1093 228 N ATOM 1214 CA LEU A 154 -6.934 9.994 29.292 1.00 47.53 C ANISOU 1214 CA LEU A 154 6712 4926 6420 226 1090 255 C ATOM 1215 C LEU A 154 -7.585 9.005 30.239 1.00 48.64 C ANISOU 1215 C LEU A 154 6947 4989 6546 224 1183 291 C ATOM 1216 O LEU A 154 -7.003 7.941 30.503 1.00 48.96 O ANISOU 1216 O LEU A 154 7069 4990 6545 262 1184 314 O ATOM 1217 CB LEU A 154 -6.166 11.089 30.053 1.00 46.72 C ANISOU 1217 CB LEU A 154 6622 4875 6255 273 1043 252 C ATOM 1218 CG LEU A 154 -5.357 12.078 29.187 1.00 46.98 C ANISOU 1218 CG LEU A 154 6569 4977 6306 276 961 219 C ATOM 1219 CD1 LEU A 154 -4.610 13.076 30.047 1.00 47.57 C ANISOU 1219 CD1 LEU A 154 6656 5089 6330 319 914 210 C ATOM 1220 CD2 LEU A 154 -4.394 11.368 28.271 1.00 47.04 C ANISOU 1220 CD2 LEU A 154 6561 4990 6322 294 916 208 C ATOM 1221 N THR A 155 -8.831 9.296 30.682 1.00 49.13 N ANISOU 1221 N THR A 155 6994 5020 6651 178 1270 295 N ATOM 1222 CA THR A 155 -9.610 8.392 31.555 1.00 49.60 C ANISOU 1222 CA THR A 155 7140 4993 6713 163 1389 329 C ATOM 1223 C THR A 155 -9.894 7.086 30.797 1.00 50.83 C ANISOU 1223 C THR A 155 7287 5090 6934 127 1409 329 C ATOM 1224 O THR A 155 -9.818 6.015 31.382 1.00 51.38 O ANISOU 1224 O THR A 155 7461 5089 6970 144 1468 365 O ATOM 1225 CB THR A 155 -10.905 9.084 32.062 1.00 49.48 C ANISOU 1225 CB THR A 155 7084 4958 6757 115 1486 323 C ATOM 1226 OG1 THR A 155 -10.543 10.297 32.707 1.00 51.00 O ANISOU 1226 OG1 THR A 155 7290 5205 6882 153 1457 319 O ATOM 1227 CG2 THR A 155 -11.732 8.215 33.026 1.00 48.18 C ANISOU 1227 CG2 THR A 155 7012 4696 6599 94 1638 360 C ATOM 1228 N PHE A 156 -10.207 7.178 29.494 1.00 51.46 N ANISOU 1228 N PHE A 156 7257 5193 7103 81 1354 289 N ATOM 1229 CA PHE A 156 -10.436 6.010 28.667 1.00 53.04 C ANISOU 1229 CA PHE A 156 7448 5340 7365 48 1355 277 C ATOM 1230 C PHE A 156 -9.124 5.220 28.548 1.00 54.68 C ANISOU 1230 C PHE A 156 7735 5550 7492 111 1301 293 C ATOM 1231 O PHE A 156 -9.141 3.990 28.681 1.00 54.82 O ANISOU 1231 O PHE A 156 7821 5495 7514 112 1344 313 O ATOM 1232 CB PHE A 156 -10.983 6.407 27.276 1.00 53.41 C ANISOU 1232 CB PHE A 156 7374 5415 7505 -2 1287 224 C ATOM 1233 CG PHE A 156 -10.730 5.366 26.200 1.00 55.56 C ANISOU 1233 CG PHE A 156 7651 5657 7803 -13 1241 202 C ATOM 1234 CD1 PHE A 156 -11.335 4.115 26.259 1.00 57.16 C ANISOU 1234 CD1 PHE A 156 7883 5768 8067 -49 1304 206 C ATOM 1235 CD2 PHE A 156 -9.831 5.609 25.177 1.00 56.80 C ANISOU 1235 CD2 PHE A 156 7792 5869 7919 16 1146 179 C ATOM 1236 CE1 PHE A 156 -11.067 3.149 25.293 1.00 57.86 C ANISOU 1236 CE1 PHE A 156 7985 5824 8175 -55 1260 182 C ATOM 1237 CE2 PHE A 156 -9.574 4.649 24.209 1.00 57.40 C ANISOU 1237 CE2 PHE A 156 7887 5914 8010 11 1111 156 C ATOM 1238 CZ PHE A 156 -10.190 3.427 24.272 1.00 57.60 C ANISOU 1238 CZ PHE A 156 7941 5851 8094 -23 1162 156 C ATOM 1239 N ILE A 157 -7.997 5.921 28.278 1.00 55.35 N ANISOU 1239 N ILE A 157 7803 5712 7515 162 1211 282 N ATOM 1240 CA ILE A 157 -6.700 5.258 28.133 1.00 56.45 C ANISOU 1240 CA ILE A 157 7996 5856 7597 226 1157 289 C ATOM 1241 C ILE A 157 -6.318 4.482 29.429 1.00 57.28 C ANISOU 1241 C ILE A 157 8233 5904 7628 284 1197 337 C ATOM 1242 O ILE A 157 -5.894 3.331 29.335 1.00 57.52 O ANISOU 1242 O ILE A 157 8325 5882 7648 312 1197 349 O ATOM 1243 CB ILE A 157 -5.608 6.256 27.641 1.00 56.59 C ANISOU 1243 CB ILE A 157 7955 5961 7585 264 1066 263 C ATOM 1244 CG1 ILE A 157 -5.883 6.730 26.205 1.00 56.94 C ANISOU 1244 CG1 ILE A 157 7905 6042 7688 215 1030 221 C ATOM 1245 CG2 ILE A 157 -4.184 5.698 27.772 1.00 56.74 C ANISOU 1245 CG2 ILE A 157 8020 5985 7555 341 1014 267 C ATOM 1246 CD1 ILE A 157 -5.197 8.040 25.872 1.00 57.33 C ANISOU 1246 CD1 ILE A 157 7893 6169 7719 231 972 201 C ATOM 1247 N THR A 158 -6.548 5.065 30.623 1.00 57.38 N ANISOU 1247 N THR A 158 8300 5917 7586 302 1234 363 N ATOM 1248 CA THR A 158 -6.238 4.373 31.875 1.00 58.24 C ANISOU 1248 CA THR A 158 8558 5963 7606 362 1270 411 C ATOM 1249 C THR A 158 -7.092 3.118 32.079 1.00 59.19 C ANISOU 1249 C THR A 158 8755 5977 7758 324 1381 443 C ATOM 1250 O THR A 158 -6.649 2.201 32.772 1.00 59.58 O ANISOU 1250 O THR A 158 8938 5962 7740 379 1397 483 O ATOM 1251 CB THR A 158 -6.287 5.310 33.073 1.00 60.02 C ANISOU 1251 CB THR A 158 8843 6209 7754 393 1284 427 C ATOM 1252 OG1 THR A 158 -7.639 5.720 33.320 1.00 62.06 O ANISOU 1252 OG1 THR A 158 9075 6444 8062 322 1395 431 O ATOM 1253 CG2 THR A 158 -5.365 6.500 32.918 1.00 59.86 C ANISOU 1253 CG2 THR A 158 8752 6283 7709 431 1170 392 C ATOM 1254 N SER A 159 -8.271 3.032 31.423 1.00 59.48 N ANISOU 1254 N SER A 159 8705 5989 7904 233 1448 423 N ATOM 1255 CA SER A 159 -9.126 1.839 31.465 1.00 60.00 C ANISOU 1255 CA SER A 159 8818 5948 8033 183 1554 443 C ATOM 1256 C SER A 159 -8.582 0.702 30.576 1.00 60.42 C ANISOU 1256 C SER A 159 8877 5967 8111 192 1504 431 C ATOM 1257 O SER A 159 -8.943 -0.448 30.778 1.00 60.86 O ANISOU 1257 O SER A 159 9009 5925 8190 175 1579 456 O ATOM 1258 CB SER A 159 -10.570 2.174 31.091 1.00 61.28 C ANISOU 1258 CB SER A 159 8869 6090 8323 84 1632 414 C ATOM 1259 OG SER A 159 -10.798 2.240 29.693 1.00 63.27 O ANISOU 1259 OG SER A 159 8991 6376 8674 36 1558 358 O ATOM 1260 N THR A 160 -7.747 1.018 29.584 1.00 60.29 N ANISOU 1260 N THR A 160 8784 6026 8096 217 1390 391 N ATOM 1261 CA THR A 160 -7.123 0.019 28.716 1.00 60.54 C ANISOU 1261 CA THR A 160 8825 6031 8144 236 1342 374 C ATOM 1262 C THR A 160 -5.854 -0.575 29.425 1.00 61.26 C ANISOU 1262 C THR A 160 9034 6104 8136 339 1304 409 C ATOM 1263 O THR A 160 -5.397 -0.011 30.436 1.00 61.26 O ANISOU 1263 O THR A 160 9091 6130 8055 396 1288 437 O ATOM 1264 CB THR A 160 -6.872 0.627 27.313 1.00 60.89 C ANISOU 1264 CB THR A 160 8747 6155 8233 214 1255 314 C ATOM 1265 OG1 THR A 160 -5.785 1.559 27.376 1.00 62.03 O ANISOU 1265 OG1 THR A 160 8866 6389 8315 275 1178 308 O ATOM 1266 CG2 THR A 160 -8.121 1.292 26.727 1.00 60.53 C ANISOU 1266 CG2 THR A 160 8598 6124 8277 126 1273 280 C ATOM 1267 N PRO A 161 -5.281 -1.717 28.958 1.00 61.54 N ANISOU 1267 N PRO A 161 9113 6089 8180 371 1282 406 N ATOM 1268 CA PRO A 161 -4.119 -2.292 29.669 1.00 61.51 C ANISOU 1268 CA PRO A 161 9219 6060 8094 477 1237 438 C ATOM 1269 C PRO A 161 -2.759 -1.644 29.345 1.00 60.88 C ANISOU 1269 C PRO A 161 9075 6070 7985 552 1120 406 C ATOM 1270 O PRO A 161 -1.825 -2.336 28.896 1.00 60.69 O ANISOU 1270 O PRO A 161 9059 6032 7968 609 1070 390 O ATOM 1271 CB PRO A 161 -4.166 -3.775 29.283 1.00 62.27 C ANISOU 1271 CB PRO A 161 9381 6055 8225 475 1271 445 C ATOM 1272 CG PRO A 161 -4.734 -3.766 27.914 1.00 63.00 C ANISOU 1272 CG PRO A 161 9358 6166 8412 393 1272 389 C ATOM 1273 CD PRO A 161 -5.691 -2.580 27.829 1.00 61.39 C ANISOU 1273 CD PRO A 161 9057 6024 8245 317 1294 372 C ATOM 1274 N ILE A 162 -2.628 -0.325 29.646 1.00 59.74 N ANISOU 1274 N ILE A 162 8870 6013 7817 553 1083 395 N ATOM 1275 CA ILE A 162 -1.394 0.428 29.408 1.00 59.31 C ANISOU 1275 CA ILE A 162 8742 6040 7752 614 982 360 C ATOM 1276 C ILE A 162 -0.216 -0.087 30.242 1.00 60.06 C ANISOU 1276 C ILE A 162 8923 6107 7790 728 910 378 C ATOM 1277 O ILE A 162 0.923 0.072 29.818 1.00 60.14 O ANISOU 1277 O ILE A 162 8866 6159 7825 783 831 341 O ATOM 1278 CB ILE A 162 -1.575 1.964 29.545 1.00 58.24 C ANISOU 1278 CB ILE A 162 8525 5993 7611 584 961 343 C ATOM 1279 CG1 ILE A 162 -2.153 2.368 30.907 1.00 57.19 C ANISOU 1279 CG1 ILE A 162 8482 5840 7409 591 996 384 C ATOM 1280 CG2 ILE A 162 -2.401 2.502 28.389 1.00 58.71 C ANISOU 1280 CG2 ILE A 162 8477 6090 7741 490 995 311 C ATOM 1281 CD1 ILE A 162 -2.081 3.815 31.143 1.00 57.35 C ANISOU 1281 CD1 ILE A 162 8434 5940 7417 584 959 363 C ATOM 1282 N GLU A 163 -0.495 -0.733 31.395 1.00 60.61 N ANISOU 1282 N GLU A 163 9144 6099 7788 766 941 432 N ATOM 1283 CA GLU A 163 0.476 -1.365 32.308 1.00 61.34 C ANISOU 1283 CA GLU A 163 9354 6142 7811 883 867 457 C ATOM 1284 C GLU A 163 1.311 -2.439 31.592 1.00 61.39 C ANISOU 1284 C GLU A 163 9348 6111 7867 935 828 437 C ATOM 1285 O GLU A 163 2.403 -2.763 32.045 1.00 61.37 O ANISOU 1285 O GLU A 163 9385 6092 7840 1041 733 434 O ATOM 1286 CB GLU A 163 -0.238 -1.985 33.539 1.00 64.23 C ANISOU 1286 CB GLU A 163 9911 6409 8085 898 940 527 C ATOM 1287 CG GLU A 163 -1.284 -1.094 34.207 1.00 70.14 C ANISOU 1287 CG GLU A 163 10682 7174 8792 836 1019 549 C ATOM 1288 CD GLU A 163 -2.688 -1.147 33.618 1.00 77.04 C ANISOU 1288 CD GLU A 163 11501 8028 9741 710 1155 552 C ATOM 1289 OE1 GLU A 163 -3.015 -2.169 32.972 1.00 77.83 O ANISOU 1289 OE1 GLU A 163 11604 8066 9901 674 1206 555 O ATOM 1290 OE2 GLU A 163 -3.459 -0.174 33.802 1.00 80.15 O ANISOU 1290 OE2 GLU A 163 11847 8464 10141 650 1205 546 O ATOM 1291 N LYS A 164 0.804 -2.983 30.474 1.00 61.59 N ANISOU 1291 N LYS A 164 9317 6118 7965 863 893 419 N ATOM 1292 CA LYS A 164 1.518 -3.955 29.660 1.00 62.55 C ANISOU 1292 CA LYS A 164 9421 6206 8139 902 869 392 C ATOM 1293 C LYS A 164 2.776 -3.380 28.977 1.00 64.02 C ANISOU 1293 C LYS A 164 9475 6474 8376 952 783 331 C ATOM 1294 O LYS A 164 3.574 -4.150 28.448 1.00 64.46 O ANISOU 1294 O LYS A 164 9518 6501 8474 1006 756 306 O ATOM 1295 CB LYS A 164 0.584 -4.608 28.633 1.00 64.05 C ANISOU 1295 CB LYS A 164 9592 6355 8388 808 959 380 C ATOM 1296 CG LYS A 164 -0.440 -5.534 29.271 1.00 67.65 C ANISOU 1296 CG LYS A 164 10182 6701 8821 773 1048 436 C ATOM 1297 CD LYS A 164 -1.321 -6.229 28.249 1.00 72.29 C ANISOU 1297 CD LYS A 164 10745 7238 9485 683 1121 414 C ATOM 1298 CE LYS A 164 -2.331 -7.142 28.901 1.00 75.88 C ANISOU 1298 CE LYS A 164 11322 7574 9936 641 1221 466 C ATOM 1299 NZ LYS A 164 -3.032 -7.981 27.898 1.00 78.31 N ANISOU 1299 NZ LYS A 164 11605 7818 10330 563 1274 435 N ATOM 1300 N GLY A 165 2.942 -2.055 28.985 1.00 64.54 N ANISOU 1300 N GLY A 165 9444 6633 8447 931 749 307 N ATOM 1301 CA GLY A 165 4.114 -1.386 28.442 1.00 65.66 C ANISOU 1301 CA GLY A 165 9456 6847 8645 970 680 251 C ATOM 1302 C GLY A 165 4.118 -1.160 26.945 1.00 67.04 C ANISOU 1302 C GLY A 165 9517 7064 8890 906 728 203 C ATOM 1303 O GLY A 165 4.786 -0.239 26.456 1.00 67.68 O ANISOU 1303 O GLY A 165 9483 7216 9014 905 702 161 O ATOM 1304 N ASP A 166 3.373 -1.985 26.198 1.00 67.25 N ANISOU 1304 N ASP A 166 9582 7041 8927 853 799 207 N ATOM 1305 CA ASP A 166 3.330 -1.858 24.737 1.00 67.64 C ANISOU 1305 CA ASP A 166 9554 7120 9027 797 840 160 C ATOM 1306 C ASP A 166 1.934 -1.484 24.188 1.00 66.88 C ANISOU 1306 C ASP A 166 9455 7033 8922 687 897 165 C ATOM 1307 O ASP A 166 1.615 -1.768 23.027 1.00 67.16 O ANISOU 1307 O ASP A 166 9476 7059 8983 641 930 134 O ATOM 1308 CB ASP A 166 3.863 -3.141 24.079 1.00 69.70 C ANISOU 1308 CB ASP A 166 9847 7316 9321 842 855 138 C ATOM 1309 CG ASP A 166 2.998 -4.367 24.316 1.00 75.71 C ANISOU 1309 CG ASP A 166 10726 7979 10061 823 895 172 C ATOM 1310 OD1 ASP A 166 3.159 -5.358 23.567 1.00 78.10 O ANISOU 1310 OD1 ASP A 166 11056 8226 10393 836 919 149 O ATOM 1311 OD2 ASP A 166 2.151 -4.336 25.249 1.00 76.93 O ANISOU 1311 OD2 ASP A 166 10947 8107 10175 794 910 221 O ATOM 1312 N SER A 167 1.112 -0.861 25.030 1.00 65.50 N ANISOU 1312 N SER A 167 9299 6873 8715 649 903 200 N ATOM 1313 CA SER A 167 -0.240 -0.513 24.654 1.00 64.98 C ANISOU 1313 CA SER A 167 9222 6808 8658 552 950 203 C ATOM 1314 C SER A 167 -0.450 0.977 24.781 1.00 63.74 C ANISOU 1314 C SER A 167 8990 6734 8492 519 933 198 C ATOM 1315 O SER A 167 -0.118 1.559 25.811 1.00 63.66 O ANISOU 1315 O SER A 167 8988 6750 8449 556 905 220 O ATOM 1316 CB SER A 167 -1.235 -1.284 25.520 1.00 66.47 C ANISOU 1316 CB SER A 167 9507 6917 8833 528 1000 249 C ATOM 1317 OG SER A 167 -2.577 -0.888 25.290 1.00 68.99 O ANISOU 1317 OG SER A 167 9798 7235 9180 435 1045 249 O ATOM 1318 N CYS A 168 -0.964 1.599 23.721 1.00 62.65 N ANISOU 1318 N CYS A 168 8789 6634 8381 454 942 168 N ATOM 1319 CA CYS A 168 -1.256 3.025 23.717 1.00 62.20 C ANISOU 1319 CA CYS A 168 8664 6648 8321 418 928 162 C ATOM 1320 C CYS A 168 -2.313 3.304 22.667 1.00 61.60 C ANISOU 1320 C CYS A 168 8559 6574 8274 339 943 139 C ATOM 1321 O CYS A 168 -1.972 3.711 21.559 1.00 62.99 O ANISOU 1321 O CYS A 168 8698 6781 8453 329 929 106 O ATOM 1322 CB CYS A 168 -0.002 3.862 23.479 1.00 62.13 C ANISOU 1322 CB CYS A 168 8591 6704 8313 461 890 138 C ATOM 1323 SG CYS A 168 -0.190 5.570 24.012 1.00 63.00 S ANISOU 1323 SG CYS A 168 8637 6887 8412 437 867 143 S ATOM 1324 N VAL A 169 -3.586 3.093 22.998 1.00 59.43 N ANISOU 1324 N VAL A 169 8302 6260 8021 286 972 154 N ATOM 1325 CA VAL A 169 -4.669 3.239 22.024 1.00 57.57 C ANISOU 1325 CA VAL A 169 8034 6013 7826 215 969 125 C ATOM 1326 C VAL A 169 -5.112 4.684 21.694 1.00 55.35 C ANISOU 1326 C VAL A 169 7684 5796 7551 181 941 112 C ATOM 1327 O VAL A 169 -4.950 5.624 22.490 1.00 54.47 O ANISOU 1327 O VAL A 169 7545 5729 7421 194 941 132 O ATOM 1328 CB VAL A 169 -5.904 2.399 22.425 1.00 57.74 C ANISOU 1328 CB VAL A 169 8082 5957 7899 166 1012 135 C ATOM 1329 CG1 VAL A 169 -5.552 0.930 22.509 1.00 58.58 C ANISOU 1329 CG1 VAL A 169 8265 5988 8006 192 1038 143 C ATOM 1330 CG2 VAL A 169 -6.493 2.884 23.732 1.00 57.67 C ANISOU 1330 CG2 VAL A 169 8072 5947 7891 155 1056 174 C ATOM 1331 N ASP A 170 -5.675 4.814 20.466 1.00 53.80 N ANISOU 1331 N ASP A 170 7469 5595 7377 140 911 75 N ATOM 1332 CA ASP A 170 -6.304 6.003 19.924 1.00 52.89 C ANISOU 1332 CA ASP A 170 7303 5520 7274 105 874 58 C ATOM 1333 C ASP A 170 -7.839 5.791 20.087 1.00 52.89 C ANISOU 1333 C ASP A 170 7275 5472 7350 46 875 48 C ATOM 1334 O ASP A 170 -8.363 4.813 19.569 1.00 53.25 O ANISOU 1334 O ASP A 170 7341 5457 7434 20 869 24 O ATOM 1335 CB ASP A 170 -5.925 6.174 18.446 1.00 52.68 C ANISOU 1335 CB ASP A 170 7295 5504 7216 107 833 22 C ATOM 1336 CG ASP A 170 -6.546 7.361 17.735 1.00 56.03 C ANISOU 1336 CG ASP A 170 7689 5959 7640 78 784 4 C ATOM 1337 OD1 ASP A 170 -7.284 8.132 18.387 1.00 56.78 O ANISOU 1337 OD1 ASP A 170 7732 6071 7772 55 779 17 O ATOM 1338 OD2 ASP A 170 -6.294 7.526 16.533 1.00 58.38 O ANISOU 1338 OD2 ASP A 170 8024 6259 7899 82 754 -21 O ATOM 1339 N TYR A 171 -8.550 6.696 20.786 1.00 52.11 N ANISOU 1339 N TYR A 171 7123 5394 7282 24 886 61 N ATOM 1340 CA TYR A 171 -10.006 6.591 20.960 1.00 51.93 C ANISOU 1340 CA TYR A 171 7053 5324 7353 -32 896 46 C ATOM 1341 C TYR A 171 -10.768 6.598 19.626 1.00 53.20 C ANISOU 1341 C TYR A 171 7187 5463 7563 -67 817 -7 C ATOM 1342 O TYR A 171 -11.867 6.039 19.552 1.00 53.58 O ANISOU 1342 O TYR A 171 7200 5451 7708 -114 815 -33 O ATOM 1343 CB TYR A 171 -10.551 7.666 21.918 1.00 50.80 C ANISOU 1343 CB TYR A 171 6857 5211 7235 -42 927 66 C ATOM 1344 CG TYR A 171 -10.474 9.087 21.399 1.00 50.08 C ANISOU 1344 CG TYR A 171 6723 5182 7122 -34 867 53 C ATOM 1345 CD1 TYR A 171 -11.513 9.638 20.664 1.00 50.32 C ANISOU 1345 CD1 TYR A 171 6695 5204 7221 -69 809 17 C ATOM 1346 CD2 TYR A 171 -9.411 9.911 21.730 1.00 50.55 C ANISOU 1346 CD2 TYR A 171 6798 5304 7104 8 866 76 C ATOM 1347 CE1 TYR A 171 -11.438 10.932 20.167 1.00 50.73 C ANISOU 1347 CE1 TYR A 171 6722 5304 7247 -57 752 10 C ATOM 1348 CE2 TYR A 171 -9.345 11.226 21.276 1.00 51.05 C ANISOU 1348 CE2 TYR A 171 6828 5416 7152 11 819 67 C ATOM 1349 CZ TYR A 171 -10.358 11.732 20.489 1.00 51.59 C ANISOU 1349 CZ TYR A 171 6855 5473 7276 -20 765 38 C ATOM 1350 OH TYR A 171 -10.300 13.038 20.059 1.00 52.56 O ANISOU 1350 OH TYR A 171 6957 5635 7379 -13 719 33 O ATOM 1351 N ALA A 172 -10.172 7.189 18.562 1.00 53.51 N ANISOU 1351 N ALA A 172 7249 5544 7538 -44 752 -24 N ATOM 1352 CA ALA A 172 -10.769 7.185 17.222 1.00 54.21 C ANISOU 1352 CA ALA A 172 7344 5608 7645 -64 663 -74 C ATOM 1353 C ALA A 172 -10.830 5.773 16.644 1.00 55.49 C ANISOU 1353 C ALA A 172 7556 5703 7823 -75 653 -105 C ATOM 1354 O ALA A 172 -11.785 5.448 15.937 1.00 55.76 O ANISOU 1354 O ALA A 172 7576 5687 7922 -109 586 -154 O ATOM 1355 CB ALA A 172 -9.978 8.075 16.286 1.00 53.97 C ANISOU 1355 CB ALA A 172 7357 5628 7521 -31 618 -77 C ATOM 1356 N SER A 173 -9.826 4.925 16.982 1.00 56.12 N ANISOU 1356 N SER A 173 7693 5776 7853 -44 715 -81 N ATOM 1357 CA SER A 173 -9.684 3.558 16.502 1.00 57.06 C ANISOU 1357 CA SER A 173 7871 5831 7977 -45 717 -106 C ATOM 1358 C SER A 173 -10.078 2.471 17.487 1.00 57.97 C ANISOU 1358 C SER A 173 7981 5882 8163 -68 785 -88 C ATOM 1359 O SER A 173 -10.334 1.351 17.059 1.00 58.06 O ANISOU 1359 O SER A 173 8028 5823 8210 -86 778 -118 O ATOM 1360 CB SER A 173 -8.246 3.324 16.058 1.00 58.68 C ANISOU 1360 CB SER A 173 8149 6064 8084 11 738 -98 C ATOM 1361 OG SER A 173 -7.886 4.192 14.993 1.00 61.66 O ANISOU 1361 OG SER A 173 8552 6482 8394 28 689 -118 O ATOM 1362 N SER A 174 -10.105 2.772 18.799 1.00 58.53 N ANISOU 1362 N SER A 174 8023 5970 8247 -65 856 -39 N ATOM 1363 CA SER A 174 -10.411 1.794 19.852 1.00 59.03 C ANISOU 1363 CA SER A 174 8104 5966 8358 -81 940 -9 C ATOM 1364 C SER A 174 -11.448 2.299 20.839 1.00 59.87 C ANISOU 1364 C SER A 174 8145 6061 8541 -123 993 10 C ATOM 1365 O SER A 174 -11.643 3.495 20.991 1.00 59.73 O ANISOU 1365 O SER A 174 8073 6103 8517 -122 975 13 O ATOM 1366 CB SER A 174 -9.144 1.428 20.617 1.00 60.16 C ANISOU 1366 CB SER A 174 8317 6126 8415 -16 990 40 C ATOM 1367 OG SER A 174 -8.069 1.113 19.750 1.00 62.52 O ANISOU 1367 OG SER A 174 8663 6444 8649 30 951 22 O ATOM 1368 N GLY A 175 -12.102 1.376 21.515 1.00 61.08 N ANISOU 1368 N GLY A 175 8309 6132 8768 -159 1071 21 N ATOM 1369 CA GLY A 175 -13.129 1.713 22.489 1.00 62.59 C ANISOU 1369 CA GLY A 175 8444 6295 9041 -203 1151 38 C ATOM 1370 C GLY A 175 -14.495 1.905 21.865 1.00 63.57 C ANISOU 1370 C GLY A 175 8461 6383 9311 -273 1112 -22 C ATOM 1371 O GLY A 175 -14.632 1.958 20.642 1.00 64.52 O ANISOU 1371 O GLY A 175 8554 6512 9450 -281 1001 -77 O ATOM 1372 N ASN A 176 -15.506 2.034 22.705 1.00 63.07 N ANISOU 1372 N ASN A 176 8337 6275 9351 -319 1202 -15 N ATOM 1373 CA ASN A 176 -16.896 2.209 22.298 1.00 62.98 C ANISOU 1373 CA ASN A 176 8200 6218 9510 -388 1178 -76 C ATOM 1374 C ASN A 176 -17.091 3.342 21.270 1.00 62.31 C ANISOU 1374 C ASN A 176 8042 6203 9429 -375 1034 -125 C ATOM 1375 O ASN A 176 -16.928 4.506 21.624 1.00 62.90 O ANISOU 1375 O ASN A 176 8096 6350 9454 -345 1032 -102 O ATOM 1376 CB ASN A 176 -17.739 2.448 23.549 1.00 64.01 C ANISOU 1376 CB ASN A 176 8281 6310 9729 -424 1321 -49 C ATOM 1377 CG ASN A 176 -19.173 2.090 23.380 1.00 67.71 C ANISOU 1377 CG ASN A 176 8628 6690 10411 -505 1347 -108 C ATOM 1378 OD1 ASN A 176 -19.814 2.431 22.381 1.00 69.50 O ANISOU 1378 OD1 ASN A 176 8753 6920 10734 -528 1223 -178 O ATOM 1379 ND2 ASN A 176 -19.714 1.401 24.365 1.00 68.84 N ANISOU 1379 ND2 ASN A 176 8778 6745 10635 -550 1509 -81 N ATOM 1380 N PRO A 177 -17.454 3.022 20.000 1.00 60.88 N ANISOU 1380 N PRO A 177 7834 5996 9302 -394 910 -192 N ATOM 1381 CA PRO A 177 -17.632 4.080 18.985 1.00 60.11 C ANISOU 1381 CA PRO A 177 7693 5955 9192 -374 765 -235 C ATOM 1382 C PRO A 177 -18.720 5.088 19.312 1.00 60.10 C ANISOU 1382 C PRO A 177 7563 5958 9313 -399 761 -258 C ATOM 1383 O PRO A 177 -18.602 6.228 18.935 1.00 60.44 O ANISOU 1383 O PRO A 177 7592 6067 9305 -365 683 -260 O ATOM 1384 CB PRO A 177 -17.974 3.307 17.704 1.00 60.39 C ANISOU 1384 CB PRO A 177 7737 5933 9276 -395 643 -308 C ATOM 1385 CG PRO A 177 -17.558 1.920 17.959 1.00 60.74 C ANISOU 1385 CG PRO A 177 7854 5915 9308 -409 721 -292 C ATOM 1386 CD PRO A 177 -17.706 1.689 19.429 1.00 59.65 C ANISOU 1386 CD PRO A 177 7700 5751 9214 -431 889 -234 C ATOM 1387 N LYS A 178 -19.774 4.674 20.005 1.00 60.20 N ANISOU 1387 N LYS A 178 7484 5897 9493 -458 850 -275 N ATOM 1388 CA LYS A 178 -20.877 5.549 20.395 1.00 60.50 C ANISOU 1388 CA LYS A 178 7386 5928 9673 -483 865 -301 C ATOM 1389 C LYS A 178 -20.362 6.648 21.336 1.00 59.07 C ANISOU 1389 C LYS A 178 7231 5826 9386 -440 945 -237 C ATOM 1390 O LYS A 178 -20.678 7.810 21.113 1.00 59.49 O ANISOU 1390 O LYS A 178 7222 5924 9456 -420 877 -255 O ATOM 1391 CB LYS A 178 -21.988 4.710 21.061 1.00 64.28 C ANISOU 1391 CB LYS A 178 7769 6299 10354 -560 986 -327 C ATOM 1392 CG LYS A 178 -23.075 5.499 21.794 1.00 71.88 C ANISOU 1392 CG LYS A 178 8593 7245 11473 -588 1065 -343 C ATOM 1393 CD LYS A 178 -23.837 4.563 22.781 1.00 79.74 C ANISOU 1393 CD LYS A 178 9540 8132 12624 -661 1257 -338 C ATOM 1394 CE LYS A 178 -25.040 5.194 23.455 1.00 85.21 C ANISOU 1394 CE LYS A 178 10080 8788 13508 -699 1355 -367 C ATOM 1395 NZ LYS A 178 -24.647 6.290 24.375 1.00 88.71 N ANISOU 1395 NZ LYS A 178 10569 9307 13829 -649 1442 -305 N ATOM 1396 N TYR A 179 -19.548 6.291 22.354 1.00 57.28 N ANISOU 1396 N TYR A 179 7105 5612 9046 -421 1077 -165 N ATOM 1397 CA TYR A 179 -19.004 7.265 23.295 1.00 56.35 C ANISOU 1397 CA TYR A 179 7026 5563 8822 -377 1146 -109 C ATOM 1398 C TYR A 179 -17.875 8.090 22.674 1.00 55.25 C ANISOU 1398 C TYR A 179 6952 5520 8520 -314 1035 -91 C ATOM 1399 O TYR A 179 -17.825 9.295 22.891 1.00 54.91 O ANISOU 1399 O TYR A 179 6883 5534 8445 -287 1018 -82 O ATOM 1400 CB TYR A 179 -18.542 6.607 24.599 1.00 56.47 C ANISOU 1400 CB TYR A 179 7137 5550 8769 -372 1308 -43 C ATOM 1401 CG TYR A 179 -19.663 6.021 25.424 1.00 57.30 C ANISOU 1401 CG TYR A 179 7187 5558 9026 -434 1457 -48 C ATOM 1402 CD1 TYR A 179 -19.650 4.688 25.798 1.00 58.36 C ANISOU 1402 CD1 TYR A 179 7386 5607 9179 -464 1554 -26 C ATOM 1403 CD2 TYR A 179 -20.729 6.805 25.844 1.00 58.12 C ANISOU 1403 CD2 TYR A 179 7175 5647 9260 -462 1513 -74 C ATOM 1404 CE1 TYR A 179 -20.671 4.141 26.563 1.00 59.33 C ANISOU 1404 CE1 TYR A 179 7466 5631 9447 -527 1711 -28 C ATOM 1405 CE2 TYR A 179 -21.752 6.273 26.617 1.00 59.11 C ANISOU 1405 CE2 TYR A 179 7247 5677 9536 -523 1673 -81 C ATOM 1406 CZ TYR A 179 -21.718 4.937 26.983 1.00 60.46 C ANISOU 1406 CZ TYR A 179 7488 5761 9722 -557 1777 -56 C ATOM 1407 OH TYR A 179 -22.720 4.368 27.745 1.00 62.39 O ANISOU 1407 OH TYR A 179 7687 5898 10121 -623 1955 -59 O ATOM 1408 N SER A 180 -17.007 7.460 21.867 1.00 54.65 N ANISOU 1408 N SER A 180 6956 5455 8353 -292 964 -91 N ATOM 1409 CA SER A 180 -15.923 8.143 21.160 1.00 54.40 C ANISOU 1409 CA SER A 180 6985 5502 8180 -238 872 -80 C ATOM 1410 C SER A 180 -16.465 9.197 20.203 1.00 54.14 C ANISOU 1410 C SER A 180 6890 5497 8185 -236 750 -124 C ATOM 1411 O SER A 180 -15.853 10.254 20.079 1.00 54.31 O ANISOU 1411 O SER A 180 6934 5584 8117 -197 715 -104 O ATOM 1412 CB SER A 180 -15.066 7.152 20.380 1.00 55.24 C ANISOU 1412 CB SER A 180 7182 5599 8210 -222 831 -83 C ATOM 1413 OG SER A 180 -14.352 6.317 21.273 1.00 57.94 O ANISOU 1413 OG SER A 180 7596 5924 8494 -206 932 -35 O ATOM 1414 N LEU A 181 -17.605 8.925 19.532 1.00 53.71 N ANISOU 1414 N LEU A 181 6758 5385 8267 -275 679 -185 N ATOM 1415 CA LEU A 181 -18.234 9.866 18.586 1.00 54.07 C ANISOU 1415 CA LEU A 181 6747 5441 8356 -266 543 -233 C ATOM 1416 C LEU A 181 -18.838 11.059 19.324 1.00 53.81 C ANISOU 1416 C LEU A 181 6626 5433 8387 -263 577 -225 C ATOM 1417 O LEU A 181 -18.633 12.188 18.900 1.00 54.08 O ANISOU 1417 O LEU A 181 6669 5515 8363 -227 502 -222 O ATOM 1418 CB LEU A 181 -19.314 9.164 17.731 1.00 54.20 C ANISOU 1418 CB LEU A 181 6698 5378 8515 -305 444 -310 C ATOM 1419 CG LEU A 181 -19.917 9.957 16.570 1.00 54.80 C ANISOU 1419 CG LEU A 181 6742 5454 8624 -286 268 -366 C ATOM 1420 CD1 LEU A 181 -18.831 10.442 15.598 1.00 54.92 C ANISOU 1420 CD1 LEU A 181 6894 5525 8448 -230 183 -345 C ATOM 1421 CD2 LEU A 181 -20.959 9.119 15.840 1.00 54.74 C ANISOU 1421 CD2 LEU A 181 6671 5361 8769 -325 166 -449 C ATOM 1422 N ILE A 182 -19.531 10.820 20.466 1.00 52.87 N ANISOU 1422 N ILE A 182 6433 5276 8380 -298 704 -218 N ATOM 1423 CA ILE A 182 -20.103 11.902 21.261 1.00 52.53 C ANISOU 1423 CA ILE A 182 6311 5250 8397 -294 758 -213 C ATOM 1424 C ILE A 182 -18.976 12.819 21.749 1.00 52.26 C ANISOU 1424 C ILE A 182 6363 5298 8194 -243 789 -153 C ATOM 1425 O ILE A 182 -19.067 14.044 21.618 1.00 53.34 O ANISOU 1425 O ILE A 182 6472 5475 8322 -216 737 -157 O ATOM 1426 CB ILE A 182 -20.927 11.347 22.450 1.00 53.01 C ANISOU 1426 CB ILE A 182 6303 5248 8590 -341 920 -211 C ATOM 1427 CG1 ILE A 182 -22.151 10.535 21.980 1.00 53.81 C ANISOU 1427 CG1 ILE A 182 6290 5259 8898 -399 892 -280 C ATOM 1428 CG2 ILE A 182 -21.354 12.476 23.399 1.00 53.50 C ANISOU 1428 CG2 ILE A 182 6308 5332 8688 -328 1002 -199 C ATOM 1429 CD1 ILE A 182 -22.881 9.743 23.141 1.00 54.61 C ANISOU 1429 CD1 ILE A 182 6338 5279 9131 -458 1084 -274 C ATOM 1430 N TYR A 183 -17.898 12.217 22.260 1.00 50.76 N ANISOU 1430 N TYR A 183 6277 5130 7880 -228 862 -103 N ATOM 1431 CA TYR A 183 -16.740 12.949 22.763 1.00 50.04 C ANISOU 1431 CA TYR A 183 6264 5110 7640 -181 886 -53 C ATOM 1432 C TYR A 183 -16.024 13.743 21.646 1.00 49.10 C ANISOU 1432 C TYR A 183 6181 5045 7431 -147 762 -59 C ATOM 1433 O TYR A 183 -15.774 14.932 21.819 1.00 47.91 O ANISOU 1433 O TYR A 183 6026 4940 7240 -121 747 -46 O ATOM 1434 CB TYR A 183 -15.771 11.989 23.487 1.00 49.80 C ANISOU 1434 CB TYR A 183 6333 5079 7512 -168 972 -7 C ATOM 1435 CG TYR A 183 -14.469 12.638 23.903 1.00 50.37 C ANISOU 1435 CG TYR A 183 6480 5219 7440 -117 974 34 C ATOM 1436 CD1 TYR A 183 -14.455 13.718 24.772 1.00 51.49 C ANISOU 1436 CD1 TYR A 183 6610 5394 7559 -98 1012 49 C ATOM 1437 CD2 TYR A 183 -13.256 12.171 23.427 1.00 50.82 C ANISOU 1437 CD2 TYR A 183 6613 5303 7395 -88 936 50 C ATOM 1438 CE1 TYR A 183 -13.264 14.322 25.152 1.00 52.39 C ANISOU 1438 CE1 TYR A 183 6785 5565 7555 -54 1002 78 C ATOM 1439 CE2 TYR A 183 -12.060 12.752 23.816 1.00 52.05 C ANISOU 1439 CE2 TYR A 183 6819 5515 7443 -44 935 79 C ATOM 1440 CZ TYR A 183 -12.068 13.847 24.660 1.00 53.35 C ANISOU 1440 CZ TYR A 183 6969 5712 7591 -28 961 91 C ATOM 1441 OH TYR A 183 -10.893 14.468 25.023 1.00 55.20 O ANISOU 1441 OH TYR A 183 7243 5997 7731 13 947 110 O ATOM 1442 N SER A 184 -15.712 13.075 20.513 1.00 49.05 N ANISOU 1442 N SER A 184 6218 5026 7393 -147 682 -78 N ATOM 1443 CA SER A 184 -15.028 13.658 19.353 1.00 48.82 C ANISOU 1443 CA SER A 184 6245 5033 7271 -116 580 -82 C ATOM 1444 C SER A 184 -15.831 14.806 18.712 1.00 49.56 C ANISOU 1444 C SER A 184 6286 5127 7417 -110 482 -112 C ATOM 1445 O SER A 184 -15.245 15.816 18.317 1.00 49.86 O ANISOU 1445 O SER A 184 6365 5207 7373 -79 443 -96 O ATOM 1446 CB SER A 184 -14.699 12.573 18.337 1.00 48.53 C ANISOU 1446 CB SER A 184 6272 4968 7200 -120 530 -102 C ATOM 1447 OG SER A 184 -14.144 13.082 17.144 1.00 49.53 O ANISOU 1447 OG SER A 184 6466 5117 7236 -92 441 -110 O ATOM 1448 N LEU A 185 -17.164 14.674 18.641 1.00 49.61 N ANISOU 1448 N LEU A 185 6198 5082 7568 -137 444 -158 N ATOM 1449 CA LEU A 185 -18.032 15.727 18.099 1.00 49.93 C ANISOU 1449 CA LEU A 185 6178 5114 7678 -125 341 -192 C ATOM 1450 C LEU A 185 -18.105 16.918 19.053 1.00 50.30 C ANISOU 1450 C LEU A 185 6179 5195 7737 -110 404 -167 C ATOM 1451 O LEU A 185 -18.078 18.054 18.592 1.00 50.19 O ANISOU 1451 O LEU A 185 6176 5203 7692 -79 331 -167 O ATOM 1452 CB LEU A 185 -19.438 15.201 17.761 1.00 49.69 C ANISOU 1452 CB LEU A 185 6044 5013 7824 -156 274 -259 C ATOM 1453 CG LEU A 185 -19.499 14.296 16.527 1.00 51.20 C ANISOU 1453 CG LEU A 185 6287 5164 8003 -162 160 -300 C ATOM 1454 CD1 LEU A 185 -20.834 13.574 16.454 1.00 51.61 C ANISOU 1454 CD1 LEU A 185 6220 5139 8252 -204 118 -369 C ATOM 1455 CD2 LEU A 185 -19.217 15.091 15.236 1.00 51.63 C ANISOU 1455 CD2 LEU A 185 6429 5234 7954 -114 10 -310 C ATOM 1456 N CYS A 186 -18.137 16.668 20.376 1.00 50.66 N ANISOU 1456 N CYS A 186 6191 5243 7814 -128 542 -144 N ATOM 1457 CA CYS A 186 -18.144 17.761 21.365 1.00 51.63 C ANISOU 1457 CA CYS A 186 6287 5397 7934 -111 611 -122 C ATOM 1458 C CYS A 186 -16.831 18.507 21.393 1.00 50.93 C ANISOU 1458 C CYS A 186 6290 5370 7689 -76 609 -79 C ATOM 1459 O CYS A 186 -16.815 19.716 21.594 1.00 50.80 O ANISOU 1459 O CYS A 186 6262 5378 7662 -54 596 -73 O ATOM 1460 CB CYS A 186 -18.517 17.261 22.754 1.00 53.58 C ANISOU 1460 CB CYS A 186 6500 5621 8237 -136 763 -109 C ATOM 1461 SG CYS A 186 -20.210 16.654 22.877 1.00 60.31 S ANISOU 1461 SG CYS A 186 7212 6390 9315 -184 796 -166 S ATOM 1462 N LEU A 187 -15.736 17.779 21.209 1.00 50.57 N ANISOU 1462 N LEU A 187 6331 5346 7537 -71 625 -52 N ATOM 1463 CA LEU A 187 -14.384 18.300 21.138 1.00 50.45 C ANISOU 1463 CA LEU A 187 6395 5384 7391 -42 625 -17 C ATOM 1464 C LEU A 187 -14.159 19.045 19.817 1.00 50.50 C ANISOU 1464 C LEU A 187 6437 5399 7353 -25 518 -26 C ATOM 1465 O LEU A 187 -13.452 20.030 19.810 1.00 51.09 O ANISOU 1465 O LEU A 187 6542 5507 7362 -5 516 -6 O ATOM 1466 CB LEU A 187 -13.410 17.146 21.312 1.00 50.70 C ANISOU 1466 CB LEU A 187 6492 5422 7349 -41 674 5 C ATOM 1467 CG LEU A 187 -11.961 17.474 21.579 1.00 52.70 C ANISOU 1467 CG LEU A 187 6807 5724 7491 -12 698 37 C ATOM 1468 CD1 LEU A 187 -11.805 18.460 22.728 1.00 53.13 C ANISOU 1468 CD1 LEU A 187 6844 5806 7535 2 745 52 C ATOM 1469 CD2 LEU A 187 -11.206 16.201 21.875 1.00 53.47 C ANISOU 1469 CD2 LEU A 187 6955 5816 7546 -7 745 53 C ATOM 1470 N THR A 188 -14.791 18.627 18.719 1.00 50.41 N ANISOU 1470 N THR A 188 6427 5350 7378 -32 430 -58 N ATOM 1471 CA THR A 188 -14.724 19.349 17.441 1.00 50.79 C ANISOU 1471 CA THR A 188 6528 5393 7376 -9 322 -67 C ATOM 1472 C THR A 188 -15.458 20.679 17.595 1.00 51.62 C ANISOU 1472 C THR A 188 6579 5495 7539 6 280 -75 C ATOM 1473 O THR A 188 -14.977 21.701 17.119 1.00 52.16 O ANISOU 1473 O THR A 188 6703 5578 7538 30 247 -56 O ATOM 1474 CB THR A 188 -15.394 18.543 16.310 1.00 51.58 C ANISOU 1474 CB THR A 188 6646 5444 7507 -16 221 -108 C ATOM 1475 OG1 THR A 188 -14.729 17.301 16.194 1.00 52.90 O ANISOU 1475 OG1 THR A 188 6865 5610 7624 -28 266 -103 O ATOM 1476 CG2 THR A 188 -15.360 19.270 14.957 1.00 51.28 C ANISOU 1476 CG2 THR A 188 6693 5391 7399 16 103 -116 C ATOM 1477 N LEU A 189 -16.625 20.665 18.265 1.00 51.55 N ANISOU 1477 N LEU A 189 6462 5460 7664 -9 291 -103 N ATOM 1478 CA LEU A 189 -17.420 21.852 18.501 1.00 52.02 C ANISOU 1478 CA LEU A 189 6454 5510 7801 9 258 -118 C ATOM 1479 C LEU A 189 -16.719 22.824 19.462 1.00 52.14 C ANISOU 1479 C LEU A 189 6482 5568 7760 21 344 -81 C ATOM 1480 O LEU A 189 -16.422 23.946 19.071 1.00 52.74 O ANISOU 1480 O LEU A 189 6596 5654 7788 46 298 -68 O ATOM 1481 CB LEU A 189 -18.813 21.459 19.022 1.00 52.73 C ANISOU 1481 CB LEU A 189 6413 5555 8065 -13 269 -163 C ATOM 1482 CG LEU A 189 -19.746 22.614 19.347 1.00 55.30 C ANISOU 1482 CG LEU A 189 6650 5864 8499 7 243 -187 C ATOM 1483 CD1 LEU A 189 -20.027 23.457 18.113 1.00 55.98 C ANISOU 1483 CD1 LEU A 189 6769 5930 8571 47 82 -204 C ATOM 1484 CD2 LEU A 189 -21.045 22.108 19.968 1.00 56.42 C ANISOU 1484 CD2 LEU A 189 6650 5957 8828 -20 285 -235 C ATOM 1485 N LEU A 190 -16.411 22.391 20.690 1.00 51.46 N ANISOU 1485 N LEU A 190 6378 5502 7671 4 464 -64 N ATOM 1486 CA LEU A 190 -15.807 23.226 21.717 1.00 51.34 C ANISOU 1486 CA LEU A 190 6376 5522 7608 17 540 -39 C ATOM 1487 C LEU A 190 -14.328 23.563 21.466 1.00 50.24 C ANISOU 1487 C LEU A 190 6328 5425 7336 30 539 -4 C ATOM 1488 O LEU A 190 -13.899 24.684 21.740 1.00 50.38 O ANISOU 1488 O LEU A 190 6359 5461 7321 46 544 7 O ATOM 1489 CB LEU A 190 -16.009 22.520 23.079 1.00 52.52 C ANISOU 1489 CB LEU A 190 6496 5669 7789 0 661 -35 C ATOM 1490 CG LEU A 190 -15.633 23.279 24.358 1.00 54.74 C ANISOU 1490 CG LEU A 190 6791 5974 8033 16 744 -19 C ATOM 1491 CD1 LEU A 190 -16.385 24.571 24.481 1.00 55.45 C ANISOU 1491 CD1 LEU A 190 6823 6052 8194 31 724 -41 C ATOM 1492 CD2 LEU A 190 -15.870 22.426 25.564 1.00 55.31 C ANISOU 1492 CD2 LEU A 190 6865 6032 8118 3 861 -13 C ATOM 1493 N GLY A 191 -13.566 22.603 20.953 1.00 48.64 N ANISOU 1493 N GLY A 191 6181 5231 7069 23 539 8 N ATOM 1494 CA GLY A 191 -12.147 22.793 20.716 1.00 47.91 C ANISOU 1494 CA GLY A 191 6160 5173 6873 32 551 35 C ATOM 1495 C GLY A 191 -11.771 23.429 19.398 1.00 47.99 C ANISOU 1495 C GLY A 191 6227 5175 6831 42 483 40 C ATOM 1496 O GLY A 191 -10.783 24.166 19.328 1.00 47.40 O ANISOU 1496 O GLY A 191 6190 5121 6698 49 502 59 O ATOM 1497 N PHE A 192 -12.544 23.160 18.336 1.00 48.16 N ANISOU 1497 N PHE A 192 6262 5161 6874 43 403 21 N ATOM 1498 CA PHE A 192 -12.234 23.716 17.020 1.00 48.18 C ANISOU 1498 CA PHE A 192 6349 5146 6810 58 338 29 C ATOM 1499 C PHE A 192 -13.262 24.753 16.482 1.00 48.32 C ANISOU 1499 C PHE A 192 6359 5128 6871 79 242 15 C ATOM 1500 O PHE A 192 -12.887 25.897 16.244 1.00 48.35 O ANISOU 1500 O PHE A 192 6405 5130 6835 93 235 35 O ATOM 1501 CB PHE A 192 -12.017 22.566 16.007 1.00 47.48 C ANISOU 1501 CB PHE A 192 6328 5040 6671 55 309 20 C ATOM 1502 CG PHE A 192 -11.867 22.956 14.551 1.00 47.39 C ANISOU 1502 CG PHE A 192 6429 4998 6580 75 237 23 C ATOM 1503 CD1 PHE A 192 -11.077 24.038 14.180 1.00 48.12 C ANISOU 1503 CD1 PHE A 192 6589 5094 6602 86 261 54 C ATOM 1504 CD2 PHE A 192 -12.441 22.190 13.550 1.00 47.59 C ANISOU 1504 CD2 PHE A 192 6504 4984 6594 82 153 -5 C ATOM 1505 CE1 PHE A 192 -10.941 24.399 12.843 1.00 48.26 C ANISOU 1505 CE1 PHE A 192 6731 5072 6532 106 209 62 C ATOM 1506 CE2 PHE A 192 -12.264 22.521 12.215 1.00 48.15 C ANISOU 1506 CE2 PHE A 192 6705 5021 6570 106 89 -1 C ATOM 1507 CZ PHE A 192 -11.522 23.634 11.869 1.00 48.00 C ANISOU 1507 CZ PHE A 192 6762 5002 6473 119 123 36 C ATOM 1508 N LEU A 193 -14.510 24.340 16.226 1.00 47.90 N ANISOU 1508 N LEU A 193 6255 5041 6904 81 164 -22 N ATOM 1509 CA LEU A 193 -15.512 25.177 15.584 1.00 48.10 C ANISOU 1509 CA LEU A 193 6274 5024 6979 109 49 -43 C ATOM 1510 C LEU A 193 -15.894 26.443 16.355 1.00 49.40 C ANISOU 1510 C LEU A 193 6374 5191 7203 123 66 -39 C ATOM 1511 O LEU A 193 -16.112 27.484 15.720 1.00 49.96 O ANISOU 1511 O LEU A 193 6491 5235 7257 155 -11 -33 O ATOM 1512 CB LEU A 193 -16.767 24.361 15.228 1.00 47.31 C ANISOU 1512 CB LEU A 193 6109 4883 6985 107 -42 -95 C ATOM 1513 CG LEU A 193 -16.592 23.265 14.162 1.00 47.40 C ANISOU 1513 CG LEU A 193 6201 4873 6937 104 -101 -110 C ATOM 1514 CD1 LEU A 193 -17.879 22.562 13.911 1.00 47.20 C ANISOU 1514 CD1 LEU A 193 6094 4800 7039 99 -199 -170 C ATOM 1515 CD2 LEU A 193 -16.081 23.841 12.839 1.00 48.00 C ANISOU 1515 CD2 LEU A 193 6431 4927 6879 138 -179 -91 C ATOM 1516 N ILE A 194 -15.994 26.367 17.699 1.00 49.25 N ANISOU 1516 N ILE A 194 6264 5200 7248 104 164 -42 N ATOM 1517 CA ILE A 194 -16.353 27.533 18.525 1.00 48.88 C ANISOU 1517 CA ILE A 194 6160 5154 7258 118 191 -44 C ATOM 1518 C ILE A 194 -15.199 28.551 18.515 1.00 49.21 C ANISOU 1518 C ILE A 194 6282 5217 7197 126 224 -5 C ATOM 1519 O ILE A 194 -15.459 29.662 18.064 1.00 49.77 O ANISOU 1519 O ILE A 194 6378 5260 7272 152 164 -2 O ATOM 1520 CB ILE A 194 -16.897 27.194 19.952 1.00 48.10 C ANISOU 1520 CB ILE A 194 5957 5067 7253 100 291 -62 C ATOM 1521 CG1 ILE A 194 -18.306 26.572 19.853 1.00 48.06 C ANISOU 1521 CG1 ILE A 194 5850 5019 7391 95 249 -109 C ATOM 1522 CG2 ILE A 194 -16.936 28.453 20.837 1.00 48.26 C ANISOU 1522 CG2 ILE A 194 5950 5094 7294 117 336 -59 C ATOM 1523 CD1 ILE A 194 -18.913 26.067 21.166 1.00 48.37 C ANISOU 1523 CD1 ILE A 194 5793 5056 7528 71 367 -127 C ATOM 1524 N PRO A 195 -13.917 28.212 18.852 1.00 48.97 N ANISOU 1524 N PRO A 195 6298 5226 7080 106 306 22 N ATOM 1525 CA PRO A 195 -12.840 29.221 18.716 1.00 49.07 C ANISOU 1525 CA PRO A 195 6378 5249 7019 108 331 52 C ATOM 1526 C PRO A 195 -12.693 29.788 17.296 1.00 49.50 C ANISOU 1526 C PRO A 195 6532 5266 7012 125 259 70 C ATOM 1527 O PRO A 195 -12.457 30.978 17.170 1.00 50.69 O ANISOU 1527 O PRO A 195 6717 5396 7145 135 254 86 O ATOM 1528 CB PRO A 195 -11.577 28.461 19.176 1.00 48.78 C ANISOU 1528 CB PRO A 195 6358 5254 6920 85 415 67 C ATOM 1529 CG PRO A 195 -12.086 27.423 20.075 1.00 48.81 C ANISOU 1529 CG PRO A 195 6297 5274 6974 76 451 49 C ATOM 1530 CD PRO A 195 -13.372 26.960 19.418 1.00 47.65 C ANISOU 1530 CD PRO A 195 6122 5091 6891 82 379 25 C ATOM 1531 N LEU A 196 -12.880 28.970 16.237 1.00 48.78 N ANISOU 1531 N LEU A 196 6495 5155 6884 129 201 66 N ATOM 1532 CA LEU A 196 -12.805 29.438 14.851 1.00 48.76 C ANISOU 1532 CA LEU A 196 6613 5107 6806 152 130 84 C ATOM 1533 C LEU A 196 -13.907 30.464 14.539 1.00 48.91 C ANISOU 1533 C LEU A 196 6629 5078 6878 190 24 73 C ATOM 1534 O LEU A 196 -13.643 31.467 13.862 1.00 49.81 O ANISOU 1534 O LEU A 196 6839 5154 6932 210 -2 100 O ATOM 1535 CB LEU A 196 -12.855 28.268 13.856 1.00 48.91 C ANISOU 1535 CB LEU A 196 6698 5112 6773 154 84 73 C ATOM 1536 CG LEU A 196 -12.617 28.631 12.374 1.00 50.40 C ANISOU 1536 CG LEU A 196 7049 5252 6851 180 23 94 C ATOM 1537 CD1 LEU A 196 -11.203 29.131 12.136 1.00 50.92 C ANISOU 1537 CD1 LEU A 196 7203 5323 6822 163 133 137 C ATOM 1538 CD2 LEU A 196 -12.901 27.455 11.464 1.00 50.68 C ANISOU 1538 CD2 LEU A 196 7146 5267 6844 188 -43 71 C ATOM 1539 N SER A 197 -15.125 30.237 15.063 1.00 47.79 N ANISOU 1539 N SER A 197 6373 4930 6854 200 -28 32 N ATOM 1540 CA SER A 197 -16.268 31.136 14.900 1.00 46.65 C ANISOU 1540 CA SER A 197 6194 4740 6791 241 -132 11 C ATOM 1541 C SER A 197 -16.064 32.423 15.653 1.00 46.71 C ANISOU 1541 C SER A 197 6178 4749 6820 247 -78 27 C ATOM 1542 O SER A 197 -16.508 33.459 15.186 1.00 47.08 O ANISOU 1542 O SER A 197 6263 4748 6876 286 -155 31 O ATOM 1543 CB SER A 197 -17.535 30.482 15.412 1.00 47.17 C ANISOU 1543 CB SER A 197 6119 4800 7003 242 -172 -42 C ATOM 1544 OG SER A 197 -17.767 29.320 14.647 1.00 51.00 O ANISOU 1544 OG SER A 197 6628 5274 7476 236 -235 -63 O ATOM 1545 N VAL A 198 -15.431 32.369 16.840 1.00 46.33 N ANISOU 1545 N VAL A 198 6072 4750 6782 214 45 32 N ATOM 1546 CA VAL A 198 -15.151 33.549 17.644 1.00 45.82 C ANISOU 1546 CA VAL A 198 5988 4688 6734 216 100 41 C ATOM 1547 C VAL A 198 -14.132 34.418 16.896 1.00 47.15 C ANISOU 1547 C VAL A 198 6282 4834 6800 216 106 84 C ATOM 1548 O VAL A 198 -14.350 35.612 16.797 1.00 48.40 O ANISOU 1548 O VAL A 198 6466 4952 6973 241 74 92 O ATOM 1549 CB VAL A 198 -14.739 33.205 19.102 1.00 44.87 C ANISOU 1549 CB VAL A 198 5789 4620 6638 186 216 30 C ATOM 1550 CG1 VAL A 198 -14.138 34.418 19.819 1.00 45.30 C ANISOU 1550 CG1 VAL A 198 5853 4676 6682 185 269 39 C ATOM 1551 CG2 VAL A 198 -15.914 32.638 19.886 1.00 43.77 C ANISOU 1551 CG2 VAL A 198 5534 4483 6612 190 225 -10 C ATOM 1552 N MET A 199 -13.111 33.828 16.260 1.00 47.51 N ANISOU 1552 N MET A 199 6410 4894 6749 192 144 111 N ATOM 1553 CA MET A 199 -12.167 34.599 15.444 1.00 48.67 C ANISOU 1553 CA MET A 199 6680 5008 6805 188 167 151 C ATOM 1554 C MET A 199 -12.859 35.238 14.227 1.00 49.98 C ANISOU 1554 C MET A 199 6952 5102 6937 233 55 166 C ATOM 1555 O MET A 199 -12.565 36.376 13.896 1.00 51.06 O ANISOU 1555 O MET A 199 7165 5192 7042 244 60 195 O ATOM 1556 CB MET A 199 -10.971 33.746 15.013 1.00 49.17 C ANISOU 1556 CB MET A 199 6801 5097 6785 155 243 171 C ATOM 1557 CG MET A 199 -9.982 33.519 16.127 1.00 51.50 C ANISOU 1557 CG MET A 199 7020 5447 7101 116 349 164 C ATOM 1558 SD MET A 199 -8.481 32.677 15.566 1.00 59.07 S ANISOU 1558 SD MET A 199 8037 6426 7980 83 441 184 S ATOM 1559 CE MET A 199 -9.119 31.024 15.278 1.00 53.13 C ANISOU 1559 CE MET A 199 7271 5697 7217 94 394 164 C ATOM 1560 N CYS A 200 -13.798 34.532 13.599 1.00 50.05 N ANISOU 1560 N CYS A 200 6966 5095 6957 263 -50 144 N ATOM 1561 CA CYS A 200 -14.588 35.016 12.468 1.00 50.62 C ANISOU 1561 CA CYS A 200 7138 5095 7001 318 -187 149 C ATOM 1562 C CYS A 200 -15.462 36.193 12.885 1.00 51.39 C ANISOU 1562 C CYS A 200 7180 5155 7190 357 -250 136 C ATOM 1563 O CYS A 200 -15.660 37.113 12.094 1.00 51.84 O ANISOU 1563 O CYS A 200 7350 5144 7202 399 -325 160 O ATOM 1564 CB CYS A 200 -15.453 33.889 11.911 1.00 51.49 C ANISOU 1564 CB CYS A 200 7231 5201 7131 338 -297 111 C ATOM 1565 SG CYS A 200 -14.547 32.681 10.924 1.00 56.79 S ANISOU 1565 SG CYS A 200 8032 5882 7663 315 -263 128 S ATOM 1566 N PHE A 201 -16.051 36.119 14.098 1.00 51.30 N ANISOU 1566 N PHE A 201 7003 5181 7306 347 -223 97 N ATOM 1567 CA PHE A 201 -16.910 37.145 14.661 1.00 51.50 C ANISOU 1567 CA PHE A 201 6954 5176 7437 383 -264 76 C ATOM 1568 C PHE A 201 -16.081 38.397 14.930 1.00 52.25 C ANISOU 1568 C PHE A 201 7113 5253 7487 374 -190 113 C ATOM 1569 O PHE A 201 -16.521 39.502 14.607 1.00 52.66 O ANISOU 1569 O PHE A 201 7210 5242 7556 418 -257 121 O ATOM 1570 CB PHE A 201 -17.596 36.640 15.945 1.00 51.62 C ANISOU 1570 CB PHE A 201 6790 5237 7588 367 -216 26 C ATOM 1571 CG PHE A 201 -18.394 37.701 16.671 1.00 52.61 C ANISOU 1571 CG PHE A 201 6830 5333 7827 401 -228 -1 C ATOM 1572 CD1 PHE A 201 -19.593 38.161 16.159 1.00 53.69 C ANISOU 1572 CD1 PHE A 201 6938 5409 8052 462 -363 -29 C ATOM 1573 CD2 PHE A 201 -17.924 38.265 17.843 1.00 53.52 C ANISOU 1573 CD2 PHE A 201 6898 5476 7959 377 -111 -1 C ATOM 1574 CE1 PHE A 201 -20.308 39.163 16.804 1.00 54.27 C ANISOU 1574 CE1 PHE A 201 6933 5451 8236 498 -370 -55 C ATOM 1575 CE2 PHE A 201 -18.633 39.279 18.476 1.00 54.59 C ANISOU 1575 CE2 PHE A 201 6969 5580 8193 411 -117 -27 C ATOM 1576 CZ PHE A 201 -19.820 39.720 17.953 1.00 54.34 C ANISOU 1576 CZ PHE A 201 6904 5489 8255 472 -241 -54 C ATOM 1577 N PHE A 202 -14.871 38.236 15.491 1.00 52.31 N ANISOU 1577 N PHE A 202 7124 5308 7444 318 -58 132 N ATOM 1578 CA PHE A 202 -14.020 39.385 15.780 1.00 53.05 C ANISOU 1578 CA PHE A 202 7267 5381 7510 300 15 160 C ATOM 1579 C PHE A 202 -13.388 39.963 14.523 1.00 55.74 C ANISOU 1579 C PHE A 202 7779 5658 7742 307 3 212 C ATOM 1580 O PHE A 202 -13.144 41.161 14.491 1.00 55.78 O ANISOU 1580 O PHE A 202 7839 5612 7743 313 19 234 O ATOM 1581 CB PHE A 202 -13.002 39.089 16.879 1.00 51.97 C ANISOU 1581 CB PHE A 202 7062 5309 7376 244 143 151 C ATOM 1582 CG PHE A 202 -13.655 39.248 18.225 1.00 51.62 C ANISOU 1582 CG PHE A 202 6888 5292 7433 252 161 107 C ATOM 1583 CD1 PHE A 202 -13.866 40.503 18.766 1.00 51.86 C ANISOU 1583 CD1 PHE A 202 6905 5286 7512 269 165 98 C ATOM 1584 CD2 PHE A 202 -14.164 38.154 18.897 1.00 52.18 C ANISOU 1584 CD2 PHE A 202 6860 5415 7551 245 176 75 C ATOM 1585 CE1 PHE A 202 -14.528 40.655 19.975 1.00 52.29 C ANISOU 1585 CE1 PHE A 202 6852 5360 7654 281 189 54 C ATOM 1586 CE2 PHE A 202 -14.827 38.310 20.107 1.00 52.68 C ANISOU 1586 CE2 PHE A 202 6820 5494 7703 255 208 36 C ATOM 1587 CZ PHE A 202 -15.003 39.560 20.638 1.00 52.09 C ANISOU 1587 CZ PHE A 202 6736 5386 7670 274 215 24 C ATOM 1588 N TYR A 203 -13.223 39.166 13.441 1.00 57.83 N ANISOU 1588 N TYR A 203 8140 5915 7917 310 -28 232 N ATOM 1589 CA TYR A 203 -12.754 39.722 12.168 1.00 60.22 C ANISOU 1589 CA TYR A 203 8632 6144 8104 326 -40 283 C ATOM 1590 C TYR A 203 -13.850 40.673 11.649 1.00 61.01 C ANISOU 1590 C TYR A 203 8792 6164 8224 398 -178 287 C ATOM 1591 O TYR A 203 -13.560 41.789 11.247 1.00 61.30 O ANISOU 1591 O TYR A 203 8942 6131 8219 411 -167 326 O ATOM 1592 CB TYR A 203 -12.462 38.617 11.146 1.00 61.87 C ANISOU 1592 CB TYR A 203 8939 6358 8210 323 -51 296 C ATOM 1593 CG TYR A 203 -12.359 39.152 9.734 1.00 65.48 C ANISOU 1593 CG TYR A 203 9614 6725 8540 360 -95 344 C ATOM 1594 CD1 TYR A 203 -11.230 39.842 9.311 1.00 67.55 C ANISOU 1594 CD1 TYR A 203 10001 6942 8721 328 27 396 C ATOM 1595 CD2 TYR A 203 -13.424 39.043 8.847 1.00 67.74 C ANISOU 1595 CD2 TYR A 203 9985 6960 8793 430 -262 335 C ATOM 1596 CE1 TYR A 203 -11.144 40.367 8.027 1.00 69.41 C ANISOU 1596 CE1 TYR A 203 10458 7084 8830 364 0 446 C ATOM 1597 CE2 TYR A 203 -13.354 39.572 7.562 1.00 69.32 C ANISOU 1597 CE2 TYR A 203 10410 7068 8861 473 -312 381 C ATOM 1598 CZ TYR A 203 -12.202 40.213 7.148 1.00 71.02 C ANISOU 1598 CZ TYR A 203 10765 7239 8980 440 -172 440 C ATOM 1599 OH TYR A 203 -12.138 40.777 5.890 1.00 73.80 O ANISOU 1599 OH TYR A 203 11362 7490 9191 484 -206 492 O ATOM 1600 N TYR A 204 -15.108 40.227 11.706 1.00 61.47 N ANISOU 1600 N TYR A 204 8767 6228 8359 444 -308 242 N ATOM 1601 CA TYR A 204 -16.278 40.984 11.303 1.00 62.26 C ANISOU 1601 CA TYR A 204 8891 6258 8509 521 -460 230 C ATOM 1602 C TYR A 204 -16.416 42.284 12.127 1.00 62.05 C ANISOU 1602 C TYR A 204 8806 6205 8565 531 -428 229 C ATOM 1603 O TYR A 204 -16.745 43.315 11.556 1.00 61.92 O ANISOU 1603 O TYR A 204 8893 6104 8529 584 -504 254 O ATOM 1604 CB TYR A 204 -17.534 40.088 11.414 1.00 63.29 C ANISOU 1604 CB TYR A 204 8891 6411 8744 555 -584 167 C ATOM 1605 CG TYR A 204 -18.830 40.865 11.440 1.00 65.59 C ANISOU 1605 CG TYR A 204 9126 6644 9151 630 -727 134 C ATOM 1606 CD1 TYR A 204 -19.338 41.446 10.286 1.00 66.95 C ANISOU 1606 CD1 TYR A 204 9445 6725 9268 707 -885 151 C ATOM 1607 CD2 TYR A 204 -19.499 41.096 12.634 1.00 67.36 C ANISOU 1607 CD2 TYR A 204 9160 6897 9537 629 -699 86 C ATOM 1608 CE1 TYR A 204 -20.508 42.193 10.310 1.00 68.38 C ANISOU 1608 CE1 TYR A 204 9569 6847 9565 783 -1025 118 C ATOM 1609 CE2 TYR A 204 -20.660 41.857 12.674 1.00 68.84 C ANISOU 1609 CE2 TYR A 204 9286 7025 9843 701 -819 51 C ATOM 1610 CZ TYR A 204 -21.162 42.405 11.509 1.00 70.16 C ANISOU 1610 CZ TYR A 204 9587 7104 9967 779 -988 66 C ATOM 1611 OH TYR A 204 -22.315 43.163 11.547 1.00 73.16 O ANISOU 1611 OH TYR A 204 9899 7422 10478 858 -1119 28 O ATOM 1612 N LYS A 205 -16.197 42.226 13.465 1.00 61.62 N ANISOU 1612 N LYS A 205 8596 6216 8600 485 -321 199 N ATOM 1613 CA LYS A 205 -16.275 43.394 14.353 1.00 61.00 C ANISOU 1613 CA LYS A 205 8461 6117 8599 490 -279 190 C ATOM 1614 C LYS A 205 -15.182 44.408 13.994 1.00 61.47 C ANISOU 1614 C LYS A 205 8662 6124 8571 464 -202 245 C ATOM 1615 O LYS A 205 -15.411 45.620 14.043 1.00 61.62 O ANISOU 1615 O LYS A 205 8719 6075 8619 496 -226 256 O ATOM 1616 CB LYS A 205 -16.142 42.981 15.828 1.00 62.06 C ANISOU 1616 CB LYS A 205 8428 6333 8819 444 -174 146 C ATOM 1617 CG LYS A 205 -17.319 42.183 16.394 1.00 65.37 C ANISOU 1617 CG LYS A 205 8694 6790 9354 467 -222 88 C ATOM 1618 CD LYS A 205 -18.625 42.970 16.404 1.00 69.39 C ANISOU 1618 CD LYS A 205 9150 7238 9978 540 -331 55 C ATOM 1619 CE LYS A 205 -18.702 43.985 17.525 1.00 72.76 C ANISOU 1619 CE LYS A 205 9510 7654 10482 544 -263 33 C ATOM 1620 NZ LYS A 205 -19.513 45.174 17.142 1.00 74.42 N ANISOU 1620 NZ LYS A 205 9750 7775 10750 619 -369 30 N ATOM 1621 N MET A 206 -13.988 43.911 13.633 1.00 61.85 N ANISOU 1621 N MET A 206 8783 6197 8520 406 -104 280 N ATOM 1622 CA MET A 206 -12.866 44.733 13.198 1.00 62.30 C ANISOU 1622 CA MET A 206 8971 6199 8501 371 -11 332 C ATOM 1623 C MET A 206 -13.216 45.443 11.889 1.00 63.51 C ANISOU 1623 C MET A 206 9316 6245 8571 429 -98 381 C ATOM 1624 O MET A 206 -12.995 46.639 11.786 1.00 63.91 O ANISOU 1624 O MET A 206 9447 6219 8618 435 -75 411 O ATOM 1625 CB MET A 206 -11.618 43.883 12.993 1.00 62.28 C ANISOU 1625 CB MET A 206 8994 6245 8426 303 107 350 C ATOM 1626 CG MET A 206 -10.907 43.499 14.253 1.00 64.74 C ANISOU 1626 CG MET A 206 9155 6638 8803 243 211 313 C ATOM 1627 SD MET A 206 -9.553 42.338 13.838 1.00 68.09 S ANISOU 1627 SD MET A 206 9607 7114 9150 179 326 330 S ATOM 1628 CE MET A 206 -8.448 42.737 15.063 1.00 65.20 C ANISOU 1628 CE MET A 206 9134 6783 8856 115 443 305 C ATOM 1629 N VAL A 207 -13.773 44.723 10.901 1.00 64.19 N ANISOU 1629 N VAL A 207 9484 6318 8587 474 -204 388 N ATOM 1630 CA VAL A 207 -14.167 45.301 9.617 1.00 65.49 C ANISOU 1630 CA VAL A 207 9853 6377 8655 541 -309 433 C ATOM 1631 C VAL A 207 -15.235 46.404 9.801 1.00 67.00 C ANISOU 1631 C VAL A 207 10027 6499 8930 616 -432 420 C ATOM 1632 O VAL A 207 -15.144 47.463 9.180 1.00 67.77 O ANISOU 1632 O VAL A 207 10285 6495 8969 649 -450 469 O ATOM 1633 CB VAL A 207 -14.603 44.192 8.627 1.00 66.16 C ANISOU 1633 CB VAL A 207 10014 6468 8656 578 -416 428 C ATOM 1634 CG1 VAL A 207 -15.412 44.758 7.465 1.00 66.71 C ANISOU 1634 CG1 VAL A 207 10267 6429 8651 674 -586 453 C ATOM 1635 CG2 VAL A 207 -13.391 43.425 8.113 1.00 66.70 C ANISOU 1635 CG2 VAL A 207 10176 6562 8603 516 -281 461 C ATOM 1636 N VAL A 208 -16.217 46.169 10.671 1.00 67.29 N ANISOU 1636 N VAL A 208 9872 6587 9110 641 -505 355 N ATOM 1637 CA VAL A 208 -17.276 47.130 10.954 1.00 67.92 C ANISOU 1637 CA VAL A 208 9902 6608 9296 714 -615 330 C ATOM 1638 C VAL A 208 -16.684 48.390 11.604 1.00 69.93 C ANISOU 1638 C VAL A 208 10167 6825 9578 685 -506 352 C ATOM 1639 O VAL A 208 -17.033 49.500 11.205 1.00 70.75 O ANISOU 1639 O VAL A 208 10374 6829 9679 743 -573 378 O ATOM 1640 CB VAL A 208 -18.405 46.477 11.794 1.00 67.77 C ANISOU 1640 CB VAL A 208 9658 6656 9437 736 -684 250 C ATOM 1641 CG1 VAL A 208 -19.291 47.515 12.469 1.00 68.33 C ANISOU 1641 CG1 VAL A 208 9634 6683 9646 791 -736 215 C ATOM 1642 CG2 VAL A 208 -19.240 45.551 10.936 1.00 67.89 C ANISOU 1642 CG2 VAL A 208 9684 6667 9442 787 -841 226 C ATOM 1643 N PHE A 209 -15.760 48.223 12.564 1.00 70.55 N ANISOU 1643 N PHE A 209 10151 6974 9681 599 -347 340 N ATOM 1644 CA PHE A 209 -15.113 49.348 13.239 1.00 71.18 C ANISOU 1644 CA PHE A 209 10232 7020 9794 563 -243 350 C ATOM 1645 C PHE A 209 -14.339 50.227 12.246 1.00 73.47 C ANISOU 1645 C PHE A 209 10737 7204 9973 556 -202 426 C ATOM 1646 O PHE A 209 -14.437 51.452 12.312 1.00 73.70 O ANISOU 1646 O PHE A 209 10824 7147 10031 580 -208 442 O ATOM 1647 CB PHE A 209 -14.181 48.841 14.348 1.00 69.97 C ANISOU 1647 CB PHE A 209 9949 6962 9674 474 -97 320 C ATOM 1648 CG PHE A 209 -13.497 49.934 15.122 1.00 69.33 C ANISOU 1648 CG PHE A 209 9854 6849 9638 433 0 317 C ATOM 1649 CD1 PHE A 209 -14.129 50.549 16.182 1.00 69.36 C ANISOU 1649 CD1 PHE A 209 9745 6855 9753 459 -18 265 C ATOM 1650 CD2 PHE A 209 -12.214 50.346 14.789 1.00 69.54 C ANISOU 1650 CD2 PHE A 209 9981 6839 9604 368 113 359 C ATOM 1651 CE1 PHE A 209 -13.506 51.571 16.880 1.00 69.86 C ANISOU 1651 CE1 PHE A 209 9806 6883 9856 424 61 256 C ATOM 1652 CE2 PHE A 209 -11.587 51.360 15.498 1.00 69.72 C ANISOU 1652 CE2 PHE A 209 9984 6825 9682 327 193 348 C ATOM 1653 CZ PHE A 209 -12.232 51.960 16.545 1.00 69.52 C ANISOU 1653 CZ PHE A 209 9854 6802 9756 356 161 296 C ATOM 1654 N LEU A 210 -13.588 49.601 11.326 1.00 75.12 N ANISOU 1654 N LEU A 210 11072 7413 10059 523 -153 471 N ATOM 1655 CA LEU A 210 -12.797 50.305 10.321 1.00 77.50 C ANISOU 1655 CA LEU A 210 11593 7611 10244 509 -87 547 C ATOM 1656 C LEU A 210 -13.657 50.983 9.241 1.00 80.59 C ANISOU 1656 C LEU A 210 12171 7883 10566 609 -234 589 C ATOM 1657 O LEU A 210 -13.257 52.012 8.696 1.00 80.87 O ANISOU 1657 O LEU A 210 12378 7807 10543 614 -191 647 O ATOM 1658 CB LEU A 210 -11.750 49.374 9.709 1.00 77.40 C ANISOU 1658 CB LEU A 210 11651 7633 10124 447 25 576 C ATOM 1659 CG LEU A 210 -10.675 48.912 10.683 1.00 78.70 C ANISOU 1659 CG LEU A 210 11661 7890 10353 348 180 544 C ATOM 1660 CD1 LEU A 210 -9.820 47.808 10.086 1.00 79.25 C ANISOU 1660 CD1 LEU A 210 11777 8003 10332 301 268 562 C ATOM 1661 CD2 LEU A 210 -9.822 50.067 11.132 1.00 79.14 C ANISOU 1661 CD2 LEU A 210 11724 7888 10460 292 301 559 C ATOM 1662 N LYS A 211 -14.846 50.433 8.958 1.00 82.63 N ANISOU 1662 N LYS A 211 12397 8160 10840 691 -411 556 N ATOM 1663 CA LYS A 211 -15.779 51.033 8.004 1.00 85.05 C ANISOU 1663 CA LYS A 211 12864 8356 11097 800 -586 583 C ATOM 1664 C LYS A 211 -16.345 52.342 8.581 1.00 87.53 C ANISOU 1664 C LYS A 211 13135 8601 11522 847 -632 572 C ATOM 1665 O LYS A 211 -16.505 53.319 7.852 1.00 88.12 O ANISOU 1665 O LYS A 211 13397 8551 11535 907 -692 623 O ATOM 1666 CB LYS A 211 -16.921 50.054 7.677 1.00 87.13 C ANISOU 1666 CB LYS A 211 13061 8661 11383 871 -773 533 C ATOM 1667 CG LYS A 211 -16.580 49.057 6.572 1.00 91.79 C ANISOU 1667 CG LYS A 211 13805 9255 11815 870 -792 562 C ATOM 1668 CD LYS A 211 -17.736 48.091 6.317 1.00 96.74 C ANISOU 1668 CD LYS A 211 14351 9920 12487 937 -989 500 C ATOM 1669 CE LYS A 211 -17.418 47.033 5.286 1.00100.97 C ANISOU 1669 CE LYS A 211 15026 10466 12870 933 -1011 517 C ATOM 1670 NZ LYS A 211 -18.238 45.797 5.482 1.00103.36 N ANISOU 1670 NZ LYS A 211 15159 10852 13262 946 -1126 439 N ATOM 1671 N LYS A 212 -16.624 52.360 9.892 1.00 88.94 N ANISOU 1671 N LYS A 212 13080 8855 11857 820 -597 505 N ATOM 1672 CA LYS A 212 -17.135 53.508 10.632 1.00 90.96 C ANISOU 1672 CA LYS A 212 13266 9062 12234 857 -621 480 C ATOM 1673 C LYS A 212 -16.051 54.614 10.687 1.00 92.70 C ANISOU 1673 C LYS A 212 13605 9204 12412 799 -474 534 C ATOM 1674 O LYS A 212 -16.343 55.794 10.457 1.00 92.74 O ANISOU 1674 O LYS A 212 13715 9094 12427 852 -520 561 O ATOM 1675 CB LYS A 212 -17.522 53.038 12.047 1.00 93.41 C ANISOU 1675 CB LYS A 212 13308 9484 12700 828 -585 394 C ATOM 1676 CG LYS A 212 -18.113 54.099 12.968 1.00 98.66 C ANISOU 1676 CG LYS A 212 13874 10110 13502 866 -598 353 C ATOM 1677 CD LYS A 212 -18.375 53.530 14.367 1.00104.06 C ANISOU 1677 CD LYS A 212 14317 10906 14313 829 -533 272 C ATOM 1678 CE LYS A 212 -17.097 53.149 15.083 1.00108.71 C ANISOU 1678 CE LYS A 212 14867 11574 14866 716 -356 273 C ATOM 1679 NZ LYS A 212 -17.370 52.420 16.352 1.00111.75 N ANISOU 1679 NZ LYS A 212 15046 12064 15350 688 -302 200 N ATOM 1680 N ARG A 213 -14.792 54.219 10.952 1.00 93.78 N ANISOU 1680 N ARG A 213 13728 9397 12508 690 -300 548 N ATOM 1681 CA ARG A 213 -13.665 55.151 11.026 1.00 95.18 C ANISOU 1681 CA ARG A 213 13994 9505 12665 618 -147 590 C ATOM 1682 C ARG A 213 -13.266 55.725 9.646 1.00 96.21 C ANISOU 1682 C ARG A 213 14404 9501 12651 637 -132 683 C ATOM 1683 O ARG A 213 -12.622 56.779 9.587 1.00 96.54 O ANISOU 1683 O ARG A 213 14546 9445 12689 602 -33 723 O ATOM 1684 CB ARG A 213 -12.454 54.509 11.746 1.00 96.76 C ANISOU 1684 CB ARG A 213 14075 9804 12886 500 23 565 C ATOM 1685 CG ARG A 213 -12.708 54.134 13.211 1.00100.32 C ANISOU 1685 CG ARG A 213 14282 10368 13468 477 30 479 C ATOM 1686 CD ARG A 213 -12.966 55.328 14.106 1.00104.35 C ANISOU 1686 CD ARG A 213 14734 10827 14086 490 32 446 C ATOM 1687 NE ARG A 213 -13.958 55.022 15.141 1.00107.93 N ANISOU 1687 NE ARG A 213 15004 11357 14647 534 -40 369 N ATOM 1688 CZ ARG A 213 -13.766 55.207 16.445 1.00110.40 C ANISOU 1688 CZ ARG A 213 15175 11720 15051 497 24 308 C ATOM 1689 NH1 ARG A 213 -12.615 55.697 16.893 1.00109.83 N ANISOU 1689 NH1 ARG A 213 15111 11634 14985 416 143 307 N ATOM 1690 NH2 ARG A 213 -14.726 54.907 17.311 1.00110.43 N ANISOU 1690 NH2 ARG A 213 15031 11784 15144 542 -30 242 N ATOM 1691 N SER A 214 -13.662 55.048 8.542 1.00 96.42 N ANISOU 1691 N SER A 214 14564 9513 12556 694 -230 716 N ATOM 1692 CA SER A 214 -13.366 55.480 7.175 1.00 96.94 C ANISOU 1692 CA SER A 214 14924 9450 12460 725 -224 806 C ATOM 1693 C SER A 214 -14.439 56.432 6.640 1.00 97.52 C ANISOU 1693 C SER A 214 15136 9396 12519 847 -399 832 C ATOM 1694 O SER A 214 -14.863 57.361 7.331 1.00 97.76 O ANISOU 1694 O SER A 214 15086 9391 12668 873 -432 806 O ATOM 1695 CB SER A 214 -13.245 54.272 6.251 1.00 98.00 C ANISOU 1695 CB SER A 214 15152 9625 12457 732 -248 825 C ATOM 1696 N ASN A 224 -5.029 46.225 6.510 1.00 81.13 N ANISOU 1696 N ASN A 224 12533 8113 10179 87 912 736 N ATOM 1697 CA ASN A 224 -4.575 46.662 7.832 1.00 81.49 C ANISOU 1697 CA ASN A 224 12362 8209 10392 28 960 690 C ATOM 1698 C ASN A 224 -3.948 45.507 8.626 1.00 80.53 C ANISOU 1698 C ASN A 224 12038 8211 10348 -21 1009 630 C ATOM 1699 O ASN A 224 -4.305 44.348 8.411 1.00 80.47 O ANISOU 1699 O ASN A 224 12017 8271 10287 9 947 613 O ATOM 1700 CB ASN A 224 -5.728 47.299 8.617 1.00 83.87 C ANISOU 1700 CB ASN A 224 12580 8523 10766 81 797 662 C ATOM 1701 CG ASN A 224 -6.416 48.408 7.868 1.00 89.06 C ANISOU 1701 CG ASN A 224 13430 9056 11352 142 726 716 C ATOM 1702 OD1 ASN A 224 -6.010 49.584 7.928 1.00 90.84 O ANISOU 1702 OD1 ASN A 224 13712 9191 11611 114 802 745 O ATOM 1703 ND2 ASN A 224 -7.471 48.055 7.137 1.00 90.28 N ANISOU 1703 ND2 ASN A 224 13694 9199 11411 229 571 729 N ATOM 1704 N LYS A 225 -3.018 45.831 9.548 1.00 79.60 N ANISOU 1704 N LYS A 225 11768 8117 10360 -93 1110 596 N ATOM 1705 CA LYS A 225 -2.325 44.847 10.394 1.00 79.17 C ANISOU 1705 CA LYS A 225 11521 8171 10390 -137 1153 538 C ATOM 1706 C LYS A 225 -3.248 44.014 11.294 1.00 78.53 C ANISOU 1706 C LYS A 225 11299 8201 10337 -92 1005 487 C ATOM 1707 O LYS A 225 -3.046 42.793 11.372 1.00 78.53 O ANISOU 1707 O LYS A 225 11236 8278 10323 -94 1008 463 O ATOM 1708 CB LYS A 225 -1.204 45.496 11.243 1.00 80.93 C ANISOU 1708 CB LYS A 225 11612 8384 10755 -214 1263 504 C ATOM 1709 CG LYS A 225 -0.189 46.332 10.443 1.00 85.13 C ANISOU 1709 CG LYS A 225 12258 8798 11291 -273 1436 548 C ATOM 1710 CD LYS A 225 0.856 47.002 11.350 1.00 89.32 C ANISOU 1710 CD LYS A 225 12637 9313 11986 -352 1524 503 C ATOM 1711 CE LYS A 225 1.801 47.908 10.594 1.00 93.76 C ANISOU 1711 CE LYS A 225 13302 9748 12575 -418 1706 543 C ATOM 1712 NZ LYS A 225 2.370 48.994 11.451 1.00 96.63 N ANISOU 1712 NZ LYS A 225 13560 10063 13093 -478 1742 506 N ATOM 1713 N PRO A 226 -4.254 44.613 11.988 1.00 77.62 N ANISOU 1713 N PRO A 226 11133 8093 10266 -52 884 468 N ATOM 1714 CA PRO A 226 -5.118 43.790 12.851 1.00 76.75 C ANISOU 1714 CA PRO A 226 10889 8081 10190 -15 769 419 C ATOM 1715 C PRO A 226 -5.879 42.750 12.051 1.00 75.82 C ANISOU 1715 C PRO A 226 10842 7988 9979 35 688 432 C ATOM 1716 O PRO A 226 -6.029 41.621 12.498 1.00 76.43 O ANISOU 1716 O PRO A 226 10819 8149 10070 38 659 398 O ATOM 1717 CB PRO A 226 -6.070 44.803 13.495 1.00 77.77 C ANISOU 1717 CB PRO A 226 10987 8185 10378 21 675 404 C ATOM 1718 CG PRO A 226 -5.480 46.135 13.254 1.00 78.62 C ANISOU 1718 CG PRO A 226 11173 8194 10504 -10 751 434 C ATOM 1719 CD PRO A 226 -4.663 46.035 12.018 1.00 77.08 C ANISOU 1719 CD PRO A 226 11127 7937 10223 -38 857 488 C ATOM 1720 N LEU A 227 -6.310 43.109 10.846 1.00 74.29 N ANISOU 1720 N LEU A 227 10829 7712 9686 75 651 481 N ATOM 1721 CA LEU A 227 -7.021 42.193 9.972 1.00 73.06 C ANISOU 1721 CA LEU A 227 10762 7565 9434 126 560 490 C ATOM 1722 C LEU A 227 -6.108 41.089 9.460 1.00 72.14 C ANISOU 1722 C LEU A 227 10673 7480 9256 92 660 494 C ATOM 1723 O LEU A 227 -6.557 39.965 9.305 1.00 72.33 O ANISOU 1723 O LEU A 227 10676 7557 9249 116 594 472 O ATOM 1724 CB LEU A 227 -7.643 42.973 8.805 1.00 73.12 C ANISOU 1724 CB LEU A 227 10978 7462 9340 184 488 541 C ATOM 1725 CG LEU A 227 -9.124 43.354 8.949 1.00 74.63 C ANISOU 1725 CG LEU A 227 11153 7640 9565 261 303 524 C ATOM 1726 CD1 LEU A 227 -9.392 44.091 10.226 1.00 75.14 C ANISOU 1726 CD1 LEU A 227 11053 7730 9765 249 293 489 C ATOM 1727 CD2 LEU A 227 -9.562 44.239 7.825 1.00 75.52 C ANISOU 1727 CD2 LEU A 227 11483 7633 9578 320 235 577 C ATOM 1728 N ARG A 228 -4.823 41.391 9.237 1.00 71.22 N ANISOU 1728 N ARG A 228 10594 7330 9135 33 823 517 N ATOM 1729 CA ARG A 228 -3.837 40.444 8.721 1.00 70.64 C ANISOU 1729 CA ARG A 228 10548 7276 9016 -1 942 520 C ATOM 1730 C ARG A 228 -3.674 39.212 9.610 1.00 68.42 C ANISOU 1730 C ARG A 228 10084 7108 8803 -16 928 464 C ATOM 1731 O ARG A 228 -3.781 38.098 9.105 1.00 68.53 O ANISOU 1731 O ARG A 228 10135 7152 8753 3 911 458 O ATOM 1732 CB ARG A 228 -2.483 41.151 8.467 1.00 73.48 C ANISOU 1732 CB ARG A 228 10947 7570 9400 -67 1132 546 C ATOM 1733 CG ARG A 228 -1.677 40.590 7.294 1.00 78.97 C ANISOU 1733 CG ARG A 228 11788 8223 9995 -83 1266 578 C ATOM 1734 CD ARG A 228 -0.548 41.521 6.865 1.00 84.54 C ANISOU 1734 CD ARG A 228 12566 8833 10721 -143 1457 613 C ATOM 1735 NE ARG A 228 -1.044 42.708 6.153 1.00 89.41 N ANISOU 1735 NE ARG A 228 13377 9336 11258 -117 1441 673 N ATOM 1736 CZ ARG A 228 -0.733 43.965 6.472 1.00 91.80 C ANISOU 1736 CZ ARG A 228 13670 9572 11639 -155 1499 689 C ATOM 1737 NH1 ARG A 228 -1.235 44.977 5.777 1.00 91.57 N ANISOU 1737 NH1 ARG A 228 13834 9433 11525 -123 1478 747 N ATOM 1738 NH2 ARG A 228 0.080 44.216 7.491 1.00 91.61 N ANISOU 1738 NH2 ARG A 228 13447 9585 11777 -221 1572 644 N ATOM 1739 N LEU A 229 -3.442 39.411 10.922 1.00 66.36 N ANISOU 1739 N LEU A 229 9643 6904 8668 -45 931 424 N ATOM 1740 CA LEU A 229 -3.257 38.338 11.903 1.00 65.10 C ANISOU 1740 CA LEU A 229 9316 6843 8573 -57 918 374 C ATOM 1741 C LEU A 229 -4.501 37.423 12.007 1.00 63.84 C ANISOU 1741 C LEU A 229 9136 6736 8386 -5 781 355 C ATOM 1742 O LEU A 229 -4.360 36.202 11.993 1.00 63.58 O ANISOU 1742 O LEU A 229 9067 6754 8336 -4 785 337 O ATOM 1743 CB LEU A 229 -2.903 38.929 13.294 1.00 65.08 C ANISOU 1743 CB LEU A 229 9157 6875 8694 -87 927 336 C ATOM 1744 CG LEU A 229 -2.526 37.927 14.394 1.00 66.69 C ANISOU 1744 CG LEU A 229 9204 7171 8964 -98 923 286 C ATOM 1745 CD1 LEU A 229 -1.503 38.516 15.324 1.00 67.11 C ANISOU 1745 CD1 LEU A 229 9150 7230 9120 -143 985 254 C ATOM 1746 CD2 LEU A 229 -3.760 37.464 15.201 1.00 67.57 C ANISOU 1746 CD2 LEU A 229 9247 7341 9087 -56 801 260 C ATOM 1747 N VAL A 230 -5.699 38.022 12.143 1.00 62.64 N ANISOU 1747 N VAL A 230 8995 6565 8242 36 665 356 N ATOM 1748 CA VAL A 230 -6.950 37.295 12.297 1.00 62.03 C ANISOU 1748 CA VAL A 230 8877 6524 8168 82 537 331 C ATOM 1749 C VAL A 230 -7.271 36.492 11.057 1.00 61.62 C ANISOU 1749 C VAL A 230 8954 6449 8012 111 493 347 C ATOM 1750 O VAL A 230 -7.637 35.328 11.177 1.00 61.80 O ANISOU 1750 O VAL A 230 8923 6520 8037 120 450 320 O ATOM 1751 CB VAL A 230 -8.129 38.198 12.725 1.00 62.29 C ANISOU 1751 CB VAL A 230 8879 6533 8254 120 431 322 C ATOM 1752 CG1 VAL A 230 -9.317 37.350 13.161 1.00 62.46 C ANISOU 1752 CG1 VAL A 230 8808 6603 8322 154 324 283 C ATOM 1753 CG2 VAL A 230 -7.711 39.126 13.854 1.00 62.97 C ANISOU 1753 CG2 VAL A 230 8868 6628 8428 91 484 307 C ATOM 1754 N VAL A 231 -7.087 37.084 9.863 1.00 60.81 N ANISOU 1754 N VAL A 231 9030 6264 7811 126 509 392 N ATOM 1755 CA VAL A 231 -7.339 36.393 8.593 1.00 60.12 C ANISOU 1755 CA VAL A 231 9100 6142 7603 160 466 407 C ATOM 1756 C VAL A 231 -6.372 35.215 8.428 1.00 58.98 C ANISOU 1756 C VAL A 231 8943 6041 7428 125 573 396 C ATOM 1757 O VAL A 231 -6.805 34.127 8.075 1.00 59.36 O ANISOU 1757 O VAL A 231 9005 6113 7438 147 509 375 O ATOM 1758 CB VAL A 231 -7.305 37.361 7.383 1.00 60.80 C ANISOU 1758 CB VAL A 231 9406 6120 7575 186 471 461 C ATOM 1759 CG1 VAL A 231 -7.376 36.602 6.069 1.00 61.16 C ANISOU 1759 CG1 VAL A 231 9637 6125 7474 219 449 477 C ATOM 1760 CG2 VAL A 231 -8.441 38.364 7.465 1.00 61.38 C ANISOU 1760 CG2 VAL A 231 9498 6148 7676 238 329 466 C ATOM 1761 N LEU A 232 -5.090 35.403 8.761 1.00 57.72 N ANISOU 1761 N LEU A 232 8739 5891 7303 71 728 405 N ATOM 1762 CA LEU A 232 -4.108 34.331 8.678 1.00 57.30 C ANISOU 1762 CA LEU A 232 8656 5876 7241 41 835 390 C ATOM 1763 C LEU A 232 -4.471 33.207 9.665 1.00 57.05 C ANISOU 1763 C LEU A 232 8458 5934 7283 43 772 342 C ATOM 1764 O LEU A 232 -4.381 32.033 9.315 1.00 57.38 O ANISOU 1764 O LEU A 232 8516 6000 7286 51 775 326 O ATOM 1765 CB LEU A 232 -2.678 34.851 8.924 1.00 57.68 C ANISOU 1765 CB LEU A 232 8661 5911 7344 -16 1005 399 C ATOM 1766 CG LEU A 232 -1.583 33.796 8.719 1.00 60.18 C ANISOU 1766 CG LEU A 232 8948 6256 7661 -42 1124 382 C ATOM 1767 CD1 LEU A 232 -1.512 33.349 7.273 1.00 60.79 C ANISOU 1767 CD1 LEU A 232 9223 6277 7597 -19 1167 409 C ATOM 1768 CD2 LEU A 232 -0.234 34.264 9.217 1.00 60.95 C ANISOU 1768 CD2 LEU A 232 8948 6351 7860 -99 1271 374 C ATOM 1769 N ALA A 233 -4.939 33.558 10.872 1.00 56.07 N ANISOU 1769 N ALA A 233 8190 5854 7261 40 716 319 N ATOM 1770 CA ALA A 233 -5.333 32.562 11.852 1.00 55.23 C ANISOU 1770 CA ALA A 233 7944 5823 7220 42 667 279 C ATOM 1771 C ALA A 233 -6.537 31.767 11.339 1.00 54.94 C ANISOU 1771 C ALA A 233 7948 5784 7143 82 547 266 C ATOM 1772 O ALA A 233 -6.475 30.549 11.321 1.00 55.40 O ANISOU 1772 O ALA A 233 7981 5875 7192 81 548 246 O ATOM 1773 CB ALA A 233 -5.632 33.221 13.188 1.00 55.06 C ANISOU 1773 CB ALA A 233 7789 5834 7299 34 642 259 C ATOM 1774 N VAL A 234 -7.585 32.438 10.841 1.00 54.36 N ANISOU 1774 N VAL A 234 7944 5663 7048 118 440 275 N ATOM 1775 CA VAL A 234 -8.772 31.769 10.314 1.00 54.30 C ANISOU 1775 CA VAL A 234 7967 5643 7020 158 307 254 C ATOM 1776 C VAL A 234 -8.414 30.844 9.144 1.00 54.43 C ANISOU 1776 C VAL A 234 8117 5636 6925 167 318 259 C ATOM 1777 O VAL A 234 -8.868 29.704 9.132 1.00 54.82 O ANISOU 1777 O VAL A 234 8130 5711 6986 173 265 226 O ATOM 1778 CB VAL A 234 -9.915 32.763 9.977 1.00 54.95 C ANISOU 1778 CB VAL A 234 8097 5671 7111 203 179 259 C ATOM 1779 CG1 VAL A 234 -11.032 32.087 9.197 1.00 55.28 C ANISOU 1779 CG1 VAL A 234 8192 5686 7128 248 30 233 C ATOM 1780 CG2 VAL A 234 -10.470 33.409 11.243 1.00 55.49 C ANISOU 1780 CG2 VAL A 234 8010 5769 7305 199 160 239 C ATOM 1781 N VAL A 235 -7.547 31.295 8.217 1.00 53.80 N ANISOU 1781 N VAL A 235 8191 5508 6745 163 403 297 N ATOM 1782 CA VAL A 235 -7.090 30.493 7.072 1.00 53.63 C ANISOU 1782 CA VAL A 235 8317 5456 6604 172 439 302 C ATOM 1783 C VAL A 235 -6.243 29.268 7.512 1.00 54.05 C ANISOU 1783 C VAL A 235 8278 5569 6689 139 538 278 C ATOM 1784 O VAL A 235 -6.498 28.137 7.077 1.00 54.36 O ANISOU 1784 O VAL A 235 8350 5615 6689 154 495 252 O ATOM 1785 CB VAL A 235 -6.341 31.368 6.012 1.00 53.81 C ANISOU 1785 CB VAL A 235 8534 5400 6510 174 535 353 C ATOM 1786 CG1 VAL A 235 -5.677 30.506 4.946 1.00 53.96 C ANISOU 1786 CG1 VAL A 235 8701 5392 6409 179 612 357 C ATOM 1787 CG2 VAL A 235 -7.280 32.380 5.364 1.00 53.78 C ANISOU 1787 CG2 VAL A 235 8663 5324 6447 223 412 378 C ATOM 1788 N ILE A 236 -5.243 29.482 8.375 1.00 53.85 N ANISOU 1788 N ILE A 236 8139 5584 6739 97 661 282 N ATOM 1789 CA ILE A 236 -4.378 28.389 8.834 1.00 54.01 C ANISOU 1789 CA ILE A 236 8070 5656 6797 73 748 259 C ATOM 1790 C ILE A 236 -5.190 27.287 9.527 1.00 53.96 C ANISOU 1790 C ILE A 236 7956 5701 6847 84 653 221 C ATOM 1791 O ILE A 236 -5.076 26.128 9.146 1.00 54.14 O ANISOU 1791 O ILE A 236 8006 5730 6835 90 658 202 O ATOM 1792 CB ILE A 236 -3.178 28.905 9.694 1.00 54.63 C ANISOU 1792 CB ILE A 236 8034 5762 6961 32 873 263 C ATOM 1793 CG1 ILE A 236 -2.143 29.645 8.813 1.00 54.88 C ANISOU 1793 CG1 ILE A 236 8178 5733 6942 13 1007 295 C ATOM 1794 CG2 ILE A 236 -2.503 27.749 10.469 1.00 55.54 C ANISOU 1794 CG2 ILE A 236 8024 5938 7140 20 920 231 C ATOM 1795 CD1 ILE A 236 -0.972 30.181 9.539 1.00 55.85 C ANISOU 1795 CD1 ILE A 236 8186 5870 7162 -29 1121 291 C ATOM 1796 N PHE A 237 -6.060 27.657 10.485 1.00 53.45 N ANISOU 1796 N PHE A 237 7779 5664 6867 86 572 209 N ATOM 1797 CA PHE A 237 -6.866 26.682 11.210 1.00 53.04 C ANISOU 1797 CA PHE A 237 7623 5651 6879 90 502 176 C ATOM 1798 C PHE A 237 -7.967 26.075 10.355 1.00 52.55 C ANISOU 1798 C PHE A 237 7634 5555 6778 118 382 156 C ATOM 1799 O PHE A 237 -8.192 24.883 10.470 1.00 53.36 O ANISOU 1799 O PHE A 237 7702 5675 6899 116 364 129 O ATOM 1800 CB PHE A 237 -7.403 27.266 12.530 1.00 53.00 C ANISOU 1800 CB PHE A 237 7481 5680 6977 82 475 167 C ATOM 1801 CG PHE A 237 -6.299 27.487 13.546 1.00 53.56 C ANISOU 1801 CG PHE A 237 7466 5792 7093 56 577 171 C ATOM 1802 CD1 PHE A 237 -5.654 26.415 14.141 1.00 54.35 C ANISOU 1802 CD1 PHE A 237 7503 5932 7214 46 630 156 C ATOM 1803 CD2 PHE A 237 -5.875 28.760 13.868 1.00 54.06 C ANISOU 1803 CD2 PHE A 237 7516 5845 7177 45 613 187 C ATOM 1804 CE1 PHE A 237 -4.622 26.623 15.043 1.00 54.81 C ANISOU 1804 CE1 PHE A 237 7487 6023 7316 30 702 154 C ATOM 1805 CE2 PHE A 237 -4.835 28.962 14.766 1.00 54.63 C ANISOU 1805 CE2 PHE A 237 7508 5950 7297 22 690 182 C ATOM 1806 CZ PHE A 237 -4.224 27.898 15.352 1.00 54.42 C ANISOU 1806 CZ PHE A 237 7420 5965 7293 18 728 164 C ATOM 1807 N SER A 238 -8.615 26.845 9.466 1.00 51.79 N ANISOU 1807 N SER A 238 7646 5404 6628 147 296 166 N ATOM 1808 CA SER A 238 -9.643 26.280 8.576 1.00 51.90 C ANISOU 1808 CA SER A 238 7738 5378 6605 181 161 139 C ATOM 1809 C SER A 238 -9.028 25.230 7.653 1.00 52.12 C ANISOU 1809 C SER A 238 7882 5389 6531 184 200 132 C ATOM 1810 O SER A 238 -9.609 24.181 7.465 1.00 52.66 O ANISOU 1810 O SER A 238 7942 5454 6611 191 126 94 O ATOM 1811 CB SER A 238 -10.277 27.354 7.698 1.00 52.81 C ANISOU 1811 CB SER A 238 7977 5429 6661 222 59 155 C ATOM 1812 OG SER A 238 -10.995 28.303 8.455 1.00 55.78 O ANISOU 1812 OG SER A 238 8249 5809 7134 228 6 155 O ATOM 1813 N VAL A 239 -7.872 25.520 7.066 1.00 51.83 N ANISOU 1813 N VAL A 239 7956 5335 6402 177 320 165 N ATOM 1814 CA VAL A 239 -7.221 24.601 6.148 1.00 51.94 C ANISOU 1814 CA VAL A 239 8092 5326 6314 183 376 158 C ATOM 1815 C VAL A 239 -6.587 23.393 6.854 1.00 52.13 C ANISOU 1815 C VAL A 239 8002 5405 6401 156 459 135 C ATOM 1816 O VAL A 239 -6.824 22.261 6.440 1.00 52.41 O ANISOU 1816 O VAL A 239 8073 5431 6408 167 420 103 O ATOM 1817 CB VAL A 239 -6.218 25.347 5.234 1.00 51.93 C ANISOU 1817 CB VAL A 239 8255 5277 6198 186 495 201 C ATOM 1818 CG1 VAL A 239 -5.418 24.370 4.384 1.00 52.12 C ANISOU 1818 CG1 VAL A 239 8394 5281 6128 190 589 191 C ATOM 1819 CG2 VAL A 239 -6.949 26.354 4.352 1.00 51.63 C ANISOU 1819 CG2 VAL A 239 8378 5170 6071 226 393 223 C ATOM 1820 N LEU A 240 -5.822 23.616 7.932 1.00 51.67 N ANISOU 1820 N LEU A 240 7807 5397 6428 126 560 147 N ATOM 1821 CA LEU A 240 -5.097 22.531 8.595 1.00 51.09 C ANISOU 1821 CA LEU A 240 7637 5368 6406 109 637 129 C ATOM 1822 C LEU A 240 -5.934 21.675 9.561 1.00 51.37 C ANISOU 1822 C LEU A 240 7545 5440 6534 104 560 100 C ATOM 1823 O LEU A 240 -5.703 20.457 9.623 1.00 52.22 O ANISOU 1823 O LEU A 240 7637 5556 6646 103 581 78 O ATOM 1824 CB LEU A 240 -3.815 23.060 9.293 1.00 50.41 C ANISOU 1824 CB LEU A 240 7470 5314 6371 84 771 149 C ATOM 1825 CG LEU A 240 -2.830 23.838 8.386 1.00 50.67 C ANISOU 1825 CG LEU A 240 7615 5304 6335 79 884 176 C ATOM 1826 CD1 LEU A 240 -1.606 24.324 9.156 1.00 50.79 C ANISOU 1826 CD1 LEU A 240 7519 5346 6432 50 1004 183 C