HEADER MEMBRANE PROTEIN 12-JUL-19 6PS5 TITLE XFEL BETA2 AR STRUCTURE BY LIGAND EXCHANGE FROM TIMOLOL TO TITLE 2 PROPRANOLOL. COMPND MOL_ID: 1; COMPND 2 MOLECULE: FUSION PROTEIN OF BETA-2 ADRENERGIC RECEPTOR AND T4 COMPND 3 LYSOZYME; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: BETA-2 ADRENORECEPTOR,BETA-2 ADRENOCEPTOR,LYSIS PROTEIN, COMPND 6 LYSOZYME,MURAMIDASE; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 10665; SOURCE 5 GENE: ADRB2, ADRB2R, B2AR, E, T4TP126; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS KEYWDS GPCR, COMPLEX-LCP METHOD, SBDD, DRUG DESIGN, XFEL, LCP-SFX, LIGAND KEYWDS 2 EXCHANGE, TIMOLOL, PROPRANOLOL, B2AR, BETA2AR, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR A.ISHCHENKO,B.STAUCH,G.W.HAN,A.BATYUK,A.SHIRIAEVA,C.LI,N.A.ZATSEPIN, AUTHOR 2 U.WEIERSTALL,W.LIU,E.NANGO,T.NAKANE,R.TANAKA,K.TONO,Y.JOTI,S.IWATA, AUTHOR 3 I.MORAES,C.GATI,C.CHEREZOV REVDAT 3 01-JAN-20 6PS5 1 REMARK REVDAT 2 25-DEC-19 6PS5 1 JRNL REVDAT 1 13-NOV-19 6PS5 0 JRNL AUTH A.ISHCHENKO,B.STAUCH,G.W.HAN,A.BATYUK,A.SHIRIAEVA,C.LI, JRNL AUTH 2 N.ZATSEPIN,U.WEIERSTALL,W.LIU,E.NANGO,T.NAKANE,R.TANAKA, JRNL AUTH 3 K.TONO,Y.JOTI,S.IWATA,I.MORAES,C.GATI,V.CHEREZOV JRNL TITL TOWARD G PROTEIN-COUPLED RECEPTOR STRUCTURE-BASED DRUG JRNL TITL 2 DESIGN USING X-RAY LASERS. JRNL REF IUCRJ V. 6 1106 2019 JRNL REFN ESSN 2052-2525 JRNL PMID 31709066 JRNL DOI 10.1107/S2052252519013137 REMARK 2 REMARK 2 RESOLUTION. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.10.2 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.44 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 13418 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) : 0.223 REMARK 3 R VALUE (WORKING SET) : 0.221 REMARK 3 FREE R VALUE : 0.258 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020 REMARK 3 FREE R VALUE TEST SET COUNT : 673 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 7 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.13 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.68 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2649 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2290 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2513 REMARK 3 BIN R VALUE (WORKING SET) : 0.2290 REMARK 3 BIN FREE R VALUE : 0.2390 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.13 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 136 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 : 3466 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 155 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 105.2 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -7.18170 REMARK 3 B22 (A**2) : 9.36810 REMARK 3 B33 (A**2) : -2.18650 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.520 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.384 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 3698 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 5023 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1679 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 67 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 531 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 3698 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 497 ; 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 : 4031 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.009 REMARK 3 BOND ANGLES (DEGREES) : 0.92 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.78 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.82 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|* } REMARK 3 ORIGIN FOR THE GROUP (A): 8.4218 3.0831 26.0663 REMARK 3 T TENSOR REMARK 3 T11: 0.0901 T22: -0.2011 REMARK 3 T33: -0.3044 T12: 0.0142 REMARK 3 T13: 0.0110 T23: 0.0212 REMARK 3 L TENSOR REMARK 3 L11: 0.6061 L22: 0.5919 REMARK 3 L33: 2.7059 L12: -0.2455 REMARK 3 L13: -0.8568 L23: 0.6758 REMARK 3 S TENSOR REMARK 3 S11: 0.0184 S12: -0.0389 S13: 0.0123 REMARK 3 S21: 0.0452 S22: -0.0333 S23: -0.0357 REMARK 3 S31: -0.2207 S32: 0.0232 S33: 0.0149 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6PS5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-19. REMARK 100 THE DEPOSITION ID IS D_1000242976. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-MAY-15 REMARK 200 TEMPERATURE (KELVIN) : 293 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : FREE ELECTRON LASER REMARK 200 BEAMLINE : BL3 REMARK 200 X-RAY GENERATOR MODEL : SACLA BEAMLINE BL3 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.76 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MPCCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL REMARK 200 DATA SCALING SOFTWARE : CRYSTFEL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13464 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 REMARK 200 RESOLUTION RANGE LOW (A) : 46.440 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 104.0 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 2.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.13 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 3D4S REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.70 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.0, 0.1 M AMMONIUM REMARK 280 SULFATE, 30% PEG 400, 2 MM OF TARGET LIGAND PROPRANOLOL, LIPIDIC REMARK 280 CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 21.36500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 86.94000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.80000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 86.94000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.36500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.80000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A -23 REMARK 465 LYS A -22 REMARK 465 THR A -21 REMARK 465 ILE A -20 REMARK 465 ILE A -19 REMARK 465 ALA A -18 REMARK 465 LEU A -17 REMARK 465 SER A -16 REMARK 465 TYR A -15 REMARK 465 ILE A -14 REMARK 465 PHE A -13 REMARK 465 CYS A -12 REMARK 465 LEU A -11 REMARK 465 VAL A -10 REMARK 465 PHE A -9 REMARK 465 ALA A -8 REMARK 465 ASP A -7 REMARK 465 TYR A -6 REMARK 465 LYS A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 ASP A -2 REMARK 465 ASP A -1 REMARK 465 ALA A 0 REMARK 465 MET A 1 REMARK 465 GLY A 2 REMARK 465 GLN A 3 REMARK 465 PRO A 4 REMARK 465 GLY A 5 REMARK 465 ASN A 6 REMARK 465 GLY A 7 REMARK 465 SER A 8 REMARK 465 ALA A 9 REMARK 465 PHE A 10 REMARK 465 LEU A 11 REMARK 465 LEU A 12 REMARK 465 ALA A 13 REMARK 465 PRO A 14 REMARK 465 ASN A 15 REMARK 465 ARG A 16 REMARK 465 SER A 17 REMARK 465 HIS A 18 REMARK 465 ALA A 19 REMARK 465 PRO A 20 REMARK 465 ASP A 21 REMARK 465 HIS A 22 REMARK 465 ASP A 23 REMARK 465 VAL A 24 REMARK 465 THR A 25 REMARK 465 GLN A 26 REMARK 465 GLN A 27 REMARK 465 ARG A 28 REMARK 465 ARG A 343 REMARK 465 ARG A 344 REMARK 465 SER A 345 REMARK 465 SER A 346 REMARK 465 LEU A 347 REMARK 465 LYS A 348 REMARK 465 HIS A 349 REMARK 465 HIS A 350 REMARK 465 HIS A 351 REMARK 465 HIS A 352 REMARK 465 HIS A 353 REMARK 465 HIS A 354 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 TRP A 32 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 32 CZ3 CH2 REMARK 470 LYS A1016 CG CD CE NZ REMARK 470 LYS A1019 CG CD CE NZ REMARK 470 LYS A1043 CG CD CE NZ REMARK 470 GLU A1045 CG CD OE1 OE2 REMARK 470 LYS A1048 CG CD CE NZ REMARK 470 ASN A1055 CG OD1 ND2 REMARK 470 LYS A1060 CG CD CE NZ REMARK 470 GLU A1064 CG CD OE1 OE2 REMARK 470 LYS A1065 CG CD CE NZ REMARK 470 GLN A1069 CG CD OE1 NE2 REMARK 470 ARG A1076 CG CD NE CZ NH1 NH2 REMARK 470 LYS A1083 CG CD CE NZ REMARK 470 LYS A1124 CG CD CE NZ REMARK 470 LYS A1135 CG CD CE NZ REMARK 470 ARG A1137 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 267 CG CD CE NZ REMARK 470 LEU A 302 CG CD1 CD2 REMARK 470 ARG A 304 CG CD NE CZ NH1 NH2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 VAL A 86 -65.63 -106.84 REMARK 500 LYS A 140 -49.95 59.44 REMARK 500 PHE A1114 59.02 -90.62 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLA A 1207 REMARK 610 OLA A 1208 REMARK 610 OLC A 1209 REMARK 610 OLC A 1210 REMARK 610 OLC A 1211 REMARK 610 OLC A 1212 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SNP A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1203 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1204 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1205 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1206 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1207 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1208 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1209 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1210 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1211 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1212 DBREF 6PS5 A 1 230 UNP P07550 ADRB2_HUMAN 1 230 DBREF 6PS5 A 1002 1161 UNP D9IEF7 D9IEF7_BPT4 2 161 DBREF 6PS5 A 263 348 UNP P07550 ADRB2_HUMAN 263 348 SEQADV 6PS5 MET A -23 UNP P07550 INITIATING METHIONINE SEQADV 6PS5 LYS A -22 UNP P07550 EXPRESSION TAG SEQADV 6PS5 THR A -21 UNP P07550 EXPRESSION TAG SEQADV 6PS5 ILE A -20 UNP P07550 EXPRESSION TAG SEQADV 6PS5 ILE A -19 UNP P07550 EXPRESSION TAG SEQADV 6PS5 ALA A -18 UNP P07550 EXPRESSION TAG SEQADV 6PS5 LEU A -17 UNP P07550 EXPRESSION TAG SEQADV 6PS5 SER A -16 UNP P07550 EXPRESSION TAG SEQADV 6PS5 TYR A -15 UNP P07550 EXPRESSION TAG SEQADV 6PS5 ILE A -14 UNP P07550 EXPRESSION TAG SEQADV 6PS5 PHE A -13 UNP P07550 EXPRESSION TAG SEQADV 6PS5 CYS A -12 UNP P07550 EXPRESSION TAG SEQADV 6PS5 LEU A -11 UNP P07550 EXPRESSION TAG SEQADV 6PS5 VAL A -10 UNP P07550 EXPRESSION TAG SEQADV 6PS5 PHE A -9 UNP P07550 EXPRESSION TAG SEQADV 6PS5 ALA A -8 UNP P07550 EXPRESSION TAG SEQADV 6PS5 ASP A -7 UNP P07550 EXPRESSION TAG SEQADV 6PS5 TYR A -6 UNP P07550 EXPRESSION TAG SEQADV 6PS5 LYS A -5 UNP P07550 EXPRESSION TAG SEQADV 6PS5 ASP A -4 UNP P07550 EXPRESSION TAG SEQADV 6PS5 ASP A -3 UNP P07550 EXPRESSION TAG SEQADV 6PS5 ASP A -2 UNP P07550 EXPRESSION TAG SEQADV 6PS5 ASP A -1 UNP P07550 EXPRESSION TAG SEQADV 6PS5 ALA A 0 UNP P07550 EXPRESSION TAG SEQADV 6PS5 ARG A 16 UNP P07550 GLY 16 VARIANT SEQADV 6PS5 GLN A 27 UNP P07550 GLU 27 VARIANT SEQADV 6PS5 TRP A 122 UNP P07550 GLU 122 ENGINEERED MUTATION SEQADV 6PS5 GLU A 187 UNP P07550 ASN 187 ENGINEERED MUTATION SEQADV 6PS5 THR A 1054 UNP D9IEF7 CYS 54 ENGINEERED MUTATION SEQADV 6PS5 ALA A 1097 UNP D9IEF7 CYS 97 ENGINEERED MUTATION SEQADV 6PS5 HIS A 349 UNP P07550 EXPRESSION TAG SEQADV 6PS5 HIS A 350 UNP P07550 EXPRESSION TAG SEQADV 6PS5 HIS A 351 UNP P07550 EXPRESSION TAG SEQADV 6PS5 HIS A 352 UNP P07550 EXPRESSION TAG SEQADV 6PS5 HIS A 353 UNP P07550 EXPRESSION TAG SEQADV 6PS5 HIS A 354 UNP P07550 EXPRESSION TAG SEQRES 1 A 506 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 A 506 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP ALA MET GLY SEQRES 3 A 506 GLN PRO GLY ASN GLY SER ALA PHE LEU LEU ALA PRO ASN SEQRES 4 A 506 ARG SER HIS ALA PRO ASP HIS ASP VAL THR GLN GLN ARG SEQRES 5 A 506 ASP GLU VAL TRP VAL VAL GLY MET GLY ILE VAL MET SER SEQRES 6 A 506 LEU ILE VAL LEU ALA ILE VAL PHE GLY ASN VAL LEU VAL SEQRES 7 A 506 ILE THR ALA ILE ALA LYS PHE GLU ARG LEU GLN THR VAL SEQRES 8 A 506 THR ASN TYR PHE ILE THR SER LEU ALA CYS ALA ASP LEU SEQRES 9 A 506 VAL MET GLY LEU ALA VAL VAL PRO PHE GLY ALA ALA HIS SEQRES 10 A 506 ILE LEU MET LYS MET TRP THR PHE GLY ASN PHE TRP CYS SEQRES 11 A 506 GLU PHE TRP THR SER ILE ASP VAL LEU CYS VAL THR ALA SEQRES 12 A 506 SER ILE TRP THR LEU CYS VAL ILE ALA VAL ASP ARG TYR SEQRES 13 A 506 PHE ALA ILE THR SER PRO PHE LYS TYR GLN SER LEU LEU SEQRES 14 A 506 THR LYS ASN LYS ALA ARG VAL ILE ILE LEU MET VAL TRP SEQRES 15 A 506 ILE VAL SER GLY LEU THR SER PHE LEU PRO ILE GLN MET SEQRES 16 A 506 HIS TRP TYR ARG ALA THR HIS GLN GLU ALA ILE ASN CYS SEQRES 17 A 506 TYR ALA GLU GLU THR CYS CYS ASP PHE PHE THR ASN GLN SEQRES 18 A 506 ALA TYR ALA ILE ALA SER SER ILE VAL SER PHE TYR VAL SEQRES 19 A 506 PRO LEU VAL ILE MET VAL PHE VAL TYR SER ARG VAL PHE SEQRES 20 A 506 GLN GLU ALA LYS ARG GLN LEU ASN ILE PHE GLU MET LEU SEQRES 21 A 506 ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP SEQRES 22 A 506 THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU SEQRES 23 A 506 THR LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU SEQRES 24 A 506 ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR SEQRES 25 A 506 LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP SEQRES 26 A 506 ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS SEQRES 27 A 506 PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA SEQRES 28 A 506 LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL SEQRES 29 A 506 ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS SEQRES 30 A 506 ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG SEQRES 31 A 506 TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE SEQRES 32 A 506 THR THR PHE ARG THR GLY THR TRP ASP ALA TYR LYS PHE SEQRES 33 A 506 CYS LEU LYS GLU HIS LYS ALA LEU LYS THR LEU GLY ILE SEQRES 34 A 506 ILE MET GLY THR PHE THR LEU CYS TRP LEU PRO PHE PHE SEQRES 35 A 506 ILE VAL ASN ILE VAL HIS VAL ILE GLN ASP ASN LEU ILE SEQRES 36 A 506 ARG LYS GLU VAL TYR ILE LEU LEU ASN TRP ILE GLY TYR SEQRES 37 A 506 VAL ASN SER GLY PHE ASN PRO LEU ILE TYR CYS ARG SER SEQRES 38 A 506 PRO ASP PHE ARG ILE ALA PHE GLN GLU LEU LEU CYS LEU SEQRES 39 A 506 ARG ARG SER SER LEU LYS HIS HIS HIS HIS HIS HIS HET SNP A1201 19 HET SO4 A1202 5 HET SO4 A1203 5 HET SO4 A1204 5 HET SO4 A1205 5 HET CLR A1206 28 HET OLA A1207 14 HET OLA A1208 14 HET OLC A1209 17 HET OLC A1210 16 HET OLC A1211 15 HET OLC A1212 12 HETNAM SNP 1-(ISOPROPYLAMINO)-3-(1-NAPHTHYLOXY)-2-PROPANOL HETNAM SO4 SULFATE ION HETNAM CLR CHOLESTEROL HETNAM OLA OLEIC ACID HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETSYN SNP S-PROPRANOLOL HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 SNP C16 H21 N O2 FORMUL 3 SO4 4(O4 S 2-) FORMUL 7 CLR C27 H46 O FORMUL 8 OLA 2(C18 H34 O2) FORMUL 10 OLC 4(C21 H40 O4) HELIX 1 AA1 ASP A 29 PHE A 61 1 33 HELIX 2 AA2 THR A 66 VAL A 86 1 21 HELIX 3 AA3 VAL A 86 MET A 96 1 11 HELIX 4 AA4 PHE A 101 THR A 136 1 36 HELIX 5 AA5 THR A 146 MET A 171 1 26 HELIX 6 AA6 HIS A 178 GLU A 187 1 10 HELIX 7 AA7 ASN A 196 PHE A 208 1 13 HELIX 8 AA8 PHE A 208 GLN A 229 1 22 HELIX 9 AA9 ASN A 1002 GLY A 1012 1 11 HELIX 10 AB1 SER A 1038 GLY A 1051 1 14 HELIX 11 AB2 THR A 1059 ASN A 1081 1 23 HELIX 12 AB3 LEU A 1084 LEU A 1091 1 8 HELIX 13 AB4 ASP A 1092 GLY A 1107 1 16 HELIX 14 AB5 GLY A 1107 ALA A 1112 1 6 HELIX 15 AB6 PHE A 1114 GLN A 1123 1 10 HELIX 16 AB7 ARG A 1125 LYS A 1135 1 11 HELIX 17 AB8 SER A 1136 THR A 1142 1 7 HELIX 18 AB9 THR A 1142 GLY A 1156 1 15 HELIX 19 AC1 TRP A 1158 LYS A 263 5 5 HELIX 20 AC2 LEU A 266 GLN A 299 1 34 HELIX 21 AC3 ARG A 304 ASN A 318 1 15 HELIX 22 AC4 PHE A 321 TYR A 326 1 6 HELIX 23 AC5 SER A 329 LEU A 340 1 12 SHEET 1 AA1 3 ARG A1014 LYS A1019 0 SHEET 2 AA1 3 TYR A1025 GLY A1028 -1 O GLY A1028 N ARG A1014 SHEET 3 AA1 3 HIS A1031 THR A1034 -1 O LEU A1033 N TYR A1025 SSBOND 1 CYS A 106 CYS A 191 1555 1555 2.03 SSBOND 2 CYS A 184 CYS A 190 1555 1555 2.03 SITE 1 AC1 7 ASP A 113 PHE A 193 SER A 203 TRP A 286 SITE 2 AC1 7 PHE A 289 PHE A 290 ASN A 312 SITE 1 AC2 7 THR A 66 VAL A 67 THR A 68 ARG A 131 SITE 2 AC2 7 TYR A 141 GLN A 142 SER A 143 SITE 1 AC3 3 LYS A 270 LYS A 273 ARG A 328 SITE 1 AC4 4 PHE A1114 THR A1115 ASN A1116 SER A1117 SITE 1 AC5 4 THR A1142 PRO A1143 ASN A1144 ARG A1145 SITE 1 AC6 4 TYR A 70 ARG A 151 ILE A 154 TRP A 158 SITE 1 AC7 3 GLU A 306 ILE A 309 TRP A 313 SITE 1 AC8 2 ILE A 201 OLC A1209 SITE 1 AC9 4 PHE A 49 GLN A 197 LEU A 339 OLA A1208 SITE 1 AD1 2 ILE A 55 CYS A 77 SITE 1 AD2 1 LEU A 144 SITE 1 AD3 4 PHE A 89 PHE A 101 PHE A 217 ARG A 221 CRYST1 42.730 77.600 173.880 90.00 90.00 90.00 P 21 21 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.023403 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012887 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005751 0.00000 ATOM 1 N ASP A 29 18.109 22.606 62.037 1.00147.29 N ANISOU 1 N ASP A 29 21741 19722 14501 -2341 52 -2160 N ATOM 2 CA ASP A 29 18.372 24.038 62.169 1.00148.83 C ANISOU 2 CA ASP A 29 22100 19817 14631 -2631 182 -2337 C ATOM 3 C ASP A 29 17.420 24.861 61.283 1.00151.47 C ANISOU 3 C ASP A 29 22724 19752 15077 -2647 330 -2267 C ATOM 4 O ASP A 29 16.732 24.295 60.430 1.00149.20 O ANISOU 4 O ASP A 29 22462 19310 14917 -2458 321 -2097 O ATOM 5 CB ASP A 29 19.841 24.352 61.826 1.00152.58 C ANISOU 5 CB ASP A 29 22410 20537 15026 -2897 186 -2525 C ATOM 6 CG ASP A 29 20.416 25.531 62.591 1.00165.40 C ANISOU 6 CG ASP A 29 24105 22232 16509 -3200 268 -2758 C ATOM 7 OD1 ASP A 29 20.034 26.681 62.285 1.00166.32 O ANISOU 7 OD1 ASP A 29 24487 22063 16643 -3370 428 -2814 O ATOM 8 OD2 ASP A 29 21.266 25.304 63.478 1.00173.26 O ANISOU 8 OD2 ASP A 29 24894 23572 17367 -3266 178 -2890 O ATOM 9 N GLU A 30 17.385 26.195 61.497 1.00149.17 N ANISOU 9 N GLU A 30 22654 19298 14726 -2869 469 -2401 N ATOM 10 CA GLU A 30 16.546 27.166 60.786 1.00148.48 C ANISOU 10 CA GLU A 30 22878 18830 14705 -2894 627 -2359 C ATOM 11 C GLU A 30 16.812 27.160 59.267 1.00150.97 C ANISOU 11 C GLU A 30 23210 19032 15118 -2932 681 -2308 C ATOM 12 O GLU A 30 15.854 27.178 58.490 1.00149.23 O ANISOU 12 O GLU A 30 23145 18554 15003 -2767 730 -2162 O ATOM 13 CB GLU A 30 16.768 28.577 61.371 1.00152.10 C ANISOU 13 CB GLU A 30 23558 19185 15049 -3165 770 -2547 C ATOM 14 CG GLU A 30 15.928 29.680 60.748 1.00162.38 C ANISOU 14 CG GLU A 30 25220 20085 16391 -3185 949 -2515 C ATOM 15 CD GLU A 30 16.718 30.612 59.851 1.00181.79 C ANISOU 15 CD GLU A 30 27813 22434 18825 -3473 1098 -2642 C ATOM 16 OE1 GLU A 30 17.396 31.518 60.389 1.00177.22 O ANISOU 16 OE1 GLU A 30 27320 21890 18126 -3764 1193 -2843 O ATOM 17 OE2 GLU A 30 16.666 30.435 58.613 1.00173.55 O ANISOU 17 OE2 GLU A 30 26792 21273 17876 -3417 1127 -2547 O ATOM 18 N VAL A 31 18.097 27.114 58.854 1.00147.83 N ANISOU 18 N VAL A 31 22644 18844 14682 -3140 669 -2432 N ATOM 19 CA VAL A 31 18.505 27.117 57.445 1.00146.86 C ANISOU 19 CA VAL A 31 22519 18643 14636 -3205 722 -2404 C ATOM 20 C VAL A 31 18.064 25.806 56.744 1.00147.48 C ANISOU 20 C VAL A 31 22440 18752 14843 -2911 601 -2198 C ATOM 21 O VAL A 31 17.734 25.842 55.558 1.00146.09 O ANISOU 21 O VAL A 31 22359 18383 14764 -2858 658 -2104 O ATOM 22 CB VAL A 31 20.026 27.411 57.278 1.00152.73 C ANISOU 22 CB VAL A 31 23106 19634 15292 -3520 744 -2609 C ATOM 23 CG1 VAL A 31 20.909 26.252 57.751 1.00152.52 C ANISOU 23 CG1 VAL A 31 22703 20028 15220 -3454 563 -2636 C ATOM 24 CG2 VAL A 31 20.366 27.824 55.848 1.00152.66 C ANISOU 24 CG2 VAL A 31 23193 19465 15345 -3650 859 -2611 C ATOM 25 N TRP A 32 18.014 24.681 57.487 1.00142.64 N ANISOU 25 N TRP A 32 21610 18365 14223 -2718 445 -2130 N ATOM 26 CA TRP A 32 17.609 23.375 56.966 1.00140.18 C ANISOU 26 CA TRP A 32 21154 18091 14017 -2447 335 -1945 C ATOM 27 C TRP A 32 16.101 23.305 56.709 1.00141.52 C ANISOU 27 C TRP A 32 21512 17971 14288 -2223 370 -1773 C ATOM 28 O TRP A 32 15.680 22.536 55.849 1.00139.34 O ANISOU 28 O TRP A 32 21188 17637 14120 -2053 335 -1631 O ATOM 29 CB TRP A 32 18.024 22.256 57.929 1.00138.92 C ANISOU 29 CB TRP A 32 20742 18246 13794 -2316 178 -1933 C ATOM 30 N VAL A 33 15.296 24.092 57.455 1.00138.09 N ANISOU 30 N VAL A 33 21281 17372 13815 -2221 440 -1793 N ATOM 31 CA VAL A 33 13.831 24.137 57.329 1.00136.37 C ANISOU 31 CA VAL A 33 21239 16902 13672 -2011 480 -1652 C ATOM 32 C VAL A 33 13.443 25.005 56.119 1.00139.14 C ANISOU 32 C VAL A 33 21814 16972 14082 -2052 613 -1627 C ATOM 33 O VAL A 33 12.603 24.587 55.317 1.00137.41 O ANISOU 33 O VAL A 33 21626 16624 13962 -1861 609 -1485 O ATOM 34 CB VAL A 33 13.145 24.625 58.639 1.00141.03 C ANISOU 34 CB VAL A 33 21954 17445 14187 -1981 502 -1686 C ATOM 35 CG1 VAL A 33 11.637 24.803 58.457 1.00139.73 C ANISOU 35 CG1 VAL A 33 21975 17026 14089 -1775 558 -1558 C ATOM 36 CG2 VAL A 33 13.429 23.673 59.797 1.00140.87 C ANISOU 36 CG2 VAL A 33 21724 17693 14106 -1902 368 -1687 C ATOM 37 N VAL A 34 14.050 26.206 56.002 1.00136.32 N ANISOU 37 N VAL A 34 21617 16525 13653 -2301 735 -1771 N ATOM 38 CA VAL A 34 13.808 27.160 54.913 1.00136.01 C ANISOU 38 CA VAL A 34 21828 16208 13641 -2363 883 -1765 C ATOM 39 C VAL A 34 14.195 26.509 53.572 1.00137.87 C ANISOU 39 C VAL A 34 21940 16474 13969 -2327 850 -1688 C ATOM 40 O VAL A 34 13.392 26.526 52.638 1.00136.71 O ANISOU 40 O VAL A 34 21912 16133 13899 -2170 890 -1566 O ATOM 41 CB VAL A 34 14.550 28.503 55.155 1.00142.28 C ANISOU 41 CB VAL A 34 22814 16923 14323 -2673 1029 -1954 C ATOM 42 CG1 VAL A 34 14.426 29.438 53.954 1.00142.72 C ANISOU 42 CG1 VAL A 34 23141 16690 14395 -2744 1192 -1946 C ATOM 43 CG2 VAL A 34 14.039 29.191 56.419 1.00143.07 C ANISOU 43 CG2 VAL A 34 23069 16958 14333 -2691 1074 -2021 C ATOM 44 N GLY A 35 15.387 25.906 53.526 1.00133.58 N ANISOU 44 N GLY A 35 21150 16192 13412 -2455 771 -1758 N ATOM 45 CA GLY A 35 15.921 25.214 52.357 1.00131.87 C ANISOU 45 CA GLY A 35 20783 16050 13273 -2437 730 -1702 C ATOM 46 C GLY A 35 15.072 24.048 51.890 1.00132.00 C ANISOU 46 C GLY A 35 20693 16058 13401 -2142 629 -1513 C ATOM 47 O GLY A 35 14.867 23.886 50.686 1.00130.85 O ANISOU 47 O GLY A 35 20580 15801 13336 -2074 655 -1428 O ATOM 48 N MET A 36 14.554 23.242 52.843 1.00126.55 N ANISOU 48 N MET A 36 19887 15483 12712 -1971 523 -1450 N ATOM 49 CA MET A 36 13.701 22.077 52.571 1.00123.80 C ANISOU 49 CA MET A 36 19440 15138 12459 -1704 434 -1283 C ATOM 50 C MET A 36 12.346 22.495 52.005 1.00124.16 C ANISOU 50 C MET A 36 19694 14915 12567 -1551 510 -1179 C ATOM 51 O MET A 36 11.815 21.801 51.140 1.00122.34 O ANISOU 51 O MET A 36 19414 14643 12428 -1394 480 -1060 O ATOM 52 CB MET A 36 13.494 21.239 53.843 1.00126.04 C ANISOU 52 CB MET A 36 19588 15596 12707 -1586 327 -1258 C ATOM 53 CG MET A 36 13.732 19.759 53.645 1.00128.90 C ANISOU 53 CG MET A 36 19720 16136 13120 -1439 207 -1164 C ATOM 54 SD MET A 36 15.465 19.351 53.315 1.00134.45 S ANISOU 54 SD MET A 36 20195 17112 13778 -1592 144 -1261 S ATOM 55 CE MET A 36 15.463 17.620 53.697 1.00130.17 C ANISOU 55 CE MET A 36 19437 16769 13254 -1358 3 -1143 C ATOM 56 N GLY A 37 11.815 23.616 52.499 1.00119.57 N ANISOU 56 N GLY A 37 19339 14166 11928 -1594 608 -1230 N ATOM 57 CA GLY A 37 10.538 24.175 52.071 1.00118.09 C ANISOU 57 CA GLY A 37 19365 13732 11770 -1440 688 -1149 C ATOM 58 C GLY A 37 10.529 24.602 50.617 1.00119.66 C ANISOU 58 C GLY A 37 19684 13767 12014 -1443 767 -1111 C ATOM 59 O GLY A 37 9.561 24.333 49.900 1.00118.25 O ANISOU 59 O GLY A 37 19542 13489 11900 -1244 767 -995 O ATOM 60 N ILE A 38 11.626 25.252 50.174 1.00115.43 N ANISOU 60 N ILE A 38 19203 13217 11438 -1675 838 -1214 N ATOM 61 CA ILE A 38 11.830 25.747 48.807 1.00114.42 C ANISOU 61 CA ILE A 38 19205 12935 11335 -1722 930 -1197 C ATOM 62 C ILE A 38 11.892 24.564 47.828 1.00115.14 C ANISOU 62 C ILE A 38 19085 13133 11529 -1600 833 -1090 C ATOM 63 O ILE A 38 11.221 24.600 46.793 1.00114.15 O ANISOU 63 O ILE A 38 19053 12865 11454 -1460 866 -995 O ATOM 64 CB ILE A 38 13.108 26.642 48.730 1.00119.10 C ANISOU 64 CB ILE A 38 19881 13522 11849 -2039 1032 -1356 C ATOM 65 CG1 ILE A 38 12.935 27.938 49.560 1.00120.99 C ANISOU 65 CG1 ILE A 38 20387 13602 11981 -2162 1159 -1461 C ATOM 66 CG2 ILE A 38 13.498 26.967 47.274 1.00119.92 C ANISOU 66 CG2 ILE A 38 20082 13501 11981 -2105 1118 -1338 C ATOM 67 CD1 ILE A 38 14.232 28.553 50.110 1.00128.49 C ANISOU 67 CD1 ILE A 38 21329 14655 12835 -2500 1218 -1655 C ATOM 68 N VAL A 39 12.690 23.524 48.166 1.00109.88 N ANISOU 68 N VAL A 39 18143 12721 10885 -1643 714 -1108 N ATOM 69 CA VAL A 39 12.895 22.318 47.354 1.00107.77 C ANISOU 69 CA VAL A 39 17665 12577 10707 -1543 619 -1020 C ATOM 70 C VAL A 39 11.551 21.585 47.172 1.00109.20 C ANISOU 70 C VAL A 39 17829 12700 10963 -1271 567 -874 C ATOM 71 O VAL A 39 11.166 21.320 46.032 1.00107.77 O ANISOU 71 O VAL A 39 17659 12443 10847 -1170 575 -791 O ATOM 72 CB VAL A 39 14.005 21.401 47.948 1.00111.57 C ANISOU 72 CB VAL A 39 17874 13347 11170 -1624 507 -1075 C ATOM 73 CG1 VAL A 39 14.064 20.048 47.240 1.00109.80 C ANISOU 73 CG1 VAL A 39 17447 13238 11034 -1480 408 -969 C ATOM 74 CG2 VAL A 39 15.370 22.084 47.890 1.00113.04 C ANISOU 74 CG2 VAL A 39 18046 13619 11284 -1902 562 -1228 C ATOM 75 N MET A 40 10.824 21.328 48.283 1.00104.77 N ANISOU 75 N MET A 40 17250 12175 10382 -1165 524 -854 N ATOM 76 CA MET A 40 9.521 20.652 48.305 1.00102.72 C ANISOU 76 CA MET A 40 16966 11883 10179 -931 483 -738 C ATOM 77 C MET A 40 8.456 21.415 47.501 1.00105.65 C ANISOU 77 C MET A 40 17539 12039 10563 -812 571 -686 C ATOM 78 O MET A 40 7.632 20.774 46.849 1.00103.83 O ANISOU 78 O MET A 40 17255 11799 10398 -642 541 -591 O ATOM 79 CB MET A 40 9.043 20.434 49.747 1.00105.00 C ANISOU 79 CB MET A 40 17226 12244 10425 -877 443 -750 C ATOM 80 CG MET A 40 9.742 19.283 50.434 1.00108.23 C ANISOU 80 CG MET A 40 17413 12879 10832 -891 334 -752 C ATOM 81 SD MET A 40 9.096 18.946 52.085 1.00112.51 S ANISOU 81 SD MET A 40 17934 13497 11319 -806 291 -750 S ATOM 82 CE MET A 40 10.198 17.657 52.591 1.00109.10 C ANISOU 82 CE MET A 40 17261 13324 10868 -824 174 -752 C ATOM 83 N SER A 41 8.494 22.767 47.522 1.00103.14 N ANISOU 83 N SER A 41 17457 11555 10175 -900 684 -752 N ATOM 84 CA SER A 41 7.561 23.624 46.781 1.00103.11 C ANISOU 84 CA SER A 41 17681 11339 10158 -775 779 -707 C ATOM 85 C SER A 41 7.757 23.496 45.265 1.00106.30 C ANISOU 85 C SER A 41 18090 11689 10612 -750 798 -653 C ATOM 86 O SER A 41 6.768 23.468 44.530 1.00105.68 O ANISOU 86 O SER A 41 18065 11531 10557 -556 810 -570 O ATOM 87 CB SER A 41 7.714 25.082 47.201 1.00108.37 C ANISOU 87 CB SER A 41 18621 11832 10724 -892 908 -796 C ATOM 88 OG SER A 41 7.360 25.262 48.562 1.00117.23 O ANISOU 88 OG SER A 41 19760 12986 11795 -889 897 -840 O ATOM 89 N LEU A 42 9.027 23.406 44.804 1.00102.28 N ANISOU 89 N LEU A 42 17512 11238 10112 -942 799 -706 N ATOM 90 CA LEU A 42 9.378 23.262 43.387 1.00101.11 C ANISOU 90 CA LEU A 42 17359 11051 10008 -946 818 -664 C ATOM 91 C LEU A 42 8.970 21.884 42.853 1.00102.29 C ANISOU 91 C LEU A 42 17278 11333 10253 -786 704 -564 C ATOM 92 O LEU A 42 8.568 21.790 41.692 1.00101.33 O ANISOU 92 O LEU A 42 17189 11144 10167 -678 720 -496 O ATOM 93 CB LEU A 42 10.882 23.498 43.153 1.00101.94 C ANISOU 93 CB LEU A 42 17431 11210 10091 -1209 851 -762 C ATOM 94 CG LEU A 42 11.414 24.923 43.354 1.00108.46 C ANISOU 94 CG LEU A 42 18510 11881 10819 -1412 996 -873 C ATOM 95 CD1 LEU A 42 12.925 24.932 43.352 1.00109.46 C ANISOU 95 CD1 LEU A 42 18529 12138 10923 -1689 1006 -990 C ATOM 96 CD2 LEU A 42 10.889 25.883 42.286 1.00111.48 C ANISOU 96 CD2 LEU A 42 19182 12005 11171 -1341 1128 -829 C ATOM 97 N ILE A 43 9.059 20.825 43.702 1.00 97.36 N ANISOU 97 N ILE A 43 16436 10892 9662 -768 597 -558 N ATOM 98 CA ILE A 43 8.672 19.444 43.370 1.00 95.21 C ANISOU 98 CA ILE A 43 15959 10745 9473 -630 498 -471 C ATOM 99 C ILE A 43 7.158 19.418 43.088 1.00 97.93 C ANISOU 99 C ILE A 43 16366 11006 9836 -412 509 -393 C ATOM 100 O ILE A 43 6.747 18.829 42.088 1.00 96.77 O ANISOU 100 O ILE A 43 16154 10869 9745 -306 486 -326 O ATOM 101 CB ILE A 43 9.095 18.418 44.475 1.00 97.74 C ANISOU 101 CB ILE A 43 16080 11257 9800 -655 401 -484 C ATOM 102 CG1 ILE A 43 10.629 18.407 44.680 1.00 98.81 C ANISOU 102 CG1 ILE A 43 16124 11516 9904 -852 381 -569 C ATOM 103 CG2 ILE A 43 8.596 16.997 44.155 1.00 96.81 C ANISOU 103 CG2 ILE A 43 15788 11236 9759 -510 321 -393 C ATOM 104 CD1 ILE A 43 11.109 17.937 46.078 1.00105.21 C ANISOU 104 CD1 ILE A 43 16812 12496 10667 -897 312 -617 C ATOM 105 N VAL A 44 6.348 20.105 43.936 1.00 94.47 N ANISOU 105 N VAL A 44 16056 10496 9343 -349 549 -410 N ATOM 106 CA VAL A 44 4.885 20.213 43.801 1.00 93.81 C ANISOU 106 CA VAL A 44 16033 10354 9256 -138 565 -354 C ATOM 107 C VAL A 44 4.535 20.881 42.460 1.00 97.72 C ANISOU 107 C VAL A 44 16674 10716 9741 -50 631 -318 C ATOM 108 O VAL A 44 3.736 20.327 41.703 1.00 96.97 O ANISOU 108 O VAL A 44 16503 10658 9684 106 601 -256 O ATOM 109 CB VAL A 44 4.223 20.958 45.000 1.00 98.60 C ANISOU 109 CB VAL A 44 16766 10906 9792 -100 606 -391 C ATOM 110 CG1 VAL A 44 2.742 21.240 44.744 1.00 98.44 C ANISOU 110 CG1 VAL A 44 16822 10829 9752 126 636 -343 C ATOM 111 CG2 VAL A 44 4.392 20.182 46.301 1.00 98.03 C ANISOU 111 CG2 VAL A 44 16544 10977 9727 -151 536 -413 C ATOM 112 N LEU A 45 5.159 22.041 42.161 1.00 94.83 N ANISOU 112 N LEU A 45 16516 10200 9314 -155 725 -363 N ATOM 113 CA LEU A 45 4.934 22.813 40.933 1.00 95.01 C ANISOU 113 CA LEU A 45 16725 10070 9305 -77 806 -332 C ATOM 114 C LEU A 45 5.284 22.010 39.667 1.00 97.17 C ANISOU 114 C LEU A 45 16861 10409 9649 -68 759 -281 C ATOM 115 O LEU A 45 4.538 22.082 38.690 1.00 96.55 O ANISOU 115 O LEU A 45 16833 10285 9566 101 773 -222 O ATOM 116 CB LEU A 45 5.726 24.135 40.961 1.00 96.73 C ANISOU 116 CB LEU A 45 17201 10110 9440 -241 929 -401 C ATOM 117 CG LEU A 45 5.368 25.141 42.073 1.00102.78 C ANISOU 117 CG LEU A 45 18164 10768 10119 -249 1003 -457 C ATOM 118 CD1 LEU A 45 6.449 26.194 42.223 1.00104.58 C ANISOU 118 CD1 LEU A 45 18595 10862 10278 -490 1118 -551 C ATOM 119 CD2 LEU A 45 4.003 25.790 41.844 1.00105.49 C ANISOU 119 CD2 LEU A 45 18690 10991 10402 13 1058 -401 C ATOM 120 N ALA A 46 6.385 21.227 39.702 1.00 92.70 N ANISOU 120 N ALA A 46 16118 9963 9142 -235 701 -306 N ATOM 121 CA ALA A 46 6.848 20.390 38.587 1.00 91.41 C ANISOU 121 CA ALA A 46 15811 9872 9047 -245 655 -265 C ATOM 122 C ALA A 46 5.872 19.243 38.281 1.00 92.70 C ANISOU 122 C ALA A 46 15798 10150 9276 -63 570 -193 C ATOM 123 O ALA A 46 5.696 18.880 37.114 1.00 91.42 O ANISOU 123 O ALA A 46 15597 9992 9145 12 559 -145 O ATOM 124 CB ALA A 46 8.226 19.825 38.896 1.00 92.01 C ANISOU 124 CB ALA A 46 15734 10071 9156 -450 611 -317 C ATOM 125 N ILE A 47 5.243 18.682 39.328 1.00 88.22 N ANISOU 125 N ILE A 47 15126 9674 8719 -5 517 -191 N ATOM 126 CA ILE A 47 4.289 17.578 39.210 1.00 86.72 C ANISOU 126 CA ILE A 47 14771 9596 8582 138 450 -140 C ATOM 127 C ILE A 47 2.928 18.102 38.702 1.00 90.33 C ANISOU 127 C ILE A 47 15324 9998 9000 340 486 -109 C ATOM 128 O ILE A 47 2.326 17.469 37.833 1.00 88.88 O ANISOU 128 O ILE A 47 15044 9877 8850 449 456 -69 O ATOM 129 CB ILE A 47 4.154 16.801 40.559 1.00 89.24 C ANISOU 129 CB ILE A 47 14960 10028 8917 114 396 -154 C ATOM 130 CG1 ILE A 47 5.485 16.110 40.948 1.00 89.28 C ANISOU 130 CG1 ILE A 47 14845 10125 8953 -47 347 -176 C ATOM 131 CG2 ILE A 47 3.027 15.772 40.495 1.00 89.01 C ANISOU 131 CG2 ILE A 47 14794 10098 8929 250 354 -112 C ATOM 132 CD1 ILE A 47 5.583 15.603 42.409 1.00 96.67 C ANISOU 132 CD1 ILE A 47 15704 11154 9874 -84 305 -199 C ATOM 133 N VAL A 48 2.453 19.245 39.243 1.00 88.07 N ANISOU 133 N VAL A 48 15224 9604 8634 395 551 -132 N ATOM 134 CA VAL A 48 1.160 19.846 38.892 1.00 88.31 C ANISOU 134 CA VAL A 48 15357 9591 8604 612 588 -109 C ATOM 135 C VAL A 48 1.199 20.380 37.443 1.00 93.47 C ANISOU 135 C VAL A 48 16131 10153 9228 691 632 -74 C ATOM 136 O VAL A 48 0.443 19.874 36.616 1.00 92.53 O ANISOU 136 O VAL A 48 15916 10118 9123 838 597 -37 O ATOM 137 CB VAL A 48 0.702 20.925 39.918 1.00 92.72 C ANISOU 137 CB VAL A 48 16098 10053 9077 656 651 -143 C ATOM 138 CG1 VAL A 48 -0.535 21.674 39.432 1.00 93.40 C ANISOU 138 CG1 VAL A 48 16317 10089 9083 902 698 -118 C ATOM 139 CG2 VAL A 48 0.428 20.299 41.281 1.00 91.87 C ANISOU 139 CG2 VAL A 48 15856 10057 8993 616 603 -170 C ATOM 140 N PHE A 49 2.085 21.356 37.133 1.00 91.54 N ANISOU 140 N PHE A 49 16093 9748 8940 586 711 -91 N ATOM 141 CA PHE A 49 2.195 21.950 35.792 1.00 92.17 C ANISOU 141 CA PHE A 49 16326 9717 8979 653 770 -56 C ATOM 142 C PHE A 49 2.607 20.938 34.720 1.00 94.85 C ANISOU 142 C PHE A 49 16483 10157 9398 621 707 -23 C ATOM 143 O PHE A 49 2.174 21.067 33.574 1.00 95.01 O ANISOU 143 O PHE A 49 16552 10157 9390 761 720 20 O ATOM 144 CB PHE A 49 3.173 23.139 35.773 1.00 95.38 C ANISOU 144 CB PHE A 49 16993 9923 9321 501 883 -93 C ATOM 145 CG PHE A 49 2.679 24.424 36.406 1.00 98.72 C ANISOU 145 CG PHE A 49 17689 10184 9635 576 983 -115 C ATOM 146 CD1 PHE A 49 1.337 24.789 36.331 1.00102.47 C ANISOU 146 CD1 PHE A 49 18242 10650 10042 850 993 -76 C ATOM 147 CD2 PHE A 49 3.567 25.302 37.018 1.00101.99 C ANISOU 147 CD2 PHE A 49 18290 10457 10004 375 1074 -180 C ATOM 148 CE1 PHE A 49 0.886 25.984 36.899 1.00104.83 C ANISOU 148 CE1 PHE A 49 18807 10791 10230 937 1092 -94 C ATOM 149 CE2 PHE A 49 3.116 26.501 37.580 1.00106.27 C ANISOU 149 CE2 PHE A 49 19107 10831 10438 442 1179 -202 C ATOM 150 CZ PHE A 49 1.779 26.834 37.516 1.00104.87 C ANISOU 150 CZ PHE A 49 19014 10635 10196 731 1187 -154 C ATOM 151 N GLY A 50 3.426 19.958 35.100 1.00 89.62 N ANISOU 151 N GLY A 50 15623 9605 8823 450 641 -43 N ATOM 152 CA GLY A 50 3.907 18.911 34.206 1.00 88.04 C ANISOU 152 CA GLY A 50 15246 9504 8703 405 582 -17 C ATOM 153 C GLY A 50 2.815 17.986 33.709 1.00 90.47 C ANISOU 153 C GLY A 50 15389 9942 9044 576 516 22 C ATOM 154 O GLY A 50 2.690 17.771 32.500 1.00 90.01 O ANISOU 154 O GLY A 50 15311 9897 8992 648 510 55 O ATOM 155 N ASN A 51 2.009 17.441 34.639 1.00 86.00 N ANISOU 155 N ASN A 51 14705 9478 8492 633 472 11 N ATOM 156 CA ASN A 51 0.925 16.515 34.315 1.00 84.89 C ANISOU 156 CA ASN A 51 14394 9481 8378 766 419 29 C ATOM 157 C ASN A 51 -0.315 17.238 33.769 1.00 90.07 C ANISOU 157 C ASN A 51 15142 10129 8950 992 448 40 C ATOM 158 O ASN A 51 -1.126 16.599 33.097 1.00 89.03 O ANISOU 158 O ASN A 51 14880 10122 8826 1106 411 49 O ATOM 159 CB ASN A 51 0.575 15.638 35.507 1.00 82.75 C ANISOU 159 CB ASN A 51 13972 9321 8149 725 375 7 C ATOM 160 CG ASN A 51 1.648 14.620 35.789 1.00 98.76 C ANISOU 160 CG ASN A 51 15872 11397 10255 555 332 7 C ATOM 161 OD1 ASN A 51 1.789 13.612 35.091 1.00 90.65 O ANISOU 161 OD1 ASN A 51 14712 10446 9286 539 295 26 O ATOM 162 ND2 ASN A 51 2.462 14.887 36.791 1.00 91.34 N ANISOU 162 ND2 ASN A 51 14977 10420 9310 431 337 -17 N ATOM 163 N VAL A 52 -0.449 18.561 34.021 1.00 88.52 N ANISOU 163 N VAL A 52 15175 9796 8664 1062 518 37 N ATOM 164 CA VAL A 52 -1.545 19.379 33.482 1.00 89.71 C ANISOU 164 CA VAL A 52 15448 9927 8711 1305 554 53 C ATOM 165 C VAL A 52 -1.315 19.515 31.963 1.00 94.99 C ANISOU 165 C VAL A 52 16174 10560 9359 1371 567 92 C ATOM 166 O VAL A 52 -2.256 19.365 31.180 1.00 94.95 O ANISOU 166 O VAL A 52 16108 10657 9310 1564 543 107 O ATOM 167 CB VAL A 52 -1.658 20.747 34.220 1.00 94.90 C ANISOU 167 CB VAL A 52 16362 10422 9272 1357 638 41 C ATOM 168 CG1 VAL A 52 -2.116 21.880 33.300 1.00 96.29 C ANISOU 168 CG1 VAL A 52 16776 10482 9327 1567 710 74 C ATOM 169 CG2 VAL A 52 -2.580 20.635 35.425 1.00 94.72 C ANISOU 169 CG2 VAL A 52 16264 10490 9234 1427 619 9 C ATOM 170 N LEU A 53 -0.045 19.726 31.564 1.00 92.11 N ANISOU 170 N LEU A 53 15904 10071 9024 1201 601 102 N ATOM 171 CA LEU A 53 0.401 19.872 30.182 1.00 92.31 C ANISOU 171 CA LEU A 53 15999 10040 9033 1220 625 138 C ATOM 172 C LEU A 53 0.188 18.583 29.369 1.00 95.50 C ANISOU 172 C LEU A 53 16153 10621 9511 1237 539 150 C ATOM 173 O LEU A 53 -0.161 18.676 28.192 1.00 96.04 O ANISOU 173 O LEU A 53 16249 10706 9535 1373 542 179 O ATOM 174 CB LEU A 53 1.885 20.273 30.171 1.00 92.48 C ANISOU 174 CB LEU A 53 16143 9913 9080 987 682 126 C ATOM 175 CG LEU A 53 2.457 20.846 28.874 1.00 98.11 C ANISOU 175 CG LEU A 53 17026 10502 9748 989 749 159 C ATOM 176 CD1 LEU A 53 1.918 22.245 28.594 1.00100.08 C ANISOU 176 CD1 LEU A 53 17590 10579 9858 1164 853 183 C ATOM 177 CD2 LEU A 53 3.964 20.903 28.945 1.00101.10 C ANISOU 177 CD2 LEU A 53 17436 10800 10176 716 789 128 C ATOM 178 N VAL A 54 0.384 17.396 29.995 1.00 90.33 N ANISOU 178 N VAL A 54 15269 10092 8958 1106 471 126 N ATOM 179 CA VAL A 54 0.231 16.074 29.361 1.00 88.90 C ANISOU 179 CA VAL A 54 14857 10069 8852 1093 400 128 C ATOM 180 C VAL A 54 -1.257 15.827 29.009 1.00 93.03 C ANISOU 180 C VAL A 54 15280 10741 9325 1303 369 119 C ATOM 181 O VAL A 54 -1.566 15.579 27.840 1.00 92.60 O ANISOU 181 O VAL A 54 15179 10753 9252 1397 352 132 O ATOM 182 CB VAL A 54 0.828 14.932 30.245 1.00 91.33 C ANISOU 182 CB VAL A 54 14988 10449 9264 909 353 107 C ATOM 183 CG1 VAL A 54 0.513 13.549 29.682 1.00 89.99 C ANISOU 183 CG1 VAL A 54 14601 10430 9159 906 295 105 C ATOM 184 CG2 VAL A 54 2.334 15.098 30.419 1.00 90.99 C ANISOU 184 CG2 VAL A 54 15009 10305 9260 715 