ATOM 1827 CD2 LEU A 240 -2.435 23.037 7.157 1.00 50.80 C ANISOU 1827 CD2 LEU A 240 7779 5278 6246 96 936 169 C ATOM 1828 N PHE A 241 -6.899 22.260 10.286 1.00 50.65 N ANISOU 1828 N PHE A 241 7368 5362 6516 100 481 98 N ATOM 1829 CA PHE A 241 -7.706 21.468 11.232 1.00 50.41 C ANISOU 1829 CA PHE A 241 7219 5357 6578 91 431 72 C ATOM 1830 C PHE A 241 -8.944 20.784 10.633 1.00 51.31 C ANISOU 1830 C PHE A 241 7363 5433 6699 103 309 37 C ATOM 1831 O PHE A 241 -9.450 19.840 11.236 1.00 51.91 O ANISOU 1831 O PHE A 241 7357 5518 6846 90 291 12 O ATOM 1832 CB PHE A 241 -8.137 22.296 12.451 1.00 49.28 C ANISOU 1832 CB PHE A 241 6955 5244 6524 81 424 81 C ATOM 1833 CG PHE A 241 -7.120 22.529 13.545 1.00 49.35 C ANISOU 1833 CG PHE A 241 6885 5299 6567 66 524 97 C ATOM 1834 CD1 PHE A 241 -5.758 22.457 13.280 1.00 49.81 C ANISOU 1834 CD1 PHE A 241 6978 5365 6582 63 617 110 C ATOM 1835 CD2 PHE A 241 -7.524 22.906 14.820 1.00 49.54 C ANISOU 1835 CD2 PHE A 241 6803 5352 6669 59 522 95 C ATOM 1836 CE1 PHE A 241 -4.823 22.713 14.279 1.00 50.29 C ANISOU 1836 CE1 PHE A 241 6959 5463 6687 54 689 116 C ATOM 1837 CE2 PHE A 241 -6.588 23.176 15.813 1.00 50.15 C ANISOU 1837 CE2 PHE A 241 6820 5465 6768 52 595 105 C ATOM 1838 CZ PHE A 241 -5.245 23.075 15.538 1.00 50.18 C ANISOU 1838 CZ PHE A 241 6850 5477 6738 50 669 113 C ATOM 1839 N THR A 242 -9.485 21.285 9.511 1.00 51.25 N ANISOU 1839 N THR A 242 7468 5378 6627 127 218 32 N ATOM 1840 CA THR A 242 -10.722 20.730 8.947 1.00 51.23 C ANISOU 1840 CA THR A 242 7486 5335 6646 142 76 -11 C ATOM 1841 C THR A 242 -10.570 19.287 8.440 1.00 52.09 C ANISOU 1841 C THR A 242 7644 5425 6722 139 74 -44 C ATOM 1842 O THR A 242 -11.399 18.469 8.839 1.00 52.50 O ANISOU 1842 O THR A 242 7609 5470 6866 124 15 -81 O ATOM 1843 CB THR A 242 -11.326 21.670 7.890 1.00 51.31 C ANISOU 1843 CB THR A 242 7615 5291 6589 179 -40 -10 C ATOM 1844 OG1 THR A 242 -11.553 22.936 8.490 1.00 50.95 O ANISOU 1844 OG1 THR A 242 7504 5259 6596 181 -41 15 O ATOM 1845 CG2 THR A 242 -12.625 21.150 7.303 1.00 51.89 C ANISOU 1845 CG2 THR A 242 7701 5317 6698 200 -211 -65 C ATOM 1846 N PRO A 243 -9.566 18.914 7.596 1.00 52.57 N ANISOU 1846 N PRO A 243 7838 5471 6663 150 143 -34 N ATOM 1847 CA PRO A 243 -9.490 17.511 7.140 1.00 52.38 C ANISOU 1847 CA PRO A 243 7861 5426 6614 150 137 -71 C ATOM 1848 C PRO A 243 -9.351 16.521 8.290 1.00 52.09 C ANISOU 1848 C PRO A 243 7682 5426 6683 120 200 -80 C ATOM 1849 O PRO A 243 -9.990 15.472 8.260 1.00 52.48 O ANISOU 1849 O PRO A 243 7709 5451 6780 111 141 -120 O ATOM 1850 CB PRO A 243 -8.261 17.490 6.228 1.00 53.32 C ANISOU 1850 CB PRO A 243 8130 5530 6597 168 242 -51 C ATOM 1851 CG PRO A 243 -8.023 18.923 5.850 1.00 54.03 C ANISOU 1851 CG PRO A 243 8293 5612 6625 181 259 -10 C ATOM 1852 CD PRO A 243 -8.475 19.726 7.013 1.00 52.44 C ANISOU 1852 CD PRO A 243 7935 5451 6539 162 240 7 C ATOM 1853 N TYR A 244 -8.549 16.875 9.319 1.00 51.19 N ANISOU 1853 N TYR A 244 7478 5365 6608 105 314 -43 N ATOM 1854 CA TYR A 244 -8.337 16.056 10.508 1.00 50.30 C ANISOU 1854 CA TYR A 244 7246 5284 6580 85 376 -43 C ATOM 1855 C TYR A 244 -9.632 15.860 11.303 1.00 49.63 C ANISOU 1855 C TYR A 244 7049 5194 6612 64 304 -63 C ATOM 1856 O TYR A 244 -9.915 14.746 11.730 1.00 49.21 O ANISOU 1856 O TYR A 244 6952 5130 6616 49 311 -83 O ATOM 1857 CB TYR A 244 -7.218 16.650 11.390 1.00 50.06 C ANISOU 1857 CB TYR A 244 7156 5305 6559 82 489 -4 C ATOM 1858 CG TYR A 244 -7.168 16.064 12.780 1.00 51.16 C ANISOU 1858 CG TYR A 244 7178 5475 6783 69 532 1 C ATOM 1859 CD1 TYR A 244 -6.745 14.756 12.991 1.00 52.18 C ANISOU 1859 CD1 TYR A 244 7307 5598 6921 71 573 -10 C ATOM 1860 CD2 TYR A 244 -7.619 16.787 13.878 1.00 52.06 C ANISOU 1860 CD2 TYR A 244 7197 5617 6966 58 528 16 C ATOM 1861 CE1 TYR A 244 -6.743 14.195 14.264 1.00 53.03 C ANISOU 1861 CE1 TYR A 244 7330 5724 7094 65 609 -1 C ATOM 1862 CE2 TYR A 244 -7.662 16.221 15.147 1.00 52.75 C ANISOU 1862 CE2 TYR A 244 7203 5724 7116 50 567 21 C ATOM 1863 CZ TYR A 244 -7.189 14.938 15.343 1.00 53.71 C ANISOU 1863 CZ TYR A 244 7334 5837 7236 54 608 15 C ATOM 1864 OH TYR A 244 -7.173 14.402 16.607 1.00 55.17 O ANISOU 1864 OH TYR A 244 7460 6033 7468 53 648 27 O ATOM 1865 N HIS A 245 -10.381 16.946 11.551 1.00 49.30 N ANISOU 1865 N HIS A 245 6959 5158 6615 63 249 -57 N ATOM 1866 CA HIS A 245 -11.611 16.850 12.323 1.00 48.99 C ANISOU 1866 CA HIS A 245 6803 5111 6701 44 199 -79 C ATOM 1867 C HIS A 245 -12.674 16.079 11.574 1.00 49.92 C ANISOU 1867 C HIS A 245 6935 5172 6861 40 84 -132 C ATOM 1868 O HIS A 245 -13.389 15.306 12.197 1.00 50.03 O ANISOU 1868 O HIS A 245 6859 5170 6983 13 83 -157 O ATOM 1869 CB HIS A 245 -12.091 18.220 12.811 1.00 48.33 C ANISOU 1869 CB HIS A 245 6657 5044 6661 48 178 -63 C ATOM 1870 CG HIS A 245 -11.325 18.684 14.014 1.00 48.10 C ANISOU 1870 CG HIS A 245 6568 5066 6642 41 289 -25 C ATOM 1871 ND1 HIS A 245 -10.144 19.397 13.887 1.00 49.48 N ANISOU 1871 ND1 HIS A 245 6796 5269 6735 53 351 9 N ATOM 1872 CD2 HIS A 245 -11.565 18.471 15.328 1.00 48.11 C ANISOU 1872 CD2 HIS A 245 6470 5088 6722 24 347 -20 C ATOM 1873 CE1 HIS A 245 -9.721 19.616 15.122 1.00 49.53 C ANISOU 1873 CE1 HIS A 245 6727 5314 6778 44 425 28 C ATOM 1874 NE2 HIS A 245 -10.542 19.079 16.022 1.00 49.02 N ANISOU 1874 NE2 HIS A 245 6581 5247 6799 30 427 14 N ATOM 1875 N ILE A 246 -12.738 16.209 10.235 1.00 50.19 N ANISOU 1875 N ILE A 246 7092 5170 6809 66 -7 -152 N ATOM 1876 CA ILE A 246 -13.690 15.421 9.451 1.00 50.51 C ANISOU 1876 CA ILE A 246 7158 5151 6884 66 -134 -212 C ATOM 1877 C ILE A 246 -13.330 13.941 9.556 1.00 51.11 C ANISOU 1877 C ILE A 246 7239 5213 6966 45 -78 -231 C ATOM 1878 O ILE A 246 -14.185 13.134 9.903 1.00 52.03 O ANISOU 1878 O ILE A 246 7270 5298 7200 16 -115 -270 O ATOM 1879 CB ILE A 246 -13.747 15.888 7.972 1.00 50.91 C ANISOU 1879 CB ILE A 246 7371 5160 6813 109 -249 -228 C ATOM 1880 CG1 ILE A 246 -14.334 17.308 7.856 1.00 51.43 C ANISOU 1880 CG1 ILE A 246 7430 5222 6889 134 -331 -216 C ATOM 1881 CG2 ILE A 246 -14.516 14.886 7.102 1.00 51.55 C ANISOU 1881 CG2 ILE A 246 7501 5176 6910 113 -383 -298 C ATOM 1882 CD1 ILE A 246 -14.260 17.917 6.465 1.00 52.29 C ANISOU 1882 CD1 ILE A 246 7726 5288 6853 184 -428 -216 C ATOM 1883 N MET A 247 -12.047 13.594 9.338 1.00 50.62 N ANISOU 1883 N MET A 247 7266 5172 6794 57 23 -202 N ATOM 1884 CA MET A 247 -11.585 12.202 9.342 1.00 50.24 C ANISOU 1884 CA MET A 247 7242 5107 6739 46 77 -219 C ATOM 1885 C MET A 247 -11.580 11.532 10.695 1.00 50.08 C ANISOU 1885 C MET A 247 7098 5106 6823 15 166 -203 C ATOM 1886 O MET A 247 -11.867 10.349 10.753 1.00 50.07 O ANISOU 1886 O MET A 247 7087 5067 6871 -3 163 -233 O ATOM 1887 CB MET A 247 -10.220 12.060 8.662 1.00 51.02 C ANISOU 1887 CB MET A 247 7470 5217 6699 75 161 -198 C ATOM 1888 CG MET A 247 -10.287 12.230 7.133 1.00 53.92 C ANISOU 1888 CG MET A 247 8004 5538 6945 106 76 -226 C ATOM 1889 SD MET A 247 -11.493 11.089 6.378 1.00 61.41 S ANISOU 1889 SD MET A 247 8990 6408 7936 100 -82 -309 S ATOM 1890 CE MET A 247 -12.557 12.211 5.787 1.00 58.71 C ANISOU 1890 CE MET A 247 8667 6042 7597 118 -242 -327 C ATOM 1891 N ARG A 248 -11.320 12.256 11.797 1.00 50.00 N ANISOU 1891 N ARG A 248 7003 5147 6848 9 241 -159 N ATOM 1892 CA ARG A 248 -11.375 11.649 13.132 1.00 49.86 C ANISOU 1892 CA ARG A 248 6888 5140 6916 -15 324 -141 C ATOM 1893 C ARG A 248 -12.815 11.198 13.407 1.00 50.76 C ANISOU 1893 C ARG A 248 6916 5206 7164 -51 264 -181 C ATOM 1894 O ARG A 248 -13.020 10.082 13.843 1.00 51.37 O ANISOU 1894 O ARG A 248 6969 5250 7300 -74 302 -192 O ATOM 1895 CB ARG A 248 -10.909 12.626 14.218 1.00 49.54 C ANISOU 1895 CB ARG A 248 6786 5157 6879 -9 398 -94 C ATOM 1896 CG ARG A 248 -10.829 11.955 15.573 1.00 50.32 C ANISOU 1896 CG ARG A 248 6822 5263 7036 -23 486 -72 C ATOM 1897 CD ARG A 248 -10.358 12.908 16.630 1.00 51.47 C ANISOU 1897 CD ARG A 248 6923 5460 7173 -12 547 -32 C ATOM 1898 NE ARG A 248 -11.382 13.892 16.979 1.00 52.61 N ANISOU 1898 NE ARG A 248 6997 5608 7386 -26 513 -38 N ATOM 1899 CZ ARG A 248 -11.134 15.065 17.552 1.00 52.08 C ANISOU 1899 CZ ARG A 248 6901 5581 7305 -15 534 -14 C ATOM 1900 NH1 ARG A 248 -9.888 15.428 17.825 1.00 52.21 N ANISOU 1900 NH1 ARG A 248 6949 5639 7249 8 583 15 N ATOM 1901 NH2 ARG A 248 -12.128 15.878 17.861 1.00 50.43 N ANISOU 1901 NH2 ARG A 248 6627 5367 7167 -25 506 -24 N ATOM 1902 N ASN A 249 -13.804 12.040 13.063 1.00 50.57 N ANISOU 1902 N ASN A 249 6852 5170 7193 -53 168 -206 N ATOM 1903 CA ASN A 249 -15.217 11.748 13.225 1.00 50.82 C ANISOU 1903 CA ASN A 249 6784 5151 7374 -86 102 -253 C ATOM 1904 C ASN A 249 -15.705 10.661 12.244 1.00 52.20 C ANISOU 1904 C ASN A 249 7001 5258 7573 -98 7 -316 C ATOM 1905 O ASN A 249 -16.500 9.821 12.634 1.00 52.53 O ANISOU 1905 O ASN A 249 6963 5251 7745 -138 10 -350 O ATOM 1906 CB ASN A 249 -16.034 13.034 13.117 1.00 50.53 C ANISOU 1906 CB ASN A 249 6689 5121 7390 -75 20 -265 C ATOM 1907 CG ASN A 249 -15.878 13.909 14.337 1.00 52.43 C ANISOU 1907 CG ASN A 249 6855 5410 7654 -76 120 -217 C ATOM 1908 OD1 ASN A 249 -16.159 13.495 15.463 1.00 53.48 O ANISOU 1908 OD1 ASN A 249 6906 5541 7872 -105 214 -207 O ATOM 1909 ND2 ASN A 249 -15.417 15.138 14.154 1.00 52.33 N ANISOU 1909 ND2 ASN A 249 6881 5439 7564 -44 106 -188 N ATOM 1910 N VAL A 250 -15.220 10.659 10.988 1.00 52.81 N ANISOU 1910 N VAL A 250 7211 5326 7527 -64 -70 -332 N ATOM 1911 CA VAL A 250 -15.586 9.640 9.996 1.00 53.59 C ANISOU 1911 CA VAL A 250 7377 5359 7628 -68 -168 -396 C ATOM 1912 C VAL A 250 -14.962 8.269 10.382 1.00 55.03 C ANISOU 1912 C VAL A 250 7579 5525 7806 -89 -63 -389 C ATOM 1913 O VAL A 250 -15.587 7.212 10.208 1.00 55.78 O ANISOU 1913 O VAL A 250 7653 5554 7986 -119 -105 -441 O ATOM 1914 CB VAL A 250 -15.223 10.087 8.546 1.00 53.73 C ANISOU 1914 CB VAL A 250 7557 5366 7492 -19 -272 -413 C ATOM 1915 CG1 VAL A 250 -15.363 8.941 7.547 1.00 53.93 C ANISOU 1915 CG1 VAL A 250 7680 5324 7488 -17 -356 -477 C ATOM 1916 CG2 VAL A 250 -16.059 11.285 8.106 1.00 53.59 C ANISOU 1916 CG2 VAL A 250 7524 5342 7494 4 -404 -429 C ATOM 1917 N ARG A 251 -13.754 8.287 10.956 1.00 55.19 N ANISOU 1917 N ARG A 251 7632 5598 7742 -73 71 -327 N ATOM 1918 CA ARG A 251 -13.065 7.074 11.412 1.00 55.39 C ANISOU 1918 CA ARG A 251 7678 5609 7759 -81 172 -314 C ATOM 1919 C ARG A 251 -13.904 6.412 12.525 1.00 56.34 C ANISOU 1919 C ARG A 251 7680 5694 8034 -130 219 -317 C ATOM 1920 O ARG A 251 -14.108 5.196 12.504 1.00 56.81 O ANISOU 1920 O ARG A 251 7747 5693 8144 -154 229 -345 O ATOM 1921 CB ARG A 251 -11.642 7.423 11.906 1.00 55.36 C ANISOU 1921 CB ARG A 251 7711 5671 7653 -47 291 -249 C ATOM 1922 CG ARG A 251 -10.940 6.334 12.693 1.00 56.93 C ANISOU 1922 CG ARG A 251 7908 5862 7860 -47 398 -225 C ATOM 1923 CD ARG A 251 -10.644 5.171 11.806 1.00 58.96 C ANISOU 1923 CD ARG A 251 8260 6066 8078 -38 379 -265 C ATOM 1924 NE ARG A 251 -9.662 4.271 12.393 1.00 61.97 N ANISOU 1924 NE ARG A 251 8663 6446 8439 -19 482 -236 N ATOM 1925 CZ ARG A 251 -9.742 2.945 12.352 1.00 64.19 C ANISOU 1925 CZ ARG A 251 8974 6663 8753 -30 494 -261 C ATOM 1926 NH1 ARG A 251 -10.782 2.350 11.775 1.00 63.64 N ANISOU 1926 NH1 ARG A 251 8908 6525 8748 -66 412 -319 N ATOM 1927 NH2 ARG A 251 -8.785 2.201 12.891 1.00 64.48 N ANISOU 1927 NH2 ARG A 251 9035 6698 8767 -2 583 -231 N ATOM 1928 N ILE A 252 -14.418 7.220 13.470 1.00 56.27 N ANISOU 1928 N ILE A 252 7566 5714 8099 -146 254 -290 N ATOM 1929 CA ILE A 252 -15.239 6.709 14.563 1.00 56.58 C ANISOU 1929 CA ILE A 252 7500 5716 8283 -193 320 -289 C ATOM 1930 C ILE A 252 -16.604 6.216 14.056 1.00 57.60 C ANISOU 1930 C ILE A 252 7559 5765 8559 -238 223 -364 C ATOM 1931 O ILE A 252 -17.018 5.109 14.397 1.00 57.60 O ANISOU 1931 O ILE A 252 7530 5700 8654 -279 266 -384 O ATOM 1932 CB ILE A 252 -15.368 7.741 15.702 1.00 56.11 C ANISOU 1932 CB ILE A 252 7361 5706 8252 -193 394 -242 C ATOM 1933 CG1 ILE A 252 -13.990 8.098 16.282 1.00 56.47 C ANISOU 1933 CG1 ILE A 252 7469 5820 8165 -151 484 -176 C ATOM 1934 CG2 ILE A 252 -16.278 7.214 16.776 1.00 56.34 C ANISOU 1934 CG2 ILE A 252 7293 5686 8426 -242 477 -243 C ATOM 1935 CD1 ILE A 252 -13.949 9.389 17.079 1.00 57.55 C ANISOU 1935 CD1 ILE A 252 7556 6017 8295 -138 521 -139 C ATOM 1936 N ALA A 253 -17.262 7.003 13.204 1.00 58.34 N ANISOU 1936 N ALA A 253 7634 5857 8674 -227 86 -409 N ATOM 1937 CA ALA A 253 -18.555 6.657 12.616 1.00 60.18 C ANISOU 1937 CA ALA A 253 7795 6015 9056 -260 -39 -492 C ATOM 1938 C ALA A 253 -18.501 5.349 11.801 1.00 62.77 C ANISOU 1938 C ALA A 253 8198 6274 9376 -274 -95 -545 C ATOM 1939 O ALA A 253 -19.410 4.524 11.894 1.00 63.84 O ANISOU 1939 O ALA A 253 8254 6332 9670 -325 -117 -600 O ATOM 1940 CB ALA A 253 -19.049 7.801 11.741 1.00 60.13 C ANISOU 1940 CB ALA A 253 7790 6023 9036 -226 -196 -526 C ATOM 1941 N SER A 254 -17.411 5.126 11.047 1.00 63.41 N ANISOU 1941 N SER A 254 8433 6380 9282 -230 -105 -530 N ATOM 1942 CA SER A 254 -17.243 3.896 10.275 1.00 63.96 C ANISOU 1942 CA SER A 254 8592 6385 9325 -235 -148 -579 C ATOM 1943 C SER A 254 -17.150 2.641 11.162 1.00 65.01 C ANISOU 1943 C SER A 254 8689 6473 9539 -279 -19 -564 C ATOM 1944 O SER A 254 -17.346 1.524 10.667 1.00 66.40 O ANISOU 1944 O SER A 254 8902 6574 9753 -301 -58 -617 O ATOM 1945 CB SER A 254 -16.029 3.994 9.351 1.00 65.30 C ANISOU 1945 CB SER A 254 8935 6591 9286 -175 -157 -561 C ATOM 1946 OG SER A 254 -14.794 3.824 10.032 1.00 67.72 O ANISOU 1946 OG SER A 254 9280 6949 9503 -155 0 -488 O ATOM 1947 N ARG A 255 -16.832 2.803 12.454 1.00 64.24 N ANISOU 1947 N ARG A 255 8534 6414 9462 -289 131 -492 N ATOM 1948 CA ARG A 255 -16.750 1.669 13.371 1.00 63.82 C ANISOU 1948 CA ARG A 255 8463 6311 9474 -325 259 -468 C ATOM 1949 C ARG A 255 -18.103 1.341 14.028 1.00 64.90 C ANISOU 1949 C ARG A 255 8459 6374 9824 -397 283 -500 C ATOM 1950 O ARG A 255 -18.185 0.355 14.756 1.00 65.23 O ANISOU 1950 O ARG A 255 8491 6356 9936 -435 391 -484 O ATOM 1951 CB ARG A 255 -15.688 1.915 14.450 1.00 63.30 C ANISOU 1951 CB ARG A 255 8428 6311 9312 -292 406 -375 C ATOM 1952 CG ARG A 255 -14.274 1.992 13.901 1.00 64.08 C ANISOU 1952 CG ARG A 255 8652 6465 9231 -228 409 -347 C ATOM 1953 CD ARG A 255 -13.231 1.846 14.981 1.00 64.49 C ANISOU 1953 CD ARG A 255 8731 6556 9216 -198 542 -271 C ATOM 1954 NE ARG A 255 -13.298 2.950 15.932 1.00 66.23 N ANISOU 1954 NE ARG A 255 8883 6838 9442 -194 592 -222 N ATOM 1955 CZ ARG A 255 -13.578 2.818 17.224 1.00 66.73 C ANISOU 1955 CZ ARG A 255 8898 6888 9566 -214 693 -181 C ATOM 1956 NH1 ARG A 255 -13.791 1.616 17.744 1.00 64.00 N ANISOU 1956 NH1 ARG A 255 8569 6468 9282 -242 763 -176 N ATOM 1957 NH2 ARG A 255 -13.604 3.885 18.015 1.00 67.00 N ANISOU 1957 NH2 ARG A 255 8884 6980 9592 -205 731 -143 N ATOM 1958 N LEU A 256 -19.157 2.149 13.791 1.00 65.32 N ANISOU 1958 N LEU A 256 8404 6424 9989 -416 190 -546 N ATOM 1959 CA LEU A 256 -20.459 1.903 14.407 1.00 66.32 C ANISOU 1959 CA LEU A 256 8379 6479 10342 -486 222 -584 C ATOM 1960 C LEU A 256 -21.119 0.596 13.941 1.00 67.70 C ANISOU 1960 C LEU A 256 8532 6539 10651 -542 175 -661 C ATOM 1961 O LEU A 256 -21.121 0.264 12.755 1.00 68.44 O ANISOU 1961 O LEU A 256 8685 6605 10714 -528 22 -728 O ATOM 1962 CB LEU A 256 -21.405 3.100 14.228 1.00 66.13 C ANISOU 1962 CB LEU A 256 8235 6475 10417 -485 123 -622 C ATOM 1963 CG LEU A 256 -21.136 4.303 15.125 1.00 67.25 C ANISOU 1963 CG LEU A 256 8344 6701 10506 -457 215 -551 C ATOM 1964 CD1 LEU A 256 -21.871 5.513 14.633 1.00 67.91 C ANISOU 1964 CD1 LEU A 256 8347 6809 10647 -437 81 -592 C ATOM 1965 CD2 LEU A 256 -21.511 4.022 16.553 1.00 67.67 C ANISOU 1965 CD2 LEU A 256 8315 6726 10672 -505 402 -510 C ATOM 1966 N GLY A 262 -13.771 -4.636 7.177 1.00 89.41 N ANISOU 1966 N GLY A 262 12505 9213 12253 -197 -23 -778 N ATOM 1967 CA GLY A 262 -14.057 -4.243 5.803 1.00 89.62 C ANISOU 1967 CA GLY A 262 12633 9225 12192 -170 -179 -852 C ATOM 1968 C GLY A 262 -12.965 -3.382 5.201 1.00 89.43 C ANISOU 1968 C GLY A 262 12730 9282 11969 -96 -147 -813 C ATOM 1969 O GLY A 262 -12.170 -2.778 5.937 1.00 89.80 O ANISOU 1969 O GLY A 262 12738 9410 11972 -73 -24 -729 O ATOM 1970 N CYS A 263 -12.908 -3.319 3.853 1.00 88.41 N ANISOU 1970 N CYS A 263 12753 9125 11715 -57 -255 -876 N ATOM 1971 CA CYS A 263 -11.898 -2.503 3.165 1.00 87.87 C ANISOU 1971 CA CYS A 263 12816 9118 11452 11 -214 -843 C ATOM 1972 C CYS A 263 -12.176 -1.002 3.268 1.00 86.39 C ANISOU 1972 C CYS A 263 12576 9004 11242 18 -254 -800 C ATOM 1973 O CYS A 263 -11.242 -0.206 3.275 1.00 86.43 O ANISOU 1973 O CYS A 263 12623 9080 11136 57 -158 -737 O ATOM 1974 CB CYS A 263 -11.709 -2.952 1.716 1.00 88.80 C ANISOU 1974 CB CYS A 263 13138 9174 11429 53 -298 -920 C ATOM 1975 SG CYS A 263 -10.837 -4.537 1.516 1.00 92.64 S ANISOU 1975 SG CYS A 263 13727 9593 11879 73 -194 -950 S ATOM 1976 N SER A 264 -13.454 -0.628 3.377 1.00 85.00 N ANISOU 1976 N SER A 264 12301 8808 11186 -21 -390 -835 N ATOM 1977 CA SER A 264 -13.881 0.751 3.519 1.00 84.26 C ANISOU 1977 CA SER A 264 12146 8772 11098 -16 -443 -802 C ATOM 1978 C SER A 264 -13.317 1.331 4.824 1.00 82.96 C ANISOU 1978 C SER A 264 11854 8692 10974 -27 -280 -705 C ATOM 1979 O SER A 264 -12.801 2.451 4.814 1.00 83.17 O ANISOU 1979 O SER A 264 11902 8788 10911 4 -242 -651 O ATOM 1980 CB SER A 264 -15.404 0.818 3.516 1.00 85.92 C ANISOU 1980 CB SER A 264 12244 8931 11473 -59 -612 -869 C ATOM 1981 OG SER A 264 -15.878 2.140 3.705 1.00 88.82 O ANISOU 1981 OG SER A 264 12543 9348 11858 -50 -669 -841 O ATOM 1982 N GLN A 265 -13.357 0.535 5.925 1.00 81.31 N ANISOU 1982 N GLN A 265 11531 8472 10891 -70 -182 -683 N ATOM 1983 CA GLN A 265 -12.838 0.903 7.245 1.00 80.13 C ANISOU 1983 CA GLN A 265 11275 8391 10781 -78 -34 -596 C ATOM 1984 C GLN A 265 -11.329 1.150 7.227 1.00 77.84 C ANISOU 1984 C GLN A 265 11069 8162 10345 -25 90 -538 C ATOM 1985 O GLN A 265 -10.876 2.126 7.808 1.00 78.09 O ANISOU 1985 O GLN A 265 11051 8267 10351 -11 154 -476 O ATOM 1986 CB GLN A 265 -13.192 -0.165 8.292 1.00 83.03 C ANISOU 1986 CB GLN A 265 11544 8712 11294 -128 39 -591 C ATOM 1987 CG GLN A 265 -14.088 0.359 9.417 1.00 89.37 C ANISOU 1987 CG GLN A 265 12183 9531 12243 -176 60 -562 C ATOM 1988 CD GLN A 265 -13.917 -0.376 10.742 1.00 96.47 C ANISOU 1988 CD GLN A 265 13015 10416 13225 -205 202 -512 C ATOM 1989 OE1 GLN A 265 -14.880 -0.940 11.293 1.00 99.05 O ANISOU 1989 OE1 GLN A 265 13251 10677 13705 -263 209 -534 O ATOM 1990 NE2 GLN A 265 -12.694 -0.382 11.291 1.00 97.04 N ANISOU 1990 NE2 GLN A 265 13131 10540 13201 -163 319 -445 N ATOM 1991 N LYS A 266 -10.555 0.287 6.548 1.00 75.75 N ANISOU 1991 N LYS A 266 10926 7862 9993 6 123 -563 N ATOM 1992 CA LYS A 266 -9.111 0.451 6.424 1.00 74.07 C ANISOU 1992 CA LYS A 266 10787 7696 9659 59 244 -520 C ATOM 1993 C LYS A 266 -8.756 1.623 5.505 1.00 72.01 C ANISOU 1993 C LYS A 266 10620 7476 9266 95 219 -513 C ATOM 1994 O LYS A 266 -7.784 2.334 5.766 1.00 72.50 O ANISOU 1994 O LYS A 266 10675 7601 9272 122 322 -458 O ATOM 1995 CB LYS A 266 -8.446 -0.844 5.940 1.00 75.97 C ANISOU 1995 CB LYS A 266 11129 7879 9857 84 291 -555 C ATOM 1996 CG LYS A 266 -8.249 -1.835 7.059 1.00 80.76 C ANISOU 1996 CG LYS A 266 11653 8465 10565 68 375 -529 C ATOM 1997 CD LYS A 266 -7.172 -2.837 6.735 1.00 87.20 C ANISOU 1997 CD LYS A 266 12561 9247 11323 112 459 -542 C ATOM 1998 CE LYS A 266 -6.876 -3.715 7.922 1.00 91.88 C ANISOU 1998 CE LYS A 266 13081 9820 12008 107 542 -505 C ATOM 1999 NZ LYS A 266 -6.416 -2.908 9.086 1.00 94.77 N ANISOU 1999 NZ LYS A 266 13344 10267 12398 116 616 -426 N ATOM 2000 N ALA A 267 -9.561 1.859 4.461 1.00 69.68 N ANISOU 2000 N ALA A 267 10410 7139 8926 96 80 -569 N ATOM 2001 CA ALA A 267 -9.330 2.983 3.563 1.00 68.07 C ANISOU 2001 CA ALA A 267 10316 6959 8588 133 49 -559 C ATOM 2002 C ALA A 267 -9.545 4.295 4.317 1.00 66.35 C ANISOU 2002 C ALA A 267 9982 6812 8418 119 56 -500 C ATOM 2003 O ALA A 267 -8.736 5.207 4.179 1.00 66.54 O ANISOU 2003 O ALA A 267 10047 6883 8352 146 134 -453 O ATOM 2004 CB ALA A 267 -10.261 2.903 2.366 1.00 67.94 C ANISOU 2004 CB ALA A 267 10421 6874 8519 142 -127 -635 C ATOM 2005 N ILE A 268 -10.601 4.370 5.151 1.00 64.50 N ANISOU 2005 N ILE A 268 9598 6578 8331 75 -10 -503 N ATOM 2006 CA ILE A 268 -10.914 5.558 5.942 1.00 63.33 C ANISOU 2006 CA ILE A 268 9332 6490 8241 61 -4 -454 C ATOM 2007 C ILE A 268 -9.794 5.840 6.963 1.00 62.66 C ANISOU 2007 C ILE A 268 9181 6475 8153 66 161 -380 C ATOM 2008 O ILE A 268 -9.401 6.997 7.148 1.00 62.46 O ANISOU 2008 O ILE A 268 9140 6504 8089 79 198 -334 O ATOM 2009 CB ILE A 268 -12.340 5.445 6.561 1.00 63.09 C ANISOU 2009 CB ILE A 268 9159 6432 8381 12 -101 -485 C ATOM 2010 CG1 ILE A 268 -13.404 5.724 5.499 1.00 64.08 C ANISOU 2010 CG1 ILE A 268 9341 6505 8504 20 -290 -553 C ATOM 2011 CG2 ILE A 268 -12.536 6.365 7.759 1.00 63.16 C ANISOU 2011 CG2 ILE A 268 9022 6502 8475 -8 -45 -428 C ATOM 2012 CD1 ILE A 268 -14.764 5.102 5.793 1.00 65.73 C ANISOU 2012 CD1 ILE A 268 9428 6652 8893 -29 -397 -616 C ATOM 2013 N ASN A 269 -9.219 4.773 7.553 1.00 61.80 N ANISOU 2013 N ASN A 269 9046 6357 8080 62 253 -372 N ATOM 2014 CA ASN A 269 -8.117 4.902 8.503 1.00 61.35 C ANISOU 2014 CA ASN A 269 8932 6356 8022 76 391 -312 C ATOM 2015 C ASN A 269 -6.861 5.491 7.824 1.00 61.49 C ANISOU 2015 C ASN A 269 9042 6407 7916 120 467 -292 C ATOM 2016 O ASN A 269 -6.136 6.277 8.434 1.00 61.38 O ANISOU 2016 O ASN A 269 8971 6450 7899 130 544 -244 O ATOM 2017 CB ASN A 269 -7.802 3.559 9.135 1.00 61.76 C ANISOU 2017 CB ASN A 269 8959 6377 8131 72 454 -315 C ATOM 2018 CG ASN A 269 -6.846 3.673 10.287 1.00 64.32 C ANISOU 2018 CG ASN A 269 9211 6752 8474 89 567 -256 C ATOM 2019 OD1 ASN A 269 -6.917 4.606 11.107 1.00 65.97 O ANISOU 2019 OD1 ASN A 269 9337 7014 8714 80 583 -215 O ATOM 2020 ND2 ASN A 269 -5.928 2.727 10.372 1.00 63.72 N ANISOU 2020 ND2 ASN A 269 9170 6658 8383 119 640 -256 N ATOM 2021 N CYS A 270 -6.618 5.117 6.554 1.00 61.48 N ANISOU 2021 N CYS A 270 9185 6361 7814 145 448 -333 N ATOM 2022 CA CYS A 270 -5.501 5.631 5.761 1.00 61.11 C ANISOU 2022 CA CYS A 270 9243 6328 7646 184 533 -319 C ATOM 2023 C CYS A 270 -5.700 7.119 5.505 1.00 60.56 C ANISOU 2023 C CYS A 270 9187 6293 7531 182 504 -289 C ATOM 2024 O CYS A 270 -4.760 7.889 5.690 1.00 60.96 O ANISOU 2024 O CYS A 270 9222 6386 7555 195 606 -248 O ATOM 2025 CB CYS A 270 -5.357 4.848 4.459 1.00 61.55 C ANISOU 2025 CB CYS A 270 9470 6319 7600 211 518 -374 C ATOM 2026 SG CYS A 270 -4.739 3.155 4.676 1.00 63.26 S ANISOU 2026 SG CYS A 270 9688 6493 7854 225 591 -405 S ATOM 2027 N LEU A 271 -6.937 7.540 5.151 1.00 59.49 N ANISOU 2027 N LEU A 271 9069 6135 7402 168 361 -312 N ATOM 2028 CA LEU A 271 -7.265 8.958 4.941 1.00 58.82 C ANISOU 2028 CA LEU A 271 8995 6072 7280 170 315 -284 C ATOM 2029 C LEU A 271 -7.047 9.740 6.243 1.00 56.46 C ANISOU 2029 C LEU A 271 8537 5842 7074 149 380 -230 C ATOM 2030 O LEU A 271 -6.508 10.843 6.208 1.00 56.96 O ANISOU 2030 O LEU A 271 8610 5937 7093 158 433 -190 O ATOM 2031 CB LEU A 271 -8.741 9.131 4.519 1.00 59.93 C ANISOU 2031 CB LEU A 271 9149 6173 7449 161 132 -326 C ATOM 2032 CG LEU A 271 -9.123 8.928 3.061 1.00 62.12 C ANISOU 2032 CG LEU A 271 9613 6380 7608 192 20 -380 C ATOM 2033 CD1 LEU A 271 -10.591 9.296 2.867 1.00 62.85 C ANISOU 2033 CD1 LEU A 271 9678 6442 7762 185 -174 -418 C ATOM 2034 CD2 LEU A 271 -8.264 9.790 2.140 1.00 62.63 C ANISOU 2034 CD2 LEU A 271 9849 6442 7505 232 90 -350 C ATOM 2035 N TYR A 272 -7.498 9.170 7.377 1.00 53.54 N ANISOU 2035 N TYR A 272 8028 5487 6828 121 375 -229 N ATOM 2036 CA TYR A 272 -7.360 9.721 8.711 1.00 51.11 C ANISOU 2036 CA TYR A 272 7578 5235 6606 103 430 -184 C ATOM 2037 C TYR A 272 -5.861 9.916 9.062 1.00 50.64 C ANISOU 2037 C TYR A 272 7512 5219 6512 124 568 -146 C ATOM 2038 O TYR A 272 -5.497 11.006 9.504 1.00 50.22 O ANISOU 2038 O TYR A 272 7409 5208 6463 123 605 -110 O ATOM 2039 CB TYR A 272 -8.133 8.833 9.723 1.00 49.72 C ANISOU 2039 CB TYR A 272 7293 5046 6551 73 409 -195 C ATOM 2040 CG TYR A 272 -7.863 9.096 11.191 1.00 48.97 C ANISOU 2040 CG TYR A 272 7077 5000 6530 62 483 -150 C ATOM 2041 CD1 TYR A 272 -8.026 10.365 11.735 1.00 49.34 C ANISOU 2041 CD1 TYR A 272 7060 5091 6595 56 482 -119 C ATOM 2042 CD2 TYR A 272 -7.509 8.062 12.049 1.00 49.18 C ANISOU 2042 CD2 TYR A 272 7062 5019 6604 60 547 -141 C ATOM 2043 CE1 TYR A 272 -7.800 10.606 13.087 1.00 50.17 C ANISOU 2043 CE1 TYR A 272 7069 5236 6757 50 543 -84 C ATOM 2044 CE2 TYR A 272 -7.259 8.294 13.396 1.00 49.83 C ANISOU 2044 CE2 TYR A 272 7057 5140 6737 58 607 -101 C ATOM 2045 CZ TYR A 272 -7.405 9.569 13.916 1.00 50.99 C ANISOU 2045 CZ TYR A 272 7146 5333 6895 53 604 -74 C ATOM 2046 OH TYR A 272 -7.144 9.808 15.251 1.00 51.83 O ANISOU 2046 OH TYR A 272 7181 5474 7039 55 657 -39 O ATOM 2047 N ILE A 273 -4.991 8.899 8.798 1.00 50.35 N ANISOU 2047 N ILE A 273 7522 5163 6447 145 639 -160 N ATOM 2048 CA ILE A 273 -3.536 8.960 9.033 1.00 50.62 C ANISOU 2048 CA ILE A 273 7541 5226 6467 170 765 -137 C ATOM 2049 C ILE A 273 -2.933 10.158 8.303 1.00 51.56 C ANISOU 2049 C ILE A 273 7720 5359 6511 179 813 -120 C ATOM 2050 O ILE A 273 -2.150 10.904 8.893 1.00 51.92 O ANISOU 2050 O ILE A 273 7693 5447 6588 180 884 -89 O ATOM 2051 CB ILE A 273 -2.832 7.634 8.614 1.00 50.95 C ANISOU 2051 CB ILE A 273 7641 5230 6487 197 822 -167 C ATOM 2052 CG1 ILE A 273 -3.116 6.491 9.621 1.00 51.85 C ANISOU 2052 CG1 ILE A 273 7679 5333 6689 191 807 -170 C ATOM 2053 CG2 ILE A 273 -1.313 7.810 8.388 1.00 51.18 C ANISOU 2053 CG2 ILE A 273 7681 5276 6491 228 953 -158 C ATOM 2054 CD1 ILE A 273 -2.852 5.091 9.064 1.00 52.58 C ANISOU 2054 CD1 ILE A 273 7847 5368 6762 212 826 -209 C ATOM 2055 N LEU A 274 -3.313 10.350 7.027 1.00 51.63 N ANISOU 2055 N LEU A 274 7870 5326 6422 187 772 -140 N ATOM 2056 CA LEU A 274 -2.830 11.452 6.199 1.00 51.69 C ANISOU 2056 CA LEU A 274 7970 5330 6341 196 822 -121 C ATOM 2057 C LEU A 274 -3.102 12.852 6.799 1.00 52.48 C ANISOU 2057 C LEU A 274 7992 5470 6479 176 800 -81 C ATOM 2058 O LEU A 274 -2.239 13.735 6.726 1.00 53.85 O ANISOU 2058 O LEU A 274 8168 5659 6635 177 895 -53 O ATOM 2059 CB LEU A 274 -3.436 11.360 4.789 1.00 51.76 C ANISOU 2059 CB LEU A 274 8163 5277 6226 213 750 -151 C ATOM 2060 CG LEU A 274 -3.017 10.182 3.882 1.00 52.51 C ANISOU 2060 CG LEU A 274 8385 5320 6247 239 790 -193 C ATOM 2061 CD1 LEU A 274 -3.715 10.273 2.558 1.00 52.65 C ANISOU 2061 CD1 LEU A 274 8595 5275 6133 259 695 -223 C ATOM 2062 CD2 LEU A 274 -1.533 10.181 3.620 1.00 52.59 C ANISOU 2062 CD2 LEU A 274 8424 5333 6227 258 970 -181 C ATOM 2063 N THR A 275 -4.283 13.048 7.406 1.00 51.18 N ANISOU 2063 N THR A 275 7753 5317 6375 157 684 -81 N ATOM 2064 CA THR A 275 -4.704 14.322 7.966 1.00 50.02 C ANISOU 2064 CA THR A 275 7536 5201 6267 142 650 -50 C ATOM 2065 C THR A 275 -4.025 14.732 9.271 1.00 49.70 C ANISOU 2065 C THR A 275 7353 5217 6313 129 725 -21 C ATOM 2066 O THR A 275 -4.014 15.927 9.586 1.00 50.18 O ANISOU 2066 O THR A 275 7378 5300 6388 120 729 6 O ATOM 2067 CB THR A 275 -6.230 14.332 8.149 1.00 50.02 C ANISOU 2067 CB THR A 275 7501 5187 6317 129 505 -70 C ATOM 2068 OG1 THR A 275 -6.589 13.437 9.199 1.00 50.26 O ANISOU 2068 OG1 THR A 275 7415 5234 6449 111 498 -81 O ATOM 2069 CG2 THR A 275 -6.979 14.009 6.866 1.00 49.71 C ANISOU 2069 CG2 THR A 275 7602 5088 6199 146 399 -108 C ATOM 2070 N ARG A 276 -3.517 13.767 10.053 1.00 48.78 N ANISOU 2070 N ARG A 276 7161 5118 6254 132 772 -28 N ATOM 2071 CA ARG A 276 -2.918 14.056 11.361 1.00 47.84 C ANISOU 2071 CA ARG A 276 6916 5047 6212 128 821 -5 C ATOM 2072 C ARG A 276 -1.686 14.961 11.293 1.00 47.96 C ANISOU 2072 C ARG A 276 6919 5083 6222 133 915 12 C ATOM 2073 O ARG A 276 -1.765 16.003 11.926 1.00 48.47 O ANISOU 2073 O ARG A 276 6920 5175 6321 119 905 32 O ATOM 2074 CB ARG A 276 -2.635 12.780 12.161 1.00 47.35 C ANISOU 2074 CB ARG A 276 6798 4989 6203 139 841 -15 C ATOM 2075 CG ARG A 276 -3.893 11.958 12.370 1.00 47.11 C ANISOU 2075 CG ARG A 276 6766 4933 6200 125 760 -31 C ATOM 2076 CD ARG A 276 -3.799 11.092 13.588 1.00 47.50 C ANISOU 2076 CD ARG A 276 6742 4990 6314 129 778 -24 C ATOM 2077 NE ARG A 276 -2.749 10.073 13.475 1.00 49.31 N ANISOU 2077 NE ARG A 276 6995 5207 6534 160 840 -35 N ATOM 2078 CZ ARG A 276 -2.949 8.840 13.025 1.00 49.93 C ANISOU 2078 CZ ARG A 276 7127 5239 6604 165 832 -59 C ATOM 2079 NH1 ARG A 276 -4.143 8.471 12.589 1.00 47.17 N ANISOU 2079 NH1 ARG A 276 6814 4853 6257 139 761 -80 N ATOM 2080 NH2 ARG A 276 -1.954 7.969 13.000 1.00 52.23 N ANISOU 2080 NH2 ARG A 276 7433 5517 6893 199 891 -68 N ATOM 2081 N PRO A 277 -0.570 14.673 10.554 1.00 47.54 N ANISOU 2081 N PRO A 277 6918 5011 6134 149 1012 3 N ATOM 2082 CA PRO A 277 0.546 15.640 10.522 1.00 47.04 C ANISOU 2082 CA PRO A 277 6824 4959 6088 144 1108 17 C ATOM 2083 C PRO A 277 0.185 16.952 9.812 1.00 47.54 C ANISOU 2083 C PRO A 277 6963 5005 6094 126 1104 39 C ATOM 2084 O PRO A 277 0.815 17.977 10.092 1.00 47.48 O ANISOU 2084 O PRO A 277 6906 5010 6124 111 1160 55 O ATOM 2085 CB PRO A 277 1.684 14.867 9.842 1.00 46.81 C ANISOU 2085 CB PRO A 277 6835 4906 6047 166 1218 -5 C ATOM 2086 CG PRO A 277 1.011 13.876 9.012 1.00 47.45 C ANISOU 2086 CG PRO A 277 7031 4948 6050 180 1176 -25 C ATOM 2087 CD PRO A 277 -0.260 13.490 9.722 1.00 46.64 C ANISOU 2087 CD PRO A 277 6890 4860 5973 170 1047 -25 C ATOM 2088 N LEU A 278 -0.845 16.944 8.934 1.00 47.90 N ANISOU 2088 N LEU A 278 7127 5016 6055 128 1028 38 N ATOM 2089 CA LEU A 278 -1.322 18.161 8.284 1.00 49.03 C ANISOU 2089 CA LEU A 278 7355 5135 6137 120 1000 61 C ATOM 2090 C LEU A 278 -1.885 19.132 9.359 1.00 49.91 C ANISOU 2090 C LEU A 278 7354 5285 6325 101 936 80 C ATOM 2091 O LEU A 278 -1.518 20.310 9.338 1.00 50.63 O ANISOU 2091 O LEU A 278 7445 5373 6419 89 979 103 O ATOM 2092 CB LEU A 278 -2.357 17.868 7.179 1.00 49.21 C ANISOU 2092 CB LEU A 278 7529 5110 6059 137 904 48 C ATOM 2093 CG LEU A 278 -2.914 19.102 6.445 1.00 50.11 C ANISOU 2093 CG LEU A 278 7754 5189 6098 140 856 72 C ATOM 2094 CD1 LEU A 278 -1.842 19.785 5.653 1.00 50.02 C ANISOU 2094 CD1 LEU A 278 7845 5143 6017 139 995 98 C ATOM 2095 CD2 LEU A 278 -4.089 18.723 5.555 1.00 50.79 C ANISOU 2095 CD2 LEU A 278 7966 5230 6103 164 718 49 C ATOM 2096 N ALA A 279 -2.687 18.632 10.337 1.00 49.46 N ANISOU 2096 N ALA A 279 7200 5258 6334 99 852 68 N ATOM 2097 CA ALA A 279 -3.173 19.474 11.453 1.00 49.63 C ANISOU 2097 CA ALA A 279 7114 5313 6429 84 808 82 C ATOM 2098 C ALA A 279 -1.996 20.021 12.309 1.00 50.00 C ANISOU 2098 C ALA A 279 7067 5394 6536 76 894 92 C ATOM 2099 O ALA A 279 -2.022 21.168 12.704 1.00 50.64 O ANISOU 2099 O ALA A 279 7113 5485 6644 63 890 107 O ATOM 2100 CB ALA A 279 -4.143 18.694 12.343 1.00 49.10 C ANISOU 2100 CB ALA A 279 6970 5264 6421 83 731 67 C ATOM 2101 N PHE A 280 -0.963 19.219 12.559 1.00 49.81 N ANISOU 2101 N PHE A 280 7004 5383 6539 85 964 79 N ATOM 2102 CA PHE A 280 0.182 19.612 13.377 1.00 50.47 C ANISOU 2102 CA PHE A 280 6988 5494 6694 82 1027 77 C ATOM 2103 C PHE A 280 1.229 20.444 12.653 1.00 52.99 C ANISOU 2103 C PHE A 280 7333 5789 7010 69 1128 83 C ATOM 2104 O PHE A 280 2.192 20.902 13.293 1.00 53.35 O ANISOU 2104 O PHE A 280 7285 5852 7133 62 1177 74 O ATOM 2105 CB PHE A 280 0.821 18.400 14.052 1.00 49.58 C ANISOU 2105 CB PHE A 280 6812 5400 6627 106 1043 57 C ATOM 2106 CG PHE A 280 -0.031 17.939 15.200 1.00 48.62 C ANISOU 2106 CG PHE A 280 6639 5303 6533 113 962 59 C ATOM 2107 CD1 PHE A 280 -1.066 17.049 14.996 1.00 48.71 C ANISOU 2107 CD1 PHE A 280 6695 5298 6513 115 909 56 C ATOM 2108 CD2 PHE A 280 0.115 18.498 16.456 1.00 48.87 C ANISOU 2108 CD2 PHE A 280 6583 5366 6618 113 938 61 C ATOM 2109 CE1 PHE A 280 -1.901 16.686 16.032 1.00 49.31 C ANISOU 2109 CE1 PHE A 280 6728 5388 6621 115 854 60 C ATOM 2110 CE2 PHE A 280 -0.703 18.108 17.502 1.00 49.59 C ANISOU 2110 CE2 PHE A 280 6646 5472 6724 120 881 66 C ATOM 2111 CZ PHE A 280 -1.704 17.197 17.285 1.00 49.28 C ANISOU 2111 CZ PHE A 280 6649 5414 6661 119 848 67 C ATOM 2112 N LEU A 281 1.036 20.687 11.320 1.00 54.25 N ANISOU 2112 N LEU A 281 7626 5904 7082 65 1161 95 N ATOM 2113 CA LEU A 281 1.878 21.617 10.557 1.00 54.87 C ANISOU 2113 CA LEU A 281 7755 5947 7148 47 1271 108 C ATOM 2114 C LEU A 281 1.721 23.023 11.190 1.00 55.99 C ANISOU 2114 C LEU A 281 7840 6098 7337 22 1247 126 C ATOM 2115 O LEU A 281 2.660 23.812 11.183 1.00 56.85 O ANISOU 2115 O LEU A 281 7914 6191 7497 -1 1338 129 O ATOM 2116 CB LEU A 281 1.497 21.611 9.068 1.00 55.05 C ANISOU 2116 CB LEU A 281 7961 5912 7043 55 1294 123 C ATOM 2117 CG LEU A 281 2.282 22.552 8.102 1.00 56.92 C ANISOU 2117 CG LEU A 281 8294 6094 7240 37 1426 145 C ATOM 2118 CD1 LEU A 281 3.809 22.425 8.275 1.00 57.73 C ANISOU 2118 CD1 LEU A 281 8302 6195 7436 22 1579 126 C ATOM 2119 CD2 LEU A 281 1.893 22.301 6.642 1.00 56.96 C ANISOU 2119 CD2 LEU A 281 8508 6038 7096 57 1442 155 C ATOM 2120 N ASN A 282 0.568 23.282 11.830 1.00 56.23 N ANISOU 2120 N ASN A 282 7845 6151 7368 26 1128 133 N ATOM 2121 CA ASN A 282 0.230 24.453 12.611 1.00 56.82 C ANISOU 2121 CA ASN A 282 7859 6240 7492 10 1085 144 C ATOM 2122 C ASN A 282 1.370 24.797 13.610 1.00 56.55 C ANISOU 2122 C ASN A 282 7693 6232 7562 -5 1138 126 C ATOM 2123 O ASN A 282 1.835 25.923 13.641 1.00 56.57 O ANISOU 2123 O ASN A 282 7678 6214 7600 -30 1182 132 O ATOM 2124 CB ASN A 282 -1.105 24.164 13.327 1.00 58.25 C ANISOU 2124 CB ASN A 282 8008 6449 7676 24 961 140 C ATOM 2125 CG ASN A 282 -1.366 24.986 14.543 1.00 62.78 C ANISOU 2125 CG ASN A 282 8485 7050 8317 15 920 139 C ATOM 2126 OD1 ASN A 282 -1.471 24.454 15.655 1.00 64.13 O ANISOU 2126 OD1 ASN A 282 8572 7260 8536 24 888 122 O ATOM 2127 ND2 ASN A 282 -1.445 26.296 14.343 1.00 63.82 N ANISOU 2127 ND2 ASN A 282 8644 7157 8449 1 925 155 N ATOM 2128 N SER A 283 1.838 23.822 14.376 1.00 56.36 N ANISOU 2128 N SER A 283 7584 6244 7588 12 1130 100 N ATOM 2129 CA SER A 283 2.892 24.019 15.373 1.00 56.20 C ANISOU 2129 CA SER A 283 7439 6247 7669 9 1153 74 C ATOM 2130 C SER A 283 4.260 24.388 14.780 1.00 55.01 C ANISOU 2130 C SER A 283 7263 6065 7575 -11 1274 61 C ATOM 2131 O SER A 283 5.104 24.948 15.470 1.00 54.46 O ANISOU 2131 O SER A 283 7088 6000 7603 -24 1290 36 O ATOM 2132 CB SER A 283 2.985 22.794 16.277 1.00 58.25 C ANISOU 2132 CB SER A 283 7636 6543 7953 43 1104 52 C ATOM 2133 OG SER A 283 1.708 22.532 16.850 1.00 61.23 O ANISOU 2133 OG SER A 283 8035 6941 8290 54 1013 65 O ATOM 2134 N ALA A 284 4.467 24.107 13.497 1.00 54.64 N ANISOU 2134 N ALA A 284 7314 5978 7470 -15 1361 73 N ATOM 2135 CA ALA A 284 5.707 