374 107 C ATOM 185 N ILE A 55 -2.158 15.916 30.016 1.00 89.89 N ANISOU 185 N ILE A 55 14846 10407 8899 1374 365 89 N ATOM 186 CA ILE A 55 -3.612 15.721 29.906 1.00 90.14 C ANISOU 186 CA ILE A 55 14765 10610 8875 1563 340 60 C ATOM 187 C ILE A 55 -4.208 16.680 28.840 1.00 95.55 C ANISOU 187 C ILE A 55 15586 11281 9439 1799 365 84 C ATOM 188 O ILE A 55 -4.994 16.226 28.007 1.00 95.09 O ANISOU 188 O ILE A 55 15395 11386 9350 1924 328 68 O ATOM 189 CB ILE A 55 -4.303 15.879 31.307 1.00 93.38 C ANISOU 189 CB ILE A 55 15156 11058 9266 1583 348 24 C ATOM 190 CG1 ILE A 55 -3.868 14.747 32.279 1.00 92.37 C ANISOU 190 CG1 ILE A 55 14874 10975 9246 1376 319 2 C ATOM 191 CG2 ILE A 55 -5.840 15.939 31.194 1.00 95.03 C ANISOU 191 CG2 ILE A 55 15271 11446 9391 1801 335 -14 C ATOM 192 CD1 ILE A 55 -4.049 15.031 33.800 1.00 97.80 C ANISOU 192 CD1 ILE A 55 15601 11635 9926 1337 339 -21 C ATOM 193 N THR A 56 -3.806 17.978 28.853 1.00 93.65 N ANISOU 193 N THR A 56 15613 10845 9123 1856 433 118 N ATOM 194 CA THR A 56 -4.279 19.011 27.915 1.00 95.18 C ANISOU 194 CA THR A 56 15994 10985 9183 2095 475 152 C ATOM 195 C THR A 56 -3.873 18.670 26.464 1.00 99.18 C ANISOU 195 C THR A 56 16479 11509 9697 2102 458 183 C ATOM 196 O THR A 56 -4.693 18.835 25.556 1.00 99.67 O ANISOU 196 O THR A 56 16531 11674 9664 2326 443 191 O ATOM 197 CB THR A 56 -3.774 20.407 28.340 1.00104.60 C ANISOU 197 CB THR A 56 17510 11929 10302 2107 572 180 C ATOM 198 OG1 THR A 56 -4.141 20.642 29.700 1.00104.68 O ANISOU 198 OG1 THR A 56 17526 11936 10311 2090 583 146 O ATOM 199 CG2 THR A 56 -4.339 21.533 27.476 1.00104.54 C ANISOU 199 CG2 THR A 56 17737 11847 10136 2383 630 221 C ATOM 200 N ALA A 57 -2.631 18.178 26.260 1.00 94.95 N ANISOU 200 N ALA A 57 15923 10888 9264 1868 459 196 N ATOM 201 CA ALA A 57 -2.103 17.798 24.948 1.00 94.65 C ANISOU 201 CA ALA A 57 15862 10856 9246 1843 447 223 C ATOM 202 C ALA A 57 -2.918 16.667 24.310 1.00 98.82 C ANISOU 202 C ALA A 57 16126 11624 9796 1915 366 194 C ATOM 203 O ALA A 57 -3.205 16.740 23.119 1.00 99.14 O ANISOU 203 O ALA A 57 16179 11718 9774 2052 357 212 O ATOM 204 CB ALA A 57 -0.644 17.387 25.064 1.00 94.33 C ANISOU 204 CB ALA A 57 15815 10709 9317 1568 458 229 C ATOM 205 N ILE A 58 -3.317 15.649 25.101 1.00 94.94 N ANISOU 205 N ILE A 58 15409 11280 9385 1824 314 145 N ATOM 206 CA ILE A 58 -4.107 14.506 24.622 1.00 94.47 C ANISOU 206 CA ILE A 58 15096 11450 9349 1853 251 99 C ATOM 207 C ILE A 58 -5.561 14.957 24.334 1.00100.15 C ANISOU 207 C ILE A 58 15780 12336 9937 2122 237 68 C ATOM 208 O ILE A 58 -6.096 14.628 23.276 1.00100.21 O ANISOU 208 O ILE A 58 15687 12492 9895 2234 203 50 O ATOM 209 CB ILE A 58 -4.026 13.305 25.625 1.00 96.27 C ANISOU 209 CB ILE A 58 15128 11755 9693 1656 222 56 C ATOM 210 CG1 ILE A 58 -2.614 12.664 25.606 1.00 95.46 C ANISOU 210 CG1 ILE A 58 15023 11540 9707 1426 222 84 C ATOM 211 CG2 ILE A 58 -5.100 12.235 25.349 1.00 96.78 C ANISOU 211 CG2 ILE A 58 14948 12063 9760 1690 178 -11 C ATOM 212 CD1 ILE A 58 -2.125 12.093 26.945 1.00101.11 C ANISOU 212 CD1 ILE A 58 15685 12223 10509 1248 221 71 C ATOM 213 N ALA A 59 -6.167 15.735 25.251 1.00 97.78 N ANISOU 213 N ALA A 59 15565 12016 9570 2233 262 59 N ATOM 214 CA ALA A 59 -7.551 16.219 25.171 1.00 99.11 C ANISOU 214 CA ALA A 59 15698 12354 9605 2502 251 24 C ATOM 215 C ALA A 59 -7.829 17.151 23.979 1.00105.08 C ANISOU 215 C ALA A 59 16615 13094 10216 2764 267 66 C ATOM 216 O ALA A 59 -8.978 17.212 23.532 1.00106.07 O ANISOU 216 O ALA A 59 16637 13435 10230 2993 234 26 O ATOM 217 CB ALA A 59 -7.921 16.934 26.460 1.00100.32 C ANISOU 217 CB ALA A 59 15949 12445 9724 2550 288 15 C ATOM 218 N LYS A 60 -6.807 17.881 23.478 1.00101.89 N ANISOU 218 N LYS A 60 16463 12448 9802 2736 321 141 N ATOM 219 CA LYS A 60 -6.974 18.844 22.379 1.00103.10 C ANISOU 219 CA LYS A 60 16822 12543 9808 2983 354 193 C ATOM 220 C LYS A 60 -6.462 18.330 21.016 1.00106.69 C ANISOU 220 C LYS A 60 17232 13022 10282 2944 330 216 C ATOM 221 O LYS A 60 -7.129 18.554 20.003 1.00107.32 O ANISOU 221 O LYS A 60 17314 13225 10237 3183 310 222 O ATOM 222 CB LYS A 60 -6.286 20.182 22.718 1.00106.05 C ANISOU 222 CB LYS A 60 17558 12612 10126 3002 457 259 C ATOM 223 CG LYS A 60 -7.018 21.021 23.767 1.00119.24 C ANISOU 223 CG LYS A 60 19339 14254 11711 3152 494 247 C ATOM 224 CD LYS A 60 -8.111 21.907 23.161 1.00129.56 C ANISOU 224 CD LYS A 60 20771 15639 12816 3542 509 266 C ATOM 225 CE LYS A 60 -9.072 22.436 24.199 1.00138.85 C ANISOU 225 CE LYS A 60 21963 16879 13915 3709 521 233 C ATOM 226 NZ LYS A 60 -10.012 21.386 24.680 1.00145.18 N ANISOU 226 NZ LYS A 60 22396 17997 14769 3692 428 144 N ATOM 227 N PHE A 61 -5.282 17.679 20.983 1.00101.75 N ANISOU 227 N PHE A 61 16573 12288 9800 2662 333 229 N ATOM 228 CA PHE A 61 -4.677 17.171 19.749 1.00101.10 C ANISOU 228 CA PHE A 61 16456 12212 9747 2600 317 250 C ATOM 229 C PHE A 61 -5.305 15.838 19.356 1.00104.22 C ANISOU 229 C PHE A 61 16527 12878 10192 2569 230 182 C ATOM 230 O PHE A 61 -5.342 14.903 20.157 1.00102.77 O ANISOU 230 O PHE A 61 16150 12778 10121 2394 198 131 O ATOM 231 CB PHE A 61 -3.148 17.051 19.889 1.00101.95 C ANISOU 231 CB PHE A 61 16657 12103 9976 2320 361 285 C ATOM 232 CG PHE A 61 -2.386 18.357 19.795 1.00104.74 C ANISOU 232 CG PHE A 61 17348 12186 10262 2333 463 347 C ATOM 233 CD1 PHE A 61 -2.565 19.361 20.743 1.00108.74 C ANISOU 233 CD1 PHE A 61 18045 12562 10710 2389 523 355 C ATOM 234 CD2 PHE A 61 -1.450 18.562 18.789 1.00107.43 C ANISOU 234 CD2 PHE A 61 17823 12397 10599 2266 509 392 C ATOM 235 CE1 PHE A 61 -1.859 20.564 20.656 1.00110.82 C ANISOU 235 CE1 PHE A 61 18639 12563 10904 2381 634 403 C ATOM 236 CE2 PHE A 61 -0.736 19.764 18.710 1.00111.42 C ANISOU 236 CE2 PHE A 61 18653 12645 11037 2252 621 439 C ATOM 237 CZ PHE A 61 -0.949 20.758 19.641 1.00110.32 C ANISOU 237 CZ PHE A 61 18711 12372 10834 2306 686 443 C ATOM 238 N GLU A 62 -5.820 15.776 18.119 1.00101.59 N ANISOU 238 N GLU A 62 16150 12684 9765 2744 200 179 N ATOM 239 CA GLU A 62 -6.518 14.632 17.518 1.00101.10 C ANISOU 239 CA GLU A 62 15799 12899 9715 2745 125 104 C ATOM 240 C GLU A 62 -5.626 13.400 17.393 1.00102.40 C ANISOU 240 C GLU A 62 15823 13042 10043 2455 108 88 C ATOM 241 O GLU A 62 -6.074 12.304 17.728 1.00101.28 O ANISOU 241 O GLU A 62 15442 13069 9970 2341 69 13 O ATOM 242 CB GLU A 62 -7.092 14.981 16.121 1.00104.02 C ANISOU 242 CB GLU A 62 16192 13399 9931 3003 102 111 C ATOM 243 CG GLU A 62 -7.050 16.453 15.719 1.00116.94 C ANISOU 243 CG GLU A 62 18145 14871 11414 3253 161 196 C ATOM 244 CD GLU A 62 -5.751 17.016 15.161 1.00135.54 C ANISOU 244 CD GLU A 62 20770 16936 13792 3161 234 288 C ATOM 245 OE1 GLU A 62 -4.687 16.366 15.285 1.00125.72 O ANISOU 245 OE1 GLU A 62 19485 15582 12701 2877 243 294 O ATOM 246 OE2 GLU A 62 -5.800 18.141 14.617 1.00130.97 O ANISOU 246 OE2 GLU A 62 20456 16238 13067 3380 289 353 O ATOM 247 N ARG A 63 -4.380 13.577 16.902 1.00 98.10 N ANISOU 247 N ARG A 63 15432 12291 9551 2338 146 155 N ATOM 248 CA ARG A 63 -3.411 12.497 16.681 1.00 96.60 C ANISOU 248 CA ARG A 63 15135 12066 9502 2087 136 151 C ATOM 249 C ARG A 63 -2.948 11.826 17.986 1.00 99.08 C ANISOU 249 C ARG A 63 15362 12330 9954 1859 138 129 C ATOM 250 O ARG A 63 -2.553 10.657 17.953 1.00 97.88 O ANISOU 250 O ARG A 63 15058 12226 9907 1685 116 101 O ATOM 251 CB ARG A 63 -2.193 12.991 15.877 1.00 97.81 C ANISOU 251 CB ARG A 63 15484 12018 9661 2033 184 225 C ATOM 252 CG ARG A 63 -1.364 14.090 16.541 1.00112.35 C ANISOU 252 CG ARG A 63 17577 13608 11501 1981 259 283 C ATOM 253 CD ARG A 63 -0.148 14.442 15.703 1.00126.92 C ANISOU 253 CD ARG A 63 19588 15279 13356 1892 314 338 C ATOM 254 NE ARG A 63 0.336 15.792 15.994 1.00138.44 N ANISOU 254 NE ARG A 63 21339 16515 14748 1917 404 388 N ATOM 255 CZ ARG A 63 -0.108 16.894 15.397 1.00155.15 C ANISOU 255 CZ ARG A 63 23678 18557 16713 2139 454 431 C ATOM 256 NH1 ARG A 63 -1.053 16.819 14.466 1.00143.28 N ANISOU 256 NH1 ARG A 63 22124 17211 15106 2371 411 430 N ATOM 257 NH2 ARG A 63 0.382 18.078 15.730 1.00143.58 N ANISOU 257 NH2 ARG A 63 22496 16866 15190 2133 552 470 N ATOM 258 N LEU A 64 -3.004 12.555 19.120 1.00 95.15 N ANISOU 258 N LEU A 64 14972 11735 9447 1870 167 142 N ATOM 259 CA LEU A 64 -2.601 12.041 20.432 1.00 93.51 C ANISOU 259 CA LEU A 64 14702 11480 9349 1678 170 125 C ATOM 260 C LEU A 64 -3.743 11.283 21.137 1.00 96.08 C ANISOU 260 C LEU A 64 14821 12003 9683 1691 134 50 C ATOM 261 O LEU A 64 -3.593 10.906 22.300 1.00 95.17 O ANISOU 261 O LEU A 64 14662 11859 9639 1562 140 34 O ATOM 262 CB LEU A 64 -2.096 13.187 21.330 1.00 93.91 C ANISOU 262 CB LEU A 64 14966 11336 9380 1669 223 166 C ATOM 263 CG LEU A 64 -0.745 13.809 20.987 1.00 98.49 C ANISOU 263 CG LEU A 64 15740 11703 9978 1565 276 222 C ATOM 264 CD1 LEU A 64 -0.512 15.036 21.819 1.00 99.46 C ANISOU 264 CD1 LEU A 64 16082 11656 10051 1580 337 244 C ATOM 265 CD2 LEU A 64 0.399 12.830 21.210 1.00 99.36 C ANISOU 265 CD2 LEU A 64 15745 11785 10222 1321 262 218 C ATOM 266 N GLN A 65 -4.870 11.050 20.439 1.00 92.29 N ANISOU 266 N GLN A 65 14211 11731 9122 1840 102 -3 N ATOM 267 CA GLN A 65 -6.017 10.342 21.001 1.00 91.87 C ANISOU 267 CA GLN A 65 13952 11890 9063 1844 78 -91 C ATOM 268 C GLN A 65 -5.998 8.877 20.546 1.00 94.57 C ANISOU 268 C GLN A 65 14095 12354 9484 1682 58 -148 C ATOM 269 O GLN A 65 -6.692 8.483 19.603 1.00 94.85 O ANISOU 269 O GLN A 65 14002 12576 9461 1757 31 -204 O ATOM 270 CB GLN A 65 -7.334 11.052 20.648 1.00 94.67 C ANISOU 270 CB GLN A 65 14278 12428 9265 2111 59 -131 C ATOM 271 CG GLN A 65 -7.544 12.323 21.465 1.00108.36 C ANISOU 271 CG GLN A 65 16191 14055 10927 2255 89 -92 C ATOM 272 CD GLN A 65 -8.831 13.041 21.161 1.00129.85 C ANISOU 272 CD GLN A 65 18891 16961 13485 2546 72 -128 C ATOM 273 OE1 GLN A 65 -9.920 12.457 21.166 1.00127.92 O ANISOU 273 OE1 GLN A 65 18424 16982 13200 2595 39 -222 O ATOM 274 NE2 GLN A 65 -8.741 14.346 20.950 1.00120.85 N ANISOU 274 NE2 GLN A 65 17991 15688 12239 2748 103 -59 N ATOM 275 N THR A 66 -5.146 8.086 21.215 1.00 89.43 N ANISOU 275 N THR A 66 13431 11590 8957 1464 76 -132 N ATOM 276 CA THR A 66 -4.961 6.659 20.962 1.00 88.24 C ANISOU 276 CA THR A 66 13134 11503 8890 1291 75 -175 C ATOM 277 C THR A 66 -5.244 5.869 22.243 1.00 91.59 C ANISOU 277 C THR A 66 13474 11950 9376 1152 99 -219 C ATOM 278 O THR A 66 -5.264 6.448 23.334 1.00 91.43 O ANISOU 278 O THR A 66 13527 11859 9354 1166 112 -197 O ATOM 279 CB THR A 66 -3.542 6.373 20.421 1.00 94.52 C ANISOU 279 CB THR A 66 14014 12133 9766 1176 81 -107 C ATOM 280 OG1 THR A 66 -2.562 6.752 21.386 1.00 92.05 O ANISOU 280 OG1 THR A 66 13827 11636 9513 1092 101 -46 O ATOM 281 CG2 THR A 66 -3.261 7.058 19.090 1.00 94.44 C ANISOU 281 CG2 THR A 66 14090 12101 9694 1298 68 -68 C ATOM 282 N VAL A 67 -5.457 4.547 22.102 1.00 87.58 N ANISOU 282 N VAL A 67 12828 11533 8917 1014 114 -280 N ATOM 283 CA VAL A 67 -5.718 3.597 23.191 1.00 87.04 C ANISOU 283 CA VAL A 67 12688 11481 8902 864 154 -325 C ATOM 284 C VAL A 67 -4.555 3.659 24.211 1.00 90.51 C ANISOU 284 C VAL A 67 13260 11710 9421 773 168 -241 C ATOM 285 O VAL A 67 -4.814 3.769 25.411 1.00 90.27 O ANISOU 285 O VAL A 67 13247 11659 9393 749 187 -246 O ATOM 286 CB VAL A 67 -5.954 2.157 22.639 1.00 90.76 C ANISOU 286 CB VAL A 67 13030 12048 9406 722 183 -399 C ATOM 287 CG1 VAL A 67 -6.213 1.156 23.759 1.00 90.31 C ANISOU 287 CG1 VAL A 67 12933 11985 9395 564 243 -441 C ATOM 288 CG2 VAL A 67 -7.106 2.131 21.636 1.00 91.73 C ANISOU 288 CG2 VAL A 67 13005 12408 9439 807 166 -497 C ATOM 289 N THR A 68 -3.291 3.662 23.723 1.00 86.51 N ANISOU 289 N THR A 68 12842 11062 8965 732 156 -169 N ATOM 290 CA THR A 68 -2.078 3.743 24.547 1.00 85.77 C ANISOU 290 CA THR A 68 12857 10796 8934 652 162 -97 C ATOM 291 C THR A 68 -2.014 5.095 25.286 1.00 90.51 C ANISOU 291 C THR A 68 13572 11323 9494 737 153 -61 C ATOM 292 O THR A 68 -1.634 5.123 26.460 1.00 90.00 O ANISOU 292 O THR A 68 13554 11185 9457 676 164 -41 O ATOM 293 CB THR A 68 -0.832 3.501 23.682 1.00 93.92 C ANISOU 293 CB THR A 68 13934 11736 10014 602 152 -45 C ATOM 294 OG1 THR A 68 -0.993 2.264 22.986 1.00 95.87 O ANISOU 294 OG1 THR A 68 14084 12053 10290 532 167 -84 O ATOM 295 CG2 THR A 68 0.460 3.458 24.497 1.00 91.51 C ANISOU 295 CG2 THR A 68 13710 11293 9766 515 155 15 C ATOM 296 N ASN A 69 -2.410 6.198 24.615 1.00 87.87 N ANISOU 296 N ASN A 69 13294 11008 9086 883 138 -54 N ATOM 297 CA ASN A 69 -2.410 7.530 25.226 1.00 88.09 C ANISOU 297 CA ASN A 69 13457 10952 9063 975 143 -24 C ATOM 298 C ASN A 69 -3.557 7.690 26.240 1.00 92.32 C ANISOU 298 C ASN A 69 13944 11580 9555 1032 152 -72 C ATOM 299 O ASN A 69 -3.473 8.569 27.101 1.00 92.15 O ANISOU 299 O ASN A 69 14030 11474 9508 1067 163 -50 O ATOM 300 CB ASN A 69 -2.459 8.630 24.171 1.00 89.63 C ANISOU 300 CB ASN A 69 13756 11120 9178 1126 138 4 C ATOM 301 CG ASN A 69 -1.152 8.863 23.443 1.00111.63 C ANISOU 301 CG ASN A 69 16648 13768 11998 1063 145 62 C ATOM 302 OD1 ASN A 69 -0.061 8.835 24.025 1.00103.51 O ANISOU 302 OD1 ASN A 69 15678 12621 11030 935 157 94 O ATOM 303 ND2 ASN A 69 -1.239 9.158 22.156 1.00105.45 N ANISOU 303 ND2 ASN A 69 15893 13008 11166 1160 140 74 N ATOM 304 N TYR A 70 -4.605 6.831 26.161 1.00 88.86 N ANISOU 304 N TYR A 70 13342 11314 9105 1027 153 -145 N ATOM 305 CA TYR A 70 -5.713 6.836 27.120 1.00 89.10 C ANISOU 305 CA TYR A 70 13303 11455 9097 1059 169 -204 C ATOM 306 C TYR A 70 -5.239 6.269 28.465 1.00 91.11 C ANISOU 306 C TYR A 70 13577 11619 9420 909 195 -190 C ATOM 307 O TYR A 70 -5.659 6.767 29.510 1.00 90.79 O ANISOU 307 O TYR A 70 13570 11574 9351 942 209 -199 O ATOM 308 CB TYR A 70 -6.936 6.059 26.595 1.00 91.30 C ANISOU 308 CB TYR A 70 13392 11961 9337 1073 173 -302 C ATOM 309 CG TYR A 70 -7.778 6.795 25.569 1.00 94.77 C ANISOU 309 CG TYR A 70 13791 12547 9669 1273 143 -335 C ATOM 310 CD1 TYR A 70 -7.729 8.183 25.457 1.00 97.38 C ANISOU 310 CD1 TYR A 70 14267 12807 9927 1456 128 -281 C ATOM 311 CD2 TYR A 70 -8.669 6.108 24.749 1.00 96.48 C ANISOU 311 CD2 TYR A 70 13831 12983 9844 1284 135 -426 C ATOM 312 CE1 TYR A 70 -8.506 8.863 24.519 1.00 99.75 C ANISOU 312 CE1 TYR A 70 14548 13243 10111 1670 102 -304 C ATOM 313 CE2 TYR A 70 -9.459 6.778 23.815 1.00 98.66 C ANISOU 313 CE2 TYR A 70 14060 13422 10006 1489 101 -460 C ATOM 314 CZ TYR A 70 -9.374 8.156 23.702 1.00107.00 C ANISOU 314 CZ TYR A 70 15271 14399 10985 1694 83 -393 C ATOM 315 OH TYR A 70 -10.152 8.820 22.782 1.00109.01 O ANISOU 315 OH TYR A 70 15497 14813 11110 1925 52 -419 O ATOM 316 N PHE A 71 -4.339 5.258 28.437 1.00 86.28 N ANISOU 316 N PHE A 71 12957 10936 8890 760 204 -165 N ATOM 317 CA PHE A 71 -3.763 4.662 29.646 1.00 85.40 C ANISOU 317 CA PHE A 71 12877 10737 8832 636 227 -142 C ATOM 318 C PHE A 71 -2.725 5.608 30.256 1.00 90.31 C ANISOU 318 C PHE A 71 13643 11209 9463 645 209 -75 C ATOM 319 O PHE A 71 -2.566 5.621 31.475 1.00 90.26 O ANISOU 319 O PHE A 71 13676 11157 9463 600 221 -66 O ATOM 320 CB PHE A 71 -3.141 3.280 29.376 1.00 86.32 C ANISOU 320 CB PHE A 71 12952 10829 9016 503 245 -136 C ATOM 321 CG PHE A 71 -4.054 2.232 28.773 1.00 87.77 C ANISOU 321 CG PHE A 71 13007 11145 9195 456 278 -212 C ATOM 322 CD1 PHE A 71 -5.184 1.791 29.454 1.00 91.01 C ANISOU 322 CD1 PHE A 71 13340 11663 9576 421 323 -286 C ATOM 323 CD2 PHE A 71 -3.749 1.642 27.553 1.00 88.99 C ANISOU 323 CD2 PHE A 71 13121 11319 9373 429 272 -217 C ATOM 324 CE1 PHE A 71 -6.025 0.824 28.895 1.00 92.04 C ANISOU 324 CE1 PHE A 71 13350 11927 9696 352 364 -373 C ATOM 325 CE2 PHE A 71 -4.587 0.670 26.999 1.00 91.95 C ANISOU 325 CE2 PHE A 71 13379 11820 9736 367 309 -301 C ATOM 326 CZ PHE A 71 -5.720 0.270 27.672 1.00 90.64 C ANISOU 326 CZ PHE A 71 13135 11767 9539 323 357 -382 C ATOM 327 N ILE A 72 -2.044 6.419 29.414 1.00 87.51 N ANISOU 327 N ILE A 72 13369 10782 9097 696 186 -35 N ATOM 328 CA ILE A 72 -1.061 7.426 29.848 1.00 87.40 C ANISOU 328 CA ILE A 72 13497 10632 9080 689 181 13 C ATOM 329 C ILE A 72 -1.814 8.557 30.611 1.00 92.14 C ANISOU 329 C ILE A 72 14174 11225 9610 790 194 -2 C ATOM 330 O ILE A 72 -1.299 9.055 31.616 1.00 91.80 O ANISOU 330 O ILE A 72 14218 11096 9566 746 202 14 O ATOM 331 CB ILE A 72 -0.206 7.928 28.638 1.00 90.27 C ANISOU 331 CB ILE A 72 13929 10924 9445 703 171 50 C ATOM 332 CG1 ILE A 72 0.910 6.905 28.310 1.00 89.70 C ANISOU 332 CG1 ILE A 72 13807 10827 9446 579 161 73 C ATOM 333 CG2 ILE A 72 0.386 9.336 28.864 1.00 91.40 C ANISOU 333 CG2 ILE A 72 14241 10941 9545 729 186 78 C ATOM 334 CD1 ILE A 72 1.408 6.892 26.851 1.00 98.01 C ANISOU 334 CD1 ILE A 72 14863 11868 10508 591 154 92 C ATOM 335 N THR A 73 -3.052 8.898 30.164 1.00 89.29 N ANISOU 335 N THR A 73 13772 10970 9185 927 197 -39 N ATOM 336 CA THR A 73 -3.943 9.895 30.776 1.00 89.92 C ANISOU 336 CA THR A 73 13910 11069 9186 1055 212 -59 C ATOM 337 C THR A 73 -4.328 9.420 32.195 1.00 93.83 C ANISOU 337 C THR A 73 14353 11598 9699 984 227 -89 C ATOM 338 O THR A 73 -4.343 10.234 33.121 1.00 93.92 O ANISOU 338 O THR A 73 14465 11544 9677 1014 242 -82 O ATOM 339 CB THR A 73 -5.169 10.146 29.868 1.00 98.19 C ANISOU 339 CB THR A 73 14888 12266 10154 1228 204 -99 C ATOM 340 OG1 THR A 73 -4.716 10.550 28.574 1.00 99.59 O ANISOU 340 OG1 THR A 73 15130 12399 10312 1292 192 -64 O ATOM 341 CG2 THR A 73 -6.114 11.209 30.416 1.00 96.62 C ANISOU 341 CG2 THR A 73 14751 12100 9859 1395 220 -120 C ATOM 342 N SER A 74 -4.591 8.099 32.358 1.00 89.67 N ANISOU 342 N SER A 74 13687 11162 9221 883 232 -121 N ATOM 343 CA SER A 74 -4.919 7.454 33.636 1.00 89.26 C ANISOU 343 CA SER A 74 13590 11138 9186 799 258 -146 C ATOM 344 C SER A 74 -3.729 7.541 34.607 1.00 92.69 C ANISOU 344 C SER A 74 14131 11429 9659 703 255 -94 C ATOM 345 O SER A 74 -3.917 7.780 35.803 1.00 91.85 O ANISOU 345 O SER A 74 14062 11305 9531 692 271 -102 O ATOM 346 CB SER A 74 -5.305 5.997 33.404 1.00 91.98 C ANISOU 346 CB SER A 74 13798 11581 9570 700 280 -187 C ATOM 347 OG SER A 74 -5.667 5.348 34.611 1.00 99.33 O ANISOU 347 OG SER A 74 14703 12531 10508 618 320 -212 O ATOM 348 N LEU A 75 -2.506 7.365 34.069 1.00 89.18 N ANISOU 348 N LEU A 75 13726 10898 9260 637 233 -48 N ATOM 349 CA LEU A 75 -1.239 7.438 34.796 1.00 88.56 C ANISOU 349 CA LEU A 75 13727 10714 9210 549 221 -7 C ATOM 350 C LEU A 75 -0.937 8.893 35.206 1.00 92.42 C ANISOU 350 C LEU A 75 14351 11114 9651 592 222 1 C ATOM 351 O LEU A 75 -0.486 9.118 36.329 1.00 91.92 O ANISOU 351 O LEU A 75 14342 11006 9579 540 223 5 O ATOM 352 CB LEU A 75 -0.116 6.861 33.906 1.00 88.11 C ANISOU 352 CB LEU A 75 13652 10621 9205 482 201 27 C ATOM 353 CG LEU A 75 1.255 6.583 34.533 1.00 92.77 C ANISOU 353 CG LEU A 75 14276 11149 9823 386 184 60 C ATOM 354 CD1 LEU A 75 1.173 5.529 35.621 1.00 93.16 C ANISOU 354 CD1 LEU A 75 14285 11227 9883 336 196 60 C ATOM 355 CD2 LEU A 75 2.218 6.092 33.487 1.00 94.89 C ANISOU 355 CD2 LEU A 75 14517 11403 10135 344 166 86 C ATOM 356 N ALA A 76 -1.211 9.871 34.307 1.00 89.14 N ANISOU 356 N ALA A 76 14001 10674 9195 692 226 3 N ATOM 357 CA ALA A 76 -0.999 11.307 34.531 1.00 89.37 C ANISOU 357 CA ALA A 76 14191 10598 9166 742 246 9 C ATOM 358 C ALA A 76 -2.011 11.889 35.530 1.00 93.37 C ANISOU 358 C ALA A 76 14734 11128 9614 826 268 -20 C ATOM 359 O ALA A 76 -1.689 12.858 36.221 1.00 93.42 O ANISOU 359 O ALA A 76 14876 11038 9581 822 290 -20 O ATOM 360 CB ALA A 76 -1.075 12.063 33.213 1.00 90.48 C ANISOU 360 CB ALA A 76 14407 10701 9269 841 256 25 C ATOM 361 N CYS A 77 -3.231 11.307 35.597 1.00 89.48 N ANISOU 361 N CYS A 77 14120 10768 9109 896 269 -54 N ATOM 362 CA CYS A 77 -4.287 11.723 36.527 1.00 89.47 C ANISOU 362 CA CYS A 77 14125 10820 9052 980 292 -90 C ATOM 363 C CYS A 77 -3.880 11.385 37.963 1.00 92.77 C ANISOU 363 C CYS A 77 14553 11203 9493 864 298 -91 C ATOM 364 O CYS A 77 -4.068 12.215 38.851 1.00 92.92 O ANISOU 364 O CYS A 77 14668 11175 9464 900 318 -102 O ATOM 365 CB CYS A 77 -5.620 11.077 36.166 1.00 89.83 C ANISOU 365 CB CYS A 77 14012 11043 9078 1058 294 -138 C ATOM 366 SG CYS A 77 -6.562 11.962 34.899 1.00 94.60 S ANISOU 366 SG CYS A 77 14626 11725 9593 1281 291 -154 S ATOM 367 N ALA A 78 -3.304 10.176 38.177 1.00 88.19 N ANISOU 367 N ALA A 78 13886 10643 8979 734 284 -79 N ATOM 368 CA ALA A 78 -2.824 9.675 39.470 1.00 87.33 C ANISOU 368 CA ALA A 78 13783 10511 8886 632 286 -74 C ATOM 369 C ALA A 78 -1.656 10.507 39.991 1.00 90.55 C ANISOU 369 C ALA A 78 14318 10806 9282 578 273 -53 C ATOM 370 O ALA A 78 -1.584 10.751 41.194 1.00 90.28 O ANISOU 370 O ALA A 78 14331 10752 9219 549 281 -64 O ATOM 371 CB ALA A 78 -2.407 8.217 39.347 1.00 87.37 C ANISOU 371 CB ALA A 78 13691 10554 8951 535 279 -57 C ATOM 372 N ASP A 79 -0.756 10.951 39.085 1.00 86.87 N ANISOU 372 N ASP A 79 13904 10272 8830 555 258 -31 N ATOM 373 CA ASP A 79 0.406 11.782 39.410 1.00 87.02 C ANISOU 373 CA ASP A 79 14037 10193 8833 480 256 -28 C ATOM 374 C ASP A 79 -0.019 13.216 39.746 1.00 91.78 C ANISOU 374 C ASP A 79 14791 10717 9365 548 294 -50 C ATOM 375 O ASP A 79 0.611 13.843 40.594 1.00 92.04 O ANISOU 375 O ASP A 79 14916 10688 9368 477 305 -68 O ATOM 376 CB ASP A 79 1.427 11.791 38.258 1.00 88.71 C ANISOU 376 CB ASP A 79 14258 10368 9081 427 242 -6 C ATOM 377 CG ASP A 79 1.987 10.436 37.852 1.00 99.05 C ANISOU 377 CG ASP A 79 15436 11742 10455 365 208 17 C ATOM 378 OD1 ASP A 79 2.107 9.549 38.730 1.00 99.50 O ANISOU 378 OD1 ASP A 79 15429 11850 10526 323 193 21 O ATOM 379 OD2 ASP A 79 2.346 10.276 36.663 1.00104.75 O ANISOU 379 OD2 ASP A 79 16136 12457 11206 364 201 35 O ATOM 380 N LEU A 80 -1.087 13.727 39.096 1.00 88.35 N ANISOU 380 N LEU A 80 14385 10290 8893 692 318 -54 N ATOM 381 CA LEU A 80 -1.636 15.066 39.335 1.00 88.96 C ANISOU 381 CA LEU A 80 14621 10291 8890 797 363 -70 C ATOM 382 C LEU A 80 -2.352 15.119 40.694 1.00 92.28 C ANISOU 382 C LEU A 80 15035 10750 9277 821 375 -100 C ATOM 383 O LEU A 80 -2.184 16.095 41.429 1.00 92.50 O ANISOU 383 O LEU A 80 15207 10687 9252 816 408 -117 O ATOM 384 CB LEU A 80 -2.594 15.455 38.191 1.00 89.65 C ANISOU 384 CB LEU A 80 14722 10406 8936 974 377 -62 C ATOM 385 CG LEU A 80 -3.259 16.835 38.235 1.00 95.71 C ANISOU 385 CG LEU A 80 15668 11094 9602 1132 429 -70 C ATOM 386 CD1 LEU A 80 -2.240 17.957 38.043 1.00 96.43 C ANISOU 386 CD1 LEU A 80 15981 10997 9659 1071 477 -58 C ATOM 387 CD2 LEU A 80 -4.333 16.934 37.177 1.00 98.82 C ANISOU 387 CD2 LEU A 80 16023 11575 9949 1332 428 -65 C ATOM 388 N VAL A 81 -3.135 14.059 41.026 1.00 87.79 N ANISOU 388 N VAL A 81 14306 10313 8736 836 357 -110 N ATOM 389 CA VAL A 81 -3.865 13.898 42.294 1.00 87.57 C ANISOU 389 CA VAL A 81 14249 10342 8681 849 373 -139 C ATOM 390 C VAL A 81 -2.820 13.771 43.425 1.00 91.90 C ANISOU 390 C VAL A 81 14842 10835 9243 705 361 -136 C ATOM 391 O VAL A 81 -3.022 14.319 44.513 1.00 92.46 O ANISOU 391 O VAL A 81 14985 10879 9265 710 383 -159 O ATOM 392 CB VAL A 81 -4.873 12.700 42.231 1.00 90.80 C ANISOU 392 CB VAL A 81 14478 10905 9117 870 370 -156 C ATOM 393 CG1 VAL A 81 -5.361 12.273 43.612 1.00 90.59 C ANISOU 393 CG1 VAL A 81 14415 10929 9075 833 391 -182 C ATOM 394 CG2 VAL A 81 -6.067 13.036 41.344 1.00 91.19 C ANISOU 394 CG2 VAL A 81 14480 11044 9123 1033 383 -181 C ATOM 395 N MET A 82 -1.680 13.105 43.131 1.00 87.79 N ANISOU 395 N MET A 82 14277 10304 8777 588 327 -111 N ATOM 396 CA MET A 82 -0.548 12.918 44.041 1.00 87.54 C ANISOU 396 CA MET A 82 14265 10249 8749 461 304 -110 C ATOM 397 C MET A 82 0.109 14.270 44.384 1.00 91.42 C ANISOU 397 C MET A 82 14915 10634 9187 421 325 -137 C ATOM 398 O MET A 82 0.406 14.522 45.548 1.00 91.42 O ANISOU 398 O MET A 82 14959 10627 9149 365 327 -163 O ATOM 399 CB MET A 82 0.484 11.959 43.411 1.00 89.37 C ANISOU 399 CB MET A 82 14409 10508 9041 376 264 -80 C ATOM 400 CG MET A 82 1.491 11.388 44.389 1.00 93.46 C ANISOU 400 CG MET A 82 14899 11056 9555 277 233 -77 C ATOM 401 SD MET A 82 0.785 10.154 45.508 1.00 98.05 S ANISOU 401 SD MET A 82 15405 11719 10132 295 238 -64 S ATOM 402 CE MET A 82 2.111 8.966 45.554 1.00 94.37 C ANISOU 402 CE MET A 82 14867 11297 9690 223 192 -28 C ATOM 403 N GLY A 83 0.298 15.121 43.377 1.00 87.47 N ANISOU 403 N GLY A 83 14508 10051 8676 447 349 -136 N ATOM 404 CA GLY A 83 0.926 16.429 43.536 1.00 87.57 C ANISOU 404 CA GLY A 83 14697 9942 8634 394 389 -166 C ATOM 405 C GLY A 83 0.059 17.532 44.108 1.00 90.99 C ANISOU 405 C GLY A 83 15279 10302 8990 491 446 -192 C ATOM 406 O GLY A 83 0.591 18.549 44.554 1.00 91.57 O ANISOU 406 O GLY A 83 15511 10273 9011 424 489 -228 O ATOM 407 N LEU A 84 -1.274 17.356 44.091 1.00 86.44 N ANISOU 407 N LEU A 84 14657 9784 8401 648 453 -182 N ATOM 408 CA LEU A 84 -2.217 18.359 44.588 1.00 86.78 C ANISOU 408 CA LEU A 84 14832 9776 8365 775 506 -205 C ATOM 409 C LEU A 84 -2.792 18.032 45.962 1.00 89.90 C ANISOU 409 C LEU A 84 15171 10244 8742 776 502 -230 C ATOM 410 O LEU A 84 -3.014 18.952 46.746 1.00 90.43 O ANISOU 410 O LEU A 84 15376 10240 8741 804 546 -261 O ATOM 411 CB LEU A 84 -3.389 18.532 43.605 1.00 87.19 C ANISOU 411 CB LEU A 84 14872 9865 8391 977 522 -186 C ATOM 412 CG LEU A 84 -3.169 19.445 42.403 1.00 92.70 C ANISOU 412 CG LEU A 84 15724 10446 9052 1050 560 -165 C ATOM 413 CD1 LEU A 84 -4.109 19.080 41.278 1.00 92.96 C ANISOU 413 CD1 LEU A 84 15658 10580 9083 1221 541 -142 C ATOM 414 CD2 LEU A 84 -3.342 20.917 42.776 1.00 96.33 C ANISOU 414 CD2 LEU A 84 16439 10752 9411 1128 640 -185 C ATOM 415 N ALA A 85 -3.087 16.745 46.236 1.00 85.13 N ANISOU 415 N ALA A 85 14382 9773 8192 751 460 -218 N ATOM 416 CA ALA A 85 -3.739 16.320 47.475 1.00 84.68 C ANISOU 416 CA ALA A 85 14267 9792 8115 758 464 -239 C ATOM 417 C ALA A 85 -2.876 15.433 48.393 1.00 87.08 C ANISOU 417 C ALA A 85 14504 10134 8449 610 427 -234 C ATOM 418 O ALA A 85 -3.257 15.233 49.549 1.00 87.06 O ANISOU 418 O ALA A 85 14492 10171 8416 604 438 -251 O ATOM 419 CB ALA A 85 -5.024 15.584 47.133 1.00 85.29 C ANISOU 419 CB ALA A 85 14202 9998 8206 866 468 -239 C ATOM 420 N VAL A 86 -1.746 14.893 47.902 1.00 82.17 N ANISOU 420 N VAL A 86 13835 9508 7876 505 386 -210 N ATOM 421 CA VAL A 86 -0.903 14.005 48.711 1.00 81.15 C ANISOU 421 CA VAL A 86 13639 9431 7761 395 347 -201 C ATOM 422 C VAL A 86 0.392 14.725 49.141 1.00 85.10 C ANISOU 422 C VAL A 86 14228 9879 8227 282 332 -230 C ATOM 423 O VAL A 86 0.584 14.944 50.337 1.00 85.30 O ANISOU 423 O VAL A 86 14295 9916 8201 241 332 -260 O ATOM 424 CB VAL A 86 -0.603 12.652 48.002 1.00 83.84 C ANISOU 424 CB VAL A 86 13843 9840 8171 369 312 -158 C ATOM 425 CG1 VAL A 86 0.179 11.713 48.910 1.00 83.40 C ANISOU 425 CG1 VAL A 86 13737 9840 8112 293 278 -142 C ATOM 426 CG2 VAL A 86 -1.881 11.978 47.515 1.00 83.31 C ANISOU 426 CG2 VAL A 86 13688 9834 8133 456 337 -148 C ATOM 427 N VAL A 87 1.270 15.072 48.169 1.00 81.01 N ANISOU 427 N VAL A 87 13734 9315 7733 225 322 -230 N ATOM 428 CA VAL A 87 2.572 15.729 48.366 1.00 81.01 C ANISOU 428 CA VAL A 87 13798 9280 7701 92 315 -272 C ATOM 429 C VAL A 87 2.426 17.055 49.186 1.00 86.78 C ANISOU 429 C VAL A 87 14697 9925 8352 70 368 -331 C ATOM 430 O VAL A 87 3.208 17.202 50.128 1.00 87.29 O ANISOU 430 O VAL A 87 14770 10024 8372 -37 351 -377 O ATOM 431 CB VAL A 87 3.347 15.940 47.028 1.00 84.19 C ANISOU 431 CB VAL A 87 14207 9640 8141 40 315 -264 C ATOM 432 CG1 VAL A 87 4.686 16.632 47.257 1.00 84.51 C ANISOU 432 CG1 VAL A 87 14306 9662 8141 -119 319 -325 C ATOM 433 CG2 VAL A 87 3.568 14.614 46.303 1.00 82.94 C ANISOU 433 CG2 VAL A 87 13889 9568 8056 56 264 -210 C ATOM 434 N PRO A 88 1.445 17.981 48.938 1.00 83.78 N ANISOU 434 N PRO A 88 14446 9443 7941 174 430 -336 N ATOM 435 CA PRO A 88 1.365 19.205 49.761 1.00 84.52 C ANISOU 435 CA PRO A 88 14716 9444 7953 151 488 -394 C ATOM 436 C PRO A 88 1.152 18.960 51.262 1.00 88.90 C ANISOU 436 C PRO A 88 15243 10069 8467 136 472 -420 C ATOM 437 O PRO A 88 1.825 19.609 52.067 1.00 89.55 O ANISOU 437 O PRO A 88 15411 10125 8490 24 487 -482 O ATOM 438 CB PRO A 88 0.167 19.949 49.164 1.00 86.56 C ANISOU 438 CB PRO A 88 15091 9610 8188 321 550 -375 C ATOM 439 CG PRO A 88 0.105 19.484 47.769 1.00 90.46 C ANISOU 439 CG PRO A 88 15511 10117 8743 376 531 -325 C ATOM 440 CD PRO A 88 0.425 18.025 47.868 1.00 85.07 C ANISOU 440 CD PRO A 88 14615 9577 8131 324 454 -294 C ATOM 441 N PHE A 89 0.244 18.030 51.642 1.00 84.59 N ANISOU 441 N PHE A 89 14581 9614 7946 234 447 -381 N ATOM 442 CA PHE A 89 -0.042 17.721 53.048 1.00 84.41 C ANISOU 442 CA PHE A 89 14535 9656 7880 230 439 -399 C ATOM 443 C PHE A 89 1.108 16.958 53.716 1.00 88.42 C ANISOU 443 C PHE A 89 14952 10261 8384 109 375 -405 C ATOM 444 O PHE A 89 1.300 17.085 54.926 1.00 88.42 O ANISOU 444 O PHE A 89 14980 10296 8322 66 370 -441 O ATOM 445 CB PHE A 89 -1.358 16.947 53.188 1.00 85.62 C ANISOU 445 CB PHE A 89 14598 9877 8056 358 447 -362 C ATOM 446 CG PHE A 89 -2.569 17.781 52.849 1.00 87.58 C ANISOU 446 CG PHE A 89 14931 10068 8279 499 507 -371 C ATOM 447 CD1 PHE A 89 -3.104 18.669 53.774 1.00 91.63 C ANISOU 447 CD1 PHE A 89 15566 10535 8716 543 555 -413 C ATOM 448 CD2 PHE A 89 -3.163 17.696 51.598 1.00 89.49 C ANISOU 448 CD2 PHE A 89 15132 10310 8560 599 515 -342 C ATOM 449 CE1 PHE A 89 -4.218 19.453 53.454 1.00 93.16 C ANISOU 449 CE1 PHE A 89 15840 10683 8872 699 612 -422 C ATOM 450 CE2 PHE A 89 -4.279 18.476 51.280 1.00 93.04 C ANISOU 450 CE2 PHE A 89 15655 10728 8968 756 566 -352 C ATOM 451 CZ PHE A 89 -4.800 19.348 52.212 1.00 92.03 C ANISOU 451 CZ PHE A 89 15649 10555 8763 812 615 -391 C ATOM 452 N GLY A 90 1.861 16.198 52.924 1.00 84.87 N ANISOU 452 N GLY A 90 14396 9860 7990 66 329 -373 N ATOM 453 CA GLY A 90 3.022 15.448 53.389 1.00 84.79 C ANISOU 453 CA GLY A 90 14292 9956 7968 -23 265 -375 C ATOM 454 C GLY A 90 4.203 16.351 53.679 1.00 90.06 C ANISOU 454 C GLY A 90 15021 10620 8578 -163 260 -453 C ATOM 455 O GLY A 90 4.972 16.087 54.604 1.00 89.63 O ANISOU 455 O GLY A 90 14919 10668 8467 -228 217 -486 O ATOM 456 N ALA A 91 4.341 17.434 52.884 1.00 88.11 N ANISOU 456 N ALA A 91 14885 10258 8334 -210 311 -488 N ATOM 457 CA ALA A 91 5.392 18.447 53.005 1.00 89.54 C ANISOU 457 CA ALA A 91 15152 10411 8459 -368 334 -576 C ATOM 458 C ALA A 91 5.214 19.264 54.289 1.00 95.65 C ANISOU 458 C ALA A 91 16040 11161 9142 -409 368 -647 C ATOM 459 O ALA A 91 6.203 19.574 54.958 1.00 96.21 O ANISOU 459 O ALA A 91 16105 11303 9148 -550 352 -727 O ATOM 460 CB ALA A 91 5.375 19.366 51.790 1.00 90.52 C ANISOU 460 CB ALA A 91 15401 10387 8605 -389 402 -584 C ATOM 461 N ALA A 92 3.951 19.592 54.636 1.00 92.79 N ANISOU 461 N ALA A 92 15771 10716 8770 -285 415 -623 N ATOM 462 CA ALA A 92 3.584 20.336 55.840 1.00 93.75 C ANISOU 462 CA ALA A 92 16009 10803 8809 -296 454 -681 C ATOM 463 C ALA A 92 3.863 19.509 57.103 1.00 98.61 C ANISOU 463 C ALA A 92 16509 11575 9384 -313 387 -687 C ATOM 464 O ALA A 92 4.320 20.065 58.098 1.00 99.39 O ANISOU 464 O ALA A 92 16665 11700 9399 -406 393 -765 O ATOM 465 CB ALA A 92 2.116 20.724 55.777 1.00 94.39 C ANISOU 465 CB ALA A 92 16189 10781 8894 -131 515 -644 C ATOM 466 N HIS A 93 3.629 18.177 57.039 1.00 94.72 N ANISOU 466 N HIS A 93 15863 11183 8942 -226 328 -608 N ATOM 467 CA HIS A 93 3.841 17.208 58.121 1.00 94.74 C ANISOU 467 CA HIS A 93 15764 11326 8905 -210 269 -592 C ATOM 468 C HIS A 93 5.329 17.082 58.501 1.00 99.63 C ANISOU 468 C HIS A 93 16310 12077 9468 -336 205 -649 C ATOM 469 O HIS A 93 5.634 16.797 59.659 1.00 99.93 O ANISOU 469 O HIS A 93 16318 12223 9426 -345 168 -673 O ATOM 470 CB HIS A 93 3.277 15.832 57.702 1.00 94.50 C ANISOU 470 CB HIS A 93 15616 11343 8946 -95 243 -492 C ATOM 471 CG HIS A 93 3.233 14.792 58.787 1.00 98.01 C ANISOU 471 CG HIS A 93 15996 11896 9346 -49 207 -459 C ATOM 472 ND1 HIS A 93 2.950 15.120 60.104 1.00100.61 N ANISOU 472 ND1 HIS A 93 16390 12248 9591 -46 221 -496 N ATOM 473 CD2 HIS A 93 3.376 13.449 58.697 1.00 99.15 C ANISOU 473 CD2 HIS A 93 16040 12119 9516 6 170 -388 C ATOM 474 CE1 HIS A 93 2.968 13.977 60.772 1.00 99.84 C ANISOU 474 CE1 HIS A 93 16228 12243 9465 9 190 -445 C ATOM 475 NE2 HIS A 93 3.214 12.944 59.968 1.00 99.35 N ANISOU 475 NE2 HIS A 93 16074 12211 9465 44 163 -379 N ATOM 476 N ILE A 94 6.243 17.296 57.534 1.00 96.41 N ANISOU 476 N ILE A 94 15868 11673 9091 -428 193 -674 N ATOM 477 CA ILE A 94 7.694 17.218 57.731 1.00 97.07 C ANISOU 477 CA ILE A 94 15859 11905 9119 -554 135 -741 C ATOM 478 C ILE A 94 8.230 18.547 58.304 1.00102.56 C ANISOU 478 C ILE A 94 16662 12580 9725 -716 177 -872 C ATOM 479 O ILE A 94 8.990 18.525 59.277 1.00103.19 O ANISOU 479 O ILE A 94 16686 12810 9712 -789 131 -944 O ATOM 480 CB ILE A 94 8.401 16.827 56.398 1.00 99.76 C ANISOU 480 CB ILE A 94 16107 12265 9532 -585 112 -715 C ATOM 481 CG1 ILE A 94 8.026 15.386 55.982 1.00 99.25 C ANISOU 481 CG1 ILE A 94 15929 12245 9538 -438 66 -597 C ATOM 482 CG2 ILE A 94 9.932 17.004 56.479 1.00101.46 C ANISOU 482 CG2 ILE A 94 16231 12636 9684 -739 67 -811 C ATOM 483 CD1 ILE A 94 8.154 15.077 54.511 1.00106.38 C ANISOU 483 CD1 ILE A 94 16785 13098 10536 -427 70 -549 C ATOM 484 N LEU A 95 7.844 19.688 57.694 1.00 99.31 N ANISOU 484 N LEU A 95 16413 11986 9334 -769 268 -905 N ATOM 485 CA LEU A 95 8.296 21.027 58.085 1.00100.53 C ANISOU 485 CA LEU A 95 16710 12078 9407 -937 336 -1032 C ATOM 486 C LEU A 95 7.780 21.454 59.468 1.00106.20 C ANISOU 486 C LEU A 95 17517 12794 10039 -923 355 -1077 C ATOM 487 O LEU A 95 8.511 22.131 60.194 1.00107.14 O ANISOU 487 O LEU A 95 17674 12971 10064 -1080 367 -1197 O ATOM 488 CB LEU A 95 7.894 22.074 57.032 1.00100.48 C ANISOU 488 CB LEU A 95 16890 11848 9439 -963 444 -1036 C ATOM 489 CG LEU A 95 8.548 21.958 55.647 1.00104.38 C ANISOU 489 CG LEU A 95 17336 12324 9998 -1021 447 -1018 C ATOM 490 CD1 LEU A 95 7.832 22.828 54.639 1.00104.38 C ANISOU 490 CD1 LEU A 95 17533 12091 10034 -974 551 -988 C ATOM 491 CD2 LEU A 95 10.037 22.305 55.687 1.00107.92 C ANISOU 491 CD2 LEU A 95 17728 12890 10387 -1252 441 -1142 C ATOM 492 N MET A 96 6.546 21.057 59.836 1.00102.82 N ANISOU 492 N MET A 96 17115 12312 9638 -747 360 -991 N ATOM 493 CA MET A 96 5.944 21.406 61.129 1.00103.65 C ANISOU 493 CA MET A 96 17304 12411 9666 -715 382 -1024 C ATOM 494 C MET A 96 6.226 20.348 62.201 1.00107.72 C ANISOU 494 C MET A 96 17672 13125 10133 -672 289 -1005 C ATOM 495 O MET A 96 6.048 20.631 63.388 1.00107.95 O ANISOU 495 O MET A 96 17752 13188 10075 -681 295 -1053 O ATOM 496 CB MET A 96 4.427 21.625 61.000 1.00105.55 C ANISOU 496 CB MET A 96 17658 12497 9948 -549 448 -954 C ATOM 497 CG MET A 96 4.056 22.806 60.119 1.00109.78 C ANISOU 497 CG MET A 96 18381 12829 10501 -559 548 -975 C ATOM 498 SD MET A 96 2.294 23.212 60.142 1.00113.97 S ANISOU 498 SD MET A 96 19047 13213 11045 -346 626 -915 S ATOM 499 CE MET A 96 1.607 21.781 59.334 1.00109.00 C ANISOU 499 CE MET A 96 18220 12665 10527 -183 562 -786 C ATOM 500 N LYS A 97 6.655 19.132 61.780 1.00103.89 N ANISOU 500 N LYS A 97 17016 12762 9694 -615 211 -932 N ATOM 501 CA LYS A 97 6.982 17.964 62.623 1.00103.71 C ANISOU 501 CA LYS A 97 16860 12923 9622 -545 125 -893 C ATOM 502 C LYS A 97 5.755 17.496 63.455 1.00107.45 C ANISOU 502 C LYS A 97 17380 13357 10087 -400 147 -823 C ATOM 503 O LYS A 97 5.918 16.864 64.502 1.00107.65 O ANISOU 503 O LYS A 97 17359 13508 10036 -355 101 -814 O ATOM 504 CB LYS A 97 8.214 18.234 63.523 1.00107.41 C ANISOU 504 CB LYS A 97 17273 13573 9966 -671 70 -1007 C ATOM 505 CG LYS A 97 9.526 18.320 62.744 1.00119.63 C ANISOU 505 CG LYS A 97 18716 15224 11515 -801 32 -1069 C ATOM 506 CD LYS A 97 10.678 18.850 63.584 1.00129.47 C ANISOU 506 CD LYS A 97 19914 16653 12627 -957 -5 -1215 C ATOM 507 CE LYS A 97 11.884 19.146 62.726 1.00139.27 C ANISOU 507 CE LYS A 97 21065 17979 13872 -1116 -17 -1299 C ATOM 508 NZ LYS A 97 12.989 19.753 63.512 1.00149.52 N ANISOU 508 NZ LYS A 97 22308 19470 15032 -1295 -42 -1465 N ATOM 509 N MET A 98 4.532 17.769 62.945 1.00103.24 N ANISOU 509 N MET A 98 16933 12663 9629 -321 219 -774 N ATOM 510 CA MET A 98 3.251 17.406 63.562 1.00102.68 C ANISOU 510 CA MET A 98 16902 12551 9561 -194 257 -718 C ATOM 511 C MET A 98 2.113 17.428 62.529 1.00103.90 C ANISOU 511 C MET A 98 17083 12576 9817 -100 316 -656 C ATOM 512 O MET A 98 2.255 18.039 61.464 1.00103.90 O ANISOU 512 O MET A 98 17119 12490 9870 -134 339 -669 O ATOM 513 CB MET A 98 2.921 18.341 64.746 1.00106.52 C ANISOU 513 CB MET A 98 17513 13009 9951 -224 299 -795 C ATOM 514 CG MET A 98 2.574 19.768 64.340 1.00111.42 C ANISOU 514 CG MET A 98 18288 13470 10575 -273 380 -860 C ATOM 515 SD MET A 98 2.284 20.860 65.750 1.00117.91 S ANISOU 515 SD MET A 98 19269 14257 11276 -317 434 -959 S ATOM 516 CE MET A 98 0.684 20.269 66.310 1.00114.13 C ANISOU 516 CE MET A 98 18794 13757 10814 -131 472 -876 C ATOM 517 N TRP A 99 0.979 16.789 62.863 1.00 97.97 N ANISOU 517 N TRP A 99 16319 11823 9084 15 345 -597 N ATOM 518 CA TRP A 99 -0.200 16.744 62.002 1.00 96.31 C ANISOU 518 CA TRP A 99 16110 11530 8954 112 399 -551 C ATOM 519 C TRP A 99 -1.248 17.742 62.518 1.00100.79 C ANISOU 519 C TRP A 99 16801 12017 9479 168 473 -593 C ATOM 520 O TRP A 99 -1.690 17.640 63.665 1.00100.86 O ANISOU 520 O TRP A 99 16835 12062 9425 193 491 -605 O ATOM 521 CB TRP A 99 -0.758 15.313 61.924 1.00 93.68 C ANISOU 521 CB TRP A 99 15667 11263 8666 187 392 -469 C ATOM 522 CG TRP A 99 -1.806 15.115 60.871 1.00 93.49 C ANISOU 522 CG TRP A 99 15604 11192 8725 268 435 -432 C ATOM 523 CD1 TRP A 99 -3.135 14.892 61.073 1.00 96.27 C ANISOU 523 CD1 TRP A 99 15946 11548 9083 353 494 -420 C ATOM 524 CD2 TRP A 99 -1.604 15.084 59.451 1.00 92.49 C ANISOU 524 CD2 TRP A 99 15431 11031 8681 269 421 -408 C ATOM 525 NE1 TRP A 99 -3.778 14.737 59.867 1.00 95.06 N ANISOU 525 NE1 TRP A 99 15735 11378 9006 409 514 -397 N ATOM 526 CE2 TRP A 99 -2.863 14.854 58.854 1.00 96.00 C ANISOU 526 CE2 TRP A 99 15837 11466 9173 363 469 -385 C ATOM 527 CE3 TRP A 99 -0.480 15.241 58.620 1.00 93.38 C ANISOU 527 CE3 TRP A 99 15526 11130 8826 197 375 -410 C ATOM 528 CZ2 TRP A 99 -3.033 14.783 57.466 1.00 94.69 C ANISOU 528 CZ2 TRP A 99 15621 11276 9082 395 467 -361 C ATOM 529 CZ3 TRP A 99 -0.650 15.174 57.245 1.00 94.16 C ANISOU 529 CZ3 TRP A 99 15585 11190 9004 226 379 -381 C ATOM 530 CH2 TRP A 99 -1.913 14.947 56.681 1.00 94.45 C ANISOU 530 CH2 TRP A 99 15589 11216 9083 328 422 -355 C ATOM 531 N THR A 100 -1.609 18.733 61.682 1.00 97.13 N ANISOU 531 N THR A 100 16423 11441 9040 196 520 -614 N ATOM 532 CA THR A 100 -2.567 19.783 62.048 1.00 97.58 C ANISOU 532 CA THR A 100 16616 11411 9050 272 597 -654 C ATOM 533 C THR A 100 -3.822 19.730 61.146 1.00101.10 C ANISOU 533 C THR A 100 17034 11829 9550 422 640 -613 C ATOM 534 O THR A 100 -4.397 20.779 60.829 1.00101.64 O ANISOU 534 O THR A 100 17226 11801 9592 501 699 -639 O ATOM 535 CB THR A 100 -1.878 21.164 61.973 1.00105.48 C ANISOU 535 CB THR A 100 17784 12294 9999 185 630 -729 C ATOM 536 OG1 THR A 100 -1.451 21.408 60.632 1.00103.15 O ANISOU 536 OG1 THR A 100 17499 11932 9763 165 630 -712 O ATOM 537 CG2 THR A 100 -0.700 21.297 62.931 1.00105.22 C ANISOU 537 CG2 THR A 100 17768 12316 9896 28 592 -793 C ATOM 538 N PHE A 101 -4.256 18.510 60.749 1.00 96.15 N ANISOU 538 N PHE A 101 16251 11294 8988 465 615 -553 N ATOM 539 CA PHE A 101 -5.399 18.334 59.844 1.00 95.39 C ANISOU 539 CA PHE A 101 16094 11211 8939 593 648 -525 C ATOM 540 C PHE A 101 -6.461 17.342 60.374 1.00 99.30 C ANISOU 540 C PHE A 101 16475 11817 9439 650 671 -507 C ATOM 541 O PHE A 101 -7.433 17.048 59.670 1.00 98.40 O ANISOU 541 O PHE A 101 16278 11751 9360 741 697 -496 O ATOM 542 CB PHE A 101 -4.909 17.899 58.449 1.00 96.20 C ANISOU 542 CB PHE A 101 16119 11308 9124 575 609 -484 C ATOM 543 CG PHE A 101 -3.864 18.818 57.859 1.00 97.77 C ANISOU 543 CG PHE A 101 16428 11401 9319 504 597 -504 C ATOM 544 CD1 PHE A 101 -4.229 20.017 57.257 1.00101.29 C ANISOU 544 CD1 PHE A 101 17011 11735 9739 582 650 -527 C ATOM 545 CD2 PHE A 101 -2.513 18.499 57.932 1.00 99.48 C ANISOU 545 CD2 PHE A 101 16617 11632 9546 363 542 -506 C ATOM 546 CE1 PHE A 101 -3.259 20.876 56.732 1.00102.45 C ANISOU 546 CE1 PHE A 101 17283 11770 9875 498 659 -551 C ATOM 547 CE2 PHE A 101 -1.544 19.359 57.406 1.00102.46 C ANISOU 547 CE2 PHE A 101 17092 11923 9915 275 543 -539 C ATOM 548 CZ PHE A 101 -1.924 20.540 56.808 1.00101.10 C ANISOU 548 CZ PHE A 101 17071 11622 9720 333 607 -561 C ATOM 549 N GLY A 102 -6.286 16.873 61.608 1.00 96.73 N ANISOU 549 N GLY A 102 16149 11536 9067 593 668 -512 N ATOM 550 CA GLY A 102 -7.224 15.962 62.255 1.00 96.82 C ANISOU 550 CA GLY A 102 16080 11639 9068 624 707 -500 C ATOM 551 C GLY A 102 -7.078 14.504 61.876 1.00100.28 C ANISOU 551 C GLY A 102 16394 12144 9565 578 687 -445 C ATOM 552 O GLY A 102 -6.272 14.154 61.009 1.00 99.22 O ANISOU 552 O GLY A 102 16219 11992 9487 535 637 -412 O ATOM 553 N ASN A 103 -7.875 13.644 62.527 1.00 97.42 N ANISOU 553 N ASN A 103 15980 11852 9184 583 738 -439 N ATOM 554 CA ASN A 103 -7.848 12.199 62.310 1.00 96.86 C ANISOU 554 CA ASN A 103 15820 11829 9153 534 746 -391 C ATOM 555 C ASN A 103 -8.644 11.767 61.071 1.00100.74 C ANISOU 555 C ASN A 103 16196 12364 9717 563 774 -393 C ATOM 556 O ASN A 103 -8.359 10.695 60.530 1.00 99.91 O ANISOU 556 O ASN A 103 16027 12273 9660 513 767 -353 O ATOM 557 CB ASN A 103 -8.352 11.458 63.551 1.00 97.62 C ANISOU 557 CB ASN A 103 15934 11970 9187 511 807 -388 C ATOM 558 CG ASN A 103 -7.333 11.341 64.667 1.00118.95 C ANISOU 558 CG ASN A 103 18726 14651 11818 470 767 -365 C ATOM 559 OD1 ASN A 103 -6.111 11.315 64.453 1.00109.41 O ANISOU 559 OD1 ASN A 103 17534 13420 10616 437 691 -337 O ATOM 560 ND2 ASN A 103 -7.821 11.209 65.891 1.00112.69 N ANISOU 560 ND2 ASN A 103 17987 13884 10948 473 820 -378 N ATOM 561 N PHE A 104 -9.622 12.583 60.617 1.00 97.83 N ANISOU 561 N PHE A 104 15801 12022 9347 653 804 -441 N ATOM 562 CA PHE A 104 -10.440 12.269 59.442 1.00 97.67 C ANISOU 562 CA PHE A 104 15658 12073 9379 695 826 -456 C ATOM 563 C PHE A 104 -9.642 12.454 58.156 1.00100.69 C ANISOU 563 C PHE A 104 16030 12401 9826 698 760 -424 C ATOM 564 O PHE A 104 -9.660 11.558 57.306 1.00 99.65 O ANISOU 564 O PHE A 104 15801 12307 9753 662 756 -404 O ATOM 565 CB PHE A 104 -11.725 13.115 59.404 1.00100.62 C ANISOU 565 CB PHE A 104 16003 12517 9710 818 875 -520 C ATOM 566 CG PHE A 104 -12.606 12.874 58.196 1.00102.54 C ANISOU 566 CG PHE A 104 16105 12865 9989 880 891 -549 C ATOM 567 CD1 PHE A 104 -13.462 11.778 58.144 1.00106.14 C ANISOU 567 CD1 PHE A 104 16425 13447 10456 825 951 -579 C ATOM 568 CD2 PHE A 104 -12.588 13.750 57.116 1.00104.83 C ANISOU 568 CD2 PHE A 104 16407 13134 10292 989 853 -551 C ATOM 569 CE1 PHE A 104 -14.275 11.558 57.029 1.00107.28 C ANISOU 569 CE1 PHE A 104 16424 13714 10624 874 964 -620 C ATOM 570 CE2 PHE A 104 -13.400 13.529 56.001 1.00107.83 C ANISOU 570 CE2 PHE A 104 16649 13631 10691 1058 862 -581 C ATOM 571 CZ PHE A 104 -14.241 12.437 55.966 1.00106.22 C ANISOU 571 CZ PHE A 104 16290 13572 10498 998 913 -620 C ATOM 572 N TRP A 105 -8.962 13.614 58.000 1.00 97.39 N ANISOU 572 N TRP A 105 15719 11892 9395 732 717 -424 N ATOM 573 CA TRP A 105 -8.163 13.884 56.809 1.00 96.57 C ANISOU 573 CA TRP A 105 15622 11727 9344 727 663 -397 C ATOM 574 C TRP A 105 -6.899 13.010 56.790 1.00 99.05 C ANISOU 574 C TRP A 105 15922 12014 9698 609 611 -348 C ATOM 575 O TRP A 105 -6.417 12.709 55.705 1.00 98.42 O ANISOU 575 O TRP A 105 15795 11923 9678 592 576 -320 O ATOM 576 CB TRP A 105 -7.816 15.379 56.649 1.00 95.97 C ANISOU 576 CB TRP A 105 15684 11549 9231 783 653 -418 C ATOM 577 CG TRP A 105 -7.050 15.681 55.387 1.00 96.69 C ANISOU 577 CG TRP A 105 15792 11574 9370 774 612 -393 C ATOM 578 CD1 TRP A 105 -5.750 16.083 55.300 1.00 99.48 C ANISOU 578 CD1 TRP A 105 16230 11838 9730 685 573 -383 C ATOM 579 CD2 TRP A 105 -7.494 15.460 54.035 1.00 96.24 C ANISOU 579 CD2 TRP A 105 15650 11554 9362 842 607 -380 C ATOM 580 NE1 TRP A 105 -5.370 16.180 53.979 1.00 98.64 N ANISOU 580 NE1 TRP A 105 16108 11696 9673 693 550 -360 N ATOM 581 CE2 TRP A 105 -6.420 15.802 53.182 1.00 99.90 C ANISOU 581 CE2 TRP A 105 16169 11929 9859 795 568 -354 C ATOM 582 CE3 TRP A 105 -8.703 15.029 53.458 1.00 97.53 C ANISOU 582 CE3 TRP A 105 15690 11830 9535 934 634 -395 C ATOM 583 CZ2 TRP A 105 -6.520 15.729 51.785 1.00 98.82 C ANISOU 583 CZ2 TRP A 105 15981 11800 9767 847 554 -334 C ATOM 584 CZ3 TRP A 105 -8.799 14.956 52.077 1.00 98.62 C ANISOU 584 CZ3 TRP A 105 15768 11989 9713 986 615 -381 C ATOM 585 CH2 TRP A 105 -7.718 15.303 51.256 1.00 98.83 C ANISOU 585 CH2 TRP A 105 15864 11913 9774 947 575 -347 C ATOM 586 N CYS A 106 -6.402 12.557 57.965 1.00 94.68 N ANISOU 586 N CYS A 106 15405 11464 9105 543 606 -336 N ATOM 587 CA CYS A 106 -5.231 11.676 58.055 1.00 93.53 C ANISOU 587 CA CYS A 106 15247 11315 8977 460 557 -288 C ATOM 588 C CYS A 106 -5.505 10.343 57.341 1.00 97.13 C ANISOU 588 C CYS A 106 15600 11814 9492 443 575 -251 C ATOM 589 O CYS A 106 -4.729 9.966 56.463 1.00 96.40 O ANISOU 589 O CYS A 106 15472 11705 9451 415 530 -218 O ATOM 590 CB CYS A 106 -4.820 11.455 59.509 1.00 93.85 C ANISOU 590 CB CYS A 106 15350 11369 8941 424 555 -285 C ATOM 591 SG CYS A 106 -3.616 10.120 59.749 1.00 97.01 S ANISOU 591 SG CYS A 106 15727 11795 9336 367 508 -221 S ATOM 592 N GLU A 107 -6.616 9.659 57.698 1.00 93.91 N ANISOU 592 N GLU A 107 15148 11461 9073 451 647 -263 N ATOM 593 CA GLU A 107 -7.033 8.377 57.116 1.00 93.46 C ANISOU 593 CA GLU A 107 15006 11443 9060 414 689 -244 C ATOM 594 C GLU A 107 -7.462 8.526 55.653 1.00 96.82 C ANISOU 594 C GLU A 107 15339 11896 9554 444 681 -262 C ATOM 595 O GLU A 107 -7.309 7.581 54.878 1.00 96.38 O ANISOU 595 O GLU A 107 15223 11849 9547 403 685 -238 O ATOM 596 CB GLU A 107 -8.175 7.747 57.929 1.00 95.55 C ANISOU 596 CB GLU A 107 15255 11765 9284 396 785 -272 C ATOM 597 CG GLU A 107 -7.725 7.144 59.251 1.00106.27 C ANISOU 597 CG GLU A 107 16706 13096 10577 357 807 -236 C ATOM 598 CD GLU A 107 -8.756 6.382 60.064 1.00123.24 C ANISOU 598 CD GLU A 107 18860 15285 12680 320 917 -258 C ATOM 599 OE1 GLU A 107 -9.974 6.540 59.815 1.00111.74 O ANISOU 599 OE1 GLU A 107 17324 13902 11231 326 980 -321 O ATOM 600 OE2 GLU A 107 -8.337 5.647 60.985 1.00117.42 O ANISOU 600 OE2 GLU A 107 18211 14515 11889 290 943 -215 O ATOM 601 N PHE A 108 -8.000 9.701 55.281 1.00 92.84 N ANISOU 601 N PHE A 108 14832 11403 9040 526 673 -304 N ATOM 602 CA PHE A 108 -8.440 9.984 53.920 1.00 92.17 C ANISOU 602 CA PHE A 108 14669 11352 8999 583 662 -322 C ATOM 603 C PHE A 108 -7.236 10.267 53.007 1.00 92.86 C ANISOU 603 C PHE A 108 14790 11360 9134 569 589 -279 C ATOM 604 O PHE A 108 -7.229 9.818 51.862 1.00 92.30 O ANISOU 604 O PHE A 108 14643 11310 9115 567 577 -269 O ATOM 605 CB PHE A 108 -9.435 11.154 53.908 1.00 95.32 C ANISOU 605 CB PHE A 108 15076 11790 9351 704 684 -376 C ATOM 606 CG PHE A 108 -10.467 11.047 52.813 1.00 97.91 C ANISOU 606 CG PHE A 108 15278 12229 9696 775 705 -416 C ATOM 607 CD1 PHE A 108 -11.589 10.240 52.969 1.00102.21 C ANISOU 607 CD1 PHE A 108 15700 12907 10228 752 770 -466 C ATOM 608 CD2 PHE A 108 -10.312 11.741 51.620 1.00100.56 C ANISOU 608 CD2 PHE A 108 15617 12544 10049 860 664 -409 C ATOM 609 CE1 PHE A 108 -12.537 10.127 51.947 1.00103.87 C ANISOU 609 CE1 PHE A 108 15773 13251 10442 813 786 -518 C ATOM 610 CE2 PHE A 108 -11.257 11.625 50.596 1.00104.11 C ANISOU 610 CE2 PHE A 108 15941 13116 10499 939 676 -449 C ATOM 611 CZ PHE A 108 -12.363 10.819 50.766 1.00102.96 C ANISOU 611 CZ PHE A 108 15655 13124 10340 915 733 -507 C ATOM 612 N TRP A 109 -6.218 10.983 53.525 1.00 87.24 N ANISOU 612 N TRP A 109 14185 10564 8397 550 547 -263 N ATOM 613 CA TRP A 109 -4.972 11.334 52.835 1.00 85.61 C ANISOU 613 CA TRP A 109 14017 10287 8222 515 486 -235 C ATOM 614 C TRP A 109 -4.159 10.069 52.555 1.00 87.98 C ANISOU 614 C TRP A 109 14258 10602 8568 440 458 -187 C ATOM 615 O TRP A 109 -3.595 9.934 51.469 1.00 86.88 O ANISOU 615 O TRP A 109 14084 10445 8480 427 424 -166 O ATOM 616 CB TRP A 109 -4.173 12.335 53.694 1.00 84.49 C ANISOU 616 CB TRP A 109 13997 10080 8026 488 463 -250 C ATOM 617 CG TRP A 109 -2.768 12.612 53.259 1.00 84.86 C ANISOU 617 CG TRP A 109 14079 10075 8091 418 407 -236 C ATOM 618 CD1 TRP A 109 -2.372 13.416 52.231 1.00 87.66 C ANISOU 618 CD1 TRP A 109 14472 10368 8467 424 395 -242 C ATOM 619 CD2 TRP A 109 -1.569 12.195 53.926 1.00 84.55 C ANISOU 619 CD2 TRP A 109 14044 10051 8030 334 362 -222 C ATOM 620 NE1 TRP A 109 -0.998 13.471 52.174 1.00 86.93 N ANISOU 620 NE1 TRP A 109 14397 10254 8377 329 349 -238 N ATOM 621 CE2 TRP A 109 -0.479 12.729 53.205 1.00 88.32 C ANISOU 621 CE2 TRP A 109 14542 10490 8525 279 323 -228 C ATOM 622 CE3 TRP A 109 -1.308 11.398 55.056 1.00 85.81 C ANISOU 622 CE3 TRP A 109 14192 10263 8148 307 354 -206 C ATOM 623 CZ2 TRP A 109 0.852 12.488 53.569 1.00 87.61 C ANISOU 623 CZ2 TRP A 109 14440 10435 8414 196 271 -229 C ATOM 624 CZ3 TRP A 109 0.009 11.163 55.418 1.00 87.30 C ANISOU 624 CZ3 TRP A 109 14379 10481 8309 246 297 -198 C ATOM 625 CH2 TRP A 109 1.072 11.709 54.684 1.00 87.88 C ANISOU 625 CH2 TRP A 109 14451 10537 8401 190 254 -214 C ATOM 626 N THR A 110 -4.133 9.134 53.525 1.00 84.45 N ANISOU 626 N THR A 110 13809 10183 8095 400 478 -169 N ATOM 627 CA THR A 110 -3.428 7.853 53.432 1.00 83.68 C ANISOU 627 CA THR A 110 13682 10092 8020 350 466 -119 C ATOM 628 C THR A 110 -4.114 6.947 52.391 1.00 87.29 C ANISOU 628 C THR A 110 14050 10579 8537 344 506 -114 C ATOM 629 O THR A 110 -3.427 6.220 51.671 1.00 86.83 O ANISOU 629 O THR A 110 13963 10508 8521 317 482 -78 O ATOM 630 CB THR A 110 -3.355 7.188 54.816 1.00 90.70 C ANISOU 630 CB THR A 110 14623 10994 8844 331 493 -101 C ATOM 631 OG1 THR A 110 -2.858 8.129 55.764 1.00 89.60 O ANISOU 631 OG1 THR A 110 14556 10843 8643 336 459 -121 O ATOM 632 CG2 THR A 110 -2.456 5.973 54.831 1.00 90.04 C ANISOU 632 CG2 THR A 110 14543 10907 8761 307 478 -42 C ATOM 633 N SER A 111 -5.460 7.003 52.314 1.00 83.54 N ANISOU 633 N SER A 111 13527 10155 8058 369 567 -160 N ATOM 634 CA SER A 111 -6.276 6.229 51.376 1.00 82.76 C ANISOU 634 CA SER A 111 13329 10112 8002 354 612 -180 C ATOM 635 C SER A 111 -6.038 6.669 49.931 1.00 85.30 C ANISOU 635 C SER A 111 13599 10434 8379 389 563 -180 C ATOM 636 O SER A 111 -5.953 5.816 49.046 1.00 84.71 O ANISOU 636 O SER A 111 13464 10372 8350 352 570 -169 O ATOM 637 CB SER A 111 -7.753 6.361 51.723 1.00 86.89 C ANISOU 637 CB SER A 111 13799 10723 8492 376 684 -247 C ATOM 638 OG SER A 111 -8.047 5.752 52.969 1.00 95.90 O ANISOU 638 OG SER A 111 14986 11866 9585 327 748 -247 O ATOM 639 N ILE A 112 -5.924 7.996 49.698 1.00 81.16 N ANISOU 639 N ILE A 112 13113 9884 7841 459 522 -193 N ATOM 640 CA ILE A 112 -5.665 8.589 48.380 1.00 80.24 C ANISOU 640 CA ILE A 112 12978 9750 7761 505 480 -190 C ATOM 641 C ILE A 112 -4.234 8.227 47.940 1.00 83.31 C ANISOU 641 C ILE A 112 13390 10072 8191 442 427 -137 C ATOM 642 O ILE A 112 -4.038 7.835 46.788 1.00 82.95 O ANISOU 642 O ILE A 112 13290 10034 8195 436 411 -124 O ATOM 643 CB ILE A 112 -5.911 10.128 48.386 1.00 83.57 C ANISOU 643 CB ILE A 112 13475 10138 8138 600 470 -215 C ATOM 644 CG1 ILE A 112 -7.404 10.461 48.589 1.00 84.59 C ANISOU 644 CG1 ILE A 112 13558 10361 8222 693 519 -271 C ATOM 645 CG2 ILE A 112 -5.383 10.788 47.109 1.00 84.28 C ANISOU 645 CG2 ILE A 112 13590 10178 8254 639 431 -199 C ATOM 646 CD1 ILE A 112 -7.677 11.867 49.171 1.00 92.88 C ANISOU 646 CD1 ILE A 112 14720 11367 9205 788 528 -294 C ATOM 647 N ASP A 113 -3.253 8.336 48.868 1.00 79.08 N ANISOU 647 N ASP A 113 12929 9489 7630 398 400 -114 N ATOM 648 CA ASP A 113 -1.834 8.028 48.647 1.00 78.07 C ANISOU 648 CA ASP A 113 12815 9327 7523 344 347 -74 C ATOM 649 C ASP A 113 -1.657 6.608 48.099 1.00 81.55 C ANISOU 649 C ASP A 113 13187 9790 8007 313 356 -38 C ATOM 650 O ASP A 113 -0.992 6.428 47.076 1.00 80.62 O ANISOU 650 O ASP A 113 13038 9660 7936 301 324 -17 O ATOM 651 CB ASP A 113 -1.046 8.193 49.965 1.00 79.72 C ANISOU 651 CB ASP A 113 13090 9525 7673 312 324 -68 C ATOM 652 CG ASP A 113 0.471 8.244 49.849 1.00 84.17 C ANISOU 652 CG ASP A 113 13664 10081 8237 264 262 -49 C ATOM 653 OD1 ASP A 113 1.036 7.505 49.012 1.00 81.90 O ANISOU 653 OD1 ASP A 113 13321 9802 7993 251 242 -17 O ATOM 654 OD2 ASP A 113 1.098 8.965 50.647 1.00 91.78 O ANISOU 654 OD2 ASP A 113 14683 11042 9147 238 237 -73 O ATOM 655 N VAL A 114 -2.273 5.615 48.771 1.00 78.40 N ANISOU 655 N VAL A 114 12780 9417 7591 298 411 -33 N ATOM 656 CA VAL A 114 -2.221 4.198 48.411 1.00 78.08 C ANISOU 656 CA VAL A 114 12709 9381 7578 262 445 -4 C ATOM 657 C VAL A 114 -2.926 3.988 47.053 1.00 82.40 C ANISOU 657 C VAL A 114 13169 9958 8181 260 466 -30 C ATOM 658 O VAL A 114 -2.343 3.344 46.179 1.00 81.88 O ANISOU 658 O VAL A 114 13077 9876 8158 240 451 -3 O ATOM 659 CB VAL A 114 -2.806 3.302 49.542 1.00 82.40 C ANISOU 659 CB VAL A 114 13297 9933 8077 238 519 0 C ATOM 660 CG1 VAL A 114 -2.965 1.851 49.096 1.00 82.25 C ANISOU 660 CG1 VAL A 114 13269 9902 8081 193 583 20 C ATOM 661 CG2 VAL A 114 -1.943 3.375 50.801 1.00 82.44 C ANISOU 661 CG2 VAL A 114 13389 9918 8018 253 489 35 C ATOM 662 N LEU A 115 -4.141 4.571 46.864 1.00 79.40 N ANISOU 662 N LEU A 115 12742 9633 7794 291 496 -87 N ATOM 663 CA LEU A 115 -4.935 4.474 45.627 1.00 79.16 C ANISOU 663 CA LEU A 115 12615 9664 7797 305 512 -126 C ATOM 664 C LEU A 115 -4.138 4.971 44.411 1.00 84.27 C ANISOU 664 C LEU A 115 13254 10279 8487 335 446 -101 C ATOM 665 O LEU A 115 -4.237 4.371 43.341 1.00 83.53 O ANISOU 665 O LEU A 115 13094 10212 8432 318 452 -105 O ATOM 666 CB LEU A 115 -6.267 5.249 45.768 1.00 79.43 C ANISOU 666 CB LEU A 115 12603 9783 7793 367 541 -192 C ATOM 667 CG LEU A 115 -7.091 5.562 44.502 1.00 83.65 C ANISOU 667 CG LEU A 115 13036 10409 8339 426 538 -241 C ATOM 668 CD1 LEU A 115 -7.611 4.303 43.827 1.00 83.73 C ANISOU 668 CD1 LEU A 115 12945 10493 8376 349 588 -275 C ATOM 669 CD2 LEU A 115 -8.240 6.480 44.822 1.00 86.49 C ANISOU 669 CD2 LEU A 115 13367 10856 8641 521 556 -299 C ATOM 670 N CYS A 116 -3.338 6.040 44.589 1.00 82.37 N ANISOU 670 N CYS A 116 13084 9979 8233 368 393 -79 N ATOM 671 CA CYS A 116 -2.507 6.625 43.537 1.00 82.48 C ANISOU 671 CA CYS A 116 13110 9950 8277 384 341 -58 C ATOM 672 C CYS A 116 -1.385 5.665 43.126 1.00 86.82 C ANISOU 672 C CYS A 116 13644 10474 8869 322 317 -13 C ATOM 673 O CYS A 116 -1.149 5.502 41.928 1.00 86.50 O ANISOU 673 O CYS A 116 13562 10434 8869 324 301 -5 O ATOM 674 CB CYS A 116 -1.950 7.979 43.970 1.00 83.20 C ANISOU 674 CB CYS A 116 13298 9980 8333 407 311 -59 C ATOM 675 SG CYS A 116 -3.162 9.326 43.936 1.00 87.85 S ANISOU 675 SG CYS A 116 13929 10579 8871 519 337 -105 S ATOM 676 N VAL A 117 -0.717 5.020 44.107 1.00 83.54 N ANISOU 676 N VAL A 117 13263 10042 8435 282 316 16 N ATOM 677 CA VAL A 117 0.385 4.075 43.865 1.00 83.34 C ANISOU 677 CA VAL A 117 13231 10002 8432 249 294 61 C ATOM 678 C VAL A 117 -0.164 2.774 43.231 1.00 88.17 C ANISOU 678 C VAL A 117 13795 10628 9078 228 346 66 C ATOM 679 O VAL A 117 0.395 2.305 42.235 1.00 87.56 O ANISOU 679 O VAL A 117 13686 10541 9041 218 330 86 O ATOM 680 CB VAL A 117 1.212 3.801 45.158 1.00 87.24 C ANISOU 680 CB VAL A 117 13782 10491 8875 241 277 89 C ATOM 681 CG1 VAL A 117 2.283 2.730 44.937 1.00 86.79 C ANISOU 681 CG1 VAL A 117 13717 10433 8824 237 260 138 C ATOM 682 CG2 VAL A 117 1.846 5.085 45.682 1.00 87.11 C ANISOU 682 CG2 VAL A 117 13804 10470 8823 238 228 70 C ATOM 683 N THR A 118 -1.263 2.222 43.791 1.00 85.64 N ANISOU 683 N THR A 118 13473 10331 8737 211 416 40 N ATOM 684 CA THR A 118 -1.918 0.991 43.332 1.00 85.84 C ANISOU 684 CA THR A 118 13464 10369 8781 164 488 26 C ATOM 685 C THR A 118 -2.411 1.125 41.876 1.00 90.53 C ANISOU 685 C THR A 118 13968 11009 9421 165 482 -12 C ATOM 686 O THR A 118 -2.160 0.222 41.077 1.00 90.21 O ANISOU 686 O THR A 118 13907 10955 9413 130 501 -2 O ATOM 687 CB THR A 118 -3.070 0.620 44.282 1.00 94.25 C ANISOU 687 CB THR A 118 14543 11462 9805 131 571 -14 C ATOM 688 OG1 THR A 118 -2.605 0.678 45.632 1.00 93.44 O ANISOU 688 OG1 THR A 118 14530 11321 9651 146 568 22 O ATOM 689 CG2 THR A 118 -3.648 -0.763 44.000 1.00 94.15 C ANISOU 689 CG2 THR A 118 14523 11449 9798 53 668 -34 C ATOM 690 N ALA A 119 -3.083 2.246 41.534 1.00 87.61 N ANISOU 690 N ALA A 119 13553 10691 9045 216 456 -53 N ATOM 691 CA ALA A 119 -3.613 2.481 40.189 1.00 87.61 C ANISOU 691 CA ALA A 119 13469 10751 9070 242 446 -90 C ATOM 692 C ALA A 119 -2.507 2.701 39.145 1.00 91.95 C ANISOU 692 C ALA A 119 14027 11251 9659 259 385 -46 C ATOM 693 O ALA A 119 -2.701 2.308 37.998 1.00 91.72 O ANISOU 693 O ALA A 119 13936 11257 9657 252 389 -63 O ATOM 694 CB ALA A 119 -4.563 3.668 40.192 1.00 88.70 C ANISOU 694 CB ALA A 119 13578 10956 9170 325 435 -137 C ATOM 695 N SER A 120 -1.360 3.309 39.534 1.00 88.27 N ANISOU 695 N SER A 120 13633 10715 9191 271 335 1 N ATOM 696 CA SER A 120 -0.241 3.606 38.631 1.00 87.35 C ANISOU 696 CA SER A 120 13526 10557 9105 274 284 35 C ATOM 697 C SER A 120 0.457 2.337 38.112 1.00 90.97 C ANISOU 697 C SER A 120 13961 11002 9602 229 291 66 C ATOM 698 O SER A 120 0.655 2.223 36.900 1.00 90.43 O ANISOU 698 O SER A 120 13853 10939 9566 231 278 67 O ATOM 699 CB SER A 120 0.777 4.519 39.309 1.00 90.36 C ANISOU 699 CB SER A 120 13980 10888 9464 275 240 58 C ATOM 700 OG SER A 120 0.254 5.821 39.512 1.00 98.12 O ANISOU 700 OG SER A 120 15007 11862 10413 322 237 31 O ATOM 701 N ILE A 121 0.818 1.391 39.015 1.00 87.30 N ANISOU 701 N ILE A 121 13532 10516 9124 199 317 93 N ATOM 702 CA ILE A 121 1.503 0.132 38.667 1.00 86.73 C ANISOU 702 CA ILE A 121 13465 10417 9071 175 334 128 C ATOM 703 C ILE A 121 0.547 -0.826 37.915 1.00 90.24 C ANISOU 703 C ILE A 121 13868 10880 9538 134 402 94 C ATOM 704 O ILE A 121 1.003 -1.558 37.033 1.00 89.24 O ANISOU 704 O ILE A 121 13728 10736 9442 119 410 109 O ATOM 705 CB ILE A 121 2.174 -0.540 39.908 1.00 89.99 C ANISOU 705 CB ILE A 121 13950 10800 9441 182 346 172 C ATOM 706 CG1 ILE A 121 3.000 -1.803 39.542 1.00 90.39 C ANISOU 706 CG1 ILE A 121 14027 10818 9499 188 364 217 C ATOM 707 CG2 ILE A 121 1.181 -0.833 41.020 1.00 91.00 C ANISOU 707 CG2 ILE A 121 14121 10928 9529 165 409 152 C ATOM 708 CD1 ILE A 121 4.279 -1.567 38.719 1.00 98.11 C ANISOU 708 CD1 ILE A 121 14969 11807 10501 213 296 243 C ATOM 709 N TRP A 122 -0.762 -0.800 38.243 1.00 87.31 N ANISOU 709 N TRP A 122 13470 10555 9148 112 454 39 N ATOM 710 CA TRP A 122 -1.756 -1.627 37.562 1.00 87.51 C ANISOU 710 CA TRP A 122 13439 10625 9184 53 524 -18 C ATOM 711 C TRP A 122 -2.024 -1.078 36.161 1.00 90.38 C ANISOU 711 C TRP A 122 13713 11052 9576 81 484 -51 C ATOM 712 O TRP A 122 -2.287 -1.865 35.256 1.00 90.43 O ANISOU 712 O TRP A 122 13674 11083 9601 34 519 -81 O ATOM 713 CB TRP A 122 -3.054 -1.757 38.375 1.00 87.17 C ANISOU 713 CB TRP A 122 13381 10638 9103 13 596 -79 C ATOM 714 CG TRP A 122 -3.015 -2.888 39.364 1.00 88.78 C ANISOU 714 CG TRP A 122 13679 10775 9280 -50 681 -60 C ATOM 715 CD1 TRP A 122 -2.896 -2.789 40.718 1.00 91.94 C ANISOU 715 CD1 TRP A 122 14159 11136 9637 -35 695 -29 C ATOM 716 CD2 TRP A 122 -3.020 -4.292 39.061 1.00 89.16 C ANISOU 716 CD2 TRP A 122 13772 10774 9331 -130 771 -64 C ATOM 717 NE1 TRP A 122 -2.843 -4.043 41.283 1.00 91.97 N ANISOU 717 NE1 TRP A 122 14262 11070 9615 -91 788 -10 N ATOM 718 CE2 TRP A 122 -2.919 -4.985 40.290 1.00 93.61 C ANISOU 718 CE2 TRP A 122 14457 11261 9848 -152 841 -31 C ATOM 719 CE3 TRP A 122 -3.104 -5.036 37.870 1.00 90.40 C ANISOU 719 CE3 TRP A 122 13892 10938 9519 -185 805 -95 C ATOM 720 CZ2 TRP A 122 -2.912 -6.385 40.362 1.00 93.64 C ANISOU 720 CZ2 TRP A 122 14563 11183 9833 -224 953 -24 C ATOM 721 CZ3 TRP A 122 -3.088 -6.422 37.943 1.00 92.58 C ANISOU 721 CZ3 TRP A 122 14259 11135 9780 -266 913 -94 C ATOM 722 CH2 TRP A 122 -2.997 -7.083 39.177 1.00 93.75 C ANISOU 722 CH2 TRP A 122 14545 11195 9879 -284 991 -57 C ATOM 723 N THR A 123 -1.903 0.255 35.967 1.00 85.85 N ANISOU 723 N THR A 123 13128 10496 8996 157 415 -45 N ATOM 724 CA THR A 123 -2.065 0.888 34.653 1.00 85.14 C ANISOU 724 CA THR A 123 12978 10453 8917 207 375 -64 C ATOM 725 C THR A 123 -0.861 0.497 33.772 1.00 87.48 C ANISOU 725 C THR A 123 13293 10690 9258 192 345 -15 C ATOM 726 O THR A 123 -1.055 0.144 32.607 1.00 87.48 O ANISOU 726 O THR A 123 13235 10727 9275 185 349 -38 O ATOM 727 CB THR A 123 -2.255 2.411 34.791 1.00 91.51 C ANISOU 727 CB THR A 123 13807 11269 9692 299 328 -65 C ATOM 728 OG1 THR A 123 -3.497 2.661 35.454 1.00 90.60 O ANISOU 728 OG1 THR A 123 13657 11233 9533 323 361 -120 O ATOM 729 CG2 THR A 123 -2.265 3.126 33.455 1.00 89.25 C ANISOU 729 CG2 THR A 123 13495 11009 9405 368 290 -70 C ATOM 730 N LEU A 124 0.364 0.504 34.352 1.00 82.13 N ANISOU 730 N LEU A 124 12684 9933 8589 186 317 45 N ATOM 731 CA LEU A 124 1.611 0.123 33.672 1.00 80.61 C ANISOU 731 CA LEU A 124 12503 9696 8429 177 290 90 C ATOM 732 C LEU A 124 1.618 -1.364 33.302 1.00 83.04 C ANISOU 732 C LEU A 124 12802 9993 8757 129 343 91 C ATOM 733 O LEU A 124 2.247 -1.745 32.316 1.00 81.86 O ANISOU 733 O LEU A 124 12637 9831 8637 126 332 107 O ATOM 734 CB LEU A 124 2.839 0.450 34.540 1.00 80.35 C ANISOU 734 CB LEU A 124 12528 9619 8384 185 250 138 C ATOM 735 CG LEU A 124 3.220 1.922 34.678 1.00 84.41 C ANISOU 735 CG LEU A 124 13068 10124 8881 209 201 138 C ATOM 736 CD1 LEU A 124 4.231 2.110 35.776 1.00 84.47 C ANISOU 736 CD1 LEU A 124 13118 10115 8861 197 174 163 C ATOM 737 CD2 LEU A 124 3.754 2.481 33.377 1.00 86.23 C ANISOU 737 CD2 LEU A 124 13283 10346 9135 216 173 142 C ATOM 738 N CYS A 125 0.910 -2.194 34.090 1.00 79.85 N ANISOU 738 N CYS A 125 12421 9586 8332 88 411 71 N ATOM 739 CA CYS A 125 0.762 -3.632 33.863 1.00 79.84 C ANISOU 739 CA CYS A 125 12443 9556 8337 29 489 62 C ATOM 740 C CYS A 125 -0.162 -3.871 32.660 1.00 83.96 C ANISOU 740 C CYS A 125 12880 10146 8876 -15 518 -8 C ATOM 741 O CYS A 125 0.143 -4.727 31.830 1.00 84.11 O ANISOU 741 O CYS A 125 12902 10141 8916 -48 547 -8 O ATOM 742 CB CYS A 125 0.238 -4.321 35.121 1.00 80.53 C ANISOU 742 CB CYS A 125 12600 9612 8385 -10 566 57 C ATOM 743 SG CYS A 125 0.123 -6.122 34.993 1.00 84.92 S ANISOU 743 SG CYS A 125 13238 10096 8933 -90 688 51 S ATOM 744 N VAL A 126 -1.262 -3.090 32.551 1.00 80.13 N ANISOU 744 N VAL A 126 12318 9757 8373 -5 508 -70 N ATOM 745 CA VAL A 126 -2.243 -3.177 31.463 1.00 80.25 C ANISOU 745 CA VAL A 126 12229 9877 8384 -29 526 -150 C ATOM 746 C VAL A 126 -1.577 -2.793 30.127 1.00 84.15 C ANISOU 746 C VAL A 126 12693 10373 8906 21 463 -126 C ATOM 747 O VAL A 126 -1.841 -3.455 29.119 1.00 84.02 O ANISOU 747 O VAL A 126 12626 10398 8898 -22 490 -169 O ATOM 748 CB VAL A 126 -3.518 -2.336 31.759 1.00 84.49 C ANISOU 748 CB VAL A 126 12687 10536 8878 4 521 -219 C ATOM 749 CG1 VAL A 126 -4.369 -2.116 30.507 1.00 84.54 C ANISOU 749 CG1 VAL A 126 12573 10683 8867 25 508 -295 C ATOM 750 CG2 VAL A 126 -4.356 -2.987 32.855 1.00 84.96 C ANISOU 750 CG2 VAL A 126 12756 10615 8908 -78 608 -267 C ATOM 751 N ILE A 127 -0.691 -1.766 30.130 1.00 80.34 N ANISOU 751 N ILE A 127 12248 9844 8433 99 388 -63 N ATOM 752 CA ILE A 127 0.041 -1.314 28.934 1.00 79.85 C ANISOU 752 CA ILE A 127 12176 9771 8392 142 335 -35 C ATOM 753 C ILE A 127 0.938 -2.466 28.411 1.00 83.22 C ANISOU 753 C ILE A 127 12626 10138 8857 91 359 -5 C ATOM 754 O ILE A 127 0.904 -2.754 27.214 1.00 82.50 O ANISOU 754 O ILE A 127 12490 10077 8778 84 359 -27 O ATOM 755 CB ILE A 127 0.850 0.006 29.179 1.00 82.71 C ANISOU 755 CB ILE A 127 12594 10083 8750 210 271 19 C ATOM 756 CG1 ILE A 127 -0.085 1.171 29.580 1.00 83.51 C ANISOU 756 CG1 ILE A 127 12692 10234 8806 277 256 -11 C ATOM 757 CG2 ILE A 127 1.676 0.401 27.936 1.00 83.32 C ANISOU 757 CG2 ILE A 127 12674 10139 8846 236 233 47 C ATOM 758 CD1 ILE A 127 0.560 2.295 30.450 1.00 90.16 C ANISOU 758 CD1 ILE A 127 13619 11005 9632 310 224 30 C ATOM 759 N ALA A 128 1.688 -3.143 29.313 1.00 79.83 N ANISOU 759 N ALA A 128 12268 9631 8435 67 382 41 N ATOM 760 CA ALA A 128 2.577 -4.261 28.974 1.00 79.80 C ANISOU 760 CA ALA A 128 12303 9564 8452 44 410 76 C ATOM 761 C ALA A 128 1.820 -5.400 28.271 1.00 85.31 C ANISOU 761 C ALA A 128 12982 10279 9154 -29 487 18 C ATOM 762 O ALA A 128 2.291 -5.905 27.246 1.00 84.74 O ANISOU 762 O ALA A 128 12902 10193 9103 -37 491 22 O ATOM 763 CB ALA A 128 3.267 -4.785 30.225 1.00 80.54 C ANISOU 763 CB ALA A 128 12484 9590 8528 55 429 129 C ATOM 764 N VAL A 129 0.630 -5.764 28.809 1.00 82.84 N ANISOU 764 N VAL A 129 12658 10002 8815 -90 552 -44 N ATOM 765 CA VAL A 129 -0.255 -6.819 28.300 1.00 83.13 C ANISOU 765 CA VAL A 129 12674 10070 8843 -191 643 -123 C ATOM 766 C VAL A 129 -0.834 -6.399 26.924 1.00 87.53 C ANISOU 766 C VAL A 129 13111 10743 9403 -189 608 -188 C ATOM 767 O VAL A 129 -0.788 -7.201 25.986 1.00 87.04 O ANISOU 767 O VAL A 129 13040 10680 9351 -242 646 -220 O ATOM 768 CB VAL A 129 -1.361 -7.169 29.342 1.00 87.39 C ANISOU 768 CB VAL A 129 13225 10634 9345 -266 725 -181 C ATOM 769 CG1 VAL A 129 -2.434 -8.085 28.757 1.00 88.02 C ANISOU 769 CG1 VAL A 129 13258 10779 9406 -395 823 -291 C ATOM 770 CG2 VAL A 129 -0.753 -7.802 30.590 1.00 87.29 C ANISOU 770 CG2 VAL A 129 13354 10495 9319 -266 775 -113 C ATOM 771 N ASP A 130 -1.338 -5.142 26.804 1.00 84.33 N ANISOU 771 N ASP A 130 12628 10433 8981 -116 537 -205 N ATOM 772 CA ASP A 130 -1.910 -4.594 25.565 1.00 84.16 C ANISOU 772 CA ASP A 130 12501 10535 8943 -78 495 -260 C ATOM 773 C ASP A 130 -0.872 -4.531 24.441 1.00 87.65 C ANISOU 773 C ASP A 130 12961 10928 9416 -37 450 -208 C ATOM 774 O ASP A 130 -1.200 -4.863 23.299 1.00 87.30 O ANISOU 774 O ASP A 130 12852 10953 9363 -57 457 -260 O ATOM 775 CB ASP A 130 -2.513 -3.200 25.798 1.00 85.83 C ANISOU 775 CB ASP A 130 12664 10830 9116 26 433 -268 C ATOM 776 CG ASP A 130 -3.145 -2.596 24.558 1.00 93.43 C ANISOU 776 CG ASP A 130 13529 11928 10041 98 389 -320 C ATOM 777 OD1 ASP A 130 -4.185 -3.122 24.107 1.00 94.31 O ANISOU 777 OD1 ASP A 130 13538 12178 10119 47 426 -420 O ATOM 778 OD2 ASP A 130 -2.583 -1.613 24.025 1.00 97.69 O ANISOU 778 OD2 ASP A 130 14100 12438 10578 202 323 -263 O ATOM 779 N ARG A 131 0.375 -4.122 24.766 1.00 83.90 N ANISOU 779 N ARG A 131 12564 10344 8970 13 407 -114 N ATOM 780 CA ARG A 131 1.475 -4.043 23.800 1.00 83.34 C ANISOU 780 CA ARG A 131 12512 10225 8928 45 369 -64 C ATOM 781 C ARG A 131 1.921 -5.448 23.362 1.00 88.68 C ANISOU 781 C ARG A 131 13216 10850 9628 -25 429 -67 C ATOM 782 O ARG A 131 2.457 -5.589 22.259 1.00 88.41 O ANISOU 782 O ARG A 131 13168 10813 9610 -14 413 -58 O ATOM 783 CB ARG A 131 2.670 -3.235 24.351 1.00 81.55 C ANISOU 783 CB ARG A 131 12348 9920 8716 99 316 19 C ATOM 784 CG ARG A 131 2.439 -1.722 24.482 1.00 86.45 C ANISOU 784 CG ARG A 131 12969 10568 9311 171 261 27 C ATOM 785 CD ARG A 131 2.220 -1.009 23.157 1.00 91.43 C ANISOU 785 CD ARG A 131 13568 11250 9923 227 230 13 C ATOM 786 NE ARG A 131 0.796 -0.851 22.848 1.00 95.99 N ANISOU 786 NE ARG A 131 14074 11943 10455 258 237 -59 N ATOM 787 CZ ARG A 131 0.311 -0.585 21.639 1.00104.80 C ANISOU 787 CZ ARG A 131 15140 13141 11539 310 219 -92 C ATOM 788 NH1 ARG A 131 1.129 -0.454 20.601 1.00 92.47 N ANISOU 788 NH1 ARG A 131 13603 11541 9991 328 199 -56 N ATOM 789 NH2 ARG A 131 -0.996 -0.461 21.454 1.00 85.44 N ANISOU 789 NH2 ARG A 131 12606 10823 9033 348 222 -166 N ATOM 790 N TYR A 132 1.681 -6.483 24.206 1.00 85.99 N ANISOU 790 N TYR A 132 12927 10461 9283 -93 505 -80 N ATOM 791 CA TYR A 132 2.009 -7.869 23.873 1.00 86.08 C ANISOU 791 CA TYR A 132 12996 10404 9305 -156 582 -86 C ATOM 792 C TYR A 132 1.012 -8.407 22.853 1.00 89.34 C ANISOU 792 C TYR A 132 13340 10901 9705 -239 631 -187 C ATOM 793 O TYR A 132 1.429 -9.020 21.874 1.00 89.11 O ANISOU 793 O TYR A 132 13319 10851 9689 -259 650 -193 O ATOM 794 CB TYR A 132 2.055 -8.773 25.122 1.00 88.16 C ANISOU 794 CB TYR A 132 13369 10574 9554 -195 662 -65 C ATOM 795 CG TYR A 132 2.170 -10.245 24.780 1.00 91.17 C ANISOU 795 CG TYR A 132 13836 10874 9930 -266 768 -83 C ATOM 796 CD1 TYR A 132 3.397 -10.809 24.440 1.00 93.11 C ANISOU 796 CD1 TYR A 132 14157 11031 10189 -209 768 -15 C ATOM 797 CD2 TYR A 132 1.043 -11.064 24.742 1.00 92.80 C ANISOU 797 CD2 TYR A 132 14050 11098 10111 -393 874 -178 C ATOM 798 CE1 TYR A 132 3.504 -12.153 24.090 1.00 94.63 C ANISOU 798 CE1 TYR A 132 14448 11135 10370 -263 872 -30 C ATOM 799 CE2 TYR A 132 1.135 -12.407 24.381 1.00 94.33 C ANISOU 799 CE2 TYR A 132 14345 11203 10295 -471 986 -202 C ATOM 800 CZ TYR A 132 2.369 -12.948 24.059 1.00101.97 C ANISOU 800 CZ TYR A 132 15405 12063 11275 -398 986 -123 C ATOM 801 OH TYR A 132 2.470 -14.273 23.711 1.00104.59 O ANISOU 801 OH TYR A 132 15858 12291 11589 -463 1105 -144 O ATOM 802 N PHE A 133 -0.296 -8.197 23.088 1.00 85.75 N ANISOU 802 N PHE A 133 12810 10555 9217 -288 654 -273 N ATOM 803 CA PHE A 133 -1.354 -8.654 22.188 1.00 86.27 C ANISOU 803 CA PHE A 133 12783 10743 9254 -374 698 -391 C ATOM 804 C PHE A 133 -1.289 -7.953 20.831 1.00 90.61 C ANISOU 804 C PHE A 133 13240 11389 9800 -301 617 -403 C ATOM 805 O PHE A 133 -1.691 -8.543 19.832 1.00 90.25 O ANISOU 805 O PHE A 133 13140 11414 9737 -365 649 -480 O ATOM 806 CB PHE A 133 -2.736 -8.459 22.820 1.00 88.69 C ANISOU 806 CB PHE A 133 13008 11174 9515 -429 731 -486 C ATOM 807 CG PHE A 133 -3.111 -9.562 23.779 1.00 90.96 C ANISOU 807 CG PHE A 133 13379 11388 9791 -561 856 -522 C ATOM 808 CD1 PHE A 133 -3.506 -10.811 23.311 1.00 94.84 C ANISOU 808 CD1 PHE A 133 13894 11873 10268 -710 970 -609 C ATOM 809 CD2 PHE A 133 -3.073 -9.353 25.151 1.00 92.89 C ANISOU 809 CD2 PHE A 133 13695 11566 10034 -543 870 -473 C ATOM 810 CE1 PHE A 133 -3.847 -11.833 24.200 1.00 96.38 C ANISOU 810 CE1 PHE A 133 14197 11980 10444 -840 1105 -642 C ATOM 811 CE2 PHE A 133 -3.419 -10.376 26.039 1.00 96.35 C ANISOU 811 CE2 PHE A 133 14230 11925 10451 -661 996 -502 C ATOM 812 CZ PHE A 133 -3.805 -11.607 25.557 1.00 95.28 C ANISOU 812 CZ PHE A 133 14132 11771 10300 -810 1117 -586 C ATOM 813 N ALA A 134 -0.759 -6.719 20.791 1.00 87.71 N ANISOU 813 N ALA A 134 12868 11018 9440 -174 520 -328 N ATOM 814 CA ALA A 134 -0.618 -5.946 19.560 1.00 87.80 C ANISOU 814 CA ALA A 134 12823 11100 9438 -88 448 -323 C ATOM 815 C ALA A 134 0.565 -6.440 18.720 1.00 92.14 C ANISOU 815 C ALA A 134 13428 11555 10027 -91 447 -269 C ATOM 816 O ALA A 134 0.402 -6.591 17.513 1.00 92.18 O ANISOU 816 O ALA A 134 13380 11628 10016 -93 440 -311 O ATOM 817 CB ALA A 134 -0.456 -4.468 19.878 1.00 88.18 C ANISOU 817 CB ALA A 134 12880 11152 9473 37 367 -263 C ATOM 818 N ILE A 135 1.736 -6.717 19.350 1.00 88.42 N ANISOU 818 N ILE A 135 13054 10942 9598 -86 455 -182 N ATOM 819 CA ILE A 135 2.951 -7.176 18.658 1.00 87.76 C ANISOU 819 CA ILE A 135 13020 10777 9549 -76 454 -128 C ATOM 820 C ILE A 135 2.803 -8.632 18.158 1.00 91.99 C ANISOU 820 C ILE A 135 13579 11287 10088 -169 541 -180 C ATOM 821 O ILE A 135 3.488 -9.015 17.210 1.00 91.63 O ANISOU 821 O ILE A 135 13546 11212 10056 -162 543 -165 O ATOM 822 CB ILE A 135 4.230 -6.977 19.537 1.00 90.36 C ANISOU 822 CB ILE A 135 13428 10997 9906 -28 431 -29 C ATOM 823 CG1 ILE A 135 5.518 -6.901 18.685 1.00 90.52 C ANISOU 823 CG1 ILE A 135 13463 10979 9951 14 399 26 C ATOM 824 CG2 ILE A 135 4.366 -8.000 20.664 1.00 91.14 C ANISOU 824 CG2 ILE A 135 13607 11013 10008 -68 498 -14 C ATOM 825 CD1 ILE A 135 5.920 -5.493 18.241 1.00 97.58 C ANISOU 825 CD1 ILE A 135 14332 11904 10842 77 324 58 C ATOM 826 N THR A 136 1.911 -9.424 18.777 1.00 89.15 N ANISOU 826 N THR A 136 13232 10932 9708 -263 622 -246 N ATOM 827 CA THR A 136 1.690 -10.824 18.402 1.00 89.66 C ANISOU 827 CA THR A 136 13345 10956 9766 -373 728 -307 C ATOM 828 C THR A 136 0.489 -10.973 17.438 1.00 95.01 C ANISOU 828 C THR A 136 13909 11784 10405 -457 749 -437 C ATOM 829 O THR A 136 0.110 -12.101 17.111 1.00 95.61 O ANISOU 829 O THR A 136 14015 11846 10466 -578 848 -514 O ATOM 830 CB THR A 136 1.516 -11.698 19.657 1.00 95.93 C ANISOU 830 CB THR A 136 14248 11648 10551 -441 826 -305 C ATOM 831 OG1 THR A 136 0.431 -11.203 20.444 1.00 95.40 O ANISOU 831 OG1 THR A 136 14121 11668 10458 -476 827 -358 O ATOM 832 CG2 THR A 136 2.791 -11.796 20.493 1.00 93.06 C ANISOU 832 CG2 THR A 136 14003 11147 10210 -350 812 -183 C ATOM 833 N SER A 137 -0.080 -9.843 16.959 1.00 91.56 N ANISOU 833 N SER A 137 13349 11496 9944 -388 661 -464 N ATOM 834 CA SER A 137 -1.228 -9.830 16.041 1.00 92.03 C ANISOU 834 CA SER A 137 13277 11740 9949 -435 662 -589 C ATOM 835 C SER A 137 -0.804 -9.379 14.618 1.00 95.10 C ANISOU 835 C SER A 137 13619 12184 10330 -354 592 -575 C ATOM 836 O SER A 137 0.281 -8.806 14.480 1.00 93.46 O ANISOU 836 O SER A 137 13471 11881 10158 -255 535 -465 O ATOM 837 CB SER A 137 -2.344 -8.940 16.594 1.00 96.19 C ANISOU 837 CB SER A 137 13700 12417 10430 -397 622 -640 C ATOM 838 OG SER A 137 -2.344 -7.614 16.086 1.00104.86 O ANISOU 838 OG SER A 137 14738 13602 11504 -242 513 -602 O ATOM 839 N PRO A 138 -1.634 -9.596 13.554 1.00 92.62 N ANISOU 839 N PRO A 138 13197 12033 9962 -396 597 -688 N ATOM 840 CA PRO A 138 -1.230 -9.165 12.201 1.00 92.30 C ANISOU 840 CA PRO A 138 13121 12043 9904 -310 532 -671 C ATOM 841 C PRO A 138 -1.241 -7.643 12.003 1.00 96.46 C ANISOU 841 C PRO A 138 13611 12639 10400 -136 424 -610 C ATOM 842 O PRO A 138 -0.736 -7.163 10.986 1.00 96.21 O ANISOU 842 O PRO A 138 13585 12615 10356 -50 373 -570 O ATOM 843 CB PRO A 138 -2.267 -9.838 11.288 1.00 95.14 C ANISOU 843 CB PRO A 138 13366 12582 10199 -409 572 -825 C ATOM 844 CG PRO A 138 -2.963 -10.860 12.143 1.00100.22 C ANISOU 844 CG PRO A 138 14017 13219 10842 -582 682 -918 C ATOM 845 CD PRO A 138 -2.946 -10.273 13.508 1.00 95.34 C ANISOU 845 CD PRO A 138 13442 12532 10250 -530 666 -845 C ATOM 846 N PHE A 139 -1.800 -6.890 12.968 1.00 93.07 N ANISOU 846 N PHE A 139 13161 12249 9954 -83 397 -601 N ATOM 847 CA PHE A 139 -1.877 -5.426 12.941 1.00 92.58 C ANISOU 847 CA PHE A 139 13091 12231 9853 85 311 -544 C ATOM 848 C PHE A 139 -0.552 -4.819 13.421 1.00 95.01 C ANISOU 848 C PHE A 139 13532 12343 10224 141 285 -403 C ATOM 849 O PHE A 139 -0.261 -3.661 13.127 1.00 94.29 O ANISOU 849 O PHE A 139 13477 12242 10108 266 227 -341 O ATOM 850 CB PHE A 139 -3.068 -4.942 13.783 1.00 94.96 C ANISOU 850 CB PHE A 139 13316 12663 10103 114 303 -604 C ATOM 851 CG PHE A 139 -4.371 -5.583 13.357 1.00 97.80 C ANISOU 851 CG PHE A 139 13523 13242 10392 38 334 -761 C ATOM 852 CD1 PHE A 139 -5.050 -5.135 12.230 1.00101.65 C ANISOU 852 CD1 PHE A 139 13901 13933 10788 136 281 -828 C ATOM 853 CD2 PHE A 139 -4.894 -6.665 14.056 1.00100.62 C ANISOU 853 CD2 PHE A 139 13852 13611 10768 -136 424 -848 C ATOM 854 CE1 PHE A 139 -6.239 -5.747 11.820 1.00103.93 C ANISOU 854 CE1 PHE A 139 14029 14457 11003 57 309 -990 C ATOM 855 CE2 PHE A 139 -6.085 -7.274 13.647 1.00104.72 C ANISOU 855 CE2 PHE A 139 14224 14347 11217 -233 464 -1011 C ATOM 856 CZ PHE A 139 -6.750 -6.809 12.533 1.00103.54 C ANISOU 856 CZ PHE A 139 13943 14422 10977 -139 403 -1086 C ATOM 857 N LYS A 140 0.251 -5.638 14.133 1.00 90.97 N ANISOU 857 N LYS A 140 13097 11684 9785 48 336 -361 N ATOM 858 CA LYS A 140 1.598 -5.433 14.682 1.00 89.80 C ANISOU 858 CA LYS A 140 13056 11366 9697 67 326 -248 C ATOM 859 C LYS A 140 1.739 -4.264 15.687 1.00 94.67 C ANISOU 859 C LYS A 140 13715 11942 10313 142 283 -185 C ATOM 860 O LYS A 140 2.333 -4.488 16.743 1.00 94.60 O ANISOU 860 O LYS A 140 13765 11832 10345 109 301 -138 O ATOM 861 CB LYS A 140 2.660 -5.290 13.584 1.00 90.78 C ANISOU 861 CB LYS A 140 13217 11439 9839 104 303 -194 C ATOM 862 CG LYS A 140 3.807 -6.270 13.788 1.00 91.39 C ANISOU 862 CG LYS A 140 13360 11388 9976 42 347 -148 C ATOM 863 CD LYS A 140 5.060 -5.879 13.033 1.00 94.53 C ANISOU 863 CD LYS A 140 13797 11725 10394 89 318 -78 C ATOM 864 CE LYS A 140 6.226 -6.743 13.439 1.00 98.73 C ANISOU 864 CE LYS A 140 14388 12150 10977 55 354 -29 C ATOM 865 NZ LYS A 140 7.504 -6.273 12.843 1.00104.94 N ANISOU 865 NZ LYS A 140 15198 12894 11780 96 326 34 N ATOM 866 N TYR A 141 1.260 -3.040 15.377 1.00 91.29 N ANISOU 866 N TYR A 141 13270 11583 9832 250 231 -182 N ATOM 867 CA TYR A 141 1.434 -1.915 16.308 1.00 90.69 C ANISOU 867 CA TYR A 141 13256 11451 9751 316 201 -125 C ATOM 868 C TYR A 141 0.103 -1.229 16.691 1.00 94.24 C ANISOU 868 C TYR A 141 13653 12021 10133 389 183 -178 C ATOM 869 O TYR A 141 0.117 -0.133 17.259 1.00 93.81 O ANISOU 869 O TYR A 141 13657 11930 10056 469 158 -136 O ATOM 870 CB TYR A 141 2.436 -0.895 15.736 1.00 91.74 C ANISOU 870 CB TYR A 141 13473 11503 9881 385 168 -48 C ATOM 871 CG TYR A 141 3.766 -1.512 15.355 1.00 93.22 C ANISOU 871 CG TYR A 141 13696 11596 10128 320 184 -2 C ATOM 872 CD1 TYR A 141 4.654 -1.962 16.328 1.00 94.79 C ANISOU 872 CD1 TYR A 141 13931 11703 10382 257 200 38 C ATOM 873 CD2 TYR A 141 4.119 -1.684 14.020 1.00 94.13 C ANISOU 873 CD2 TYR A 141 13802 11728 10234 332 182 -3 C ATOM 874 CE1 TYR A 141 5.867 -2.556 15.982 1.00 95.27 C ANISOU 874 CE1 TYR A 141 14012 11701 10485 216 214 75 C ATOM 875 CE2 TYR A 141 5.338 -2.258 13.662 1.00 94.63 C ANISOU 875 CE2 TYR A 141 13892 11717 10348 279 199 35 C ATOM 876 CZ TYR A 141 6.206 -2.698 14.646 1.00101.74 C ANISOU 876 CZ TYR A 141 14820 12535 11299 225 214 72 C ATOM 877 OH TYR A 141 7.404 -3.272 14.298 1.00102.64 O ANISOU 877 OH TYR A 141 14949 12597 11451 193 229 105 O ATOM 878 N GLN A 142 -1.033 -1.901 16.435 1.00 90.74 N ANISOU 878 N GLN A 142 13099 11725 9654 356 204 -277 N ATOM 879 CA GLN A 142 -2.364 -1.400 16.774 1.00 91.03 C ANISOU 879 CA GLN A 142 13056 11914 9618 423 191 -346 C ATOM 880 C GLN A 142 -2.990 -2.259 17.859 1.00 94.41 C ANISOU 880 C GLN A 142 13434 12370 10068 303 247 -409 C ATOM 881 O GLN A 142 -2.950 -3.490 17.772 1.00 94.04 O ANISOU 881 O GLN A 142 13363 12314 10055 168 304 -454 O ATOM 882 CB GLN A 142 -3.271 -1.354 15.537 1.00 93.43 C ANISOU 882 CB GLN A 142 13249 12412 9838 492 167 -429 C ATOM 883 CG GLN A 142 -3.122 -0.088 14.699 1.00111.22 C ANISOU 883 CG GLN A 142 15557 14676 12025 673 109 -374 C ATOM 884 CD GLN A 142 -3.751 -0.219 13.330 1.00134.56 C ANISOU 884 CD GLN A 142 18416 17809 14899 738 84 -445 C ATOM 885 OE1 GLN A 142 -3.081 -0.073 12.304 1.00131.20 O ANISOU 885 OE1 GLN A 142 18045 17335 14470 777 68 -400 O ATOM 886 NE2 GLN A 142 -5.052 -0.492 13.273 1.00127.32 N ANISOU 886 NE2 GLN A 142 17349 17118 13909 751 82 -563 N ATOM 887 N SER A 143 -3.555 -1.605 18.890 1.00 91.01 N ANISOU 887 N SER A 143 13004 11963 9612 352 240 -410 N ATOM 888 CA SER A 143 -4.215 -2.257 20.022 1.00 90.97 C ANISOU 888 CA SER A 143 12961 11986 9616 249 296 -467 C ATOM 889 C SER A 143 -5.468 -2.980 19.549 1.00 96.15 C ANISOU 889 C SER A 143 13466 12848 10217 181 334 -608 C ATOM 890 O SER A 143 -6.229 -2.433 18.749 1.00 97.22 O ANISOU 890 O SER A 143 13503 13160 10275 284 291 -666 O ATOM 891 CB SER A 143 -4.562 -1.233 21.099 1.00 94.06 C ANISOU 891 CB SER A 143 13384 12372 9982 338 273 -439 C ATOM 892 OG SER A 143 -5.414 -1.779 22.093 1.00101.98 O ANISOU 892 OG SER A 143 14331 13440 10975 250 328 -510 O ATOM 893 N LEU A 144 -5.679 -4.209 20.039 1.00 92.11 N ANISOU 893 N LEU A 144 12943 12319 9736 9 419 -667 N ATOM 894 CA LEU A 144 -6.835 -5.024 19.662 1.00 92.64 C ANISOU 894 CA LEU A 144 12871 12576 9750 -103 477 -819 C ATOM 895 C LEU A 144 -8.110 -4.568 20.400 1.00 97.05 C ANISOU 895 C LEU A 144 13319 13314 10242 -78 483 -906 C ATOM 896 O LEU A 144 -9.197 -5.068 20.108 1.00 97.71 O ANISOU 896 O LEU A 144 13257 13604 10265 -161 525 -1051 O ATOM 897 CB LEU A 144 -6.555 -6.519 19.901 1.00 92.68 C ANISOU 897 CB LEU A 144 12936 12472 9805 -308 587 -851 C ATOM 898 CG LEU A 144 -5.359 -7.129 19.141 1.00 96.54 C ANISOU 898 CG LEU A 144 13527 12803 10353 -336 593 -780 C ATOM 899 CD1 LEU A 144 -5.062 -8.514 19.636 1.00 97.11 C ANISOU 899 CD1 LEU A 144 13697 12735 10463 -508 711 -794 C ATOM 900 CD2 LEU A 144 -5.593 -7.165 17.634 1.00 98.75 C ANISOU 900 CD2 LEU A 144 13708 13220 10592 -314 560 -846 C ATOM 901 N LEU A 145 -7.978 -3.596 21.323 1.00 93.18 N ANISOU 901 N LEU A 145 12891 12758 9756 35 443 -827 N ATOM 902 CA LEU A 145 -9.098 -3.017 22.067 1.00 93.68 C ANISOU 902 CA LEU A 145 12863 12978 9753 89 443 -894 C ATOM 903 C LEU A 145 -9.570 -1.736 21.388 1.00 97.64 C ANISOU 903 C LEU A 145 13298 13632 10171 313 349 -894 C ATOM 904 O LEU A 145 -8.760 -1.025 20.789 1.00 96.40 O ANISOU 904 O LEU A 145 13234 13369 10025 437 286 -794 O ATOM 905 CB LEU A 145 -8.705 -2.713 23.531 1.00 92.99 C ANISOU 905 CB LEU A 145 12896 12725 9710 85 461 -810 C ATOM 906 CG LEU A 145 -8.315 -3.885 24.436 1.00 97.31 C ANISOU 906 CG LEU A 145 13531 13122 10321 -103 558 -801 C ATOM 907 CD1 LEU A 145 -7.475 -3.405 25.604 1.00 96.42 C ANISOU 907 CD1 LEU A 145 13566 12813 10255 -58 542 -678 C ATOM 908 CD2 LEU A 145 -9.541 -4.625 24.949 1.00101.16 C ANISOU 908 CD2 LEU A 145 13911 13760 10763 -246 652 -941 C ATOM 909 N THR A 146 -10.875 -1.439 21.491 1.00 95.33 N ANISOU 909 N THR A 146 12849 13587 9783 369 347 -1009 N ATOM 910 CA THR A 146 -11.470 -0.210 20.956 1.00 95.73 C ANISOU 910 CA THR A 146 12839 13804 9731 612 265 -1015 C ATOM 911 C THR A 146 -11.333 0.901 21.998 1.00 99.45 C ANISOU 911 C THR A 146 13423 14163 10199 748 240 -923 C ATOM 912 O THR A 146 -11.022 0.615 23.157 1.00 98.51 O ANISOU 912 O THR A 146 13381 13899 10148 636 288 -888 O ATOM 913 CB THR A 146 -12.939 -0.427 20.557 1.00105.16 C ANISOU 913 CB THR A 146 13797 15349 10809 625 271 -1191 C ATOM 914 OG1 THR A 146 -13.679 -0.915 21.675 1.00104.35 O ANISOU 914 OG1 THR A 146 13620 15321 10708 489 345 -1279 O ATOM 915 CG2 THR A 146 -13.097 -1.360 19.368 1.00105.09 C ANISOU 915 CG2 THR A 146 13673 15475 10781 514 286 -1290 C ATOM 916 N LYS A 147 -11.578 2.161 21.596 1.00 96.78 N ANISOU 916 N LYS A 147 13108 13890 9776 993 171 -887 N ATOM 917 CA LYS A 147 -11.500 3.330 22.481 1.00 96.68 C ANISOU 917 CA LYS A 147 13217 13773 9743 1140 152 -806 C ATOM 918 C LYS A 147 -12.573 3.277 23.590 1.00101.09 C ANISOU 918 C LYS A 147 13668 14480 10262 1119 190 -896 C ATOM 919 O LYS A 147 -12.373 3.874 24.648 1.00100.31 O ANISOU 919 O LYS A 147 13680 14250 10183 1153 199 -833 O ATOM 920 CB LYS A 147 -11.621 4.639 21.683 1.00100.34 C ANISOU 920 CB LYS A 147 13743 14281 10103 1417 86 -757 C ATOM 921 CG LYS A 147 -10.419 4.946 20.790 1.00115.87 C ANISOU 921 CG LYS A 147 15867 16048 12110 1448 58 -644 C ATOM 922 CD LYS A 147 -10.532 6.333 20.180 1.00127.86 C ANISOU 922 CD LYS A 147 17494 17570 13516 1725 13 -584 C ATOM 923 CE LYS A 147 -9.481 6.586 19.131 1.00139.95 C ANISOU 923 CE LYS A 147 19164 18943 15069 1752 -6 -492 C ATOM 924 NZ LYS A 147 -9.614 7.945 18.542 1.00151.27 N ANISOU 924 NZ LYS A 147 20733 20364 16379 2025 -34 -432 N ATOM 925 N ASN A 148 -13.692 2.550 23.349 1.00 98.49 N ANISOU 925 N ASN A 148 13122 14427 9873 1049 217 -1050 N ATOM 926 CA ASN A 148 -14.791 2.361 24.305 1.00 99.05 C ANISOU 926 CA ASN A 148 13060 14676 9899 1000 265 -1161 C ATOM 927 C ASN A 148 -14.425 1.308 25.353 1.00100.57 C ANISOU 927 C ASN A 148 13302 14710 10198 732 356 -1162 C ATOM 928 O ASN A 148 -14.763 1.476 26.525 1.00 99.94 O ANISOU 928 O ASN A 148 13239 14613 10120 710 393 -1168 O ATOM 929 CB ASN A 148 -16.084 1.952 23.586 1.00103.68 C ANISOU 929 CB ASN A 148 13386 15637 10373 1007 267 -1341 C ATOM 930 CG ASN A 148 -16.552 2.912 22.517 1.00137.67 C ANISOU 930 CG ASN A 148 17624 20137 14546 1292 178 -1352 C ATOM 931 OD1 ASN A 148 -16.560 4.138 22.693 1.00136.01 O ANISOU 931 OD1 ASN A 148 17513 19886 14277 1539 129 -1271 O ATOM 932 ND2 ASN A 148 -16.990 2.366 21.390 1.00131.07 N ANISOU 932 ND2 ASN A 148 16624 19526 13651 1268 162 -1459 N ATOM 933 N LYS A 149 -13.744 0.219 24.923 1.00 95.47 N ANISOU 933 N LYS A 149 12690 13949 9634 539 395 -1155 N ATOM 934 CA LYS A 149 -13.297 -0.879 25.786 1.00 94.06 C ANISOU 934 CA LYS A 149 12589 13602 9549 297 488 -1146 C ATOM 935 C LYS A 149 -12.184 -0.415 26.725 1.00 94.78 C ANISOU 935 C LYS A 149 12892 13400 9719 328 473 -987 C ATOM 936 O LYS A 149 -12.212 -0.764 27.902 1.00 94.31 O ANISOU 936 O LYS A 149 12885 13259 9690 224 535 -982 O ATOM 937 CB LYS A 149 -12.828 -2.083 24.955 1.00 96.64 C ANISOU 937 CB LYS A 149 12914 13880 9927 121 531 -1174 C ATOM 938 CG LYS A 149 -13.967 -2.910 24.368 1.00117.89 C ANISOU 938 CG LYS A 149 15398 16847 12548 -8 588 -1362 C ATOM 939 CD LYS A 149 -13.445 -4.025 23.459 1.00130.94 C ANISOU 939 CD LYS A 149 17070 18433 14246 -171 630 -1385 C ATOM 940 CE LYS A 149 -14.552 -4.835 22.823 1.00143.62 C ANISOU 940 CE LYS A 149 18472 20320 15777 -317 692 -1585 C ATOM 941 NZ LYS A 149 -15.241 -4.087 21.735 1.00152.85 N ANISOU 941 NZ LYS A 149 19461 21774 16839 -133 595 -1659 N ATOM 942 N ALA A 150 -11.226 0.390 26.212 1.00 89.17 N ANISOU 942 N ALA A 150 12303 12544 9033 467 396 -866 N ATOM 943 CA ALA A 150 -10.108 0.947 26.981 1.00 87.39 C ANISOU 943 CA ALA A 150 12268 12065 8873 501 375 -726 C ATOM 944 C ALA A 150 -10.612 1.831 28.132 1.00 91.03 C ANISOU 944 C ALA A 150 12755 12539 9292 594 373 -718 C ATOM 945 O ALA A 150 -10.073 1.742 29.236 1.00 90.09 O ANISOU 945 O ALA A 150 12745 12261 9223 525 400 -659 O ATOM 946 CB ALA A 150 -9.189 1.743 26.070 1.00 87.44 C ANISOU 946 CB ALA A 150 12372 11962 8888 631 302 -627 C ATOM 947 N ARG A 151 -11.675 2.643 27.879 1.00 87.84 N ANISOU 947 N ARG A 151 12249 12338 8788 758 342 -784 N ATOM 948 CA ARG A 151 -12.328 3.526 28.858 1.00 87.74 C ANISOU 948 CA ARG A 151 12245 12375 8718 873 342 -793 C ATOM 949 C ARG A 151 -12.915 2.720 30.024 1.00 90.99 C ANISOU 949 C ARG A 151 12594 12834 9144 707 424 -865 C ATOM 950 O ARG A 151 -12.901 3.189 31.163 1.00 90.31 O ANISOU 950 O ARG A 151 12587 12666 9059 730 438 -829 O ATOM 951 CB ARG A 151 -13.438 4.358 28.190 1.00 89.58 C ANISOU 951 CB ARG A 151 12355 12858 8824 1090 299 -867 C ATOM 952 CG ARG A 151 -12.938 5.564 27.404 1.00101.53 C ANISOU 952 CG ARG A 151 13993 14288 10294 1313 228 -773 C ATOM 953 CD ARG A 151 -14.088 6.365 26.821 1.00114.72 C ANISOU 953 CD ARG A 151 15554 16215 11821 1557 190 -844 C ATOM 954 NE ARG A 151 -13.619 7.483 25.999 1.00126.49 N ANISOU 954 NE ARG A 151 17191 17613 13258 1777 136 -751 N ATOM 955 CZ ARG A 151 -13.488 7.442 24.676 1.00144.03 C ANISOU 955 CZ ARG A 151 19384 19897 15444 1848 97 -750 C ATOM 956 NH1 ARG A 151 -13.788 6.337 24.005 1.00132.77 N ANISOU 956 NH1 ARG A 151 17781 18634 14033 1713 102 -842 N ATOM 957 NH2 ARG A 151 -13.058 8.508 24.013 1.00131.79 N ANISOU 957 NH2 ARG A 151 17997 18242 13837 2049 62 -660 N ATOM 958 N VAL A 152 -13.424 1.506 29.729 1.00 87.44 N ANISOU 958 N VAL A 152 12012 12509 8700 533 485 -971 N ATOM 959 CA VAL A 152 -14.002 0.580 30.703 1.00 87.47 C ANISOU 959 CA VAL A 152 11965 12557 8713 344 585 -1052 C ATOM 960 C VAL A 152 -12.867 0.000 31.553 1.00 89.86 C ANISOU 960 C VAL A 152 12455 12575 9113 210 626 -944 C ATOM 961 O VAL A 152 -13.000 -0.037 32.772 1.00 89.32 O ANISOU 961 O VAL A 152 12440 12449 9047 161 673 -935 O ATOM 962 CB VAL A 152 -14.852 -0.520 30.008 1.00 92.45 C ANISOU 962 CB VAL A 152 12413 13403 9311 186 650 -1207 C ATOM 963 CG1 VAL A 152 -15.320 -1.591 30.993 1.00 92.75 C ANISOU 963 CG1 VAL A 152 12436 13443 9362 -46 778 -1287 C ATOM 964 CG2 VAL A 152 -16.044 0.091 29.278 1.00 93.76 C ANISOU 964 CG2 VAL A 152 12371 13895 9361 335 605 -1328 C ATOM 965 N ILE A 153 -11.748 -0.417 30.912 1.00 85.80 N ANISOU 965 N ILE A 153 12038 11895 8668 168 604 -862 N ATOM 966 CA ILE A 153 -10.559 -0.980 31.571 1.00 84.91 C ANISOU 966 CA ILE A 153 12097 11529 8636 70 630 -756 C ATOM 967 C ILE A 153 -9.997 0.040 32.578 1.00 89.22 C ANISOU 967 C ILE A 153 12769 11942 9191 179 584 -655 C ATOM 968 O ILE A 153 -9.772 -0.327 33.729 1.00 88.84 O ANISOU 968 O ILE A 153 12804 11790 9161 101 633 -626 O ATOM 969 CB ILE A 153 -9.476 -1.447 30.539 1.00 87.19 C ANISOU 969 CB ILE A 153 12445 11698 8984 44 601 -692 C ATOM 970 CG1 ILE A 153 -10.007 -2.529 29.550 1.00 88.31 C ANISOU 970 CG1 ILE A 153 12475 11963 9117 -82 656 -798 C ATOM 971 CG2 ILE A 153 -8.169 -1.900 31.212 1.00 86.75 C ANISOU 971 CG2 ILE A 153 12561 11401 8998 -16 614 -576 C ATOM 972 CD1 ILE A 153 -10.539 -3.890 30.148 1.00 97.13 C ANISOU 972 CD1 ILE A 153 13584 13088 10233 -299 790 -884 C ATOM 973 N ILE A 154 -9.823 1.316 32.157 1.00 86.27 N ANISOU 973 N ILE A 154 12415 11573 8792 358 498 -609 N ATOM 974 CA ILE A 154 -9.314 2.407 33.001 1.00 86.10 C ANISOU 974 CA ILE A 154 12518 11429 8768 461 458 -526 C ATOM 975 C ILE A 154 -10.268 2.636 34.189 1.00 91.77 C ANISOU 975 C ILE A 154 13203 12229 9436 468 501 -581 C ATOM 976 O ILE A 154 -9.797 2.809 35.314 1.00 91.59 O ANISOU 976 O ILE A 154 13290 12080 9432 444 513 -525 O ATOM 977 CB ILE A 154 -9.071 3.706 32.176 1.00 89.22 C ANISOU 977 CB ILE A 154 12953 11817 9130 646 379 -481 C ATOM 978 CG1 ILE A 154 -7.893 3.518 31.198 1.00 88.97 C ANISOU 978 CG1 ILE A 154 12986 11663 9155 622 343 -410 C ATOM 979 CG2 ILE A 154 -8.833 4.929 33.077 1.00 89.76 C ANISOU 979 CG2 ILE A 154 13146 11787 9173 752 356 -424 C ATOM 980 CD1 ILE A 154 -7.971 4.356 29.922 1.00 99.23 C ANISOU 980 CD1 ILE A 154 14276 13017 10410 774 288 -404 C ATOM 981 N LEU A 155 -11.593 2.596 33.946 1.00 89.50 N ANISOU 981 N LEU A 155 12758 12167 9082 495 527 -695 N ATOM 982 CA LEU A 155 -12.600 2.772 34.993 1.00 90.21 C ANISOU 982 CA LEU A 155 12791 12367 9116 499 575 -764 C ATOM 983 C LEU A 155 -12.583 1.602 35.979 1.00 94.01 C ANISOU 983 C LEU A 155 13299 12785 9634 294 670 -783 C ATOM 984 O LEU A 155 -12.660 1.840 37.183 1.00 93.68 O ANISOU 984 O LEU A 155 13324 12688 9582 289 698 -764 O ATOM 985 CB LEU A 155 -13.996 2.949 34.385 1.00 91.73 C ANISOU 985 CB LEU A 155 12784 12850 9219 577 579 -895 C ATOM 986 CG LEU A 155 -14.613 4.344 34.513 1.00 97.38 C ANISOU 986 CG LEU A 155 13487 13664 9848 812 528 -899 C ATOM 987 CD1 LEU A 155 -13.908 5.361 33.618 1.00 97.02 C ANISOU 987 CD1 LEU A 155 13546 13521 9796 995 441 -807 C ATOM 988 CD2 LEU A 155 -16.081 4.310 34.161 1.00102.12 C ANISOU 988 CD2 LEU A 155 13865 14587 10348 870 546 -1048 C ATOM 989 N MET A 156 -12.429 0.355 35.481 1.00 90.57 N ANISOU 989 N MET A 156 12836 12340 9236 132 724 -815 N ATOM 990 CA MET A 156 -12.362 -0.850 36.318 1.00 90.52 C ANISOU 990 CA MET A 156 12889 12248 9255 -63 831 -827 C ATOM 991 C MET A 156 -11.105 -0.841 37.182 1.00 91.33 C ANISOU 991 C MET A 156 13188 12104 9411 -62 815 -692 C ATOM 992 O MET A 156 -11.182 -1.217 38.350 1.00 91.03 O ANISOU 992 O MET A 156 13222 12002 9363 -136 881 -684 O ATOM 993 CB MET A 156 -12.414 -2.138 35.474 1.00 93.63 C ANISOU 993 CB MET A 156 13235 12668 9671 -225 898 -889 C ATOM 994 CG MET A 156 -13.803 -2.484 34.943 1.00 99.43 C ANISOU 994 CG MET A 156 13767 13670 10342 -298 955 -1058 C ATOM 995 SD MET A 156 -15.129 -2.564 36.185 1.00105.80 S ANISOU 995 SD MET A 156 14489 14633 11077 -380 1059 -1175 S ATOM 996 CE MET A 156 -14.622 -4.016 37.132 1.00102.52 C ANISOU 996 CE MET A 156 14257 13993 10702 -618 1206 -1142 C ATOM 997 N VAL A 157 -9.961 -0.382 36.612 1.00 85.49 N ANISOU 997 N VAL A 157 12527 11239 8716 23 727 -592 N ATOM 998 CA VAL A 157 -8.661 -0.273 37.285 1.00 83.88 C ANISOU 998 CA VAL A 157 12486 10831 8553 38 694 -471 C ATOM 999 C VAL A 157 -8.807 0.644 38.517 1.00 87.50 C ANISOU 999 C VAL A 157 13000 11269 8977 110 679 -448 C ATOM 1000 O VAL A 157 -8.407 0.245 39.606 1.00 86.86 O ANISOU 1000 O VAL A 157 13018 11087 8898 54 716 -406 O ATOM 1001 CB VAL A 157 -7.538 0.202 36.308 1.00 86.60 C ANISOU 1001 CB VAL A 157 12872 11091 8940 116 604 -393 C ATOM 1002 CG1 VAL A 157 -6.311 0.734 37.049 1.00 85.68 C ANISOU 1002 CG1 VAL A 157 12892 10816 8845 159 553 -288 C ATOM 1003 CG2 VAL A 157 -7.130 -0.915 35.354 1.00 86.12 C ANISOU 1003 CG2 VAL A 157 12797 11005 8921 25 631 -396 C ATOM 1004 N TRP A 158 -9.438 1.823 38.349 1.00 84.23 N ANISOU 1004 N TRP A 158 12528 10955 8521 240 632 -479 N ATOM 1005 CA TRP A 158 -9.649 2.811 39.407 1.00 84.20 C ANISOU 1005 CA TRP A 158 12578 10937 8477 325 617 -465 C ATOM 1006 C TRP A 158 -10.702 2.385 40.443 1.00 88.24 C ANISOU 1006 C TRP A 158 13043 11540 8945 256 703 -539 C ATOM 1007 O TRP A 158 -10.532 2.707 41.621 1.00 87.99 O ANISOU 1007 O TRP A 158 13099 11436 8897 264 714 -505 O ATOM 1008 CB TRP A 158 -10.037 4.165 38.806 1.00 83.31 C ANISOU 1008 CB TRP A 158 12436 10898 8322 500 553 -477 C ATOM 1009 CG TRP A 158 -8.869 4.923 38.253 1.00 83.53 C ANISOU 1009 CG TRP A 158 12572 10786 8379 572 479 -389 C ATOM 1010 CD1 TRP A 158 -8.382 4.866 36.981 1.00 85.97 C ANISOU 1010 CD1 TRP A 158 12864 11084 8717 591 439 -367 C ATOM 1011 CD2 TRP A 158 -8.028 5.837 38.966 1.00 83.07 C ANISOU 1011 CD2 TRP A 158 12657 10585 8321 616 444 -319 C ATOM 1012 NE1 TRP A 158 -7.296 5.698 36.852 1.00 84.89 N ANISOU 1012 NE1 TRP A 158 12852 10804 8597 643 387 -288 N ATOM 1013 CE2 TRP A 158 -7.053 6.306 38.056 1.00 86.38 C ANISOU 1013 CE2 TRP A 158 13140 10913 8769 653 390 -261 C ATOM 1014 CE3 TRP A 158 -8.006 6.316 40.287 1.00 84.53 C ANISOU 1014 CE3 TRP A 158 12924 10715 8479 621 458 -306 C ATOM 1015 CZ2 TRP A 158 -6.069 7.231 38.424 1.00 85.44 C ANISOU 1015 CZ2 TRP A 158 13159 10654 8650 679 356 -201 C ATOM 1016 CZ3 TRP A 158 -7.029 7.230 40.652 1.00 85.65 C ANISOU 1016 CZ3 TRP A 158 13202 10721 8622 654 418 -245 C ATOM 1017 CH2 TRP A 158 -6.075 7.678 39.727 1.00 85.84 C ANISOU 1017 CH2 TRP A 158 13283 10660 8673 676 371 -197 C ATOM 1018 N ILE A 159 -11.779 1.687 40.021 1.00 84.83 N ANISOU 1018 N ILE A 159 12469 11274 8488 184 768 -646 N ATOM 1019 CA ILE A 159 -12.845 1.235 40.927 1.00 85.45 C ANISOU 1019 CA ILE A 159 12488 11460 8519 97 865 -733 C ATOM 1020 C ILE A 159 -12.315 0.115 41.837 1.00 89.65 C ANISOU 1020 C ILE A 159 13145 11841 9078 -62 948 -691 C ATOM 1021 O ILE A 159 -12.458 0.216 43.056 1.00 89.14 O ANISOU 1021 O ILE A 159 13148 11736 8985 -76 988 -679 O ATOM 1022 CB ILE A 159 -14.139 0.813 40.157 1.00 89.50 C ANISOU 1022 CB ILE A 159 12799 12218 8987 48 915 -878 C ATOM 1023 CG1 ILE A 159 -14.883 2.053 39.613 1.00 90.32 C ANISOU 1023 CG1 ILE A 159 12784 12503 9030 247 841 -925 C ATOM 1024 CG2 ILE A 159 -15.084 -0.035 41.035 1.00 91.13 C ANISOU 1024 CG2 ILE A 159 12956 12515 9156 -114 1046 -976 C ATOM 1025 CD1 ILE A 159 -15.838 1.790 38.426 1.00 98.50 C ANISOU 1025 CD1 ILE A 159 13614 13791 10022 250 846 -1050 C ATOM 1026 N VAL A 160 -11.705 -0.934 41.247 1.00 86.87 N ANISOU 1026 N VAL A 160 12832 11403 8771 -167 977 -667 N ATOM 1027 CA VAL A 160 -11.167 -2.088 41.975 1.00 87.25 C ANISOU 1027 CA VAL A 160 13019 11300 8832 -299 1064 -622 C ATOM 1028 C VAL A 160 -10.044 -1.630 42.930 1.00 91.86 C ANISOU 1028 C VAL A 160 13763 11714 9427 -218 1006 -497 C ATOM 1029 O VAL A 160 -10.079 -2.004 44.107 1.00 91.81 O ANISOU 1029 O VAL A 160 13852 11644 9389 -267 1073 -479 O ATOM 1030 CB VAL A 160 -10.715 -3.220 41.014 1.00 90.91 C ANISOU 1030 CB VAL A 160 13500 11705 9335 -400 1103 -619 C ATOM 1031 CG1 VAL A 160 -9.930 -4.309 41.745 1.00 90.64 C ANISOU 1031 CG1 VAL A 160 13650 11481 9307 -487 1180 -544 C ATOM 1032 CG2 VAL A 160 -11.918 -3.825 40.295 1.00 91.83 C ANISOU 1032 CG2 VAL A 160 13465 11999 9426 -521 1187 -764 C ATOM 1033 N SER A 161 -9.102 -0.781 42.447 1.00 88.49 N ANISOU 1033 N SER A 161 13361 11229 9035 -98 888 -422 N ATOM 1034 CA SER A 161 -8.004 -0.252 43.269 1.00 88.23 C ANISOU 1034 CA SER A 161 13455 11063 9004 -29 825 -322 C ATOM 1035 C SER A 161 -8.518 0.750 44.331 1.00 93.77 C ANISOU 1035 C SER A 161 14168 11802 9658 37 814 -338 C ATOM 1036 O SER A 161 -7.849 0.949 45.344 1.00 93.26 O ANISOU 1036 O SER A 161 14213 11645 9577 57 797 -277 O ATOM 1037 CB SER A 161 -6.918 0.385 42.406 1.00 90.95 C ANISOU 1037 CB SER A 161 13813 11350 9392 54 717 -258 C ATOM 1038 OG SER A 161 -7.382 1.541 41.728 1.00100.72 O ANISOU 1038 OG SER A 161 14972 12674 10625 152 657 -292 O ATOM 1039 N GLY A 162 -9.697 1.335 44.097 1.00 91.70 N ANISOU 1039 N GLY A 162 13790 11686 9365 76 826 -424 N ATOM 1040 CA GLY A 162 -10.355 2.251 45.026 1.00 92.25 C ANISOU 1040 CA GLY A 162 13858 11809 9382 146 828 -452 C ATOM 1041 C GLY A 162 -10.908 1.530 46.239 1.00 97.58 C ANISOU 1041 C GLY A 162 14569 12488 10018 47 931 -482 C ATOM 1042 O GLY A 162 -10.896 2.072 47.346 1.00 97.35 O ANISOU 1042 O GLY A 162 14611 12426 9953 86 930 -462 O ATOM 1043 N LEU A 163 -11.375 0.284 46.029 1.00 95.32 N ANISOU 1043 N LEU A 163 14247 12236 9734 -91 1029 -531 N ATOM 1044 CA LEU A 163 -11.931 -0.612 47.044 1.00 96.25 C ANISOU 1044 CA LEU A 163 14413 12347 9811 -216 1156 -566 C ATOM 1045 C LEU A 163 -10.830 -1.254 47.904 1.00 99.38 C ANISOU 1045 C LEU A 163 14999 12553 10208 -246 1173 -459 C ATOM 1046 O LEU A 163 -10.986 -1.336 49.119 1.00 99.05 O ANISOU 1046 O LEU A 163 15042 12474 10117 -265 1228 -448 O ATOM 1047 CB LEU A 163 -12.767 -1.709 46.358 1.00 97.30 C ANISOU 1047 CB LEU A 163 14451 12576 9942 -366 1265 -666 C ATOM 1048 CG LEU A 163 -14.288 -1.528 46.358 1.00103.45 C ANISOU 1048 CG LEU A 163 15060 13578 10670 -407 1332 -809 C ATOM 1049 CD1 LEU A 163 -14.733 -0.445 45.383 1.00103.59 C ANISOU 1049 CD1 LEU A 163 14912 13759 10686 -263 1229 -857 C ATOM 1050 CD2 LEU A 163 -14.975 -2.822 45.991 1.00107.20 C ANISOU 1050 CD2 LEU A 163 15483 14116 11132 -607 1471 -909 C ATOM 1051 N THR A 164 -9.720 -1.693 47.281 1.00 95.39 N ANISOU 1051 N THR A 164 14558 11938 9748 -237 1126 -383 N ATOM 1052 CA THR A 164 -8.594 -2.329 47.977 1.00 95.19 C ANISOU 1052 CA THR A 164 14703 11753 9712 -236 1132 -280 C ATOM 1053 C THR A 164 -7.739 -1.305 48.756 1.00 98.96 C ANISOU 1053 C THR A 164 15244 12181 10174 -117 1026 -208 C ATOM 1054 O THR A 164 -6.889 -1.715 49.555 1.00 99.00 O ANISOU 1054 O THR A 164 15380 12086 10149 -100 1026 -132 O ATOM 1055 CB THR A 164 -7.712 -3.120 46.990 1.00103.83 C ANISOU 1055 CB THR A 164 15829 12768 10853 -254 1116 -232 C ATOM 1056 OG1 THR A 164 -7.193 -2.233 45.998 1.00104.37 O ANISOU 1056 OG1 THR A 164 15811 12871 10974 -166 991 -217 O ATOM 1057 CG2 THR A 164 -8.449 -4.291 46.336 1.00102.24 C ANISOU 1057 CG2 THR A 164 15601 12590 10657 -393 1239 -303 C ATOM 1058 N SER A 165 -7.963 0.012 48.530 1.00 94.85 N ANISOU 1058 N SER A 165 14640 11733 9664 -32 941 -235 N ATOM 1059 CA SER A 165 -7.217 1.091 49.186 1.00 94.05 C ANISOU 1059 CA SER A 165 14598 11590 9546 63 849 -185 C ATOM 1060 C SER A 165 -8.009 1.782 50.300 1.00 97.50 C ANISOU 1060 C SER A 165 15045 12074 9926 87 878 -225 C ATOM 1061 O SER A 165 -7.453 1.998 51.375 1.00 96.95 O ANISOU 1061 O SER A 165 15074 11946 9816 111 861 -181 O ATOM 1062 CB SER A 165 -6.766 2.134 48.169 1.00 97.11 C ANISOU 1062 CB SER A 165 14928 11993 9978 142 745 -180 C ATOM 1063 OG SER A 165 -5.939 1.555 47.174 1.00105.86 O ANISOU 1063 OG SER A 165 16029 13056 11137 123 713 -140 O ATOM 1064 N PHE A 166 -9.285 2.144 50.046 1.00 94.19 N ANISOU 1064 N PHE A 166 14518 11774 9497 89 919 -312 N ATOM 1065 CA PHE A 166 -10.137 2.850 51.010 1.00 94.49 C ANISOU 1065 CA PHE A 166 14550 11875 9478 125 949 -360 C ATOM 1066 C PHE A 166 -10.751 1.938 52.083 1.00 98.17 C ANISOU 1066 C PHE A 166 15060 12345 9893 27 1069 -384 C ATOM 1067 O PHE A 166 -10.719 2.310 53.252 1.00 97.71 O ANISOU 1067 O PHE A 166 15082 12259 9786 52 1077 -367 O ATOM 1068 CB PHE A 166 -11.261 3.614 50.294 1.00 96.87 C ANISOU 1068 CB PHE A 166 14709 12323 9773 189 944 -447 C ATOM 1069 CG PHE A 166 -10.894 5.018 49.883 1.00 98.21 C ANISOU 1069 CG PHE A 166 14890 12477 9947 328 843 -427 C ATOM 1070 CD1 PHE A 166 -10.226 5.259 48.687 1.00100.67 C ANISOU 1070 CD1 PHE A 166 15186 12755 10309 368 770 -394 C ATOM 1071 CD2 PHE A 166 -11.230 6.104 50.682 1.00100.96 C ANISOU 1071 CD2 PHE A 166 15280 12836 10244 417 832 -442 C ATOM 1072 CE1 PHE A 166 -9.887 6.560 48.307 1.00101.42 C ANISOU 1072 CE1 PHE A 166 15318 12818 10399 487 695 -376 C ATOM 1073 CE2 PHE A 166 -10.895 7.407 50.299 1.00103.64 C ANISOU 1073 CE2 PHE A 166 15660 13140 10578 540 757 -426 C ATOM 1074 CZ PHE A 166 -10.224 7.626 49.115 1.00101.12 C ANISOU 1074 CZ PHE A 166 15337 12779 10306 571 693 -392 C ATOM 1075 N LEU A 167 -11.323 0.773 51.699 1.00 94.77 N ANISOU 1075 N LEU A 167 14589 11950 9470 -91 1170 -427 N ATOM 1076 CA LEU A 167 -11.976 -0.150 52.639 1.00 95.22 C ANISOU 1076 CA LEU A 167 14702 12005 9473 -206 1308 -460 C ATOM 1077 C LEU A 167 -11.034 -0.691 53.743 1.00 98.11 C ANISOU 1077 C LEU A 167 15260 12215 9800 -211 1326 -361 C ATOM 1078 O LEU A 167 -11.437 -0.598 54.898 1.00 98.28 O ANISOU 1078 O LEU A 167 15343 12239 9761 -221 1383 -371 O ATOM 1079 CB LEU A 167 -12.669 -1.336 51.936 1.00 95.98 C ANISOU 1079 CB LEU A 167 14735 12151 9580 -354 1425 -531 C ATOM 1080 CG LEU A 167 -13.872 -1.038 51.029 1.00101.29 C ANISOU 1080 CG LEU A 167 15201 13025 10261 -376 1442 -658 C ATOM 1081 CD1 LEU A 167 -14.285 -2.282 50.272 1.00102.11 C ANISOU 1081 CD1 LEU A 167 15260 13158 10377 -539 1549 -723 C ATOM 1082 CD2 LEU A 167 -15.069 -0.499 51.821 1.00104.95 C ANISOU 1082 CD2 LEU A 167 15583 13633 10662 -373 1500 -750 C ATOM 1083 N PRO A 168 -9.809 -1.231 53.487 1.00 93.44 N ANISOU 1083 N PRO A 168 14769 11503 9233 -192 1281 -268 N ATOM 1084 CA PRO A 168 -9.004 -1.746 54.612 1.00 93.23 C ANISOU 1084 CA PRO A 168 14920 11357 9146 -173 1301 -182 C ATOM 1085 C PRO A 168 -8.512 -0.664 55.578 1.00 96.29 C ANISOU 1085 C PRO A 168 15348 11744 9495 -69 1209 -147 C ATOM 1086 O PRO A 168 -8.175 -0.992 56.714 1.00 96.33 O ANISOU 1086 O PRO A 168 15484 11688 9428 -55 1241 -99 O ATOM 1087 CB PRO A 168 -7.824 -2.437 53.919 1.00 94.42 C ANISOU 1087 CB PRO A 168 15132 11414 9329 -150 1257 -102 C ATOM 1088 CG PRO A 168 -8.255 -2.642 52.506 1.00 98.57 C ANISOU 1088 CG PRO A 168 15531 11994 9928 -208 1264 -159 C ATOM 1089 CD PRO A 168 -9.115 -1.465 52.204 1.00 94.04 C ANISOU 1089 CD PRO A 168 14803 11553 9377 -180 1217 -240 C ATOM 1090 N ILE A 169 -8.492 0.614 55.143 1.00 92.06 N ANISOU 1090 N ILE A 169 14712 11270 8996 4 1103 -174 N ATOM 1091 CA ILE A 169 -8.041 1.754 55.949 1.00 91.66 C ANISOU 1091 CA ILE A 169 14700 11217 8911 90 1020 -156 C ATOM 1092 C ILE A 169 -9.231 2.387 56.712 1.00 96.89 C ANISOU 1092 C ILE A 169 15330 11954 9528 91 1076 -227 C ATOM 1093 O ILE A 169 -9.110 2.600 57.919 1.00 97.08 O ANISOU 1093 O ILE A 169 15446 11955 9487 111 1086 -210 O ATOM 1094 CB ILE A 169 -7.246 2.790 55.091 1.00 93.56 C ANISOU 1094 CB ILE A 169 14887 11456 9205 163 889 -142 C ATOM 1095 CG1 ILE A 169 -5.857 2.214 54.703 1.00 93.24 C ANISOU 1095 CG1 ILE A 169 14897 11346 9186 171 827 -64 C ATOM 1096 CG2 ILE A 169 -7.096 4.145 55.814 1.00 94.04 C ANISOU 1096 CG2 ILE A 169 14977 11525 9228 232 826 -156 C ATOM 1097 CD1 ILE A 169 -5.083 2.951 53.603 1.00 98.68 C ANISOU 1097 CD1 ILE A 169 15525 12032 9935 211 722 -55 C ATOM 1098 N GLN A 170 -10.358 2.678 56.029 1.00 94.09 N ANISOU 1098 N GLN A 170 14846 11704 9201 79 1111 -310 N ATOM 1099 CA GLN A 170 -11.537 3.287 56.667 1.00 95.04 C ANISOU 1099 CA GLN A 170 14917 11920 9274 94 1166 -387 C ATOM 1100 C GLN A 170 -12.222 2.311 57.653 1.00101.08 C ANISOU 1100 C GLN A 170 15734 12691 9979 -9 1304 -411 C ATOM 1101 O GLN A 170 -12.752 2.765 58.667 1.00101.07 O ANISOU 1101 O GLN A 170 15760 12723 9918 10 1341 -439 O ATOM 1102 CB GLN A 170 -12.556 3.807 55.629 1.00 96.47 C ANISOU 1102 CB GLN A 170 14931 12239 9485 127 1164 -475 C ATOM 1103 CG GLN A 170 -12.034 4.891 54.663 1.00110.63 C ANISOU 1103 CG GLN A 170 16688 14024 11322 242 1043 -457 C ATOM 1104 CD GLN A 170 -11.636 6.208 55.298 1.00130.71 C ANISOU 1104 CD GLN A 170 19312 16520 13833 349 974 -436 C ATOM 1105 OE1 GLN A 170 -12.299 6.730 56.201 1.00128.07 O ANISOU 1105 OE1 GLN A 170 18994 16228 13441 383 1011 -475 O ATOM 1106 NE2 GLN A 170 -10.564 6.802 54.795 1.00120.76 N ANISOU 1106 NE2 GLN A 170 18104 15173 12605 397 878 -382 N ATOM 1107 N MET A 171 -12.182 0.985 57.375 1.00 99.19 N ANISOU 1107 N MET A 171 15528 12409 9749 -118 1389 -398 N ATOM 1108 CA MET A 171 -12.758 -0.052 58.247 1.00100.80 C ANISOU 1108 CA MET A 171 15817 12592 9891 -232 1542 -415 C ATOM 1109 C MET A 171 -11.815 -0.393 59.416 1.00105.35 C ANISOU 1109 C MET A 171 16591 13033 10404 -200 1540 -314 C ATOM 1110 O MET A 171 -12.202 -1.132 60.329 1.00105.67 O ANISOU 1110 O MET A 171 16740 13036 10375 -272 1664 -314 O ATOM 1111 CB MET A 171 -13.101 -1.331 57.458 1.00103.82 C ANISOU 1111 CB MET A 171 16181 12968 10299 -370 1650 -447 C ATOM 1112 CG MET A 171 -14.314 -1.197 56.555 1.00108.40 C ANISOU 1112 CG MET A 171 16560 13720 10908 -433 1693 -575 C ATOM 1113 SD MET A 171 -15.816 -0.653 57.409 1.00114.58 S ANISOU 1113 SD MET A 171 17241 14673 11623 -462 1784 -695 S ATOM 1114 CE MET A 171 -16.297 -2.175 58.235 1.00112.85 C ANISOU 1114 CE MET A 171 17158 14385 11336 -668 2002 -720 C ATOM 1115 N HIS A 172 -10.581 0.161 59.376 1.00101.59 N ANISOU 1115 N HIS A 172 16161 12496 9944 -92 1402 -235 N ATOM 1116 CA HIS A 172 -9.493 0.021 60.350 1.00101.83 C ANISOU 1116 CA HIS A 172 16348 12431 9910 -28 1359 -142 C ATOM 1117 C HIS A 172 -9.012 -1.438 60.470 1.00105.66 C ANISOU 1117 C HIS A 172 16976 12811 10360 -72 1444 -74 C ATOM 1118 O HIS A 172 -8.811 -1.941 61.578 1.00106.38 O ANISOU 1118 O HIS A 172 17219 12841 10359 -59 1503 -26 O ATOM 1119 CB HIS A 172 -9.870 0.601 61.734 1.00103.74 C ANISOU 1119 CB HIS A 172 16652 12695 10070 0 1383 -158 C ATOM 1120 CG HIS A 172 -10.381 2.013 61.710 1.00107.19 C ANISOU 1120 CG HIS A 172 16979 13222 10527 53 1317 -224 C ATOM 1121 ND1 HIS A 172 -11.336 2.446 62.614 1.00109.87 N ANISOU 1121 ND1 HIS A 172 17316 13619 10810 45 1384 -282 N ATOM 1122 CD2 HIS A 172 -10.055 3.044 60.894 1.00108.24 C ANISOU 1122 CD2 HIS A 172 17020 13386 10722 120 1202 -239 C ATOM 1123 CE1 HIS A 172 -11.557 3.717 62.320 1.00108.98 C ANISOU 1123 CE1 HIS A 172 17114 13569 10725 118 1306 -328 C ATOM 1124 NE2 HIS A 172 -10.812 4.120 61.291 1.00108.36 N ANISOU 1124 NE2 HIS A 172 16987 13469 10714 163 1199 -303 N ATOM 1125 N TRP A 173 -8.791 -2.097 59.317 1.00100.96 N ANISOU 1125 N TRP A 173 16342 12188 9828 -111 1450 -66 N ATOM 1126 CA TRP A 173 -8.268 -3.463 59.233 1.00100.77 C ANISOU 1126 CA TRP A 173 16462 12052 9776 -139 1529 1 C ATOM 1127 C TRP A 173 -6.737 -3.438 59.237 1.00102.18 C ANISOU 1127 C TRP A 173 16707 12177 9940 -9 1402 102 C ATOM 1128 O TRP A 173 -6.098 -4.470 59.451 1.00102.46 O ANISOU 1128 O TRP A 173 16892 12117 9920 20 1450 177 O ATOM 1129 CB TRP A 173 -8.775 -4.164 57.957 1.00 99.78 C ANISOU 1129 CB TRP A 173 16260 11930 9723 -246 1598 -49 C ATOM 1130 CG TRP A 173 -10.260 -4.388 57.866 1.00101.89 C ANISOU 1130 CG TRP A 173 16449 12272 9992 -392 1737 -163 C ATOM 1131 CD1 TRP A 173 -11.172 -4.322 58.880 1.00105.86 C ANISOU 1131 CD1 TRP A 173 16982 12811 10430 -449 1839 -213 C ATOM 1132 CD2 TRP A 173 -10.989 -4.786 56.696 1.00101.94 C ANISOU 1132 CD2 TRP A 173 16331 12340 10060 -507 1796 -249 C ATOM 1133 NE1 TRP A 173 -12.429 -4.623 58.408 1.00106.15 N ANISOU 1133 NE1 TRP A 173 16907 12941 10484 -595 1957 -331 N ATOM 1134 CE2 TRP A 173 -12.346 -4.911 57.070 1.00107.03 C ANISOU 1134 CE2 TRP A 173 16920 13075 10672 -634 1931 -357 C ATOM 1135 CE3 TRP A 173 -10.628 -5.039 55.360 1.00102.55 C ANISOU 1135 CE3 TRP A 173 16332 12418 10215 -517 1748 -251 C ATOM 1136 CZ2 TRP A 173 -13.344 -5.273 56.157 1.00106.92 C ANISOU 1136 CZ2 TRP A 173 16764 13167 10693 -771 2015 -475 C ATOM 1137 CZ3 TRP A 173 -11.617 -5.400 54.456 1.00104.56 C ANISOU 1137 CZ3 TRP A 173 16458 12765 10506 -649 1830 -360 C ATOM 1138 CH2 TRP A 173 -12.956 -5.514 54.856 1.00106.45 C ANISOU 1138 CH2 TRP A 173 16632 13108 10705 -776 1960 -475 C ATOM 1139 N TYR A 174 -6.160 -2.250 58.986 1.00 96.32 N ANISOU 1139 N TYR A 174 15857 11501 9240 68 1248 97 N ATOM 1140 CA TYR A 174 -4.726 -1.991 58.896 1.00 94.95 C ANISOU 1140 CA TYR A 174 15699 11318 9058 175 1114 165 C ATOM 1141 C TYR A 174 -4.074 -1.761 60.261 1.00 99.39 C ANISOU 1141 C TYR A 174 16368 11884 9512 263 1073 212 C ATOM 1142 O TYR A 174 -2.905 -2.099 60.425 1.00 99.23 O ANISOU 1142 O TYR A 174 16410 11851 9444 352 1008 280 O ATOM 1143 CB TYR A 174 -4.479 -0.758 57.994 1.00 94.43 C ANISOU 1143 CB TYR A 174 15474 11322 9081 192 986 123 C ATOM 1144 CG TYR A 174 -4.711 0.586 58.662 1.00 95.04 C ANISOU 1144 CG TYR A 174 15512 11460 9139 219 926 78 C ATOM 1145 CD1 TYR A 174 -5.997 1.054 58.912 1.00 96.90 C ANISOU 1145 CD1 TYR A 174 15702 11736 9379 174 993 7 C ATOM 1146 CD2 TYR A 174 -3.639 1.386 59.051 1.00 95.36 C ANISOU 1146 CD2 TYR A 174 15561 11523 9150 288 808 99 C ATOM 1147 CE1 TYR A 174 -6.214 2.285 59.531 1.00 96.93 C ANISOU 1147 CE1 TYR A 174 15686 11784 9358 210 946 -34 C ATOM 1148 CE2 TYR A 174 -3.843 2.614 59.680 1.00 96.19 C ANISOU 1148 CE2 TYR A 174 15649 11669 9231 303 765 52 C ATOM 1149 CZ TYR A 174 -5.133 3.059 59.919 1.00102.64 C ANISOU 1149 CZ TYR A 174 16438 12508 10054 271 835 -9 C ATOM 1150 OH TYR A 174 -5.335 4.273 60.532 1.00103.05 O ANISOU 1150 OH TYR A 174 16488 12589 10075 296 799 -54 O ATOM 1151 N ARG A 175 -4.818 -1.153 61.211 1.00 96.26 N ANISOU 1151 N ARG A 175 15983 11521 9072 244 1106 169 N ATOM 1152 CA ARG A 175 -4.383 -0.726 62.545 1.00 96.74 C ANISOU 1152 CA ARG A 175 16127 11603 9028 316 1066 193 C ATOM 1153 C ARG A 175 -3.619 -1.789 63.359 1.00103.08 C ANISOU 1153 C ARG A 175 17101 12351 9713 395 1098 283 C ATOM 1154 O ARG A 175 -4.085 -2.921 63.524 1.00103.81 O ANISOU 1154 O ARG A 175 17314 12362 9767 363 1233 314 O ATOM 1155 CB ARG A 175 -5.574 -0.207 63.366 1.00 96.14 C ANISOU 1155 CB ARG A 175 16053 11553 8923 264 1142 130 C ATOM 1156 CG ARG A 175 -5.976 1.209 62.976 1.00101.09 C ANISOU 1156 CG ARG A 175 