24.463 12.804 1.00 54.69 C ANISOU 2135 CA ALA A 284 7309 5942 7528 -38 1504 63 C ATOM 2136 C ALA A 284 5.603 25.856 12.148 1.00 54.88 C ANISOU 2136 C ALA A 284 7408 5916 7527 -78 1563 94 C ATOM 2137 O ALA A 284 6.615 26.539 12.009 1.00 55.24 O ANISOU 2137 O ALA A 284 7403 5929 7658 -110 1670 83 O ATOM 2138 CB ALA A 284 6.048 23.410 11.752 1.00 54.27 C ANISOU 2138 CB ALA A 284 7338 5864 7419 -19 1589 59 C ATOM 2139 N VAL A 285 4.385 26.295 11.780 1.00 54.63 N ANISOU 2139 N VAL A 285 7491 5874 7390 -74 1490 130 N ATOM 2140 CA VAL A 285 4.202 27.592 11.131 1.00 54.76 C ANISOU 2140 CA VAL A 285 7601 5836 7371 -102 1534 165 C ATOM 2141 C VAL A 285 3.715 28.711 12.069 1.00 54.58 C ANISOU 2141 C VAL A 285 7511 5827 7399 -117 1450 169 C ATOM 2142 O VAL A 285 3.903 29.857 11.724 1.00 54.61 O ANISOU 2142 O VAL A 285 7556 5782 7413 -147 1506 189 O ATOM 2143 CB VAL A 285 3.311 27.502 9.871 1.00 55.37 C ANISOU 2143 CB VAL A 285 7875 5870 7294 -82 1519 202 C ATOM 2144 CG1 VAL A 285 3.896 26.519 8.847 1.00 55.72 C ANISOU 2144 CG1 VAL A 285 8006 5887 7278 -69 1622 196 C ATOM 2145 CG2 VAL A 285 1.878 27.139 10.233 1.00 55.44 C ANISOU 2145 CG2 VAL A 285 7901 5916 7249 -51 1352 205 C ATOM 2146 N ASN A 286 3.143 28.394 13.241 1.00 54.60 N ANISOU 2146 N ASN A 286 7419 5890 7436 -98 1330 149 N ATOM 2147 CA ASN A 286 2.679 29.319 14.301 1.00 54.67 C ANISOU 2147 CA ASN A 286 7357 5919 7497 -105 1248 143 C ATOM 2148 C ASN A 286 3.623 30.439 14.633 1.00 53.59 C ANISOU 2148 C ASN A 286 7150 5753 7458 -144 1312 129 C ATOM 2149 O ASN A 286 3.144 31.522 14.941 1.00 54.05 O ANISOU 2149 O ASN A 286 7217 5796 7525 -157 1273 140 O ATOM 2150 CB ASN A 286 2.484 28.565 15.624 1.00 57.02 C ANISOU 2150 CB ASN A 286 7545 6281 7837 -79 1157 111 C ATOM 2151 CG ASN A 286 1.150 28.043 15.829 1.00 63.49 C ANISOU 2151 CG ASN A 286 8405 7127 8592 -51 1059 123 C ATOM 2152 OD1 ASN A 286 0.180 28.497 15.211 1.00 67.77 O ANISOU 2152 OD1 ASN A 286 9034 7643 9072 -48 1024 150 O ATOM 2153 ND2 ASN A 286 1.066 27.060 16.683 1.00 63.66 N ANISOU 2153 ND2 ASN A 286 8365 7193 8631 -27 1012 103 N ATOM 2154 N PRO A 287 4.952 30.214 14.698 1.00 52.34 N ANISOU 2154 N PRO A 287 6904 5588 7393 -163 1402 98 N ATOM 2155 CA PRO A 287 5.856 31.325 15.038 1.00 51.81 C ANISOU 2155 CA PRO A 287 6755 5487 7442 -207 1459 76 C ATOM 2156 C PRO A 287 5.717 32.554 14.139 1.00 51.03 C ANISOU 2156 C PRO A 287 6764 5314 7313 -244 1538 116 C ATOM 2157 O PRO A 287 6.169 33.612 14.523 1.00 51.60 O ANISOU 2157 O PRO A 287 6778 5354 7473 -281 1561 102 O ATOM 2158 CB PRO A 287 7.243 30.679 14.969 1.00 52.39 C ANISOU 2158 CB PRO A 287 6729 5557 7619 -216 1553 35 C ATOM 2159 CG PRO A 287 6.968 29.206 15.215 1.00 52.72 C ANISOU 2159 CG PRO A 287 6763 5657 7612 -165 1487 25 C ATOM 2160 CD PRO A 287 5.703 28.959 14.490 1.00 51.26 C ANISOU 2160 CD PRO A 287 6730 5471 7276 -145 1452 74 C ATOM 2161 N ILE A 288 5.050 32.439 12.983 1.00 50.73 N ANISOU 2161 N ILE A 288 6888 5241 7144 -232 1568 166 N ATOM 2162 CA ILE A 288 4.821 33.568 12.064 1.00 51.36 C ANISOU 2162 CA ILE A 288 7105 5242 7169 -256 1634 213 C ATOM 2163 C ILE A 288 3.979 34.673 12.734 1.00 51.20 C ANISOU 2163 C ILE A 288 7078 5217 7156 -256 1529 222 C ATOM 2164 O ILE A 288 4.147 35.837 12.411 1.00 51.02 O ANISOU 2164 O ILE A 288 7107 5127 7151 -288 1587 245 O ATOM 2165 CB ILE A 288 4.179 33.113 10.708 1.00 51.97 C ANISOU 2165 CB ILE A 288 7379 5283 7085 -227 1656 261 C ATOM 2166 CG1 ILE A 288 4.352 34.168 9.616 1.00 52.98 C ANISOU 2166 CG1 ILE A 288 7663 5310 7158 -254 1771 310 C ATOM 2167 CG2 ILE A 288 2.686 32.743 10.859 1.00 52.22 C ANISOU 2167 CG2 ILE A 288 7466 5355 7018 -176 1487 274 C ATOM 2168 CD1 ILE A 288 5.720 34.242 9.066 1.00 55.13 C ANISOU 2168 CD1 ILE A 288 7927 5527 7494 -299 1970 304 C ATOM 2169 N PHE A 289 3.085 34.305 13.665 1.00 50.78 N ANISOU 2169 N PHE A 289 6968 5232 7093 -220 1384 205 N ATOM 2170 CA PHE A 289 2.240 35.261 14.358 1.00 50.82 C ANISOU 2170 CA PHE A 289 6962 5237 7109 -213 1288 207 C ATOM 2171 C PHE A 289 3.026 36.269 15.199 1.00 50.82 C ANISOU 2171 C PHE A 289 6855 5219 7235 -254 1315 174 C ATOM 2172 O PHE A 289 2.546 37.397 15.397 1.00 51.30 O ANISOU 2172 O PHE A 289 6944 5243 7303 -262 1283 186 O ATOM 2173 CB PHE A 289 1.176 34.545 15.173 1.00 51.00 C ANISOU 2173 CB PHE A 289 6944 5332 7103 -168 1153 192 C ATOM 2174 CG PHE A 289 0.162 33.899 14.260 1.00 52.24 C ANISOU 2174 CG PHE A 289 7219 5484 7144 -131 1108 225 C ATOM 2175 CD1 PHE A 289 -0.759 34.674 13.559 1.00 53.32 C ANISOU 2175 CD1 PHE A 289 7474 5570 7214 -115 1066 262 C ATOM 2176 CD2 PHE A 289 0.143 32.527 14.078 1.00 52.67 C ANISOU 2176 CD2 PHE A 289 7272 5580 7162 -110 1099 215 C ATOM 2177 CE1 PHE A 289 -1.682 34.085 12.704 1.00 54.11 C ANISOU 2177 CE1 PHE A 289 7683 5661 7214 -78 1006 284 C ATOM 2178 CE2 PHE A 289 -0.772 31.938 13.216 1.00 53.68 C ANISOU 2178 CE2 PHE A 289 7508 5697 7190 -79 1049 238 C ATOM 2179 CZ PHE A 289 -1.678 32.719 12.533 1.00 53.93 C ANISOU 2179 CZ PHE A 289 7653 5680 7159 -62 998 269 C ATOM 2180 N TYR A 290 4.254 35.902 15.630 1.00 49.88 N ANISOU 2180 N TYR A 290 6616 5116 7220 -280 1373 130 N ATOM 2181 CA TYR A 290 5.137 36.810 16.372 1.00 50.14 C ANISOU 2181 CA TYR A 290 6538 5125 7390 -322 1396 87 C ATOM 2182 C TYR A 290 5.429 38.094 15.581 1.00 51.70 C ANISOU 2182 C TYR A 290 6810 5224 7609 -372 1501 118 C ATOM 2183 O TYR A 290 5.744 39.131 16.167 1.00 51.89 O ANISOU 2183 O TYR A 290 6775 5215 7727 -406 1496 92 O ATOM 2184 CB TYR A 290 6.482 36.119 16.659 1.00 49.10 C ANISOU 2184 CB TYR A 290 6274 5011 7372 -339 1452 35 C ATOM 2185 CG TYR A 290 6.500 35.313 17.934 1.00 49.02 C ANISOU 2185 CG TYR A 290 6151 5080 7393 -299 1331 -16 C ATOM 2186 CD1 TYR A 290 5.846 34.085 18.019 1.00 48.94 C ANISOU 2186 CD1 TYR A 290 6173 5132 7289 -248 1268 -2 C ATOM 2187 CD2 TYR A 290 7.157 35.779 19.063 1.00 49.50 C ANISOU 2187 CD2 TYR A 290 6085 5149 7574 -311 1275 -78 C ATOM 2188 CE1 TYR A 290 5.858 33.343 19.193 1.00 49.19 C ANISOU 2188 CE1 TYR A 290 6122 5227 7340 -209 1166 -43 C ATOM 2189 CE2 TYR A 290 7.165 35.050 20.249 1.00 49.84 C ANISOU 2189 CE2 TYR A 290 6051 5257 7628 -266 1158 -122 C ATOM 2190 CZ TYR A 290 6.518 33.832 20.308 1.00 50.34 C ANISOU 2190 CZ TYR A 290 6158 5378 7591 -215 1110 -101 C ATOM 2191 OH TYR A 290 6.633 33.092 21.457 1.00 51.89 O ANISOU 2191 OH TYR A 290 6290 5629 7798 -171 1009 -141 O ATOM 2192 N PHE A 291 5.385 37.991 14.249 1.00 52.64 N ANISOU 2192 N PHE A 291 7066 5292 7642 -377 1602 172 N ATOM 2193 CA PHE A 291 5.686 39.051 13.307 1.00 54.30 C ANISOU 2193 CA PHE A 291 7385 5398 7850 -421 1728 214 C ATOM 2194 C PHE A 291 4.449 39.818 12.818 1.00 55.66 C ANISOU 2194 C PHE A 291 7720 5528 7900 -392 1664 272 C ATOM 2195 O PHE A 291 4.578 40.681 11.957 1.00 56.87 O ANISOU 2195 O PHE A 291 7998 5587 8024 -418 1761 317 O ATOM 2196 CB PHE A 291 6.482 38.469 12.128 1.00 54.25 C ANISOU 2196 CB PHE A 291 7448 5349 7816 -440 1892 236 C ATOM 2197 CG PHE A 291 7.695 37.716 12.602 1.00 55.01 C ANISOU 2197 CG PHE A 291 7371 5482 8049 -462 1951 173 C ATOM 2198 CD1 PHE A 291 8.773 38.383 13.139 1.00 56.06 C ANISOU 2198 CD1 PHE A 291 7360 5579 8361 -520 2016 124 C ATOM 2199 CD2 PHE A 291 7.708 36.337 12.617 1.00 56.39 C ANISOU 2199 CD2 PHE A 291 7515 5726 8184 -420 1918 156 C ATOM 2200 CE1 PHE A 291 9.868 37.689 13.622 1.00 57.02 C ANISOU 2200 CE1 PHE A 291 7310 5733 8622 -532 2047 58 C ATOM 2201 CE2 PHE A 291 8.801 35.644 13.112 1.00 57.34 C ANISOU 2201 CE2 PHE A 291 7471 5878 8436 -431 1954 96 C ATOM 2202 CZ PHE A 291 9.884 36.327 13.595 1.00 56.98 C ANISOU 2202 CZ PHE A 291 7283 5796 8571 -484 2017 46 C ATOM 2203 N LEU A 292 3.275 39.555 13.387 1.00 55.43 N ANISOU 2203 N LEU A 292 7689 5561 7810 -338 1506 270 N ATOM 2204 CA LEU A 292 2.053 40.220 12.963 1.00 55.22 C ANISOU 2204 CA LEU A 292 7799 5497 7685 -302 1429 316 C ATOM 2205 C LEU A 292 1.403 41.070 14.044 1.00 55.17 C ANISOU 2205 C LEU A 292 7722 5504 7735 -291 1320 292 C ATOM 2206 O LEU A 292 0.239 41.440 13.871 1.00 55.92 O ANISOU 2206 O LEU A 292 7901 5584 7760 -248 1229 319 O ATOM 2207 CB LEU A 292 1.060 39.181 12.408 1.00 54.99 C ANISOU 2207 CB LEU A 292 7858 5511 7527 -241 1345 339 C ATOM 2208 CG LEU A 292 1.562 38.392 11.202 1.00 55.75 C ANISOU 2208 CG LEU A 292 8061 5581 7539 -243 1447 366 C ATOM 2209 CD1 LEU A 292 0.581 37.337 10.805 1.00 56.23 C ANISOU 2209 CD1 LEU A 292 8189 5687 7490 -185 1344 374 C ATOM 2210 CD2 LEU A 292 1.844 39.291 10.040 1.00 55.92 C ANISOU 2210 CD2 LEU A 292 8256 5490 7500 -263 1559 422 C ATOM 2211 N VAL A 293 2.140 41.420 15.132 1.00 54.25 N ANISOU 2211 N VAL A 293 7457 5407 7747 -327 1326 236 N ATOM 2212 CA VAL A 293 1.579 42.214 16.233 1.00 53.72 C ANISOU 2212 CA VAL A 293 7329 5351 7732 -316 1228 205 C ATOM 2213 C VAL A 293 2.150 43.664 16.306 1.00 53.92 C ANISOU 2213 C VAL A 293 7355 5285 7846 -368 1290 200 C ATOM 2214 O VAL A 293 2.129 44.286 17.361 1.00 54.20 O ANISOU 2214 O VAL A 293 7307 5328 7958 -374 1232 154 O ATOM 2215 CB VAL A 293 1.644 41.481 17.599 1.00 53.58 C ANISOU 2215 CB VAL A 293 7162 5428 7766 -298 1143 141 C ATOM 2216 CG1 VAL A 293 0.661 40.326 17.635 1.00 53.63 C ANISOU 2216 CG1 VAL A 293 7188 5508 7681 -240 1062 152 C ATOM 2217 CG2 VAL A 293 3.053 40.989 17.912 1.00 54.07 C ANISOU 2217 CG2 VAL A 293 7110 5510 7925 -338 1209 95 C ATOM 2218 N GLY A 294 2.591 44.193 15.173 1.00 53.89 N ANISOU 2218 N GLY A 294 7461 5190 7825 -403 1410 249 N ATOM 2219 CA GLY A 294 3.007 45.586 15.009 1.00 54.69 C ANISOU 2219 CA GLY A 294 7601 5185 7995 -453 1484 260 C ATOM 2220 C GLY A 294 4.175 46.194 15.766 1.00 55.62 C ANISOU 2220 C GLY A 294 7577 5274 8282 -523 1542 198 C ATOM 2221 O GLY A 294 4.393 47.405 15.686 1.00 56.00 O ANISOU 2221 O GLY A 294 7659 5228 8392 -564 1593 205 O ATOM 2222 N ASP A 295 4.962 45.383 16.461 1.00 55.72 N ANISOU 2222 N ASP A 295 7435 5357 8378 -537 1534 135 N ATOM 2223 CA ASP A 295 6.083 45.848 17.279 1.00 55.78 C ANISOU 2223 CA ASP A 295 7288 5344 8560 -596 1558 60 C ATOM 2224 C ASP A 295 7.434 45.896 16.586 1.00 57.34 C ANISOU 2224 C ASP A 295 7444 5474 8870 -670 1731 54 C ATOM 2225 O ASP A 295 8.422 46.286 17.219 1.00 57.94 O ANISOU 2225 O ASP A 295 7376 5524 9113 -723 1752 -16 O ATOM 2226 CB ASP A 295 6.194 44.940 18.505 1.00 55.89 C ANISOU 2226 CB ASP A 295 7158 5470 8609 -561 1435 -12 C ATOM 2227 CG ASP A 295 6.255 43.450 18.198 1.00 56.76 C ANISOU 2227 CG ASP A 295 7255 5660 8650 -524 1437 -1 C ATOM 2228 OD1 ASP A 295 6.384 43.089 17.016 1.00 56.42 O ANISOU 2228 OD1 ASP A 295 7301 5588 8550 -533 1546 53 O ATOM 2229 OD2 ASP A 295 6.185 42.657 19.135 1.00 58.26 O ANISOU 2229 OD2 ASP A 295 7358 5936 8842 -485 1333 -46 O ATOM 2230 N HIS A 296 7.505 45.444 15.317 1.00 57.74 N ANISOU 2230 N HIS A 296 7613 5493 8834 -672 1855 119 N ATOM 2231 CA HIS A 296 8.753 45.367 14.558 1.00 58.16 C ANISOU 2231 CA HIS A 296 7637 5478 8982 -738 2046 118 C ATOM 2232 C HIS A 296 9.716 44.371 15.193 1.00 58.78 C ANISOU 2232 C HIS A 296 7520 5630 9182 -745 2034 40 C ATOM 2233 O HIS A 296 10.914 44.628 15.242 1.00 58.76 O ANISOU 2233 O HIS A 296 7394 5575 9355 -811 2140 -10 O ATOM 2234 CB HIS A 296 9.399 46.749 14.355 1.00 58.39 C ANISOU 2234 CB HIS A 296 7672 5377 9139 -821 2169 117 C ATOM 2235 CG HIS A 296 8.650 47.626 13.399 1.00 60.95 C ANISOU 2235 CG HIS A 296 8220 5605 9335 -816 2227 209 C ATOM 2236 ND1 HIS A 296 9.021 47.733 12.070 1.00 62.93 N ANISOU 2236 ND1 HIS A 296 8620 5759 9530 -847 2420 278 N ATOM 2237 CD2 HIS A 296 7.572 48.414 13.613 1.00 62.64 C ANISOU 2237 CD2 HIS A 296 8535 5802 9465 -778 2115 241 C ATOM 2238 CE1 HIS A 296 8.171 48.587 11.524 1.00 63.67 C ANISOU 2238 CE1 HIS A 296 8908 5779 9505 -825 2409 350 C ATOM 2239 NE2 HIS A 296 7.288 49.034 12.416 1.00 63.95 N ANISOU 2239 NE2 HIS A 296 8913 5858 9528 -783 2226 329 N ATOM 2240 N PHE A 297 9.183 43.235 15.689 1.00 59.37 N ANISOU 2240 N PHE A 297 7566 5821 9173 -675 1903 26 N ATOM 2241 CA PHE A 297 9.977 42.175 16.310 1.00 60.64 C ANISOU 2241 CA PHE A 297 7560 6055 9426 -663 1869 -43 C ATOM 2242 C PHE A 297 10.967 41.568 15.324 1.00 64.65 C ANISOU 2242 C PHE A 297 8055 6526 9984 -696 2048 -35 C ATOM 2243 O PHE A 297 12.080 41.254 15.729 1.00 64.89 O ANISOU 2243 O PHE A 297 7914 6560 10180 -722 2079 -106 O ATOM 2244 CB PHE A 297 9.083 41.077 16.901 1.00 58.80 C ANISOU 2244 CB PHE A 297 7335 5938 9068 -580 1710 -42 C ATOM 2245 CG PHE A 297 9.785 39.888 17.527 1.00 57.08 C ANISOU 2245 CG PHE A 297 6974 5795 8919 -554 1662 -103 C ATOM 2246 CD1 PHE A 297 10.641 40.055 18.600 1.00 56.48 C ANISOU 2246 CD1 PHE A 297 6726 5729 9004 -570 1595 -190 C ATOM 2247 CD2 PHE A 297 9.531 38.601 17.086 1.00 56.64 C ANISOU 2247 CD2 PHE A 297 6962 5797 8762 -507 1665 -77 C ATOM 2248 CE1 PHE A 297 11.233 38.962 19.210 1.00 56.48 C ANISOU 2248 CE1 PHE A 297 6606 5794 9059 -533 1530 -246 C ATOM 2249 CE2 PHE A 297 10.115 37.508 17.708 1.00 56.54 C ANISOU 2249 CE2 PHE A 297 6827 5849 8806 -475 1609 -131 C ATOM 2250 CZ PHE A 297 10.963 37.695 18.762 1.00 56.24 C ANISOU 2250 CZ PHE A 297 6624 5819 8925 -486 1541 -213 C ATOM 2251 N ARG A 298 10.604 41.444 14.024 1.00 67.40 N ANISOU 2251 N ARG A 298 8582 6829 10196 -692 2169 45 N ATOM 2252 CA ARG A 298 11.526 40.916 13.006 1.00 70.34 C ANISOU 2252 CA ARG A 298 8966 7155 10603 -722 2364 56 C ATOM 2253 C ARG A 298 12.774 41.787 12.920 1.00 72.48 C ANISOU 2253 C ARG A 298 9128 7325 11085 -813 2525 16 C ATOM 2254 O ARG A 298 13.889 41.279 12.858 1.00 72.75 O ANISOU 2254 O ARG A 298 9025 7352 11267 -842 2627 -36 O ATOM 2255 CB ARG A 298 10.856 40.866 11.627 1.00 73.00 C ANISOU 2255 CB ARG A 298 9552 7443 10742 -703 2462 151 C ATOM 2256 CG ARG A 298 11.766 40.295 10.528 1.00 78.46 C ANISOU 2256 CG ARG A 298 10284 8081 11448 -730 2679 164 C ATOM 2257 CD ARG A 298 11.572 40.979 9.184 1.00 84.26 C ANISOU 2257 CD ARG A 298 11256 8698 12060 -754 2847 250 C ATOM 2258 NE ARG A 298 10.160 40.981 8.783 1.00 90.33 N ANISOU 2258 NE ARG A 298 12235 9488 12599 -686 2718 319 N ATOM 2259 CZ ARG A 298 9.615 41.863 7.949 1.00 94.41 C ANISOU 2259 CZ ARG A 298 12969 9910 12992 -688 2771 395 C ATOM 2260 NH1 ARG A 298 10.359 42.819 7.403 1.00 94.71 N ANISOU 2260 NH1 ARG A 298 13059 9823 13104 -759 2968 419 N ATOM 2261 NH2 ARG A 298 8.322 41.797 7.655 1.00 94.86 N ANISOU 2261 NH2 ARG A 298 13193 9990 12858 -619 2628 446 N ATOM 2262 N ASP A 299 12.575 43.102 12.958 1.00 73.86 N ANISOU 2262 N ASP A 299 9356 7420 11288 -858 2543 36 N ATOM 2263 CA ASP A 299 13.643 44.082 12.923 1.00 75.67 C ANISOU 2263 CA ASP A 299 9487 7540 11724 -951 2689 -1 C ATOM 2264 C ASP A 299 14.436 43.999 14.242 1.00 77.18 C ANISOU 2264 C ASP A 299 9413 7780 12134 -968 2573 -117 C ATOM 2265 O ASP A 299 15.658 44.036 14.210 1.00 77.33 O ANISOU 2265 O ASP A 299 9275 7746 12361 -1029 2694 -178 O ATOM 2266 CB ASP A 299 13.060 45.498 12.682 1.00 77.28 C ANISOU 2266 CB ASP A 299 9834 7648 11881 -984 2710 54 C ATOM 2267 CG ASP A 299 12.134 45.621 11.466 1.00 80.80 C ANISOU 2267 CG ASP A 299 10562 8047 12091 -950 2778 168 C ATOM 2268 OD1 ASP A 299 12.383 46.497 10.625 1.00 81.95 O ANISOU 2268 OD1 ASP A 299 10832 8064 12240 -1005 2953 220 O ATOM 2269 OD2 ASP A 299 11.136 44.853 11.381 1.00 81.47 O ANISOU 2269 OD2 ASP A 299 10745 8219 11990 -867 2649 204 O ATOM 2270 N MET A 300 13.749 43.828 15.382 1.00 78.42 N ANISOU 2270 N MET A 300 9520 8032 12242 -909 2341 -151 N ATOM 2271 CA MET A 300 14.364 43.685 16.701 1.00 80.33 C ANISOU 2271 CA MET A 300 9543 8325 12652 -905 2196 -260 C ATOM 2272 C MET A 300 15.259 42.456 16.773 1.00 82.34 C ANISOU 2272 C MET A 300 9652 8633 13000 -885 2214 -314 C ATOM 2273 O MET A 300 16.308 42.504 17.410 1.00 82.60 O ANISOU 2273 O MET A 300 9484 8651 13249 -915 2194 -409 O ATOM 2274 CB MET A 300 13.288 43.595 17.798 1.00 81.26 C ANISOU 2274 CB MET A 300 9689 8538 12648 -832 1959 -269 C ATOM 2275 CG MET A 300 12.747 44.949 18.248 1.00 83.97 C ANISOU 2275 CG MET A 300 10084 8827 12993 -857 1900 -266 C ATOM 2276 SD MET A 300 11.271 44.873 19.304 1.00 87.97 S ANISOU 2276 SD MET A 300 10668 9432 13324 -767 1664 -258 S ATOM 2277 CE MET A 300 11.799 43.723 20.497 1.00 85.92 C ANISOU 2277 CE MET A 300 10240 9278 13127 -715 1513 -349 C ATOM 2278 N LEU A 301 14.843 41.358 16.119 1.00 83.66 N ANISOU 2278 N LEU A 301 9920 8856 13011 -830 2245 -259 N ATOM 2279 CA LEU A 301 15.551 40.079 16.067 1.00 85.36 C ANISOU 2279 CA LEU A 301 10027 9122 13284 -799 2267 -299 C ATOM 2280 C LEU A 301 16.884 40.221 15.331 1.00 87.78 C ANISOU 2280 C LEU A 301 10229 9334 13789 -873 2491 -332 C ATOM 2281 O LEU A 301 17.897 39.696 15.790 1.00 87.94 O ANISOU 2281 O LEU A 301 10050 9368 13995 -873 2478 -417 O ATOM 2282 CB LEU A 301 14.682 39.019 15.357 1.00 84.95 C ANISOU 2282 CB LEU A 301 10143 9131 13002 -732 2271 -222 C ATOM 2283 CG LEU A 301 14.088 37.911 16.215 1.00 85.44 C ANISOU 2283 CG LEU A 301 10181 9313 12968 -644 2070 -239 C ATOM 2284 CD1 LEU A 301 13.257 36.991 15.378 1.00 85.41 C ANISOU 2284 CD1 LEU A 301 10346 9349 12759 -593 2095 -165 C ATOM 2285 CD2 LEU A 301 15.160 37.115 16.905 1.00 86.28 C ANISOU 2285 CD2 LEU A 301 10083 9456 13245 -626 2018 -330 C ATOM 2286 N PHE A 302 16.883 40.944 14.203 1.00 89.47 N ANISOU 2286 N PHE A 302 10579 9447 13970 -933 2696 -265 N ATOM 2287 CA PHE A 302 18.066 41.167 13.368 1.00 91.57 C ANISOU 2287 CA PHE A 302 10778 9605 14410 -1011 2952 -283 C ATOM 2288 C PHE A 302 19.089 42.076 14.040 1.00 93.04 C ANISOU 2288 C PHE A 302 10746 9719 14884 -1091 2968 -376 C ATOM 2289 O PHE A 302 20.283 41.904 13.830 1.00 93.48 O ANISOU 2289 O PHE A 302 10639 9720 15160 -1140 3113 -438 O ATOM 2290 CB PHE A 302 17.666 41.725 11.992 1.00 92.13 C ANISOU 2290 CB PHE A 302 11095 9579 14330 -1046 3164 -175 C ATOM 2291 CG PHE A 302 16.834 40.819 11.104 1.00 93.68 C ANISOU 2291 CG PHE A 302 11511 9822 14262 -976 3184 -90 C ATOM 2292 CD1 PHE A 302 16.389 39.586 11.557 1.00 94.80 C ANISOU 2292 CD1 PHE A 302 11624 10088 14306 -890 3017 -106 C ATOM 2293 CD2 PHE A 302 16.495 41.205 9.817 1.00 95.00 C ANISOU 2293 CD2 PHE A 302 11920 9900 14274 -994 3364 4 C ATOM 2294 CE1 PHE A 302 15.608 38.766 10.746 1.00 95.82 C ANISOU 2294 CE1 PHE A 302 11950 10253 14202 -829 3026 -35 C ATOM 2295 CE2 PHE A 302 15.726 40.374 9.001 1.00 95.94 C ANISOU 2295 CE2 PHE A 302 12245 10058 14149 -926 3364 74 C ATOM 2296 CZ PHE A 302 15.288 39.162 9.472 1.00 95.73 C ANISOU 2296 CZ PHE A 302 12173 10156 14043 -846 3194 51 C ATOM 2297 N SER A 303 18.631 43.026 14.861 1.00 93.92 N ANISOU 2297 N SER A 303 10850 9829 15007 -1103 2817 -393 N ATOM 2298 CA SER A 303 19.501 43.934 15.612 1.00 95.20 C ANISOU 2298 CA SER A 303 10809 9924 15437 -1175 2794 -491 C ATOM 2299 C SER A 303 20.384 43.142 16.609 1.00 96.61 C ANISOU 2299 C SER A 303 10729 10169 15810 -1142 2652 -614 C ATOM 2300 O SER A 303 21.554 43.485 16.789 1.00 97.20 O ANISOU 2300 O SER A 303 10596 10172 16165 -1208 2720 -705 O ATOM 2301 CB SER A 303 18.665 44.982 16.347 1.00 95.94 C ANISOU 2301 CB SER A 303 10974 10016 15463 -1175 2634 -483 C ATOM 2302 OG SER A 303 19.473 45.871 17.100 1.00 97.72 O ANISOU 2302 OG SER A 303 11015 10171 15943 -1246 2603 -581 O ATOM 2303 N LYS A 304 19.827 42.065 17.218 1.00 96.94 N ANISOU 2303 N LYS A 304 10786 10340 15708 -1040 2458 -616 N ATOM 2304 CA LYS A 304 20.528 41.180 18.157 1.00 97.55 C ANISOU 2304 CA LYS A 304 10655 10484 15924 -987 2300 -720 C ATOM 2305 C LYS A 304 21.294 40.082 17.387 1.00 97.86 C ANISOU 2305 C LYS A 304 10623 10523 16036 -976 2456 -727 C ATOM 2306 O LYS A 304 22.518 39.956 17.485 1.00 97.88 O ANISOU 2306 O LYS A 304 10401 10489 16298 -1000 2488 -825 O ATOM 2307 CB LYS A 304 19.519 40.530 19.126 1.00 99.43 C ANISOU 2307 CB LYS A 304 10971 10850 15958 -882 2042 -707 C ATOM 2308 CG LYS A 304 19.050 41.439 20.259 1.00103.81 C ANISOU 2308 CG LYS A 304 11524 11415 16505 -878 1844 -745 C ATOM 2309 CD LYS A 304 19.743 41.129 21.583 1.00108.61 C ANISOU 2309 CD LYS A 304 11936 12061 17270 -838 1630 -870 C ATOM 2310 CE LYS A 304 19.443 42.182 22.630 1.00112.43 C ANISOU 2310 CE LYS A 304 12416 12529 17771 -848 1464 -919 C ATOM 2311 NZ LYS A 304 20.248 41.987 23.868 1.00114.55 N ANISOU 2311 NZ LYS A 304 12501 12818 18205 -812 1254 -1049 N TER 2312 LYS A 304 ATOM 2313 N GLU B 9 18.703 59.920 14.838 1.00 85.59 N ANISOU 2313 N GLU B 9 9765 8398 14355 -2024 4599 -1565 N ATOM 2314 CA GLU B 9 19.459 60.785 15.743 1.00 85.68 C ANISOU 2314 CA GLU B 9 9403 8381 14770 -2044 4524 -1703 C ATOM 2315 C GLU B 9 18.710 62.071 16.152 1.00 84.93 C ANISOU 2315 C GLU B 9 9585 8328 14356 -2065 4346 -1467 C ATOM 2316 O GLU B 9 19.024 63.146 15.627 1.00 86.16 O ANISOU 2316 O GLU B 9 9921 8333 14482 -2288 4721 -1501 O ATOM 2317 CB GLU B 9 20.832 61.141 15.126 1.00 88.30 C ANISOU 2317 CB GLU B 9 9487 8497 15564 -2300 5106 -2060 C ATOM 2318 N VAL B 10 17.768 61.989 17.107 1.00 82.88 N ANISOU 2318 N VAL B 10 9357 8243 13892 -1846 3816 -1247 N ATOM 2319 CA VAL B 10 17.063 63.188 17.577 1.00 81.62 C ANISOU 2319 CA VAL B 10 9411 8114 13488 -1854 3642 -1056 C ATOM 2320 C VAL B 10 17.090 63.336 19.109 1.00 79.40 C ANISOU 2320 C VAL B 10 8795 7960 13412 -1677 3171 -1074 C ATOM 2321 O VAL B 10 17.125 62.344 19.839 1.00 79.34 O ANISOU 2321 O VAL B 10 8557 8060 13528 -1479 2848 -1097 O ATOM 2322 CB VAL B 10 15.616 63.351 17.030 1.00 82.87 C ANISOU 2322 CB VAL B 10 10108 8319 13060 -1814 3536 -738 C ATOM 2323 CG1 VAL B 10 15.595 63.432 15.503 1.00 83.69 C ANISOU 2323 CG1 VAL B 10 10636 8280 12883 -1995 3979 -712 C ATOM 2324 CG2 VAL B 10 14.692 62.250 17.540 1.00 83.26 C ANISOU 2324 CG2 VAL B 10 10149 8540 12946 -1584 3125 -602 C ATOM 2325 N GLN B 11 17.083 64.598 19.583 1.00 77.24 N ANISOU 2325 N GLN B 11 8537 7655 13157 -1753 3145 -1065 N ATOM 2326 CA GLN B 11 17.025 64.959 21.002 1.00 75.53 C ANISOU 2326 CA GLN B 11 8090 7551 13056 -1617 2722 -1083 C ATOM 2327 C GLN B 11 15.693 65.670 21.229 1.00 72.15 C ANISOU 2327 C GLN B 11 8039 7177 12198 -1576 2548 -801 C ATOM 2328 O GLN B 11 15.313 66.492 20.400 1.00 72.46 O ANISOU 2328 O GLN B 11 8402 7099 12029 -1716 2812 -690 O ATOM 2329 CB GLN B 11 18.157 65.912 21.390 1.00 78.75 C ANISOU 2329 CB GLN B 11 8157 7861 13904 -1758 2854 -1369 C ATOM 2330 CG GLN B 11 19.526 65.514 20.866 1.00 87.08 C ANISOU 2330 CG GLN B 11 8839 8794 15452 -1872 3174 -1701 C ATOM 2331 CD GLN B 11 20.329 64.773 21.902 1.00 94.99 C ANISOU 2331 CD GLN B 11 9320 9885 16887 -1686 2785 -1947 C ATOM 2332 OE1 GLN B 11 20.251 63.543 22.016 1.00 97.57 O ANISOU 2332 OE1 GLN B 11 9527 10271 17275 -1511 2610 -1951 O ATOM 2333 NE2 GLN B 11 21.125 65.508 22.677 1.00 96.14 N ANISOU 2333 NE2 GLN B 11 9156 10028 17346 -1710 2624 -2166 N ATOM 2334 N LEU B 12 14.990 65.380 22.343 1.00 68.72 N ANISOU 2334 N LEU B 12 7581 6895 11636 -1385 2119 -693 N ATOM 2335 CA LEU B 12 13.705 66.026 22.625 1.00 65.95 C ANISOU 2335 CA LEU B 12 7532 6584 10941 -1342 1964 -469 C ATOM 2336 C LEU B 12 13.744 66.930 23.843 1.00 63.25 C ANISOU 2336 C LEU B 12 7059 6282 10693 -1322 1746 -534 C ATOM 2337 O LEU B 12 14.404 66.617 24.827 1.00 63.52 O ANISOU 2337 O LEU B 12 6805 6392 10938 -1238 1518 -690 O ATOM 2338 CB LEU B 12 12.589 64.990 22.814 1.00 65.56 C ANISOU 2338 CB LEU B 12 7640 6654 10616 -1170 1723 -283 C ATOM 2339 CG LEU B 12 12.391 63.997 21.673 1.00 66.33 C ANISOU 2339 CG LEU B 12 7877 6731 10596 -1173 1887 -229 C ATOM 2340 CD1 LEU B 12 11.404 62.923 22.047 1.00 66.48 C ANISOU 2340 CD1 LEU B 12 7970 6854 10434 -1008 1644 -102 C ATOM 2341 CD2 LEU B 12 11.987 64.694 20.398 1.00 66.86 C ANISOU 2341 CD2 LEU B 12 8280 6686 10439 -1307 2155 -135 C ATOM 2342 N VAL B 13 13.024 68.048 23.785 1.00 60.59 N ANISOU 2342 N VAL B 13 6948 5882 10191 -1387 1795 -424 N ATOM 2343 CA VAL B 13 12.898 68.946 24.923 1.00 59.27 C ANISOU 2343 CA VAL B 13 6697 5744 10077 -1375 1606 -485 C ATOM 2344 C VAL B 13 11.420 69.326 25.049 1.00 57.97 C ANISOU 2344 C VAL B 13 6833 5596 9599 -1303 1490 -265 C ATOM 2345 O VAL B 13 10.868 69.876 24.101 1.00 58.64 O ANISOU 2345 O VAL B 13 7178 5559 9542 -1363 1667 -130 O ATOM 2346 CB VAL B 13 13.770 70.235 24.812 1.00 59.58 C ANISOU 2346 CB VAL B 13 6620 5630 10388 -1568 1845 -666 C ATOM 2347 CG1 VAL B 13 13.448 71.201 25.945 1.00 59.89 C ANISOU 2347 CG1 VAL B 13 6621 5695 10439 -1556 1647 -722 C ATOM 2348 CG2 VAL B 13 15.263 69.919 24.791 1.00 59.97 C ANISOU 2348 CG2 VAL B 13 6290 5653 10844 -1647 1957 -955 C ATOM 2349 N GLU B 14 10.785 69.068 26.200 1.00 56.31 N ANISOU 2349 N GLU B 14 6600 5510 9284 -1176 1202 -241 N ATOM 2350 CA GLU B 14 9.398 69.495 26.424 1.00 55.48 C ANISOU 2350 CA GLU B 14 6717 5402 8960 -1120 1118 -91 C ATOM 2351 C GLU B 14 9.404 70.887 27.047 1.00 54.92 C ANISOU 2351 C GLU B 14 6630 5257 8981 -1197 1128 -178 C ATOM 2352 O GLU B 14 10.269 71.207 27.866 1.00 54.66 O ANISOU 2352 O GLU B 14 6393 5257 9119 -1238 1061 -366 O ATOM 2353 CB GLU B 14 8.623 68.564 27.376 1.00 56.78 C ANISOU 2353 CB GLU B 14 6899 5705 8971 -975 882 -38 C ATOM 2354 CG GLU B 14 8.552 67.116 26.952 1.00 60.09 C ANISOU 2354 CG GLU B 14 7328 6186 9318 -889 856 37 C ATOM 2355 CD GLU B 14 9.740 66.279 27.373 1.00 63.56 C ANISOU 2355 CD GLU B 14 7560 6686 9904 -843 768 -77 C ATOM 2356 OE1 GLU B 14 9.655 65.043 27.245 1.00 66.59 O ANISOU 2356 OE1 GLU B 14 7953 7109 10240 -753 722 -19 O ATOM 2357 OE2 GLU B 14 10.745 66.838 27.860 1.00 63.48 O ANISOU 2357 OE2 GLU B 14 7364 6673 10083 -887 725 -242 O ATOM 2358 N SER B 15 8.411 71.694 26.688 1.00 54.35 N ANISOU 2358 N SER B 15 6763 5079 8808 -1201 1184 -59 N ATOM 2359 CA SER B 15 8.257 73.027 27.231 1.00 54.49 C ANISOU 2359 CA SER B 15 6791 4996 8916 -1265 1209 -129 C ATOM 2360 C SER B 15 6.760 73.417 27.338 1.00 54.43 C ANISOU 2360 C SER B 15 6962 4943 8775 -1173 1126 -6 C ATOM 2361 O SER B 15 5.895 72.732 26.794 1.00 54.80 O ANISOU 2361 O SER B 15 7127 5018 8678 -1075 1067 131 O ATOM 2362 CB SER B 15 9.078 74.038 26.430 1.00 55.86 C ANISOU 2362 CB SER B 15 6993 4972 9259 -1423 1477 -173 C ATOM 2363 OG SER B 15 8.385 74.564 25.312 1.00 58.27 O ANISOU 2363 OG SER B 15 7597 5100 9443 -1420 1610 21 O ATOM 2364 N GLY B 16 6.466 74.465 28.099 1.00 53.85 N ANISOU 2364 N GLY B 16 6874 4803 8786 -1202 1114 -93 N ATOM 2365 CA GLY B 16 5.103 74.933 28.282 1.00 53.56 C ANISOU 2365 CA GLY B 16 6952 4697 8703 -1119 1052 -28 C ATOM 2366 C GLY B 16 4.487 74.654 29.634 1.00 53.65 C ANISOU 2366 C GLY B 16 6886 4832 8666 -1072 929 -136 C ATOM 2367 O GLY B 16 3.376 75.111 29.901 1.00 53.70 O ANISOU 2367 O GLY B 16 6943 4767 8693 -1020 915 -135 O ATOM 2368 N GLY B 17 5.172 73.889 30.474 1.00 53.93 N ANISOU 2368 N GLY B 17 6820 5035 8637 -1082 843 -232 N ATOM 2369 CA GLY B 17 4.653 73.549 31.794 1.00 55.01 C ANISOU 2369 CA GLY B 17 6966 5278 8658 -1046 748 -321 C ATOM 2370 C GLY B 17 4.430 74.757 32.683 1.00 55.57 C ANISOU 2370 C GLY B 17 7034 5275 8804 -1112 784 -482 C ATOM 2371 O GLY B 17 5.239 75.686 32.675 1.00 56.15 O ANISOU 2371 O GLY B 17 7032 5277 9026 -1204 826 -592 O ATOM 2372 N GLY B 18 3.339 74.754 33.441 1.00 55.17 N ANISOU 2372 N GLY B 18 7058 5225 8680 -1080 801 -521 N ATOM 2373 CA GLY B 18 3.023 75.870 34.316 1.00 55.11 C ANISOU 2373 CA GLY B 18 7056 5138 8744 -1146 863 -697 C ATOM 2374 C GLY B 18 1.923 75.567 35.299 1.00 55.75 C ANISOU 2374 C GLY B 18 7231 5245 8706 -1126 918 -767 C ATOM 2375 O GLY B 18 1.646 74.407 35.571 1.00 56.50 O ANISOU 2375 O GLY B 18 7403 5443 8620 -1077 892 -698 O ATOM 2376 N LEU B 19 1.332 76.607 35.888 1.00 55.92 N ANISOU 2376 N LEU B 19 7255 5154 8837 -1178 1027 -923 N ATOM 2377 CA LEU B 19 0.255 76.505 36.860 1.00 56.42 C ANISOU 2377 CA LEU B 19 7403 5202 8831 -1192 1155 -1041 C ATOM 2378 C LEU B 19 -1.030 76.910 36.184 1.00 58.01 C ANISOU 2378 C LEU B 19 7515 5227 9298 -1130 1264 -1015 C ATOM 2379 O LEU B 19 -1.114 77.956 35.565 1.00 57.88 O ANISOU 2379 O LEU B 19 7418 5050 9522 -1114 1269 -1018 O ATOM 2380 CB LEU B 19 0.519 77.428 38.057 1.00 56.42 C ANISOU 2380 CB LEU B 19 7459 5188 8788 -1299 1210 -1288 C ATOM 2381 CG LEU B 19 -0.564 77.450 39.143 1.00 56.98 C ANISOU 2381 CG LEU B 19 7651 5219 8781 -1347 1410 -1453 C ATOM 2382 CD1 LEU B 19 -0.758 76.087 39.753 1.00 57.05 C ANISOU 2382 CD1 LEU B 19 7855 5358 8462 -1331 1426 -1386 C ATOM 2383 CD2 LEU B 19 -0.224 78.440 40.215 1.00 57.40 C ANISOU 2383 CD2 LEU B 19 7770 5252 8787 -1459 1459 -1712 C ATOM 2384 N VAL B 20 -2.033 76.059 36.282 1.00 59.82 N ANISOU 2384 N VAL B 20 7757 5467 9505 -1088 1344 -997 N ATOM 2385 CA VAL B 20 -3.344 76.235 35.663 1.00 60.95 C ANISOU 2385 CA VAL B 20 7770 5455 9935 -1008 1406 -1009 C ATOM 2386 C VAL B 20 -4.411 76.154 36.756 1.00 61.86 C ANISOU 2386 C VAL B 20 7891 5514 10097 -1073 1649 -1225 C ATOM 2387 O VAL B 20 -4.276 75.359 37.683 1.00 62.22 O ANISOU 2387 O VAL B 20 8100 5671 9869 -1152 1758 -1263 O ATOM 2388 CB VAL B 20 -3.544 75.106 34.616 1.00 61.79 C ANISOU 2388 CB VAL B 20 7842 5622 10015 -911 1291 -821 C ATOM 2389 CG1 VAL B 20 -4.869 75.238 33.897 1.00 62.32 C ANISOU 2389 CG1 VAL B 20 7751 5537 10393 -805 1280 -857 C ATOM 2390 CG2 VAL B 20 -2.396 75.055 33.604 1.00 62.61 C ANISOU 2390 CG2 VAL B 20 7980 5787 10024 -877 1110 -624 C ATOM 2391 N GLN B 21 -5.436 76.994 36.687 1.00 62.40 N ANISOU 2391 N GLN B 21 7807 5391 10511 -1042 1748 -1376 N ATOM 2392 CA GLN B 21 -6.555 76.900 37.627 1.00 63.74 C ANISOU 2392 CA GLN B 21 7943 5477 10800 -1114 2035 -1617 C ATOM 2393 C GLN B 21 -7.469 75.750 37.081 1.00 64.02 C ANISOU 2393 C GLN B 21 7864 5512 10950 -1052 2060 -1577 C ATOM 2394 O GLN B 21 -7.489 75.518 35.862 1.00 64.32 O ANISOU 2394 O GLN B 21 7789 5549 11099 -919 1821 -1415 O ATOM 2395 CB GLN B 21 -7.299 78.256 37.693 1.00 67.07 C ANISOU 2395 CB GLN B 21 8188 5667 11629 -1088 2123 -1823 C ATOM 2396 CG GLN B 21 -6.908 79.166 38.882 1.00 73.92 C ANISOU 2396 CG GLN B 21 9179 6507 12400 -1231 2305 -2030 C ATOM 2397 CD GLN B 21 -5.421 79.506 38.973 1.00 83.47 C ANISOU 2397 CD GLN B 21 10553 7850 13312 -1281 2131 -1918 C ATOM 2398 OE1 GLN B 21 -4.643 78.853 39.695 1.00 86.79 O ANISOU 2398 OE1 GLN B 21 11184 8460 13333 -1369 2122 -1897 O ATOM 2399 NE2 GLN B 21 -4.981 80.553 38.265 1.00 84.56 N ANISOU 2399 NE2 GLN B 21 10602 7870 13655 -1224 1988 -1861 N ATOM 2400 N PRO B 22 -8.195 74.977 37.928 1.00 63.58 N ANISOU 2400 N PRO B 22 7857 5447 10853 -1155 2356 -1726 N ATOM 2401 CA PRO B 22 -9.061 73.910 37.391 1.00 63.29 C ANISOU 2401 CA PRO B 22 7678 5387 10983 -1115 2402 -1726 C ATOM 2402 C PRO B 22 -10.025 74.419 36.327 1.00 63.42 C ANISOU 2402 C PRO B 22 7346 5246 11504 -960 2238 -1808 C ATOM 2403 O PRO B 22 -10.707 75.414 36.540 1.00 64.10 O ANISOU 2403 O PRO B 22 7262 5161 11934 -940 2320 -2016 O ATOM 2404 CB PRO B 22 -9.815 73.407 38.628 1.00 63.86 C ANISOU 2404 CB PRO B 22 7849 5389 11025 -1286 2848 -1952 C ATOM 2405 CG PRO B 22 -8.950 73.757 39.767 1.00 64.42 C ANISOU 2405 CG PRO B 22 8254 5542 10681 -1403 2949 -1952 C ATOM 2406 CD PRO B 22 -8.322 75.072 39.393 1.00 63.13 C ANISOU 2406 CD PRO B 22 8002 5373 10610 -1326 2694 -1926 C ATOM 2407 N GLY B 23 -10.031 73.762 35.181 1.00 62.66 N ANISOU 2407 N GLY B 23 7164 5203 11440 -839 1980 -1648 N ATOM 2408 CA GLY B 23 -10.840 74.158 34.038 1.00 62.70 C ANISOU 2408 CA GLY B 23 6892 5077 11852 -654 1720 -1692 C ATOM 2409 C GLY B 23 -10.067 74.944 32.995 1.00 62.47 C ANISOU 2409 C GLY B 23 6949 5051 11735 -507 1359 -1454 C ATOM 2410 O GLY B 23 -10.557 75.151 31.886 1.00 62.46 O ANISOU 2410 O GLY B 23 6820 4960 11953 -328 1070 -1417 O ATOM 2411 N GLY B 24 -8.860 75.375 33.346 1.00 62.22 N ANISOU 2411 N GLY B 24 7151 5108 11384 -585 1375 -1306 N ATOM 2412 CA GLY B 24 -8.000 76.130 32.460 1.00 62.73 C ANISOU 2412 CA GLY B 24 7331 5152 11351 -495 1125 -1091 C ATOM 2413 C GLY B 24 -7.325 75.300 31.388 1.00 63.65 C ANISOU 2413 C GLY B 24 7564 5403 11217 -441 918 -843 C ATOM 2414 O GLY B 24 -7.353 74.068 31.428 1.00 64.80 O ANISOU 2414 O GLY B 24 7713 5686 11222 -483 964 -823 O ATOM 2415 N SER B 25 -6.691 75.982 30.426 1.00 63.18 N ANISOU 2415 N SER B 25 7626 5281 11097 -358 723 -657 N ATOM 2416 CA SER B 25 -5.999 75.383 29.289 1.00 62.83 C ANISOU 2416 CA SER B 25 7727 5329 10816 -312 553 -429 C ATOM 2417 C SER B 25 -4.517 75.661 29.346 1.00 62.11 C ANISOU 2417 C SER B 25 7815 5314 10471 -424 622 -290 C ATOM 2418 O SER B 25 -4.082 76.615 29.992 1.00 62.51 O ANISOU 2418 O SER B 25 7886 5297 10569 -499 730 -352 O ATOM 2419 CB SER B 25 -6.547 75.947 27.982 1.00 64.73 C ANISOU 2419 CB SER B 25 8011 5398 11187 -119 279 -332 C ATOM 2420 OG SER B 25 -7.850 75.452 27.725 1.00 68.30 O ANISOU 2420 OG SER B 25 8262 5808 11881 5 143 -475 O ATOM 2421 N LEU B 26 -3.735 74.845 28.631 1.00 60.92 N ANISOU 2421 N LEU B 26 7773 5289 10086 -438 566 -131 N ATOM 2422 CA LEU B 26 -2.282 74.968 28.548 1.00 60.15 C ANISOU 2422 CA LEU B 26 7798 5258 9797 -544 635 -27 C ATOM 2423 C LEU B 26 -1.812 74.229 27.290 1.00 58.73 C ANISOU 2423 C LEU B 26 7738 5131 9444 -507 547 145 C ATOM 2424 O LEU B 26 -2.376 73.196 26.949 1.00 58.81 O ANISOU 2424 O LEU B 26 7708 5225 9413 -448 470 151 O ATOM 2425 CB LEU B 26 -1.641 74.341 29.804 1.00 60.42 C ANISOU 2425 CB LEU B 26 7777 5470 9711 -668 760 -125 C ATOM 2426 CG LEU B 26 -0.205 74.691 30.109 1.00 61.71 C ANISOU 2426 CG LEU B 26 7981 5687 9778 -779 816 -119 C ATOM 2427 CD1 LEU B 26 -0.093 76.101 30.544 1.00 61.91 C ANISOU 2427 CD1 LEU B 26 8002 5569 9953 -831 883 -216 C ATOM 2428 CD2 LEU B 26 0.304 73.847 31.228 1.00 62.86 C ANISOU 2428 CD2 LEU B 26 8099 6013 9772 -843 845 -201 C ATOM 2429 N ARG B 27 -0.806 74.756 26.597 1.00 57.55 N ANISOU 2429 N ARG B 27 7740 4918 9210 -555 591 262 N ATOM 2430 CA ARG B 27 -0.256 74.088 25.426 1.00 57.27 C ANISOU 2430 CA ARG B 27 7848 4922 8991 -549 568 404 C ATOM 2431 C ARG B 27 1.187 73.713 25.672 1.00 56.42 C ANISOU 2431 C ARG B 27 7711 4927 8800 -693 725 394 C ATOM 2432 O ARG B 27 1.989 74.568 26.021 1.00 56.56 O ANISOU 2432 O ARG B 27 7721 4876 8891 -793 844 352 O ATOM 2433 CB ARG B 27 -0.372 74.926 24.144 1.00 58.95 C ANISOU 2433 CB ARG B 27 8322 4922 9153 -476 508 557 C ATOM 2434 CG ARG B 27 -0.006 74.121 22.910 1.00 62.63 C ANISOU 2434 CG ARG B 27 8977 5432 9389 -465 486 682 C ATOM 2435 CD ARG B 27 -0.058 74.923 21.648 1.00 67.13 C ANISOU 2435 CD ARG B 27 9898 5779 9829 -399 440 851 C ATOM 2436 NE ARG B 27 1.017 75.902 21.627 1.00 72.98 N ANISOU 2436 NE ARG B 27 10773 6371 10587 -541 693 900 N ATOM 2437 CZ ARG B 27 1.241 76.752 20.629 1.00 78.11 C ANISOU 2437 CZ ARG B 27 11789 6776 11115 -535 760 1062 C ATOM 2438 NH1 ARG B 27 0.469 76.736 19.544 1.00 78.63 N ANISOU 2438 NH1 ARG B 27 12156 6732 10987 -367 540 1205 N ATOM 2439 NH2 ARG B 