16538 12252 9618 254 1067 52 C ATOM 1157 CD ARG A 175 -6.999 1.822 63.906 1.00106.23 C ANISOU 1157 CD ARG A 175 17198 12941 10225 234 1127 -6 C ATOM 1158 NE ARG A 175 -7.307 3.198 63.510 1.00111.40 N ANISOU 1158 NE ARG A 175 17740 13652 10933 249 1056 -74 N ATOM 1159 CZ ARG A 175 -8.060 4.037 64.215 1.00126.04 C ANISOU 1159 CZ ARG A 175 19589 15548 12753 257 1080 -130 C ATOM 1160 NH1 ARG A 175 -8.596 3.654 65.366 1.00118.04 N ANISOU 1160 NH1 ARG A 175 18662 14533 11656 240 1170 -132 N ATOM 1161 NH2 ARG A 175 -8.278 5.268 63.773 1.00109.19 N ANISOU 1161 NH2 ARG A 175 17376 13450 10662 289 1020 -184 N ATOM 1162 N ALA A 176 -2.430 -1.388 63.865 1.00100.10 N ANISOU 1162 N ALA A 176 16736 12027 9270 502 976 319 N ATOM 1163 CA ALA A 176 -1.546 -2.194 64.711 1.00100.78 C ANISOU 1163 CA ALA A 176 16969 12101 9221 621 973 404 C ATOM 1164 C ALA A 176 -2.059 -2.174 66.153 1.00105.85 C ANISOU 1164 C ALA A 176 17734 12739 9746 638 1041 407 C ATOM 1165 O ALA A 176 -2.797 -1.260 66.525 1.00105.16 O ANISOU 1165 O ALA A 176 17586 12688 9683 573 1043 338 O ATOM 1166 CB ALA A 176 -0.120 -1.664 64.637 1.00101.20 C ANISOU 1166 CB ALA A 176 16950 12255 9247 720 808 418 C ATOM 1167 N THR A 177 -1.682 -3.181 66.958 1.00103.99 N ANISOU 1167 N THR A 177 17680 12456 9377 734 1101 488 N ATOM 1168 CA THR A 177 -2.160 -3.334 68.338 1.00105.17 C ANISOU 1168 CA THR A 177 17975 12586 9399 758 1183 503 C ATOM 1169 C THR A 177 -1.145 -2.908 69.421 1.00109.93 C ANISOU 1169 C THR A 177 18612 13293 9862 901 1066 531 C ATOM 1170 O THR A 177 -1.473 -3.001 70.608 1.00110.52 O ANISOU 1170 O THR A 177 18812 13361 9820 933 1125 546 O ATOM 1171 CB THR A 177 -2.585 -4.789 68.579 1.00115.16 C ANISOU 1171 CB THR A 177 19455 13712 10590 762 1362 574 C ATOM 1172 OG1 THR A 177 -1.615 -5.667 68.002 1.00116.40 O ANISOU 1172 OG1 THR A 177 19676 13831 10722 868 1337 652 O ATOM 1173 CG2 THR A 177 -3.971 -5.094 68.024 1.00113.35 C ANISOU 1173 CG2 THR A 177 19210 13399 10458 580 1519 515 C ATOM 1174 N HIS A 178 0.067 -2.451 69.041 1.00106.08 N ANISOU 1174 N HIS A 178 18013 12913 9378 980 905 530 N ATOM 1175 CA HIS A 178 1.052 -2.029 70.041 1.00106.59 C ANISOU 1175 CA HIS A 178 18087 13110 9303 1105 790 537 C ATOM 1176 C HIS A 178 0.709 -0.629 70.564 1.00108.51 C ANISOU 1176 C HIS A 178 18230 13433 9568 1022 729 441 C ATOM 1177 O HIS A 178 0.016 0.131 69.884 1.00106.90 O ANISOU 1177 O HIS A 178 17914 13202 9502 893 736 371 O ATOM 1178 CB HIS A 178 2.495 -2.112 69.515 1.00107.74 C ANISOU 1178 CB HIS A 178 18146 13365 9423 1216 650 561 C ATOM 1179 CG HIS A 178 2.800 -1.208 68.365 1.00110.14 C ANISOU 1179 CG HIS A 178 18247 13724 9879 1118 551 488 C ATOM 1180 ND1 HIS A 178 2.621 -1.618 67.056 1.00111.21 N ANISOU 1180 ND1 HIS A 178 18332 13777 10147 1060 584 500 N ATOM 1181 CD2 HIS A 178 3.311 0.044 68.365 1.00111.76 C ANISOU 1181 CD2 HIS A 178 18306 14052 10107 1070 427 403 C ATOM 1182 CE1 HIS A 178 3.005 -0.598 66.305 1.00109.75 C ANISOU 1182 CE1 HIS A 178 17975 13665 10062 987 480 429 C ATOM 1183 NE2 HIS A 178 3.429 0.425 67.049 1.00110.39 N ANISOU 1183 NE2 HIS A 178 17998 13863 10080 985 389 368 N ATOM 1184 N GLN A 179 1.164 -0.318 71.792 1.00105.19 N ANISOU 1184 N GLN A 179 17861 13107 8999 1106 676 438 N ATOM 1185 CA GLN A 179 0.900 0.932 72.513 1.00104.53 C ANISOU 1185 CA GLN A 179 17720 13096 8900 1043 629 351 C ATOM 1186 C GLN A 179 1.310 2.185 71.726 1.00105.81 C ANISOU 1186 C GLN A 179 17697 13332 9176 953 513 258 C ATOM 1187 O GLN A 179 0.559 3.160 71.740 1.00104.83 O ANISOU 1187 O GLN A 179 17527 13184 9122 849 531 184 O ATOM 1188 CB GLN A 179 1.595 0.920 73.888 1.00107.40 C ANISOU 1188 CB GLN A 179 18166 13574 9066 1169 573 367 C ATOM 1189 CG GLN A 179 0.962 1.841 74.944 1.00119.08 C ANISOU 1189 CG GLN A 179 19669 15080 10497 1112 590 299 C ATOM 1190 CD GLN A 179 -0.447 1.455 75.347 1.00135.33 C ANISOU 1190 CD GLN A 179 21848 17000 12571 1052 757 318 C ATOM 1191 OE1 GLN A 179 -0.779 0.277 75.542 1.00130.29 O ANISOU 1191 OE1 GLN A 179 21358 16269 11878 1104 871 402 O ATOM 1192 NE2 GLN A 179 -1.306 2.453 75.500 1.00126.64 N ANISOU 1192 NE2 GLN A 179 20694 15886 11536 942 783 235 N ATOM 1193 N GLU A 180 2.472 2.158 71.036 1.00101.30 N ANISOU 1193 N GLU A 180 17029 12845 8617 994 404 261 N ATOM 1194 CA GLU A 180 2.966 3.298 70.251 1.00100.00 C ANISOU 1194 CA GLU A 180 16704 12743 8549 901 303 174 C ATOM 1195 C GLU A 180 2.017 3.655 69.095 1.00101.63 C ANISOU 1195 C GLU A 180 16852 12827 8936 781 365 148 C ATOM 1196 O GLU A 180 1.922 4.828 68.737 1.00100.49 O ANISOU 1196 O GLU A 180 16626 12693 8863 690 326 66 O ATOM 1197 CB GLU A 180 4.386 3.040 69.716 1.00101.62 C ANISOU 1197 CB GLU A 180 16818 13069 8724 970 190 186 C ATOM 1198 CG GLU A 180 5.495 3.323 70.721 1.00114.61 C ANISOU 1198 CG GLU A 180 18441 14906 10200 1051 82 152 C ATOM 1199 CD GLU A 180 5.656 2.338 71.866 1.00137.75 C ANISOU 1199 CD GLU A 180 21510 17878 12952 1218 106 232 C ATOM 1200 OE1 GLU A 180 5.654 2.786 73.037 1.00133.77 O ANISOU 1200 OE1 GLU A 180 21046 17452 12326 1238 86 195 O ATOM 1201 OE2 GLU A 180 5.806 1.124 71.595 1.00130.55 O ANISOU 1201 OE2 GLU A 180 20674 16916 12011 1336 148 332 O ATOM 1202 N ALA A 181 1.295 2.656 68.547 1.00 97.47 N ANISOU 1202 N ALA A 181 16378 12186 8471 784 468 211 N ATOM 1203 CA ALA A 181 0.338 2.845 67.459 1.00 96.02 C ANISOU 1203 CA ALA A 181 16134 11907 8442 683 531 186 C ATOM 1204 C ALA A 181 -1.006 3.364 67.975 1.00100.24 C ANISOU 1204 C ALA A 181 16701 12392 8994 617 622 138 C ATOM 1205 O ALA A 181 -1.514 4.343 67.429 1.00 99.40 O ANISOU 1205 O ALA A 181 16513 12275 8978 547 612 72 O ATOM 1206 CB ALA A 181 0.137 1.543 66.703 1.00 96.48 C ANISOU 1206 CB ALA A 181 16230 11882 8545 701 608 258 C ATOM 1207 N ILE A 182 -1.571 2.720 69.027 1.00 97.67 N ANISOU 1207 N ILE A 182 16501 12037 8573 648 715 173 N ATOM 1208 CA ILE A 182 -2.866 3.059 69.640 1.00 97.73 C ANISOU 1208 CA ILE A 182 16546 12008 8577 592 816 130 C ATOM 1209 C ILE A 182 -2.876 4.531 70.089 1.00101.95 C ANISOU 1209 C ILE A 182 17030 12602 9104 568 747 47 C ATOM 1210 O ILE A 182 -3.857 5.228 69.825 1.00101.43 O ANISOU 1210 O ILE A 182 16917 12513 9110 510 792 -13 O ATOM 1211 CB ILE A 182 -3.226 2.081 70.800 1.00101.98 C ANISOU 1211 CB ILE A 182 17248 12512 8988 636 922 187 C ATOM 1212 CG1 ILE A 182 -3.442 0.645 70.260 1.00102.47 C ANISOU 1212 CG1 ILE A 182 17385 12481 9066 634 1028 260 C ATOM 1213 CG2 ILE A 182 -4.465 2.557 71.585 1.00103.20 C ANISOU 1213 CG2 ILE A 182 17435 12653 9122 578 1018 133 C ATOM 1214 CD1 ILE A 182 -3.425 -0.470 71.314 1.00111.63 C ANISOU 1214 CD1 ILE A 182 18745 13591 10078 705 1126 338 C ATOM 1215 N ASN A 183 -1.779 5.003 70.723 1.00 99.06 N ANISOU 1215 N ASN A 183 16673 12319 8648 616 640 36 N ATOM 1216 CA ASN A 183 -1.633 6.389 71.182 1.00 98.98 C ANISOU 1216 CA ASN A 183 16631 12360 8615 582 577 -49 C ATOM 1217 C ASN A 183 -1.616 7.373 69.998 1.00102.21 C ANISOU 1217 C ASN A 183 16934 12749 9154 514 532 -109 C ATOM 1218 O ASN A 183 -2.183 8.460 70.114 1.00102.07 O ANISOU 1218 O ASN A 183 16913 12712 9159 473 546 -179 O ATOM 1219 CB ASN A 183 -0.364 6.561 72.027 1.00 99.91 C ANISOU 1219 CB ASN A 183 16768 12593 8601 635 473 -57 C ATOM 1220 CG ASN A 183 -0.340 5.792 73.331 1.00122.61 C ANISOU 1220 CG ASN A 183 19763 15501 11321 722 508 -4 C ATOM 1221 OD1 ASN A 183 -1.372 5.414 73.899 1.00115.90 O ANISOU 1221 OD1 ASN A 183 19003 14585 10450 722 619 18 O ATOM 1222 ND2 ASN A 183 0.856 5.561 73.848 1.00116.19 N ANISOU 1222 ND2 ASN A 183 18955 14805 10388 801 414 12 N ATOM 1223 N CYS A 184 -0.988 6.982 68.864 1.00 97.81 N ANISOU 1223 N CYS A 184 16302 12187 8673 510 486 -79 N ATOM 1224 CA CYS A 184 -0.896 7.798 67.649 1.00 96.66 C ANISOU 1224 CA CYS A 184 16067 12016 8645 453 447 -124 C ATOM 1225 C CYS A 184 -2.273 7.948 66.982 1.00 99.48 C ANISOU 1225 C CYS A 184 16402 12293 9102 426 537 -139 C ATOM 1226 O CYS A 184 -2.567 9.021 66.449 1.00 98.81 O ANISOU 1226 O CYS A 184 16285 12183 9075 395 527 -197 O ATOM 1227 CB CYS A 184 0.134 7.221 66.680 1.00 96.64 C ANISOU 1227 CB CYS A 184 15995 12038 8686 463 380 -84 C ATOM 1228 SG CYS A 184 0.388 8.209 65.180 1.00 99.74 S ANISOU 1228 SG CYS A 184 16290 12398 9208 391 334 -135 S ATOM 1229 N TYR A 185 -3.113 6.889 67.020 1.00 95.85 N ANISOU 1229 N TYR A 185 15966 11802 8653 438 631 -93 N ATOM 1230 CA TYR A 185 -4.460 6.910 66.431 1.00 95.17 C ANISOU 1230 CA TYR A 185 15838 11676 8647 410 722 -118 C ATOM 1231 C TYR A 185 -5.377 7.863 67.199 1.00 99.57 C ANISOU 1231 C TYR A 185 16424 12241 9167 410 766 -183 C ATOM 1232 O TYR A 185 -6.079 8.663 66.573 1.00 99.10 O ANISOU 1232 O TYR A 185 16310 12173 9170 407 780 -235 O ATOM 1233 CB TYR A 185 -5.089 5.500 66.368 1.00 96.24 C ANISOU 1233 CB TYR A 185 15996 11784 8786 398 824 -68 C ATOM 1234 CG TYR A 185 -4.280 4.470 65.605 1.00 97.16 C ANISOU 1234 CG TYR A 185 16103 11879 8934 406 798 -1 C ATOM 1235 CD1 TYR A 185 -3.708 4.774 64.373 1.00 98.30 C ANISOU 1235 CD1 TYR A 185 16156 12024 9169 398 723 -5 C ATOM 1236 CD2 TYR A 185 -4.148 3.169 66.080 1.00 98.33 C ANISOU 1236 CD2 TYR A 185 16346 11997 9017 427 862 67 C ATOM 1237 CE1 TYR A 185 -2.967 3.830 63.665 1.00 98.83 C ANISOU 1237 CE1 TYR A 185 16213 12074 9263 411 701 54 C ATOM 1238 CE2 TYR A 185 -3.405 2.217 65.385 1.00 98.89 C ANISOU 1238 CE2 TYR A 185 16424 12041 9109 450 845 130 C ATOM 1239 CZ TYR A 185 -2.824 2.550 64.172 1.00105.43 C ANISOU 1239 CZ TYR A 185 17146 12881 10032 441 762 121 C ATOM 1240 OH TYR A 185 -2.103 1.615 63.471 1.00106.48 O ANISOU 1240 OH TYR A 185 17283 12990 10183 468 748 180 O ATOM 1241 N ALA A 186 -5.340 7.795 68.549 1.00 96.55 N ANISOU 1241 N ALA A 186 16131 11879 8674 428 786 -180 N ATOM 1242 CA ALA A 186 -6.129 8.630 69.459 1.00 96.86 C ANISOU 1242 CA ALA A 186 16214 11929 8660 434 831 -239 C ATOM 1243 C ALA A 186 -5.753 10.108 69.339 1.00100.25 C ANISOU 1243 C ALA A 186 16640 12356 9097 434 759 -304 C ATOM 1244 O ALA A 186 -6.646 10.955 69.319 1.00100.24 O ANISOU 1244 O ALA A 186 16635 12340 9111 447 802 -360 O ATOM 1245 CB ALA A 186 -5.939 8.163 70.892 1.00 98.57 C ANISOU 1245 CB ALA A 186 16537 12169 8748 455 855 -213 C ATOM 1246 N GLU A 187 -4.441 10.410 69.242 1.00 96.19 N ANISOU 1246 N GLU A 187 16128 11857 8564 420 658 -302 N ATOM 1247 CA GLU A 187 -3.915 11.768 69.109 1.00 95.82 C ANISOU 1247 CA GLU A 187 16095 11798 8515 394 599 -370 C ATOM 1248 C GLU A 187 -4.298 12.365 67.761 1.00 99.59 C ANISOU 1248 C GLU A 187 16518 12219 9104 390 605 -390 C ATOM 1249 O GLU A 187 -4.115 11.723 66.723 1.00 98.45 O ANISOU 1249 O GLU A 187 16300 12067 9038 386 589 -348 O ATOM 1250 CB GLU A 187 -2.390 11.784 69.281 1.00 97.24 C ANISOU 1250 CB GLU A 187 16270 12034 8642 362 497 -371 C ATOM 1251 CG GLU A 187 -1.926 11.700 70.725 1.00107.10 C ANISOU 1251 CG GLU A 187 17585 13355 9753 374 475 -382 C ATOM 1252 CD GLU A 187 -0.483 11.274 70.925 1.00123.01 C ANISOU 1252 CD GLU A 187 19569 15469 11698 372 376 -367 C ATOM 1253 OE1 GLU A 187 0.404 11.781 70.202 1.00114.83 O ANISOU 1253 OE1 GLU A 187 18476 14455 10698 319 309 -404 O ATOM 1254 OE2 GLU A 187 -0.235 10.458 71.841 1.00115.47 O ANISOU 1254 OE2 GLU A 187 18650 14580 10642 429 370 -324 O ATOM 1255 N GLU A 188 -4.842 13.593 67.789 1.00 97.28 N ANISOU 1255 N GLU A 188 16272 11882 8808 401 633 -455 N ATOM 1256 CA GLU A 188 -5.266 14.354 66.604 1.00 96.95 C ANISOU 1256 CA GLU A 188 16209 11781 8846 424 645 -478 C ATOM 1257 C GLU A 188 -4.052 15.004 65.918 1.00100.89 C ANISOU 1257 C GLU A 188 16723 12244 9368 365 573 -497 C ATOM 1258 O GLU A 188 -4.180 15.538 64.812 1.00100.32 O ANISOU 1258 O GLU A 188 16642 12115 9361 379 577 -505 O ATOM 1259 CB GLU A 188 -6.297 15.439 66.991 1.00 99.10 C ANISOU 1259 CB GLU A 188 16553 12016 9084 482 711 -538 C ATOM 1260 CG GLU A 188 -7.518 14.948 67.759 1.00112.38 C ANISOU 1260 CG GLU A 188 18219 13748 10732 532 790 -538 C ATOM 1261 CD GLU A 188 -8.590 14.222 66.969 1.00139.45 C ANISOU 1261 CD GLU A 188 21538 17218 14229 575 844 -517 C ATOM 1262 OE1 GLU A 188 -8.861 14.618 65.811 1.00132.47 O ANISOU 1262 OE1 GLU A 188 20608 16315 13410 616 839 -524 O ATOM 1263 OE2 GLU A 188 -9.195 13.279 67.530 1.00139.21 O ANISOU 1263 OE2 GLU A 188 21472 17243 14178 564 900 -499 O ATOM 1264 N THR A 189 -2.880 14.960 66.591 1.00 97.70 N ANISOU 1264 N THR A 189 16339 11883 8898 299 512 -509 N ATOM 1265 CA THR A 189 -1.613 15.536 66.136 1.00 97.49 C ANISOU 1265 CA THR A 189 16317 11852 8871 217 447 -545 C ATOM 1266 C THR A 189 -0.603 14.448 65.693 1.00100.77 C ANISOU 1266 C THR A 189 16631 12344 9312 194 376 -490 C ATOM 1267 O THR A 189 0.580 14.752 65.512 1.00100.51 O ANISOU 1267 O THR A 189 16581 12351 9259 121 314 -524 O ATOM 1268 CB THR A 189 -1.015 16.437 67.232 1.00107.00 C ANISOU 1268 CB THR A 189 17612 13076 9967 152 432 -625 C ATOM 1269 OG1 THR A 189 -0.866 15.688 68.439 1.00106.63 O ANISOU 1269 OG1 THR A 189 17554 13125 9833 170 411 -606 O ATOM 1270 CG2 THR A 189 -1.848 17.689 67.488 1.00107.25 C ANISOU 1270 CG2 THR A 189 17766 13009 9975 170 505 -687 C ATOM 1271 N CYS A 190 -1.070 13.196 65.490 1.00 96.76 N ANISOU 1271 N CYS A 190 16060 11860 8843 254 392 -412 N ATOM 1272 CA CYS A 190 -0.210 12.099 65.043 1.00 96.17 C ANISOU 1272 CA CYS A 190 15907 11844 8788 254 337 -353 C ATOM 1273 C CYS A 190 -0.832 11.395 63.843 1.00 99.25 C ANISOU 1273 C CYS A 190 16234 12189 9290 286 370 -297 C ATOM 1274 O CYS A 190 -1.958 10.890 63.931 1.00 98.76 O ANISOU 1274 O CYS A 190 16173 12104 9248 328 441 -272 O ATOM 1275 CB CYS A 190 0.080 11.116 66.177 1.00 96.92 C ANISOU 1275 CB CYS A 190 16017 12021 8789 295 324 -312 C ATOM 1276 SG CYS A 190 1.363 9.885 65.795 1.00100.55 S ANISOU 1276 SG CYS A 190 16402 12567 9236 322 248 -245 S ATOM 1277 N CYS A 191 -0.092 11.379 62.718 1.00 95.02 N ANISOU 1277 N CYS A 191 15638 11647 8819 257 324 -288 N ATOM 1278 CA CYS A 191 -0.486 10.700 61.487 1.00 93.95 C ANISOU 1278 CA CYS A 191 15434 11478 8784 279 343 -239 C ATOM 1279 C CYS A 191 0.720 9.944 60.922 1.00 98.18 C ANISOU 1279 C CYS A 191 15906 12062 9337 264 277 -199 C ATOM 1280 O CYS A 191 1.208 10.237 59.825 1.00 97.21 O ANISOU 1280 O CYS A 191 15738 11920 9278 232 247 -206 O ATOM 1281 CB CYS A 191 -1.087 11.666 60.470 1.00 93.75 C ANISOU 1281 CB CYS A 191 15410 11381 8831 277 369 -274 C ATOM 1282 SG CYS A 191 -1.856 10.853 59.044 1.00 96.64 S ANISOU 1282 SG CYS A 191 15686 11725 9306 314 403 -227 S ATOM 1283 N ASP A 192 1.219 8.984 61.719 1.00 95.65 N ANISOU 1283 N ASP A 192 15590 11807 8945 297 258 -158 N ATOM 1284 CA ASP A 192 2.327 8.106 61.357 1.00 95.64 C ANISOU 1284 CA ASP A 192 15535 11868 8936 316 200 -112 C ATOM 1285 C ASP A 192 1.730 6.771 60.932 1.00 99.76 C ANISOU 1285 C ASP A 192 16054 12347 9501 367 257 -35 C ATOM 1286 O ASP A 192 0.895 6.218 61.655 1.00 99.53 O ANISOU 1286 O ASP A 192 16086 12294 9437 397 326 -10 O ATOM 1287 CB ASP A 192 3.322 7.948 62.523 1.00 98.39 C ANISOU 1287 CB ASP A 192 15901 12329 9156 343 140 -119 C ATOM 1288 CG ASP A 192 4.009 9.219 62.994 1.00108.75 C ANISOU 1288 CG ASP A 192 17211 13700 10410 270 86 -212 C ATOM 1289 OD1 ASP A 192 3.697 10.304 62.454 1.00109.66 O ANISOU 1289 OD1 ASP A 192 17338 13746 10584 198 105 -268 O ATOM 1290 OD2 ASP A 192 4.854 9.130 63.909 1.00114.71 O ANISOU 1290 OD2 ASP A 192 17961 14572 11051 287 30 -232 O ATOM 1291 N PHE A 193 2.107 6.287 59.735 1.00 96.27 N ANISOU 1291 N PHE A 193 15550 11892 9138 364 240 -5 N ATOM 1292 CA PHE A 193 1.568 5.057 59.159 1.00 96.08 C ANISOU 1292 CA PHE A 193 15524 11818 9162 393 302 57 C ATOM 1293 C PHE A 193 2.068 3.800 59.888 1.00101.37 C ANISOU 1293 C PHE A 193 16254 12517 9744 466 311 126 C ATOM 1294 O PHE A 193 3.150 3.279 59.591 1.00101.30 O ANISOU 1294 O PHE A 193 16219 12556 9714 510 255 160 O ATOM 1295 CB PHE A 193 1.877 4.977 57.653 1.00 97.16 C ANISOU 1295 CB PHE A 193 15581 11933 9401 368 278 64 C ATOM 1296 CG PHE A 193 1.027 4.015 56.852 1.00 98.38 C ANISOU 1296 CG PHE A 193 15726 12028 9627 367 355 100 C ATOM 1297 CD1 PHE A 193 -0.345 3.918 57.074 1.00101.62 C ANISOU 1297 CD1 PHE A 193 16160 12400 10052 349 444 82 C ATOM 1298 CD2 PHE A 193 1.582 3.261 55.826 1.00100.16 C ANISOU 1298 CD2 PHE A 193 15909 12245 9904 376 340 138 C ATOM 1299 CE1 PHE A 193 -1.132 3.043 56.320 1.00102.21 C ANISOU 1299 CE1 PHE A 193 16213 12437 10184 327 520 96 C ATOM 1300 CE2 PHE A 193 0.790 2.396 55.063 1.00102.68 C ANISOU 1300 CE2 PHE A 193 16220 12510 10284 359 415 159 C ATOM 1301 CZ PHE A 193 -0.564 2.303 55.307 1.00100.87 C ANISOU 1301 CZ PHE A 193 16009 12252 10064 328 505 133 C ATOM 1302 N PHE A 194 1.257 3.330 60.858 1.00 98.47 N ANISOU 1302 N PHE A 194 15977 12119 9318 487 390 145 N ATOM 1303 CA PHE A 194 1.494 2.120 61.649 1.00 98.83 C ANISOU 1303 CA PHE A 194 16121 12163 9265 566 429 215 C ATOM 1304 C PHE A 194 0.537 1.038 61.163 1.00102.66 C ANISOU 1304 C PHE A 194 16656 12551 9801 543 549 253 C ATOM 1305 O PHE A 194 -0.679 1.249 61.182 1.00102.22 O ANISOU 1305 O PHE A 194 16600 12453 9785 478 630 216 O ATOM 1306 CB PHE A 194 1.307 2.386 63.158 1.00101.35 C ANISOU 1306 CB PHE A 194 16526 12517 9467 596 442 205 C ATOM 1307 CG PHE A 194 2.356 3.247 63.825 1.00103.30 C ANISOU 1307 CG PHE A 194 16741 12878 9632 621 329 165 C ATOM 1308 CD1 PHE A 194 3.614 2.735 64.123 1.00106.94 C ANISOU 1308 CD1 PHE A 194 17200 13434 9997 713 254 201 C ATOM 1309 CD2 PHE A 194 2.062 4.548 64.220 1.00105.35 C ANISOU 1309 CD2 PHE A 194 16976 13157 9894 557 306 86 C ATOM 1310 CE1 PHE A 194 4.576 3.526 64.758 1.00108.46 C ANISOU 1310 CE1 PHE A 194 17345 13760 10103 722 152 147 C ATOM 1311 CE2 PHE A 194 3.022 5.334 64.868 1.00108.70 C ANISOU 1311 CE2 PHE A 194 17376 13691 10235 558 213 35 C ATOM 1312 CZ PHE A 194 4.274 4.821 65.125 1.00107.44 C ANISOU 1312 CZ PHE A 194 17194 13644 9984 632 135 61 C ATOM 1313 N THR A 195 1.075 -0.091 60.673 1.00 99.12 N ANISOU 1313 N THR A 195 16242 12072 9346 592 566 318 N ATOM 1314 CA THR A 195 0.242 -1.178 60.150 1.00 98.74 C ANISOU 1314 CA THR A 195 16251 11924 9340 553 690 347 C ATOM 1315 C THR A 195 0.564 -2.514 60.802 1.00102.69 C ANISOU 1315 C THR A 195 16915 12371 9732 639 762 430 C ATOM 1316 O THR A 195 1.693 -2.727 61.253 1.00103.01 O ANISOU 1316 O THR A 195 16993 12466 9681 757 689 478 O ATOM 1317 CB THR A 195 0.385 -1.307 58.624 1.00107.41 C ANISOU 1317 CB THR A 195 17250 13004 10557 512 670 339 C ATOM 1318 OG1 THR A 195 1.754 -1.520 58.278 1.00109.01 O ANISOU 1318 OG1 THR A 195 17430 13252 10737 595 576 381 O ATOM 1319 CG2 THR A 195 -0.159 -0.113 57.884 1.00105.26 C ANISOU 1319 CG2 THR A 195 16845 12761 10387 433 629 262 C ATOM 1320 N ASN A 196 -0.430 -3.423 60.837 1.00 98.53 N ANISOU 1320 N ASN A 196 16491 11742 9205 582 913 443 N ATOM 1321 CA ASN A 196 -0.229 -4.771 61.352 1.00 98.93 C ANISOU 1321 CA ASN A 196 16733 11705 9151 655 1012 525 C ATOM 1322 C ASN A 196 0.547 -5.554 60.296 1.00102.02 C ANISOU 1322 C ASN A 196 17125 12061 9577 704 996 573 C ATOM 1323 O ASN A 196 0.369 -5.306 59.100 1.00100.67 O ANISOU 1323 O ASN A 196 16827 11894 9529 623 973 531 O ATOM 1324 CB ASN A 196 -1.550 -5.454 61.742 1.00 99.04 C ANISOU 1324 CB ASN A 196 16868 11616 9148 551 1196 511 C ATOM 1325 CG ASN A 196 -2.588 -5.580 60.651 1.00114.70 C ANISOU 1325 CG ASN A 196 18763 13563 11256 396 1279 443 C ATOM 1326 OD1 ASN A 196 -2.438 -6.334 59.688 1.00105.40 O ANISOU 1326 OD1 ASN A 196 17595 12326 10125 372 1318 460 O ATOM 1327 ND2 ASN A 196 -3.722 -4.938 60.848 1.00105.86 N ANISOU 1327 ND2 ASN A 196 17567 12481 10175 289 1323 363 N ATOM 1328 N GLN A 197 1.426 -6.467 60.735 1.00 99.06 N ANISOU 1328 N GLN A 197 16894 11659 9084 850 1004 661 N ATOM 1329 CA GLN A 197 2.304 -7.277 59.883 1.00 98.42 C ANISOU 1329 CA GLN A 197 16838 11550 9008 936 987 717 C ATOM 1330 C GLN A 197 1.540 -8.055 58.796 1.00100.80 C ANISOU 1330 C GLN A 197 17170 11725 9407 814 1114 703 C ATOM 1331 O GLN A 197 2.121 -8.333 57.751 1.00 99.94 O ANISOU 1331 O GLN A 197 17003 11614 9356 836 1074 716 O ATOM 1332 CB GLN A 197 3.158 -8.223 60.738 1.00101.33 C ANISOU 1332 CB GLN A 197 17399 11898 9203 1134 1007 818 C ATOM 1333 CG GLN A 197 4.165 -7.458 61.607 1.00118.63 C ANISOU 1333 CG GLN A 197 19518 14260 11295 1269 851 822 C ATOM 1334 CD GLN A 197 5.035 -8.311 62.498 1.00142.67 C ANISOU 1334 CD GLN A 197 22737 17323 14149 1494 854 917 C ATOM 1335 OE1 GLN A 197 4.701 -9.441 62.864 1.00141.15 O ANISOU 1335 OE1 GLN A 197 22777 16986 13869 1554 1000 990 O ATOM 1336 NE2 GLN A 197 6.162 -7.755 62.914 1.00134.89 N ANISOU 1336 NE2 GLN A 197 21647 16523 13083 1625 698 912 N ATOM 1337 N ALA A 198 0.237 -8.338 59.009 1.00 96.94 N ANISOU 1337 N ALA A 198 16751 11146 8935 674 1263 664 N ATOM 1338 CA ALA A 198 -0.616 -9.028 58.039 1.00 96.27 C ANISOU 1338 CA ALA A 198 16680 10962 8934 529 1394 626 C ATOM 1339 C ALA A 198 -0.996 -8.107 56.864 1.00 98.02 C ANISOU 1339 C ALA A 198 16660 11272 9313 415 1310 538 C ATOM 1340 O ALA A 198 -0.960 -8.556 55.721 1.00 97.07 O ANISOU 1340 O ALA A 198 16500 11116 9265 369 1331 527 O ATOM 1341 CB ALA A 198 -1.867 -9.558 58.720 1.00 97.99 C ANISOU 1341 CB ALA A 198 17036 11090 9108 406 1580 597 C ATOM 1342 N TYR A 199 -1.349 -6.828 57.142 1.00 93.86 N ANISOU 1342 N TYR A 199 15983 10852 8826 381 1221 477 N ATOM 1343 CA TYR A 199 -1.717 -5.813 56.137 1.00 92.27 C ANISOU 1343 CA TYR A 199 15570 10735 8753 301 1140 397 C ATOM 1344 C TYR A 199 -0.498 -5.432 55.287 1.00 94.87 C ANISOU 1344 C TYR A 199 15799 11116 9130 382 995 424 C ATOM 1345 O TYR A 199 -0.616 -5.328 54.067 1.00 93.30 O ANISOU 1345 O TYR A 199 15493 10927 9030 325 976 390 O ATOM 1346 CB TYR A 199 -2.312 -4.555 56.822 1.00 93.16 C ANISOU 1346 CB TYR A 199 15593 10933 8869 274 1091 337 C ATOM 1347 CG TYR A 199 -2.682 -3.421 55.885 1.00 93.62 C ANISOU 1347 CG TYR A 199 15460 11072 9038 221 1009 262 C ATOM 1348 CD1 TYR A 199 -3.947 -3.349 55.311 1.00 95.36 C ANISOU 1348 CD1 TYR A 199 15599 11312 9320 111 1086 184 C ATOM 1349 CD2 TYR A 199 -1.783 -2.394 55.611 1.00 93.64 C ANISOU 1349 CD2 TYR A 199 15369 11140 9069 284 861 264 C ATOM 1350 CE1 TYR A 199 -4.296 -2.303 54.457 1.00 95.28 C ANISOU 1350 CE1 TYR A 199 15428 11379 9394 92 1013 121 C ATOM 1351 CE2 TYR A 199 -2.118 -1.346 54.753 1.00 93.62 C ANISOU 1351 CE2 TYR A 199 15225 11193 9155 247 800 202 C ATOM 1352 CZ TYR A 199 -3.378 -1.303 54.180 1.00100.68 C ANISOU 1352 CZ TYR A 199 16048 12100 10104 164 873 136 C ATOM 1353 OH TYR A 199 -3.721 -0.273 53.338 1.00100.53 O ANISOU 1353 OH TYR A 199 15902 12139 10156 155 813 81 O ATOM 1354 N ALA A 200 0.663 -5.220 55.942 1.00 91.77 N ANISOU 1354 N ALA A 200 15437 10770 8661 512 896 478 N ATOM 1355 CA ALA A 200 1.932 -4.838 55.322 1.00 90.97 C ANISOU 1355 CA ALA A 200 15240 10743 8583 590 760 497 C ATOM 1356 C ALA A 200 2.401 -5.850 54.269 1.00 94.67 C ANISOU 1356 C ALA A 200 15735 11151 9083 615 790 538 C ATOM 1357 O ALA A 200 3.047 -5.451 53.303 1.00 93.63 O ANISOU 1357 O ALA A 200 15481 11071 9021 620 700 525 O ATOM 1358 CB ALA A 200 3.001 -4.672 56.388 1.00 92.42 C ANISOU 1358 CB ALA A 200 15468 11002 8647 725 675 541 C ATOM 1359 N ILE A 201 2.073 -7.141 54.445 1.00 91.95 N ANISOU 1359 N ILE A 201 15560 10691 8686 625 926 585 N ATOM 1360 CA ILE A 201 2.454 -8.196 53.506 1.00 91.78 C ANISOU 1360 CA ILE A 201 15596 10592 8684 649 977 624 C ATOM 1361 C ILE A 201 1.361 -8.359 52.429 1.00 95.43 C ANISOU 1361 C ILE A 201 15999 11000 9260 480 1064 556 C ATOM 1362 O ILE A 201 1.689 -8.364 51.242 1.00 94.50 O ANISOU 1362 O ILE A 201 15787 10896 9223 462 1021 543 O ATOM 1363 CB ILE A 201 2.772 -9.528 54.243 1.00 96.14 C ANISOU 1363 CB ILE A 201 16392 11036 9102 763 1086 713 C ATOM 1364 CG1 ILE A 201 3.997 -9.365 55.164 1.00 97.12 C ANISOU 1364 CG1 ILE A 201 16548 11252 9103 960 977 777 C ATOM 1365 CG2 ILE A 201 2.995 -10.683 53.257 1.00 97.08 C ANISOU 1365 CG2 ILE A 201 16601 11047 9240 772 1170 747 C ATOM 1366 CD1 ILE A 201 4.168 -10.479 56.176 1.00106.86 C ANISOU 1366 CD1 ILE A 201 18035 12389 10175 1094 1083 865 C ATOM 1367 N ALA A 202 0.080 -8.482 52.836 1.00 92.44 N ANISOU 1367 N ALA A 202 15664 10578 8881 358 1184 506 N ATOM 1368 CA ALA A 202 -1.047 -8.674 51.917 1.00 92.03 C ANISOU 1368 CA ALA A 202 15546 10505 8918 193 1275 425 C ATOM 1369 C ALA A 202 -1.220 -7.510 50.933 1.00 94.36 C ANISOU 1369 C ALA A 202 15611 10914 9327 146 1158 357 C ATOM 1370 O ALA A 202 -1.275 -7.755 49.729 1.00 93.73 O ANISOU 1370 O ALA A 202 15462 10831 9321 95 1161 330 O ATOM 1371 CB ALA A 202 -2.335 -8.885 52.695 1.00 93.67 C ANISOU 1371 CB ALA A 202 15821 10681 9087 76 1416 374 C ATOM 1372 N SER A 203 -1.272 -6.259 51.437 1.00 90.19 N ANISOU 1372 N SER A 203 14982 10478 8806 172 1058 331 N ATOM 1373 CA SER A 203 -1.455 -5.061 50.615 1.00 88.87 C ANISOU 1373 CA SER A 203 14630 10406 8730 144 956 271 C ATOM 1374 C SER A 203 -0.237 -4.757 49.717 1.00 91.84 C ANISOU 1374 C SER A 203 14936 10808 9152 215 835 305 C ATOM 1375 O SER A 203 -0.429 -4.161 48.662 1.00 90.85 O ANISOU 1375 O SER A 203 14686 10727 9108 177 787 261 O ATOM 1376 CB SER A 203 -1.785 -3.851 51.482 1.00 92.61 C ANISOU 1376 CB SER A 203 15055 10949 9182 160 899 239 C ATOM 1377 OG SER A 203 -2.279 -2.774 50.702 1.00102.08 O ANISOU 1377 OG SER A 203 16107 12222 10458 127 840 173 O ATOM 1378 N SER A 204 0.991 -5.169 50.104 1.00 88.42 N ANISOU 1378 N SER A 204 14579 10358 8659 321 789 380 N ATOM 1379 CA SER A 204 2.188 -4.945 49.276 1.00 87.35 C ANISOU 1379 CA SER A 204 14368 10263 8558 384 682 406 C ATOM 1380 C SER A 204 2.202 -5.873 48.061 1.00 90.47 C ANISOU 1380 C SER A 204 14768 10600 9007 354 735 414 C ATOM 1381 O SER A 204 2.557 -5.429 46.969 1.00 89.39 O ANISOU 1381 O SER A 204 14519 10501 8943 341 667 394 O ATOM 1382 CB SER A 204 3.468 -5.142 50.083 1.00 91.37 C ANISOU 1382 CB SER A 204 14941 10804 8973 516 618 471 C ATOM 1383 OG SER A 204 3.683 -4.080 50.998 1.00100.62 O ANISOU 1383 OG SER A 204 16073 12056 10103 537 538 450 O ATOM 1384 N ILE A 205 1.808 -7.154 48.254 1.00 87.35 N ANISOU 1384 N ILE A 205 14514 10105 8568 339 865 440 N ATOM 1385 CA ILE A 205 1.778 -8.189 47.215 1.00 86.99 C ANISOU 1385 CA ILE A 205 14508 9985 8558 303 942 446 C ATOM 1386 C ILE A 205 0.726 -7.843 46.141 1.00 89.86 C ANISOU 1386 C ILE A 205 14744 10379 9020 164 967 357 C ATOM 1387 O ILE A 205 1.092 -7.746 44.972 1.00 88.49 O ANISOU 1387 O ILE A 205 14481 10227 8912 160 916 347 O ATOM 1388 CB ILE A 205 1.571 -9.620 47.820 1.00 91.07 C ANISOU 1388 CB ILE A 205 15246 10370 8988 312 1097 491 C ATOM 1389 CG1 ILE A 205 2.848 -10.093 48.556 1.00 92.08 C ANISOU 1389 CG1 ILE A 205 15498 10479 9011 495 1058 591 C ATOM 1390 CG2 ILE A 205 1.168 -10.649 46.749 1.00 91.59 C ANISOU 1390 CG2 ILE A 205 15359 10346 9093 222 1211 468 C ATOM 1391 CD1 ILE A 205 2.636 -11.193 49.589 1.00101.86 C ANISOU 1391 CD1 ILE A 205 16979 11594 10129 540 1199 647 C ATOM 1392 N VAL A 206 -0.547 -7.632 46.533 1.00 86.41 N ANISOU 1392 N VAL A 206 14289 9957 8584 62 1040 291 N ATOM 1393 CA VAL A 206 -1.651 -7.356 45.603 1.00 85.63 C ANISOU 1393 CA VAL A 206 14061 9916 8557 -58 1070 196 C ATOM 1394 C VAL A 206 -1.508 -5.962 44.933 1.00 88.53 C ANISOU 1394 C VAL A 206 14255 10390 8991 -24 930 167 C ATOM 1395 O VAL A 206 -1.716 -5.867 43.720 1.00 87.97 O ANISOU 1395 O VAL A 206 14085 10356 8982 -61 912 126 O ATOM 1396 CB VAL A 206 -3.048 -7.534 46.269 1.00 89.97 C ANISOU 1396 CB VAL A 206 14630 10478 9075 -171 1192 125 C ATOM 1397 CG1 VAL A 206 -4.167 -7.506 45.229 1.00 89.64 C ANISOU 1397 CG1 VAL A 206 14453 10516 9090 -294 1238 17 C ATOM 1398 CG2 VAL A 206 -3.117 -8.836 47.066 1.00 90.96 C ANISOU 1398 CG2 VAL A 206 14962 10478 9120 -204 1341 161 C ATOM 1399 N SER A 207 -1.141 -4.904 45.695 1.00 84.39 N ANISOU 1399 N SER A 207 13708 9910 8446 47 838 186 N ATOM 1400 CA SER A 207 -1.011 -3.545 45.144 1.00 83.08 C ANISOU 1400 CA SER A 207 13415 9821 8329 76 724 158 C ATOM 1401 C SER A 207 0.265 -3.312 44.321 1.00 86.48 C ANISOU 1401 C SER A 207 13811 10252 8796 135 627 201 C ATOM 1402 O SER A 207 0.181 -2.609 43.321 1.00 85.48 O ANISOU 1402 O SER A 207 13587 10167 8725 126 575 169 O ATOM 1403 CB SER A 207 -1.071 -2.486 46.242 1.00 85.55 C ANISOU 1403 CB SER A 207 13733 10170 8603 116 675 154 C ATOM 1404 OG SER A 207 -2.368 -2.335 46.795 1.00 93.30 O ANISOU 1404 OG SER A 207 14704 11182 9564 65 747 96 O ATOM 1405 N PHE A 208 1.433 -3.853 44.738 1.00 83.17 N ANISOU 1405 N PHE A 208 13467 9798 8335 201 602 270 N ATOM 1406 CA PHE A 208 2.698 -3.567 44.056 1.00 82.36 C ANISOU 1406 CA PHE A 208 13317 9720 8257 256 508 301 C ATOM 1407 C PHE A 208 3.381 -4.767 43.372 1.00 85.36 C ANISOU 1407 C PHE A 208 13740 10053 8642 285 539 346 C ATOM 1408 O PHE A 208 3.656 -4.675 42.177 1.00 84.41 O ANISOU 1408 O PHE A 208 13547 9945 8581 269 508 335 O ATOM 1409 CB PHE A 208 3.687 -2.917 45.046 1.00 84.64 C ANISOU 1409 CB PHE A 208 13619 10054 8486 325 425 329 C ATOM 1410 CG PHE A 208 5.061 -2.582 44.507 1.00 86.38 C ANISOU 1410 CG PHE A 208 13780 10326 8715 370 331 349 C ATOM 1411 CD1 PHE A 208 5.252 -1.487 43.671 1.00 89.17 C ANISOU 1411 CD1 PHE A 208 14040 10716 9126 331 268 310 C ATOM 1412 CD2 PHE A 208 6.172 -3.336 44.871 1.00 89.48 C ANISOU 1412 CD2 PHE A 208 14215 10737 9045 458 311 402 C ATOM 1413 CE1 PHE A 208 6.524 -1.171 43.181 1.00 90.13 C ANISOU 1413 CE1 PHE A 208 14104 10890 9250 354 193 318 C ATOM 1414 CE2 PHE A 208 7.445 -3.016 44.385 1.00 92.41 C ANISOU 1414 CE2 PHE A 208 14512 11183 9417 496 225 408 C ATOM 1415 CZ PHE A 208 7.611 -1.939 43.542 1.00 89.87 C ANISOU 1415 CZ PHE A 208 14091 10896 9160 431 170 362 C ATOM 1416 N TYR A 209 3.722 -5.836 44.122 1.00 81.95 N ANISOU 1416 N TYR A 209 13434 9565 8137 340 597 400 N ATOM 1417 CA TYR A 209 4.501 -6.979 43.624 1.00 81.58 C ANISOU 1417 CA TYR A 209 13457 9468 8074 400 628 452 C ATOM 1418 C TYR A 209 3.826 -7.816 42.520 1.00 84.01 C ANISOU 1418 C TYR A 209 13778 9705 8436 317 721 425 C ATOM 1419 O TYR A 209 4.520 -8.170 41.568 1.00 82.73 O ANISOU 1419 O TYR A 209 13591 9538 8303 346 698 443 O ATOM 1420 CB TYR A 209 4.927 -7.894 44.775 1.00 83.87 C ANISOU 1420 CB TYR A 209 13906 9706 8253 499 680 519 C ATOM 1421 CG TYR A 209 5.908 -7.230 45.720 1.00 86.15 C ANISOU 1421 CG TYR A 209 14171 10089 8474 606 573 549 C ATOM 1422 CD1 TYR A 209 7.227 -6.996 45.337 1.00 87.97 C ANISOU 1422 CD1 TYR A 209 14324 10407 8695 693 470 570 C ATOM 1423 CD2 TYR A 209 5.522 -6.840 46.999 1.00 87.53 C ANISOU 1423 CD2 TYR A 209 14392 10279 8586 613 578 546 C ATOM 1424 CE1 TYR A 209 8.133 -6.378 46.199 1.00 88.90 C ANISOU 1424 CE1 TYR A 209 14402 10637 8740 775 374 579 C ATOM 1425 CE2 TYR A 209 6.419 -6.227 47.872 1.00 88.72 C ANISOU 1425 CE2 TYR A 209 14514 10530 8665 702 480 562 C ATOM 1426 CZ TYR A 209 7.725 -5.999 47.468 1.00 95.87 C ANISOU 1426 CZ TYR A 209 15333 11533 9559 779 378 574 C ATOM 1427 OH TYR A 209 8.615 -5.398 48.323 1.00 97.27 O ANISOU 1427 OH TYR A 209 15467 11834 9657 854 283 573 O ATOM 1428 N VAL A 210 2.516 -8.137 42.637 1.00 80.64 N ANISOU 1428 N VAL A 210 13385 9238 8017 208 827 374 N ATOM 1429 CA VAL A 210 1.772 -8.927 41.639 1.00 80.45 C ANISOU 1429 CA VAL A 210 13365 9166 8035 104 926 327 C ATOM 1430 C VAL A 210 1.807 -8.208 40.266 1.00 83.60 C ANISOU 1430 C VAL A 210 13600 9641 8522 75 843 283 C ATOM 1431 O VAL A 210 2.332 -8.827 39.337 1.00 83.22 O ANISOU 1431 O VAL A 210 13562 9560 8497 85 852 299 O ATOM 1432 CB VAL A 210 0.329 -9.301 42.091 1.00 85.01 C ANISOU 1432 CB VAL A 210 13986 9719 8595 -24 1056 260 C ATOM 1433 CG1 VAL A 210 -0.580 -9.629 40.907 1.00 84.75 C ANISOU 1433 CG1 VAL A 210 13874 9707 8618 -155 1121 173 C ATOM 1434 CG2 VAL A 210 0.354 -10.460 43.078 1.00 86.07 C ANISOU 1434 CG2 VAL A 210 14331 9732 8640 -11 1183 308 C ATOM 1435 N PRO A 211 1.361 -6.924 40.101 1.00 79.56 N ANISOU 1435 N PRO A 211 12955 9224 8050 55 763 236 N ATOM 1436 CA PRO A 211 1.448 -6.297 38.767 1.00 78.57 C ANISOU 1436 CA PRO A 211 12702 9158 7994 44 694 205 C ATOM 1437 C PRO A 211 2.883 -6.104 38.262 1.00 81.14 C ANISOU 1437 C PRO A 211 13010 9484 8334 128 603 263 C ATOM 1438 O PRO A 211 3.087 -6.206 37.060 1.00 80.48 O ANISOU 1438 O PRO A 211 12872 9410 8298 114 588 251 O ATOM 1439 CB PRO A 211 0.740 -4.949 38.948 1.00 79.96 C ANISOU 1439 CB PRO A 211 12782 9417 8183 36 637 156 C ATOM 1440 CG PRO A 211 0.758 -4.687 40.397 1.00 84.77 C ANISOU 1440 CG PRO A 211 13459 10015 8737 67 638 181 C ATOM 1441 CD PRO A 211 0.708 -6.016 41.069 1.00 81.16 C ANISOU 1441 CD PRO A 211 13131 9476 8230 48 744 209 C ATOM 1442 N LEU A 212 3.864 -5.865 39.165 1.00 77.01 N ANISOU 1442 N LEU A 212 12530 8965 7767 211 548 318 N ATOM 1443 CA LEU A 212 5.283 -5.653 38.838 1.00 76.13 C ANISOU 1443 CA LEU A 212 12388 8885 7655 288 462 361 C ATOM 1444 C LEU A 212 5.933 -6.893 38.190 1.00 80.22 C ANISOU 1444 C LEU A 212 12960 9351 8167 328 504 401 C ATOM 1445 O LEU A 212 6.651 -6.735 37.202 1.00 78.87 O ANISOU 1445 O LEU A 212 12722 9210 8034 344 454 404 O ATOM 1446 CB LEU A 212 6.069 -5.236 40.102 1.00 76.29 C ANISOU 1446 CB LEU A 212 12437 8946 7607 362 404 396 C ATOM 1447 CG LEU A 212 7.591 -5.066 39.999 1.00 80.51 C ANISOU 1447 CG LEU A 212 12928 9545 8115 443 318 429 C ATOM 1448 CD1 LEU A 212 7.962 -3.866 39.152 1.00 79.92 C ANISOU 1448 CD1 LEU A 212 12736 9532 8098 396 240 390 C ATOM 1449 CD2 LEU A 212 8.201 -4.916 41.368 1.00 82.84 C ANISOU 1449 CD2 LEU A 212 13262 9892 8322 518 280 455 C ATOM 1450 N VAL A 213 5.694 -8.104 38.742 1.00 78.13 N ANISOU 1450 N VAL A 213 12831 9003 7851 345 604 430 N ATOM 1451 CA VAL A 213 6.259 -9.364 38.225 1.00 78.62 C ANISOU 1451 CA VAL A 213 12984 8994 7894 395 665 471 C ATOM 1452 C VAL A 213 5.663 -9.662 36.829 1.00 83.10 C ANISOU 1452 C VAL A 213 13504 9536 8535 296 710 420 C ATOM 1453 O VAL A 213 6.405 -10.050 35.922 1.00 82.54 O ANISOU 1453 O VAL A 213 13418 9459 8484 335 694 439 O ATOM 1454 CB VAL A 213 6.075 -10.549 39.219 1.00 83.22 C ANISOU 1454 CB VAL A 213 13760 9472 8389 439 779 515 C ATOM 1455 CG1 VAL A 213 6.634 -11.854 38.651 1.00 83.55 C ANISOU 1455 CG1 VAL A 213 13922 9421 8402 500 856 559 C ATOM 1456 CG2 VAL A 213 6.733 -10.241 40.562 1.00 83.39 C ANISOU 1456 CG2 VAL A 213 13822 9537 8326 555 724 567 C ATOM 1457 N ILE A 214 4.344 -9.421 36.656 1.00 80.20 N ANISOU 1457 N ILE A 214 13096 9173 8202 174 759 349 N ATOM 1458 CA ILE A 214 3.624 -9.604 35.392 1.00 79.90 C ANISOU 1458 CA ILE A 214 12992 9144 8222 74 797 283 C ATOM 1459 C ILE A 214 4.150 -8.584 34.353 1.00 84.59 C ANISOU 1459 C ILE A 214 13441 9824 8876 99 679 274 C ATOM 1460 O ILE A 214 4.590 -9.005 33.290 1.00 84.37 O ANISOU 1460 O ILE A 214 13396 9783 8877 101 680 277 O ATOM 1461 CB ILE A 214 2.079 -9.521 35.593 1.00 82.83 C ANISOU 1461 CB ILE A 214 13336 9538 8596 -51 871 199 C ATOM 1462 CG1 ILE A 214 1.573 -10.666 36.518 1.00 84.01 C ANISOU 1462 CG1 ILE A 214 13650 9587 8683 -100 1015 201 C ATOM 1463 CG2 ILE A 214 1.342 -9.538 34.243 1.00 82.80 C ANISOU 1463 CG2 ILE A 214 13228 9588 8643 -144 889 118 C ATOM 1464 CD1 ILE A 214 0.221 -10.412 37.232 1.00 88.76 C ANISOU 1464 CD1 ILE A 214 14232 10228 9267 -203 1078 130 C ATOM 1465 N MET A 215 4.146 -7.271 34.681 1.00 82.20 N ANISOU 1465 N MET A 215 13053 9596 8584 118 588 266 N ATOM 1466 CA MET A 215 4.615 -6.159 33.834 1.00 82.17 C ANISOU 1466 CA MET A 215 12938 9658 8624 137 489 259 C ATOM 1467 C MET A 215 6.045 -6.404 33.300 1.00 88.88 C ANISOU 1467 C MET A 215 13787 10505 9479 204 442 310 C ATOM 1468 O MET A 215 6.269 -6.251 32.099 1.00 87.73 O ANISOU 1468 O MET A 215 13580 10378 9376 190 418 296 O ATOM 1469 CB MET A 215 4.558 -4.835 34.627 1.00 84.10 C ANISOU 1469 CB MET A 215 13147 9952 8855 157 420 254 C ATOM 1470 CG MET A 215 4.974 -3.602 33.849 1.00 86.93 C ANISOU 1470 CG MET A 215 13424 10360 9246 167 336 243 C ATOM 1471 SD MET A 215 5.354 -2.216 34.947 1.00 90.81 S ANISOU 1471 SD MET A 215 13917 10882 9704 193 267 248 S ATOM 1472 CE MET A 215 7.009 -2.650 35.469 1.00 87.70 C ANISOU 1472 CE MET A 215 13546 10501 9276 247 226 303 C ATOM 1473 N VAL A 216 6.990 -6.798 34.186 1.00 88.44 N ANISOU 1473 N VAL A 216 13793 10436 9372 282 430 365 N ATOM 1474 CA VAL A 216 8.396 -7.076 33.854 1.00 89.36 C ANISOU 1474 CA VAL A 216 13900 10578 9476 363 385 409 C ATOM 1475 C VAL A 216 8.490 -8.275 32.876 1.00 95.60 C ANISOU 1475 C VAL A 216 14735 11306 10281 368 453 419 C ATOM 1476 O VAL A 216 9.141 -8.146 31.837 1.00 95.04 O ANISOU 1476 O VAL A 216 14599 11266 10244 377 415 418 O ATOM 1477 CB VAL A 216 9.254 -7.285 35.143 1.00 93.97 C ANISOU 1477 CB VAL A 216 14538 11186 9979 464 361 459 C ATOM 1478 CG1 VAL A 216 10.559 -8.033 34.862 1.00 94.19 C ANISOU 1478 CG1 VAL A 216 14578 11238 9970 573 345 505 C ATOM 1479 CG2 VAL A 216 9.542 -5.951 35.827 1.00 93.56 C ANISOU 1479 CG2 VAL A 216 14413 11220 9916 455 274 440 C ATOM 1480 N PHE A 217 7.828 -9.411 33.198 1.00 94.07 N ANISOU 1480 N PHE A 217 14661 11020 10060 352 560 424 N ATOM 1481 CA PHE A 217 7.837 -10.630 32.385 1.00 94.83 C ANISOU 1481 CA PHE A 217 14834 11038 10160 345 646 427 C ATOM 1482 C PHE A 217 7.171 -10.433 31.014 1.00 96.99 C ANISOU 1482 C PHE A 217 15019 11328 10504 241 654 363 C ATOM 1483 O PHE A 217 7.725 -10.893 30.014 1.00 97.26 O ANISOU 1483 O PHE A 217 15046 11349 10558 259 659 370 O ATOM 1484 CB PHE A 217 7.163 -11.791 33.140 1.00 98.51 C ANISOU 1484 CB PHE A 217 15469 11389 10571 326 778 436 C ATOM 1485 CG PHE A 217 6.748 -12.972 32.288 1.00101.98 C ANISOU 1485 CG PHE A 217 15999 11731 11018 262 897 409 C ATOM 1486 CD1 PHE A 217 7.698 -13.848 31.770 1.00106.56 C ANISOU 1486 CD1 PHE A 217 16658 12255 11575 354 923 456 C ATOM 1487 CD2 PHE A 217 5.406 -13.213 32.009 1.00105.33 C ANISOU 1487 CD2 PHE A 217 16428 12128 11466 108 986 329 C ATOM 1488 CE1 PHE A 217 7.314 -14.934 30.974 1.00108.42 C ANISOU 1488 CE1 PHE A 217 16991 12390 11814 286 1042 427 C ATOM 1489 CE2 PHE A 217 5.024 -14.303 31.218 1.00109.21 C ANISOU 1489 CE2 PHE A 217 17002 12535 11957 27 1104 290 C ATOM 1490 CZ PHE A 217 5.980 -15.157 30.708 1.00107.86 C ANISOU 1490 CZ PHE A 217 16927 12290 11767 114 1134 341 C ATOM 1491 N VAL A 218 5.984 -9.790 30.971 1.00 91.53 N ANISOU 1491 N VAL A 218 14263 10674 9841 143 657 299 N ATOM 1492 CA VAL A 218 5.213 -9.572 29.738 1.00 90.04 C ANISOU 1492 CA VAL A 218 13985 10526 9702 56 663 230 C ATOM 1493 C VAL A 218 5.931 -8.565 28.806 1.00 92.32 C ANISOU 1493 C VAL A 218 14161 10886 10031 96 556 239 C ATOM 1494 O VAL A 218 6.019 -8.842 27.610 1.00 91.48 O ANISOU 1494 O VAL A 218 14020 10784 9952 75 563 219 O ATOM 1495 CB VAL A 218 3.734 -9.163 30.022 1.00 93.33 C ANISOU 1495 CB VAL A 218 14355 10989 10119 -37 695 155 C ATOM 1496 CG1 VAL A 218 2.986 -8.822 28.739 1.00 92.68 C ANISOU 1496 CG1 VAL A 218 14160 10984 10071 -100 683 81 C ATOM 1497 CG2 VAL A 218 2.993 -10.268 30.770 1.00 93.94 C ANISOU 1497 CG2 VAL A 218 14548 10992 10155 -107 823 132 C ATOM 1498 N TYR A 219 6.458 -7.434 29.338 1.00 88.34 N ANISOU 1498 N TYR A 219 13610 10430 9524 145 468 266 N ATOM 1499 CA TYR A 219 7.132 -6.428 28.504 1.00 87.43 C ANISOU 1499 CA TYR A 219 13410 10371 9439 165 384 270 C ATOM 1500 C TYR A 219 8.528 -6.862 28.035 1.00 92.31 C ANISOU 1500 C TYR A 219 14030 10986 10057 223 362 314 C ATOM 1501 O TYR A 219 9.026 -6.301 27.056 1.00 91.65 O ANISOU 1501 O TYR A 219 13883 10939 10002 221 318 309 O ATOM 1502 CB TYR A 219 7.209 -5.054 29.180 1.00 87.93 C ANISOU 1502 CB TYR A 219 13438 10479 9493 178 315 271 C ATOM 1503 CG TYR A 219 7.100 -3.916 28.186 1.00 88.66 C ANISOU 1503 CG TYR A 219 13464 10611 9613 162 266 245 C ATOM 1504 CD1 TYR A 219 5.887 -3.613 27.573 1.00 90.53 C ANISOU 1504 CD1 TYR A 219 13668 10870 9860 133 283 196 C ATOM 1505 CD2 TYR A 219 8.214 -3.158 27.839 1.00 88.92 C ANISOU 1505 CD2 TYR A 219 13471 10666 9651 179 211 266 C ATOM 1506 CE1 TYR A 219 5.783 -2.578 26.646 1.00 90.74 C ANISOU 1506 CE1 TYR A 219 13654 10927 9895 144 244 180 C ATOM 1507 CE2 TYR A 219 8.120 -2.115 26.917 1.00 89.33 C ANISOU 1507 CE2 TYR A 219 13491 10734 9718 165 182 247 C ATOM 1508 CZ TYR A 219 6.901 -1.830 26.324 1.00 95.70 C ANISOU 1508 CZ TYR A 219 14284 11550 10529 159 198 210 C ATOM 1509 OH TYR A 219 6.784 -0.807 25.419 1.00 95.55 O ANISOU 1509 OH TYR A 219 14253 11542 10508 170 174 198 O ATOM 1510 N SER A 220 9.148 -7.861 28.690 1.00 90.38 N ANISOU 1510 N SER A 220 13863 10703 9774 284 396 358 N ATOM 1511 CA SER A 220 10.443 -8.383 28.245 1.00 91.17 C ANISOU 1511 CA SER A 220 13963 10816 9863 360 380 397 C ATOM 1512 C SER A 220 10.245 -9.201 26.955 1.00 96.48 C ANISOU 1512 C SER A 220 14649 11443 10567 330 436 379 C ATOM 1513 O SER A 220 11.163 -9.296 26.139 1.00 96.13 O ANISOU 1513 O SER A 220 14566 11426 10534 368 411 393 O ATOM 1514 CB SER A 220 11.105 -9.223 29.334 1.00 95.80 C ANISOU 1514 CB SER A 220 14639 11381 10381 462 403 450 C ATOM 1515 OG SER A 220 10.378 -10.409 29.610 1.00106.08 O ANISOU 1515 OG SER A 220 16071 12577 11659 455 509 456 O ATOM 1516 N ARG A 221 9.025 -9.762 26.776 1.00 93.77 N ANISOU 1516 N ARG A 221 14353 11041 10234 253 514 338 N ATOM 1517 CA ARG A 221 8.592 -10.521 25.603 1.00 93.74 C ANISOU 1517 CA ARG A 221 14362 11000 10254 197 577 301 C ATOM 1518 C ARG A 221 8.277 -9.588 24.433 1.00 96.61 C ANISOU 1518 C ARG A 221 14607 11437 10664 147 521 257 C ATOM 1519 O ARG A 221 8.545 -9.958 23.291 1.00 96.89 O ANISOU 1519 O ARG A 221 14625 11470 10719 139 533 245 O ATOM 1520 CB ARG A 221 7.354 -11.374 25.924 1.00 95.64 C ANISOU 1520 CB ARG A 221 14686 11175 10479 110 686 254 C ATOM 1521 CG ARG A 221 7.630 -12.648 26.723 1.00113.25 C ANISOU 1521 CG ARG A 221 17082 13294 12655 154 783 296 C ATOM 1522 CD ARG A 221 8.305 -13.749 25.909 1.00131.46 C ANISOU 1522 CD ARG A 221 19468 15528 14951 193 844 315 C ATOM 1523 NE ARG A 221 7.639 -14.011 24.628 1.00143.17 N ANISOU 1523 NE ARG A 221 20910 17015 16471 83 885 242 N ATOM 1524 CZ ARG A 221 6.653 -14.886 24.454 1.00158.98 C ANISOU 1524 CZ ARG A 221 22992 18952 18461 -33 1005 177 C ATOM 1525 NH1 ARG A 221 6.195 -15.597 25.478 1.00147.18 N ANISOU 1525 NH1 ARG A 221 21638 17365 16918 -60 1106 181 N ATOM 1526 NH2 ARG A 221 6.115 -15.055 23.253 1.00146.04 N ANISOU 1526 NH2 ARG A 221 21295 17344 16849 -129 1030 102 N ATOM 1527 N VAL A 222 7.691 -8.392 24.713 1.00 91.61 N ANISOU 1527 N VAL A 222 13905 10862 10039 122 465 234 N ATOM 1528 CA VAL A 222 7.328 -7.375 23.708 1.00 90.60 C ANISOU 1528 CA VAL A 222 13686 10800 9937 98 413 199 C ATOM 1529 C VAL A 222 8.608 -6.900 22.989 1.00 93.68 C ANISOU 1529 C VAL A 222 14042 11209 10343 144 356 236 C ATOM 1530 O VAL A 222 8.616 -6.806 21.759 1.00 92.76 O ANISOU 1530 O VAL A 222 13887 11113 10245 130 351 216 O ATOM 1531 CB VAL A 222 6.519 -6.186 24.308 1.00 94.10 C ANISOU 1531 CB VAL A 222 14093 11290 10371 90 373 176 C ATOM 1532 CG1 VAL A 222 6.059 -5.213 23.222 1.00 93.49 C ANISOU 1532 CG1 VAL A 222 13947 11273 10303 89 332 143 C ATOM 1533 CG2 VAL A 222 5.318 -6.680 25.107 1.00 94.31 C ANISOU 1533 CG2 VAL A 222 14145 11310 10377 42 434 135 C ATOM 1534 N PHE A 223 9.693 -6.656 23.756 1.00 90.27 N ANISOU 1534 N PHE A 223 13619 10782 9896 194 319 283 N ATOM 1535 CA PHE A 223 10.996 -6.258 23.220 1.00 89.89 C ANISOU 1535 CA PHE A 223 13530 10771 9854 226 274 308 C ATOM 1536 C PHE A 223 11.644 -7.404 22.418 1.00 94.49 C ANISOU 1536 C PHE A 223 14128 11333 10442 257 311 323 C ATOM 1537 O PHE A 223 12.358 -7.136 21.449 1.00 94.13 O ANISOU 1537 O PHE A 223 14035 11319 10411 260 289 323 O ATOM 1538 CB PHE A 223 11.938 -5.799 24.346 1.00 91.71 C ANISOU 1538 CB PHE A 223 13752 11039 10053 265 229 337 C ATOM 1539 CG PHE A 223 11.756 -4.381 24.842 1.00 92.96 C ANISOU 1539 CG PHE A 223 13887 11228 10207 229 182 321 C ATOM 1540 CD1 PHE A 223 11.400 -3.357 23.968 1.00 95.71 C ANISOU 1540 CD1 PHE A 223 14212 11579 10575 185 166 296 C ATOM 1541 CD2 PHE A 223 12.020 -4.052 26.165 1.00 95.36 C ANISOU 1541 CD2 PHE A 223 14202 11554 10476 245 157 331 C ATOM 1542 CE1 PHE A 223 11.248 -2.045 24.425 1.00 96.53 C ANISOU 1542 CE1 PHE A 223 14321 11690 10665 158 136 283 C ATOM 1543 CE2 PHE A 223 11.884 -2.736 26.617 1.00 98.07 C ANISOU 1543 CE2 PHE A 223 14536 11915 10810 206 122 311 C ATOM 1544 CZ PHE A 223 11.505 -1.741 25.743 1.00 95.88 C ANISOU 1544 CZ PHE A 223 14252 11625 10554 162 116 288 C ATOM 1545 N GLN A 224 11.384 -8.670 22.821 1.00 91.49 N ANISOU 1545 N GLN A 224 13826 10892 10043 280 378 333 N ATOM 1546 CA GLN A 224 11.888 -9.876 22.161 1.00 91.79 C ANISOU 1546 CA GLN A 224 13911 10887 10075 318 432 346 C ATOM 1547 C GLN A 224 11.201 -10.092 20.810 1.00 95.63 C ANISOU 1547 C GLN A 224 14380 11360 10596 247 466 298 C ATOM 1548 O GLN A 224 11.891 -10.322 19.815 1.00 95.74 O ANISOU 1548 O GLN A 224 14371 11385 10621 268 464 303 O ATOM 1549 CB GLN A 224 11.695 -11.115 23.050 1.00 93.90 C ANISOU 1549 CB GLN A 224 14305 11072 10302 358 511 369 C ATOM 1550 CG GLN A 224 12.797 -11.319 24.084 1.00114.74 C ANISOU 1550 CG GLN A 224 16975 13733 12888 479 485 429 C ATOM 1551 CD GLN A 224 12.541 -12.499 25.000 1.00141.39 C ANISOU 1551 CD GLN A 224 20503 17011 16208 533 572 459 C ATOM 1552 OE1 GLN A 224 11.917 -13.504 24.626 1.00138.40 O ANISOU 1552 OE1 GLN A 224 20229 16531 15827 494 672 442 O ATOM 1553 NE2 GLN A 224 13.058 -12.420 26.219 1.00135.63 N ANISOU 1553 NE2 GLN A 224 19801 16310 15423 625 543 503 N ATOM 1554 N GLU A 225 9.847 -10.012 20.777 1.00 91.32 N ANISOU 1554 N GLU A 225 13835 10805 10058 166 495 246 N ATOM 1555 CA GLU A 225 9.023 -10.201 19.577 1.00 90.63 C ANISOU 1555 CA GLU A 225 13717 10732 9987 95 525 185 C ATOM 1556 C GLU A 225 9.354 -9.180 18.488 1.00 93.51 C ANISOU 1556 C GLU A 225 13993 11165 10373 104 455 181 C ATOM 1557 O GLU A 225 9.480 -9.568 17.328 1.00 93.18 O ANISOU 1557 O GLU A 225 13937 11127 10339 91 473 160 O ATOM 1558 CB GLU A 225 7.524 -10.132 19.918 1.00 92.08 C ANISOU 1558 CB GLU A 225 13891 10935 10162 15 557 120 C ATOM 1559 CG GLU A 225 6.989 -11.344 20.663 1.00104.08 C ANISOU 1559 CG GLU A 225 15513 12377 11657 -32 660 101 C ATOM 1560 CD GLU A 225 6.928 -12.621 19.851 1.00128.89 C ANISOU 1560 CD GLU A 225 18722 15459 14792 -81 754 66 C ATOM 1561 OE1 GLU A 225 7.834 -13.470 20.010 1.00122.68 O ANISOU 1561 OE1 GLU A 225 18036 14585 13993 -21 797 118 O ATOM 1562 OE2 GLU A 225 5.987 -12.764 19.039 1.00127.68 O ANISOU 1562 OE2 GLU A 225 18519 15353 14639 -174 785 -18 O ATOM 1563 N ALA A 226 9.518 -7.892 18.868 1.00 89.52 N ANISOU 1563 N ALA A 226 13441 10703 9868 124 385 200 N ATOM 1564 CA ALA A 226 9.831 -6.770 17.977 1.00 89.00 C ANISOU 1564 CA ALA A 226 13321 10685 9810 132 330 201 C ATOM 1565 C ALA A 226 11.162 -6.972 17.232 1.00 93.51 C ANISOU 1565 C ALA A 226 13881 11256 10392 160 322 232 C ATOM 1566 O ALA A 226 11.212 -6.760 16.017 1.00 93.02 O ANISOU 1566 O ALA A 226 13793 11215 10336 151 318 217 O ATOM 1567 CB ALA A 226 9.868 -5.472 18.770 1.00 89.48 C ANISOU 1567 CB ALA A 226 13373 10766 9861 144 277 218 C ATOM 1568 N LYS A 227 12.223 -7.401 17.954 1.00 90.68 N ANISOU 1568 N LYS A 227 13539 10889 10027 203 321 272 N ATOM 1569 CA LYS A 227 13.557 -7.657 17.399 1.00 90.90 C ANISOU 1569 CA LYS A 227 13543 10940 10055 242 316 297 C ATOM 1570 C LYS A 227 13.537 -8.873 16.458 1.00 96.12 C ANISOU 1570 C LYS A 227 14235 11564 10723 252 373 287 C ATOM 1571 O LYS A 227 14.181 -8.847 15.411 1.00 95.66 O ANISOU 1571 O LYS A 227 14144 11529 10673 257 370 286 O ATOM 1572 CB LYS A 227 14.573 -7.869 18.537 1.00 93.56 C ANISOU 1572 CB LYS A 227 13881 11302 10366 304 298 334 C ATOM 1573 CG LYS A 227 16.032 -7.805 18.099 1.00108.48 C ANISOU 1573 CG LYS A 227 15712 13262 12245 344 277 349 C ATOM 1574 CD LYS A 227 16.989 -7.980 19.278 1.00120.07 C ANISOU 1574 CD LYS A 227 17162 14790 13670 418 251 374 C ATOM 1575 CE LYS A 227 18.423 -8.186 18.843 1.00132.71 C ANISOU 1575 CE LYS A 227 18693 16484 15247 474 239 380 C ATOM 1576 NZ LYS A 227 18.647 -9.531 18.243 1.00142.45 N ANISOU 1576 NZ LYS A 227 19975 17676 16473 556 291 399 N ATOM 1577 N ARG A 228 12.776 -9.919 16.834 1.00 93.89 N ANISOU 1577 N ARG A 228 14022 11218 10432 244 433 273 N ATOM 1578 CA ARG A 228 12.616 -11.185 16.114 1.00 94.38 C ANISOU 1578 CA ARG A 228 14143 11224 10492 238 508 254 C ATOM 1579 C ARG A 228 11.762 -11.044 14.842 1.00 97.82 C ANISOU 1579 C ARG A 228 14543 11681 10944 164 518 195 C ATOM 1580 O ARG A 228 12.043 -11.724 13.851 1.00 97.67 O ANISOU 1580 O ARG A 228 14539 11646 10926 163 555 181 O ATOM 1581 CB ARG A 228 11.976 -12.224 17.054 1.00 96.54 C ANISOU 1581 CB ARG A 228 14523 11416 10742 231 583 250 C ATOM 1582 CG ARG A 228 12.053 -13.668 16.563 1.00111.46 C ANISOU 1582 CG ARG A 228 16516 13220 12616 238 681 240 C ATOM 1583 CD ARG A 228 11.324 -14.645 17.475 1.00124.72 C ANISOU 1583 CD ARG A 228 18325 14800 14264 210 776 229 C ATOM 1584 NE ARG A 228 9.907 -14.311 17.661 1.00134.34 N ANISOU 1584 NE ARG A 228 19514 16037 15491 89 790 162 N ATOM 1585 CZ ARG A 228 8.930 -14.657 16.827 1.00149.55 C ANISOU 1585 CZ ARG A 228 21429 17970 17422 -22 842 80 C ATOM 1586 NH1 ARG A 228 7.677 -14.308 17.086 1.00138.42 N ANISOU 1586 NH1 ARG A 228 19974 16609 16010 -119 849 14 N ATOM 1587 NH2 ARG A 228 9.198 -15.347 15.725 1.00135.13 N ANISOU 1587 NH2 ARG A 228 19629 16119 15597 -36 887 55 N ATOM 1588 N GLN A 229 10.718 -10.187 14.875 1.00 93.91 N ANISOU 1588 N GLN A 229 14001 11229 10450 112 486 159 N ATOM 1589 CA GLN A 229 9.796 -9.991 13.751 1.00 93.59 C ANISOU 1589 CA GLN A 229 13917 11238 10407 59 488 97 C ATOM 1590 C GLN A 229 10.271 -8.930 12.724 1.00 96.49 C ANISOU 1590 C GLN A 229 14225 11661 10777 87 427 111 C ATOM 1591 O GLN A 229 9.500 -8.578 11.824 1.00 95.93 O ANISOU 1591 O GLN A 229 14116 11644 10689 66 416 66 O ATOM 1592 CB GLN A 229 8.391 -9.648 14.260 1.00 95.02 C ANISOU 1592 CB GLN A 229 14073 11458 10571 10 487 44 C ATOM 1593 CG GLN A 229 7.611 -10.875 14.720 1.00109.58 C ANISOU 1593 CG GLN A 229 15973 13259 12404 -60 576 -6 C ATOM 1594 CD GLN A 229 6.297 -10.522 15.369 1.00128.25 C ANISOU 1594 CD GLN A 229 18301 15678 14749 -111 578 -62 C ATOM 1595 OE1 GLN A 229 5.481 -9.765 14.828 1.00122.49 O ANISOU 1595 OE1 GLN A 229 17488 15050 14002 -117 537 -110 O ATOM 1596 NE2 GLN A 229 6.047 -11.097 16.535 1.00121.21 N ANISOU 1596 NE2 GLN A 229 17477 14726 13851 -139 632 -58 N ATOM 1597 N LEU A 230 11.543 -8.468 12.825 1.00 92.39 N ANISOU 1597 N LEU A 230 13700 11135 10268 132 396 167 N ATOM 1598 CA LEU A 230 12.134 -7.525 11.866 1.00 91.50 C ANISOU 1598 CA LEU A 230 13553 11060 10153 143 358 181 C ATOM 1599 C LEU A 230 12.402 -8.239 10.543 1.00 95.51 C ANISOU 1599 C LEU A 230 14058 11570 10662 140 391 162 C ATOM 1600 O LEU A 230 12.930 -9.355 10.546 1.00 95.70 O ANISOU 1600 O LEU A 230 14109 11558 10694 153 434 168 O ATOM 1601 CB LEU A 230 13.432 -6.891 12.405 1.00 91.17 C ANISOU 1601 CB LEU A 230 13500 11025 10117 167 328 229 C ATOM 1602 CG LEU A 230 13.289 -5.613 13.234 1.00 95.28 C ANISOU 1602 CG LEU A 230 14019 11557 10628 157 286 241 C ATOM 1603 CD1 LEU A 230 14.593 -5.259 13.906 1.00 95.50 C ANISOU 1603 CD1 LEU A 230 14026 11606 10655 163 268 271 C ATOM 1604 CD2 LEU A 230 12.846 -4.441 12.381 1.00 97.36 C ANISOU 1604 CD2 LEU A 230 14288 11833 10872 146 268 231 C ATOM 1605 N ASN A1002 12.002 -7.615 9.422 1.00 91.43 N ANISOU 1605 N ASN A1002 13519 11093 10127 133 374 139 N ATOM 1606 CA ASN A1002 12.162 -8.165 8.071 1.00 91.08 C ANISOU 1606 CA ASN A1002 13469 11063 10076 127 400 115 C ATOM 1607 C ASN A1002 12.995 -7.216 7.187 1.00 94.51 C ANISOU 1607 C ASN A1002 13893 11517 10499 147 376 146 C ATOM 1608 O ASN A1002 13.513 -6.217 7.690 1.00 94.30 O ANISOU 1608 O ASN A1002 13870 11486 10472 153 348 181 O ATOM 1609 CB ASN A1002 10.782 -8.462 7.435 1.00 90.60 C ANISOU 1609 CB ASN A1002 13391 11047 9986 98 411 45 C ATOM 1610 CG ASN A1002 9.740 -7.375 7.594 1.00107.08 C ANISOU 1610 CG ASN A1002 15453 13194 12040 114 365 27 C ATOM 1611 OD1 ASN A1002 9.986 -6.187 7.358 1.00 97.79 O ANISOU 1611 OD1 ASN A1002 14284 12028 10844 156 327 62 O ATOM 1612 ND2 ASN A1002 8.531 -7.769 7.965 1.00 99.24 N ANISOU 1612 ND2 ASN A1002 14435 12242 11030 83 377 -33 N ATOM 1613 N ILE A1003 13.138 -7.543 5.883 1.00 90.33 N ANISOU 1613 N ILE A1003 13360 11006 9957 147 395 127 N ATOM 1614 CA ILE A1003 13.880 -6.751 4.894 1.00 89.70 C ANISOU 1614 CA ILE A1003 13283 10941 9859 158 388 150 C ATOM 1615 C ILE A1003 13.150 -5.415 4.608 1.00 92.89 C ANISOU 1615 C ILE A1003 13709 11367 10219 178 354 153 C ATOM 1616 O ILE A1003 13.806 -4.400 4.367 1.00 92.53 O ANISOU 1616 O ILE A1003 13694 11307 10157 180 351 187 O ATOM 1617 CB ILE A1003 14.146 -7.577 3.590 1.00 92.99 C ANISOU 1617 CB ILE A1003 13694 11370 10268 158 423 126 C ATOM 1618 CG1 ILE A1003 14.951 -6.791 2.525 1.00 93.63 C ANISOU 1618 CG1 ILE A1003 13785 11465 10326 165 425 150 C ATOM 1619 CG2 ILE A1003 12.862 -8.160 2.982 1.00 93.87 C ANISOU 1619 CG2 ILE A1003 13799 11517 10352 146 430 62 C ATOM 1620 CD1 ILE A1003 16.334 -6.329 2.939 1.00101.74 C ANISOU 1620 CD1 ILE A1003 14803 12481 11373 152 432 192 C ATOM 1621 N PHE A1004 11.806 -5.424 4.661 1.00 89.14 N ANISOU 1621 N PHE A1004 13223 10931 9716 194 336 113 N ATOM 1622 CA PHE A1004 10.951 -4.262 4.413 1.00 89.01 C ANISOU 1622 CA PHE A1004 13230 10949 9641 245 303 112 C ATOM 1623 C PHE A1004 11.119 -3.210 5.507 1.00 91.28 C ANISOU 1623 C PHE A1004 13556 11192 9933 253 285 153 C ATOM 1624 O PHE A1004 11.187 -2.017 5.203 1.00 90.81 O ANISOU 1624 O PHE A1004 13560 11114 9830 289 279 182 O ATOM 1625 CB PHE A1004 9.480 -4.687 4.281 1.00 91.39 C ANISOU 1625 CB PHE A1004 13483 11335 9906 262 289 44 C ATOM 1626 CG PHE A1004 9.247 -5.714 3.195 1.00 93.68 C ANISOU 1626 CG PHE A1004 13735 11678 10182 239 312 -13 C ATOM 1627 CD1 PHE A1004 9.066 -5.324 1.873 1.00 97.52 C ANISOU 1627 CD1 PHE A1004 14226 12223 10605 288 300 -25 C ATOM 1628 CD2 PHE A1004 9.224 -7.073 3.493 1.00 96.02 C ANISOU 1628 CD2 PHE A1004 14004 11958 10519 168 352 -54 C ATOM 1629 CE1 PHE A1004 8.868 -6.275 0.868 1.00 98.90 C ANISOU 1629 CE1 PHE A1004 14363 12451 10763 260 322 -84 C ATOM 1630 CE2 PHE A1004 9.027 -8.022 2.487 1.00 99.35 C ANISOU 1630 CE2 PHE A1004 14405 12419 10925 134 384 -114 C ATOM 1631 CZ PHE A1004 8.848 -7.616 1.182 1.00 97.90 C ANISOU 1631 CZ PHE A1004 14209 12306 10682 177 365 -131 C ATOM 1632 N GLU A1005 11.218 -3.654 6.771 1.00 86.74 N ANISOU 1632 N GLU A1005 12961 10593 9405 219 284 156 N ATOM 1633 CA GLU A1005 11.432 -2.775 7.918 1.00 86.13 C ANISOU 1633 CA GLU A1005 12914 10476 9334 215 269 187 C ATOM 1634 C GLU A1005 12.888 -2.318 7.957 1.00 89.00 C ANISOU 1634 C GLU A1005 13301 10800 9715 177 284 226 C ATOM 1635 O GLU A1005 13.163 -1.200 8.389 1.00 88.72 O ANISOU 1635 O GLU A1005 13315 10732 9661 167 281 248 O ATOM 1636 CB GLU A1005 11.053 -3.476 9.231 1.00 87.34 C ANISOU 1636 CB GLU A1005 13037 10627 9523 194 265 174 C ATOM 1637 CG GLU A1005 9.556 -3.602 9.463 1.00 99.14 C ANISOU 1637 CG GLU A1005 14509 12170 10991 215 253 128 C ATOM 1638 CD GLU A1005 9.146 -4.203 10.795 1.00122.84 C ANISOU 1638 CD GLU A1005 17494 15160 14020 186 260 115 C ATOM 1639 OE1 GLU A1005 8.283 -3.599 11.470 1.00120.18 O ANISOU 1639 OE1 GLU A1005 17157 14845 13660 207 240 103 O ATOM 1640 OE2 GLU A1005 9.661 -5.288 11.153 1.00117.23 O ANISOU 1640 OE2 GLU A1005 16778 14416 13345 150 290 118 O ATOM 1641 N MET A1006 13.813 -3.188 7.490 1.00 84.77 N ANISOU 1641 N MET A1006 12728 10271 9208 153 306 227 N ATOM 1642 CA MET A1006 15.261 -2.958 7.433 1.00 84.38 C ANISOU 1642 CA MET A1006 12671 10219 9172 115 325 249 C ATOM 1643 C MET A1006 15.601 -1.789 6.500 1.00 88.27 C ANISOU 1643 C MET A1006 13224 10693 9623 98 345 261 C ATOM 1644 O MET A1006 16.315 -0.872 6.909 1.00 88.36 O ANISOU 1644 O MET A1006 13264 10686 9623 49 358 272 O ATOM 1645 CB MET A1006 15.977 -4.240 6.964 1.00 86.62 C ANISOU 1645 CB MET A1006 12903 10525 9482 119 347 242 C ATOM 1646 CG MET A1006 17.473 -4.229 7.166 1.00 90.34 C ANISOU 1646 CG MET A1006 13335 11027 9964 93 361 255 C ATOM 1647 SD MET A1006 18.264 -5.439 6.085 1.00 94.56 S ANISOU 1647 SD MET A1006 13829 11589 10508 118 396 247 S ATOM 1648 CE MET A1006 19.877 -5.494 6.794 1.00 91.75 C ANISOU 1648 CE MET A1006 13400 11303 10156 111 399 254 C ATOM 1649 N LEU A1007 15.088 -1.824 5.258 1.00 84.43 N ANISOU 1649 N LEU A1007 12764 10213 9104 134 354 255 N ATOM 1650 CA LEU A1007 15.346 -0.800 4.250 1.00 84.45 C ANISOU 1650 CA LEU A1007 12845 10188 9054 133 382 271 C ATOM 1651 C LEU A1007 14.632 0.516 4.561 1.00 88.66 C ANISOU 1651 C LEU A1007 13477 10675 9533 165 378 287 C ATOM 1652 O LEU A1007 15.153 1.568 4.199 1.00 88.96 O ANISOU 1652 O LEU A1007 13610 10660 9530 138 418 308 O ATOM 1653 CB LEU A1007 14.971 -1.297 2.848 1.00 84.56 C ANISOU 1653 CB LEU A1007 12859 10232 9039 178 390 259 C ATOM 1654 CG LEU A1007 15.889 -2.368 2.253 1.00 89.10 C ANISOU 1654 CG LEU A1007 13368 10835 9651 146 414 247 C ATOM 1655 CD1 LEU A1007 15.175 -3.153 1.175 1.00 89.35 C ANISOU 1655 CD1 LEU A1007 13383 10905 9662 190 410 219 C ATOM 1656 CD2 LEU A1007 17.192 -1.765 1.724 1.00 91.19 C ANISOU 1656 CD2 LEU A1007 13661 11084 9904 89 460 265 C ATOM 1657 N ARG A1008 13.474 0.478 5.256 1.00 84.91 N ANISOU 1657 N ARG A1008 12992 10215 9053 220 338 277 N ATOM 1658 CA ARG A1008 12.756 1.702 5.633 1.00 84.85 C ANISOU 1658 CA ARG A1008 13082 10168 8990 270 334 292 C ATOM 1659 C ARG A1008 13.592 2.493 6.657 1.00 87.93 C ANISOU 1659 C ARG A1008 13519 10494 9397 190 357 307 C ATOM 1660 O ARG A1008 13.491 3.717 6.711 1.00 87.85 O ANISOU 1660 O ARG A1008 13632 10417 9332 202 385 326 O ATOM 1661 CB ARG A1008 11.348 1.386 6.177 1.00 85.49 C ANISOU 1661 CB ARG A1008 13117 10303 9062 344 287 267 C ATOM 1662 CG ARG A1008 10.357 2.557 6.083 1.00 99.64 C ANISOU 1662 CG ARG A1008 15007 12083 10767 450 280 279 C ATOM 1663 CD ARG A1008 10.283 3.356 7.375 1.00113.83 C ANISOU 1663 CD ARG A1008 16859 13823 12568 436 280 292 C ATOM 1664 NE ARG A1008 9.489 4.580 7.254 1.00124.94 N ANISOU 1664 NE ARG A1008 18390 15199 13883 548 287 311 N ATOM 1665 CZ ARG A1008 9.634 5.645 8.040 1.00142.33 C ANISOU 1665 CZ ARG A1008 20705 17313 16062 540 312 333 C ATOM 1666 NH1 ARG A1008 10.562 5.658 8.990 1.00131.05 N ANISOU 1666 NH1 ARG A1008 19264 15833 14695 415 329 333 N ATOM 1667 NH2 ARG A1008 8.861 6.709 7.874 1.00130.48 N ANISOU 1667 NH2 ARG A1008 19332 15779 14466 664 324 353 N ATOM 1668 N ILE A1009 14.442 1.790 7.431 1.00 83.78 N ANISOU 1668 N ILE A1009 12902 9993 8936 113 351 296 N ATOM 1669 CA ILE A1009 15.345 2.381 8.418 1.00 83.59 C ANISOU 1669 CA ILE A1009 12890 9944 8926 26 368 295 C ATOM 1670 C ILE A1009 16.527 3.056 7.685 1.00 89.49 C ANISOU 1670 C ILE A1009 13689 10666 9648 -58 429 295 C ATOM 1671 O ILE A1009 16.835 4.214 7.971 1.00 89.79 O ANISOU 1671 O ILE A1009 13826 10643 9648 -117 470 294 O ATOM 1672 CB ILE A1009 15.806 1.310 9.459 1.00 85.62 C ANISOU 1672 CB ILE A1009 13025 10262 9245 -1 335 281 C ATOM 1673 CG1 ILE A1009 14.675 0.999 10.462 1.00 85.05 C ANISOU 1673 CG1 ILE A1009 12937 10192 9186 54 293 278 C ATOM 1674 CG2 ILE A1009 17.092 1.733 10.192 1.00 86.64 C ANISOU 1674 CG2 ILE A1009 13129 10411 9381 -98 353 267 C ATOM 1675 CD1 ILE A1009 14.767 -0.346 11.179 1.00 89.51 C ANISOU 1675 CD1 ILE A1009 13405 10803 9799 63 269 270 C ATOM 1676 N ASP A1010 17.161 2.339 6.735 1.00 86.99 N ANISOU 1676 N ASP A1010 13315 10392 9348 -70 443 291 N ATOM 1677 CA ASP A1010 18.332 2.802 5.991 1.00 87.93 C ANISOU 1677 CA ASP A1010 13460 10505 9444 -158 506 283 C ATOM 1678 C ASP A1010 18.020 3.871 4.934 1.00 94.11 C ANISOU 1678 C ASP A1010 14403 11201 10154 -143 562 305 C ATOM 1679 O ASP A1010 18.742 4.869 4.864 1.00 94.44 O ANISOU 1679 O ASP A1010 14536 11190 10157 -239 631 298 O ATOM 1680 CB ASP A1010 19.041 1.611 5.324 1.00 89.50 C ANISOU 1680 CB ASP A1010 13543 10782 9681 -157 503 272 C ATOM 1681 CG ASP A1010 19.701 0.638 6.286 1.00 98.22 C ANISOU 1681 CG ASP A1010 14509 11971 10839 -170 468 253 C ATOM 1682 OD1 ASP A1010 20.146 1.078 7.367 1.00 98.97 O ANISOU 1682 OD1 ASP A1010 14583 12086 10936 -227 463 237 O ATOM 1683 OD2 ASP A1010 19.834 -0.548 5.928 1.00103.65 O ANISOU 1683 OD2 ASP A1010 15119 12707 11557 -121 452 252 O ATOM 1684 N GLU A1011 16.980 3.655 4.104 1.00 92.01 N ANISOU 1684 N GLU A1011 14176 10927 9859 -26 539 327 N ATOM 1685 CA GLU A1011 16.599 4.561 3.012 1.00 93.39 C ANISOU 1685 CA GLU A1011 14507 11030 9946 27 586 354 C ATOM 1686 C GLU A1011 15.651 5.691 3.452 1.00100.96 C ANISOU 1686 C GLU A1011 15613 11909 10839 101 591 377 C ATOM 1687 O GLU A1011 15.721 6.791 2.896 1.00101.62 O ANISOU 1687 O GLU A1011 15873 11898 10841 109 660 402 O ATOM 1688 CB GLU A1011 15.952 3.785 1.850 1.00 94.27 C ANISOU 1688 CB GLU A1011 14581 11196 10041 131 556 359 C ATOM 1689 CG GLU A1011 16.849 2.748 1.188 1.00100.94 C ANISOU 1689 CG GLU A1011 15316 12104 10934 76 565 341 C ATOM 1690 CD GLU A1011 17.898 3.238 0.206 1.00118.49 C ANISOU 1690 CD GLU A1011 17609 14292 13120 3 645 348 C ATOM 1691 OE1 GLU A1011 18.071 4.468 0.049 1.00113.86 O ANISOU 1691 OE1 GLU A1011 17177 13616 12469 -28 709 367 O ATOM 1692 OE2 GLU A1011 18.589 2.372 -0.375 1.00110.90 O ANISOU 1692 OE2 GLU A1011 16554 13390 12194 -29 652 331 O ATOM 1693 N GLY A1012 14.767 5.406 4.408 1.00 99.17 N ANISOU 1693 N GLY A1012 15325 11716 10639 161 527 370 N ATOM 1694 CA GLY A1012 13.791 6.371 4.904 1.00100.33 C ANISOU 1694 CA GLY A1012 15592 11805 10724 250 523 388 C ATOM 1695 C GLY A1012 12.535 6.431 4.059 1.00106.76 C ANISOU 1695 C GLY A1012 16449 12653 11462 423 493 404 C ATOM 1696 O GLY A1012 12.396 5.668 3.099 1.00106.10 O ANISOU 1696 O GLY A1012 16294 12643 11378 462 471 395 O ATOM 1697 N LEU A1013 11.607 7.339 4.413 1.00105.61 N ANISOU 1697 N LEU A1013 16418 12466 11242 535 491 421 N ATOM 1698 CA LEU A1013 10.345 7.519 3.694 1.00106.69 C ANISOU 1698 CA LEU A1013 16592 12660 11284 726 458 431 C ATOM 1699 C LEU A1013 10.060 9.003 3.475 1.00112.37 C ANISOU 1699 C LEU A1013 17555 13261 11880 833 520 477 C ATOM 1700 O LEU A1013 9.864 9.753 4.437 1.00112.17 O ANISOU 1700 O LEU A1013 17616 13163 11841 837 538 485 O ATOM 1701 CB LEU A1013 9.180 6.850 4.450 1.00106.45 C ANISOU 1701 CB LEU A1013 16413 12751 11281 797 375 393 C ATOM 1702 CG LEU A1013 8.146 6.097 3.604 1.00111.47 C ANISOU 1702 CG LEU A1013 16937 13541 11876 916 316 359 C ATOM 1703 CD1 LEU A1013 7.495 4.987 4.407 1.00110.89 C ANISOU 1703 CD1 LEU A1013 16670 13584 11877 879 254 301 C ATOM 1704 CD2 LEU A1013 7.085 7.036 3.036 1.00115.14 C ANISOU 1704 CD2 LEU A1013 17517 14035 12196 1126 309 378 C ATOM 1705 N ARG A1014 10.068 9.424 2.203 1.00110.41 N ANISOU 1705 N ARG A1014 17431 12984 11536 922 560 509 N ATOM 1706 CA ARG A1014 9.803 10.800 1.785 1.00112.10 C ANISOU 1706 CA ARG A1014 17911 13073 11609 1049 634 562 C ATOM 1707 C ARG A1014 8.870 10.769 0.584 1.00117.53 C ANISOU 1707 C ARG A1014 18623 13856 12177 1268 599 578 C ATOM 1708 O ARG A1014 9.182 10.126 -0.419 1.00116.87 O ANISOU 1708 O ARG A1014 18470 13834 12099 1249 590 571 O ATOM 1709 CB ARG A1014 11.109 11.557 1.473 1.00113.56 C ANISOU 1709 CB ARG A1014 18282 13084 11781 898 757 589 C ATOM 1710 CG ARG A1014 11.944 11.885 2.708 1.00125.91 C ANISOU 1710 CG ARG A1014 19856 14558 13426 701 802 566 C ATOM 1711 CD ARG A1014 13.190 12.674 2.368 1.00139.45 C ANISOU 1711 CD ARG A1014 21752 16119 15115 537 934 575 C ATOM 1712 NE ARG A1014 14.283 12.388 3.300 1.00149.78 N ANISOU 1712 NE ARG A1014 22942 17434 16535 300 949 524 N ATOM 1713 CZ ARG A1014 15.490 12.944 3.239 1.00164.89 C ANISOU 1713 CZ ARG A1014 24952 19252 18444 106 1059 504 C ATOM 1714 NH1 ARG A1014 15.774 13.833 2.295 1.00152.92 N ANISOU 1714 NH1 ARG A1014 23677 17602 16822 108 1178 536 N ATOM 1715 NH2 ARG A1014 16.420 12.619 4.127 1.00150.97 N ANISOU 1715 NH2 ARG A1014 23050 17538 16776 -91 1057 448 N ATOM 1716 N LEU A1015 7.711 11.436 0.694 1.00115.61 N ANISOU 1716 N LEU A1015 18468 13641 11819 1485 575 596 N ATOM 1717 CA LEU A1015 6.692 11.453 -0.361 1.00116.41 C ANISOU 1717 CA LEU A1015 18576 13869 11784 1726 530 603 C ATOM 1718 C LEU A1015 6.958 12.545 -1.426 1.00122.45 C ANISOU 1718 C LEU A1015 19636 14495 12395 1849 626 676 C ATOM 1719 O LEU A1015 6.233 12.616 -2.421 1.00123.08 O ANISOU 1719 O LEU A1015 19744 14676 12343 2060 596 689 O ATOM 1720 CB LEU A1015 5.279 11.603 0.249 1.00116.62 C ANISOU 1720 CB LEU A1015 18536 14029 11746 1921 454 578 C ATOM 1721 CG LEU A1015 4.674 10.395 1.021 1.00119.65 C ANISOU 1721 CG LEU A1015 18615 14603 12244 1849 351 495 C ATOM 1722 CD1 LEU A1015 4.917 9.059 0.314 1.00118.63 C ANISOU 1722 CD1 LEU A1015 18276 14605 12192 1741 305 443 C ATOM 1723 CD2 LEU A1015 5.138 10.348 2.471 1.00121.12 C ANISOU 1723 CD2 LEU A1015 18766 14696 12560 1672 365 484 C ATOM 1724 N LYS A1016 8.021 13.350 -1.239 1.00119.67 N ANISOU 1724 N LYS A1016 19498 13920 12053 1708 747 717 N ATOM 1725 CA LYS A1016 8.438 14.396 -2.173 1.00121.27 C ANISOU 1725 CA LYS A1016 20010 13951 12116 1778 867 785 C ATOM 1726 C LYS A1016 9.791 14.041 -2.789 1.00124.95 C ANISOU 1726 C LYS A1016 20472 14345 12657 1548 938 781 C ATOM 1727 O LYS A1016 10.617 13.425 -2.109 1.00123.37 O ANISOU 1727 O LYS A1016 20111 14152 12613 1309 930 735 O ATOM 1728 CB LYS A1016 8.512 15.753 -1.459 1.00125.12 C ANISOU 1728 CB LYS A1016 20788 14222 12529 1798 976 828 C ATOM 1729 N ILE A1017 10.020 14.428 -4.069 1.00122.70 N ANISOU 1729 N ILE A1017 20366 14000 12255 1629 1008 827 N ATOM 1730 CA ILE A1017 11.282 14.162 -4.775 1.00122.53 C ANISOU 1730 CA ILE A1017 20358 13914 12285 1425 1087 824 C ATOM 1731 C ILE A1017 12.404 14.934 -4.075 1.00127.72 C ANISOU 1731 C ILE A1017 21176 14365 12986 1188 1221 823 C ATOM 1732 O ILE A1017 12.376 16.164 -4.034 1.00128.79 O ANISOU 1732 O ILE A1017 21618 14312 13002 1242 1337 869 O ATOM 1733 CB ILE A1017 11.238 14.470 -6.305 1.00126.84 C ANISOU 1733 CB ILE A1017 21081 14434 12679 1573 1141 876 C ATOM 1734 CG1 ILE A1017 10.043 13.777 -7.002 1.00127.19 C ANISOU 1734 CG1 ILE A1017 20965 14706 12656 1822 1006 866 C ATOM 1735 CG2 ILE A1017 12.569 14.077 -6.975 1.00127.11 C ANISOU 1735 CG2 ILE A1017 21092 14422 12783 1342 1218 861 C ATOM 1736 CD1 ILE A1017 9.695 14.288 -8.418 1.00135.59 C ANISOU 1736 CD1 ILE A1017 22237 15758 13523 2048 1047 926 C ATOM 1737 N TYR A1018 13.361 14.197 -3.492 1.00123.92 N ANISOU 1737 N TYR A1018 20487 13930 12669 931 1207 763 N ATOM 1738 CA TYR A1018 14.499 14.774 -2.781 1.00124.42 C ANISOU 1738 CA TYR A1018 20640 13850 12785 677 1321 737 C ATOM 1739 C TYR A1018 15.810 14.455 -3.517 1.00129.52 C ANISOU 1739 C TYR A1018 21252 14485 13473 468 1400 713 C ATOM 1740 O TYR A1018 15.790 13.811 -4.569 1.00128.34 O ANISOU 1740 O TYR A1018 21028 14424 13312 534 1366 724 O ATOM 1741 CB TYR A1018 14.535 14.307 -1.303 1.00124.21 C ANISOU 1741 CB TYR A1018 20401 13898 12896 560 1241 682 C ATOM 1742 CG TYR A1018 14.777 12.827 -1.074 1.00124.00 C ANISOU 1742 CG TYR A1018 20026 14068 13021 478 1119 629 C ATOM 1743 CD1 TYR A1018 13.729 11.912 -1.126 1.00124.97 C ANISOU 1743 CD1 TYR A1018 19961 14352 13170 643 983 625 C ATOM 1744 CD2 TYR A1018 16.035 12.355 -0.708 1.00124.08 C ANISOU 1744 CD2 TYR A1018 19898 14106 13141 235 1146 577 C ATOM 1745 CE1 TYR A1018 13.937 10.556 -0.874 1.00124.20 C ANISOU 1745 CE1 TYR A1018 19577 14410 13204 565 888 578 C ATOM 1746 CE2 TYR A1018 16.256 11.001 -0.455 1.00123.43 C ANISOU 1746 CE2 TYR A1018 19520 14191 13185 182 1042 535 C ATOM 1747 CZ TYR A1018 15.203 10.104 -0.540 1.00129.45 C ANISOU 1747 CZ TYR A1018 20130 15083 13972 345 919 539 C ATOM 1748 OH TYR A1018 15.413 8.767 -0.290 1.00128.31 O ANISOU 1748 OH TYR A1018 19728 15081 13944 291 833 498 O ATOM 1749 N LYS A1019 16.935 14.949 -2.983 1.00128.34 N ANISOU 1749 N LYS A1019 21166 14236 13363 217 1511 673 N ATOM 1750 CA LYS A1019 18.257 14.740 -3.557 1.00129.42 C ANISOU 1750 CA LYS A1019 21266 14373 13535 -4 1599 636 C ATOM 1751 C LYS A1019 19.007 13.667 -2.788 1.00134.75 C ANISOU 1751 C LYS A1019 21608 15215 14375 -181 1515 560 C ATOM 1752 O LYS A1019 19.083 13.718 -1.557 1.00133.94 O ANISOU 1752 O LYS A1019 21423 15130 14339 -266 1484 521 O ATOM 1753 CB LYS A1019 19.058 16.049 -3.569 1.00133.78 C ANISOU 1753 CB LYS A1019 22117 14715 13999 -179 1797 629 C ATOM 1754 N ASP A1020 19.571 12.700 -3.531 1.00132.88 N ANISOU 1754 N ASP A1020 21192 15100 14195 -225 1483 540 N ATOM 1755 CA ASP A1020 20.375 11.582 -3.028 1.00132.49 C ANISOU 1755 CA ASP A1020 20837 15217 14285 -366 1412 474 C ATOM 1756 C ASP A1020 21.698 12.115 -2.455 1.00139.54 C ANISOU 1756 C ASP A1020 21739 16079 15200 -636 1524 406 C ATOM 1757 O ASP A1020 22.039 13.283 -2.684 1.00140.88 O ANISOU 1757 O ASP A1020 22160 16091 15275 -732 1671 408 O ATOM 1758 CB ASP A1020 20.640 10.590 -4.185 1.00133.87 C ANISOU 1758 CB ASP A1020 20883 15499 14482 -326 1379 477 C ATOM 1759 CG ASP A1020 20.891 9.145 -3.796 1.00143.00 C ANISOU 1759 CG ASP A1020 21724 16840 15770 -344 1260 434 C ATOM 1760 OD1 ASP A1020 21.874 8.886 -3.069 1.00143.59 O ANISOU 1760 OD1 ASP A1020 21658 16980 15919 -511 1271 377 O ATOM 1761 OD2 ASP A1020 20.170 8.262 -4.306 1.00148.14 O ANISOU 1761 OD2 ASP A1020 22276 17573 16437 -194 1166 455 O ATOM 1762 N THR A1021 22.451 11.265 -1.722 1.00136.58 N ANISOU 1762 N THR A1021 21095 15860 14938 -759 1462 340 N ATOM 1763 CA THR A1021 23.757 11.631 -1.153 1.00137.63 C ANISOU 1763 CA THR A1021 21179 16024 15091 -1017 1551 256 C ATOM 1764 C THR A1021 24.784 11.816 -2.299 1.00142.86 C ANISOU 1764 C THR A1021 21897 16677 15706 -1153 1679 231 C ATOM 1765 O THR A1021 25.824 12.447 -2.098 1.00143.76 O ANISOU 1765 O THR A1021 22047 16780 15795 -1383 1799 159 O ATOM 1766 CB THR A1021 24.212 10.617 -0.075 1.00146.09 C ANISOU 1766 CB THR A1021 21942 17286 16280 -1067 1438 198 C ATOM 1767 OG1 THR A1021 25.342 11.150 0.618 1.00147.86 O ANISOU 1767 OG1 THR A1021 22130 17547 16501 -1305 1521 109 O ATOM 1768 CG2 THR A1021 24.537 9.225 -0.637 1.00143.67 C ANISOU 1768 CG2 THR A1021 21400 17143 16045 -1004 1354 194 C ATOM 1769 N GLU A1022 24.451 11.294 -3.499 1.00139.09 N ANISOU 1769 N GLU A1022 21431 16208 15209 -1016 1656 284 N ATOM 1770 CA GLU A1022 25.248 11.387 -4.721 1.00139.92 C ANISOU 1770 CA GLU A1022 21599 16301 15263 -1104 1767 274 C ATOM 1771 C GLU A1022 24.601 12.370 -5.726 1.00144.78 C ANISOU 1771 C GLU A1022 22552 16715 15742 -1003 1869 351 C ATOM 1772 O GLU A1022 25.005 12.429 -6.892 1.00145.28 O ANISOU 1772 O GLU A1022 22703 16750 15747 -1024 1953 365 O ATOM 1773 CB GLU A1022 25.433 9.995 -5.344 1.00140.24 C ANISOU 1773 CB GLU A1022 21398 16511 15377 -1023 1669 273 C ATOM 1774 CG GLU A1022 26.329 9.083 -4.521 1.00150.09 C ANISOU 1774 CG GLU A1022 22342 17952 16733 -1131 1603 195 C ATOM 1775 CD GLU A1022 26.771 7.787 -5.172 1.00170.63 C ANISOU 1775 CD GLU A1022 24729 20710 19394 -1081 1542 182 C ATOM 1776 OE1 GLU A1022 26.192 7.397 -6.212 1.00167.17 O ANISOU 1776 OE1 GLU A1022 24345 20242 18930 -939 1519 237 O ATOM 1777 OE2 GLU A1022 27.696 7.146 -4.625 1.00164.48 O ANISOU 1777 OE2 GLU A1022 23726 20090 18679 -1174 1516 115 O ATOM 1778 N GLY A1023 23.626 13.142 -5.244 1.00141.21 N ANISOU 1778 N GLY A1023 22292 16129 15233 -888 1864 401 N ATOM 1779 CA GLY A1023 22.923 14.170 -6.006 1.00142.15 C ANISOU 1779 CA GLY A1023 22755 16050 15205 -758 1959 479 C ATOM 1780 C GLY A1023 21.933 13.703 -7.055 1.00145.16 C ANISOU 1780 C GLY A1023 23165 16456 15535 -489 1876 558 C ATOM 1781 O GLY A1023 21.644 14.451 -7.994 1.00146.32 O ANISOU 1781 O GLY A1023 23588 16463 15546 -394 1973 618 O ATOM 1782 N TYR A1024 21.389 12.483 -6.904 1.00139.24 N ANISOU 1782 N TYR A1024 22143 15881 14880 -362 1703 555 N ATOM 1783 CA TYR A1024 20.396 11.929 -7.828 1.00138.16 C ANISOU 1783 CA TYR A1024 21992 15804 14699 -117 1611 610 C ATOM 1784 C TYR A1024 18.970 12.220 -7.352 1.00140.14 C ANISOU 1784 C TYR A1024 22311 16034 14900 112 1521 657 C ATOM 1785 O TYR A1024 18.768 12.532 -6.179 1.00139.47 O ANISOU 1785 O TYR A1024 22212 15923 14857 76 1499 640 O ATOM 1786 CB TYR A1024 20.579 10.412 -7.983 1.00138.14 C ANISOU 1786 CB TYR A1024 21668 16002 14817 -118 1488 570 C ATOM 1787 CG TYR A1024 21.952 9.951 -8.421 1.00140.56 C ANISOU 1787 CG TYR A1024 21861 16366 15177 -315 1556 519 C ATOM 1788 CD1 TYR A1024 22.576 10.508 -9.535 1.00143.98 C ANISOU 1788 CD1 TYR A1024 22473 16715 15519 -378 1692 535 C ATOM 1789 CD2 TYR A1024 22.583 8.885 -7.789 1.00140.37 C ANISOU 1789 CD2 TYR A1024 21551 16495 15289 -416 1481 458 C ATOM 1790 CE1 TYR A1024 23.827 10.064 -9.962 1.00145.17 C ANISOU 1790 CE1 TYR A1024 22506 16938 15715 -557 1755 481 C ATOM 1791 CE2 TYR A1024 23.824 8.419 -8.218 1.00141.61 C ANISOU 1791 CE2 TYR A1024 21590 16729 15486 -572 1538 408 C ATOM 1792 CZ TYR A1024 24.448 9.017 -9.301 1.00150.53 C ANISOU 1792 CZ TYR A1024 22885 17782 16527 -648 1675 416 C ATOM 1793 OH TYR A1024 25.677 8.563 -9.718 1.00151.68 O ANISOU 1793 OH TYR A1024 22903 18019 16709 -804 1734 360 O ATOM 1794 N TYR A1025 17.979 12.104 -8.252 1.00135.58 N ANISOU 1794 N TYR A1025 21795 15488 14230 349 1467 708 N ATOM 1795 CA TYR A1025 16.578 12.316 -7.894 1.00134.69 