27 2.232 77.633 20.710 1.00 79.07 N ANISOU 2439 NH2 ARG B 27 11996 6743 11304 -696 1047 1073 N ATOM 2440 N LEU B 28 1.516 72.435 25.516 1.00 55.95 N ANISOU 2440 N LEU B 28 7606 5025 8626 -700 719 407 N ATOM 2441 CA LEU B 28 2.893 71.977 25.659 1.00 55.84 C ANISOU 2441 CA LEU B 28 7532 5107 8579 -807 836 380 C ATOM 2442 C LEU B 28 3.518 71.796 24.278 1.00 56.08 C ANISOU 2442 C LEU B 28 7724 5077 8507 -840 929 485 C ATOM 2443 O LEU B 28 2.813 71.556 23.297 1.00 55.87 O ANISOU 2443 O LEU B 28 7863 5002 8362 -759 853 584 O ATOM 2444 CB LEU B 28 2.987 70.661 26.429 1.00 55.33 C ANISOU 2444 CB LEU B 28 7327 5226 8468 -789 787 321 C ATOM 2445 CG LEU B 28 2.302 70.583 27.778 1.00 56.02 C ANISOU 2445 CG LEU B 28 7327 5373 8586 -765 734 226 C ATOM 2446 CD1 LEU B 28 2.436 69.192 28.354 1.00 56.20 C ANISOU 2446 CD1 LEU B 28 7300 5535 8519 -740 707 214 C ATOM 2447 CD2 LEU B 28 2.827 71.634 28.745 1.00 56.10 C ANISOU 2447 CD2 LEU B 28 7286 5355 8674 -839 769 116 C ATOM 2448 N SER B 29 4.841 71.920 24.206 1.00 56.34 N ANISOU 2448 N SER B 29 7710 5102 8593 -964 1098 438 N ATOM 2449 CA SER B 29 5.596 71.691 22.989 1.00 56.93 C ANISOU 2449 CA SER B 29 7929 5113 8589 -1034 1269 499 C ATOM 2450 C SER B 29 6.654 70.643 23.223 1.00 57.73 C ANISOU 2450 C SER B 29 7822 5352 8760 -1089 1339 394 C ATOM 2451 O SER B 29 7.231 70.555 24.296 1.00 57.42 O ANISOU 2451 O SER B 29 7547 5401 8867 -1110 1292 265 O ATOM 2452 CB SER B 29 6.265 72.965 22.517 1.00 58.22 C ANISOU 2452 CB SER B 29 8235 5066 8821 -1158 1489 514 C ATOM 2453 OG SER B 29 5.250 73.894 22.198 1.00 61.81 O ANISOU 2453 OG SER B 29 8917 5362 9207 -1074 1397 634 O ATOM 2454 N CYS B 30 6.903 69.843 22.206 1.00 58.81 N ANISOU 2454 N CYS B 30 8059 5496 8791 -1100 1432 439 N ATOM 2455 CA CYS B 30 7.938 68.835 22.197 1.00 60.15 C ANISOU 2455 CA CYS B 30 8043 5755 9057 -1145 1526 335 C ATOM 2456 C CYS B 30 8.773 69.244 21.014 1.00 62.24 C ANISOU 2456 C CYS B 30 8467 5867 9316 -1289 1838 333 C ATOM 2457 O CYS B 30 8.297 69.158 19.887 1.00 62.21 O ANISOU 2457 O CYS B 30 8766 5789 9083 -1282 1902 452 O ATOM 2458 CB CYS B 30 7.343 67.441 22.012 1.00 60.19 C ANISOU 2458 CB CYS B 30 8045 5882 8942 -1036 1396 376 C ATOM 2459 SG CYS B 30 8.581 66.130 21.848 1.00 62.18 S ANISOU 2459 SG CYS B 30 8089 6203 9332 -1067 1518 254 S ATOM 2460 N GLU B 31 9.952 69.813 21.261 1.00 64.37 N ANISOU 2460 N GLU B 31 8568 6063 9827 -1428 2040 189 N ATOM 2461 CA GLU B 31 10.807 70.276 20.178 1.00 67.30 C ANISOU 2461 CA GLU B 31 9094 6248 10229 -1605 2425 159 C ATOM 2462 C GLU B 31 11.957 69.331 19.987 1.00 69.86 C ANISOU 2462 C GLU B 31 9165 6620 10758 -1677 2600 -22 C ATOM 2463 O GLU B 31 12.561 68.874 20.954 1.00 69.63 O ANISOU 2463 O GLU B 31 8755 6709 10993 -1635 2458 -188 O ATOM 2464 CB GLU B 31 11.326 71.684 20.445 1.00 71.49 C ANISOU 2464 CB GLU B 31 9613 6604 10946 -1745 2609 90 C ATOM 2465 CG GLU B 31 10.238 72.693 20.784 1.00 78.48 C ANISOU 2465 CG GLU B 31 10699 7421 11698 -1663 2428 241 C ATOM 2466 CD GLU B 31 10.543 73.510 22.026 1.00 84.45 C ANISOU 2466 CD GLU B 31 11177 8189 12720 -1696 2343 87 C ATOM 2467 OE1 GLU B 31 11.342 74.469 21.909 1.00 84.57 O ANISOU 2467 OE1 GLU B 31 11164 8025 12944 -1869 2616 -24 O ATOM 2468 OE2 GLU B 31 10.018 73.168 23.117 1.00 85.15 O ANISOU 2468 OE2 GLU B 31 11087 8457 12812 -1565 2029 58 O ATOM 2469 N ALA B 32 12.248 69.022 18.733 1.00 72.34 N ANISOU 2469 N ALA B 32 9709 6831 10946 -1773 2897 2 N ATOM 2470 CA ALA B 32 13.312 68.105 18.397 1.00 75.41 C ANISOU 2470 CA ALA B 32 9871 7234 11548 -1850 3117 -187 C ATOM 2471 C ALA B 32 14.510 68.789 17.750 1.00 78.70 C ANISOU 2471 C ALA B 32 10282 7433 12189 -2100 3618 -353 C ATOM 2472 O ALA B 32 14.372 69.791 17.043 1.00 78.56 O ANISOU 2472 O ALA B 32 10636 7216 11998 -2228 3880 -245 O ATOM 2473 CB ALA B 32 12.782 67.014 17.488 1.00 75.76 C ANISOU 2473 CB ALA B 32 10144 7334 11308 -1785 3116 -91 C ATOM 2474 N SER B 33 15.692 68.212 17.994 1.00 81.16 N ANISOU 2474 N SER B 33 10168 7760 12908 -2164 3759 -628 N ATOM 2475 CA SER B 33 16.971 68.624 17.433 1.00 83.70 C ANISOU 2475 CA SER B 33 10361 7876 13563 -2414 4274 -874 C ATOM 2476 C SER B 33 17.521 67.401 16.703 1.00 86.38 C ANISOU 2476 C SER B 33 10610 8227 13985 -2439 4489 -1008 C ATOM 2477 O SER B 33 17.644 66.339 17.313 1.00 86.91 O ANISOU 2477 O SER B 33 10334 8463 14224 -2268 4187 -1095 O ATOM 2478 CB SER B 33 17.930 69.018 18.550 1.00 85.33 C ANISOU 2478 CB SER B 33 10015 8100 14307 -2443 4181 -1165 C ATOM 2479 OG SER B 33 18.032 70.427 18.664 1.00 88.60 O ANISOU 2479 OG SER B 33 10531 8343 14790 -2602 4370 -1177 O ATOM 2480 N GLY B 34 17.822 67.532 15.413 1.00 87.70 N ANISOU 2480 N GLY B 34 11117 8196 14009 -2646 5012 -1018 N ATOM 2481 CA GLY B 34 18.345 66.408 14.642 1.00 89.26 C ANISOU 2481 CA GLY B 34 11258 8381 14276 -2696 5279 -1169 C ATOM 2482 C GLY B 34 18.226 66.562 13.140 1.00 90.55 C ANISOU 2482 C GLY B 34 12023 8354 14030 -2887 5776 -1071 C ATOM 2483 O GLY B 34 17.443 67.380 12.652 1.00 91.22 O ANISOU 2483 O GLY B 34 12652 8348 13659 -2912 5790 -804 O ATOM 2484 N THR B 36 15.874 65.054 10.773 1.00 92.43 N ANISOU 2484 N THR B 36 13558 8716 12846 -2704 5587 -570 N ATOM 2485 CA THR B 36 14.448 65.148 10.472 1.00 92.52 C ANISOU 2485 CA THR B 36 14042 8816 12296 -2529 5173 -267 C ATOM 2486 C THR B 36 13.568 64.383 11.464 1.00 91.21 C ANISOU 2486 C THR B 36 13531 8919 12207 -2252 4554 -203 C ATOM 2487 O THR B 36 13.968 63.345 11.988 1.00 91.32 O ANISOU 2487 O THR B 36 13093 9055 12551 -2187 4474 -371 O ATOM 2488 CB THR B 36 14.159 64.733 9.016 1.00 94.24 C ANISOU 2488 CB THR B 36 14865 8950 11992 -2608 5409 -219 C ATOM 2489 OG1 THR B 36 12.802 65.061 8.690 1.00 95.29 O ANISOU 2489 OG1 THR B 36 15481 9130 11596 -2437 4987 61 O ATOM 2490 CG2 THR B 36 14.426 63.255 8.760 1.00 94.82 C ANISOU 2490 CG2 THR B 36 14700 9144 12184 -2590 5461 -426 C ATOM 2491 N LEU B 37 12.365 64.929 11.712 1.00 89.69 N ANISOU 2491 N LEU B 37 13571 8786 11719 -2092 4136 38 N ATOM 2492 CA LEU B 37 11.304 64.392 12.576 1.00 88.23 C ANISOU 2492 CA LEU B 37 13164 8818 11542 -1849 3584 123 C ATOM 2493 C LEU B 37 10.195 63.698 11.735 1.00 86.79 C ANISOU 2493 C LEU B 37 13338 8707 10930 -1738 3355 216 C ATOM 2494 O LEU B 37 9.400 62.949 12.288 1.00 87.00 O ANISOU 2494 O LEU B 37 13156 8898 11000 -1570 2985 224 O ATOM 2495 CB LEU B 37 10.688 65.538 13.422 1.00 87.84 C ANISOU 2495 CB LEU B 37 13096 8765 11516 -1758 3301 278 C ATOM 2496 CG LEU B 37 9.849 65.139 14.647 1.00 88.76 C ANISOU 2496 CG LEU B 37 12876 9078 11773 -1551 2825 314 C ATOM 2497 CD1 LEU B 37 10.699 64.454 15.703 1.00 89.32 C ANISOU 2497 CD1 LEU B 37 12415 9252 12272 -1540 2821 139 C ATOM 2498 CD2 LEU B 37 9.159 66.333 15.262 1.00 88.93 C ANISOU 2498 CD2 LEU B 37 12965 9062 11761 -1479 2600 455 C ATOM 2499 N ALA B 38 10.159 63.938 10.410 1.00 85.00 N ANISOU 2499 N ALA B 38 13661 8344 10291 -1838 3583 267 N ATOM 2500 CA ALA B 38 9.180 63.418 9.465 1.00 83.81 C ANISOU 2500 CA ALA B 38 13919 8237 9686 -1745 3365 329 C ATOM 2501 C ALA B 38 8.804 61.957 9.671 1.00 81.89 C ANISOU 2501 C ALA B 38 13368 8183 9564 -1646 3160 188 C ATOM 2502 O ALA B 38 7.616 61.656 9.748 1.00 82.08 O ANISOU 2502 O ALA B 38 13429 8317 9441 -1475 2731 246 O ATOM 2503 CB ALA B 38 9.655 63.650 8.032 1.00 83.83 C ANISOU 2503 CB ALA B 38 14523 8053 9276 -1922 3780 331 C ATOM 2504 N ASN B 39 9.801 61.062 9.803 1.00 79.76 N ANISOU 2504 N ASN B 39 12767 7929 9607 -1746 3464 -12 N ATOM 2505 CA ASN B 39 9.568 59.629 9.945 1.00 78.00 C ANISOU 2505 CA ASN B 39 12274 7838 9524 -1667 3337 -153 C ATOM 2506 C ASN B 39 9.373 59.148 11.381 1.00 73.81 C ANISOU 2506 C ASN B 39 11202 7438 9405 -1516 3041 -157 C ATOM 2507 O ASN B 39 9.321 57.944 11.594 1.00 73.88 O ANISOU 2507 O ASN B 39 10971 7517 9583 -1457 2983 -269 O ATOM 2508 CB ASN B 39 10.694 58.821 9.251 1.00 80.89 C ANISOU 2508 CB ASN B 39 12600 8125 10010 -1836 3818 -379 C ATOM 2509 CG ASN B 39 12.020 58.821 9.987 1.00 85.93 C ANISOU 2509 CG ASN B 39 12762 8706 11183 -1916 4104 -520 C ATOM 2510 OD1 ASN B 39 12.313 57.922 10.804 1.00 87.23 O ANISOU 2510 OD1 ASN B 39 12451 8944 11746 -1819 3991 -627 O ATOM 2511 ND2 ASN B 39 12.848 59.833 9.705 1.00 87.45 N ANISOU 2511 ND2 ASN B 39 13080 8742 11403 -2090 4473 -533 N ATOM 2512 N TYR B 40 9.264 60.055 12.350 1.00 70.53 N ANISOU 2512 N TYR B 40 10629 7035 9133 -1458 2870 -39 N ATOM 2513 CA TYR B 40 9.065 59.671 13.744 1.00 68.09 C ANISOU 2513 CA TYR B 40 9888 6836 9148 -1322 2600 -32 C ATOM 2514 C TYR B 40 7.621 59.755 14.208 1.00 65.08 C ANISOU 2514 C TYR B 40 9554 6547 8628 -1168 2189 92 C ATOM 2515 O TYR B 40 6.864 60.606 13.779 1.00 64.82 O ANISOU 2515 O TYR B 40 9814 6485 8331 -1144 2052 204 O ATOM 2516 CB TYR B 40 9.922 60.525 14.689 1.00 68.20 C ANISOU 2516 CB TYR B 40 9644 6815 9455 -1357 2668 -31 C ATOM 2517 CG TYR B 40 11.388 60.159 14.735 1.00 69.65 C ANISOU 2517 CG TYR B 40 9543 6932 9987 -1460 2989 -223 C ATOM 2518 CD1 TYR B 40 12.280 60.660 13.797 1.00 71.54 C ANISOU 2518 CD1 TYR B 40 9947 7026 10208 -1655 3419 -316 C ATOM 2519 CD2 TYR B 40 11.905 59.414 15.784 1.00 70.64 C ANISOU 2519 CD2 TYR B 40 9237 7117 10485 -1358 2861 -317 C ATOM 2520 CE1 TYR B 40 13.639 60.372 13.862 1.00 72.96 C ANISOU 2520 CE1 TYR B 40 9804 7128 10791 -1758 3733 -541 C ATOM 2521 CE2 TYR B 40 13.260 59.100 15.850 1.00 72.19 C ANISOU 2521 CE2 TYR B 40 9122 7241 11064 -1423 3105 -523 C ATOM 2522 CZ TYR B 40 14.128 59.578 14.883 1.00 74.04 C ANISOU 2522 CZ TYR B 40 9459 7336 11336 -1629 3550 -656 C ATOM 2523 OH TYR B 40 15.483 59.308 14.934 1.00 76.09 O ANISOU 2523 OH TYR B 40 9357 7504 12048 -1707 3821 -910 O ATOM 2524 N ALA B 41 7.247 58.865 15.101 1.00 63.00 N ANISOU 2524 N ALA B 41 9002 6371 8566 -1060 2003 62 N ATOM 2525 CA ALA B 41 5.961 58.925 15.786 1.00 60.99 C ANISOU 2525 CA ALA B 41 8706 6186 8282 -934 1672 141 C ATOM 2526 C ALA B 41 6.308 59.582 17.117 1.00 59.02 C ANISOU 2526 C ALA B 41 8227 5951 8247 -901 1609 202 C ATOM 2527 O ALA B 41 7.385 59.352 17.682 1.00 58.46 O ANISOU 2527 O ALA B 41 7936 5872 8404 -925 1732 146 O ATOM 2528 CB ALA B 41 5.392 57.533 16.029 1.00 60.47 C ANISOU 2528 CB ALA B 41 8487 6172 8317 -864 1577 60 C ATOM 2529 N ILE B 42 5.428 60.462 17.588 1.00 57.60 N ANISOU 2529 N ILE B 42 8101 5782 8002 -845 1408 294 N ATOM 2530 CA ILE B 42 5.637 61.178 18.838 1.00 55.70 C ANISOU 2530 CA ILE B 42 7686 5555 7924 -822 1341 336 C ATOM 2531 C ILE B 42 4.464 60.922 19.753 1.00 53.06 C ANISOU 2531 C ILE B 42 7258 5273 7628 -720 1119 359 C ATOM 2532 O ILE B 42 3.333 61.142 19.384 1.00 52.67 O ANISOU 2532 O ILE B 42 7321 5217 7474 -675 979 375 O ATOM 2533 CB ILE B 42 5.855 62.691 18.595 1.00 55.95 C ANISOU 2533 CB ILE B 42 7874 5506 7878 -883 1393 404 C ATOM 2534 CG1 ILE B 42 6.999 62.954 17.578 1.00 57.14 C ANISOU 2534 CG1 ILE B 42 8164 5564 7983 -1020 1696 368 C ATOM 2535 CG2 ILE B 42 6.049 63.452 19.920 1.00 56.24 C ANISOU 2535 CG2 ILE B 42 7723 5558 8088 -867 1317 414 C ATOM 2536 CD1 ILE B 42 8.433 62.780 18.098 1.00 58.75 C ANISOU 2536 CD1 ILE B 42 8089 5760 8474 -1098 1895 249 C ATOM 2537 N GLY B 43 4.750 60.432 20.931 1.00 51.56 N ANISOU 2537 N GLY B 43 6873 5120 7596 -682 1094 346 N ATOM 2538 CA GLY B 43 3.745 60.169 21.937 1.00 50.71 C ANISOU 2538 CA GLY B 43 6702 5037 7528 -613 962 360 C ATOM 2539 C GLY B 43 4.008 61.029 23.153 1.00 50.30 C ANISOU 2539 C GLY B 43 6581 4996 7533 -606 910 389 C ATOM 2540 O GLY B 43 5.157 61.337 23.472 1.00 50.16 O ANISOU 2540 O GLY B 43 6487 4985 7586 -631 952 375 O ATOM 2541 N TRP B 44 2.936 61.458 23.814 1.00 49.81 N ANISOU 2541 N TRP B 44 6531 4930 7463 -579 823 398 N ATOM 2542 CA TRP B 44 2.984 62.216 25.045 1.00 49.58 C ANISOU 2542 CA TRP B 44 6465 4909 7465 -577 782 403 C ATOM 2543 C TRP B 44 2.566 61.262 26.146 1.00 49.08 C ANISOU 2543 C TRP B 44 6385 4853 7411 -536 781 399 C ATOM 2544 O TRP B 44 1.604 60.521 26.008 1.00 48.80 O ANISOU 2544 O TRP B 44 6362 4789 7391 -524 812 378 O ATOM 2545 CB TRP B 44 2.038 63.435 24.992 1.00 49.78 C ANISOU 2545 CB TRP B 44 6537 4890 7486 -583 727 398 C ATOM 2546 CG TRP B 44 2.613 64.639 24.290 1.00 50.10 C ANISOU 2546 CG TRP B 44 6646 4885 7506 -625 743 429 C ATOM 2547 CD1 TRP B 44 2.420 64.998 22.990 1.00 51.04 C ANISOU 2547 CD1 TRP B 44 6904 4945 7545 -627 739 469 C ATOM 2548 CD2 TRP B 44 3.462 65.645 24.862 1.00 49.79 C ANISOU 2548 CD2 TRP B 44 6571 4828 7517 -678 778 416 C ATOM 2549 NE1 TRP B 44 3.084 66.170 22.719 1.00 51.33 N ANISOU 2549 NE1 TRP B 44 7021 4907 7574 -685 806 504 N ATOM 2550 CE2 TRP B 44 3.731 66.590 23.853 1.00 50.88 C ANISOU 2550 CE2 TRP B 44 6829 4875 7626 -724 838 457 C ATOM 2551 CE3 TRP B 44 3.996 65.857 26.138 1.00 49.84 C ANISOU 2551 CE3 TRP B 44 6479 4877 7579 -692 757 362 C ATOM 2552 CZ2 TRP B 44 4.519 67.720 24.079 1.00 51.31 C ANISOU 2552 CZ2 TRP B 44 6874 4867 7754 -801 918 436 C ATOM 2553 CZ3 TRP B 44 4.783 66.968 26.355 1.00 50.60 C ANISOU 2553 CZ3 TRP B 44 6542 4937 7747 -758 791 318 C ATOM 2554 CH2 TRP B 44 5.048 67.878 25.333 1.00 51.01 C ANISOU 2554 CH2 TRP B 44 6679 4887 7816 -821 890 349 C ATOM 2555 N PHE B 45 3.342 61.239 27.206 1.00 49.19 N ANISOU 2555 N PHE B 45 6387 4890 7414 -515 748 411 N ATOM 2556 CA PHE B 45 3.159 60.420 28.398 1.00 49.56 C ANISOU 2556 CA PHE B 45 6504 4920 7406 -468 743 436 C ATOM 2557 C PHE B 45 3.207 61.348 29.622 1.00 49.45 C ANISOU 2557 C PHE B 45 6545 4924 7319 -478 684 416 C ATOM 2558 O PHE B 45 3.678 62.468 29.520 1.00 49.08 O ANISOU 2558 O PHE B 45 6435 4908 7307 -513 635 374 O ATOM 2559 CB PHE B 45 4.288 59.371 28.480 1.00 49.83 C ANISOU 2559 CB PHE B 45 6514 4952 7465 -394 697 469 C ATOM 2560 CG PHE B 45 4.277 58.435 27.299 1.00 50.80 C ANISOU 2560 CG PHE B 45 6587 5048 7666 -395 782 464 C ATOM 2561 CD1 PHE B 45 4.911 58.782 26.107 1.00 52.17 C ANISOU 2561 CD1 PHE B 45 6670 5246 7905 -438 817 421 C ATOM 2562 CD2 PHE B 45 3.621 57.219 27.368 1.00 51.32 C ANISOU 2562 CD2 PHE B 45 6720 5045 7734 -369 861 488 C ATOM 2563 CE1 PHE B 45 4.836 57.950 24.991 1.00 53.00 C ANISOU 2563 CE1 PHE B 45 6765 5327 8046 -452 910 395 C ATOM 2564 CE2 PHE B 45 3.556 56.381 26.265 1.00 52.24 C ANISOU 2564 CE2 PHE B 45 6789 5135 7926 -381 942 453 C ATOM 2565 CZ PHE B 45 4.150 56.753 25.079 1.00 52.76 C ANISOU 2565 CZ PHE B 45 6777 5245 8027 -420 956 403 C ATOM 2566 N ARG B 46 2.699 60.898 30.760 1.00 49.75 N ANISOU 2566 N ARG B 46 6728 4927 7248 -461 718 434 N ATOM 2567 CA ARG B 46 2.715 61.691 31.986 1.00 50.62 C ANISOU 2567 CA ARG B 46 6940 5051 7241 -477 675 398 C ATOM 2568 C ARG B 46 2.912 60.801 33.194 1.00 53.44 C ANISOU 2568 C ARG B 46 7524 5371 7409 -412 648 460 C ATOM 2569 O ARG B 46 2.536 59.627 33.182 1.00 53.73 O ANISOU 2569 O ARG B 46 7662 5331 7421 -383 746 532 O ATOM 2570 CB ARG B 46 1.447 62.567 32.134 1.00 49.47 C ANISOU 2570 CB ARG B 46 6797 4865 7134 -560 807 322 C ATOM 2571 CG ARG B 46 0.189 61.791 32.442 1.00 49.87 C ANISOU 2571 CG ARG B 46 6938 4823 7185 -593 1002 309 C ATOM 2572 CD ARG B 46 -0.999 62.693 32.478 1.00 52.36 C ANISOU 2572 CD ARG B 46 7182 5089 7624 -663 1117 189 C ATOM 2573 NE ARG B 46 -2.258 61.969 32.647 1.00 54.48 N ANISOU 2573 NE ARG B 46 7464 5251 7984 -713 1334 122 N ATOM 2574 CZ ARG B 46 -3.458 62.546 32.655 1.00 56.39 C ANISOU 2574 CZ ARG B 46 7592 5420 8413 -769 1458 -25 C ATOM 2575 NH1 ARG B 46 -3.573 63.857 32.487 1.00 56.72 N ANISOU 2575 NH1 ARG B 46 7525 5477 8549 -765 1368 -92 N ATOM 2576 NH2 ARG B 46 -4.552 61.814 32.827 1.00 55.70 N ANISOU 2576 NH2 ARG B 46 7483 5222 8460 -829 1682 -124 N ATOM 2577 N GLN B 47 3.529 61.346 34.235 1.00 55.60 N ANISOU 2577 N GLN B 47 7902 5686 7538 -385 506 431 N ATOM 2578 CA GLN B 47 3.711 60.606 35.475 1.00 57.96 C ANISOU 2578 CA GLN B 47 8503 5937 7583 -307 441 501 C ATOM 2579 C GLN B 47 3.390 61.491 36.666 1.00 59.94 C ANISOU 2579 C GLN B 47 8950 6199 7627 -364 453 424 C ATOM 2580 O GLN B 47 4.005 62.541 36.852 1.00 59.73 O ANISOU 2580 O GLN B 47 8814 6257 7622 -378 295 316 O ATOM 2581 CB GLN B 47 5.099 59.973 35.571 1.00 60.16 C ANISOU 2581 CB GLN B 47 8758 6244 7857 -152 156 547 C ATOM 2582 CG GLN B 47 5.284 59.130 36.826 1.00 65.30 C ANISOU 2582 CG GLN B 47 9785 6815 8210 -30 38 651 C ATOM 2583 CD GLN B 47 6.400 58.131 36.646 1.00 73.18 C ANISOU 2583 CD GLN B 47 10734 7784 9288 153 -206 723 C ATOM 2584 OE1 GLN B 47 7.470 58.426 36.086 1.00 75.92 O ANISOU 2584 OE1 GLN B 47 10767 8213 9868 207 -407 628 O ATOM 2585 NE2 GLN B 47 6.169 56.912 37.097 1.00 74.94 N ANISOU 2585 NE2 GLN B 47 11260 7863 9353 247 -165 879 N ATOM 2586 N ALA B 48 2.354 61.102 37.412 1.00 61.79 N ANISOU 2586 N ALA B 48 9463 6328 7687 -424 690 452 N ATOM 2587 CA ALA B 48 1.899 61.785 38.624 1.00 64.20 C ANISOU 2587 CA ALA B 48 10026 6612 7756 -498 782 370 C ATOM 2588 C ALA B 48 2.689 61.220 39.819 1.00 67.03 C ANISOU 2588 C ALA B 48 10775 6955 7738 -378 568 455 C ATOM 2589 O ALA B 48 3.189 60.093 39.741 1.00 66.98 O ANISOU 2589 O ALA B 48 10878 6896 7674 -249 450 602 O ATOM 2590 CB ALA B 48 0.406 61.543 38.819 1.00 64.26 C ANISOU 2590 CB ALA B 48 10152 6482 7782 -632 1192 338 C ATOM 2591 N PRO B 49 2.874 61.992 40.913 1.00 69.39 N ANISOU 2591 N PRO B 49 11296 7293 7775 -400 477 359 N ATOM 2592 CA PRO B 49 3.660 61.463 42.048 1.00 70.59 C ANISOU 2592 CA PRO B 49 11866 7431 7524 -257 201 438 C ATOM 2593 C PRO B 49 3.069 60.184 42.654 1.00 71.37 C ANISOU 2593 C PRO B 49 12447 7341 7331 -230 419 627 C ATOM 2594 O PRO B 49 1.884 60.140 43.012 1.00 71.46 O ANISOU 2594 O PRO B 49 12668 7230 7256 -391 850 610 O ATOM 2595 CB PRO B 49 3.691 62.631 43.048 1.00 71.35 C ANISOU 2595 CB PRO B 49 12125 7594 7391 -333 144 259 C ATOM 2596 CG PRO B 49 2.543 63.518 42.665 1.00 71.46 C ANISOU 2596 CG PRO B 49 11927 7585 7639 -539 539 124 C ATOM 2597 CD PRO B 49 2.399 63.369 41.174 1.00 69.52 C ANISOU 2597 CD PRO B 49 11215 7357 7843 -543 597 165 C ATOM 2598 N GLY B 50 3.899 59.141 42.693 1.00 71.38 N ANISOU 2598 N GLY B 50 12588 7295 7236 -31 142 793 N ATOM 2599 CA GLY B 50 3.536 57.833 43.230 1.00 71.58 C ANISOU 2599 CA GLY B 50 13103 7107 6987 30 303 1006 C ATOM 2600 C GLY B 50 2.808 56.902 42.281 1.00 71.40 C ANISOU 2600 C GLY B 50 12910 6956 7262 -36 646 1096 C ATOM 2601 O GLY B 50 2.516 55.757 42.640 1.00 72.12 O ANISOU 2601 O GLY B 50 13384 6839 7179 5 813 1272 O ATOM 2602 N LYS B 51 2.506 57.382 41.072 1.00 70.51 N ANISOU 2602 N LYS B 51 12254 6949 7588 -138 753 973 N ATOM 2603 CA LYS B 51 1.797 56.626 40.049 1.00 70.23 C ANISOU 2603 CA LYS B 51 11998 6822 7865 -209 1040 1003 C ATOM 2604 C LYS B 51 2.723 56.175 38.909 1.00 69.64 C ANISOU 2604 C LYS B 51 11550 6825 8085 -74 772 1040 C ATOM 2605 O LYS B 51 3.811 56.714 38.725 1.00 69.30 O ANISOU 2605 O LYS B 51 11297 6929 8105 33 414 991 O ATOM 2606 CB LYS B 51 0.668 57.480 39.458 1.00 72.25 C ANISOU 2606 CB LYS B 51 11939 7121 8391 -416 1349 820 C ATOM 2607 CG LYS B 51 -0.470 57.751 40.405 1.00 76.95 C ANISOU 2607 CG LYS B 51 12831 7594 8811 -584 1734 742 C ATOM 2608 CD LYS B 51 -1.625 58.374 39.645 1.00 82.59 C ANISOU 2608 CD LYS B 51 13160 8315 9904 -753 2018 550 C ATOM 2609 CE LYS B 51 -2.824 58.593 40.543 1.00 88.33 C ANISOU 2609 CE LYS B 51 14123 8890 10548 -937 2466 426 C ATOM 2610 NZ LYS B 51 -3.934 57.630 40.267 1.00 91.61 N ANISOU 2610 NZ LYS B 51 14521 9104 11183 -1058 2890 387 N ATOM 2611 N GLU B 52 2.273 55.183 38.138 1.00 69.27 N ANISOU 2611 N GLU B 52 11411 6665 8243 -96 979 1095 N ATOM 2612 CA GLU B 52 3.007 54.705 36.981 1.00 68.86 C ANISOU 2612 CA GLU B 52 11015 6667 8482 -1 810 1103 C ATOM 2613 C GLU B 52 2.830 55.692 35.801 1.00 66.56 C ANISOU 2613 C GLU B 52 10258 6546 8485 -112 826 937 C ATOM 2614 O GLU B 52 1.887 56.489 35.765 1.00 66.46 O ANISOU 2614 O GLU B 52 10179 6564 8508 -259 1015 832 O ATOM 2615 CB GLU B 52 2.518 53.305 36.561 1.00 73.51 C ANISOU 2615 CB GLU B 52 11685 7063 9183 -2 1049 1194 C ATOM 2616 CG GLU B 52 2.308 52.314 37.695 1.00 84.90 C ANISOU 2616 CG GLU B 52 13662 8265 10331 55 1177 1371 C ATOM 2617 CD GLU B 52 3.491 52.042 38.608 1.00 97.64 C ANISOU 2617 CD GLU B 52 15596 9845 11658 292 790 1521 C ATOM 2618 OE1 GLU B 52 4.650 52.095 38.128 1.00100.80 O ANISOU 2618 OE1 GLU B 52 15725 10360 12214 456 414 1499 O ATOM 2619 OE2 GLU B 52 3.252 51.754 39.805 1.00100.42 O ANISOU 2619 OE2 GLU B 52 16484 10040 11634 316 866 1650 O ATOM 2620 N ARG B 53 3.746 55.626 34.843 1.00 64.39 N ANISOU 2620 N ARG B 53 9684 6357 8422 -35 635 913 N ATOM 2621 CA ARG B 53 3.688 56.451 33.657 1.00 62.93 C ANISOU 2621 CA ARG B 53 9139 6300 8472 -127 654 789 C ATOM 2622 C ARG B 53 2.525 55.991 32.792 1.00 61.38 C ANISOU 2622 C ARG B 53 8857 6040 8425 -236 925 753 C ATOM 2623 O ARG B 53 2.296 54.788 32.643 1.00 61.54 O ANISOU 2623 O ARG B 53 8962 5936 8485 -212 1045 811 O ATOM 2624 CB ARG B 53 4.990 56.300 32.871 1.00 64.06 C ANISOU 2624 CB ARG B 53 9036 6509 8794 -30 448 766 C ATOM 2625 CG ARG B 53 5.173 57.313 31.751 1.00 67.09 C ANISOU 2625 CG ARG B 53 9121 7009 9360 -124 461 650 C ATOM 2626 CD ARG B 53 6.357 56.933 30.893 1.00 70.24 C ANISOU 2626 CD ARG B 53 9301 7429 9959 -58 367 612 C ATOM 2627 NE ARG B 53 6.150 55.636 30.248 1.00 72.78 N ANISOU 2627 NE ARG B 53 9630 7656 10368 -27 489 657 N ATOM 2628 CZ ARG B 53 7.119 54.767 29.979 1.00 73.79 C ANISOU 2628 CZ ARG B 53 9666 7732 10640 84 410 656 C ATOM 2629 NH1 ARG B 53 6.837 53.616 29.380 1.00 72.25 N ANISOU 2629 NH1 ARG B 53 9483 7437 10530 97 551 682 N ATOM 2630 NH2 ARG B 53 8.377 55.040 30.313 1.00 73.68 N ANISOU 2630 NH2 ARG B 53 9520 7753 10723 185 188 600 N ATOM 2631 N GLU B 54 1.794 56.945 32.214 1.00 59.68 N ANISOU 2631 N GLU B 54 8471 5893 8310 -347 1002 644 N ATOM 2632 CA GLU B 54 0.683 56.626 31.346 1.00 58.41 C ANISOU 2632 CA GLU B 54 8192 5685 8315 -434 1186 567 C ATOM 2633 C GLU B 54 0.681 57.489 30.078 1.00 57.31 C ANISOU 2633 C GLU B 54 7808 5654 8315 -464 1096 483 C ATOM 2634 O GLU B 54 0.861 58.711 30.150 1.00 57.37 O ANISOU 2634 O GLU B 54 7762 5736 8301 -482 1004 452 O ATOM 2635 CB GLU B 54 -0.648 56.767 32.104 1.00 60.22 C ANISOU 2635 CB GLU B 54 8531 5818 8530 -536 1417 500 C ATOM 2636 CG GLU B 54 -0.951 58.180 32.555 1.00 64.72 C ANISOU 2636 CG GLU B 54 9070 6456 9067 -586 1386 422 C ATOM 2637 CD GLU B 54 -2.350 58.475 33.073 1.00 72.09 C ANISOU 2637 CD GLU B 54 10019 7291 10081 -700 1638 292 C ATOM 2638 OE1 GLU B 54 -3.324 57.853 32.586 1.00 72.97 O ANISOU 2638 OE1 GLU B 54 10021 7314 10391 -759 1808 198 O ATOM 2639 OE2 GLU B 54 -2.471 59.362 33.953 1.00 74.34 O ANISOU 2639 OE2 GLU B 54 10401 7584 10261 -738 1671 251 O ATOM 2640 N GLY B 55 0.448 56.847 28.931 1.00 55.64 N ANISOU 2640 N GLY B 55 7484 5430 8229 -474 1132 443 N ATOM 2641 CA GLY B 55 0.307 57.543 27.661 1.00 54.65 C ANISOU 2641 CA GLY B 55 7208 5376 8181 -499 1054 373 C ATOM 2642 C GLY B 55 -0.963 58.371 27.657 1.00 54.02 C ANISOU 2642 C GLY B 55 7073 5280 8173 -549 1075 274 C ATOM 2643 O GLY B 55 -1.958 57.993 28.291 1.00 54.23 O ANISOU 2643 O GLY B 55 7116 5223 8268 -592 1216 208 O ATOM 2644 N VAL B 56 -0.935 59.539 26.999 1.00 53.09 N ANISOU 2644 N VAL B 56 6895 5217 8060 -545 952 255 N ATOM 2645 CA VAL B 56 -2.107 60.397 26.934 1.00 52.56 C ANISOU 2645 CA VAL B 56 6756 5115 8099 -560 925 154 C ATOM 2646 C VAL B 56 -2.538 60.635 25.495 1.00 52.36 C ANISOU 2646 C VAL B 56 6672 5099 8124 -526 783 102 C ATOM 2647 O VAL B 56 -3.723 60.612 25.188 1.00 52.13 O ANISOU 2647 O VAL B 56 6542 5020 8244 -515 742 -29 O ATOM 2648 CB VAL B 56 -1.978 61.721 27.741 1.00 53.30 C ANISOU 2648 CB VAL B 56 6874 5215 8162 -570 901 166 C ATOM 2649 CG1 VAL B 56 -1.973 61.457 29.230 1.00 54.27 C ANISOU 2649 CG1 VAL B 56 7091 5311 8219 -607 1041 170 C ATOM 2650 CG2 VAL B 56 -0.765 62.532 27.345 1.00 53.31 C ANISOU 2650 CG2 VAL B 56 6913 5277 8066 -556 797 256 C ATOM 2651 N SER B 57 -1.579 60.814 24.603 1.00 52.48 N ANISOU 2651 N SER B 57 6760 5165 8017 -509 709 186 N ATOM 2652 CA SER B 57 -1.866 61.118 23.214 1.00 52.60 C ANISOU 2652 CA SER B 57 6818 5178 7991 -474 570 162 C ATOM 2653 C SER B 57 -0.675 60.756 22.335 1.00 52.11 C ANISOU 2653 C SER B 57 6862 5156 7781 -495 609 236 C ATOM 2654 O SER B 57 0.454 60.785 22.805 1.00 52.25 O ANISOU 2654 O SER B 57 6887 5199 7769 -526 705 307 O ATOM 2655 CB SER B 57 -2.196 62.597 23.105 1.00 54.92 C ANISOU 2655 CB SER B 57 7149 5430 8288 -436 447 184 C ATOM 2656 OG SER B 57 -2.544 62.870 21.767 1.00 59.64 O ANISOU 2656 OG SER B 57 7852 6004 8806 -378 277 178 O ATOM 2657 N CYS B 58 -0.909 60.397 21.072 1.00 51.87 N ANISOU 2657 N CYS B 58 6911 5126 7671 -480 538 193 N ATOM 2658 CA CYS B 58 0.175 59.945 20.179 1.00 52.15 C ANISOU 2658 CA CYS B 58 7059 5184 7571 -522 635 228 C ATOM 2659 C CYS B 58 -0.129 60.358 18.739 1.00 51.41 C ANISOU 2659 C CYS B 58 7174 5069 7291 -501 513 217 C ATOM 2660 O CYS B 58 -1.283 60.323 18.317 1.00 51.19 O ANISOU 2660 O CYS B 58 7148 5029 7273 -436 318 131 O ATOM 2661 CB CYS B 58 0.364 58.423 20.311 1.00 53.49 C ANISOU 2661 CB CYS B 58 7134 5367 7822 -542 750 162 C ATOM 2662 SG CYS B 58 1.737 57.716 19.344 1.00 60.34 S ANISOU 2662 SG CYS B 58 8083 6243 8601 -596 919 159 S ATOM 2663 N ILE B 59 0.907 60.744 17.995 1.00 51.24 N ANISOU 2663 N ILE B 59 7337 5029 7102 -555 629 289 N ATOM 2664 CA ILE B 59 0.810 61.126 16.592 1.00 52.22 C ANISOU 2664 CA ILE B 59 7764 5111 6967 -549 561 306 C ATOM 2665 C ILE B 59 1.795 60.301 15.758 1.00 54.03 C ANISOU 2665 C ILE B 59 8101 5350 7078 -643 786 263 C ATOM 2666 O ILE B 59 2.978 60.253 16.061 1.00 54.05 O ANISOU 2666 O ILE B 59 8031 5344 7162 -726 1028 285 O ATOM 2667 CB ILE B 59 0.903 62.675 16.324 1.00 52.36 C ANISOU 2667 CB ILE B 59 8010 5034 6851 -533 511 439 C ATOM 2668 CG1 ILE B 59 0.573 63.006 14.846 1.00 53.03 C ANISOU 2668 CG1 ILE B 59 8493 5049 6607 -493 384 472 C ATOM 2669 CG2 ILE B 59 2.235 63.320 16.784 1.00 51.75 C ANISOU 2669 CG2 ILE B 59 7915 4919 6830 -642 781 518 C ATOM 2670 CD1 ILE B 59 0.042 64.390 14.627 1.00 53.57 C ANISOU 2670 CD1 ILE B 59 8785 4996 6571 -399 191 592 C ATOM 2671 N SER B 60 1.294 59.588 14.745 1.00 55.42 N ANISOU 2671 N SER B 60 8419 5541 7099 -627 701 166 N ATOM 2672 CA SER B 60 2.132 58.777 13.870 1.00 56.69 C ANISOU 2672 CA SER B 60 8704 5700 7137 -723 931 94 C ATOM 2673 C SER B 60 2.858 59.668 12.843 1.00 58.34 C ANISOU 2673 C SER B 60 9300 5823 7042 -799 1086 180 C ATOM 2674 O SER B 60 2.497 60.839 12.664 1.00 58.10 O ANISOU 2674 O SER B 60 9487 5728 6858 -751 948 302 O ATOM 2675 CB SER B 60 1.269 57.755 13.144 1.00 57.49 C ANISOU 2675 CB SER B 60 8844 5841 7160 -687 776 -67 C ATOM 2676 OG SER B 60 0.437 58.404 12.200 1.00 59.49 O ANISOU 2676 OG SER B 60 9406 6072 7125 -613 501 -60 O ATOM 2677 N SER B 61 3.862 59.106 12.137 1.00 59.46 N ANISOU 2677 N SER B 61 9552 5937 7102 -922 1399 109 N ATOM 2678 CA SER B 61 4.565 59.853 11.089 1.00 60.27 C ANISOU 2678 CA SER B 61 10072 5929 6898 -1029 1632 170 C ATOM 2679 C SER B 61 3.627 60.195 9.916 1.00 61.72 C ANISOU 2679 C SER B 61 10733 6079 6639 -958 1377 204 C ATOM 2680 O SER B 61 3.810 61.236 9.279 1.00 62.58 O ANISOU 2680 O SER B 61 11256 6066 6456 -984 1433 338 O ATOM 2681 CB SER B 61 5.784 59.089 10.599 1.00 60.38 C ANISOU 2681 CB SER B 61 10072 5908 6960 -1186 2055 40 C ATOM 2682 OG SER B 61 5.377 57.837 10.085 1.00 62.45 O ANISOU 2682 OG SER B 61 10324 6235 7168 -1169 1998 -117 O ATOM 2683 N GLY B 62 2.609 59.364 9.689 1.00 61.76 N ANISOU 2683 N GLY B 62 10678 6174 6612 -859 1077 80 N ATOM 2684 CA GLY B 62 1.593 59.598 8.674 1.00 62.47 C ANISOU 2684 CA GLY B 62 11156 6251 6327 -749 722 68 C ATOM 2685 C GLY B 62 0.574 60.666 9.041 1.00 63.26 C ANISOU 2685 C GLY B 62 11279 6319 6439 -574 315 193 C ATOM 2686 O GLY B 62 -0.205 61.085 8.180 1.00 63.74 O ANISOU 2686 O GLY B 62 11709 6334 6176 -452 -22 213 O ATOM 2687 N GLY B 63 0.559 61.096 10.312 1.00 63.10 N ANISOU 2687 N GLY B 63 10875 6310 6788 -550 326 262 N ATOM 2688 CA GLY B 63 -0.326 62.149 10.802 1.00 63.19 C ANISOU 2688 CA GLY B 63 10851 6273 6886 -398 2 362 C ATOM 2689 C GLY B 63 -1.542 61.709 11.596 1.00 63.32 C ANISOU 2689 C GLY B 63 10444 6374 7241 -274 -311 221 C ATOM 2690 O GLY B 63 -2.327 62.564 12.019 1.00 63.83 O ANISOU 2690 O GLY B 63 10438 6387 7428 -146 -569 268 O ATOM 2691 N SER B 64 -1.733 60.381 11.780 1.00 62.46 N ANISOU 2691 N SER B 64 10056 6369 7307 -318 -266 32 N ATOM 2692 CA SER B 64 -2.857 59.811 12.523 1.00 62.20 C ANISOU 2692 CA SER B 64 9618 6391 7625 -242 -474 -138 C ATOM 2693 C SER B 64 -2.706 60.078 14.005 1.00 62.15 C ANISOU 2693 C SER B 64 9271 6385 7956 -273 -307 -69 C ATOM 2694 O SER B 64 -1.610 59.929 14.537 1.00 62.92 O ANISOU 2694 O SER B 64 9317 6496 8094 -382 11 22 O ATOM 2695 CB SER B 64 -2.922 58.307 12.311 1.00 63.70 C ANISOU 2695 CB SER B 64 9649 6653 7903 -314 -381 -343 C ATOM 2696 OG SER B 64 -3.268 58.004 10.973 1.00 66.95 O ANISOU 2696 OG SER B 64 10352 7073 8011 -276 -593 -463 O ATOM 2697 N THR B 65 -3.800 60.434 14.694 1.00 61.08 N ANISOU 2697 N THR B 65 8896 6232 8080 -177 -522 -140 N ATOM 2698 CA THR B 65 -3.729 60.747 16.123 1.00 60.25 C ANISOU 2698 CA THR B 65 8519 6119 8254 -211 -360 -87 C ATOM 2699 C THR B 65 -4.556 59.795 16.982 1.00 59.20 C ANISOU 2699 C THR B 65 8027 6007 8457 -230 -322 -272 C ATOM 2700 O THR B 65 -5.632 59.364 16.567 1.00 59.81 O ANISOU 2700 O THR B 65 7990 6077 8656 -171 -536 -472 O ATOM 2701 CB THR B 65 -4.162 62.209 16.364 1.00 61.53 C ANISOU 2701 CB THR B 65 8737 6198 8444 -110 -539 7 C ATOM 2702 OG1 THR B 65 -5.532 62.353 16.012 1.00 63.10 O ANISOU 2702 OG1 THR B 65 8845 6357 8772 33 -897 -152 O ATOM 2703 CG2 THR B 65 -3.346 63.211 15.564 1.00 61.29 C ANISOU 2703 CG2 THR B 65 9100 6099 8090 -105 -526 206 C ATOM 2704 N VAL B 66 -4.060 59.465 18.181 1.00 57.55 N ANISOU 2704 N VAL B 66 7658 5810 8400 -315 -51 -219 N ATOM 2705 CA VAL B 66 -4.786 58.621 19.141 1.00 56.41 C ANISOU 2705 CA VAL B 66 7238 5644 8551 -354 62 -360 C ATOM 2706 C VAL B 66 -4.784 59.293 20.503 1.00 55.76 C ANISOU 2706 C VAL B 66 7058 5531 8598 -372 188 -283 C ATOM 2707 O VAL B 66 -3.826 59.987 20.840 1.00 56.19 O ANISOU 2707 O VAL B 66 7230 5605 8516 -387 262 -111 O ATOM 2708 CB VAL B 66 -4.336 57.134 19.223 1.00 56.56 C ANISOU 2708 CB VAL B 66 7209 5675 8606 -441 284 -408 C ATOM 2709 CG1 VAL B 66 -4.669 56.398 17.948 1.00 57.51 C ANISOU 2709 CG1 VAL B 66 7377 5814 8659 -432 153 -566 C ATOM 2710 CG2 VAL B 66 -2.857 56.995 19.550 1.00 56.40 C ANISOU 2710 CG2 VAL B 66 7304 5683 8442 -489 494 -222 C ATOM 2711 N TYR B 67 -5.851 59.102 21.284 1.00 54.90 N ANISOU 2711 N TYR B 67 6734 5363 8762 -385 231 -435 N ATOM 2712 CA TYR B 67 -5.985 59.712 22.604 1.00 54.70 C ANISOU 2712 CA TYR B 67 6639 5295 8851 -415 375 -399 C ATOM 2713 C TYR B 67 -6.398 58.687 23.638 1.00 55.02 C ANISOU 2713 C TYR B 67 6563 5274 9066 -510 649 -491 C ATOM 2714 O TYR B 67 -7.182 57.793 23.310 1.00 55.19 O ANISOU 2714 O TYR B 67 6448 5248 9271 -538 674 -675 O ATOM 2715 CB TYR B 67 -7.056 60.832 22.553 1.00 54.37 C ANISOU 2715 CB TYR B 67 6474 5190 8993 -332 178 -516 C ATOM 2716 CG TYR B 67 -6.682 61.948 21.605 1.00 54.26 C ANISOU 2716 CG TYR B 67 6640 5190 8785 -226 -85 -391 C ATOM 2717 CD1 TYR B 67 -7.092 61.927 20.277 1.00 54.64 C ANISOU 2717 CD1 TYR B 67 6759 5238 8762 -126 -377 -454 C ATOM 2718 CD2 TYR B 67 -5.823 62.960 21.999 1.00 54.46 C ANISOU 2718 CD2 TYR B 67 6811 5217 8663 -234 -26 -206 C ATOM 2719 CE1 TYR B 67 -6.676 62.901 19.377 1.00 54.95 C ANISOU 2719 CE1 TYR B 67 7061 5261 8557 -34 -583 -304 C ATOM 2720 CE2 TYR B 67 -5.409 63.946 21.108 1.00 54.83 C ANISOU 2720 CE2 TYR B 67 7071 5239 8522 -159 -204 -76 C ATOM 2721 CZ TYR B 67 -5.834 63.910 19.796 1.00 55.08 C ANISOU 2721 CZ TYR B 67 7224 5254 8452 -59 -471 -109 C ATOM 2722 OH TYR B 67 -5.454 64.889 18.917 1.00 55.28 O ANISOU 2722 OH TYR B 67 7536 5219 8250 16 -626 40 O ATOM 2723 N SER B 68 -5.905 58.810 24.891 1.00 54.89 N ANISOU 2723 N SER B 68 6622 5242 8992 -564 857 -378 N ATOM 2724 CA SER B 68 -6.375 57.923 25.949 1.00 55.60 C ANISOU 2724 CA SER B 68 6681 5235 9209 -657 1145 -448 C ATOM 2725 C SER B 68 -7.801 58.343 26.316 1.00 57.72 C ANISOU 2725 C SER B 68 6740 5403 9787 -689 1204 -683 C ATOM 2726 O SER B 68 -8.215 59.474 26.022 1.00 58.49 O ANISOU 2726 O SER B 68 6743 5514 9967 -619 1009 -741 O ATOM 2727 CB SER B 68 -5.455 57.943 27.159 1.00 55.80 C ANISOU 2727 CB SER B 68 6904 5263 9034 -686 1307 -264 C ATOM 2728 OG SER B 68 -5.556 59.145 27.897 1.00 58.21 O ANISOU 2728 OG SER B 68 7225 5574 9318 -686 1298 -254 O ATOM 2729 N GLU B 69 -8.579 57.426 26.893 1.00 58.38 N ANISOU 2729 N GLU B 69 6740 5361 10079 -794 1481 -838 N ATOM 2730 CA GLU B 69 -9.963 57.702 27.235 1.00 59.62 C ANISOU 2730 CA GLU B 69 6649 5397 10607 -849 1596 -1118 C ATOM 2731 C GLU B 69 -10.100 58.833 28.233 1.00 60.25 C ANISOU 2731 C GLU B 69 6763 5448 10682 -863 1693 -1102 C ATOM 2732 O GLU B 69 -11.091 59.556 28.184 1.00 60.92 O ANISOU 2732 O GLU B 69 6605 5469 11074 -844 1639 -1322 O ATOM 2733 CB GLU B 69 -10.679 56.438 27.729 1.00 62.75 C ANISOU 2733 CB GLU B 69 6978 5631 11232 -997 1967 -1290 C ATOM 2734 CG GLU B 69 -10.696 55.311 26.714 1.00 69.57 C ANISOU 2734 CG GLU B 69 7764 6501 12167 -995 1884 -1367 C ATOM 2735 CD GLU B 69 -11.562 55.554 25.494 1.00 79.68 C ANISOU 2735 CD GLU B 69 8731 7818 13725 -915 1548 -1637 C ATOM 2736 OE1 GLU B 69 -11.025 55.493 24.364 1.00 80.75 O ANISOU 2736 OE1 GLU B 69 8927 8081 13675 -812 1230 -1559 O ATOM 2737 OE2 GLU B 69 -12.777 55.812 25.665 1.00 84.38 O ANISOU 2737 OE2 GLU B 69 9027 8307 14727 -952 1597 -1942 O ATOM 2738 N SER B 70 -9.115 59.018 29.127 1.00 60.02 N ANISOU 2738 N SER B 70 7019 5459 10326 -887 1811 -868 N ATOM 2739 CA SER B 70 -9.180 60.093 30.123 1.00 60.33 C ANISOU 2739 CA SER B 70 7121 5475 10326 -912 1909 -867 C ATOM 2740 C SER B 70 -8.950 61.511 29.562 1.00 59.80 C ANISOU 2740 C SER B 70 6978 5493 10249 -792 1583 -829 C ATOM 2741 O SER B 70 -9.273 62.492 30.233 1.00 60.12 O ANISOU 2741 O SER B 70 6994 5488 10362 -809 1652 -899 O ATOM 2742 CB SER B 70 -8.220 59.820 31.277 1.00 62.49 C ANISOU 2742 CB SER B 70 7741 5761 10240 -967 2097 -658 C ATOM 2743 OG SER B 70 -6.917 59.534 30.799 1.00 66.60 O ANISOU 2743 OG SER B 70 8411 6412 10482 -880 1875 -422 O ATOM 2744 N VAL B 71 -8.386 61.631 28.353 1.00 58.90 N ANISOU 2744 N VAL B 71 6862 5482 10036 -680 1263 -720 N ATOM 2745 CA VAL B 71 -8.110 62.945 27.757 1.00 58.65 C ANISOU 2745 CA VAL B 71 6827 5495 9964 -570 982 -652 C ATOM 2746 C VAL B 71 -8.807 63.174 26.404 1.00 60.75 C ANISOU 2746 C VAL B 71 6932 5743 10406 -445 664 -759 C ATOM 2747 O VAL B 71 -8.652 64.253 25.828 1.00 61.55 O ANISOU 2747 O VAL B 71 7076 5843 10467 -339 424 -689 O ATOM 2748 CB VAL B 71 -6.580 63.232 27.639 1.00 56.78 C ANISOU 2748 CB VAL B 71 6827 5373 9374 -550 897 -390 C ATOM 2749 CG1 VAL B 71 -5.822 62.861 28.906 1.00 56.48 C ANISOU 2749 CG1 VAL B 71 6958 5360 9142 -639 1123 -294 C ATOM 2750 CG2 VAL B 71 -5.975 62.554 26.425 1.00 56.03 C ANISOU 2750 CG2 VAL B 71 6793 5353 9141 -503 740 -291 C ATOM 2751 N LYS B 72 -9.532 62.169 25.891 1.00 61.59 N ANISOU 2751 N LYS B 72 6885 5824 10693 -454 652 -925 N ATOM 2752 CA LYS B 72 -10.161 62.173 24.576 1.00 63.53 C ANISOU 2752 CA LYS B 72 7004 6067 11068 -330 309 -1049 C ATOM 2753 C LYS B 72 -11.018 63.413 24.253 1.00 64.93 C ANISOU 2753 C LYS B 72 7026 6157 11487 -185 29 -1176 C ATOM 2754 O LYS B 72 -10.905 63.962 23.150 1.00 65.63 O ANISOU 2754 O LYS B 72 7219 6264 11453 -35 -334 -1100 O ATOM 2755 CB LYS B 72 -10.973 60.898 24.389 1.00 66.60 C ANISOU 2755 CB LYS B 72 7187 6415 11705 -395 401 -1290 C ATOM 2756 CG LYS B 72 -11.134 60.451 22.949 1.00 73.03 C ANISOU 2756 CG LYS B 72 7980 7281 12487 -294 59 -1363 C ATOM 2757 CD LYS B 72 -11.855 59.090 22.914 1.00 79.26 C ANISOU 2757 CD LYS B 72 8549 8018 13549 -396 214 -1627 C ATOM 2758 CE LYS B 72 -11.929 58.439 21.553 1.00 83.76 C ANISOU 2758 CE LYS B 72 9120 8650 14053 -327 -85 -1723 C ATOM 2759 NZ LYS B 72 -10.588 58.287 20.954 1.00 86.41 N ANISOU 2759 NZ LYS B 72 9808 9107 13915 -316 -121 -1425 N ATOM 2760 N ASP B 73 -11.847 63.871 25.192 1.00 64.91 N ANISOU 2760 N ASP B 73 6808 6042 11815 -223 200 -1364 N ATOM 2761 CA ASP B 73 -12.709 65.029 24.926 1.00 65.25 C ANISOU 2761 CA ASP B 73 6664 5971 12157 -68 -69 -1512 C ATOM 2762 C ASP B 73 -12.043 66.380 25.198 1.00 64.02 C ANISOU 2762 C ASP B 73 6707 5796 11820 -12 -113 -1300 C ATOM 2763 O ASP B 73 -12.735 67.408 25.170 1.00 64.97 O ANISOU 2763 O ASP B 73 6679 5789 12217 110 -279 -1418 O ATOM 2764 CB ASP B 73 -13.987 64.938 25.776 1.00 68.92 C ANISOU 2764 CB ASP B 73 6749 6290 13147 -138 163 -1874 C ATOM 2765 CG ASP B 73 -14.873 63.728 25.523 1.00 78.64 C ANISOU 2765 CG ASP B 73 7701 7486 14694 -203 228 -2169 C ATOM 2766 OD1 ASP B 73 -15.904 63.596 26.228 1.00 81.57 O ANISOU 2766 OD1 ASP B 73 7748 7716 15529 -292 485 -2494 O ATOM 2767 OD2 ASP B 73 -14.549 62.918 24.603 1.00 81.52 O ANISOU 2767 OD2 ASP B 73 8161 7949 14864 -175 44 -2102 O ATOM 2768 N ARG B 74 -10.735 66.395 25.527 1.00 61.37 N ANISOU 2768 N ARG B 74 6673 5566 11077 -103 47 -1021 N ATOM 2769 CA ARG B 74 -10.079 67.617 25.964 1.00 58.82 C ANISOU 2769 CA ARG B 74 6509 5216 10624 -94 74 -865 C ATOM 2770 C ARG B 74 -8.742 67.944 25.324 1.00 57.76 C ANISOU 2770 C ARG B 74 6691 5165 10089 -76 -32 -568 C ATOM 2771 O ARG B 74 -8.370 69.112 25.323 1.00 57.87 O ANISOU 2771 O ARG B 74 6818 5112 10057 -30 -94 -466 O ATOM 2772 CB ARG B 74 -9.833 67.533 27.469 1.00 58.47 C ANISOU 2772 CB ARG B 74 6472 5182 10562 -267 472 -899 C ATOM 2773 CG ARG B 74 -11.035 67.172 28.315 1.00 59.96 C ANISOU 2773 CG ARG B 74 6397 5267 11119 -346 720 -1196 C ATOM 2774 CD ARG B 74 -10.625 66.282 29.474 1.00 62.10 C ANISOU 2774 CD ARG B 74 6802 5587 11207 -537 1120 -1170 C ATOM 2775 NE ARG B 74 -9.748 67.023 30.364 1.00 62.85 N ANISOU 2775 NE ARG B 74 7113 5717 11048 -597 1242 -1034 N ATOM 2776 CZ ARG B 74 -8.826 66.486 31.147 1.00 62.41 C ANISOU 2776 CZ ARG B 74 7303 5751 10660 -702 1425 -889 C ATOM 2777 NH1 ARG B 74 -8.657 65.170 31.182 1.00 58.75 N ANISOU 2777 NH1 ARG B 74 6919 5330 10074 -759 1540 -837 N ATOM 2778 NH2 ARG B 74 -8.064 67.259 31.903 1.00 63.13 N ANISOU 2778 NH2 ARG B 74 7562 5875 10549 -740 1473 -807 N ATOM 2779 N PHE B 75 -7.950 66.941 24.908 1.00 56.88 N ANISOU 2779 N PHE B 75 6719 5180 9712 -136 12 -445 N ATOM 2780 CA PHE B 75 -6.611 67.221 24.361 1.00 55.90 C ANISOU 2780 CA PHE B 75 6868 5121 9250 -150 -17 -200 C ATOM 2781 C PHE B 75 -6.576 67.131 22.837 1.00 56.18 C ANISOU 2781 C PHE B 75 7058 5153 9133 -41 -285 -124 C ATOM 2782 O PHE B 75 -7.394 66.432 22.241 1.00 56.30 O ANISOU 2782 O PHE B 75 6970 5174 9248 23 -443 -257 O ATOM 2783 CB PHE B 75 -5.522 66.293 24.974 1.00 54.42 C ANISOU 2783 CB PHE B 75 6755 5060 8861 -287 227 -109 C ATOM 2784 CG PHE B 75 -5.198 66.407 26.453 1.00 53.55 C ANISOU 2784 CG PHE B 75 6618 4967 8760 -392 466 -128 C ATOM 2785 CD1 PHE B 75 -6.016 67.122 27.311 1.00 53.72 C ANISOU 2785 CD1 PHE B 75 6523 4899 8988 -400 541 -265 C ATOM 2786 CD2 PHE B 75 -4.095 65.773 26.986 1.00 54.08 C ANISOU 2786 CD2 PHE B 75 6788 5131 8630 -472 603 -27 C ATOM 2787 CE1 PHE B 75 -5.731 67.205 28.674 1.00 54.05 C ANISOU 2787 CE1 PHE B 75 6598 4956 8982 -503 764 -294 C ATOM 2788 CE2 PHE B 75 -3.812 65.858 28.348 1.00 54.54 C ANISOU 2788 CE2 PHE B 75 6872 5202 8647 -548 771 -47 C ATOM 2789 CZ PHE B 75 -4.637 66.564 29.182 1.00 53.97 C ANISOU 2789 CZ PHE B 75 6731 5050 8727 -571 859 -178 C ATOM 2790 N THR B 76 -5.624 67.837 22.215 1.00 56.33 N ANISOU 2790 N THR B 76 7342 5152 8907 -32 -320 73 N ATOM 2791 CA THR B 76 -5.387 67.783 20.777 1.00 57.23 C ANISOU 2791 CA THR B 76 7711 5252 8781 43 -511 178 C ATOM 2792 C THR B 76 -3.881 67.692 20.539 1.00 58.28 C ANISOU 2792 C THR B 76 8064 5444 8637 -82 -293 352 C ATOM 2793 O THR B 76 -3.148 68.545 21.011 1.00 58.73 O ANISOU 2793 O THR B 76 8180 5455 8680 -145 -149 442 O ATOM 2794 CB THR B 76 -5.933 69.012 20.040 1.00 58.42 C ANISOU 2794 CB THR B 76 8031 5234 8932 210 -795 236 C ATOM 2795 OG1 THR B 76 -7.234 69.346 20.517 1.00 60.26 O ANISOU 2795 OG1 THR B 76 7992 5386 9518 328 -972 47 O ATOM 2796 CG2 THR B 76 -5.972 68.818 18.538 1.00 58.29 C ANISOU 2796 CG2 THR B 76 8322 5192 8633 311 -1040 318 C ATOM 2797 N ILE B 77 -3.418 66.662 19.833 1.00 58.62 N ANISOU 2797 N ILE B 77 8195 5576 8502 -127 -252 365 N ATOM 2798 CA ILE B 77 -2.012 66.529 19.479 1.00 59.76 C ANISOU 2798 CA ILE B 77 8519 5754 8432 -243 -33 489 C ATOM 2799 C ILE B 77 -1.869 66.952 18.006 1.00 61.75 C ANISOU 2799 C ILE B 77 9141 5917 8406 -193 -143 595 C ATOM 2800 O ILE B 77 -2.742 66.667 17.175 1.00 62.27 O ANISOU 2800 O ILE B 77 9300 5967 8391 -77 -402 543 O ATOM 2801 CB ILE B 77 -1.455 65.098 19.756 1.00 59.88 C ANISOU 2801 CB ILE B 77 8395 5904 8452 -335 139 427 C ATOM 2802 CG1 ILE B 77 0.090 65.052 19.711 1.00 59.93 C ANISOU 2802 CG1 ILE B 77 8482 5934 8353 -456 389 510 C ATOM 2803 CG2 ILE B 77 -2.081 64.043 18.846 1.00 60.21 C ANISOU 2803 CG2 ILE B 77 8463 5987 8427 -289 10 334 C ATOM 2804 CD1 ILE B 77 0.710 63.779 20.191 1.00 60.13 C ANISOU 2804 CD1 ILE B 77 8344 6063 8441 -518 537 454 C ATOM 2805 N SER B 78 -0.822 67.707 17.700 1.00 62.68 N ANISOU 2805 N SER B 78 9486 5952 8378 -277 46 730 N ATOM 2806 CA SER B 78 -0.559 68.151 16.336 1.00 64.31 C ANISOU 2806 CA SER B 78 10128 6038 8270 -259 23 854 C ATOM 2807 C SER B 78 0.940 68.241 16.080 1.00 66.77 C ANISOU 2807 C SER B 78 10586 6319 8464 -444 404 924 C ATOM 2808 O SER B 78 1.720 68.237 17.030 1.00 66.61 O ANISOU 2808 O SER B 78 10309 6352 8648 -555 617 880 O ATOM 2809 CB SER B 78 -1.268 69.464 16.030 1.00 64.63 C ANISOU 2809 CB SER B 78 10392 5887 8276 -116 -206 958 C ATOM 2810 OG SER B 78 -1.013 70.417 17.042 1.00 66.66 O ANISOU 2810 OG SER B 78 10494 6074 8759 -161 -78 982 O ATOM 2811 N ARG B 79 1.355 68.245 14.800 1.00 68.81 N ANISOU 2811 N ARG B 79 11252 6491 8401 -483 496 1003 N ATOM 2812 CA ARG B 79 2.778 68.304 14.483 1.00 71.16 C ANISOU 2812 CA ARG B 79 11675 6735 8628 -682 917 1028 C ATOM 2813 C ARG B 79 3.079 69.236 13.357 1.00 74.59 C ANISOU 2813 C ARG B 79 12654 6942 8743 -719 1046 1186 C ATOM 2814 O ARG B 79 2.270 69.393 12.444 1.00 75.51 O ANISOU 2814 O ARG B 79 13146 6982 8561 -582 785 1273 O ATOM 2815 CB ARG B 79 3.377 66.912 14.209 1.00 71.24 C ANISOU 2815 CB ARG B 79 11561 6888 8620 -775 1087 902 C ATOM 2816 CG ARG B 79 2.960 66.280 12.881 1.00 72.55 C ANISOU 2816 CG ARG B 79 12085 7050 8430 -733 990 899 C ATOM 2817 CD ARG B 79 3.387 64.818 12.774 1.00 73.48 C ANISOU 2817 CD ARG B 79 12003 7314 8601 -807 1130 741 C ATOM 2818 NE ARG B 79 4.843 64.683 12.821 1.00 73.75 N ANISOU 2818 NE ARG B 79 11959 7317 8748 -998 1574 693 N ATOM 2819 CZ ARG B 79 5.486 63.580 13.180 1.00 73.69 C ANISOU 2819 CZ ARG B 79 11632 7415 8954 -1062 1735 551 C ATOM 2820 NH1 ARG B 79 4.810 62.493 13.523 1.00 72.79 N ANISOU 2820 NH1 ARG B 79 11286 7436 8935 -967 1522 463 N ATOM 2821 NH2 ARG B 79 6.811 63.556 13.204 1.00 72.65 N ANISOU 2821 NH2 ARG B 79 11398 7230 8975 -1219 2115 480 N ATOM 2822 N ASP B 80 4.260 69.856 13.418 1.00 76.41 N ANISOU 2822 N ASP B 80 12943 7050 9040 -905 1451 1211 N ATOM 2823 CA ASP B 80 4.781 70.749 12.392 1.00 78.47 C ANISOU 2823 CA ASP B 80 13749 7050 9016 -1003 1718 1357 C ATOM 2824 C ASP B 80 6.173 70.223 12.055 1.00 79.75 C ANISOU 2824 C ASP B 80 13882 7209 9212 -1251 2227 1243 C ATOM 2825 O ASP B 80 7.134 70.551 12.741 1.00 80.15 O ANISOU 2825 O ASP B 80 13639 7231 9584 -1406 2524 1150 O ATOM 2826 CB ASP B 80 4.855 72.191 12.910 1.00 81.11 C ANISOU 2826 CB ASP B 80 14129 7181 9508 -1013 1778 1460 C ATOM 2827 CG ASP B 80 5.021 73.225 11.816 1.00 89.42 C ANISOU 2827 CG ASP B 80 15847 7910 10220 -1053 1963 1665 C ATOM 2828 OD1 ASP B 80 4.688 74.412 12.066 1.00 91.22 O ANISOU 2828 OD1 ASP B 80 16211 7937 10512 -983 1883 1791 O ATOM 2829 OD2 ASP B 80 5.481 72.851 10.697 1.00 92.60 O ANISOU 2829 OD2 ASP B 80 16669 8236 10278 -1155 2206 1702 O ATOM 2830 N ASN B 81 6.275 69.376 11.030 1.00 80.19 N ANISOU 2830 N ASN B 81 14205 7295 8971 -1287 2317 1213 N ATOM 2831 CA ASN B 81 7.551 68.789 10.644 1.00 81.33 C ANISOU 2831 CA ASN B 81 14305 7424 9173 -1520 2817 1069 C ATOM 2832 C ASN B 81 8.569 69.817 10.192 1.00 82.42 C ANISOU 2832 C ASN B 81 14753 7281 9282 -1742 3333 1117 C ATOM 2833 O ASN B 81 9.763 69.561 10.336 1.00 82.90 O ANISOU 2833 O ASN B 81 14557 7322 9619 -1952 3772 939 O ATOM 2834 CB ASN B 81 7.356 67.747 9.553 1.00 82.46 C ANISOU 2834 CB ASN B 81 14741 7630 8961 -1515 2818 1022 C ATOM 2835 CG ASN B 81 6.856 66.423 10.046 1.00 84.70 C ANISOU 2835 CG ASN B 81 14586 8182 9415 -1397 2522 875 C ATOM 2836 OD1 ASN B 81 6.882 66.132 11.240 1.00 86.10 O ANISOU 2836 OD1 ASN B 81 14219 8501 9994 -1351 2400 792 O ATOM 2837 ND2 ASN B 81 6.390 65.590 9.133 1.00 84.99 N ANISOU 2837 ND2 ASN B 81 14882 8278 9132 -1352 2410 834 N ATOM 2838 N ALA B 82 8.117 70.981 9.666 1.00 82.59 N ANISOU 2838 N ALA B 82 15311 7062 9007 -1697 3293 1342 N ATOM 2839 CA ALA B 82 9.019 72.038 9.192 1.00 83.17 C ANISOU 2839 CA ALA B 82 15755 6812 9033 -1921 3826 1409 C ATOM 2840 C ALA B 82 9.757 72.686 10.358 1.00 83.05 C ANISOU 2840 C ALA B 82 15212 6771 9573 -2041 4017 1283 C ATOM 2841 O ALA B 82 10.946 72.969 10.253 1.00 83.53 O ANISOU 2841 O ALA B 82 15217 6675 9845 -2303 4566 1151 O ATOM 2842 CB ALA B 82 8.247 73.087 8.403 1.00 83.51 C ANISOU 2842 CB ALA B 82 16529 6587 8616 -1799 3669 1706 C ATOM 2843 N LYS B 83 9.049 72.914 11.462 1.00 82.27 N ANISOU 2843 N LYS B 83 14720 6817 9720 -1858 3575 1294 N ATOM 2844 CA LYS B 83 9.613 73.465 12.696 1.00 81.87 C ANISOU 2844 CA LYS B 83 14148 6785 10173 -1939 3656 1153 C ATOM 2845 C LYS B 83 10.096 72.340 13.649 1.00 80.72 C ANISOU 2845 C LYS B 83 13323 6943 10402 -1945 3571 899 C ATOM 2846 O LYS B 83 10.648 72.649 14.705 1.00 81.22 O ANISOU 2846 O LYS B 83 12933 7054 10874 -2003 3601 746 O ATOM 2847 CB LYS B 83 8.553 74.324 13.420 1.00 84.08 C ANISOU 2847 CB LYS B 83 14396 7048 10501 -1736 3231 1288 C ATOM 2848 CG LYS B 83 8.036 75.488 12.583 1.00 89.25 C ANISOU 2848 CG LYS B 83 15704 7377 10832 -1683 3246 1550 C ATOM 2849 CD LYS B 83 6.984 76.320 13.328 1.00 95.42 C ANISOU 2849 CD LYS B 83 16395 8129 11731 -1468 2821 1649 C ATOM 2850 CE LYS B 83 6.493 77.494 12.494 1.00 99.43 C ANISOU 2850 CE LYS B 83 17564 8273 11943 -1386 2812 1919 C ATOM 2851 NZ LYS B 83 5.637 78.428 13.280 1.00101.13 N ANISOU 2851 NZ LYS B 83 17644 8413 12368 -1199 2470 1979 N ATOM 2852 N LYS B 84 9.852 71.052 13.291 1.00 78.86 N ANISOU 2852 N LYS B 84 13041 6901 10019 -1868 3437 855 N ATOM 2853 CA LYS B 84 10.152 69.846 14.052 1.00 77.47 C ANISOU 2853 CA LYS B 84 12323 6988 10125 -1829 3312 661 C ATOM 2854 C LYS B 84 9.573 69.935 15.471 1.00 74.67 C ANISOU 2854 C LYS B 84 11553 6802 10017 -1672 2908 643 C ATOM 2855 O LYS B 84 10.261 69.653 16.452 1.00 74.80 O ANISOU 2855 O LYS B 84 11107 6925 10390 -1707 2917 470 O ATOM 2856 CB LYS B 84 11.664 69.541 14.058 1.00 80.53 C ANISOU 2856 CB LYS B 84 12420 7330 10850 -2050 3768 420 C ATOM 2857 CG LYS B 84 12.220 69.071 12.704 1.00 85.57 C ANISOU 2857 CG LYS B 84 13405 7843 11266 -2209 4195 380 C ATOM 2858 CD LYS B 84 13.334 68.025 12.812 1.00 90.07 C ANISOU 2858 CD LYS B 84 13536 8494 12193 -2316 4450 98 C ATOM 2859 CE LYS B 84 14.455 68.406 13.741 1.00 94.09 C ANISOU 2859 CE LYS B 84 13514 8973 13263 -2429 4618 -135 C ATOM 2860 NZ LYS B 84 15.117 69.667 13.319 1.00 96.58 N ANISOU 2860 NZ LYS B 84 14048 8998 13648 -2669 5092 -161 N ATOM 2861 N ILE B 85 8.312 70.360 15.576 1.00 72.00 N ANISOU 2861 N ILE B 85 11397 6471 9490 -1497 2553 808 N ATOM 2862 CA ILE B 85 7.638 70.518 16.858 1.00 69.79 C ANISOU 2862 CA ILE B 85 10789 6321 9407 -1361 2215 790 C ATOM 2863 C ILE B 85 6.346 69.713 16.895 1.00 66.66 C ANISOU 2863 C ILE B 85 10388 6080 8859 -1160 1827 843 C ATOM 2864 O ILE B 85 5.608 69.664 15.917 1.00 66.46 O ANISOU 2864 O ILE B 85 10714 5997 8540 -1078 1707 955 O ATOM 2865 CB ILE B 85 7.368 72.032 17.159 1.00 70.80 C ANISOU 2865 CB ILE B 85 11057 6259 9585 -1364 2208 881 C ATOM 2866 CG1 ILE B 85 8.671 72.792 17.455 1.00 72.62 C ANISOU 2866 CG1 ILE B 85 11152 6356 10085 -1578 2582 758 C ATOM 2867 CG2 ILE B 85 6.399 72.224 18.320 1.00 71.14 C ANISOU 2867 CG2 ILE B 85 10851 6414 9764 -1206 1849 872 C ATOM 2868 CD1 ILE B 85 8.510 74.348 17.606 1.00 74.21 C ANISOU 2868 CD1 ILE B 85 11546 6313 10339 -1616 2658 843 C ATOM 2869 N VAL B 86 6.055 69.116 18.038 1.00 64.16 N ANISOU 2869 N VAL B 86 9691 5944 8743 -1082 1627 752 N ATOM 2870 CA VAL B 86 4.793 68.439 18.261 1.00 62.39 C ANISOU 2870 CA VAL B 86 9409 5842 8456 -916 1303 768 C ATOM 2871 C VAL B 86 4.114 69.185 19.405 1.00 61.23 C ANISOU 2871 C VAL B 86 9091 5698 8476 -841 1122 763 C ATOM 2872 O VAL B 86 4.735 69.387 20.440 1.00 61.87 O ANISOU 2872 O VAL B 86 8927 5823 8756 -903 1195 680 O ATOM 2873 CB VAL B 86 4.967 66.931 18.554 1.00 62.01 C ANISOU 2873 CB VAL B 86 9114 5970 8475 -902 1284 663 C ATOM 2874 CG1 VAL B 86 3.690 66.326 19.128 1.00 62.05 C ANISOU 2874 CG1 VAL B 86 8986 6081 8509 -761 1000 644 C ATOM 2875 CG2 VAL B 86 5.400 66.192 17.299 1.00 61.96 C ANISOU 2875 CG2 VAL B 86 9309 5948 8287 -961 1446 653 C ATOM 2876 N TYR B 87 2.861 69.619 19.224 1.00 59.42 N ANISOU 2876 N TYR B 87 8985 5412 8179 -705 880 827 N ATOM 2877 CA TYR B 87 2.134 70.319 20.282 1.00 58.15 C ANISOU 2877 CA TYR B 87 8656 5236 8203 -636 737 793 C ATOM 2878 C TYR B 87 1.111 69.431 20.962 1.00 55.79 C ANISOU 2878 C TYR B 87 8125 5075 7998 -538 546 700 C ATOM 2879 O TYR B 87 0.525 68.569 20.323 1.00 55.80 O ANISOU 2879 O TYR B 87 8167 5129 7907 -471 427 688 O ATOM 2880 CB TYR B 87 1.371 71.517 19.708 1.00 58.69 C ANISOU 2880 CB TYR B 87 8982 5102 8215 -536 600 900 C ATOM 2881 CG TYR B 87 2.238 72.514 18.986 1.00 60.37 C ANISOU 2881 CG TYR B 87 9503 5115 8318 -634 817 1016 C ATOM 2882 CD1 TYR B 87 2.318 72.519 17.601 1.00 61.73 C ANISOU 2882 CD1 TYR B 87 10084 5171 8201 -621 844 1145 C ATOM 2883 CD2 TYR B 87 2.951 73.479 19.684 1.00 61.64 C ANISOU 2883 CD2 TYR B 87 9578 5184 8660 -749 1012 985 C ATOM 2884 CE1 TYR B 87 3.109 73.441 16.928 1.00 63.10 C ANISOU 2884 CE1 TYR B 87 10597 5121 8258 -732 1108 1259 C ATOM 2885 CE2 TYR B 87 3.717 74.427 19.023 1.00 63.14 C ANISOU 2885 CE2 TYR B 87 10055 5150 8786 -859 1260 1077 C ATOM 2886 CZ TYR B 87 3.794 74.408 17.640 1.00 64.80 C ANISOU 2886 CZ TYR B 87 10697 5226 8699 -855 1329 1225 C ATOM 2887 OH TYR B 87 4.574 75.333 16.968 1.00 67.69 O ANISOU 2887 OH TYR B 87 11401 5334 8983 -990 1643 1323 O ATOM 2888 N LEU B 88 0.847 69.693 22.243 1.00 53.91 N ANISOU 2888 N LEU B 88 7665 4874 7943 -540 534 618 N ATOM 2889 CA LEU B 88 -0.222 69.039 22.982 1.00 52.33 C ANISOU 2889 CA LEU B 88 7274 4754 7855 -469 417 518 C ATOM 2890 C LEU B 88 -1.065 70.160 23.554 1.00 52.14 C ANISOU 2890 C LEU B 88 7203 4619 7991 -411 337 475 C ATOM 2891 O LEU B 88 -0.624 70.847 24.465 1.00 52.25 O ANISOU 2891 O LEU B 88 7150 4615 8087 -479 441 439 O ATOM 2892 CB LEU B 88 0.265 68.113 24.111 1.00 51.01 C ANISOU 2892 CB LEU B 88 6922 4727 7732 -536 526 444 C ATOM 2893 CG LEU B 88 -0.859 67.268 24.773 1.00 50.65 C ANISOU 2893 CG LEU B 88 6735 4732 7778 -489 477 347 C ATOM 2894 CD1 LEU B 88 -1.507 66.314 23.764 1.00 50.58 C ANISOU 2894 CD1 LEU B 88 6747 4740 7733 -429 382 334 C ATOM 2895 CD2 LEU B 88 -0.350 66.512 25.994 1.00 50.09 C ANISOU 2895 CD2 LEU B 88 6575 4756 7702 -547 591 309 C ATOM 2896 N GLN B 89 -2.235 70.404 22.977 1.00 51.85 N ANISOU 2896 N GLN B 89 7196 4491 8014 -280 138 460 N ATOM 2897 CA GLN B 89 -3.150 71.417 23.481 1.00 52.28 C ANISOU 2897 CA GLN B 89 7166 4416 8282 -202 50 389 C ATOM 2898 C GLN B 89 -3.992 70.701 24.539 1.00 52.29 C ANISOU 2898 C GLN B 89 6895 4502 8471 -214 91 209 C ATOM 2899 O GLN B 89 -4.632 69.704 24.229 1.00 51.72 O ANISOU 2899 O GLN B 89 6737 4490 8424 -173 15 139 O ATOM 2900 CB GLN B 89 -4.041 71.955 22.345 1.00 54.16 C ANISOU 2900 CB GLN B 89 7549 4500 8532 -24 -228 436 C ATOM 2901 CG GLN B 89 -5.069 72.984 22.792 1.00 57.29 C ANISOU 2901 CG GLN B 89 7824 4732 9213 91 -353 342 C ATOM 2902 CD GLN B 89 -4.413 74.212 23.356 1.00 62.44 C ANISOU 2902 CD GLN B 89 8549 5266 9910 18 -187 397 C ATOM 2903 OE1 GLN B 89 -3.523 74.814 22.741 1.00 63.42 O ANISOU 2903 OE1 GLN B 89 8939 5300 9858 -23 -121 563 O ATOM 2904 NE2 GLN B 89 -4.839 74.606 24.548 1.00 63.95 N ANISOU 2904 NE2 GLN B 89 8512 5439 10345 -17 -86 238 N ATOM 2905 N MET B 90 -3.934 71.156 25.792 1.00 52.44 N ANISOU 2905 N MET B 90 6803 4518 8604 -289 243 122 N ATOM 2906 CA MET B 90 -4.669 70.529 26.879 1.00 52.89 C ANISOU 2906 CA MET B 90 6670 4627 8801 -330 357 -46 C ATOM 2907 C MET B 90 -5.745 71.459 27.373 1.00 54.77 C ANISOU 2907 C MET B 90 6770 4717 9322 -275 343 -199 C ATOM 2908 O MET B 90 -5.438 72.480 27.987 1.00 55.19 O ANISOU 2908 O MET B 90 6850 4703 9418 -315 424 -214 O ATOM 2909 CB MET B 90 -3.733 70.171 28.027 1.00 52.76 C ANISOU 2909 CB MET B 90 6680 4725 8641 -465 559 -43 C ATOM 2910 CG MET B 90 -2.596 69.264 27.592 1.00 55.30 C ANISOU 2910 CG MET B 90 7098 5173 8740 -505 566 85 C ATOM 2911 SD MET B 90 -1.536 68.741 28.948 1.00 60.11 S ANISOU 2911 SD MET B 90 7734 5905 9200 -610 709 75 S ATOM 2912 CE MET B 90 -0.953 70.308 29.515 1.00 57.74 C ANISOU 2912 CE MET B 90 7453 5543 8942 -663 729 34 C ATOM 2913 N ASN B 91 -7.006 71.123 27.094 1.00 55.51 N ANISOU 2913 N ASN B 91 6692 4750 9650 -183 240 -342 N ATOM 2914 CA ASN B 91 -8.105 71.953 27.533 1.00 57.25 C ANISOU 2914 CA ASN B 91 6725 4811 10217 -118 228 -531 C ATOM 2915 C ASN B 91 -8.765 71.335 28.742 1.00 57.67 C ANISOU 2915 C ASN B 91 6595 4885 10433 -236 507 -751 C ATOM 2916 O ASN B 91 -8.617 70.128 28.975 1.00 57.75 O ANISOU 2916 O ASN B 91 6619 5011 10312 -326 639 -748 O ATOM 2917 CB ASN B 91 -9.111 72.179 26.396 1.00 59.74 C ANISOU 2917 CB ASN B 91 6946 5001 10752 87 -107 -585 C ATOM 2918 CG ASN B 91 -8.553 72.970 25.235 1.00 64.18 C ANISOU 2918 CG ASN B 91 7777 5487 11122 211 -364 -354 C ATOM 2919 OD1 ASN B 91 -7.705 73.855 25.388 1.00 65.09 O ANISOU 2919 OD1 ASN B 91 8072 5549 11110 165 -277 -216 O ATOM 2920 ND2 ASN B 91 -9.017 72.657 24.042 1.00 65.82 N ANISOU 2920 ND2 ASN B 91 8041 5673 11293 363 -673 -320 N ATOM 2921 N SER B 92 -9.473 72.179 29.531 1.00 57.32 N ANISOU 2921 N SER B 92 6404 4703 10670 -245 631 -942 N ATOM 2922 CA SER B 92 -10.230 71.766 30.716 1.00 57.21 C ANISOU 2922 CA SER B 92 6238 4659 10841 -373 959 -1189 C ATOM 2923 C SER B 92 -9.438 70.894 31.682 1.00 56.55 C ANISOU 2923 C SER B 92 6358 4722 10408 -555 1239 -1113 C ATOM 2924 O SER B 92 -9.837 69.769 31.983 1.00 56.92 O ANISOU 2924 O SER B 92 6371 4797 10458 -634 1418 -1189 O ATOM 2925 CB SER B 92 -11.530 71.090 30.294 1.00 58.74 C ANISOU 2925 CB SER B 92 6141 4775 11403 -312 915 -1411 C ATOM 2926 OG SER B 92 -12.337 72.036 29.615 1.00 61.61 O ANISOU 2926 OG SER B 92 6303 4973 12132 -122 636 -1524 O ATOM 2927 N LEU B 93 -8.293 71.402 32.133 1.00 55.69 N ANISOU 2927 N LEU B 93 6466 4690 10004 -611 1259 -967 N ATOM 2928 CA LEU B 93 -7.421 70.654 33.023 1.00 55.80 C ANISOU 2928 CA LEU B 93 6699 4840 9663 -740 1433 -882 C ATOM 2929 C LEU B 93 -7.961 70.600 34.436 1.00 56.98 C ANISOU 2929 C LEU B 93 6897 4932 9822 -878 1776 -1076 C ATOM 2930 O LEU B 93 -8.569 71.543 34.887 1.00 56.94 O ANISOU 2930 O LEU B 93 6789 4804 10039 -896 1885 -1258 O ATOM 2931 CB LEU B 93 -6.006 71.234 32.990 1.00 55.24 C ANISOU 2931 CB LEU B 93 6802 4864 9323 -744 1298 -708 C ATOM 2932 CG LEU B 93 -5.228 70.954 31.721 1.00 55.32 C ANISOU 2932 CG LEU B 93 6847 4948 9224 -660 1058 -499 C ATOM 2933 CD1 LEU B 93 -4.109 71.960 31.537 1.00 55.69 C ANISOU 2933 CD1 LEU B 93 6984 5002 9172 -667 961 -401 C ATOM 2934 CD2 LEU B 93 -4.720 69.528 31.702 1.00 55.37 C ANISOU 2934 CD2 LEU B 93 6942 5086 9010 -689 1082 -395 C ATOM 2935 N GLN B 94 -7.806 69.469 35.118 1.00 58.21 N ANISOU 2935 N GLN B 94 7227 5149 9743 -973 1969 -1045 N ATOM 2936 CA GLN B 94 -8.303 69.308 36.487 1.00 59.25 C ANISOU 2936 CA GLN B 94 7500 5207 9806 -1122 2344 -1211 C ATOM 2937 C GLN B 94 -7.156 68.919 37.415 1.00 59.65 C ANISOU 2937 C GLN B 94 7922 5378 9363 -1183 2364 -1062 C ATOM 2938 O GLN B 94 -6.146 68.445 36.919 1.00 59.62 O ANISOU 2938 O GLN B 94 7998 5503 9153 -1110 2120 -850 O ATOM 2939 CB GLN B 94 -9.412 68.239 36.522 1.00 60.80 C ANISOU 2939 CB GLN B 94 7599 5299 10206 -1187 2612 -1343 C ATOM 2940 CG GLN B 94 -10.648 68.562 35.685 1.00 64.48 C ANISOU 2940 CG GLN B 94 7653 5635 11213 -1117 2567 -1556 C ATOM 2941 CD GLN B 94 -11.337 69.871 36.012 1.00 69.33 C ANISOU 2941 CD GLN B 94 8077 6112 12153 -1113 2640 -1789 C ATOM 2942 OE1 GLN B 94 -11.220 70.435 37.110 1.00 72.42 O ANISOU 2942 OE1 GLN B 94 8635 6467 12416 -1224 2884 -1880 O ATOM 2943 NE2 GLN B 94 -12.087 70.378 35.055 1.00 68.36 N ANISOU 2943 NE2 GLN B 94 7610 5898 12464 -971 2414 -1904 N ATOM 2944 N PRO B 95 -7.261 69.098 38.752 1.00 59.75 N ANISOU 2944 N PRO B 95 8179 5346 9175 -1308 2635 -1179 N ATOM 2945 CA PRO B 95 -6.156 68.698 39.642 1.00 59.64 C ANISOU 2945 CA PRO B 95 8554 5445 8661 -1333 2579 -1039 C ATOM 2946 C PRO B 95 -5.555 67.313 39.402 1.00 60.07 C ANISOU 2946 C PRO B 95 8775 5572 8478 -1276 2475 -812 C ATOM 2947 O PRO B 95 -4.353 67.142 39.565 1.00 60.56 O ANISOU 2947 O PRO B 95 9010 5759 8240 -1209 2222 -657 O ATOM 2948 CB PRO B 95 -6.779 68.803 41.028 1.00 60.22 C ANISOU 2948 CB PRO B 95 8900 5408 8575 -1489 2974 -1225 C ATOM 2949 CG PRO B 95 -7.785 69.870 40.890 1.00 60.73 C ANISOU 2949 CG PRO B 95 8657 5343 9074 -1532 3139 -1482 C ATOM 2950 CD PRO B 95 -8.373 69.689 39.523 1.00 59.44 C ANISOU 2950 CD PRO B 95 8089 5144 9352 -1426 2997 -1462 C ATOM 2951 N GLU B 96 -6.375 66.346 38.972 1.00 59.65 N ANISOU 2951 N GLU B 96 8631 5428 8606 -1295 2656 -816 N ATOM 2952 CA GLU B 96 -5.968 64.985 38.641 1.00 59.63 C ANISOU 2952 CA GLU B 96 8748 5453 8456 -1246 2599 -623 C ATOM 2953 C GLU B 96 -5.033 64.897 37.412 1.00 58.88 C ANISOU 2953 C GLU B 96 8463 5501 8409 -1100 2198 -451 C ATOM 2954 O GLU B 96 -4.448 63.841 37.172 1.00 60.04 O ANISOU 2954 O GLU B 96 8718 5686 8410 -1043 2109 -287 O ATOM 2955 CB GLU B 96 -7.204 64.087 38.449 1.00 62.62 C ANISOU 2955 CB GLU B 96 9026 5671 9096 -1330 2933 -733 C ATOM 2956 CG GLU B 96 -8.021 63.868 39.713 1.00 68.88 C ANISOU 2956 CG GLU B 96 10083 6290 9799 -1504 3419 -885 C ATOM 2957 CD GLU B 96 -9.011 64.967 40.060 1.00 77.80 C ANISOU 2957 CD GLU B 96 11009 7319 11233 -1603 3656 -1181 C ATOM 2958 OE1 GLU B 96 -9.120 65.939 39.276 1.00 76.52 O ANISOU 2958 OE1 GLU B 96 10487 7213 11376 -1514 3404 -1258 O ATOM 2959 OE2 GLU B 96 -9.685 64.852 41.115 1.00 82.64 O ANISOU 2959 OE2 GLU B 96 11841 7775 11785 -1769 4112 -1338 O ATOM 2960 N ASP B 97 -4.907 65.975 36.632 1.00 57.00 N ANISOU 2960 N ASP B 97 7965 5316 8377 -1045 1990 -492 N ATOM 2961 CA ASP B 97 -3.991 66.058 35.488 1.00 56.18 C ANISOU 2961 CA ASP B 97 7724 5324 8299 -935 1668 -347 C ATOM 2962 C ASP B 97 -2.610 66.602 35.874 1.00 54.52 C ANISOU 2962 C ASP B 97 7632 5227 7855 -905 1460 -269 C ATOM 2963 O ASP B 97 -1.774 66.755 34.989 1.00 54.22 O ANISOU 2963 O ASP B 97 7481 5264 7858 -839 1244 -176 O ATOM 2964 CB ASP B 97 -4.558 66.925 34.355 1.00 58.28 C ANISOU 2964 CB ASP B 97 7701 5553 8892 -886 1555 -415 C ATOM 2965 CG ASP B 97 -5.873 66.419 33.835 1.00 63.86 C ANISOU 2965 CG ASP B 97 8225 6156 9883 -887 1673 -529 C ATOM 2966 OD1 ASP B 97 -5.878 65.380 33.135 1.00 63.91 O ANISOU 2966 OD1 ASP B 97 8200 6186 9896 -853 1627 -456 O ATOM 2967 OD2 ASP B 97 -6.908 67.053 34.135 1.00 67.34 O ANISOU 2967 OD2 ASP B 97 8531 6482 10571 -922 1812 -722 O ATOM 2968 N THR B 98 -2.377 66.903 37.171 1.00 53.41 N ANISOU 2968 N THR B 98 7719 5090 7484 -962 1532 -333 N ATOM 2969 CA THR B 98 -1.100 67.365 37.697 1.00 52.95 C ANISOU 2969 CA THR B 98 7768 5137 7212 -935 1311 -311 C ATOM 2970 C THR B 98 -0.127 66.219 37.567 1.00 52.70 C ANISOU 2970 C THR B 98 7837 5182 7005 -841 1129 -144 C ATOM 2971 O THR B 98 -0.365 65.137 38.124 1.00 53.62 O ANISOU 2971 O THR B 98 8189 5252 6932 -830 1233 -69 O ATOM 2972 CB THR B 98 -1.230 67.753 39.166 1.00 53.76 C ANISOU 2972 CB THR B 98 8146 5218 7063 -1012 1430 -434 C ATOM 2973 OG1 THR B 98 -2.158 68.833 39.284 1.00 55.09 O ANISOU 2973 OG1 THR B 98 8191 5296 7445 -1101 1625 -617 O ATOM 2974 CG2 THR B 98 0.105 68.130 39.782 1.00 53.88 C ANISOU 2974 CG2 THR B 98 8276 5348 6845 -971 1148 -444 C ATOM 2975 N ALA B 99 0.940 66.427 36.781 1.00 51.28 N ANISOU 2975 N ALA B 99 7476 5088 6919 -776 888 -92 N ATOM 2976 CA ALA B 99 1.942 65.407 36.468 1.00 49.85 C ANISOU 2976 CA ALA B 99 7306 4967 6667 -675 705 37 C ATOM 2977 C ALA B 99 3.108 66.041 35.686 1.00 48.81 C ANISOU 2977 C ALA B 99 6932 4911 6704 -649 505 13 C ATOM 2978 O ALA B 99 3.000 67.164 35.213 1.00 48.52 O ANISOU 2978 O ALA B 99 6742 4857 6836 -712 541 -64 O ATOM 2979 CB ALA B 99 1.293 64.301 35.610 1.00 49.15 C ANISOU 2979 CB ALA B 99 7173 4822 6681 -652 833 144 C ATOM 2980 N VAL B 100 4.229 65.313 35.555 1.00 48.14 N ANISOU 2980 N VAL B 100 6814 4881 6596 -558 315 69 N ATOM 2981 CA VAL B 100 5.310 65.697 34.683 1.00 47.24 C ANISOU 2981 CA VAL B 100 6448 4809 6691 -552 199 31 C ATOM 2982 C VAL B 100 4.923 65.048 33.349 1.00 47.05 C ANISOU 2982 C VAL B 100 6327 4747 6803 -548 329 139 C ATOM 2983 O VAL B 100 4.652 63.846 33.299 1.00 47.25 O ANISOU 2983 O VAL B 100 6441 4752 6759 -486 358 237 O ATOM 2984 CB VAL B 100 6.648 65.143 35.180 1.00 47.50 C ANISOU 2984 CB VAL B 100 6455 4902 6690 -445 -66 0 C ATOM 2985 CG1 VAL B 100 7.775 65.507 34.218 1.00 47.87 C ANISOU 2985 CG1 VAL B 100 6196 4970 7024 -465 -119 -81 C ATOM 2986 CG2 VAL B 100 6.942 65.638 36.587 1.00 47.61 C ANISOU 2986 CG2 VAL B 100 6628 4959 6504 -428 -246 -112 C ATOM 2987 N TYR B 101 4.837 65.845 32.294 1.00 46.61 N ANISOU 2987 N TYR B 101 6128 4664 6918 -615 415 120 N ATOM 2988 CA TYR B 101 4.508 65.405 30.944 1.00 46.46 C ANISOU 2988 CA TYR B 101 6051 4611 6992 -615 513 201 C ATOM 2989 C TYR B 101 5.793 65.244 30.130 1.00 47.37 C ANISOU 2989 C TYR B 101 6024 4745 7230 -616 482 188 C ATOM 2990 O TYR B 101 6.640 66.142 30.118 1.00 47.61 O ANISOU 2990 O TYR B 101 5949 4773 7368 -671 462 97 O ATOM 2991 CB TYR B 101 3.587 66.429 30.273 1.00 46.11 C ANISOU 2991 CB TYR B 101 6001 4496 7023 -672 609 195 C ATOM 2992 CG TYR B 101 2.177 66.376 30.807 1.00 46.52 C ANISOU 2992 CG TYR B 101 6131 4506 7037 -668 678 180 C ATOM 2993 CD1 TYR B 101 1.130 65.904 30.023 1.00 47.10 C ANISOU 2993 CD1 TYR B 101 6195 4534 7168 -646 733 212 C ATOM 2994 CD2 TYR B 101 1.897 66.732 32.118 1.00 47.10 C ANISOU 2994 CD2 TYR B 101 6286 4581 7030 -693 697 104 C ATOM 2995 CE1 TYR B 101 -0.159 65.784 30.536 1.00 47.45 C ANISOU 2995 CE1 TYR B 101 6258 4523 7248 -653 823 150 C ATOM 2996 CE2 TYR B 101 0.620 66.596 32.647 1.00 47.67 C ANISOU 2996 CE2 TYR B 101 6424 4594 7095 -710 825 61 C ATOM 2997 CZ TYR B 101 -0.408 66.144 31.847 1.00 48.50 C ANISOU 2997 CZ TYR B 101 6466 4643 7320 -694 896 74 C ATOM 2998 OH TYR B 101 -1.656 66.044 32.406 1.00 50.58 O ANISOU 2998 OH TYR B 101 6744 4830 7646 -726 1050 -18 O ATOM 2999 N TYR B 102 5.958 64.089 29.485 1.00 48.14 N ANISOU 2999 N TYR B 102 6107 4845 7340 -566 505 250 N ATOM 3000 CA TYR B 102 7.122 63.775 28.654 1.00 49.45 C ANISOU 3000 CA TYR B 102 6131 5011 7648 -573 528 215 C ATOM 3001 C TYR B 102 6.661 63.442 27.231 1.00 51.24 C ANISOU 3001 C TYR B 102 6398 5196 7876 -609 680 276 C ATOM 3002 O TYR B 102 5.551 62.946 27.023 1.00 51.60 O ANISOU 3002 O TYR B 102 6547 5230 7828 -584 703 342 O ATOM 3003 CB TYR B 102 7.868 62.520 29.165 1.00 49.09 C ANISOU 3003 CB TYR B 102 6035 4989 7628 -459 406 213 C ATOM 3004 CG TYR B 102 8.272 62.522 30.619 1.00 49.37 C ANISOU 3004 CG TYR B 102 6106 5063 7591 -376 188 173 C ATOM 3005 CD1 TYR B 102 9.572 62.841 31.000 1.00 50.53 C ANISOU 3005 CD1 TYR B 102 6071 5237 7891 -345 24 34 C ATOM 3006 CD2 TYR B 102 7.397 62.080 31.605 1.00 49.51 C ANISOU 3006 CD2 TYR B 102 6350 5073 7387 -321 145 259 C ATOM 3007 CE1 TYR B 102 9.957 62.823 32.336 1.00 51.38 C ANISOU 3007 CE1 TYR B 102 6241 5384 7898 -246 -239 -15 C ATOM 3008 CE2 TYR B 102 7.768 62.051 32.942 1.00 50.46 C ANISOU 3008 CE2 TYR B 102 6585 5218 7369 -238 -62 233 C ATOM 3009 CZ TYR B 102 9.049 62.422 33.307 1.00 52.05 C ANISOU 3009 CZ TYR B 102 6623 5465 7690 -188 -287 100 C ATOM 3010 OH TYR B 102 9.386 62.399 34.638 1.00 53.61 O ANISOU 3010 OH TYR B 102 6968 5690 7712 -88 -547 63 O ATOM 3011 N CYS B 103 7.541 63.649 26.266 1.00 51.75 N ANISOU 3011 N CYS B 103 6383 5229 8050 -672 791 230 N ATOM 3012 CA CYS B 103 7.322 63.222 24.903 1.00 52.97 C ANISOU 3012 CA CYS B 103 6615 5345 8167 -706 933 271 C ATOM 3013 C CYS B 103 8.393 62.181 24.548 1.00 53.71 C ANISOU 3013 C CYS B 103 6574 5439 8396 -689 996 203 C ATOM 3014 O CYS B 103 9.522 62.220 25.060 1.00 54.04 O ANISOU 3014 O CYS B 103 6429 5486 8618 -679 957 100 O ATOM 3015 CB CYS B 103 7.264 64.379 23.902 1.00 54.67 C ANISOU 3015 CB CYS B 103 6946 5481 8344 -809 1069 288 C ATOM 3016 SG CYS B 103 8.803 65.348 23.722 1.00 61.73 S ANISOU 3016 SG CYS B 103 7709 6304 9440 -940 1240 165 S ATOM 3017 N ALA B 104 8.013 61.200 23.736 1.00 53.67 N ANISOU 3017 N ALA B 104 6639 5423 8332 -672 1069 235 N ATOM 3018 CA ALA B 104 8.929 60.161 23.299 1.00 54.14 C ANISOU 3018 CA ALA B 104 6575 5460 8535 -654 1158 159 C ATOM 3019 C ALA B 104 8.852 60.033 21.782 1.00 54.83 C ANISOU 3019 C ALA B 104 6788 5501 8544 -749 1374 142 C ATOM 3020 O ALA B 104 7.783 60.201 21.197 1.00 54.74 O ANISOU 3020 O ALA B 104 6977 5492 8329 -764 1364 215 O ATOM 3021 CB ALA B 104 8.570 58.838 23.955 1.00 54.28 C ANISOU 3021 CB ALA B 104 6579 5490 8557 -527 1037 202 C ATOM 3022 N ALA B 105 9.972 59.695 21.146 1.00 55.39 N ANISOU 3022 N ALA B 105 6745 5522 8779 -807 1564 24 N ATOM 3023 CA ALA B 105 10.021 59.556 19.698 1.00 56.50 C ANISOU 3023 CA ALA B 105 7049 5606 8813 -916 1814 -12 C ATOM 3024 C ALA B 105 10.345 58.132 19.269 1.00 57.36 C ANISOU 3024 C ALA B 105 7073 5696 9026 -879 1903 -100 C ATOM 3025 O ALA B 105 11.342 57.543 19.727 1.00 58.26 O ANISOU 3025 O ALA B 105 6924 5782 9430 -828 1915 -208 O ATOM 3026 CB ALA B 105 11.051 60.521 19.115 1.00 56.99 C ANISOU 3026 CB ALA B 105 7100 5581 8972 -1070 2079 -106 C ATOM 3027 N ASP B 106 9.526 57.589 18.344 1.00 56.78 N ANISOU 3027 N ASP B 106 7215 5623 8734 -899 1952 -75 N ATOM 3028 CA ASP B 106 9.718 56.253 17.784 1.00 56.67 C ANISOU 3028 CA ASP B 106 7159 5577 8795 -886 2068 -174 C ATOM 3029 C ASP B 106 10.185 56.398 16.337 1.00 56.98 C ANISOU 3029 C ASP B 106 7379 5553 8717 -1041 2384 -278 C ATOM 3030 O ASP B 106 9.441 56.922 15.508 1.00 56.48 O ANISOU 3030 O ASP B 106 7632 5497 8330 -1102 2392 -216 O ATOM 3031 CB ASP B 106 8.399 55.452 17.842 1.00 57.82 C ANISOU 3031 CB ASP B 106 7413 5764 8791 -807 1895 -112 C ATOM 3032 CG ASP B 106 8.502 53.959 17.556 1.00 61.93 C ANISOU 3032 CG ASP B 106 7855 6236 9438 -771 1979 -212 C ATOM 3033 OD1 ASP B 106 9.576 53.512 17.120 1.00 61.83 O ANISOU 3033 OD1 ASP B 106 7728 6159 9607 -808 2187 -339 O ATOM 3034 OD2 ASP B 106 7.496 53.235 17.774 1.00 64.29 O ANISOU 3034 OD2 ASP B 106 8194 6545 9688 -712 1858 -183 O ATOM 3035 N PRO B 107 11.399 55.911 15.999 1.00 57.51 N ANISOU 3035 N PRO B 107 7268 5541 9042 -1100 2647 -448 N ATOM 3036 CA PRO B 107 11.858 55.982 14.600 1.00 58.25 C ANISOU 3036 CA PRO B 107 7572 5553 9009 -1274 3020 -569 C ATOM 3037 C PRO B 107 11.001 55.157 13.624 1.00 59.48 C ANISOU 3037 C PRO B 107 8002 5726 8872 -1286 3036 -588 C ATOM 3038 O PRO B 107 11.058 55.399 12.411 1.00 61.22 O ANISOU 3038 O PRO B 107 8540 5895 8827 -1426 3285 -643 O ATOM 3039 CB PRO B 107 13.298 55.473 14.688 1.00 58.54 C ANISOU 3039 CB PRO B 107 7259 5495 9490 -1307 3272 -786 C ATOM 3040 CG PRO B 107 13.269 54.526 15.871 1.00 58.53 C ANISOU 3040 CG PRO B 107 6939 5532 9767 -1097 2962 -765 C ATOM 3041 CD PRO B 107 12.394 55.235 16.856 1.00 56.88 C ANISOU 3041 CD PRO B 107 6799 5426 9388 -1002 2612 -554 C ATOM 3042 N PHE B 108 10.226 54.185 14.133 1.00 58.25 N ANISOU 3042 N PHE B 108 7748 5628 8758 -1150 2788 -556 N ATOM 3043 CA PHE B 108 9.286 53.412 13.332 1.00 58.15 C ANISOU 3043 CA PHE B 108 7950 5638 8505 -1154 2747 -599 C ATOM 3044 C PHE B 108 7.984 54.199 13.444 1.00 57.67 C ANISOU 3044 C PHE B 108 8104 5662 8145 -1104 2441 -441 C ATOM 3045 O PHE B 108 7.193 53.976 14.351 1.00 57.80 O ANISOU 3045 O PHE B 108 7985 5729 8247 -990 2181 -362 O ATOM 3046 CB PHE B 108 9.135 51.979 13.874 1.00 58.42 C ANISOU 3046 CB PHE B 108 7743 5652 8801 -1045 2672 -667 C ATOM 3047 CG PHE B 108 10.354 51.098 13.665 1.00 60.01 C ANISOU 3047 CG PHE B 108 7728 5744 9328 -1069 2953 -847 C ATOM 3048 CD1 PHE B 108 10.768 50.745 12.387 1.00 61.23 C ANISOU 3048 CD1 PHE B 108 8037 5839 9388 -1210 3278 -1034 C ATOM 3049 CD2 PHE B 108 11.070 50.606 14.742 1.00 60.94 C ANISOU 3049 CD2 PHE B 108 7504 5806 9845 -939 2882 -844 C ATOM 3050 CE1 PHE B 108 11.881 49.938 12.196 1.00 62.06 C ANISOU 3050 CE1 PHE B 108 7909 5825 9844 -1232 3561 -1232 C ATOM 3051 CE2 PHE B 108 12.178 49.786 14.543 1.00 61.83 C ANISOU 3051 CE2 PHE B 108 7383 5797 10311 -933 3109 -1030 C ATOM 3052 CZ PHE B 108 12.574 49.460 13.273 1.00 61.85 C ANISOU 3052 CZ PHE B 108 7496 5736 10266 -1085 3464 -1233 C ATOM 3053 N GLY B 109 7.834 55.174 12.560 1.00 57.13 N ANISOU 3053 