C ANISOU 1795 CA TYR A1025 21720 15397 14058 586 1375 743 C ATOM 1796 C TYR A1025 15.991 11.013 -7.347 1.00134.60 C ANISOU 1796 C TYR A1025 21383 15587 14170 630 1206 697 C ATOM 1797 O TYR A1025 16.057 9.976 -8.012 1.00133.40 O ANISOU 1797 O TYR A1025 21058 15565 14063 639 1144 673 O ATOM 1798 CB TYR A1025 15.774 12.854 -9.086 1.00137.39 C ANISOU 1798 CB TYR A1025 22279 15700 14222 832 1397 811 C ATOM 1799 CG TYR A1025 16.105 14.292 -9.429 1.00141.36 C ANISOU 1799 CG TYR A1025 23161 15970 14578 830 1572 868 C ATOM 1800 CD1 TYR A1025 15.507 15.349 -8.747 1.00144.14 C ANISOU 1800 CD1 TYR A1025 23731 16189 14846 930 1615 905 C ATOM 1801 CD2 TYR A1025 17.010 14.597 -10.442 1.00143.34 C ANISOU 1801 CD2 TYR A1025 23568 16125 14768 727 1706 884 C ATOM 1802 CE1 TYR A1025 15.808 16.674 -9.059 1.00146.82 C ANISOU 1802 CE1 TYR A1025 24453 16291 15042 926 1793 958 C ATOM 1803 CE2 TYR A1025 17.317 15.919 -10.764 1.00146.23 C ANISOU 1803 CE2 TYR A1025 24311 16259 14991 712 1887 935 C ATOM 1804 CZ TYR A1025 16.713 16.955 -10.070 1.00154.70 C ANISOU 1804 CZ TYR A1025 25612 17188 15978 812 1933 972 C ATOM 1805 OH TYR A1025 17.009 18.260 -10.385 1.00157.93 O ANISOU 1805 OH TYR A1025 26423 17347 16238 797 2127 1022 O ATOM 1806 N THR A1026 15.469 11.064 -6.107 1.00128.81 N ANISOU 1806 N THR A1026 20580 14869 13492 642 1143 680 N ATOM 1807 CA THR A1026 14.911 9.916 -5.384 1.00126.38 C ANISOU 1807 CA THR A1026 19990 14728 13300 663 1001 634 C ATOM 1808 C THR A1026 13.531 10.272 -4.797 1.00129.47 C ANISOU 1808 C THR A1026 20411 15149 13634 858 928 650 C ATOM 1809 O THR A1026 13.271 11.440 -4.510 1.00130.20 O ANISOU 1809 O THR A1026 20726 15110 13635 924 992 690 O ATOM 1810 CB THR A1026 15.903 9.480 -4.277 1.00130.45 C ANISOU 1810 CB THR A1026 20349 15252 13963 435 1004 584 C ATOM 1811 OG1 THR A1026 17.239 9.539 -4.782 1.00129.29 O ANISOU 1811 OG1 THR A1026 20230 15059 13835 256 1102 570 O ATOM 1812 CG2 THR A1026 15.628 8.079 -3.740 1.00126.68 C ANISOU 1812 CG2 THR A1026 19585 14939 13610 427 880 537 C ATOM 1813 N ILE A1027 12.655 9.260 -4.629 1.00124.31 N ANISOU 1813 N ILE A1027 19538 14667 13028 947 802 613 N ATOM 1814 CA ILE A1027 11.310 9.392 -4.053 1.00123.82 C ANISOU 1814 CA ILE A1027 19445 14680 12922 1122 720 609 C ATOM 1815 C ILE A1027 10.946 8.088 -3.302 1.00125.87 C ANISOU 1815 C ILE A1027 19416 15095 13312 1061 612 542 C ATOM 1816 O ILE A1027 11.295 6.999 -3.757 1.00124.79 O ANISOU 1816 O ILE A1027 19120 15048 13246 985 581 506 O ATOM 1817 CB ILE A1027 10.245 9.791 -5.124 1.00127.97 C ANISOU 1817 CB ILE A1027 20074 15270 13277 1381 696 638 C ATOM 1818 CG1 ILE A1027 8.894 10.175 -4.470 1.00128.77 C ANISOU 1818 CG1 ILE A1027 20172 15446 13310 1575 627 634 C ATOM 1819 CG2 ILE A1027 10.075 8.714 -6.209 1.00128.21 C ANISOU 1819 CG2 ILE A1027 19943 15462 13308 1413 636 602 C ATOM 1820 CD1 ILE A1027 8.112 11.272 -5.146 1.00137.62 C ANISOU 1820 CD1 ILE A1027 21523 16535 14230 1838 656 691 C ATOM 1821 N GLY A1028 10.269 8.226 -2.163 1.00121.72 N ANISOU 1821 N GLY A1028 18846 14590 12812 1094 566 528 N ATOM 1822 CA GLY A1028 9.836 7.103 -1.338 1.00120.20 C ANISOU 1822 CA GLY A1028 18415 14525 12729 1041 479 468 C ATOM 1823 C GLY A1028 10.961 6.453 -0.562 1.00122.55 C ANISOU 1823 C GLY A1028 18607 14783 13173 825 495 448 C ATOM 1824 O GLY A1028 11.804 7.147 0.015 1.00122.01 O ANISOU 1824 O GLY A1028 18639 14591 13128 719 558 470 O ATOM 1825 N ILE A1029 10.976 5.109 -0.550 1.00118.10 N ANISOU 1825 N ILE A1029 17844 14329 12698 763 442 400 N ATOM 1826 CA ILE A1029 11.994 4.326 0.153 1.00116.75 C ANISOU 1826 CA ILE A1029 17560 14144 12654 592 449 379 C ATOM 1827 C ILE A1029 13.096 3.942 -0.851 1.00119.79 C ANISOU 1827 C ILE A1029 17943 14516 13058 511 496 384 C ATOM 1828 O ILE A1029 13.014 2.904 -1.514 1.00118.98 O ANISOU 1828 O ILE A1029 17732 14498 12978 516 469 355 O ATOM 1829 CB ILE A1029 11.405 3.095 0.919 1.00118.92 C ANISOU 1829 CB ILE A1029 17649 14524 13012 572 379 329 C ATOM 1830 CG1 ILE A1029 10.160 3.470 1.749 1.00119.35 C ANISOU 1830 CG1 ILE A1029 17700 14616 13033 667 334 317 C ATOM 1831 CG2 ILE A1029 12.458 2.441 1.816 1.00118.86 C ANISOU 1831 CG2 ILE A1029 17555 14488 13117 427 390 319 C ATOM 1832 CD1 ILE A1029 8.852 2.982 1.179 1.00125.84 C ANISOU 1832 CD1 ILE A1029 18440 15577 13795 785 279 272 C ATOM 1833 N GLY A1030 14.083 4.833 -0.969 1.00116.23 N ANISOU 1833 N GLY A1030 17621 13956 12586 434 575 415 N ATOM 1834 CA GLY A1030 15.261 4.708 -1.825 1.00115.90 C ANISOU 1834 CA GLY A1030 17595 13890 12552 339 639 419 C ATOM 1835 C GLY A1030 15.048 4.407 -3.297 1.00118.85 C ANISOU 1835 C GLY A1030 17991 14304 12862 419 644 425 C ATOM 1836 O GLY A1030 15.931 3.819 -3.930 1.00118.30 O ANISOU 1836 O GLY A1030 17865 14256 12827 341 674 413 O ATOM 1837 N HIS A1031 13.895 4.813 -3.863 1.00114.93 N ANISOU 1837 N HIS A1031 17574 13832 12264 583 616 442 N ATOM 1838 CA HIS A1031 13.593 4.573 -5.272 1.00114.79 C ANISOU 1838 CA HIS A1031 17578 13869 12166 678 615 444 C ATOM 1839 C HIS A1031 14.142 5.717 -6.134 1.00118.84 C ANISOU 1839 C HIS A1031 18314 14263 12575 694 712 498 C ATOM 1840 O HIS A1031 13.591 6.819 -6.142 1.00118.81 O ANISOU 1840 O HIS A1031 18488 14187 12466 806 739 540 O ATOM 1841 CB HIS A1031 12.083 4.364 -5.493 1.00115.64 C ANISOU 1841 CB HIS A1031 17638 14097 12202 854 532 422 C ATOM 1842 CG HIS A1031 11.716 3.992 -6.897 1.00119.47 C ANISOU 1842 CG HIS A1031 18116 14673 12603 951 517 410 C ATOM 1843 ND1 HIS A1031 12.013 2.744 -7.415 1.00120.60 N ANISOU 1843 ND1 HIS A1031 18111 14901 12810 878 497 361 N ATOM 1844 CD2 HIS A1031 11.073 4.714 -7.844 1.00122.21 C ANISOU 1844 CD2 HIS A1031 18593 15041 12799 1122 521 439 C ATOM 1845 CE1 HIS A1031 11.549 2.747 -8.653 1.00120.66 C ANISOU 1845 CE1 HIS A1031 18153 14983 12710 992 487 357 C ATOM 1846 NE2 HIS A1031 10.977 3.911 -8.957 1.00122.03 N ANISOU 1846 NE2 HIS A1031 18490 15127 12749 1147 498 404 N ATOM 1847 N LEU A1032 15.249 5.439 -6.841 1.00115.48 N ANISOU 1847 N LEU A1032 17886 13814 12176 583 774 497 N ATOM 1848 CA LEU A1032 15.933 6.371 -7.733 1.00116.46 C ANISOU 1848 CA LEU A1032 18214 13826 12209 562 884 539 C ATOM 1849 C LEU A1032 15.123 6.552 -9.020 1.00121.98 C ANISOU 1849 C LEU A1032 19013 14562 12771 749 873 567 C ATOM 1850 O LEU A1032 14.736 5.568 -9.657 1.00120.93 O ANISOU 1850 O LEU A1032 18742 14559 12648 803 806 534 O ATOM 1851 CB LEU A1032 17.365 5.861 -8.028 1.00116.24 C ANISOU 1851 CB LEU A1032 18111 13797 12259 377 946 514 C ATOM 1852 CG LEU A1032 18.069 6.312 -9.321 1.00121.89 C ANISOU 1852 CG LEU A1032 18972 14450 12890 351 1049 540 C ATOM 1853 CD1 LEU A1032 18.479 7.768 -9.261 1.00123.22 C ANISOU 1853 CD1 LEU A1032 19394 14452 12972 299 1173 580 C ATOM 1854 CD2 LEU A1032 19.283 5.458 -9.595 1.00123.99 C ANISOU 1854 CD2 LEU A1032 19091 14773 13246 197 1078 499 C ATOM 1855 N LEU A1033 14.878 7.819 -9.393 1.00120.67 N ANISOU 1855 N LEU A1033 19100 14280 12469 849 943 625 N ATOM 1856 CA LEU A1033 14.123 8.180 -10.591 1.00121.88 C ANISOU 1856 CA LEU A1033 19385 14460 12463 1055 941 662 C ATOM 1857 C LEU A1033 15.052 8.319 -11.797 1.00128.03 C ANISOU 1857 C LEU A1033 20281 15175 13190 993 1041 685 C ATOM 1858 O LEU A1033 14.833 7.640 -12.800 1.00127.71 O ANISOU 1858 O LEU A1033 20165 15243 13114 1065 1001 670 O ATOM 1859 CB LEU A1033 13.319 9.478 -10.377 1.00122.94 C ANISOU 1859 CB LEU A1033 19757 14499 12457 1232 970 720 C ATOM 1860 CG LEU A1033 12.142 9.413 -9.403 1.00126.90 C ANISOU 1860 CG LEU A1033 20156 15090 12968 1354 865 699 C ATOM 1861 CD1 LEU A1033 11.858 10.773 -8.816 1.00128.16 C ANISOU 1861 CD1 LEU A1033 20563 15096 13036 1438 931 755 C ATOM 1862 CD2 LEU A1033 10.898 8.853 -10.067 1.00129.09 C ANISOU 1862 CD2 LEU A1033 20318 15569 13162 1567 753 673 C ATOM 1863 N THR A1034 16.082 9.193 -11.704 1.00126.62 N ANISOU 1863 N THR A1034 20285 14825 13002 850 1177 715 N ATOM 1864 CA THR A1034 17.041 9.439 -12.789 1.00128.04 C ANISOU 1864 CA THR A1034 20595 14928 13127 767 1295 735 C ATOM 1865 C THR A1034 18.376 10.014 -12.268 1.00133.30 C ANISOU 1865 C THR A1034 21340 15458 13851 514 1429 722 C ATOM 1866 O THR A1034 18.438 10.568 -11.167 1.00132.77 O ANISOU 1866 O THR A1034 21310 15315 13821 440 1449 716 O ATOM 1867 CB THR A1034 16.426 10.363 -13.879 1.00139.75 C ANISOU 1867 CB THR A1034 22360 16334 14405 978 1353 807 C ATOM 1868 OG1 THR A1034 17.280 10.377 -15.025 1.00141.52 O ANISOU 1868 OG1 THR A1034 22678 16514 14581 904 1453 820 O ATOM 1869 CG2 THR A1034 16.152 11.797 -13.387 1.00139.37 C ANISOU 1869 CG2 THR A1034 22607 16099 14247 1043 1444 866 C ATOM 1870 N LYS A1035 19.434 9.879 -13.093 1.00131.15 N ANISOU 1870 N LYS A1035 21087 15166 13578 380 1523 711 N ATOM 1871 CA LYS A1035 20.784 10.394 -12.835 1.00131.86 C ANISOU 1871 CA LYS A1035 21242 15156 13702 126 1665 683 C ATOM 1872 C LYS A1035 20.900 11.829 -13.359 1.00138.91 C ANISOU 1872 C LYS A1035 22506 15840 14435 131 1832 741 C ATOM 1873 O LYS A1035 21.695 12.613 -12.837 1.00139.19 O ANISOU 1873 O LYS A1035 22661 15755 14472 -64 1960 720 O ATOM 1874 CB LYS A1035 21.852 9.504 -13.501 1.00133.57 C ANISOU 1874 CB LYS A1035 21289 15473 13990 -16 1688 636 C ATOM 1875 CG LYS A1035 21.794 8.024 -13.117 1.00138.08 C ANISOU 1875 CG LYS A1035 21525 16234 14705 -10 1541 583 C ATOM 1876 CD LYS A1035 21.755 7.117 -14.345 1.00141.76 C ANISOU 1876 CD LYS A1035 21908 16800 15154 70 1506 580 C ATOM 1877 CE LYS A1035 20.355 6.896 -14.869 1.00146.10 C ANISOU 1877 CE LYS A1035 22486 17401 15626 315 1403 615 C ATOM 1878 NZ LYS A1035 20.361 6.206 -16.182 1.00153.11 N ANISOU 1878 NZ LYS A1035 23336 18369 16469 383 1392 611 N ATOM 1879 N SER A1036 20.103 12.155 -14.403 1.00137.35 N ANISOU 1879 N SER A1036 22494 15605 14087 356 1836 809 N ATOM 1880 CA SER A1036 20.049 13.453 -15.077 1.00139.68 C ANISOU 1880 CA SER A1036 23177 15698 14199 424 1992 879 C ATOM 1881 C SER A1036 19.613 14.577 -14.129 1.00145.30 C ANISOU 1881 C SER A1036 24104 16249 14855 454 2046 909 C ATOM 1882 O SER A1036 18.652 14.398 -13.375 1.00143.87 O ANISOU 1882 O SER A1036 23821 16138 14703 601 1916 913 O ATOM 1883 CB SER A1036 19.097 13.394 -16.270 1.00144.03 C ANISOU 1883 CB SER A1036 23834 16292 14601 712 1942 944 C ATOM 1884 OG SER A1036 19.051 14.624 -16.975 1.00154.86 O ANISOU 1884 OG SER A1036 25600 17460 15777 803 2098 1021 O ATOM 1885 N PRO A1037 20.275 15.758 -14.181 1.00144.59 N ANISOU 1885 N PRO A1037 24327 15937 14672 319 2246 929 N ATOM 1886 CA PRO A1037 19.870 16.865 -13.302 1.00145.59 C ANISOU 1886 CA PRO A1037 24691 15892 14736 347 2313 956 C ATOM 1887 C PRO A1037 18.692 17.645 -13.900 1.00151.44 C ANISOU 1887 C PRO A1037 25739 16528 15274 683 2324 1059 C ATOM 1888 O PRO A1037 18.806 18.835 -14.206 1.00153.17 O ANISOU 1888 O PRO A1037 26347 16513 15336 701 2502 1113 O ATOM 1889 CB PRO A1037 21.150 17.712 -13.172 1.00148.73 C ANISOU 1889 CB PRO A1037 25287 16106 15118 33 2535 917 C ATOM 1890 CG PRO A1037 22.162 17.098 -14.125 1.00153.11 C ANISOU 1890 CG PRO A1037 25727 16740 15708 -128 2587 880 C ATOM 1891 CD PRO A1037 21.429 16.146 -15.012 1.00147.62 C ANISOU 1891 CD PRO A1037 24872 16212 15003 120 2431 919 C ATOM 1892 N SER A1038 17.552 16.953 -14.072 1.00147.32 N ANISOU 1892 N SER A1038 25041 16189 14746 955 2137 1080 N ATOM 1893 CA SER A1038 16.322 17.530 -14.605 1.00148.41 C ANISOU 1893 CA SER A1038 25400 16298 14690 1314 2109 1166 C ATOM 1894 C SER A1038 15.131 17.118 -13.742 1.00151.48 C ANISOU 1894 C SER A1038 25578 16848 15128 1503 1921 1151 C ATOM 1895 O SER A1038 14.830 15.926 -13.633 1.00149.63 O ANISOU 1895 O SER A1038 24989 16847 15017 1508 1755 1096 O ATOM 1896 CB SER A1038 16.110 17.122 -16.061 1.00152.13 C ANISOU 1896 CB SER A1038 25886 16862 15053 1483 2084 1202 C ATOM 1897 OG SER A1038 14.892 17.638 -16.575 1.00161.34 O ANISOU 1897 OG SER A1038 27243 18038 16020 1853 2042 1279 O ATOM 1898 N LEU A1039 14.473 18.111 -13.113 1.00148.94 N ANISOU 1898 N LEU A1039 25486 16397 14707 1648 1960 1196 N ATOM 1899 CA LEU A1039 13.302 17.907 -12.257 1.00147.97 C ANISOU 1899 CA LEU A1039 25206 16410 14607 1839 1804 1185 C ATOM 1900 C LEU A1039 12.092 17.474 -13.100 1.00152.60 C ANISOU 1900 C LEU A1039 25708 17203 15072 2182 1664 1211 C ATOM 1901 O LEU A1039 11.266 16.697 -12.617 1.00151.04 O ANISOU 1901 O LEU A1039 25216 17225 14948 2274 1493 1163 O ATOM 1902 CB LEU A1039 12.990 19.186 -11.455 1.00149.28 C ANISOU 1902 CB LEU A1039 25681 16361 14676 1910 1907 1230 C ATOM 1903 CG LEU A1039 11.911 19.095 -10.365 1.00153.21 C ANISOU 1903 CG LEU A1039 26030 16972 15209 2064 1769 1211 C ATOM 1904 CD1 LEU A1039 12.412 18.341 -9.141 1.00151.36 C ANISOU 1904 CD1 LEU A1039 25477 16820 15211 1782 1696 1122 C ATOM 1905 CD2 LEU A1039 11.447 20.473 -9.955 1.00157.58 C ANISOU 1905 CD2 LEU A1039 26963 17307 15602 2227 1884 1278 C ATOM 1906 N ASN A1040 12.010 17.958 -14.363 1.00150.99 N ANISOU 1906 N ASN A1040 25757 16937 14677 2361 1742 1280 N ATOM 1907 CA ASN A1040 10.944 17.620 -15.310 1.00151.39 C ANISOU 1907 CA ASN A1040 25748 17191 14581 2692 1622 1302 C ATOM 1908 C ASN A1040 11.060 16.164 -15.760 1.00153.26 C ANISOU 1908 C ASN A1040 25595 17683 14954 2589 1484 1223 C ATOM 1909 O ASN A1040 10.039 15.480 -15.841 1.00152.31 O ANISOU 1909 O ASN A1040 25238 17815 14819 2772 1319 1183 O ATOM 1910 CB ASN A1040 10.959 18.559 -16.514 1.00155.00 C ANISOU 1910 CB ASN A1040 26605 17495 14793 2895 1759 1401 C ATOM 1911 CG ASN A1040 10.433 19.934 -16.200 1.00182.31 C ANISOU 1911 CG ASN A1040 30456 20749 18065 3118 1865 1486 C ATOM 1912 OD1 ASN A1040 11.189 20.854 -15.870 1.00178.07 O ANISOU 1912 OD1 ASN A1040 30225 19921 17511 2957 2053 1523 O ATOM 1913 ND2 ASN A1040 9.121 20.106 -16.291 1.00175.56 N ANISOU 1913 ND2 ASN A1040 29602 20047 17057 3492 1753 1514 N ATOM 1914 N ALA A1041 12.301 15.688 -16.026 1.00148.90 N ANISOU 1914 N ALA A1041 24974 17070 14530 2291 1556 1192 N ATOM 1915 CA ALA A1041 12.587 14.304 -16.426 1.00147.07 C ANISOU 1915 CA ALA A1041 24398 17046 14437 2164 1450 1116 C ATOM 1916 C ALA A1041 12.354 13.346 -15.251 1.00148.52 C ANISOU 1916 C ALA A1041 24223 17383 14823 2038 1311 1031 C ATOM 1917 O ALA A1041 11.913 12.213 -15.464 1.00147.16 O ANISOU 1917 O ALA A1041 23761 17436 14717 2063 1175 968 O ATOM 1918 CB ALA A1041 14.015 14.182 -16.935 1.00147.72 C ANISOU 1918 CB ALA A1041 24531 17007 14590 1891 1581 1110 C ATOM 1919 N ALA A1042 12.636 13.816 -14.012 1.00143.98 N ANISOU 1919 N ALA A1042 23685 16682 14339 1901 1353 1026 N ATOM 1920 CA ALA A1042 12.416 13.074 -12.770 1.00141.61 C ANISOU 1920 CA ALA A1042 23093 16496 14217 1790 1240 956 C ATOM 1921 C ALA A1042 10.915 12.949 -12.510 1.00144.66 C ANISOU 1921 C ALA A1042 23378 17055 14530 2059 1100 946 C ATOM 1922 O ALA A1042 10.456 11.902 -12.049 1.00142.98 O ANISOU 1922 O ALA A1042 22858 17035 14432 2028 968 874 O ATOM 1923 CB ALA A1042 13.106 13.774 -11.610 1.00142.19 C ANISOU 1923 CB ALA A1042 23274 16380 14370 1594 1336 959 C ATOM 1924 N LYS A1043 10.150 14.013 -12.847 1.00142.20 N ANISOU 1924 N LYS A1043 23332 16681 14016 2330 1136 1015 N ATOM 1925 CA LYS A1043 8.693 14.051 -12.734 1.00142.26 C ANISOU 1925 CA LYS A1043 23271 16870 13913 2627 1014 1008 C ATOM 1926 C LYS A1043 8.072 13.177 -13.819 1.00145.80 C ANISOU 1926 C LYS A1043 23531 17572 14294 2772 902 967 C ATOM 1927 O LYS A1043 7.043 12.555 -13.573 1.00145.11 O ANISOU 1927 O LYS A1043 23203 17722 14209 2889 764 903 O ATOM 1928 CB LYS A1043 8.166 15.490 -12.828 1.00146.79 C ANISOU 1928 CB LYS A1043 24212 17290 14271 2889 1101 1100 C ATOM 1929 N SER A1044 8.717 13.109 -15.006 1.00142.47 N ANISOU 1929 N SER A1044 23212 17107 13814 2747 968 995 N ATOM 1930 CA SER A1044 8.280 12.300 -16.148 1.00142.25 C ANISOU 1930 CA SER A1044 23028 17305 13717 2862 879 955 C ATOM 1931 C SER A1044 8.407 10.805 -15.848 1.00143.70 C ANISOU 1931 C SER A1044 22828 17669 14101 2650 773 846 C ATOM 1932 O SER A1044 7.503 10.043 -16.193 1.00143.13 O ANISOU 1932 O SER A1044 22538 17852 13993 2766 649 776 O ATOM 1933 CB SER A1044 9.078 12.653 -17.399 1.00146.75 C ANISOU 1933 CB SER A1044 23826 17747 14184 2858 996 1017 C ATOM 1934 OG SER A1044 8.779 13.967 -17.842 1.00157.26 O ANISOU 1934 OG SER A1044 25527 18935 15292 3105 1091 1118 O ATOM 1935 N GLU A1045 9.512 10.393 -15.190 1.00138.61 N ANISOU 1935 N GLU A1045 22108 16899 13657 2344 826 827 N ATOM 1936 CA GLU A1045 9.765 9.003 -14.804 1.00136.58 C ANISOU 1936 CA GLU A1045 21526 16774 13595 2137 746 733 C ATOM 1937 C GLU A1045 8.787 8.559 -13.710 1.00139.97 C ANISOU 1937 C GLU A1045 21741 17348 14092 2169 630 670 C ATOM 1938 O GLU A1045 8.408 7.390 -13.674 1.00138.56 O ANISOU 1938 O GLU A1045 21297 17354 13995 2112 536 583 O ATOM 1939 CB GLU A1045 11.215 8.827 -14.336 1.00136.85 C ANISOU 1939 CB GLU A1045 21561 16637 13799 1837 840 737 C ATOM 1940 N LEU A1046 8.365 9.505 -12.844 1.00137.48 N ANISOU 1940 N LEU A1046 21558 16945 13736 2261 647 711 N ATOM 1941 CA LEU A1046 7.421 9.313 -11.740 1.00137.03 C ANISOU 1941 CA LEU A1046 21340 17001 13723 2309 554 663 C ATOM 1942 C LEU A1046 5.973 9.234 -12.262 1.00142.88 C ANISOU 1942 C LEU A1046 21994 17993 14302 2588 447 623 C ATOM 1943 O LEU A1046 5.238 8.324 -11.868 1.00141.57 O ANISOU 1943 O LEU A1046 21559 18033 14196 2566 343 530 O ATOM 1944 CB LEU A1046 7.578 10.473 -10.725 1.00137.35 C ANISOU 1944 CB LEU A1046 21589 16839 13759 2313 628 727 C ATOM 1945 CG LEU A1046 6.705 10.474 -9.462 1.00141.57 C ANISOU 1945 CG LEU A1046 22001 17450 14338 2358 553 689 C ATOM 1946 CD1 LEU A1046 7.153 9.416 -8.473 1.00139.91 C ANISOU 1946 CD1 LEU A1046 21541 17270 14348 2096 512 621 C ATOM 1947 CD2 LEU A1046 6.754 11.823 -8.783 1.00144.71 C ANISOU 1947 CD2 LEU A1046 22670 17644 14670 2428 638 764 C ATOM 1948 N ASP A1047 5.576 10.186 -13.146 1.00142.18 N ANISOU 1948 N ASP A1047 22133 17891 13997 2849 479 690 N ATOM 1949 CA ASP A1047 4.237 10.273 -13.750 1.00143.64 C ANISOU 1949 CA ASP A1047 22261 18328 13988 3157 383 659 C ATOM 1950 C ASP A1047 3.926 9.056 -14.633 1.00147.37 C ANISOU 1950 C ASP A1047 22476 19056 14463 3129 293 561 C ATOM 1951 O ASP A1047 2.756 8.707 -14.778 1.00147.55 O ANISOU 1951 O ASP A1047 22317 19354 14391 3292 185 481 O ATOM 1952 CB ASP A1047 4.074 11.569 -14.580 1.00147.58 C ANISOU 1952 CB ASP A1047 23101 18726 14245 3445 455 766 C ATOM 1953 CG ASP A1047 3.783 12.837 -13.789 1.00156.91 C ANISOU 1953 CG ASP A1047 24530 19744 15345 3596 514 845 C ATOM 1954 OD1 ASP A1047 2.800 12.847 -13.019 1.00157.09 O ANISOU 1954 OD1 ASP A1047 24421 19915 15352 3714 429 800 O ATOM 1955 OD2 ASP A1047 4.474 13.851 -14.019 1.00163.04 O ANISOU 1955 OD2 ASP A1047 25646 20252 16049 3616 651 949 O ATOM 1956 N LYS A1048 4.964 8.421 -15.217 1.00143.20 N ANISOU 1956 N LYS A1048 21929 18444 14035 2921 342 558 N ATOM 1957 CA LYS A1048 4.818 7.257 -16.093 1.00142.89 C ANISOU 1957 CA LYS A1048 21673 18613 14005 2869 276 467 C ATOM 1958 C LYS A1048 4.766 5.944 -15.306 1.00145.11 C ANISOU 1958 C LYS A1048 21650 18999 14487 2630 215 355 C ATOM 1959 O LYS A1048 3.930 5.095 -15.619 1.00144.80 O ANISOU 1959 O LYS A1048 21386 19215 14415 2661 124 246 O ATOM 1960 CB LYS A1048 5.956 7.204 -17.124 1.00145.49 C ANISOU 1960 CB LYS A1048 22141 18801 14338 2772 366 518 C ATOM 1961 N ALA A1049 5.656 5.774 -14.298 1.00140.34 N ANISOU 1961 N ALA A1049 21044 18201 14078 2394 269 377 N ATOM 1962 CA ALA A1049 5.752 4.570 -13.461 1.00138.61 C ANISOU 1962 CA ALA A1049 20579 18035 14050 2167 230 289 C ATOM 1963 C ALA A1049 4.461 4.296 -12.682 1.00143.10 C ANISOU 1963 C ALA A1049 20964 18802 14604 2240 136 205 C ATOM 1964 O ALA A1049 4.102 3.131 -12.502 1.00142.18 O ANISOU 1964 O ALA A1049 20618 18833 14569 2118 86 98 O ATOM 1965 CB ALA A1049 6.918 4.689 -12.496 1.00137.96 C ANISOU 1965 CB ALA A1049 20566 17713 14142 1954 307 343 C ATOM 1966 N ILE A1050 3.768 5.362 -12.236 1.00140.78 N ANISOU 1966 N ILE A1050 20780 18510 14201 2436 123 250 N ATOM 1967 CA ILE A1050 2.502 5.277 -11.500 1.00141.04 C ANISOU 1967 CA ILE A1050 20653 18739 14196 2535 39 175 C ATOM 1968 C ILE A1050 1.329 5.385 -12.500 1.00147.57 C ANISOU 1968 C ILE A1050 21413 19850 14806 2795 -38 117 C ATOM 1969 O ILE A1050 0.286 4.763 -12.287 1.00147.60 O ANISOU 1969 O ILE A1050 21185 20112 14785 2817 -120 -1 O ATOM 1970 CB ILE A1050 2.445 6.350 -10.369 1.00143.96 C ANISOU 1970 CB ILE A1050 21173 18952 14574 2600 71 251 C ATOM 1971 CG1 ILE A1050 3.537 6.076 -9.314 1.00142.61 C ANISOU 1971 CG1 ILE A1050 21013 18553 14619 2326 132 281 C ATOM 1972 CG2 ILE A1050 1.057 6.430 -9.698 1.00145.12 C ANISOU 1972 CG2 ILE A1050 21174 19316 14648 2749 -13 180 C ATOM 1973 CD1 ILE A1050 4.073 7.280 -8.635 1.00149.69 C ANISOU 1973 CD1 ILE A1050 22150 19207 15517 2347 209 386 C ATOM 1974 N GLY A1051 1.532 6.132 -13.587 1.00145.82 N ANISOU 1974 N GLY A1051 21391 19588 14427 2979 -7 194 N ATOM 1975 CA GLY A1051 0.519 6.340 -14.618 1.00147.79 C ANISOU 1975 CA GLY A1051 21607 20102 14445 3257 -78 153 C ATOM 1976 C GLY A1051 -0.582 7.262 -14.139 1.00153.76 C ANISOU 1976 C GLY A1051 22400 20975 15046 3537 -124 164 C ATOM 1977 O GLY A1051 -1.767 6.977 -14.330 1.00154.47 O ANISOU 1977 O GLY A1051 22291 21388 15014 3688 -222 58 O ATOM 1978 N ARG A1052 -0.183 8.370 -13.487 1.00150.77 N ANISOU 1978 N ARG A1052 22277 20339 14669 3600 -50 286 N ATOM 1979 CA ARG A1052 -1.078 9.367 -12.904 1.00151.97 C ANISOU 1979 CA ARG A1052 22517 20539 14686 3863 -72 318 C ATOM 1980 C ARG A1052 -0.411 10.750 -12.910 1.00157.35 C ANISOU 1980 C ARG A1052 23595 20898 15292 3985 45 479 C ATOM 1981 O ARG A1052 0.769 10.864 -13.248 1.00156.08 O ANISOU 1981 O ARG A1052 23610 20486 15207 3824 142 553 O ATOM 1982 CB ARG A1052 -1.434 8.942 -11.463 1.00150.32 C ANISOU 1982 CB ARG A1052 22116 20360 14638 3701 -106 249 C ATOM 1983 CG ARG A1052 -2.786 9.432 -10.957 1.00160.09 C ANISOU 1983 CG ARG A1052 23272 21823 15733 3961 -180 204 C ATOM 1984 CD ARG A1052 -2.914 9.280 -9.451 1.00164.98 C ANISOU 1984 CD ARG A1052 23791 22381 16515 3799 -181 174 C ATOM 1985 NE ARG A1052 -2.337 10.414 -8.724 1.00168.81 N ANISOU 1985 NE ARG A1052 24569 22550 17020 3832 -90 304 N ATOM 1986 CZ ARG A1052 -1.124 10.427 -8.180 1.00178.91 C ANISOU 1986 CZ ARG A1052 25975 23524 18481 3573 -1 370 C ATOM 1987 NH1 ARG A1052 -0.693 11.503 -7.536 1.00164.89 N ANISOU 1987 NH1 ARG A1052 24463 21486 16703 3608 83 472 N ATOM 1988 NH2 ARG A1052 -0.332 9.367 -8.275 1.00163.63 N ANISOU 1988 NH2 ARG A1052 23902 21549 16721 3281 7 328 N ATOM 1989 N ASN A1053 -1.179 11.793 -12.552 1.00156.25 N ANISOU 1989 N ASN A1053 23601 20775 14994 4270 41 527 N ATOM 1990 CA ASN A1053 -0.735 13.181 -12.435 1.00157.45 C ANISOU 1990 CA ASN A1053 24149 20624 15050 4412 160 671 C ATOM 1991 C ASN A1053 -0.191 13.392 -11.011 1.00160.35 C ANISOU 1991 C ASN A1053 24560 20754 15611 4181 220 695 C ATOM 1992 O ASN A1053 -0.907 13.861 -10.120 1.00160.55 O ANISOU 1992 O ASN A1053 24582 20817 15604 4305 195 688 O ATOM 1993 CB ASN A1053 -1.881 14.155 -12.779 1.00161.47 C ANISOU 1993 CB ASN A1053 24796 21282 15275 4859 126 707 C ATOM 1994 CG ASN A1053 -3.260 13.678 -12.372 1.00186.23 C ANISOU 1994 CG ASN A1053 27607 24800 18354 5008 -18 582 C ATOM 1995 OD1 ASN A1053 -3.689 13.828 -11.223 1.00180.64 O ANISOU 1995 OD1 ASN A1053 26826 24096 17712 4989 -36 556 O ATOM 1996 ND2 ASN A1053 -3.983 13.086 -13.311 1.00178.79 N ANISOU 1996 ND2 ASN A1053 26453 24196 17281 5150 -121 493 N ATOM 1997 N THR A1054 1.074 12.984 -10.798 1.00155.20 N ANISOU 1997 N THR A1054 23927 19881 15160 3843 295 712 N ATOM 1998 CA THR A1054 1.756 13.040 -9.501 1.00153.35 C ANISOU 1998 CA THR A1054 23707 19436 15124 3584 350 722 C ATOM 1999 C THR A1054 2.094 14.473 -9.083 1.00157.70 C ANISOU 1999 C THR A1054 24631 19695 15592 3677 475 835 C ATOM 2000 O THR A1054 1.771 14.863 -7.958 1.00156.95 O ANISOU 2000 O THR A1054 24547 19551 15536 3681 475 833 O ATOM 2001 CB THR A1054 3.034 12.180 -9.513 1.00159.19 C ANISOU 2001 CB THR A1054 24353 20056 16075 3223 392 703 C ATOM 2002 OG1 THR A1054 3.911 12.638 -10.543 1.00158.55 O ANISOU 2002 OG1 THR A1054 24512 19803 15925 3217 493 780 O ATOM 2003 CG2 THR A1054 2.746 10.692 -9.676 1.00156.66 C ANISOU 2003 CG2 THR A1054 23670 19988 15865 3091 282 586 C ATOM 2004 N ASN A1055 2.756 15.240 -9.985 1.00155.06 N ANISOU 2004 N ASN A1055 24611 19161 15142 3740 591 929 N ATOM 2005 CA ASN A1055 3.227 16.620 -9.795 1.00155.97 C ANISOU 2005 CA ASN A1055 25138 18961 15163 3802 744 1038 C ATOM 2006 C ASN A1055 4.302 16.681 -8.675 1.00157.89 C ANISOU 2006 C ASN A1055 25411 18965 15616 3451 830 1035 C ATOM 2007 O ASN A1055 4.406 17.677 -7.951 1.00158.07 O ANISOU 2007 O ASN A1055 25676 18779 15604 3470 923 1086 O ATOM 2008 CB ASN A1055 2.064 17.596 -9.535 1.00158.64 C ANISOU 2008 CB ASN A1055 25638 19341 15295 4172 729 1078 C ATOM 2009 N GLY A1056 5.099 15.611 -8.579 1.00152.21 N ANISOU 2009 N GLY A1056 24449 18285 15100 3142 801 974 N ATOM 2010 CA GLY A1056 6.193 15.476 -7.621 1.00150.30 C ANISOU 2010 CA GLY A1056 24181 17867 15058 2802 866 957 C ATOM 2011 C GLY A1056 5.840 14.924 -6.253 1.00151.83 C ANISOU 2011 C GLY A1056 24126 18156 15408 2688 778 889 C ATOM 2012 O GLY A1056 6.741 14.578 -5.485 1.00149.85 O ANISOU 2012 O GLY A1056 23793 17812 15331 2404 808 862 O ATOM 2013 N VAL A1057 4.535 14.849 -5.929 1.00148.46 N ANISOU 2013 N VAL A1057 23576 17924 14909 2913 672 858 N ATOM 2014 CA VAL A1057 4.050 14.358 -4.634 1.00146.98 C ANISOU 2014 CA VAL A1057 23160 17838 14848 2832 590 792 C ATOM 2015 C VAL A1057 3.291 13.031 -4.835 1.00149.58 C ANISOU 2015 C VAL A1057 23124 18477 15230 2841 447 695 C ATOM 2016 O VAL A1057 2.526 12.891 -5.792 1.00150.04 O ANISOU 2016 O VAL A1057 23136 18723 15151 3054 389 679 O ATOM 2017 CB VAL A1057 3.186 15.426 -3.894 1.00152.20 C ANISOU 2017 CB VAL A1057 23987 18453 15388 3056 604 826 C ATOM 2018 CG1 VAL A1057 2.753 14.943 -2.509 1.00150.75 C ANISOU 2018 CG1 VAL A1057 23578 18361 15341 2953 531 759 C ATOM 2019 CG2 VAL A1057 3.929 16.758 -3.775 1.00153.16 C ANISOU 2019 CG2 VAL A1057 24503 18250 15441 3042 765 917 C ATOM 2020 N ILE A1058 3.533 12.056 -3.937 1.00144.25 N ANISOU 2020 N ILE A1058 22203 17856 14749 2604 398 626 N ATOM 2021 CA ILE A1058 2.908 10.726 -3.941 1.00143.06 C ANISOU 2021 CA ILE A1058 21718 17967 14673 2554 285 525 C ATOM 2022 C ILE A1058 2.302 10.427 -2.549 1.00146.16 C ANISOU 2022 C ILE A1058 21947 18431 15156 2498 231 469 C ATOM 2023 O ILE A1058 2.560 11.174 -1.602 1.00145.54 O ANISOU 2023 O ILE A1058 22006 18186 15107 2466 282 512 O ATOM 2024 CB ILE A1058 3.899 9.612 -4.405 1.00144.80 C ANISOU 2024 CB ILE A1058 21804 18178 15035 2305 291 494 C ATOM 2025 CG1 ILE A1058 5.148 9.511 -3.491 1.00143.84 C ANISOU 2025 CG1 ILE A1058 21711 17851 15090 2030 357 515 C ATOM 2026 CG2 ILE A1058 4.280 9.794 -5.881 1.00146.41 C ANISOU 2026 CG2 ILE A1058 22133 18364 15131 2387 328 534 C ATOM 2027 CD1 ILE A1058 5.838 8.164 -3.502 1.00149.18 C ANISOU 2027 CD1 ILE A1058 22175 18577 15928 1799 333 459 C ATOM 2028 N THR A1059 1.487 9.355 -2.435 1.00142.37 N ANISOU 2028 N THR A1059 21183 18198 14714 2480 137 368 N ATOM 2029 CA THR A1059 0.849 8.968 -1.170 1.00141.60 C ANISOU 2029 CA THR A1059 20917 18187 14697 2420 90 306 C ATOM 2030 C THR A1059 1.576 7.786 -0.511 1.00143.83 C ANISOU 2030 C THR A1059 21032 18431 15186 2120 90 261 C ATOM 2031 O THR A1059 2.411 7.138 -1.148 1.00142.79 O ANISOU 2031 O THR A1059 20875 18256 15123 1982 110 262 O ATOM 2032 CB THR A1059 -0.641 8.644 -1.368 1.00150.21 C ANISOU 2032 CB THR A1059 21814 19585 15674 2604 -1 215 C ATOM 2033 OG1 THR A1059 -0.789 7.650 -2.382 1.00148.71 O ANISOU 2033 OG1 THR A1059 21454 19574 15474 2565 -44 143 O ATOM 2034 CG2 THR A1059 -1.477 9.874 -1.692 1.00150.92 C ANISOU 2034 CG2 THR A1059 22062 19727 15553 2934 -7 258 C ATOM 2035 N LYS A1060 1.249 7.518 0.773 1.00139.67 N ANISOU 2035 N LYS A1060 20401 17920 14747 2035 70 224 N ATOM 2036 CA LYS A1060 1.811 6.434 1.586 1.00137.91 C ANISOU 2036 CA LYS A1060 20033 17664 14704 1782 71 184 C ATOM 2037 C LYS A1060 1.465 5.055 1.012 1.00141.30 C ANISOU 2037 C LYS A1060 20242 18278 15169 1698 27 90 C ATOM 2038 O LYS A1060 2.238 4.112 1.183 1.00139.83 O ANISOU 2038 O LYS A1060 19986 18031 15113 1499 46 76 O ATOM 2039 CB LYS A1060 1.309 6.538 3.033 1.00140.12 C ANISOU 2039 CB LYS A1060 20261 17946 15034 1754 57 162 C ATOM 2040 N ASP A1061 0.305 4.946 0.339 1.00138.73 N ANISOU 2040 N ASP A1061 19810 18182 14718 1853 -27 22 N ATOM 2041 CA ASP A1061 -0.172 3.717 -0.291 1.00138.42 C ANISOU 2041 CA ASP A1061 19565 18342 14684 1782 -63 -85 C ATOM 2042 C ASP A1061 0.535 3.487 -1.636 1.00140.60 C ANISOU 2042 C ASP A1061 19896 18589 14937 1773 -46 -61 C ATOM 2043 O ASP A1061 0.686 2.339 -2.060 1.00139.43 O ANISOU 2043 O ASP A1061 19619 18509 14848 1634 -48 -128 O ATOM 2044 CB ASP A1061 -1.700 3.783 -0.478 1.00142.03 C ANISOU 2044 CB ASP A1061 19879 19087 15000 1955 -128 -180 C ATOM 2045 CG ASP A1061 -2.377 2.476 -0.859 1.00155.15 C ANISOU 2045 CG ASP A1061 21301 20982 16668 1847 -159 -322 C ATOM 2046 OD1 ASP A1061 -1.854 1.400 -0.488 1.00154.77 O ANISOU 2046 OD1 ASP A1061 21182 20862 16762 1614 -126 -356 O ATOM 2047 OD2 ASP A1061 -3.460 2.531 -1.480 1.00163.78 O ANISOU 2047 OD2 ASP A1061 22276 22337 17615 1998 -212 -406 O ATOM 2048 N GLU A1062 0.975 4.581 -2.292 1.00136.79 N ANISOU 2048 N GLU A1062 19618 17994 14362 1917 -19 35 N ATOM 2049 CA GLU A1062 1.676 4.557 -3.579 1.00136.31 C ANISOU 2049 CA GLU A1062 19642 17886 14262 1928 7 72 C ATOM 2050 C GLU A1062 3.169 4.242 -3.408 1.00137.32 C ANISOU 2050 C GLU A1062 19846 17789 14541 1713 74 129 C ATOM 2051 O GLU A1062 3.720 3.500 -4.223 1.00136.46 O ANISOU 2051 O GLU A1062 19693 17690 14467 1623 86 110 O ATOM 2052 CB GLU A1062 1.497 5.891 -4.319 1.00139.16 C ANISOU 2052 CB GLU A1062 20212 18213 14447 2178 21 152 C ATOM 2053 CG GLU A1062 0.186 5.994 -5.082 1.00151.50 C ANISOU 2053 CG GLU A1062 21686 20049 15828 2416 -51 88 C ATOM 2054 CD GLU A1062 -0.153 7.347 -5.683 1.00172.73 C ANISOU 2054 CD GLU A1062 24593 22717 18319 2710 -39 169 C ATOM 2055 OE1 GLU A1062 -1.312 7.516 -6.125 1.00169.10 O ANISOU 2055 OE1 GLU A1062 24052 22503 17696 2937 -105 115 O ATOM 2056 OE2 GLU A1062 0.731 8.234 -5.724 1.00165.88 O ANISOU 2056 OE2 GLU A1062 23982 21596 17449 2717 42 281 O ATOM 2057 N ALA A1063 3.820 4.807 -2.363 1.00132.17 N ANISOU 2057 N ALA A1063 19301 16948 13970 1635 117 192 N ATOM 2058 CA ALA A1063 5.241 4.587 -2.052 1.00130.32 C ANISOU 2058 CA ALA A1063 19123 16523 13870 1437 178 238 C ATOM 2059 C ALA A1063 5.503 3.125 -1.672 1.00131.25 C ANISOU 2059 C ALA A1063 19049 16693 14126 1250 161 171 C ATOM 2060 O ALA A1063 6.532 2.569 -2.060 1.00129.89 O ANISOU 2060 O ALA A1063 18876 16449 14028 1125 196 183 O ATOM 2061 CB ALA A1063 5.681 5.506 -0.921 1.00130.87 C ANISOU 2061 CB ALA A1063 19323 16424 13977 1403 219 297 C ATOM 2062 N GLU A1064 4.555 2.508 -0.927 1.00126.53 N ANISOU 2062 N GLU A1064 18301 16222 13554 1237 115 97 N ATOM 2063 CA GLU A1064 4.605 1.112 -0.487 1.00124.88 C ANISOU 2063 CA GLU A1064 17930 16061 13457 1073 109 28 C ATOM 2064 C GLU A1064 4.470 0.169 -1.684 1.00127.40 C ANISOU 2064 C GLU A1064 18158 16498 13750 1052 101 -36 C ATOM 2065 O GLU A1064 5.086 -0.897 -1.690 1.00126.17 O ANISOU 2065 O GLU A1064 17944 16306 13690 906 127 -61 O ATOM 2066 CB GLU A1064 3.507 0.829 0.551 1.00126.24 C ANISOU 2066 CB GLU A1064 17987 16342 13638 1074 74 -38 C ATOM 2067 N LYS A1065 3.682 0.577 -2.703 1.00124.08 N ANISOU 2067 N LYS A1065 17735 16219 13190 1207 67 -62 N ATOM 2068 CA LYS A1065 3.454 -0.181 -3.935 1.00123.95 C ANISOU 2068 CA LYS A1065 17636 16338 13121 1207 54 -129 C ATOM 2069 C LYS A1065 4.736 -0.269 -4.776 1.00126.14 C ANISOU 2069 C LYS A1065 18014 16479 13436 1149 102 -67 C ATOM 2070 O LYS A1065 5.005 -1.318 -5.366 1.00125.17 O ANISOU 2070 O LYS A1065 17814 16393 13351 1049 115 -119 O ATOM 2071 CB LYS A1065 2.319 0.452 -4.753 1.00127.96 C ANISOU 2071 CB LYS A1065 18126 17042 13451 1419 1 -165 C ATOM 2072 N LEU A1066 5.528 0.824 -4.809 1.00122.04 N ANISOU 2072 N LEU A1066 17670 15799 12901 1202 138 39 N ATOM 2073 CA LEU A1066 6.797 0.903 -5.541 1.00121.22 C ANISOU 2073 CA LEU A1066 17671 15562 12826 1142 195 100 C ATOM 2074 C LEU A1066 7.887 0.094 -4.843 1.00123.06 C ANISOU 2074 C LEU A1066 17860 15679 13218 947 233 106 C ATOM 2075 O LEU A1066 8.662 -0.583 -5.516 1.00121.91 O ANISOU 2075 O LEU A1066 17698 15511 13113 867 264 100 O ATOM 2076 CB LEU A1066 7.264 2.366 -5.694 1.00121.81 C ANISOU 2076 CB LEU A1066 17958 15498 12827 1239 237 200 C ATOM 2077 CG LEU A1066 6.447 3.287 -6.602 1.00127.85 C ANISOU 2077 CG LEU A1066 18825 16341 13411 1463 218 221 C ATOM 2078 CD1 LEU A1066 6.798 4.735 -6.346 1.00128.59 C ANISOU 2078 CD1 LEU A1066 19148 16266 13443 1546 273 317 C ATOM 2079 CD2 LEU A1066 6.667 2.961 -8.071 1.00130.78 C ANISOU 2079 CD2 LEU A1066 19207 16772 13710 1500 226 211 C ATOM 2080 N PHE A1067 7.948 0.181 -3.495 1.00118.98 N ANISOU 2080 N PHE A1067 17328 15097 12781 885 232 118 N ATOM 2081 CA PHE A1067 8.923 -0.498 -2.636 1.00117.63 C ANISOU 2081 CA PHE A1067 17118 14829 12746 729 262 127 C ATOM 2082 C PHE A1067 8.792 -2.028 -2.729 1.00120.04 C ANISOU 2082 C PHE A1067 17287 15207 13114 637 257 52 C ATOM 2083 O PHE A1067 9.810 -2.705 -2.882 1.00119.01 O ANISOU 2083 O PHE A1067 17149 15015 13056 545 294 62 O ATOM 2084 CB PHE A1067 8.773 -0.019 -1.178 1.00119.06 C ANISOU 2084 CB PHE A1067 17312 14953 12973 710 253 148 C ATOM 2085 CG PHE A1067 9.703 -0.633 -0.154 1.00119.71 C ANISOU 2085 CG PHE A1067 17355 14952 13179 574 275 158 C ATOM 2086 CD1 PHE A1067 11.080 -0.457 -0.245 1.00122.53 C ANISOU 2086 CD1 PHE A1067 17766 15209 13581 499 321 205 C ATOM 2087 CD2 PHE A1067 9.199 -1.327 0.938 1.00121.33 C ANISOU 2087 CD2 PHE A1067 17471 15186 13442 527 254 120 C ATOM 2088 CE1 PHE A1067 11.936 -1.009 0.713 1.00122.76 C ANISOU 2088 CE1 PHE A1067 17747 15189 13706 397 335 210 C ATOM 2089 CE2 PHE A1067 10.055 -1.870 1.898 1.00123.36 C ANISOU 2089 CE2 PHE A1067 17703 15371 13796 427 274 135 C ATOM 2090 CZ PHE A1067 11.417 -1.711 1.778 1.00121.24 C ANISOU 2090 CZ PHE A1067 17478 15023 13566 371 310 180 C ATOM 2091 N ASN A1068 7.548 -2.561 -2.685 1.00116.15 N ANISOU 2091 N ASN A1068 16695 14853 12586 663 220 -29 N ATOM 2092 CA ASN A1068 7.263 -3.999 -2.787 1.00115.48 C ANISOU 2092 CA ASN A1068 16498 14836 12544 566 230 -115 C ATOM 2093 C ASN A1068 7.722 -4.569 -4.140 1.00119.06 C ANISOU 2093 C ASN A1068 16952 15314 12973 550 253 -135 C ATOM 2094 O ASN A1068 7.953 -5.774 -4.244 1.00118.39 O ANISOU 2094 O ASN A1068 16817 15225 12942 450 285 -185 O ATOM 2095 CB ASN A1068 5.770 -4.279 -2.570 1.00115.95 C ANISOU 2095 CB ASN A1068 16452 15060 12546 590 193 -211 C ATOM 2096 CG ASN A1068 5.295 -4.121 -1.141 1.00137.70 C ANISOU 2096 CG ASN A1068 19181 17795 15342 568 182 -212 C ATOM 2097 OD1 ASN A1068 6.023 -4.370 -0.170 1.00129.30 O ANISOU 2097 OD1 ASN A1068 18149 16603 14376 487 211 -168 O ATOM 2098 ND2 ASN A1068 4.036 -3.745 -0.980 1.00131.81 N ANISOU 2098 ND2 ASN A1068 18371 17195 14518 645 141 -268 N ATOM 2099 N GLN A1069 7.881 -3.696 -5.156 1.00115.76 N ANISOU 2099 N GLN A1069 16607 14908 12468 653 244 -94 N ATOM 2100 CA GLN A1069 8.332 -4.054 -6.501 1.00115.77 C ANISOU 2100 CA GLN A1069 16625 14932 12432 655 265 -104 C ATOM 2101 C GLN A1069 9.866 -4.004 -6.614 1.00118.31 C ANISOU 2101 C GLN A1069 17026 15101 12826 591 320 -28 C ATOM 2102 O GLN A1069 10.444 -4.848 -7.300 1.00117.62 O ANISOU 2102 O GLN A1069 16918 15008 12765 532 353 -51 O ATOM 2103 CB GLN A1069 7.692 -3.128 -7.546 1.00118.19 C ANISOU 2103 CB GLN A1069 16979 15337 12591 811 232 -97 C ATOM 2104 N ASP A1070 10.517 -3.017 -5.953 1.00114.18 N ANISOU 2104 N ASP A1070 16591 14465 12328 598 336 53 N ATOM 2105 CA ASP A1070 11.975 -2.828 -5.955 1.00113.26 C ANISOU 2105 CA ASP A1070 16537 14225 12270 529 390 115 C ATOM 2106 C ASP A1070 12.693 -3.949 -5.193 1.00115.49 C ANISOU 2106 C ASP A1070 16743 14469 12671 417 411 97 C ATOM 2107 O ASP A1070 13.737 -4.415 -5.652 1.00114.83 O ANISOU 2107 O ASP A1070 16658 14349 12623 366 452 108 O ATOM 2108 CB ASP A1070 12.359 -1.465 -5.348 1.00115.07 C ANISOU 2108 CB ASP A1070 16877 14359 12485 550 406 186 C ATOM 2109 CG ASP A1070 11.897 -0.235 -6.106 1.00123.99 C ANISOU 2109 CG ASP A1070 18134 15487 13489 672 408 224 C ATOM 2110 OD1 ASP A1070 11.884 -0.274 -7.357 1.00124.67 O ANISOU 2110 OD1 ASP A1070 18253 15613 13503 723 420 220 O ATOM 2111 OD2 ASP A1070 11.630 0.795 -5.452 1.00129.40 