N GLY B 109 8375 5583 7750 -1190 2495 -397 N ATOM 3054 CA GLY B 109 6.737 56.125 12.524 1.00 57.43 C ANISOU 3054 CA GLY B 109 8641 5666 7515 -1135 2212 -254 C ATOM 3055 C GLY B 109 5.322 55.606 12.611 1.00 57.94 C ANISOU 3055 C GLY B 109 8707 5803 7503 -1025 1881 -263 C ATOM 3056 O GLY B 109 4.428 56.341 13.053 1.00 58.29 O ANISOU 3056 O GLY B 109 8773 5883 7493 -942 1611 -157 O ATOM 3057 N GLU B 110 5.087 54.377 12.146 1.00 57.81 N ANISOU 3057 N GLU B 110 8662 5795 7508 -1033 1915 -419 N ATOM 3058 CA GLU B 110 3.753 53.791 12.205 1.00 58.36 C ANISOU 3058 CA GLU B 110 8689 5916 7569 -950 1631 -483 C ATOM 3059 C GLU B 110 3.583 52.780 13.342 1.00 58.27 C ANISOU 3059 C GLU B 110 8318 5897 7926 -890 1619 -512 C ATOM 3060 O GLU B 110 2.535 52.143 13.413 1.00 59.48 O ANISOU 3060 O GLU B 110 8401 6063 8137 -851 1459 -602 O ATOM 3061 CB GLU B 110 3.362 53.176 10.851 1.00 61.21 C ANISOU 3061 CB GLU B 110 9310 6282 7665 -999 1624 -660 C ATOM 3062 CG GLU B 110 3.221 54.215 9.744 1.00 67.50 C ANISOU 3062 CG GLU B 110 10561 7073 8011 -1023 1542 -605 C ATOM 3063 CD GLU B 110 2.208 55.327 9.972 1.00 75.80 C ANISOU 3063 CD GLU B 110 11706 8151 8943 -904 1169 -470 C ATOM 3064 OE1 GLU B 110 2.588 56.514 9.845 1.00 77.16 O ANISOU 3064 OE1 GLU B 110 12107 8273 8936 -914 1205 -304 O ATOM 3065 OE2 GLU B 110 1.032 55.016 10.271 1.00 79.00 O ANISOU 3065 OE2 GLU B 110 11945 8605 9466 -805 859 -547 O ATOM 3066 N ARG B 111 4.577 52.652 14.252 1.00 56.76 N ANISOU 3066 N ARG B 111 7912 5667 7988 -879 1775 -441 N ATOM 3067 CA ARG B 111 4.529 51.679 15.346 1.00 55.71 C ANISOU 3067 CA ARG B 111 7517 5491 8159 -807 1770 -435 C ATOM 3068 C ARG B 111 3.904 52.190 16.647 1.00 55.40 C ANISOU 3068 C ARG B 111 7371 5475 8204 -726 1583 -294 C ATOM 3069 O ARG B 111 2.928 51.610 17.084 1.00 55.23 O ANISOU 3069 O ARG B 111 7286 5433 8266 -695 1498 -325 O ATOM 3070 CB ARG B 111 5.936 51.075 15.631 1.00 55.68 C ANISOU 3070 CB ARG B 111 7347 5410 8398 -801 1991 -459 C ATOM 3071 CG ARG B 111 5.986 50.164 16.865 1.00 55.70 C ANISOU 3071 CG ARG B 111 7142 5338 8684 -691 1949 -405 C ATOM 3072 CD ARG B 111 7.312 49.493 17.137 1.00 56.79 C ANISOU 3072 CD ARG B 111 7103 5379 9096 -641 2095 -444 C ATOM 3073 NE ARG B 111 8.390 50.434 17.456 1.00 59.04 N ANISOU 3073 NE ARG B 111 7295 5691 9447 -635 2105 -400 N ATOM 3074 CZ ARG B 111 9.599 50.071 17.878 1.00 60.14 C ANISOU 3074 CZ ARG B 111 7221 5751 9879 -564 2163 -445 C ATOM 3075 NH1 ARG B 111 9.889 48.788 18.058 1.00 61.72 N ANISOU 3075 NH1 ARG B 111 7306 5829 10317 -474 2206 -503 N ATOM 3076 NH2 ARG B 111 10.535 50.985 18.102 1.00 57.68 N ANISOU 3076 NH2 ARG B 111 6795 5463 9657 -579 2173 -454 N ATOM 3077 N LEU B 112 4.500 53.218 17.294 1.00 55.25 N ANISOU 3077 N LEU B 112 7324 5482 8188 -708 1557 -165 N ATOM 3078 CA LEU B 112 4.138 53.703 18.626 1.00 54.91 C ANISOU 3078 CA LEU B 112 7188 5452 8222 -640 1419 -43 C ATOM 3079 C LEU B 112 2.640 53.787 18.945 1.00 54.95 C ANISOU 3079 C LEU B 112 7212 5472 8197 -619 1265 -50 C ATOM 3080 O LEU B 112 2.205 53.256 19.964 1.00 54.25 O ANISOU 3080 O LEU B 112 7034 5338 8239 -580 1260 -23 O ATOM 3081 CB LEU B 112 4.801 55.062 18.904 1.00 54.33 C ANISOU 3081 CB LEU B 112 7133 5415 8093 -655 1396 48 C ATOM 3082 CG LEU B 112 4.670 55.633 20.321 1.00 54.37 C ANISOU 3082 CG LEU B 112 7052 5437 8169 -594 1272 153 C ATOM 3083 CD1 LEU B 112 5.140 54.624 21.405 1.00 54.31 C ANISOU 3083 CD1 LEU B 112 6918 5381 8337 -512 1277 179 C ATOM 3084 CD2 LEU B 112 5.450 56.930 20.424 1.00 54.35 C ANISOU 3084 CD2 LEU B 112 7053 5458 8141 -630 1278 197 C ATOM 3085 N CYS B 113 1.867 54.471 18.092 1.00 55.16 N ANISOU 3085 N CYS B 113 7361 5540 8059 -639 1144 -94 N ATOM 3086 CA CYS B 113 0.457 54.757 18.331 1.00 54.98 C ANISOU 3086 CA CYS B 113 7308 5524 8059 -608 968 -138 C ATOM 3087 C CYS B 113 -0.459 53.545 18.268 1.00 54.28 C ANISOU 3087 C CYS B 113 7118 5391 8116 -618 980 -295 C ATOM 3088 O CYS B 113 -1.636 53.660 18.637 1.00 54.55 O ANISOU 3088 O CYS B 113 7060 5407 8259 -604 876 -371 O ATOM 3089 CB CYS B 113 -0.016 55.874 17.409 1.00 56.18 C ANISOU 3089 CB CYS B 113 7627 5711 8007 -592 784 -139 C ATOM 3090 SG CYS B 113 1.044 57.352 17.433 1.00 61.01 S ANISOU 3090 SG CYS B 113 8383 6328 8469 -608 829 37 S ATOM 3091 N ILE B 114 0.070 52.369 17.857 1.00 53.19 N ANISOU 3091 N ILE B 114 6970 5212 8027 -651 1133 -367 N ATOM 3092 CA ILE B 114 -0.693 51.121 17.862 1.00 52.00 C ANISOU 3092 CA ILE B 114 6717 4986 8054 -677 1195 -526 C ATOM 3093 C ILE B 114 -0.931 50.705 19.334 1.00 51.66 C ANISOU 3093 C ILE B 114 6567 4848 8214 -662 1308 -442 C ATOM 3094 O ILE B 114 -2.043 50.317 19.707 1.00 52.25 O ANISOU 3094 O ILE B 114 6550 4857 8448 -691 1325 -553 O ATOM 3095 CB ILE B 114 0.071 50.010 17.094 1.00 51.64 C ANISOU 3095 CB ILE B 114 6701 4898 8023 -715 1360 -616 C ATOM 3096 CG1 ILE B 114 0.136 50.299 15.589 1.00 52.10 C ANISOU 3096 CG1 ILE B 114 6925 5032 7837 -753 1280 -734 C ATOM 3097 CG2 ILE B 114 -0.506 48.613 17.373 1.00 51.77 C ANISOU 3097 CG2 ILE B 114 6600 4789 8280 -744 1488 -751 C ATOM 3098 CD1 ILE B 114 1.094 49.346 14.812 1.00 52.69 C ANISOU 3098 CD1 ILE B 114 7050 5063 7907 -806 1496 -831 C ATOM 3099 N ASP B 115 0.105 50.820 20.168 1.00 50.36 N ANISOU 3099 N ASP B 115 6429 4666 8041 -617 1384 -262 N ATOM 3100 CA ASP B 115 0.052 50.389 21.559 1.00 50.17 C ANISOU 3100 CA ASP B 115 6396 4538 8130 -587 1483 -155 C ATOM 3101 C ASP B 115 1.034 51.285 22.347 1.00 50.94 C ANISOU 3101 C ASP B 115 6538 4692 8125 -522 1412 27 C ATOM 3102 O ASP B 115 2.121 50.835 22.713 1.00 51.15 O ANISOU 3102 O ASP B 115 6574 4675 8186 -459 1448 112 O ATOM 3103 CB ASP B 115 0.512 48.920 21.564 1.00 50.07 C ANISOU 3103 CB ASP B 115 6382 4384 8256 -574 1650 -175 C ATOM 3104 CG ASP B 115 0.203 48.120 22.789 1.00 51.84 C ANISOU 3104 CG ASP B 115 6666 4438 8595 -553 1791 -91 C ATOM 3105 OD1 ASP B 115 0.176 48.699 23.871 1.00 52.66 O ANISOU 3105 OD1 ASP B 115 6846 4541 8623 -519 1759 45 O ATOM 3106 OD2 ASP B 115 0.019 46.901 22.665 1.00 53.74 O ANISOU 3106 OD2 ASP B 115 6906 4526 8985 -575 1949 -162 O ATOM 3107 N PRO B 116 0.679 52.570 22.587 1.00 51.18 N ANISOU 3107 N PRO B 116 6578 4811 8059 -530 1294 63 N ATOM 3108 CA PRO B 116 1.642 53.500 23.199 1.00 51.57 C ANISOU 3108 CA PRO B 116 6652 4920 8025 -487 1221 191 C ATOM 3109 C PRO B 116 2.250 53.085 24.534 1.00 52.55 C ANISOU 3109 C PRO B 116 6819 4977 8172 -416 1241 310 C ATOM 3110 O PRO B 116 3.451 53.261 24.708 1.00 52.93 O ANISOU 3110 O PRO B 116 6840 5050 8220 -358 1181 365 O ATOM 3111 CB PRO B 116 0.849 54.797 23.325 1.00 51.84 C ANISOU 3111 CB PRO B 116 6693 5016 7990 -513 1118 185 C ATOM 3112 CG PRO B 116 -0.174 54.708 22.256 1.00 52.15 C ANISOU 3112 CG PRO B 116 6707 5062 8046 -550 1075 49 C ATOM 3113 CD PRO B 116 -0.559 53.270 22.186 1.00 50.48 C ANISOU 3113 CD PRO B 116 6457 4762 7961 -570 1199 -41 C ATOM 3114 N ASN B 117 1.451 52.525 25.452 1.00 52.38 N ANISOU 3114 N ASN B 117 6876 4854 8172 -418 1325 336 N ATOM 3115 CA ASN B 117 1.932 52.116 26.761 1.00 52.70 C ANISOU 3115 CA ASN B 117 7052 4807 8164 -339 1330 470 C ATOM 3116 C ASN B 117 2.885 50.927 26.735 1.00 53.38 C ANISOU 3116 C ASN B 117 7159 4790 8332 -241 1342 523 C ATOM 3117 O ASN B 117 3.719 50.800 27.633 1.00 53.92 O ANISOU 3117 O ASN B 117 7319 4817 8351 -125 1234 638 O ATOM 3118 CB ASN B 117 0.770 51.868 27.688 1.00 53.39 C ANISOU 3118 CB ASN B 117 7273 4784 8229 -393 1479 479 C ATOM 3119 CG ASN B 117 0.176 53.170 28.115 1.00 56.73 C ANISOU 3119 CG ASN B 117 7685 5295 8574 -448 1434 449 C ATOM 3120 OD1 ASN B 117 0.897 54.119 28.427 1.00 58.57 O ANISOU 3120 OD1 ASN B 117 7921 5630 8703 -406 1281 505 O ATOM 3121 ND2 ASN B 117 -1.132 53.273 28.121 1.00 57.39 N ANISOU 3121 ND2 ASN B 117 7727 5332 8746 -543 1567 334 N ATOM 3122 N THR B 118 2.783 50.065 25.714 1.00 52.98 N ANISOU 3122 N THR B 118 7025 4691 8415 -273 1447 426 N ATOM 3123 CA THR B 118 3.687 48.937 25.605 1.00 52.78 C ANISOU 3123 CA THR B 118 6992 4547 8514 -177 1473 453 C ATOM 3124 C THR B 118 4.903 49.346 24.801 1.00 52.95 C ANISOU 3124 C THR B 118 6847 4672 8599 -145 1383 391 C ATOM 3125 O THR B 118 6.026 49.069 25.215 1.00 53.39 O ANISOU 3125 O THR B 118 6863 4679 8743 -18 1286 441 O ATOM 3126 CB THR B 118 3.006 47.723 24.970 1.00 53.41 C ANISOU 3126 CB THR B 118 7067 4493 8734 -238 1671 352 C ATOM 3127 OG1 THR B 118 1.875 47.369 25.746 1.00 54.93 O ANISOU 3127 OG1 THR B 118 7399 4562 8909 -294 1808 382 O ATOM 3128 CG2 THR B 118 3.927 46.538 24.858 1.00 53.35 C ANISOU 3128 CG2 THR B 118 7052 4333 8887 -130 1713 373 C ATOM 3129 N PHE B 119 4.684 50.016 23.661 1.00 52.17 N ANISOU 3129 N PHE B 119 6661 4699 8463 -256 1415 273 N ATOM 3130 CA PHE B 119 5.736 50.321 22.718 1.00 52.44 C ANISOU 3130 CA PHE B 119 6574 4797 8554 -272 1429 187 C ATOM 3131 C PHE B 119 6.680 51.432 23.183 1.00 53.79 C ANISOU 3131 C PHE B 119 6676 5053 8709 -238 1302 231 C ATOM 3132 O PHE B 119 7.811 51.489 22.688 1.00 54.00 O ANISOU 3132 O PHE B 119 6568 5082 8868 -231 1340 151 O ATOM 3133 CB PHE B 119 5.154 50.576 21.318 1.00 51.83 C ANISOU 3133 CB PHE B 119 6515 4792 8386 -402 1520 56 C ATOM 3134 CG PHE B 119 4.469 49.384 20.667 1.00 51.82 C ANISOU 3134 CG PHE B 119 6534 4707 8448 -442 1641 -57 C ATOM 3135 CD1 PHE B 119 4.507 48.127 21.251 1.00 52.67 C ANISOU 3135 CD1 PHE B 119 6633 4657 8723 -373 1716 -34 C ATOM 3136 CD2 PHE B 119 3.799 49.520 19.472 1.00 52.18 C ANISOU 3136 CD2 PHE B 119 6627 4815 8383 -541 1667 -193 C ATOM 3137 CE1 PHE B 119 3.908 47.036 20.638 1.00 53.16 C ANISOU 3137 CE1 PHE B 119 6698 4623 8876 -425 1852 -163 C ATOM 3138 CE2 PHE B 119 3.203 48.425 18.860 1.00 52.86 C ANISOU 3138 CE2 PHE B 119 6714 4828 8543 -585 1763 -338 C ATOM 3139 CZ PHE B 119 3.252 47.194 19.451 1.00 52.77 C ANISOU 3139 CZ PHE B 119 6660 4658 8734 -537 1872 -331 C ATOM 3140 N ALA B 120 6.259 52.254 24.179 1.00 54.28 N ANISOU 3140 N ALA B 120 6812 5166 8646 -222 1174 329 N ATOM 3141 CA ALA B 120 7.109 53.278 24.800 1.00 54.53 C ANISOU 3141 CA ALA B 120 6777 5268 8675 -188 1034 352 C ATOM 3142 C ALA B 120 8.351 52.634 25.424 1.00 55.46 C ANISOU 3142 C ALA B 120 6791 5313 8970 -39 920 353 C ATOM 3143 O ALA B 120 9.413 53.262 25.465 1.00 55.73 O ANISOU 3143 O ALA B 120 6663 5389 9123 -21 839 280 O ATOM 3144 CB ALA B 120 6.346 54.008 25.887 1.00 53.92 C ANISOU 3144 CB ALA B 120 6827 5229 8432 -187 930 443 C ATOM 3145 N GLY B 121 8.192 51.406 25.922 1.00 55.73 N ANISOU 3145 N GLY B 121 6916 5217 9041 70 907 425 N ATOM 3146 CA GLY B 121 9.246 50.633 26.552 1.00 56.99 C ANISOU 3146 CA GLY B 121 7017 5267 9370 257 753 446 C ATOM 3147 C GLY B 121 10.390 50.266 25.635 1.00 58.05 C ANISOU 3147 C GLY B 121 6886 5368 9804 278 818 285 C ATOM 3148 O GLY B 121 11.465 49.892 26.115 1.00 58.51 O ANISOU 3148 O GLY B 121 6806 5351 10074 445 641 251 O ATOM 3149 N TYR B 122 10.167 50.333 24.309 1.00 58.14 N ANISOU 3149 N TYR B 122 6831 5418 9841 117 1067 169 N ATOM 3150 CA TYR B 122 11.207 49.999 23.325 1.00 58.45 C ANISOU 3150 CA TYR B 122 6643 5413 10154 96 1216 -14 C ATOM 3151 C TYR B 122 12.055 51.214 22.934 1.00 58.79 C ANISOU 3151 C TYR B 122 6507 5553 10277 -2 1253 -142 C ATOM 3152 O TYR B 122 13.049 51.034 22.231 1.00 59.35 O ANISOU 3152 O TYR B 122 6366 5572 10615 -31 1405 -322 O ATOM 3153 CB TYR B 122 10.597 49.441 22.017 1.00 58.38 C ANISOU 3153 CB TYR B 122 6702 5384 10096 -45 1497 -101 C ATOM 3154 CG TYR B 122 9.534 48.368 22.145 1.00 59.39 C ANISOU 3154 CG TYR B 122 7001 5421 10144 -20 1535 -22 C ATOM 3155 CD1 TYR B 122 9.532 47.481 23.214 1.00 60.48 C ANISOU 3155 CD1 TYR B 122 7203 5415 10361 152 1404 103 C ATOM 3156 CD2 TYR B 122 8.593 48.173 21.142 1.00 59.98 C ANISOU 3156 CD2 TYR B 122 7181 5525 10084 -165 1710 -94 C ATOM 3157 CE1 TYR B 122 8.571 46.485 23.322 1.00 61.19 C ANISOU 3157 CE1 TYR B 122 7457 5383 10409 150 1501 162 C ATOM 3158 CE2 TYR B 122 7.666 47.142 21.212 1.00 60.54 C ANISOU 3158 CE2 TYR B 122 7360 5492 10149 -161 1772 -75 C ATOM 3159 CZ TYR B 122 7.648 46.309 22.312 1.00 61.70 C ANISOU 3159 CZ TYR B 122 7565 5483 10395 -16 1696 54 C ATOM 3160 OH TYR B 122 6.724 45.295 22.407 1.00 62.90 O ANISOU 3160 OH TYR B 122 7835 5497 10566 -33 1810 67 O ATOM 3161 N LEU B 123 11.626 52.444 23.319 1.00 58.47 N ANISOU 3161 N LEU B 123 6558 5632 10026 -75 1166 -70 N ATOM 3162 CA LEU B 123 12.199 53.733 22.934 1.00 58.06 C ANISOU 3162 CA LEU B 123 6399 5653 10006 -204 1243 -171 C ATOM 3163 C LEU B 123 13.330 54.248 23.793 1.00 59.35 C ANISOU 3163 C LEU B 123 6324 5820 10407 -116 1047 -261 C ATOM 3164 O LEU B 123 13.246 54.246 25.020 1.00 59.64 O ANISOU 3164 O LEU B 123 6399 5875 10386 28 753 -168 O ATOM 3165 CB LEU B 123 11.101 54.811 22.863 1.00 56.79 C ANISOU 3165 CB LEU B 123 6463 5593 9523 -322 1252 -58 C ATOM 3166 CG LEU B 123 9.819 54.447 22.117 1.00 55.92 C ANISOU 3166 CG LEU B 123 6578 5492 9176 -393 1363 11 C ATOM 3167 CD1 LEU B 123 8.884 55.625 22.053 1.00 55.87 C ANISOU 3167 CD1 LEU B 123 6739 5565 8925 -480 1331 90 C ATOM 3168 CD2 LEU B 123 10.109 53.940 20.731 1.00 55.58 C ANISOU 3168 CD2 LEU B 123 6536 5404 9179 -488 1618 -113 C ATOM 3169 N GLU B 124 14.375 54.754 23.114 1.00 59.99 N ANISOU 3169 N GLU B 124 6171 5876 10745 -221 1230 -464 N ATOM 3170 CA GLU B 124 15.561 55.381 23.705 1.00 60.52 C ANISOU 3170 CA GLU B 124 5933 5938 11124 -183 1095 -636 C ATOM 3171 C GLU B 124 15.462 56.932 23.674 1.00 59.93 C ANISOU 3171 C GLU B 124 5904 5937 10931 -357 1173 -652 C ATOM 3172 O GLU B 124 16.200 57.602 24.392 1.00 60.48 O ANISOU 3172 O GLU B 124 5761 6023 11197 -329 1004 -777 O ATOM 3173 CB GLU B 124 16.835 54.932 22.966 1.00 63.54 C ANISOU 3173 CB GLU B 124 5976 6207 11958 -211 1311 -906 C ATOM 3174 CG GLU B 124 17.116 53.448 23.094 1.00 72.43 C ANISOU 3174 CG GLU B 124 7001 7229 13291 -13 1208 -923 C ATOM 3175 CD GLU B 124 18.286 52.940 22.267 1.00 83.87 C ANISOU 3175 CD GLU B 124 8101 8547 15221 -46 1464 -1217 C ATOM 3176 OE1 GLU B 124 18.369 51.709 22.034 1.00 85.25 O ANISOU 3176 OE1 GLU B 124 8234 8614 15544 73 1488 -1236 O ATOM 3177 OE2 GLU B 124 19.122 53.778 21.853 1.00 88.21 O ANISOU 3177 OE2 GLU B 124 8412 9079 16023 -201 1673 -1445 O ATOM 3178 N THR B 125 14.570 57.499 22.851 1.00 58.72 N ANISOU 3178 N THR B 125 6025 5812 10474 -524 1406 -542 N ATOM 3179 CA THR B 125 14.451 58.948 22.728 1.00 58.11 C ANISOU 3179 CA THR B 125 6026 5761 10294 -681 1503 -542 C ATOM 3180 C THR B 125 13.278 59.501 23.544 1.00 57.37 C ANISOU 3180 C THR B 125 6165 5756 9876 -634 1275 -342 C ATOM 3181 O THR B 125 12.118 59.334 23.188 1.00 57.04 O ANISOU 3181 O THR B 125 6386 5740 9548 -645 1303 -184 O ATOM 3182 CB THR B 125 14.422 59.358 21.242 1.00 58.69 C ANISOU 3182 CB THR B 125 6258 5764 10278 -892 1917 -575 C ATOM 3183 OG1 THR B 125 15.577 58.818 20.590 1.00 59.98 O ANISOU 3183 OG1 THR B 125 6179 5829 10783 -950 2170 -801 O ATOM 3184 CG2 THR B 125 14.367 60.852 21.048 1.00 58.18 C ANISOU 3184 CG2 THR B 125 6312 5676 10119 -1052 2049 -561 C ATOM 3185 N TRP B 126 13.619 60.194 24.626 1.00 56.88 N ANISOU 3185 N TRP B 126 5986 5735 9890 -588 1055 -388 N ATOM 3186 CA TRP B 126 12.695 60.810 25.556 1.00 56.79 C ANISOU 3186 CA TRP B 126 6157 5796 9625 -552 856 -253 C ATOM 3187 C TRP B 126 13.177 62.199 25.929 1.00 57.46 C ANISOU 3187 C TRP B 126 6138 5884 9811 -652 849 -368 C ATOM 3188 O TRP B 126 14.388 62.455 25.962 1.00 57.87 O ANISOU 3188 O TRP B 126 5905 5899 10183 -686 866 -578 O ATOM 3189 CB TRP B 126 12.648 59.997 26.860 1.00 56.08 C ANISOU 3189 CB TRP B 126 6068 5746 9493 -349 522 -200 C ATOM 3190 CG TRP B 126 11.925 58.698 26.762 1.00 55.74 C ANISOU 3190 CG TRP B 126 6187 5680 9312 -249 518 -55 C ATOM 3191 CD1 TRP B 126 12.456 57.491 26.421 1.00 56.55 C ANISOU 3191 CD1 TRP B 126 6185 5716 9585 -157 535 -91 C ATOM 3192 CD2 TRP B 126 10.543 58.460 27.067 1.00 55.35 C ANISOU 3192 CD2 TRP B 126 6412 5649 8970 -235 508 121 C ATOM 3193 NE1 TRP B 126 11.483 56.519 26.462 1.00 56.84 N ANISOU 3193 NE1 TRP B 126 6435 5725 9437 -95 548 64 N ATOM 3194 CE2 TRP B 126 10.305 57.082 26.878 1.00 56.27 C ANISOU 3194 CE2 TRP B 126 6587 5705 9089 -146 534 186 C ATOM 3195 CE3 TRP B 126 9.489 59.274 27.496 1.00 55.15 C ANISOU 3195 CE3 TRP B 126 6566 5667 8722 -293 498 204 C ATOM 3196 CZ2 TRP B 126 9.056 56.507 27.093 1.00 56.44 C ANISOU 3196 CZ2 TRP B 126 6833 5705 8906 -132 568 321 C ATOM 3197 CZ3 TRP B 126 8.249 58.706 27.689 1.00 55.88 C ANISOU 3197 CZ3 TRP B 126 6859 5743 8627 -273 530 326 C ATOM 3198 CH2 TRP B 126 8.040 57.339 27.492 1.00 56.12 C ANISOU 3198 CH2 TRP B 126 6939 5711 8671 -201 571 379 C ATOM 3199 N GLY B 127 12.234 63.062 26.292 1.00 56.96 N ANISOU 3199 N GLY B 127 6274 5852 9517 -693 812 -258 N ATOM 3200 CA GLY B 127 12.589 64.372 26.804 1.00 56.79 C ANISOU 3200 CA GLY B 127 6172 5824 9582 -779 785 -366 C ATOM 3201 C GLY B 127 12.783 64.330 28.315 1.00 56.42 C ANISOU 3201 C GLY B 127 6055 5860 9524 -649 438 -426 C ATOM 3202 O GLY B 127 12.599 63.285 28.958 1.00 56.45 O ANISOU 3202 O GLY B 127 6119 5908 9420 -487 229 -350 O ATOM 3203 N GLN B 128 13.140 65.481 28.893 1.00 56.07 N ANISOU 3203 N GLN B 128 5919 5817 9568 -723 380 -563 N ATOM 3204 CA GLN B 128 13.385 65.662 30.328 1.00 56.41 C ANISOU 3204 CA GLN B 128 5921 5938 9573 -621 42 -660 C ATOM 3205 C GLN B 128 12.085 65.782 31.183 1.00 55.60 C ANISOU 3205 C GLN B 128 6139 5889 9098 -572 -58 -491 C ATOM 3206 O GLN B 128 12.118 65.618 32.402 1.00 55.81 O ANISOU 3206 O GLN B 128 6242 5979 8986 -464 -334 -523 O ATOM 3207 CB GLN B 128 14.323 66.886 30.535 1.00 59.56 C ANISOU 3207 CB GLN B 128 6067 6306 10255 -746 48 -926 C ATOM 3208 CG GLN B 128 13.649 68.285 30.715 1.00 65.57 C ANISOU 3208 CG GLN B 128 6969 7034 10909 -889 174 -918 C ATOM 3209 CD GLN B 128 12.925 68.894 29.515 1.00 69.95 C ANISOU 3209 CD GLN B 128 7694 7476 11406 -1033 543 -765 C ATOM 3210 OE1 GLN B 128 13.150 68.496 28.359 1.00 73.75 O ANISOU 3210 OE1 GLN B 128 8163 7889 11968 -1083 772 -714 O ATOM 3211 NE2 GLN B 128 12.014 69.850 29.777 1.00 66.51 N ANISOU 3211 NE2 GLN B 128 7447 7008 10815 -1088 591 -693 N ATOM 3212 N GLY B 129 10.978 66.085 30.524 1.00 54.37 N ANISOU 3212 N GLY B 129 6171 5693 8794 -653 170 -335 N ATOM 3213 CA GLY B 129 9.677 66.289 31.128 1.00 54.27 C ANISOU 3213 CA GLY B 129 6409 5697 8512 -639 159 -214 C ATOM 3214 C GLY B 129 9.402 67.729 31.499 1.00 53.64 C ANISOU 3214 C GLY B 129 6349 5591 8441 -746 205 -300 C ATOM 3215 O GLY B 129 10.331 68.475 31.770 1.00 53.27 O ANISOU 3215 O GLY B 129 6132 5540 8569 -805 149 -481 O ATOM 3216 N THR B 130 8.117 68.129 31.527 1.00 53.45 N ANISOU 3216 N THR B 130 6507 5533 8270 -773 308 -200 N ATOM 3217 CA THR B 130 7.695 69.477 31.942 1.00 53.18 C ANISOU 3217 CA THR B 130 6506 5448 8251 -860 360 -280 C ATOM 3218 C THR B 130 6.515 69.346 32.928 1.00 52.97 C ANISOU 3218 C THR B 130 6674 5445 8009 -818 332 -243 C ATOM 3219 O THR B 130 5.570 68.615 32.666 1.00 53.05 O ANISOU 3219 O THR B 130 6792 5444 7921 -771 400 -116 O ATOM 3220 CB THR B 130 7.457 70.424 30.735 1.00 53.62 C ANISOU 3220 CB THR B 130 6554 5373 8446 -957 571 -236 C ATOM 3221 OG1 THR B 130 7.539 71.789 31.166 1.00 53.56 O ANISOU 3221 OG1 THR B 130 6519 5292 8539 -1049 611 -361 O ATOM 3222 CG2 THR B 130 6.129 70.159 30.009 1.00 53.90 C ANISOU 3222 CG2 THR B 130 6745 5358 8377 -913 657 -66 C ATOM 3223 N GLN B 131 6.608 70.011 34.082 1.00 52.42 N ANISOU 3223 N GLN B 131 6645 5399 7874 -846 249 -382 N ATOM 3224 CA GLN B 131 5.610 69.935 35.139 1.00 52.52 C ANISOU 3224 CA GLN B 131 6865 5421 7671 -832 267 -386 C ATOM 3225 C GLN B 131 4.371 70.764 34.860 1.00 52.67 C ANISOU 3225 C GLN B 131 6915 5333 7765 -895 468 -381 C ATOM 3226 O GLN B 131 4.461 71.985 34.690 1.00 52.85 O ANISOU 3226 O GLN B 131 6855 5282 7945 -969 523 -475 O ATOM 3227 CB GLN B 131 6.239 70.336 36.489 1.00 54.00 C ANISOU 3227 CB GLN B 131 7119 5675 7724 -839 89 -562 C ATOM 3228 CG GLN B 131 5.279 70.410 37.666 1.00 57.59 C ANISOU 3228 CG GLN B 131 7838 6121 7922 -856 156 -601 C ATOM 3229 CD GLN B 131 4.848 69.049 38.127 1.00 63.93 C ANISOU 3229 CD GLN B 131 8884 6946 8461 -766 149 -457 C ATOM 3230 OE1 GLN B 131 5.664 68.187 38.434 1.00 66.41 O ANISOU 3230 OE1 GLN B 131 9262 7322 8648 -661 -69 -412 O ATOM 3231 NE2 GLN B 131 3.549 68.821 38.204 1.00 65.57 N ANISOU 3231 NE2 GLN B 131 9228 7078 8609 -804 395 -397 N ATOM 3232 N VAL B 132 3.211 70.107 34.865 1.00 52.20 N ANISOU 3232 N VAL B 132 6966 5245 7624 -862 578 -293 N ATOM 3233 CA VAL B 132 1.927 70.766 34.702 1.00 52.91 C ANISOU 3233 CA VAL B 132 7054 5224 7824 -895 742 -322 C ATOM 3234 C VAL B 132 1.222 70.652 36.056 1.00 55.02 C ANISOU 3234 C VAL B 132 7493 5490 7922 -929 841 -423 C ATOM 3235 O VAL B 132 1.088 69.540 36.573 1.00 55.70 O ANISOU 3235 O VAL B 132 7735 5618 7812 -898 857 -363 O ATOM 3236 CB VAL B 132 1.106 70.133 33.554 1.00 52.45 C ANISOU 3236 CB VAL B 132 6944 5117 7866 -841 801 -196 C ATOM 3237 CG1 VAL B 132 -0.347 70.609 33.574 1.00 52.37 C ANISOU 3237 CG1 VAL B 132 6910 4992 7998 -847 933 -265 C ATOM 3238 CG2 VAL B 132 1.761 70.419 32.203 1.00 52.35 C ANISOU 3238 CG2 VAL B 132 6832 5084 7976 -825 738 -106 C ATOM 3239 N THR B 133 0.861 71.789 36.675 1.00 55.59 N ANISOU 3239 N THR B 133 7572 5498 8053 -1001 925 -581 N ATOM 3240 CA THR B 133 0.208 71.787 37.979 1.00 56.84 C ANISOU 3240 CA THR B 133 7923 5638 8036 -1059 1069 -709 C ATOM 3241 C THR B 133 -1.152 72.422 37.864 1.00 59.25 C ANISOU 3241 C THR B 133 8142 5796 8574 -1099 1297 -809 C ATOM 3242 O THR B 133 -1.269 73.563 37.432 1.00 59.22 O ANISOU 3242 O THR B 133 7987 5704 8812 -1110 1298 -880 O ATOM 3243 CB THR B 133 1.029 72.561 39.007 1.00 57.36 C ANISOU 3243 CB THR B 133 8084 5757 7953 -1116 970 -871 C ATOM 3244 OG1 THR B 133 2.362 72.069 39.015 1.00 58.69 O ANISOU 3244 OG1 THR B 133 8257 6052 7991 -1058 704 -815 O ATOM 3245 CG2 THR B 133 0.450 72.469 40.396 1.00 57.19 C ANISOU 3245 CG2 THR B 133 8345 5723 7662 -1182 1122 -999 C ATOM 3246 N VAL B 134 -2.187 71.669 38.205 1.00 61.19 N ANISOU 3246 N VAL B 134 8472 5992 8788 -1116 1498 -824 N ATOM 3247 CA VAL B 134 -3.547 72.172 38.170 1.00 63.59 C ANISOU 3247 CA VAL B 134 8648 6141 9370 -1151 1727 -969 C ATOM 3248 C VAL B 134 -4.046 72.248 39.614 1.00 67.38 C ANISOU 3248 C VAL B 134 9351 6575 9675 -1271 1998 -1154 C ATOM 3249 O VAL B 134 -4.232 71.231 40.270 1.00 67.04 O ANISOU 3249 O VAL B 134 9543 6548 9383 -1311 2144 -1122 O ATOM 3250 CB VAL B 134 -4.488 71.358 37.268 1.00 62.84 C ANISOU 3250 CB VAL B 134 8399 5986 9490 -1092 1782 -905 C ATOM 3251 CG1 VAL B 134 -5.783 72.131 37.051 1.00 63.12 C ANISOU 3251 CG1 VAL B 134 8211 5850 9920 -1092 1926 -1090 C ATOM 3252 CG2 VAL B 134 -3.833 71.031 35.938 1.00 62.30 C ANISOU 3252 CG2 VAL B 134 8219 5990 9463 -985 1519 -706 C ATOM 3253 N SER B 135 -4.172 73.459 40.132 1.00 70.75 N ANISOU 3253 N SER B 135 9749 6934 10200 -1333 2076 -1343 N ATOM 3254 CA SER B 135 -4.547 73.688 41.516 1.00 74.20 C ANISOU 3254 CA SER B 135 10426 7325 10443 -1463 2344 -1549 C ATOM 3255 C SER B 135 -5.347 74.982 41.608 1.00 77.86 C ANISOU 3255 C SER B 135 10689 7624 11271 -1513 2524 -1792 C ATOM 3256 O SER B 135 -5.076 75.936 40.869 1.00 78.15 O ANISOU 3256 O SER B 135 10498 7619 11575 -1448 2346 -1783 O ATOM 3257 CB SER B 135 -3.281 73.791 42.362 1.00 75.60 C ANISOU 3257 CB SER B 135 10879 7647 10199 -1487 2149 -1543 C ATOM 3258 OG SER B 135 -3.562 74.095 43.715 1.00 79.11 O ANISOU 3258 OG SER B 135 11614 8053 10391 -1614 2381 -1752 O ATOM 3259 N SER B 136 -6.354 75.009 42.486 1.00 80.48 N ANISOU 3259 N SER B 136 11111 7832 11635 -1630 2904 -2013 N ATOM 3260 CA SER B 136 -7.171 76.210 42.661 1.00 83.42 C ANISOU 3260 CA SER B 136 11279 8023 12394 -1677 3108 -2282 C ATOM 3261 C SER B 136 -6.465 77.247 43.534 1.00 85.36 C ANISOU 3261 C SER B 136 11691 8296 12447 -1763 3091 -2439 C ATOM 3262 O SER B 136 -5.509 76.907 44.240 1.00 85.81 O ANISOU 3262 O SER B 136 12066 8512 12027 -1806 2968 -2382 O ATOM 3263 CB SER B 136 -8.556 75.863 43.212 1.00 85.89 C ANISOU 3263 CB SER B 136 11570 8168 12895 -1784 3567 -2508 C ATOM 3264 OG SER B 136 -8.508 75.134 44.428 1.00 89.22 O ANISOU 3264 OG SER B 136 12424 8628 12848 -1936 3852 -2559 O ATOM 3265 N LEU B 137 -6.909 78.521 43.430 1.00 86.29 N ANISOU 3265 N LEU B 137 11578 8248 12961 -1770 3174 -2643 N ATOM 3266 CA LEU B 137 -6.412 79.705 44.159 1.00 87.77 C ANISOU 3266 CA LEU B 137 11847 8408 13094 -1860 3196 -2852 C ATOM 3267 C LEU B 137 -5.165 80.335 43.522 1.00 88.66 C ANISOU 3267 C LEU B 137 11877 8605 13205 -1787 2812 -2710 C ATOM 3268 O LEU B 137 -4.633 79.816 42.541 1.00 89.18 O ANISOU 3268 O LEU B 137 11853 8759 13271 -1672 2542 -2440 O ATOM 3269 CB LEU B 137 -6.193 79.451 45.672 1.00 88.07 C ANISOU 3269 CB LEU B 137 12313 8529 12620 -2030 3409 -3030 C TER 3270 LEU B 137 HETATM 3271 C1 Q4T A 401 2.657 6.403 18.247 1.00 53.99 C ANISOU 3271 C1 Q4T A 401 7376 5807 7332 415 978 -12 C HETATM 3272 C2 Q4T A 401 3.092 5.376 17.416 1.00 54.68 C ANISOU 3272 C2 Q4T A 401 7505 5852 7419 439 1016 -37 C HETATM 3273 C3 Q4T A 401 2.655 4.078 17.622 1.00 55.29 C ANISOU 3273 C3 Q4T A 401 7641 5877 7490 454 1004 -32 C HETATM 3274 C11 Q4T A 401 0.161 9.357 20.491 1.00 50.32 C ANISOU 3274 C11 Q4T A 401 6845 5435 6842 312 878 60 C HETATM 3275 C12 Q4T A 401 0.538 9.296 21.836 1.00 50.18 C ANISOU 3275 C12 Q4T A 401 6815 5423 6829 352 855 76 C HETATM 3276 C13 Q4T A 401 -0.679 10.526 19.975 1.00 49.65 C ANISOU 3276 C13 Q4T A 401 6745 5373 6747 259 871 61 C HETATM 3277 C16 Q4T A 401 -1.666 11.660 17.974 1.00 50.26 C ANISOU 3277 C16 Q4T A 401 6854 5452 6793 192 865 44 C HETATM 3278 C17 Q4T A 401 -1.124 12.316 16.839 1.00 50.53 C ANISOU 3278 C17 Q4T A 401 6907 5492 6802 186 889 32 C HETATM 3279 C18 Q4T A 401 -1.917 13.206 16.109 1.00 50.38 C ANISOU 3279 C18 Q4T A 401 6914 5471 6756 154 862 33 C HETATM 3280 C19 Q4T A 401 -3.221 13.472 16.514 1.00 50.57 C ANISOU 3280 C19 Q4T A 401 6925 5493 6798 128 808 40 C HETATM 3281 C20 Q4T A 401 -3.764 12.851 17.640 1.00 50.71 C ANISOU 3281 C20 Q4T A 401 6909 5506 6853 129 798 49 C HETATM 3282 C21 Q4T A 401 -2.987 11.931 18.360 1.00 50.74 C ANISOU 3282 C21 Q4T A 401 6908 5507 6866 160 829 54 C HETATM 3283 C22 Q4T A 401 0.297 12.024 16.320 1.00 50.65 C ANISOU 3283 C22 Q4T A 401 6923 5505 6818 217 950 15 C HETATM 3284 C23 Q4T A 401 0.171 10.859 15.376 1.00 50.74 C ANISOU 3284 C23 Q4T A 401 7010 5473 6797 224 965 -4 C HETATM 3285 C27 Q4T A 401 0.289 2.058 19.642 1.00 56.34 C ANISOU 3285 C27 Q4T A 401 7893 5898 7615 424 949 39 C HETATM 3286 C28 Q4T A 401 -1.057 2.350 18.908 1.00 56.51 C ANISOU 3286 C28 Q4T A 401 7927 5913 7633 345 945 28 C HETATM 3287 C30 Q4T A 401 -0.981 0.179 17.804 1.00 56.09 C ANISOU 3287 C30 Q4T A 401 7977 5747 7588 364 969 -13 C HETATM 3288 C4 Q4T A 401 1.777 3.783 18.643 1.00 54.98 C ANISOU 3288 C4 Q4T A 401 7622 5822 7445 441 965 1 C HETATM 3289 C5 Q4T A 401 1.356 4.815 19.495 1.00 54.11 C ANISOU 3289 C5 Q4T A 401 7471 5755 7332 419 936 27 C HETATM 3290 C6 Q4T A 401 1.753 6.125 19.274 1.00 53.03 C ANISOU 3290 C6 Q4T A 401 7275 5674 7200 405 937 19 C HETATM 3291 C7 Q4T A 401 1.276 8.235 22.363 1.00 50.25 C ANISOU 3291 C7 Q4T A 401 6847 5404 6843 410 848 77 C HETATM 3292 C8 Q4T A 401 1.688 7.205 21.522 1.00 51.02 C ANISOU 3292 C8 Q4T A 401 6968 5467 6950 427 874 60 C HETATM 3293 C9 Q4T A 401 1.303 7.208 20.178 1.00 51.81 C ANISOU 3293 C9 Q4T A 401 7082 5559 7042 384 906 42 C HETATM 3294 C10 Q4T A 401 0.536 8.267 19.665 1.00 51.38 C ANISOU 3294 C10 Q4T A 401 7016 5532 6974 329 904 43 C HETATM 3295 N14 Q4T A 401 -0.906 10.667 18.645 1.00 49.78 N ANISOU 3295 N14 Q4T A 401 6788 5380 6747 232 882 45 N HETATM 3296 O15 Q4T A 401 -1.143 11.293 20.804 1.00 49.10 O ANISOU 3296 O15 Q4T A 401 6649 5324 6681 248 851 76 O HETATM 3297 O24 Q4T A 401 0.097 10.949 14.159 1.00 50.47 O ANISOU 3297 O24 Q4T A 401 7044 5418 6716 213 984 -17 O HETATM 3298 O25 Q4T A 401 0.037 9.707 16.004 1.00 51.21 O ANISOU 3298 O25 Q4T A 401 7070 5511 6875 243 950 -4 O HETATM 3299 O26 Q4T A 401 1.411 2.445 18.814 1.00 55.68 O ANISOU 3299 O26 Q4T A 401 7775 5847 7535 454 965 7 O HETATM 3300 N29 Q4T A 401 -1.087 1.641 17.610 1.00 56.36 N ANISOU 3300 N29 Q4T A 401 7953 5854 7606 336 954 -12 N HETATM 3301 C31 Q4T A 401 0.343 -0.189 18.530 1.00 56.04 C ANISOU 3301 C31 Q4T A 401 7961 5743 7587 445 982 3 C HETATM 3302 C32 Q4T A 401 0.407 0.532 19.897 1.00 56.16 C ANISOU 3302 C32 Q4T A 401 7938 5798 7601 460 961 45 C HETATM 3303 F33 Q4T A 401 -3.933 14.356 15.840 1.00 50.98 F ANISOU 3303 F33 Q4T A 401 6997 5540 6832 107 771 39 F HETATM 3304 F34 Q4T A 401 0.209 8.184 18.372 1.00 51.53 F ANISOU 3304 F34 Q4T A 401 7070 5536 6975 299 922 24 F HETATM 3305 CL1 Q4T A 401 3.228 2.790 16.603 1.00 56.71 CL ANISOU 3305 CL1 Q4T A 401 7878 5998 7670 489 1051 -69 CL HETATM 3306 F36 Q4T A 401 3.073 7.647 17.992 1.00 54.05 F ANISOU 3306 F36 Q4T A 401 7330 5857 7349 398 992 -19 F HETATM 3307 C10 OLC A 402 -12.532 30.551 29.212 1.00 69.41 C ANISOU 3307 C10 OLC A 402 8817 7930 9627 149 840 -39 C HETATM 3308 C9 OLC A 402 -13.768 31.030 28.997 1.00 69.71 C ANISOU 3308 C9 OLC A 402 8795 7935 9754 152 848 -55 C HETATM 3309 C11 OLC A 402 -11.214 31.239 28.958 1.00 69.19 C ANISOU 3309 C11 OLC A 402 8824 7922 9541 148 784 -36 C HETATM 3310 C8 OLC A 402 -14.167 32.387 28.465 1.00 69.94 C ANISOU 3310 C8 OLC A 402 8793 7942 9838 164 797 -71 C HETATM 3311 C24 OLC A 402 -8.093 41.088 25.299 1.00 71.88 C ANISOU 3311 C24 OLC A 402 9270 8020 10019 84 556 -44 C HETATM 3312 C12 OLC A 402 -10.205 30.143 28.533 1.00 68.98 C ANISOU 3312 C12 OLC A 402 8823 7924 9462 137 767 -14 C HETATM 3313 C7 OLC A 402 -15.216 33.019 29.412 1.00 69.96 C ANISOU 3313 C7 OLC A 402 8764 7914 9904 186 864 -103 C HETATM 3314 C6 OLC A 402 -14.949 34.535 29.601 1.00 70.41 C ANISOU 3314 C6 OLC A 402 8840 7957 9955 206 835 -121 C HETATM 3315 C5 OLC A 402 -13.449 34.893 29.410 1.00 70.97 C ANISOU 3315 C5 OLC A 402 8974 8055 9935 195 782 -105 C HETATM 3316 C4 OLC A 402 -13.251 36.316 28.811 1.00 71.56 C ANISOU 3316 C4 OLC A 402 9051 8103 10035 200 722 -111 C HETATM 3317 C3 OLC A 402 -13.009 36.243 27.278 1.00 72.37 C ANISOU 3317 C3 OLC A 402 9150 8200 10146 184 647 -78 C HETATM 3318 C2 OLC A 402 -12.443 37.553 26.659 1.00 73.28 C ANISOU 3318 C2 OLC A 402 9298 8287 10258 182 598 -72 C HETATM 3319 C21 OLC A 402 -9.212 39.294 26.752 1.00 73.04 C ANISOU 3319 C21 OLC A 402 9360 8247 10144 126 582 -74 C HETATM 3320 C1 OLC A 402 -11.034 37.831 27.126 1.00 74.19 C ANISOU 3320 C1 OLC A 402 9455 8421 10312 161 609 -75 C HETATM 3321 C22 OLC A 402 -8.117 39.591 25.689 1.00 72.57 C ANISOU 3321 C22 OLC A 402 9328 8171 10072 90 571 -46 C HETATM 3322 O19 OLC A 402 -10.747 37.590 28.290 1.00 75.16 O ANISOU 3322 O19 OLC A 402 9586 8567 10406 167 646 -99 O HETATM 3323 O25 OLC A 402 -6.812 41.614 25.668 1.00 71.10 O ANISOU 3323 O25 OLC A 402 9173 7915 9928 52 572 -66 O HETATM 3324 O23 OLC A 402 -6.813 39.293 26.203 1.00 72.64 O ANISOU 3324 O23 OLC A 402 9330 8208 10061 66 586 -64 O HETATM 3325 O20 OLC A 402 -10.158 38.337 26.218 1.00 73.69 O ANISOU 3325 O20 OLC A 402 9423 8343 10234 139 577 -53 O HETATM 3326 C10 OLC A 403 -13.472 31.462 23.589 1.00 60.18 C ANISOU 3326 C10 OLC A 403 7594 6696 8575 124 539 0 C HETATM 3327 C9 OLC A 403 -13.692 32.788 23.743 1.00 61.32 C ANISOU 3327 C9 OLC A 403 7735 6818 8746 142 522 -9 C HETATM 3328 C11 OLC A 403 -14.441 30.326 23.815 1.00 59.33 C ANISOU 3328 C11 OLC A 403 7431 6584 8528 119 562 -15 C HETATM 3329 C8 OLC A 403 -14.954 33.520 24.161 1.00 62.41 C ANISOU 3329 C8 OLC A 403 7810 6922 8981 168 517 -38 C HETATM 3330 C24 OLC A 403 -18.747 44.300 21.426 1.00 80.46 C ANISOU 3330 C24 OLC A 403 10209 8735 11628 486 38 -75 C HETATM 3331 C12 OLC A 403 -13.721 28.953 23.889 1.00 58.87 C ANISOU 3331 C12 OLC A 403 7404 6554 8411 97 596 1 C HETATM 3332 C7 OLC A 403 -14.574 34.956 24.581 1.00 63.81 C ANISOU 3332 C7 OLC A 403 8012 7085 9147 182 522 -43 C HETATM 3333 C6 OLC A 403 -15.459 36.072 23.955 1.00 65.58 C ANISOU 3333 C6 OLC A 403 8220 7257 9441 214 452 -52 C HETATM 3334 C5 OLC A 403 -15.583 37.306 24.918 1.00 67.55 C ANISOU 3334 C5 OLC A 403 8460 7487 9719 233 489 -76 C HETATM 3335 C4 OLC A 403 -14.517 38.440 24.739 1.00 69.17 C ANISOU 3335 C4 OLC A 403 8738 7679 9864 227 473 -58 C HETATM 3336 C3 OLC A 403 -15.029 39.839 25.207 1.00 70.83 C ANISOU 3336 C3 OLC A 403 8938 7843 10130 258 470 -84 C HETATM 3337 C2 OLC A 403 -14.329 40.993 24.429 1.00 73.11 C ANISOU 3337 C2 OLC A 403 9300 8091 10387 255 422 -58 C HETATM 3338 C21 OLC A 403 -16.623 43.313 22.555 1.00 78.43 C ANISOU 3338 C21 OLC A 403 9989 8592 11217 374 219 -55 C HETATM 3339 C1 OLC A 403 -15.165 42.227 24.107 1.00 75.24 C ANISOU 3339 C1 OLC A 403 9569 8294 10725 298 370 -67 C HETATM 3340 C22 OLC A 403 -18.068 43.031 22.018 1.00 79.50 C ANISOU 3340 C22 OLC A 403 10058 8697 11450 426 131 -75 C HETATM 3341 O19 OLC A 403 -15.016 43.287 24.702 1.00 75.29 O ANISOU 3341 O19 OLC A 403 9586 8271 10748 307 391 -86 O HETATM 3342 O25 OLC A 403 -17.739 45.219 20.929 1.00 81.08 O ANISOU 3342 O25 OLC A 403 10413 8778 11617 471 38 -31 O HETATM 3343 O23 OLC A 403 -18.136 41.941 21.073 1.00 79.50 O ANISOU 3343 O23 OLC A 403 10073 8717 11416 415 75 -54 O HETATM 3344 O20 OLC A 403 -16.053 42.091 23.098 1.00 77.15 O ANISOU 3344 O20 OLC A 403 9803 8503 11007 329 288 -56 O HETATM 3345 C8 OLC A 404 -20.880 10.675 28.973 1.00 71.48 C ANISOU 3345 C8 OLC A 404 8877 7480 10801 -357 1755 3 C HETATM 3346 C24 OLC A 404 -16.037 5.014 26.852 1.00 79.64 C ANISOU 3346 C24 OLC A 404 10435 8473 11353 -269 1518 128 C HETATM 3347 C7 OLC A 404 -19.468 10.064 28.790 1.00 71.88 C ANISOU 3347 C7 OLC A 404 9075 7570 10667 -315 1692 50 C HETATM 3348 C6 OLC A 404 -18.649 10.810 27.694 1.00 72.39 C ANISOU 3348 C6 OLC A 404 9132 7727 10645 -273 1504 36 C HETATM 3349 C5 OLC A 404 -17.753 9.842 26.867 1.00 72.74 C ANISOU 3349 C5 OLC A 404 9245 7777 10613 -262 1417 45 C HETATM 3350 C4 OLC A 404 -16.347 10.454 26.664 1.00 73.16 C ANISOU 3350 C4 OLC A 404 9379 7921 10497 -198 1324 72 C HETATM 3351 C3 OLC A 404 -15.241 9.375 26.617 1.00 74.02 C ANISOU 3351 C3 OLC A 404 9599 8026 10498 -171 1315 105 C HETATM 3352 C2 OLC A 404 -15.231 8.626 25.263 1.00 75.33 C ANISOU 3352 C2 OLC A 404 9740 8173 10708 -193 1221 68 C HETATM 3353 C21 OLC A 404 -14.984 5.953 24.675 1.00 78.66 C ANISOU 3353 C21 OLC A 404 10254 8476 11158 -225 1247 67 C HETATM 3354 C1 OLC A 404 -13.858 8.082 24.935 1.00 76.77 C ANISOU 3354 C1 OLC A 404 10019 8386 10765 -147 1173 92 C HETATM 3355 C22 OLC A 404 -14.850 4.936 25.848 1.00 79.43 C ANISOU 3355 C22 OLC A 404 10446 8507 11227 -222 1380 119 C HETATM 3356 O19 OLC A 404 -12.881 8.823 24.999 1.00 76.55 O ANISOU 3356 O19 OLC A 404 10023 8427 10635 -99 1131 109 O HETATM 3357 O25 OLC A 404 -15.747 4.200 28.004 1.00 79.68 O ANISOU 3357 O25 OLC A 404 10563 8418 11295 -253 1643 186 O HETATM 3358 O23 OLC A 404 -14.725 3.592 25.340 1.00 79.88 O ANISOU 3358 O23 OLC A 404 10544 8497 11310 -241 1376 109 O HETATM 3359 O20 OLC A 404 -13.787 6.765 24.577 1.00 78.03 O ANISOU 3359 O20 OLC A 404 10217 8486 10943 -163 1181 87 O HETATM 3360 C10 OLC A 405 1.419 27.580 31.403 1.00 87.14 C ANISOU 3360 C10 OLC A 405 11148 10346 11615 279 400 -164 C HETATM 3361 C9 OLC A 405 1.464 28.853 31.860 1.00 87.29 C ANISOU 3361 C9 OLC A 405 11157 10354 11657 268 370 -200 C HETATM 3362 C11 OLC A 405 2.565 26.597 31.252 1.00 86.62 C ANISOU 3362 C11 OLC A 405 11047 10286 11580 307 363 -177 C HETATM 3363 C8 OLC A 405 0.275 29.791 31.972 1.00 87.16 C ANISOU 3363 C8 OLC A 405 11174 10327 11615 246 412 -188 C HETATM 3364 C24 OLC A 405 7.098 40.950 31.791 1.00 88.28 C ANISOU 3364 C24 OLC A 405 10746 10108 12688 -106 157 -671 C HETATM 3365 C12 OLC A 405 2.027 25.195 30.852 1.00 86.31 C ANISOU 3365 C12 OLC A 405 11051 10252 11491 319 414 -127 C HETATM 3366 C7 OLC A 405 0.669 31.143 32.616 1.00 86.94 C ANISOU 3366 C7 OLC A 405 11136 10281 11617 243 358 -242 C HETATM 3367 C13 OLC A 405 0.977 24.657 31.870 1.00 86.24 C ANISOU 3367 C13 OLC A 405 11152 10235 11379 354 426 -100 C HETATM 3368 C6 OLC A 405 1.187 32.148 31.557 1.00 87.07 C ANISOU 3368 C6 OLC A 405 11065 10282 11736 185 375 -252 C HETATM 3369 C14 OLC A 405 0.712 23.126 31.726 1.00 86.05 C ANISOU 3369 C14 OLC A 405 11176 10205 11313 376 460 -61 C HETATM 3370 C5 OLC A 405 2.743 32.235 31.589 1.00 87.45 C ANISOU 3370 C5 OLC A 405 11036 10324 11868 183 313 -303 C HETATM 3371 C4 OLC A 405 3.325 33.454 30.811 1.00 87.54 C ANISOU 3371 C4 OLC A 405 10968 10305 11990 122 335 -325 C HETATM 3372 C3 OLC A 405 4.243 34.360 31.680 1.00 87.60 C ANISOU 3372 C3 OLC A 405 10938 10286 12061 126 246 -403 C HETATM 3373 C2 OLC A 405 4.673 35.607 30.861 1.00 88.07 C ANISOU 3373 C2 OLC A 405 10926 10304 12233 57 291 -416 C HETATM 3374 C21 OLC A 405 5.654 38.876 32.317 1.00 88.59 C ANISOU 3374 C21 OLC A 405 10931 10258 12472 6 150 -583 C HETATM 3375 C1 OLC A 405 5.462 36.652 31.626 1.00 88.62 C ANISOU 3375 C1 OLC A 405 10950 10337 12385 48 209 -497 C HETATM 3376 C22 OLC A 405 6.976 39.408 31.706 1.00 88.50 C ANISOU 3376 C22 OLC A 405 10791 10201 12633 -57 162 -627 C HETATM 3377 O19 OLC A 405 6.387 36.365 32.375 1.00 89.10 O ANISOU 3377 O19 OLC A 405 10969 10398 12486 78 113 -559 O HETATM 3378 O25 OLC A 405 8.499 41.277 31.797 1.00 88.32 O ANISOU 3378 O25 OLC A 405 10623 10071 12862 -145 119 -746 O HETATM 3379 O23 OLC A 405 8.082 38.793 32.378 1.00 88.61 O ANISOU 3379 O23 OLC A 405 10733 10224 12710 -25 60 -694 O HETATM 3380 O20 OLC A 405 5.077 37.918 31.407 1.00 88.50 O ANISOU 3380 O20 OLC A 405 10943 10283 12402 6 241 -501 O HETATM 3381 C24 OLC A 406 5.578 14.088 26.712 1.00 97.35 C ANISOU 3381 C24 OLC A 406 12477 11552 12960 541 555 -33 C HETATM 3382 C7 OLC A 406 10.047 25.181 27.046 1.00 96.10 C ANISOU 3382 C7 OLC A 406 11625 11430 13457 260 445 -359 C HETATM 3383 C6 OLC A 406 10.045 23.682 26.631 1.00 96.15 C ANISOU 3383 C6 OLC A 406 11666 11446 13421 303 473 -330 C HETATM 3384 C5 OLC A 406 8.764 22.936 27.098 1.00 96.15 C ANISOU 3384 C5 OLC A 406 11806 11468 13260 335 447 -273 C HETATM 3385 C4 OLC A 406 9.034 21.429 27.344 1.00 96.35 C ANISOU 3385 C4 OLC A 406 11859 11492 13258 403 412 -267 C HETATM 3386 C3 OLC A 406 7.701 20.648 27.447 1.00 96.77 C ANISOU 3386 C3 OLC A 406 12045 11555 13169 411 439 -201 C HETATM 3387 C2 OLC A 406 7.841 19.374 28.329 1.00 97.35 C ANISOU 3387 C2 OLC A 406 12179 11620 13191 491 365 -196 C HETATM 3388 C21 OLC A 406 6.460 16.465 26.556 1.00 97.59 C ANISOU 3388 C21 OLC A 406 12356 11625 13100 487 537 -92 C HETATM 3389 C1 OLC A 406 7.785 18.085 27.534 1.00 97.84 C ANISOU 3389 C1 OLC A 406 12264 11671 13240 502 429 -168 C HETATM 3390 C22 OLC A 406 6.764 15.025 27.047 1.00 97.69 C ANISOU 3390 C22 OLC A 406 12417 11611 13088 559 497 -86 C HETATM 3391 O19 OLC A 406 8.715 17.735 26.815 1.00 98.24 O ANISOU 3391 O19 OLC A 406 12235 11712 13380 509 459 -195 O HETATM 3392 O25 OLC A 406 6.030 12.729 26.810 1.00 97.02 O ANISOU 3392 O25 OLC A 406 12471 11478 12916 601 537 -30 O HETATM 3393 O23 OLC A 406 8.000 14.509 26.505 1.00 97.85 O ANISOU 3393 O23 OLC A 406 12356 11619 13203 591 503 -123 O HETATM 3394 O20 OLC A 406 6.658 17.361 27.666 1.00 97.62 O ANISOU 3394 O20 OLC A 406 12346 11639 13105 503 456 -116 O HETATM 3395 C18 OLC A 407 -15.094 27.245 29.119 1.00 67.86 C ANISOU 3395 C18 OLC A 407 8525 7675 9584 105 986 -30 C HETATM 3396 C10 OLC A 407 -19.627 31.982 21.714 1.00 75.00 C ANISOU 3396 C10 OLC A 407 9145 8381 10970 213 265 -136 C HETATM 3397 C9 OLC A 407 -19.563 31.019 20.764 1.00 76.37 C ANISOU 3397 C9 OLC A 407 9347 8553 11115 199 197 -132 C HETATM 3398 C17 OLC A 407 -15.516 28.524 28.356 1.00 68.13 C ANISOU 3398 C17 OLC A 407 8504 7701 9680 114 909 -49 C HETATM 3399 C11 OLC A 407 -18.932 31.942 23.054 1.00 73.44 C ANISOU 3399 C11 OLC A 407 8962 8224 10718 191 406 -122 C HETATM 3400 C8 OLC A 407 -20.262 31.006 19.409 1.00 77.23 C ANISOU 3400 C8 OLC A 407 9461 8617 11267 227 38 -152 C HETATM 3401 C24 OLC A 407 -20.655 37.907 12.180 1.00 85.75 C ANISOU 3401 C24 OLC A 407 11309 9307 11966 601 -821 -16 C HETATM 3402 C16 OLC A 407 -16.530 28.204 27.222 1.00 68.54 C ANISOU 3402 C16 OLC A 407 8475 7723 9842 100 852 -63 C HETATM 3403 C12 OLC A 407 -19.055 30.495 23.605 1.00 72.09 C ANISOU 3403 C12 OLC A 407 8757 8069 10564 156 489 -128 C HETATM 3404 C7 OLC A 407 -19.299 31.389 18.254 1.00 77.91 C ANISOU 3404 C7 OLC A 407 9697 8703 11200 241 -37 -108 C HETATM 3405 C15 OLC A 407 -17.578 29.338 27.049 1.00 69.08 C ANISOU 3405 C15 OLC A 407 8469 7759 10018 119 824 -95 C HETATM 3406 C13 OLC A 407 -17.951 30.216 24.660 1.00 71.11 C ANISOU 3406 C13 OLC A 407 8698 7989 10330 138 601 -100 C HETATM 3407 C6 OLC A 407 -19.065 32.922 18.080 1.00 78.74 C ANISOU 3407 C6 OLC A 407 9862 8786 11270 278 -71 -87 C HETATM 3408 C14 OLC A 407 -18.386 29.175 25.730 1.00 70.02 C ANISOU 3408 C14 OLC A 407 8522 7850 10233 116 720 -111 C HETATM 3409 C5 OLC A 407 -20.371 33.759 18.102 1.00 79.89 C ANISOU 3409 C5 OLC A 407 9918 8879 11558 325 -153 -128 C HETATM 3410 C4 OLC A 407 -20.829 34.153 16.667 1.00 81.42 C ANISOU 3410 C4 OLC A 407 10183 9013 11739 376 -332 -131 C HETATM 3411 C3 OLC A 407 -20.091 33.328 15.567 1.00 82.76 C ANISOU 3411 C3 OLC A 407 10484 9191 11770 361 -378 -103 C HETATM 3412 C2 OLC A 407 -20.895 33.135 14.237 1.00 83.61 C ANISOU 3412 C2 OLC A 407 10637 9238 11893 409 -569 -129 C HETATM 3413 C21 OLC A 407 -20.423 35.487 12.965 1.00 85.33 C ANISOU 3413 C21 OLC A 407 11098 9366 11956 499 -694 -60 C HETATM 3414 C1 OLC A 407 -20.012 33.161 12.997 1.00 84.27 C ANISOU 3414 C1 OLC A 407 10922 9305 11792 421 -619 -82 C HETATM 3415 C22 OLC A 407 -20.417 36.440 11.746 1.00 85.71 C ANISOU 3415 C22 OLC A 407 11321 9338 11905 564 -823 -27 C HETATM 3416 O19 OLC A 407 -19.750 32.146 12.352 1.00 84.08 O ANISOU 3416 O19 OLC A 407 10958 9288 11701 404 -642 -85 O HETATM 3417 O25 OLC A 407 -22.028 38.261 11.930 1.00 85.94 O ANISOU 3417 O25 OLC A 407 11258 9271 12124 673 -989 -67 O HETATM 3418 O23 OLC A 407 -19.170 36.298 11.036 1.00 86.04 O ANISOU 3418 O23 OLC A 407 11546 9387 11759 538 -759 33 O HETATM 3419 O20 OLC A 407 -19.539 34.382 12.667 1.00 84.92 O ANISOU 3419 O20 OLC A 407 11117 9358 11792 450 -626 -39 O HETATM 3420 C24 OLC A 408 12.491 38.387 29.382 1.00 91.81 C ANISOU 3420 C24 OLC A 408 10625 10519 13739 -203 272 -789 C HETATM 3421 C3 OLC A 408 9.036 32.630 32.037 1.00 91.98 C ANISOU 3421 C3 OLC A 408 11161 10825 12963 181 22 -588 C HETATM 3422 C2 OLC A 408 9.168 34.142 32.392 1.00 92.28 C ANISOU 3422 C2 OLC A 408 11170 10823 13068 140 -13 -643 C HETATM 3423 C21 OLC A 408 10.650 36.780 30.208 1.00 91.89 C ANISOU 3423 C21 OLC A 408 10869 10646 13397 -74 194 -690 C HETATM 3424 C1 OLC A 408 9.624 34.932 31.190 1.00 92.42 C ANISOU 3424 C1 OLC A 408 11087 10805 13224 53 99 -639 C HETATM 3425 C22 OLC A 408 11.453 38.086 30.498 1.00 91.91 C ANISOU 3425 C22 OLC A 408 10776 10584 13561 -126 153 -774 C HETATM 3426 O19 OLC A 408 9.561 34.408 30.086 1.00 92.84 O ANISOU 3426 O19 OLC A 408 11122 10867 13286 26 212 -585 O HETATM 3427 O25 OLC A 408 12.774 39.800 29.348 1.00 91.73 O ANISOU 3427 O25 OLC A 408 10571 10438 13845 -274 296 -829 O HETATM 3428 O23 OLC A 408 10.581 39.223 30.642 1.00 92.04 O ANISOU 3428 O23 OLC A 408 10875 10574 13521 -154 172 -756 O HETATM 3429 O20 OLC A 408 10.098 36.180 31.407 1.00 91.95 O ANISOU 3429 O20 OLC A 408 10971 10697 13268 9 70 -698 O HETATM 3430 C24 OLC A 409 -20.884 12.574 11.414 1.00 82.49 C ANISOU 3430 C24 OLC A 409 10446 8939 11956 -120 -470 -530 C HETATM 3431 C5 OLC A 409 -15.185 19.598 11.354 1.00 79.16 C ANISOU 3431 C5 OLC A 409 10530 8842 10704 88 -169 -148 C HETATM 3432 C4 OLC A 409 -16.528 19.051 10.804 1.00 79.37 C ANISOU 3432 C4 OLC A 409 10510 8811 10837 90 -317 -216 C HETATM 3433 C3 OLC A 409 -16.932 17.689 11.434 1.00 79.90 C ANISOU 3433 C3 OLC A 409 10479 8867 11012 45 -272 -249 C HETATM 3434 C2 OLC A 409 -17.311 16.676 10.317 1.00 80.77 C ANISOU 3434 C2 OLC A 409 10664 8921 11103 49 -386 -303 C HETATM 3435 C21 OLC A 409 -19.072 13.524 9.844 1.00 82.15 C ANISOU 3435 C21 OLC A 409 10720 8957 11536 -28 -531 -464 C HETATM 3436 C1 OLC A 409 -18.154 15.513 10.784 1.00 81.73 C ANISOU 3436 C1 OLC A 409 10668 9006 11380 5 -392 -355 C HETATM 3437 C22 OLC A 409 -19.386 12.536 11.002 1.00 82.32 C ANISOU 3437 C22 OLC A 409 10605 8968 11704 -89 -408 -469 C HETATM 3438 O19 OLC A 409 -18.984 15.662 11.664 1.00 82.21 O ANISOU 3438 O19 OLC A 409 10580 9062 11595 -20 -366 -369 O HETATM 3439 O25 OLC A 409 -21.400 11.232 11.562 1.00 82.56 O ANISOU 3439 O25 OLC A 409 10389 8888 12092 -174 -453 -579 O HETATM 3440 O23 OLC A 409 -19.001 11.200 10.642 1.00 82.40 O ANISOU 3440 O23 OLC A 409 10683 8947 11680 -109 -390 -489 O HETATM 3441 O20 OLC A 409 -17.915 14.326 10.179 1.00 82.06 O ANISOU 3441 O20 OLC A 409 10782 9015 11382 -5 -415 -385 O HETATM 3442 C24 OLC A 410 -24.185 6.926 18.615 1.00101.42 C ANISOU 3442 C24 OLC A 410 12172 11018 15345 -546 540 -529 C HETATM 3443 C4 OLC A 410 -23.291 15.636 19.373 1.00100.28 C ANISOU 3443 C4 OLC A 410 12007 11277 14818 -237 356 -388 C HETATM 3444 C3 OLC A 410 -24.146 14.336 19.460 1.00100.55 C ANISOU 3444 C3 OLC A 410 11954 11231 15020 -300 401 -435 C HETATM 3445 C2 OLC A 410 -23.508 13.105 18.744 1.00100.83 C ANISOU 3445 C2 OLC A 410 12090 11251 14970 -315 348 -436 C HETATM 3446 C21 OLC A 410 -23.888 9.492 18.983 1.00101.49 C ANISOU 3446 C21 OLC A 410 12170 11169 15222 -452 505 -475 C HETATM 3447 C1 OLC A 410 -24.287 11.814 18.923 1.00101.14 C ANISOU 3447 C1 OLC A 410 12049 11204 15176 -381 404 -480 C HETATM 3448 C22 OLC A 410 -23.739 8.284 18.010 1.00101.74 C ANISOU 3448 C22 OLC A 410 12256 11150 15251 -473 409 -517 C HETATM 3449 O19 OLC A 410 -25.268 11.758 19.651 1.00101.19 O ANISOU 3449 O19 OLC A 410 11921 11159 15368 -421 498 -508 O HETATM 3450 O25 OLC A 410 -24.982 6.246 17.627 1.00101.15 O ANISOU 3450 O25 OLC A 410 12066 10905 15463 -581 400 -623 O HETATM 3451 O23 OLC A 410 -24.454 8.505 16.781 1.00102.17 O ANISOU 3451 O23 OLC A 410 12252 11174 15393 -464 201 -602 O HETATM 3452 O20 OLC A 410 -23.833 10.738 18.244 1.00101.32 O ANISOU 3452 O20 OLC A 410 12157 11205 15136 -394 355 -488 O HETATM 3453 C18 OLC A 411 1.903 21.444 2.482 1.00 83.10 C ANISOU 3453 C18 OLC A 411 12462 9149 9965 127 1600 168 C HETATM 3454 C10 OLC A 411 -4.244 15.161 3.499 1.00 84.21 C ANISOU 3454 C10 OLC A 411 12465 9364 10166 218 664 -67 C HETATM 3455 C9 OLC A 411 -5.527 14.784 3.613 1.00 84.51 C ANISOU 3455 C9 OLC A 411 12475 9392 10243 217 499 -99 C HETATM 3456 C17 OLC A 411 0.991 20.242 2.847 1.00 83.16 C ANISOU 3456 C17 OLC A 411 12426 9195 9977 152 1435 129 C HETATM 3457 C11 OLC A 411 -3.387 15.222 2.258 1.00 83.94 C ANISOU 3457 C11 OLC A 411 12625 9279 9988 244 774 -63 C HETATM 3458 C8 OLC A 411 -6.480 14.333 2.534 1.00 84.91 C ANISOU 3458 C8 OLC A 411 12676 9378 10208 244 353 -145 C HETATM 3459 C24 OLC A 411 -14.143 8.468 2.825 1.00 90.22 C ANISOU 3459 C24 OLC A 411 12945 9790 11545 133 -616 -583 C HETATM 3460 C16 OLC A 411 1.249 18.993 1.962 1.00 83.24 C ANISOU 3460 C16 OLC A 411 12553 9172 9902 182 1485 93 C HETATM 3461 C12 OLC A 411 -1.904 14.988 2.656 1.00 83.81 C ANISOU 3461 C12 OLC A 411 12534 9289 10019 233 972 -49 C HETATM 3462 C7 OLC A 411 -7.901 14.852 2.885 1.00 85.53 C ANISOU 3462 C7 OLC A 411 12680 9454 10362 238 173 -158 C HETATM 3463 C15 OLC A 411 0.897 17.685 2.721 1.00 83.53 C ANISOU 3463 C15 OLC A 411 12457 9259 10021 190 1388 51 C HETATM 3464 C13 OLC A 411 -1.219 16.274 3.199 1.00 83.75 C ANISOU 3464 C13 OLC A 411 12444 9313 10064 210 1072 0 C HETATM 3465 C6 OLC A 411 -8.779 13.759 3.562 1.00 86.15 C ANISOU 3465 C6 OLC A 411 12620 9538 10575 214 81 -206 C HETATM 3466 C14 OLC A 411 -0.331 16.950 2.112 1.00 83.74 C ANISOU 3466 C14 OLC A 411 12609 9259 9951 219 1221 23 C HETATM 3467 C5 OLC A 411 -10.271 13.858 3.133 1.00 86.64 C ANISOU 3467 C5 OLC A 411 12696 9555 10669 224 -130 -253 C HETATM 3468 C4 OLC A 411 -11.063 14.957 3.904 1.00 87.09 C ANISOU 3468 C4 OLC A 411 12612 9641 10836 211 -194 -231 C HETATM 3469 C3 OLC A 411 -12.556 14.995 3.464 1.00 87.59 C ANISOU 3469 C3 OLC A 411 12671 9653 10957 226 -410 -288 C HETATM 3470 C2 OLC A 411 -12.928 13.810 2.523 1.00 88.25 C ANISOU 3470 C2 OLC A 411 12864 9672 10995 240 -516 -359 C HETATM 3471 C21 OLC A 411 -14.733 10.850 3.677 1.00 89.67 C ANISOU 3471 C21 OLC A 411 12731 9797 11543 143 -640 -505 C HETATM 3472 C1 OLC A 411 -14.154 13.034 2.958 1.00 88.93 C ANISOU 3472 C1 OLC A 411 12801 9734 11255 211 -642 -426 C HETATM 3473 C22 OLC A 411 -15.248 9.533 3.041 1.00 89.96 C ANISOU 3473 C22 OLC A 411 12811 9761 11609 134 -745 -589 C HETATM 3474 O19 OLC A 411 -15.087 13.591 3.521 1.00 89.06 O ANISOU 3474 O19 OLC A 411 12679 9757 11404 199 -721 -434 O HETATM 3475 O25 OLC A 411 -14.777 7.211 2.496 1.00 90.39 O ANISOU 3475 O25 OLC A 411 12964 9742 11639 112 -712 -665 O HETATM 3476 O23 OLC A 411 -16.287 8.982 3.867 1.00 90.04 O ANISOU 3476 O23 OLC A 411 12624 9752 11835 82 -789 -629 O HETATM 3477 O20 OLC A 411 -14.126 11.707 2.683 1.00 89.40 O ANISOU 3477 O20 OLC A 411 12889 9758 11320 197 -652 -476 O HETATM 3478 C10 OLC A 412 -1.837 8.894 -0.634 1.00 91.36 C ANISOU 3478 C10 OLC A 412 14006 10026 10682 354 941 -296 C HETATM 3479 C9 OLC A 412 -2.788 7.962 -0.822 1.00 91.65 C ANISOU 3479 C9 OLC A 412 14076 10029 10719 357 788 -349 C HETATM 3480 C8 OLC A 412 -4.264 8.214 -1.064 1.00 92.04 C ANISOU 3480 C8 OLC A 412 14149 10058 10762 349 566 -370 C HETATM 3481 C24 OLC A 412 -12.931 -0.130 -0.367 1.00 98.94 C ANISOU 3481 C24 OLC A 412 14622 10490 12482 127 -636 -961 C HETATM 3482 C7 OLC A 412 -5.093 6.934 -0.767 1.00 92.52 C ANISOU 3482 C7 OLC A 412 14150 10095 10909 335 441 -431 C HETATM 3483 C6 OLC A 412 -6.434 7.269 -0.057 1.00 93.12 C ANISOU 3483 C6 OLC A 412 14091 10188 11103 302 260 -437 C HETATM 3484 C5 OLC A 412 -7.374 6.039 0.068 1.00 93.88 C ANISOU 3484 C5 OLC A 412 14150 10240 11282 284 130 -506 C HETATM 3485 C4 OLC A 412 -8.722 6.232 -0.687 1.00 94.94 C ANISOU 3485 C4 OLC A 412 14368 10317 11387 292 -94 -562 C HETATM 3486 C3 OLC A 412 -9.970 5.851 0.170 1.00 96.06 C ANISOU 3486 C3 OLC A 412 14319 10457 11721 244 -229 -594 C HETATM 3487 C2 OLC A 412 -11.249 5.623 -0.694 1.00 97.21 C ANISOU 3487 C2 OLC A 412 14548 10526 11860 254 -461 -678 C HETATM 3488 C21 OLC A 412 -12.951 2.451 0.028 1.00 98.67 C ANISOU 3488 C21 OLC A 412 14517 10581 12391 154 -632 -846 C HETATM 3489 C1 OLC A 412 -12.303 4.742 -0.042 1.00 98.36 C ANISOU 3489 C1 OLC A 412 14528 10644 12202 203 -563 -733 C HETATM 3490 C22 OLC A 412 -12.338 1.256 -0.751 1.00 98.90 C ANISOU 3490 C22 OLC A 412 14711 10548 12319 177 -599 -898 C HETATM 3491 O19 OLC A 412 -12.823 5.041 1.031 1.00 98.98 O ANISOU 3491 O19 OLC A 412 14408 10762 12440 160 -557 -706 O HETATM 3492 O25 OLC A 412 -12.289 -1.162 -1.148 1.00 98.96 O ANISOU 3492 O25 OLC A 412 14793 10434 12374 157 -601 -1008 O HETATM 3493 O23 OLC A 412 -12.461 1.505 -2.162 1.00 99.01 O ANISOU 3493 O23 OLC A 412 14949 10508 12161 232 -730 -953 O HETATM 3494 O20 OLC A 412 -12.637 3.634 -0.742 1.00 98.51 O ANISOU 3494 O20 OLC A 412 14639 10584 12206 206 -656 -816 O HETATM 3495 C18 OLC A 413 -3.068 15.377 33.464 1.00 81.54 C ANISOU 3495 C18 OLC A 413 11103 9434 10446 464 786 182 C HETATM 3496 C10 OLC A 413 4.534 16.253 30.453 1.00 85.68 C ANISOU 3496 C10 OLC A 413 11133 10094 11329 588 377 -33 C HETATM 3497 C9 OLC A 413 4.638 15.474 31.542 1.00 86.42 C ANISOU 3497 C9 OLC A 413 11323 10159 11355 659 319 -22 C HETATM 3498 C17 OLC A 413 -1.728 15.665 32.739 1.00 81.79 C ANISOU 3498 C17 OLC A 413 11047 9506 10522 483 688 147 C HETATM 3499 C11 OLC A 413 3.227 16.744 29.871 1.00 84.95 C ANISOU 3499 C11 OLC A 413 11055 10012 11210 512 467 0 C HETATM 3500 C8 OLC A 413 5.898 14.931 32.175 1.00 87.00 C ANISOU 3500 C8 OLC A 413 11393 10213 11451 747 207 -56 C HETATM 3501 C24 OLC A 413 6.784 3.326 31.923 1.00 87.97 C ANISOU 3501 C24 OLC A 413 12117 9895 11411 1153 274 166 C HETATM 3502 C16 OLC A 413 -1.229 14.435 31.921 1.00 82.28 C ANISOU 3502 C16 OLC A 413 11094 9554 10616 491 686 158 C HETATM 3503 C12 OLC A 413 2.410 17.487 30.961 1.00 84.44 C ANISOU 3503 C12 OLC A 413 11058 9947 11078 511 456 8 C HETATM 3504 C7 OLC A 413 5.828 13.381 32.178 1.00 87.64 C ANISOU 3504 C7 OLC A 413 11550 10254 11495 791 227 -19 C HETATM 3505 C15 OLC A 413 0.311 14.224 32.020 1.00 82.87 C ANISOU 3505 C15 OLC A 413 11148 9639 10700 556 587 130 C HETATM 3506 C13 OLC A 413 1.361 16.596 31.704 1.00 84.04 C ANISOU 3506 C13 OLC A 413 11133 9863 10935 530 497 54 C HETATM 3507 C6 OLC A 413 7.068 12.736 31.498 1.00 88.04 C ANISOU 3507 C6 OLC A 413 11503 10298 11649 831 191 -56 C HETATM 3508 C14 OLC A 413 1.118 15.181 31.084 1.00 83.55 C ANISOU 3508 C14 OLC A 413 11100 9773 10871 529 549 87 C HETATM 3509 C5 OLC A 413 7.372 11.341 32.111 1.00 88.33 C ANISOU 3509 C5 OLC A 413 11641 10284 11637 918 144 -34 C HETATM 3510 C4 OLC A 413 8.783 11.305 32.759 1.00 88.52 C ANISOU 3510 C4 OLC A 413 11630 10292 11711 1017 -8 -88 C HETATM 3511 C3 OLC A 413 9.601 10.087 32.257 1.00 88.67 C ANISOU 3511 C3 OLC A 413 11615 10278 11798 1078 -26 -100 C HETATM 3512 C2 OLC A 413 8.665 8.898 31.914 1.00 89.02 C ANISOU 3512 C2 OLC A 413 11769 10288 11768 1059 79 -34 C HETATM 3513 C21 OLC A 413 8.059 5.552 32.275 1.00 88.54 C ANISOU 3513 C21 OLC A 413 11992 10077 11573 1170 125 72 C HETATM 3514 C1 OLC A 413 9.292 7.564 32.247 1.00 89.39 C ANISOU 3514 C1 OLC A 413 11880 10275 11808 1158 17 -27 C HETATM 3515 C22 OLC A 413 7.430 4.566 31.250 1.00 88.00 C ANISOU 3515 C22 OLC A 413 11940 9981 11513 1116 251 103 C HETATM 3516 O19 OLC A 413 10.162 7.463 33.100 1.00 89.91 O ANISOU 3516 O19 OLC A 413 11964 10318 11879 1254 -119 -55 O HETATM 3517 O25 OLC A 413 7.254 3.187 33.275 1.00 88.01 O ANISOU 3517 O25 OLC A 413 12236 9863 11342 1254 160 178 O HETATM 3518 O23 OLC A 413 6.517 5.209 30.335 1.00 87.35 O ANISOU 3518 O23 OLC A 413 11802 9944 11444 1001 361 109 O HETATM 3519 O20 OLC A 413 8.829 6.521 31.532 1.00 89.08 O ANISOU 3519 O20 OLC A 413 11880 10206 11760 1137 113 8 O HETATM 3520 S SO4 A 414 -12.878 46.135 31.673 0.50 51.10 S HETATM 3521 O1 SO4 A 414 -11.976 45.255 30.950 0.50 51.45 O HETATM 3522 O2 SO4 A 414 -13.673 46.873 30.699 0.50 50.98 O HETATM 3523 O3 SO4 A 414 -13.743 45.322 32.518 0.50 51.42 O HETATM 3524 O4 SO4 A 414 -12.117 47.052 32.512 0.50 51.04 O HETATM 3525 CL CL A 415 -5.075 2.007 17.947 1.00 66.82 CL HETATM 3526 O HOH A 501 6.287 39.702 18.463 1.00 48.78 O HETATM 3527 O HOH A 502 -6.945 10.503 19.171 1.00 51.02 O HETATM 3528 O HOH A 503 5.301 41.742 15.178 1.00 44.67 O HETATM 3529 O HOH A 504 -7.345 53.885 24.763 1.00 41.92 O HETATM 3530 O HOH A 505 -1.148 50.824 25.114 1.00 50.43 O HETATM 3531 O HOH A 506 -11.617 24.944 23.591 1.00 45.29 O HETATM 3532 O HOH A 507 -4.202 50.186 18.273 1.00 47.19 O HETATM 3533 O HOH A 508 -5.324 40.757 28.735 1.00 42.59 O HETATM 3534 O HOH A 509 1.846 0.982 27.406 1.00 54.08 O HETATM 3535 O HOH A 510 -5.746 17.979 8.803 1.00 45.25 O HETATM 3536 O HOH A 511 -2.191 42.266 14.389 1.00 63.43 O HETATM 3537 O HOH A 512 -6.947 11.788 16.974 1.00 55.59 O HETATM 3538 O HOH A 513 -3.843 1.433 25.582 1.00 72.25 O HETATM 3539 O HOH A 514 -0.424 -4.982 25.311 1.00 77.34 O HETATM 3540 O HOH A 515 -2.205 5.146 12.871 1.00 59.06 O HETATM 3541 O HOH A 516 -4.772 -2.286 24.571 1.00 80.02 O HETATM 3542 O HOH A 517 -21.552 0.344 10.090 1.00 75.05 O HETATM 3543 O HOH A 518 -4.829 45.906 16.681 1.00 53.43 O HETATM 3544 O HOH A 519 -5.815 45.097 23.706 1.00 44.44 O HETATM 3545 O HOH A 520 -0.434 45.730 32.461 1.00 53.73 O HETATM 3546 O HOH A 521 -1.311 44.303 27.804 1.00 47.46 O HETATM 3547 O HOH A 522 -9.690 24.871 21.781 1.00 36.46 O HETATM 3548 O HOH A 523 -3.494 12.652 21.507 1.00 41.03 O HETATM 3549 O HOH A 524 -5.029 5.696 12.879 1.00 62.47 O HETATM 3550 O HOH A 525 -8.572 49.396 34.479 1.00 71.70 O HETATM 3551 O HOH A 526 8.489 44.167 10.612 1.00 71.97 O HETATM 3552 O HOH A 527 -19.416 47.116 19.620 1.00 85.44 O HETATM 3553 O HOH A 528 -6.508 8.011 22.348 1.00 34.94 O HETATM 3554 O HOH A 529 6.153 41.313 9.476 1.00 80.38 O HETATM 3555 O HOH A 530 3.853 1.536 11.972 1.00 58.80 O HETATM 3556 O HOH A 531 2.546 43.805 20.572 1.00 48.71 O HETATM 3557 O HOH A 532 -2.115 45.078 15.213 1.00 68.23 O HETATM 3558 O HOH A 533 -15.663 4.487 0.988 1.00 80.70 O HETATM 3559 O HOH A 534 0.047 50.812 11.715 1.00 66.76 O HETATM 3560 O HOH A 535 -6.098 51.428 33.772 1.00 56.14 O HETATM 3561 O HOH A 536 -10.020 -9.812 2.369 1.00 74.93 O HETATM 3562 O HOH A 537 -3.241 8.260 17.050 1.00 43.00 O HETATM 3563 O HOH A 538 -8.954 -5.917 -1.068 1.00 72.70 O HETATM 3564 O HOH A 539 23.334 42.279 13.580 1.00 88.21 O HETATM 3565 O HOH A 540 -3.209 51.857 30.803 1.00 67.81 O HETATM 3566 O HOH A 541 3.040 -7.118 27.653 1.00 59.94 O HETATM 3567 O HOH A 542 5.344 50.117 10.229 1.00 51.87 O HETATM 3568 O HOH A 543 -18.103 2.883 5.773 1.00 67.18 O HETATM 3569 O HOH A 544 -5.229 10.337 20.994 1.00 46.45 O HETATM 3570 O HOH A 545 -18.413 42.717 6.031 1.00 80.23 O HETATM 3571 O HOH A 546 -18.811 1.872 7.868 1.00 60.93 O HETATM 3572 O HOH A 547 -10.088 -1.974 -3.331 1.00 74.67 O HETATM 3573 O HOH A 548 5.755 44.869 12.656 1.00 63.00 O HETATM 3574 O HOH A 549 7.709 42.249 12.759 1.00 71.33 O HETATM 3575 O HOH A 550 -14.189 -1.281 20.510 1.00 78.24 O HETATM 3576 O HOH A 551 11.349 4.519 8.787 1.00 69.00 O HETATM 3577 O HOH A 552 0.716 47.481 6.736 1.00 58.01 O HETATM 3578 O HOH A 553 -8.265 -0.356 10.744 1.00 64.25 O HETATM 3579 O HOH A 554 -7.927 -3.611 30.742 1.00 63.63 O HETATM 3580 O HOH A 555 -11.729 58.998 7.278 1.00100.54 O HETATM 3581 O HOH A 556 -13.221 4.425 30.372 1.00 49.66 O HETATM 3582 O HOH A 557 -23.371 -1.834 14.080 1.00 69.97 O HETATM 3583 O HOH A 558 -9.867 -0.999 13.028 1.00 87.61 O HETATM 3584 O HOH A 559 -16.006 57.726 13.215 1.00 84.71 O HETATM 3585 O HOH A 560 -20.835 3.009 9.174 1.00 76.07 O HETATM 3586 O HOH A 561 -1.732 5.526 16.887 1.00 52.83 O HETATM 3587 O HOH A 562 12.616 10.458 9.808 1.00 76.35 O HETATM 3588 O HOH A 563 5.626 44.413 31.776 1.00 69.44 O HETATM 3589 O HOH A 564 7.069 -7.159 18.843 1.00 64.45 O HETATM 3590 O HOH A 565 -14.895 -3.155 0.953 1.00 75.35 O HETATM 3591 O HOH A 566 14.363 14.932 12.015 1.00 68.60 O HETATM 3592 O HOH A 567 24.876 42.688 15.774 1.00 76.27 O HETATM 3593 O HOH A 568 2.698 40.671 36.514 1.00 78.68 O HETATM 3594 O HOH A 569 -16.728 36.501 8.419 1.00 71.11 O HETATM 3595 O HOH A 570 -8.701 41.500 5.087 1.00 74.49 O HETATM 3596 O HOH A 571 -4.543 -6.110 25.146 1.00 74.13 O HETATM 3597 O HOH A 572 -14.522 25.077 8.622 1.00 55.39 O HETATM 3598 O HOH A 573 6.653 38.550 8.300 1.00 67.75 O HETATM 3599 O HOH A 574 -20.355 26.858 15.719 1.00 58.34 O HETATM 3600 O HOH A 575 25.799 41.665 18.202 1.00 78.65 O HETATM 3601 O HOH A 576 -17.408 56.692 15.301 1.00 75.45 O HETATM 3602 O HOH A 577 15.630 36.459 31.150 1.00 69.69 O HETATM 3603 O HOH A 578 -11.112 -0.946 27.507 1.00 70.12 O HETATM 3604 O HOH A 579 -17.282 -1.403 22.993 1.00 57.09 O HETATM 3605 O HOH A 580 -14.617 29.679 7.306 1.00 67.81 O HETATM 3606 O HOH A 581 10.713 8.541 3.458 1.00 75.85 O HETATM 3607 O HOH A 582 7.612 30.444 10.126 1.00 67.99 O HETATM 3608 O HOH A 583 -4.605 48.800 15.944 1.00 44.34 O HETATM 3609 O HOH A 584 8.943 10.002 2.165 1.00 65.55 O HETATM 3610 O HOH A 585 22.396 38.473 23.425 1.00 71.10 O HETATM 3611 O HOH A 586 12.087 6.457 6.973 1.00 70.91 O HETATM 3612 O HOH A 587 -6.312 41.118 36.782 1.00 45.40 O HETATM 3613 O HOH A 588 -20.290 19.152 15.181 1.00 50.89 O HETATM 3614 O HOH A 589 -19.141 5.105 7.112 1.00 68.99 O HETATM 3615 O HOH A 590 16.417 20.773 15.127 1.00 67.90 O HETATM 3616 O HOH A 591 5.801 15.168 3.588 1.00 58.23 O HETATM 3617 O HOH A 592 -16.032 17.105 25.640 1.00 59.87 O HETATM 3618 O HOH A 593 10.824 32.145 12.358 1.00 54.17 O HETATM 3619 O HOH A 594 -6.968 -6.418 26.325 1.00 85.07 O HETATM 3620 O HOH A 595 -24.931 13.161 14.448 1.00 74.20 O HETATM 3621 O HOH A 596 6.553 11.220 1.900 1.00 62.86 O HETATM 3622 O HOH A 597 21.915 38.424 26.410 1.00 84.88 O HETATM 3623 O HOH A 598 -11.662 46.707 5.491 1.00 68.11 O HETATM 3624 O HOH A 599 -5.779 50.264 13.988 1.00 55.35 O HETATM 3625 O HOH A 600 -1.751 24.132 34.699 1.00 69.73 O HETATM 3626 O HOH A 601 9.634 39.674 3.048 1.00 76.39 O HETATM 3627 O HOH A 602 -1.606 26.629 5.124 1.00 68.20 O HETATM 3628 O HOH A 603 -23.879 15.861 13.844 1.00 66.29 O HETATM 3629 O HOH A 604 -25.206 13.989 24.815 1.00 68.37 O HETATM 3630 O HOH A 605 -2.094 30.335 3.645 1.00 67.26 O HETATM 3631 O HOH A 606 -18.696 18.976 6.857 1.00 75.04 O HETATM 3632 O HOH A 607 -9.225 58.943 5.439 1.00 70.86 O HETATM 3633 O HOH A 609 -2.857 33.381 3.512 1.00 63.09 O HETATM 3634 O HOH B 201 7.502 76.080 31.914 1.00 47.59 O HETATM 3635 O HOH B 202 6.410 43.952 24.538 1.00 45.95 O HETATM 3636 O HOH B 203 -16.789 65.176 28.067 1.00 53.32 O HETATM 3637 O HOH B 204 -11.973 68.419 32.516 1.00 58.24 O HETATM 3638 O HOH B 205 -2.914 55.684 28.981 1.00 48.32 O HETATM 3639 O HOH B 206 5.095 43.444 21.507 1.00 51.07 O HETATM 3640 O HOH B 207 13.873 50.643 19.761 1.00 83.69 O HETATM 3641 O HOH B 208 -6.740 65.155 16.622 1.00 56.20 O HETATM 3642 O HOH B 209 -8.858 55.601 22.845 1.00 50.89 O HETATM 3643 O HOH B 210 -2.426 70.665 19.291 1.00 53.92 O HETATM 3644 O HOH B 211 0.802 58.892 36.320 1.00 54.20 O HETATM 3645 O HOH B 212 -14.462 60.177 24.755 1.00 78.68 O HETATM 3646 O HOH B 213 3.993 75.461 24.146 1.00 55.36 O HETATM 3647 O HOH B 214 4.015 73.421 37.197 1.00 46.62 O HETATM 3648 O HOH B 215 -8.015 57.436 20.159 1.00 57.16 O HETATM 3649 O HOH B 216 12.732 48.760 18.330 1.00 67.89 O HETATM 3650 O HOH B 217 3.904 68.628 9.340 1.00 64.52 O HETATM 3651 O HOH B 218 -0.852 74.695 17.773 1.00 60.52 O HETATM 3652 O HOH B 219 -6.220 60.628 12.883 1.00 61.67 O HETATM 3653 O HOH B 220 4.035 65.801 39.350 1.00 65.27 O HETATM 3654 O HOH B 221 6.707 51.968 11.157 1.00 55.07 O HETATM 3655 O HOH B 222 6.240 53.944 35.516 1.00 74.95 O HETATM 3656 O HOH B 223 8.345 55.676 9.543 1.00 69.20 O HETATM 3657 O HOH B 224 12.848 53.937 10.342 1.00 72.75 O HETATM 3658 O HOH B 225 -10.805 74.982 28.683 1.00 58.72 O HETATM 3659 O HOH B 226 -9.266 59.315 18.250 1.00 65.92 O HETATM 3660 O HOH B 227 -2.838 74.772 19.617 1.00 53.91 O HETATM 3661 O HOH B 228 8.518 56.084 34.167 1.00 67.24 O HETATM 3662 O HOH B 229 -6.922 79.271 30.286 1.00 64.25 O HETATM 3663 O HOH B 230 1.043 55.995 45.605 1.00 66.19 O HETATM 3664 O HOH B 231 -13.364 73.407 36.616 1.00 62.28 O HETATM 3665 O HOH B 232 -7.700 62.670 34.019 1.00 75.20 O HETATM 3666 O HOH B 233 11.702 53.607 28.271 1.00 70.96 O HETATM 3667 O HOH B 234 16.993 69.382 21.920 1.00 56.40 O HETATM 3668 O HOH B 235 6.385 63.640 39.376 1.00 64.08 O HETATM 3669 O HOH B 236 8.674 50.508 30.028 1.00 65.50 O HETATM 3670 O HOH B 237 14.596 53.435 19.652 1.00 60.09 O HETATM 3671 O HOH B 238 9.106 58.276 32.734 1.00 53.10 O HETATM 3672 O HOH B 239 -6.610 63.367 12.573 1.00 68.85 O HETATM 3673 O HOH B 240 4.705 70.457 41.471 1.00 76.73 O HETATM 3674 O HOH B 241 15.658 50.444 24.933 1.00 59.99 O HETATM 3675 O HOH B 242 4.757 59.929 5.605 1.00 67.66 O HETATM 3676 O HOH B 243 -11.602 66.064 33.863 1.00 65.88 O HETATM 3677 O HOH B 244 -15.132 58.863 20.108 1.00 73.09 O HETATM 3678 O HOH B 245 -0.205 70.130 43.351 1.00 54.93 O HETATM 3679 O HOH B 246 14.654 52.398 11.886 1.00 85.60 O CONECT 6 1975 CONECT 690 1323 CONECT 1323 690 CONECT 1975 6 CONECT 2459 3016 CONECT 2662 3090 CONECT 3016 2459 CONECT 3090 2662 CONECT 3271 3272 3290 3306 CONECT 3272 3271 3273 CONECT 3273 3272 3288 3305 CONECT 3274 3275 3276 3294 CONECT 3275 3274 3291 CONECT 3276 3274 3295 3296 CONECT 3277 3278 3282 3295 CONECT 3278 3277 3279 3283 CONECT 3279 3278 3280 CONECT 3280 3279 3281 3303 CONECT 3281 3280 3282 CONECT 3282 3277 3281 CONECT 3283 3278 3284 CONECT 3284 3283 3297 3298 CONECT 3285 3286 3299 3302 CONECT 3286 3285 3300 CONECT 3287 3300 3301 CONECT 3288 3273 3289 3299 CONECT 3289 3288 3290 CONECT 3290 3271 3289 3293 CONECT 3291 3275 3292 CONECT 3292 3291 3293 CONECT 3293 3290 3292 3294 CONECT 3294 3274 3293 3304 CONECT 3295 3276 3277 CONECT 3296 3276 CONECT 3297 3284 CONECT 3298 3284 CONECT 3299 3285 3288 CONECT 3300 3286 3287 CONECT 3301 3287 3302 CONECT 3302 3285 3301 CONECT 3303 3280 CONECT 3304 3294 CONECT 3305 3273 CONECT 3306 3271 CONECT 3307 3308 3309 CONECT 3308 3307 3310 CONECT 3309 3307 3312 CONECT 3310 3308 3313 CONECT 3311 3321 3323 CONECT 3312 3309 CONECT 3313 3310 3314 CONECT 3314 3313 3315 CONECT 3315 3314 3316 CONECT 3316 3315 3317 CONECT 3317 3316 3318 CONECT 3318 3317 3320 CONECT 3319 3321 3325 CONECT 3320 3318 3322 3325 CONECT 3321 3311 3319 3324 CONECT 3322 3320 CONECT 3323 3311 CONECT 3324 3321 CONECT 3325 3319 3320 CONECT 3326 3327 3328 CONECT 3327 3326 3329 CONECT 3328 3326 3331 CONECT 3329 3327 3332 CONECT 3330 3340 3342 CONECT 3331 3328 CONECT 3332 3329 3333 CONECT 3333 3332 3334 CONECT 3334 3333 3335 CONECT 3335 3334 3336 CONECT 3336 3335 3337 CONECT 3337 3336 3339 CONECT 3338 3340 3344 CONECT 3339 3337 3341 3344 CONECT 3340 3330 3338 3343 CONECT 3341 3339 CONECT 3342 3330 CONECT 3343 3340 CONECT 3344 3338 3339 CONECT 3345 3347 CONECT 3346 3355 3357 CONECT 3347 3345 3348 CONECT 3348 3347 3349 CONECT 3349 3348 3350 CONECT 3350 3349 3351 CONECT 3351 3350 3352 CONECT 3352 3351 3354 CONECT 3353 3355 3359 CONECT 3354 3352 3356 3359 CONECT 3355 3346 3353 3358 CONECT 3356 3354 CONECT 3357 3346 CONECT 3358 3355 CONECT 3359 3353 3354 CONECT 3360 3361 3362 CONECT 3361 3360 3363 CONECT 3362 3360 3365 CONECT 3363 3361 3366 CONECT 3364 3376 3378 CONECT 3365 3362 3367 CONECT 3366 3363 3368 CONECT 3367 3365 3369 CONECT 3368 3366 3370 CONECT 3369 3367 CONECT 3370 3368 3371 CONECT 3371 3370 3372 CONECT 3372 3371 3373 CONECT 3373 3372 3375 CONECT 3374 3376 3380 CONECT 3375 3373 3377 3380 CONECT 3376 3364 3374 3379 CONECT 3377 3375 CONECT 3378 3364 CONECT 3379 3376 CONECT 3380 3374 3375 CONECT 3381 3390 3392 CONECT 3382 3383 CONECT 3383 3382 3384 CONECT 3384 3383 3385 CONECT 3385 3384 3386 CONECT 3386 3385 3387 CONECT 3387 3386 3389 CONECT 3388 3390 3394 CONECT 3389 3387 3391 3394 CONECT 3390 3381 3388 3393 CONECT 3391 3389 CONECT 3392 3381 CONECT 3393 3390 CONECT 3394 3388 3389 CONECT 3395 3398 CONECT 3396 3397 3399 CONECT 3397 3396 3400 CONECT 3398 3395 3402 CONECT 3399 3396 3403 CONECT 3400 3397 3404 CONECT 3401 3415 3417 CONECT 3402 3398 3405 CONECT 3403 3399 3406 CONECT 3404 3400 3407 CONECT 3405 3402 3408 CONECT 3406 3403 3408 CONECT 3407 3404 3409 CONECT 3408 3405 3406 CONECT 3409 3407 3410 CONECT 3410 3409 3411 CONECT 3411 3410 3412 CONECT 3412 3411 3414 CONECT 3413 3415 3419 CONECT 3414 3412 3416 3419 CONECT 3415 3401 3413 3418 CONECT 3416 3414 CONECT 3417 3401 CONECT 3418 3415 CONECT 3419 3413 3414 CONECT 3420 3425 3427 CONECT 3421 3422 CONECT 3422 3421 3424 CONECT 3423 3425 3429 CONECT 3424 3422 3426 3429 CONECT 3425 3420 3423 3428 CONECT 3426 3424 CONECT 3427 3420 CONECT 3428 3425 CONECT 3429 3423 3424 CONECT 3430 3437 3439 CONECT 3431 3432 CONECT 3432 3431 3433 CONECT 3433 3432 3434 CONECT 3434 3433 3436 CONECT 3435 3437 3441 CONECT 3436 3434 3438 3441 CONECT 3437 3430 3435 3440 CONECT 3438 3436 CONECT 3439 3430 CONECT 3440 3437 CONECT 3441 3435 3436 CONECT 3442 3448 3450 CONECT 3443 3444 CONECT 3444 3443 3445 CONECT 3445 3444 3447 CONECT 3446 3448 3452 CONECT 3447 3445 3449 3452 CONECT 3448 3442 3446 3451 CONECT 3449 3447 CONECT 3450 3442 CONECT 3451 3448 CONECT 3452 3446 3447 CONECT 3453 3456 CONECT 3454 3455 3457 CONECT 3455 3454 3458 CONECT 3456 3453 3460 CONECT 3457 3454 3461 CONECT 3458 3455 3462 CONECT 3459 3473 3475 CONECT 3460 3456 3463 CONECT 3461 3457 3464 CONECT 3462 3458 3465 CONECT 3463 3460 3466 CONECT 3464 3461 3466 CONECT 3465 3462 3467 CONECT 3466 3463 3464 CONECT 3467 3465 3468 CONECT 3468 3467 3469 CONECT 3469 3468 3470 CONECT 3470 3469 3472 CONECT 3471 3473 3477 CONECT 3472 3470 3474 3477 CONECT 3473 3459 3471 3476 CONECT 3474 3472 CONECT 3475 3459 CONECT 3476 3473 CONECT 3477 3471 3472 CONECT 3478 3479 CONECT 3479 3478 3480 CONECT 3480 3479 3482 CONECT 3481 3490 3492 CONECT 3482 3480 3483 CONECT 3483 3482 3484 CONECT 3484 3483 3485 CONECT 3485 3484 3486 CONECT 3486 3485 3487 CONECT 3487 3486 3489 CONECT 3488 3490 3494 CONECT 3489 3487 3491 3494 CONECT 3490 3481 3488 3493 CONECT 3491 3489 CONECT 3492 3481 CONECT 3493 3490 CONECT 3494 3488 3489 CONECT 3495 3498 CONECT 3496 3497 3499 CONECT 3497 3496 3500 CONECT 3498 3495 3502 CONECT 3499 3496 3503 CONECT 3500 3497 3504 CONECT 3501 3515 3517 CONECT 3502 3498 3505 CONECT 3503 3499 3506 CONECT 3504 3500 3507 CONECT 3505 3502 3508 CONECT 3506 3503 3508 CONECT 3507 3504 3509 CONECT 3508 3505 3506 CONECT 3509 3507 3510 CONECT 3510 3509 3511 CONECT 3511 3510 3512 CONECT 3512 3511 3514 CONECT 3513 3515 3519 CONECT 3514 3512 3516 3519 CONECT 3515 3501 3513 3518 CONECT 3516 3514 CONECT 3517 3501 CONECT 3518 3515 CONECT 3519 3513 3514 CONECT 3520 3521 3522 3523 3524 CONECT 3521 3520 CONECT 3522 3520 CONECT 3523 3520 CONECT 3524 3520 MASTER 453 0 15 18 14 0 30 6 3677 2 262 38 END