O ANISOU 2111 OD2 ASP A1070 18904 16118 14143 719 407 262 O ATOM 2112 N VAL A1071 12.138 -4.365 -4.026 1.00111.02 N ANISOU 2112 N VAL A1071 16117 13910 12154 390 386 71 N ATOM 2113 CA VAL A1071 12.659 -5.444 -3.172 1.00109.90 C ANISOU 2113 CA VAL A1071 15920 13729 12108 308 406 57 C ATOM 2114 C VAL A1071 12.552 -6.769 -3.948 1.00113.16 C ANISOU 2114 C VAL A1071 16286 14183 12525 275 431 -5 C ATOM 2115 O VAL A1071 13.503 -7.553 -3.953 1.00112.52 O ANISOU 2115 O VAL A1071 16201 14053 12499 232 471 3 O ATOM 2116 CB VAL A1071 11.931 -5.498 -1.794 1.00113.43 C ANISOU 2116 CB VAL A1071 16334 14176 12588 296 379 44 C ATOM 2117 CG1 VAL A1071 12.347 -6.719 -0.975 1.00112.81 C ANISOU 2117 CG1 VAL A1071 16217 14056 12590 228 407 28 C ATOM 2118 CG2 VAL A1071 12.174 -4.222 -0.994 1.00113.14 C ANISOU 2118 CG2 VAL A1071 16353 14086 12550 319 363 104 C ATOM 2119 N ASP A1072 11.411 -6.979 -4.641 1.00109.58 N ANISOU 2119 N ASP A1072 15801 13829 12005 302 409 -71 N ATOM 2120 CA ASP A1072 11.121 -8.153 -5.471 1.00109.29 C ANISOU 2120 CA ASP A1072 15724 13846 11954 261 434 -148 C ATOM 2121 C ASP A1072 12.117 -8.274 -6.632 1.00110.43 C ANISOU 2121 C ASP A1072 15906 13965 12088 268 469 -124 C ATOM 2122 O ASP A1072 12.533 -9.383 -6.966 1.00109.87 O ANISOU 2122 O ASP A1072 15825 13872 12048 216 513 -158 O ATOM 2123 CB ASP A1072 9.684 -8.077 -6.012 1.00112.35 C ANISOU 2123 CB ASP A1072 16057 14380 12250 295 395 -231 C ATOM 2124 CG ASP A1072 9.261 -9.302 -6.795 1.00127.86 C ANISOU 2124 CG ASP A1072 17973 16415 14192 230 426 -332 C ATOM 2125 OD1 ASP A1072 8.986 -10.345 -6.161 1.00129.65 O ANISOU 2125 OD1 ASP A1072 18174 16620 14466 137 463 -390 O ATOM 2126 OD2 ASP A1072 9.219 -9.222 -8.043 1.00135.15 O ANISOU 2126 OD2 ASP A1072 18898 17410 15045 268 419 -355 O ATOM 2127 N ALA A1073 12.488 -7.134 -7.238 1.00105.47 N ANISOU 2127 N ALA A1073 15333 13333 11409 332 456 -66 N ATOM 2128 CA ALA A1073 13.444 -7.065 -8.340 1.00104.91 C ANISOU 2128 CA ALA A1073 15305 13237 11318 338 493 -38 C ATOM 2129 C ALA A1073 14.877 -7.300 -7.844 1.00106.73 C ANISOU 2129 C ALA A1073 15547 13373 11634 283 539 12 C ATOM 2130 O ALA A1073 15.696 -7.841 -8.592 1.00106.07 O ANISOU 2130 O ALA A1073 15466 13278 11560 264 582 9 O ATOM 2131 CB ALA A1073 13.343 -5.715 -9.030 1.00106.11 C ANISOU 2131 CB ALA A1073 15535 13403 11380 421 478 10 C ATOM 2132 N ALA A1074 15.175 -6.894 -6.583 1.00101.74 N ANISOU 2132 N ALA A1074 14913 12688 11057 265 530 51 N ATOM 2133 CA ALA A1074 16.490 -7.049 -5.947 1.00100.39 C ANISOU 2133 CA ALA A1074 14730 12457 10955 222 563 90 C ATOM 2134 C ALA A1074 16.793 -8.516 -5.661 1.00101.81 C ANISOU 2134 C ALA A1074 14866 12627 11191 198 590 57 C ATOM 2135 O ALA A1074 17.941 -8.932 -5.806 1.00100.73 O ANISOU 2135 O ALA A1074 14717 12472 11082 189 629 73 O ATOM 2136 CB ALA A1074 16.559 -6.240 -4.661 1.00100.75 C ANISOU 2136 CB ALA A1074 14782 12467 11029 212 539 129 C ATOM 2137 N VAL A1075 15.759 -9.294 -5.271 1.00 97.52 N ANISOU 2137 N VAL A1075 14305 12095 10654 189 578 6 N ATOM 2138 CA VAL A1075 15.843 -10.735 -4.993 1.00 96.95 C ANISOU 2138 CA VAL A1075 14225 11992 10621 164 619 -32 C ATOM 2139 C VAL A1075 16.002 -11.479 -6.329 1.00100.68 C ANISOU 2139 C VAL A1075 14708 12483 11061 158 660 -74 C ATOM 2140 O VAL A1075 16.786 -12.429 -6.417 1.00100.31 O ANISOU 2140 O VAL A1075 14677 12395 11043 159 712 -76 O ATOM 2141 CB VAL A1075 14.613 -11.241 -4.181 1.00100.44 C ANISOU 2141 CB VAL A1075 14658 12437 11068 133 608 -82 C ATOM 2142 CG1 VAL A1075 14.617 -12.761 -4.033 1.00100.43 C ANISOU 2142 CG1 VAL A1075 14683 12385 11090 96 672 -128 C ATOM 2143 CG2 VAL A1075 14.547 -10.579 -2.809 1.00 99.81 C ANISOU 2143 CG2 VAL A1075 14570 12332 11021 141 573 -37 C ATOM 2144 N ARG A1076 15.268 -11.018 -7.364 1.00 96.98 N ANISOU 2144 N ARG A1076 14238 12084 10526 166 637 -107 N ATOM 2145 CA ARG A1076 15.272 -11.574 -8.717 1.00 97.05 C ANISOU 2145 CA ARG A1076 14255 12129 10489 162 667 -155 C ATOM 2146 C ARG A1076 16.663 -11.485 -9.363 1.00100.14 C ANISOU 2146 C ARG A1076 14668 12489 10892 183 705 -105 C ATOM 2147 O ARG A1076 17.095 -12.445 -10.002 1.00 99.68 O ANISOU 2147 O ARG A1076 14621 12417 10836 173 755 -136 O ATOM 2148 CB ARG A1076 14.228 -10.861 -9.589 1.00 97.77 C ANISOU 2148 CB ARG A1076 14336 12320 10491 190 621 -190 C ATOM 2149 N GLY A1077 17.344 -10.353 -9.163 1.00 96.37 N ANISOU 2149 N GLY A1077 14198 12001 10418 204 689 -37 N ATOM 2150 CA GLY A1077 18.681 -10.088 -9.690 1.00 96.27 C ANISOU 2150 CA GLY A1077 14193 11974 10410 208 728 5 C ATOM 2151 C GLY A1077 19.757 -11.015 -9.160 1.00 99.84 C ANISOU 2151 C GLY A1077 14616 12395 10923 207 770 12 C ATOM 2152 O GLY A1077 20.655 -11.404 -9.910 1.00 99.49 O ANISOU 2152 O GLY A1077 14569 12359 10873 216 816 11 O ATOM 2153 N ILE A1078 19.660 -11.388 -7.865 1.00 96.24 N ANISOU 2153 N ILE A1078 14143 11908 10517 208 757 20 N ATOM 2154 CA ILE A1078 20.596 -12.285 -7.171 1.00 96.20 C ANISOU 2154 CA ILE A1078 14118 11876 10556 237 791 32 C ATOM 2155 C ILE A1078 20.559 -13.689 -7.808 1.00101.09 C ANISOU 2155 C ILE A1078 14775 12466 11169 254 847 -14 C ATOM 2156 O ILE A1078 21.620 -14.245 -8.103 1.00101.49 O ANISOU 2156 O ILE A1078 14819 12519 11223 296 892 -4 O ATOM 2157 CB ILE A1078 20.309 -12.342 -5.635 1.00 98.77 C ANISOU 2157 CB ILE A1078 14435 12171 10921 243 762 51 C ATOM 2158 CG1 ILE A1078 20.503 -10.956 -4.979 1.00 98.87 C ANISOU 2158 CG1 ILE A1078 14417 12210 10940 222 716 93 C ATOM 2159 CG2 ILE A1078 21.182 -13.399 -4.938 1.00 99.46 C ANISOU 2159 CG2 ILE A1078 14521 12234 11036 300 800 63 C ATOM 2160 CD1 ILE A1078 19.834 -10.764 -3.621 1.00104.28 C ANISOU 2160 CD1 ILE A1078 15102 12870 11651 217 676 104 C ATOM 2161 N LEU A1079 19.344 -14.244 -8.026 1.00 97.51 N ANISOU 2161 N LEU A1079 14359 11993 10697 219 850 -70 N ATOM 2162 CA LEU A1079 19.137 -15.575 -8.613 1.00 97.75 C ANISOU 2162 CA LEU A1079 14443 11985 10713 210 914 -129 C ATOM 2163 C LEU A1079 19.635 -15.637 -10.072 1.00101.56 C ANISOU 2163 C LEU A1079 14928 12503 11157 218 943 -147 C ATOM 2164 O LEU A1079 20.048 -16.706 -10.528 1.00101.50 O ANISOU 2164 O LEU A1079 14965 12458 11144 236 1009 -175 O ATOM 2165 CB LEU A1079 17.654 -15.995 -8.526 1.00 97.91 C ANISOU 2165 CB LEU A1079 14488 12001 10714 142 911 -203 C ATOM 2166 CG LEU A1079 17.035 -16.114 -7.116 1.00102.27 C ANISOU 2166 CG LEU A1079 15048 12511 11298 122 898 -198 C ATOM 2167 CD1 LEU A1079 15.532 -16.305 -7.192 1.00102.72 C ANISOU 2167 CD1 LEU A1079 15104 12603 11324 40 891 -284 C ATOM 2168 CD2 LEU A1079 17.655 -17.251 -6.318 1.00104.54 C ANISOU 2168 CD2 LEU A1079 15406 12698 11616 158 966 -181 C ATOM 2169 N ARG A1080 19.629 -14.488 -10.780 1.00 97.72 N ANISOU 2169 N ARG A1080 14408 12082 10638 212 902 -127 N ATOM 2170 CA ARG A1080 20.114 -14.363 -12.157 1.00 97.63 C ANISOU 2170 CA ARG A1080 14404 12109 10584 220 927 -136 C ATOM 2171 C ARG A1080 21.642 -14.372 -12.202 1.00100.56 C ANISOU 2171 C ARG A1080 14752 12479 10977 260 967 -89 C ATOM 2172 O ARG A1080 22.215 -14.972 -13.111 1.00100.70 O ANISOU 2172 O ARG A1080 14786 12502 10975 278 1018 -110 O ATOM 2173 CB ARG A1080 19.593 -13.076 -12.816 1.00 98.11 C ANISOU 2173 CB ARG A1080 14459 12230 10589 212 878 -123 C ATOM 2174 CG ARG A1080 18.117 -13.094 -13.194 1.00109.04 C ANISOU 2174 CG ARG A1080 15850 13662 11919 192 840 -185 C ATOM 2175 CD ARG A1080 17.807 -12.176 -14.371 1.00118.83 C ANISOU 2175 CD ARG A1080 17105 14971 13073 218 815 -182 C ATOM 2176 NE ARG A1080 18.354 -10.825 -14.206 1.00127.27 N ANISOU 2176 NE ARG A1080 18192 16028 14135 244 797 -102 N ATOM 2177 CZ ARG A1080 17.719 -9.816 -13.616 1.00141.92 C ANISOU 2177 CZ ARG A1080 20057 17892 15973 264 746 -72 C ATOM 2178 NH1 ARG A1080 18.300 -8.628 -13.515 1.00128.66 N ANISOU 2178 NH1 ARG A1080 18418 16185 14283 276 750 -4 N ATOM 2179 NH2 ARG A1080 16.498 -9.988 -13.124 1.00129.14 N ANISOU 2179 NH2 ARG A1080 18411 16311 14344 267 699 -116 N ATOM 2180 N ASN A1081 22.297 -13.688 -11.239 1.00 95.84 N ANISOU 2180 N ASN A1081 14112 11889 10416 272 944 -35 N ATOM 2181 CA ASN A1081 23.755 -13.583 -11.152 1.00 95.42 C ANISOU 2181 CA ASN A1081 14008 11870 10376 302 975 -2 C ATOM 2182 C ASN A1081 24.369 -14.900 -10.686 1.00 98.62 C ANISOU 2182 C ASN A1081 14416 12250 10805 374 1019 -11 C ATOM 2183 O ASN A1081 23.931 -15.467 -9.685 1.00 97.87 O ANISOU 2183 O ASN A1081 14345 12105 10736 396 1009 -10 O ATOM 2184 CB ASN A1081 24.157 -12.448 -10.217 1.00 95.30 C ANISOU 2184 CB ASN A1081 13943 11885 10382 278 937 42 C ATOM 2185 CG ASN A1081 25.543 -11.928 -10.477 1.00114.99 C ANISOU 2185 CG ASN A1081 16375 14448 12866 270 971 58 C ATOM 2186 OD1 ASN A1081 26.531 -12.416 -9.922 1.00108.88 O ANISOU 2186 OD1 ASN A1081 15538 13720 12111 316 990 61 O ATOM 2187 ND2 ASN A1081 25.645 -10.924 -11.334 1.00105.57 N ANISOU 2187 ND2 ASN A1081 15202 13274 11636 213 984 65 N ATOM 2188 N ALA A1082 25.382 -15.383 -11.421 1.00 95.16 N ANISOU 2188 N ALA A1082 13962 11845 10349 418 1073 -18 N ATOM 2189 CA ALA A1082 26.072 -16.640 -11.134 1.00 95.25 C ANISOU 2189 CA ALA A1082 13989 11836 10365 514 1125 -23 C ATOM 2190 C ALA A1082 27.049 -16.518 -9.961 1.00 98.75 C ANISOU 2190 C ALA A1082 14355 12337 10827 584 1109 15 C ATOM 2191 O ALA A1082 27.388 -17.536 -9.358 1.00 98.70 O ANISOU 2191 O ALA A1082 14379 12303 10819 686 1139 21 O ATOM 2192 CB ALA A1082 26.810 -17.119 -12.371 1.00 96.67 C ANISOU 2192 CB ALA A1082 14173 12046 10511 547 1187 -46 C ATOM 2193 N LYS A1083 27.511 -15.290 -9.647 1.00 94.91 N ANISOU 2193 N LYS A1083 13779 11935 10348 531 1069 37 N ATOM 2194 CA LYS A1083 28.455 -15.037 -8.553 1.00 94.72 C ANISOU 2194 CA LYS A1083 13660 11999 10332 579 1048 59 C ATOM 2195 C LYS A1083 27.732 -14.781 -7.216 1.00 97.65 C ANISOU 2195 C LYS A1083 14046 12324 10732 567 992 82 C ATOM 2196 O LYS A1083 28.265 -15.138 -6.161 1.00 97.52 O ANISOU 2196 O LYS A1083 13990 12347 10717 649 980 98 O ATOM 2197 CB LYS A1083 29.378 -13.856 -8.893 1.00 97.09 C ANISOU 2197 CB LYS A1083 13856 12418 10617 504 1049 54 C ATOM 2198 N LEU A1084 26.523 -14.179 -7.263 1.00 92.85 N ANISOU 2198 N LEU A1084 13494 11644 10140 477 957 82 N ATOM 2199 CA LEU A1084 25.731 -13.842 -6.074 1.00 91.60 C ANISOU 2199 CA LEU A1084 13351 11443 10008 455 905 100 C ATOM 2200 C LEU A1084 24.839 -15.000 -5.585 1.00 94.77 C ANISOU 2200 C LEU A1084 13845 11743 10421 500 918 92 C ATOM 2201 O LEU A1084 24.626 -15.115 -4.376 1.00 94.30 O ANISOU 2201 O LEU A1084 13791 11660 10377 528 894 112 O ATOM 2202 CB LEU A1084 24.859 -12.596 -6.330 1.00 90.86 C ANISOU 2202 CB LEU A1084 13275 11333 9915 351 864 102 C ATOM 2203 CG LEU A1084 25.570 -11.295 -6.738 1.00 95.53 C ANISOU 2203 CG LEU A1084 13814 11993 10488 283 864 112 C ATOM 2204 CD1 LEU A1084 24.571 -10.249 -7.157 1.00 95.17 C ANISOU 2204 CD1 LEU A1084 13830 11904 10426 212 839 117 C ATOM 2205 CD2 LEU A1084 26.425 -10.739 -5.611 1.00 98.21 C ANISOU 2205 CD2 LEU A1084 14071 12405 10840 274 845 125 C ATOM 2206 N LYS A1085 24.312 -15.837 -6.508 1.00 90.98 N ANISOU 2206 N LYS A1085 13442 11201 9927 497 964 57 N ATOM 2207 CA LYS A1085 23.425 -16.971 -6.208 1.00 90.75 C ANISOU 2207 CA LYS A1085 13517 11066 9898 509 1000 32 C ATOM 2208 C LYS A1085 24.037 -18.001 -5.211 1.00 95.08 C ANISOU 2208 C LYS A1085 14111 11572 10443 626 1039 58 C ATOM 2209 O LYS A1085 23.323 -18.344 -4.268 1.00 94.50 O ANISOU 2209 O LYS A1085 14098 11427 10380 621 1039 61 O ATOM 2210 CB LYS A1085 22.993 -17.687 -7.500 1.00 93.52 C ANISOU 2210 CB LYS A1085 13935 11375 10222 478 1056 -22 C ATOM 2211 CG LYS A1085 21.783 -18.594 -7.345 1.00102.87 C ANISOU 2211 CG LYS A1085 15223 12462 11402 429 1094 -72 C ATOM 2212 CD LYS A1085 21.440 -19.268 -8.665 1.00111.46 C ANISOU 2212 CD LYS A1085 16367 13526 12455 387 1150 -138 C ATOM 2213 CE LYS A1085 20.399 -20.343 -8.504 1.00122.84 C ANISOU 2213 CE LYS A1085 17920 14870 13883 327 1213 -203 C ATOM 2214 NZ LYS A1085 20.937 -21.521 -7.777 1.00134.49 N ANISOU 2214 NZ LYS A1085 19508 16236 15357 413 1295 -183 N ATOM 2215 N PRO A1086 25.300 -18.510 -5.357 1.00 92.45 N ANISOU 2215 N PRO A1086 13754 11284 10086 742 1076 76 N ATOM 2216 CA PRO A1086 25.809 -19.500 -4.387 1.00 93.03 C ANISOU 2216 CA PRO A1086 13888 11320 10139 883 1113 105 C ATOM 2217 C PRO A1086 26.109 -18.917 -3.002 1.00 97.26 C ANISOU 2217 C PRO A1086 14353 11918 10684 923 1050 147 C ATOM 2218 O PRO A1086 26.232 -19.680 -2.042 1.00 97.64 O ANISOU 2218 O PRO A1086 14471 11918 10710 1033 1073 174 O ATOM 2219 CB PRO A1086 27.093 -20.022 -5.046 1.00 95.62 C ANISOU 2219 CB PRO A1086 14186 11717 10430 1004 1158 107 C ATOM 2220 CG PRO A1086 27.036 -19.560 -6.464 1.00 99.68 C ANISOU 2220 CG PRO A1086 14661 12264 10949 906 1164 71 C ATOM 2221 CD PRO A1086 26.309 -18.264 -6.404 1.00 94.33 C ANISOU 2221 CD PRO A1086 13918 11616 10306 763 1091 69 C ATOM 2222 N VAL A1087 26.227 -17.578 -2.898 1.00 93.20 N ANISOU 2222 N VAL A1087 13713 11504 10193 836 977 152 N ATOM 2223 CA VAL A1087 26.467 -16.875 -1.635 1.00 92.68 C ANISOU 2223 CA VAL A1087 13572 11506 10135 847 915 181 C ATOM 2224 C VAL A1087 25.118 -16.750 -0.899 1.00 96.15 C ANISOU 2224 C VAL A1087 14089 11839 10604 772 892 184 C ATOM 2225 O VAL A1087 25.067 -16.983 0.307 1.00 96.30 O ANISOU 2225 O VAL A1087 14131 11840 10617 831 877 211 O ATOM 2226 CB VAL A1087 27.173 -15.502 -1.832 1.00 96.23 C ANISOU 2226 CB VAL A1087 13875 12097 10591 770 865 175 C ATOM 2227 CG1 VAL A1087 27.514 -14.851 -0.494 1.00 95.95 C ANISOU 2227 CG1 VAL A1087 13760 12141 10554 781 807 194 C ATOM 2228 CG2 VAL A1087 28.434 -15.649 -2.680 1.00 96.91 C ANISOU 2228 CG2 VAL A1087 13881 12296 10646 824 899 158 C ATOM 2229 N TYR A1088 24.029 -16.435 -1.640 1.00 91.65 N ANISOU 2229 N TYR A1088 13559 11209 10056 652 891 153 N ATOM 2230 CA TYR A1088 22.655 -16.298 -1.133 1.00 90.66 C ANISOU 2230 CA TYR A1088 13492 11004 9951 571 872 140 C ATOM 2231 C TYR A1088 22.161 -17.603 -0.477 1.00 94.74 C ANISOU 2231 C TYR A1088 14137 11404 10456 621 934 136 C ATOM 2232 O TYR A1088 21.487 -17.555 0.556 1.00 93.75 O ANISOU 2232 O TYR A1088 14044 11236 10341 601 918 146 O ATOM 2233 CB TYR A1088 21.721 -15.896 -2.289 1.00 91.27 C ANISOU 2233 CB TYR A1088 13579 11070 10032 463 869 96 C ATOM 2234 CG TYR A1088 20.344 -15.415 -1.877 1.00 92.49 C ANISOU 2234 CG TYR A1088 13749 11194 10198 376 833 75 C ATOM 2235 CD1 TYR A1088 20.172 -14.187 -1.242 1.00 94.08 C ANISOU 2235 CD1 TYR A1088 13889 11442 10414 344 764 101 C ATOM 2236 CD2 TYR A1088 19.204 -16.141 -2.209 1.00 93.25 C ANISOU 2236 CD2 TYR A1088 13918 11230 10284 319 871 19 C ATOM 2237 CE1 TYR A1088 18.904 -13.724 -0.890 1.00 94.35 C ANISOU 2237 CE1 TYR A1088 13935 11462 10453 280 731 80 C ATOM 2238 CE2 TYR A1088 17.930 -15.685 -1.869 1.00 93.69 C ANISOU 2238 CE2 TYR A1088 13968 11288 10342 242 837 -11 C ATOM 2239 CZ TYR A1088 17.784 -14.475 -1.210 1.00100.72 C ANISOU 2239 CZ TYR A1088 14796 12225 11247 234 764 23 C ATOM 2240 OH TYR A1088 16.530 -14.024 -0.872 1.00101.78 O ANISOU 2240 OH TYR A1088 14922 12372 11376 175 731 -7 O ATOM 2241 N ASP A1089 22.525 -18.759 -1.075 1.00 92.11 N ANISOU 2241 N ASP A1089 13888 11014 10095 686 1013 123 N ATOM 2242 CA ASP A1089 22.164 -20.100 -0.615 1.00 92.66 C ANISOU 2242 CA ASP A1089 14116 10951 10140 736 1100 116 C ATOM 2243 C ASP A1089 22.892 -20.491 0.672 1.00 97.85 C ANISOU 2243 C ASP A1089 14805 11602 10772 884 1103 176 C ATOM 2244 O ASP A1089 22.288 -21.146 1.520 1.00 98.49 O ANISOU 2244 O ASP A1089 15009 11574 10838 894 1149 183 O ATOM 2245 CB ASP A1089 22.454 -21.144 -1.706 1.00 95.05 C ANISOU 2245 CB ASP A1089 14509 11193 10412 770 1190 85 C ATOM 2246 CG ASP A1089 21.607 -21.016 -2.959 1.00103.42 C ANISOU 2246 CG ASP A1089 15567 12247 11482 628 1201 14 C ATOM 2247 OD1 ASP A1089 20.425 -20.619 -2.842 1.00103.43 O ANISOU 2247 OD1 ASP A1089 15560 12238 11500 503 1175 -24 O ATOM 2248 OD2 ASP A1089 22.110 -21.357 -4.051 1.00108.98 O ANISOU 2248 OD2 ASP A1089 16276 12963 12168 651 1239 -6 O ATOM 2249 N SER A1090 24.180 -20.106 0.817 1.00 94.31 N ANISOU 2249 N SER A1090 14246 11280 10306 998 1060 215 N ATOM 2250 CA SER A1090 25.005 -20.422 1.991 1.00 94.58 C ANISOU 2250 CA SER A1090 14284 11354 10300 1162 1052 267 C ATOM 2251 C SER A1090 24.701 -19.515 3.210 1.00 97.36 C ANISOU 2251 C SER A1090 14563 11756 10672 1121 971 290 C ATOM 2252 O SER A1090 25.211 -19.784 4.300 1.00 97.47 O ANISOU 2252 O SER A1090 14589 11798 10646 1251 961 331 O ATOM 2253 CB SER A1090 26.488 -20.336 1.637 1.00 98.89 C ANISOU 2253 CB SER A1090 14713 12052 10810 1293 1034 281 C ATOM 2254 OG SER A1090 26.871 -19.024 1.258 1.00107.43 O ANISOU 2254 OG SER A1090 15613 13281 11924 1192 957 263 O ATOM 2255 N LEU A1091 23.877 -18.457 3.029 1.00 92.70 N ANISOU 2255 N LEU A1091 13905 11180 10135 954 916 264 N ATOM 2256 CA LEU A1091 23.522 -17.510 4.093 1.00 91.72 C ANISOU 2256 CA LEU A1091 13719 11100 10033 901 842 280 C ATOM 2257 C LEU A1091 22.158 -17.818 4.711 1.00 94.65 C ANISOU 2257 C LEU A1091 14203 11340 10419 828 867 271 C ATOM 2258 O LEU A1091 21.251 -18.273 4.016 1.00 93.73 O ANISOU 2258 O LEU A1091 14165 11132 10314 743 918 230 O ATOM 2259 CB LEU A1091 23.529 -16.054 3.574 1.00 91.00 C ANISOU 2259 CB LEU A1091 13490 11107 9977 778 771 261 C ATOM 2260 CG LEU A1091 24.872 -15.451 3.132 1.00 96.10 C ANISOU 2260 CG LEU A1091 14002 11904 10609 810 744 261 C ATOM 2261 CD1 LEU A1091 24.662 -14.148 2.384 1.00 95.49 C ANISOU 2261 CD1 LEU A1091 13850 11872 10561 668 707 237 C ATOM 2262 CD2 LEU A1091 25.819 -15.238 4.305 1.00 99.25 C ANISOU 2262 CD2 LEU A1091 14317 12419 10975 903 702 285 C ATOM 2263 N ASP A1092 22.019 -17.538 6.019 1.00 91.21 N ANISOU 2263 N ASP A1092 13766 10912 9979 854 831 301 N ATOM 2264 CA ASP A1092 20.785 -17.719 6.789 1.00 90.83 C ANISOU 2264 CA ASP A1092 13810 10759 9941 784 850 292 C ATOM 2265 C ASP A1092 19.812 -16.561 6.508 1.00 95.22 C ANISOU 2265 C ASP A1092 14286 11347 10544 628 791 257 C ATOM 2266 O ASP A1092 20.193 -15.597 5.841 1.00 94.71 O ANISOU 2266 O ASP A1092 14112 11376 10499 588 737 250 O ATOM 2267 CB ASP A1092 21.103 -17.821 8.290 1.00 92.66 C ANISOU 2267 CB ASP A1092 14068 10999 10141 885 832 341 C ATOM 2268 CG ASP A1092 21.760 -16.585 8.857 1.00100.18 C ANISOU 2268 CG ASP A1092 14863 12099 11101 890 731 359 C ATOM 2269 OD1 ASP A1092 22.964 -16.390 8.608 1.00100.73 O ANISOU 2269 OD1 ASP A1092 14837 12286 11148 970 703 369 O ATOM 2270 OD2 ASP A1092 21.064 -15.804 9.531 1.00105.36 O ANISOU 2270 OD2 ASP A1092 15492 12757 11782 807 685 355 O ATOM 2271 N ALA A1093 18.569 -16.650 7.028 1.00 92.20 N ANISOU 2271 N ALA A1093 13967 10892 10173 546 809 233 N ATOM 2272 CA ALA A1093 17.490 -15.670 6.839 1.00 91.45 C ANISOU 2272 CA ALA A1093 13811 10829 10109 420 760 195 C ATOM 2273 C ALA A1093 17.913 -14.212 7.116 1.00 94.87 C ANISOU 2273 C ALA A1093 14123 11365 10559 413 665 222 C ATOM 2274 O ALA A1093 17.595 -13.335 6.307 1.00 94.23 O ANISOU 2274 O ALA A1093 13982 11331 10492 346 629 199 O ATOM 2275 CB ALA A1093 16.302 -16.030 7.716 1.00 92.28 C ANISOU 2275 CB ALA A1093 13991 10860 10212 361 793 173 C ATOM 2276 N VAL A1094 18.626 -13.962 8.238 1.00 90.97 N ANISOU 2276 N VAL A1094 13603 10905 10054 482 632 266 N ATOM 2277 CA VAL A1094 19.080 -12.627 8.654 1.00 90.00 C ANISOU 2277 CA VAL A1094 13380 10876 9941 463 555 282 C ATOM 2278 C VAL A1094 20.158 -12.109 7.689 1.00 93.33 C ANISOU 2278 C VAL A1094 13718 11383 10360 466 539 280 C ATOM 2279 O VAL A1094 20.078 -10.961 7.251 1.00 92.97 O ANISOU 2279 O VAL A1094 13619 11377 10327 392 503 269 O ATOM 2280 CB VAL A1094 19.581 -12.603 10.128 1.00 94.33 C ANISOU 2280 CB VAL A1094 13920 11452 10468 533 528 318 C ATOM 2281 CG1 VAL A1094 19.849 -11.176 10.606 1.00 93.68 C ANISOU 2281 CG1 VAL A1094 13746 11455 10393 481 457 319 C ATOM 2282 CG2 VAL A1094 18.592 -13.293 11.064 1.00 94.37 C ANISOU 2282 CG2 VAL A1094 14029 11361 10467 537 562 323 C ATOM 2283 N ARG A1095 21.143 -12.956 7.349 1.00 89.66 N ANISOU 2283 N ARG A1095 13252 10942 9874 555 573 291 N ATOM 2284 CA ARG A1095 22.250 -12.591 6.466 1.00 89.54 C ANISOU 2284 CA ARG A1095 13151 11020 9850 563 568 284 C ATOM 2285 C ARG A1095 21.828 -12.488 4.984 1.00 93.60 C ANISOU 2285 C ARG A1095 13681 11502 10381 493 594 255 C ATOM 2286 O ARG A1095 22.500 -11.783 4.224 1.00 93.22 O ANISOU 2286 O ARG A1095 13566 11525 10330 458 584 246 O ATOM 2287 CB ARG A1095 23.421 -13.561 6.636 1.00 89.45 C ANISOU 2287 CB ARG A1095 13128 11060 9799 702 596 301 C ATOM 2288 CG ARG A1095 24.193 -13.306 7.922 1.00 95.13 C ANISOU 2288 CG ARG A1095 13780 11879 10485 776 552 322 C ATOM 2289 CD ARG A1095 25.418 -14.177 8.018 1.00 98.74 C ANISOU 2289 CD ARG A1095 14207 12423 10887 937 572 335 C ATOM 2290 NE ARG A1095 26.147 -13.954 9.265 1.00 99.82 N ANISOU 2290 NE ARG A1095 14268 12682 10976 1019 524 348 N ATOM 2291 CZ ARG A1095 26.035 -14.706 10.355 1.00108.58 C ANISOU 2291 CZ ARG A1095 15455 13756 12044 1145 529 384 C ATOM 2292 NH1 ARG A1095 25.214 -15.750 10.365 1.00 95.38 N ANISOU 2292 NH1 ARG A1095 13952 11914 10374 1189 593 410 N ATOM 2293 NH2 ARG A1095 26.739 -14.423 11.440 1.00 92.44 N ANISOU 2293 NH2 ARG A1095 13327 11848 9948 1222 478 389 N ATOM 2294 N ARG A1096 20.716 -13.158 4.582 1.00 90.00 N ANISOU 2294 N ARG A1096 13313 10948 9933 464 630 234 N ATOM 2295 CA ARG A1096 20.165 -13.086 3.218 1.00 89.41 C ANISOU 2295 CA ARG A1096 13252 10856 9863 400 649 199 C ATOM 2296 C ARG A1096 19.580 -11.691 2.980 1.00 92.28 C ANISOU 2296 C ARG A1096 13576 11253 10234 317 597 192 C ATOM 2297 O ARG A1096 19.690 -11.156 1.877 1.00 91.65 O ANISOU 2297 O ARG A1096 13476 11202 10145 283 596 180 O ATOM 2298 CB ARG A1096 19.093 -14.166 2.982 1.00 89.50 C ANISOU 2298 CB ARG A1096 13359 10775 9872 378 704 163 C ATOM 2299 CG ARG A1096 19.639 -15.496 2.468 1.00 99.55 C ANISOU 2299 CG ARG A1096 14699 12000 11126 442 779 156 C ATOM 2300 CD ARG A1096 18.541 -16.414 1.941 1.00107.26 C ANISOU 2300 CD ARG A1096 15768 12892 12094 379 844 99 C ATOM 2301 NE ARG A1096 17.694 -16.944 3.014 1.00115.67 N ANISOU 2301 NE ARG A1096 16912 13880 13158 356 874 90 N ATOM 2302 CZ ARG A1096 17.820 -18.156 3.547 1.00131.01 C ANISOU 2302 CZ ARG A1096 18976 15722 15079 409 954 97 C ATOM 2303 NH1 ARG A1096 18.741 -18.997 3.093 1.00120.76 N ANISOU 2303 NH1 ARG A1096 17735 14391 13758 501 1010 114 N ATOM 2304 NH2 ARG A1096 17.011 -18.544 4.525 1.00116.74 N ANISOU 2304 NH2 ARG A1096 17246 13842 13267 374 987 88 N ATOM 2305 N ALA A1097 18.982 -11.099 4.043 1.00 87.96 N ANISOU 2305 N ALA A1097 13028 10697 9696 294 558 202 N ATOM 2306 CA ALA A1097 18.400 -9.758 4.055 1.00 86.91 C ANISOU 2306 CA ALA A1097 12877 10584 9562 236 512 202 C ATOM 2307 C ALA A1097 19.499 -8.698 3.955 1.00 89.90 C ANISOU 2307 C ALA A1097 13204 11021 9933 219 494 222 C ATOM 2308 O ALA A1097 19.282 -7.655 3.339 1.00 89.95 O ANISOU 2308 O ALA A1097 13219 11033 9924 174 483 220 O ATOM 2309 CB ALA A1097 17.584 -9.556 5.324 1.00 87.27 C ANISOU 2309 CB ALA A1097 12939 10602 9616 228 485 206 C ATOM 2310 N ALA A1098 20.685 -8.979 4.535 1.00 85.08 N ANISOU 2310 N ALA A1098 12544 10459 9322 257 498 237 N ATOM 2311 CA ALA A1098 21.838 -8.081 4.492 1.00 84.45 C ANISOU 2311 CA ALA A1098 12398 10459 9229 223 491 238 C ATOM 2312 C ALA A1098 22.399 -7.975 3.063 1.00 87.51 C ANISOU 2312 C ALA A1098 12774 10872 9604 199 527 225 C ATOM 2313 O ALA A1098 22.843 -6.897 2.668 1.00 86.87 O ANISOU 2313 O ALA A1098 12679 10821 9506 129 534 219 O ATOM 2314 CB ALA A1098 22.911 -8.565 5.451 1.00 85.61 C ANISOU 2314 CB ALA A1098 12477 10685 9366 284 483 245 C ATOM 2315 N LEU A1099 22.337 -9.080 2.283 1.00 83.83 N ANISOU 2315 N LEU A1099 12329 10384 9139 251 560 219 N ATOM 2316 CA LEU A1099 22.808 -9.135 0.897 1.00 83.87 C ANISOU 2316 CA LEU A1099 12329 10409 9129 238 597 205 C ATOM 2317 C LEU A1099 21.828 -8.429 -0.047 1.00 88.28 C ANISOU 2317 C LEU A1099 12949 10919 9675 184 595 198 C ATOM 2318 O LEU A1099 22.281 -7.718 -0.945 1.00 88.40 O ANISOU 2318 O LEU A1099 12965 10957 9667 142 616 196 O ATOM 2319 CB LEU A1099 23.041 -10.588 0.453 1.00 84.20 C ANISOU 2319 CB LEU A1099 12385 10437 9171 318 636 197 C ATOM 2320 CG LEU A1099 23.837 -10.801 -0.846 1.00 89.12 C ANISOU 2320 CG LEU A1099 12985 11101 9775 323 679 183 C ATOM 2321 CD1 LEU A1099 25.307 -10.440 -0.668 1.00 89.83 C ANISOU 2321 CD1 LEU A1099 12976 11307 9850 331 686 182 C ATOM 2322 CD2 LEU A1099 23.721 -12.234 -1.321 1.00 91.30 C ANISOU 2322 CD2 LEU A1099 13310 11330 10048 396 723 171 C ATOM 2323 N ILE A1100 20.494 -8.610 0.162 1.00 84.82 N ANISOU 2323 N ILE A1100 12562 10424 9242 188 573 191 N ATOM 2324 CA ILE A1100 19.421 -7.960 -0.621 1.00 84.36 C ANISOU 2324 CA ILE A1100 12553 10344 9156 164 560 179 C ATOM 2325 C ILE A1100 19.558 -6.438 -0.450 1.00 87.77 C ANISOU 2325 C ILE A1100 13004 10777 9566 123 544 203 C ATOM 2326 O ILE A1100 19.427 -5.704 -1.430 1.00 87.59 O ANISOU 2326 O ILE A1100 13026 10751 9504 110 557 206 O ATOM 2327 CB ILE A1100 17.997 -8.484 -0.228 1.00 87.17 C ANISOU 2327 CB ILE A1100 12934 10670 9515 175 539 154 C ATOM 2328 CG1 ILE A1100 17.811 -9.966 -0.639 1.00 87.94 C ANISOU 2328 CG1 ILE A1100 13042 10750 9620 191 579 119 C ATOM 2329 CG2 ILE A1100 16.873 -7.618 -0.834 1.00 87.37 C ANISOU 2329 CG2 ILE A1100 12992 10707 9498 169 512 140 C ATOM 2330 CD1 ILE A1100 16.834 -10.777 0.224 1.00 96.55 C ANISOU 2330 CD1 ILE A1100 14155 11804 10726 185 582 92 C ATOM 2331 N ASN A1101 19.879 -5.990 0.790 1.00 83.91 N ANISOU 2331 N ASN A1101 12493 10293 9097 105 524 218 N ATOM 2332 CA ASN A1101 20.106 -4.595 1.181 1.00 83.70 C ANISOU 2332 CA ASN A1101 12494 10258 9051 52 519 233 C ATOM 2333 C ASN A1101 21.223 -3.959 0.333 1.00 87.94 C ANISOU 2333 C ASN A1101 13032 10820 9561 -4 568 232 C ATOM 2334 O ASN A1101 21.094 -2.801 -0.064 1.00 88.23 O ANISOU 2334 O ASN A1101 13146 10820 9558 -45 589 242 O ATOM 2335 CB ASN A1101 20.456 -4.520 2.675 1.00 84.05 C ANISOU 2335 CB ASN A1101 12494 10320 9121 39 494 237 C ATOM 2336 CG ASN A1101 20.405 -3.138 3.283 1.00105.25 C ANISOU 2336 CG ASN A1101 15222 12982 11787 -19 488 245 C ATOM 2337 OD1 ASN A1101 21.170 -2.234 2.927 1.00 98.57 O ANISOU 2337 OD1 ASN A1101 14395 12143 10913 -88 525 240 O ATOM 2338 ND2 ASN A1101 19.550 -2.967 4.276 1.00 97.43 N ANISOU 2338 ND2 ASN A1101 14252 11961 10805 1 450 252 N ATOM 2339 N MET A1102 22.301 -4.722 0.048 1.00 84.13 N ANISOU 2339 N MET A1102 12474 10399 9092 -1 594 218 N ATOM 2340 CA MET A1102 23.438 -4.282 -0.767 1.00 84.39 C ANISOU 2340 CA MET A1102 12488 10477 9100 -60 647 206 C ATOM 2341 C MET A1102 23.063 -4.173 -2.248 1.00 88.68 C ANISOU 2341 C MET A1102 13105 10982 9608 -52 679 211 C ATOM 2342 O MET A1102 23.502 -3.237 -2.921 1.00 88.54 O ANISOU 2342 O MET A1102 13138 10953 9550 -116 727 213 O ATOM 2343 CB MET A1102 24.623 -5.241 -0.603 1.00 86.93 C ANISOU 2343 CB MET A1102 12695 10896 9439 -34 660 186 C ATOM 2344 CG MET A1102 25.441 -4.970 0.621 1.00 90.70 C ANISOU 2344 CG MET A1102 13088 11454 9921 -64 645 171 C ATOM 2345 SD MET A1102 26.768 -6.173 0.787 1.00 95.44 S ANISOU 2345 SD MET A1102 13548 12192 10521 12 653 148 S ATOM 2346 CE MET A1102 28.133 -5.236 0.182 1.00 93.09 C ANISOU 2346 CE MET A1102 13178 12008 10184 -110 713 101 C ATOM 2347 N VAL A1103 22.280 -5.152 -2.756 1.00 85.06 N ANISOU 2347 N VAL A1103 12655 10505 9158 21 660 209 N ATOM 2348 CA VAL A1103 21.815 -5.224 -4.147 1.00 84.92 C ANISOU 2348 CA VAL A1103 12695 10468 9102 43 681 206 C ATOM 2349 C VAL A1103 20.810 -4.082 -4.409 1.00 88.98 C ANISOU 2349 C VAL A1103 13312 10930 9564 47 667 224 C ATOM 2350 O VAL A1103 20.878 -3.453 -5.462 1.00 89.60 O ANISOU 2350 O VAL A1103 13464 10994 9588 41 703 234 O ATOM 2351 CB VAL A1103 21.238 -6.630 -4.484 1.00 88.45 C ANISOU 2351 CB VAL A1103 13119 10921 9568 106 668 182 C ATOM 2352 CG1 VAL A1103 20.618 -6.673 -5.880 1.00 88.48 C ANISOU 2352 CG1 VAL A1103 13177 10921 9523 128 680 169 C ATOM 2353 CG2 VAL A1103 22.313 -7.706 -4.354 1.00 88.41 C ANISOU 2353 CG2 VAL A1103 13040 10955 9596 125 696 171 C ATOM 2354 N PHE A1104 19.923 -3.789 -3.437 1.00 84.66 N ANISOU 2354 N PHE A1104 12781 10358 9028 67 620 231 N ATOM 2355 CA PHE A1104 18.928 -2.711 -3.521 1.00 84.39 C ANISOU 2355 CA PHE A1104 12843 10282 8938 96 603 250 C ATOM 2356 C PHE A1104 19.605 -1.337 -3.657 1.00 89.25 C ANISOU 2356 C PHE A1104 13551 10850 9511 38 655 277 C ATOM 2357 O PHE A1104 19.088 -0.463 -4.353 1.00 89.49 O ANISOU 2357 O PHE A1104 13697 10837 9467 74 673 298 O ATOM 2358 CB PHE A1104 18.031 -2.736 -2.268 1.00 85.49 C ANISOU 2358 CB PHE A1104 12963 10414 9106 121 549 248 C ATOM 2359 CG PHE A1104 16.907 -1.727 -2.220 1.00 87.01 C ANISOU 2359 CG PHE A1104 13243 10577 9239 175 524 263 C ATOM 2360 CD1 PHE A1104 15.626 -2.071 -2.629 1.00 89.97 C ANISOU 2360 CD1 PHE A1104 13612 10993 9577 254 484 240 C ATOM 2361 CD2 PHE A1104 17.116 -0.451 -1.708 1.00 89.40 C ANISOU 2361 CD2 PHE A1104 13632 10821 9515 148 544 292 C ATOM 2362 CE1 PHE A1104 14.580 -1.146 -2.556 1.00 91.12 C ANISOU 2362 CE1 PHE A1104 13829 11135 9657 328 458 252 C ATOM 2363 CE2 PHE A1104 16.074 0.478 -1.652 1.00 92.41 C ANISOU 2363 CE2 PHE A1104 14110 11172 9831 221 526 310 C ATOM 2364 CZ PHE A1104 14.812 0.123 -2.074 1.00 90.38 C ANISOU 2364 CZ PHE A1104 13836 10969 9535 322 479 292 C ATOM 2365 N GLN A1105 20.752 -1.162 -2.985 1.00 86.26 N ANISOU 2365 N GLN A1105 13125 10483 9168 -51 685 270 N ATOM 2366 CA GLN A1105 21.522 0.074 -2.921 1.00 86.86 C ANISOU 2366 CA GLN A1105 13276 10519 9207 -146 748 277 C ATOM 2367 C GLN A1105 22.496 0.244 -4.105 1.00 92.52 C ANISOU 2367 C GLN A1105 14018 11247 9888 -205 826 270 C ATOM 2368 O GLN A1105 22.439 1.271 -4.781 1.00 92.94 O ANISOU 2368 O GLN A1105 14213 11229 9871 -228 885 290 O ATOM 2369 CB GLN A1105 22.294 0.106 -1.589 1.00 87.93 C ANISOU 2369 CB GLN A1105 13322 10695 9392 -224 740 254 C ATOM 2370 CG GLN A1105 22.964 1.434 -1.254 1.00103.52 C ANISOU 2370 CG GLN A1105 15373 12631 11329 -345 805 245 C ATOM 2371 CD GLN A1105 23.929 1.330 -0.094 1.00123.74 C ANISOU 2371 CD GLN A1105 17812 15276 13929 -432 799 204 C ATOM 2372 OE1 GLN A1105 24.001 0.321 0.624 1.00118.99 O ANISOU 2372 OE1 GLN A1105 17082 14751 13380 -378 738 195 O ATOM 2373 NE2 GLN A1105 24.696 2.388 0.122 1.00116.55 N ANISOU 2373 NE2 GLN A1105 16946 14355 12982 -568 869 175 N ATOM 2374 N MET A1106 23.396 -0.732 -4.334 1.00 89.68 N ANISOU 2374 N MET A1106 13532 10972 9568 -223 834 242 N ATOM 2375 CA MET A1106 24.446 -0.649 -5.355 1.00 90.59 C ANISOU 2375 CA MET A1106 13646 11119 9655 -289 911 226 C ATOM 2376 C MET A1106 24.099 -1.309 -6.690 1.00 94.94 C ANISOU 2376 C MET A1106 14220 11670 10182 -212 915 235 C ATOM 2377 O MET A1106 24.654 -0.912 -7.716 1.00 95.62 O ANISOU 2377 O MET A1106 14364 11748 10219 -256 986 235 O ATOM 2378 CB MET A1106 25.743 -1.278 -4.833 1.00 93.37 C ANISOU 2378 CB MET A1106 13837 11588 10053 -346 922 184 C ATOM 2379 CG MET A1106 26.358 -0.539 -3.659 1.00 97.58 C ANISOU 2379 CG MET A1106 14331 12151 10592 -449 933 158 C ATOM 2380 SD MET A1106 27.808 -1.387 -2.980 1.00102.32 S ANISOU 2380 SD MET A1106 14715 12933 11229 -478 928 101 S ATOM 2381 CE MET A1106 27.045 -2.815 -2.280 1.00 97.96 C ANISOU 2381 CE MET A1106 14094 12389 10736 -313 828 128 C ATOM 2382 N GLY A1107 23.247 -2.328 -6.665 1.00 90.87 N ANISOU 2382 N GLY A1107 13660 11170 9697 -111 848 236 N ATOM 2383 CA GLY A1107 22.860 -3.061 -7.866 1.00 90.66 C ANISOU 2383 CA GLY A1107 13645 11156 9646 -44 848 231 C ATOM 2384 C GLY A1107 23.560 -4.397 -7.993 1.00 94.56 C ANISOU 2384 C GLY A1107 14021 11719 10190 -30 851 201 C ATOM 2385 O GLY A1107 24.641 -4.586 -7.429 1.00 94.14 O ANISOU 2385 O GLY A1107 13880 11718 10171 -75 871 187 O ATOM 2386 N GLU A1108 22.940 -5.325 -8.751 1.00 91.49 N ANISOU 2386 N GLU A1108 13633 11336 9795 38 833 187 N ATOM 2387 CA GLU A1108 23.409 -6.688 -9.042 1.00 91.39 C ANISOU 2387 CA GLU A1108 13543 11366 9815 71 845 159 C ATOM 2388 C GLU A1108 24.893 -6.702 -9.463 1.00 96.66 C ANISOU 2388 C GLU A1108 14157 12089 10481 27 909 150 C ATOM 2389 O GLU A1108 25.673 -7.495 -8.931 1.00 96.37 O ANISOU 2389 O GLU A1108 14029 12105 10485 46 914 135 O ATOM 2390 CB GLU A1108 22.533 -7.304 -10.154 1.00 92.62 C ANISOU 2390 CB GLU A1108 13742 11514 9934 122 839 138 C ATOM 2391 CG GLU A1108 22.717 -8.797 -10.380 1.00101.33 C ANISOU 2391 CG GLU A1108 14796 12637 11069 158 852 103 C ATOM 2392 CD GLU A1108 22.292 -9.312 -11.744 1.00117.80 C ANISOU 2392 CD GLU A1108 16920 14732 13106 182 871 73 C ATOM 2393 OE1 GLU A1108 21.170 -8.982 -12.193 1.00115.12 O ANISOU 2393 OE1 GLU A1108 16630 14393 12719 198 838 62 O ATOM 2394 OE2 GLU A1108 23.075 -10.074 -12.354 1.00106.41 O ANISOU 2394 OE2 GLU A1108 15455 13309 11668 191 918 55 O ATOM 2395 N THR A1109 25.270 -5.806 -10.397 1.00 94.26 N ANISOU 2395 N THR A1109 13915 11778 10122 -25 963 159 N ATOM 2396 CA THR A1109 26.628 -5.681 -10.933 1.00 94.98 C ANISOU 2396 CA THR A1109 13961 11930 10199 -85 1036 142 C ATOM 2397 C THR A1109 27.597 -5.104 -9.887 1.00 99.05 C ANISOU 2397 C THR A1109 14399 12500 10737 -167 1053 130 C ATOM 2398 O THR A1109 28.760 -5.507 -9.855 1.00 99.32 O ANISOU 2398 O THR A1109 14324 12632 10782 -188 1088 99 O ATOM 2399 CB THR A1109 26.631 -4.824 -12.211 1.00104.08 C ANISOU 2399 CB THR A1109 15226 13044 11274 -125 1098 156 C ATOM 2400 OG1 THR A1109 25.430 -5.048 -12.953 1.00103.54 O ANISOU 2400 OG1 THR A1109 15242 12928 11170 -45 1062 169 O ATOM 2401 CG2 THR A1109 27.834 -5.107 -13.097 1.00103.79 C ANISOU 2401 CG2 THR A1109 15141 13075 11220 -165 1175 130 C ATOM 2402 N GLY A1110 27.112 -4.177 -9.062 1.00 95.04 N ANISOU 2402 N GLY A1110 13943 11940 10229 -208 1029 148 N ATOM 2403 CA GLY A1110 27.900 -3.524 -8.023 1.00 95.15 C ANISOU 2403 CA GLY A1110 13894 12003 10255 -300 1043 129 C ATOM 2404 C GLY A1110 28.420 -4.451 -6.941 1.00 98.81 C ANISOU 2404 C GLY A1110 14207 12564 10773 -252 996 106 C ATOM 2405 O GLY A1110 29.621 -4.445 -6.655 1.00 99.38 O ANISOU 2405 O GLY A1110 14165 12753 10841 -304 1028 66 O ATOM 2406 N VAL A1111 27.514 -5.257 -6.339 1.00 93.85 N ANISOU 2406 N VAL A1111 13579 11896 10184 -149 924 127 N ATOM 2407 CA VAL A1111 27.800 -6.208 -5.251 1.00 93.14 C ANISOU 2407 CA VAL A1111 13384 11870 10136 -76 878 118 C ATOM 2408 C VAL A1111 28.731 -7.324 -5.747 1.00 97.40 C ANISOU 2408 C VAL A1111 13833 12499 10674 -7 907 95 C ATOM 2409 O VAL A1111 29.621 -7.750 -5.006 1.00 97.37 O ANISOU 2409 O VAL A1111 13716 12605 10675 29 900 75 O ATOM 2410 CB VAL A1111 26.496 -6.789 -4.633 1.00 95.96 C ANISOU 2410 CB VAL A1111 13795 12139 10526 4 814 145 C ATOM 2411 CG1 VAL A1111 26.785 -7.606 -3.373 1.00 95.67 C ANISOU 2411 CG1 VAL A1111 13677 12151 10520 75 776 143 C ATOM 2412 CG2 VAL A1111 25.502 -5.681 -4.320 1.00 95.27 C ANISOU 2412 CG2 VAL A1111 13801 11968 10428 -46 789 166 C ATOM 2413 N ALA A1112 28.546 -7.762 -7.010 1.00 93.99 N ANISOU 2413 N ALA A1112 13453 12031 10226 19 941 97 N ATOM 2414 CA ALA A1112 29.344 -8.805 -7.662 1.00 94.25 C ANISOU 2414 CA ALA A1112 13426 12133 10252 89 978 76 C ATOM 2415 C ALA A1112 30.846 -8.435 -7.739 1.00 98.98 C ANISOU 2415 C ALA A1112 13903 12881 10823 36 1027 38 C ATOM 2416 O ALA A1112 31.688 -9.327 -7.863 1.00 99.45 O ANISOU 2416 O ALA A1112 13874 13036 10875 118 1047 16 O ATOM 2417 CB ALA A1112 28.797 -9.078 -9.055 1.00 94.83 C ANISOU 2417 CB ALA A1112 13590 12137 10305 99 1008 79 C ATOM 2418 N GLY A1113 31.153 -7.140 -7.619 1.00 95.27 N ANISOU 2418 N GLY A1113 13432 12433 10334 -100 1052 24 N ATOM 2419 CA GLY A1113 32.511 -6.606 -7.635 1.00 96.05 C ANISOU 2419 CA GLY A1113 13413 12682 10399 -194 1109 -29 C ATOM 2420 C GLY A1113 33.331 -6.910 -6.394 1.00100.35 C ANISOU 2420 C GLY A1113 13799 13382 10948 -156 1074 -64 C ATOM 2421 O GLY A1113 34.554 -6.740 -6.408 1.00100.76 O ANISOU 2421 O GLY A1113 13715 13605 10965 -208 1116 -123 O ATOM 2422 N PHE A1114 32.667 -7.356 -5.308 1.00 96.62 N ANISOU 2422 N PHE A1114 13338 12863 10508 -66 998 -32 N ATOM 2423 CA PHE A1114 33.297 -7.708 -4.033 1.00 97.03 C ANISOU 2423 CA PHE A1114 13258 13054 10557 -1 954 -55 C ATOM 2424 C PHE A1114 33.668 -9.201 -4.044 1.00101.47 C ANISOU 2424 C PHE A1114 13766 13675 11114 194 941 -46 C ATOM 2425 O PHE A1114 33.209 -9.973 -3.200 1.00100.67 O ANISOU 2425 O PHE A1114 13690 13531 11028 321 890 -12 O ATOM 2426 CB PHE A1114 32.357 -7.363 -2.861 1.00 98.08 C ANISOU 2426 CB PHE A1114 13454 13093 10720 -5 888 -21 C ATOM 2427 CG PHE A1114 32.051 -5.893 -2.699 1.00 99.93 C ANISOU 2427 CG PHE A1114 13747 13270 10949 -179 904 -32 C ATOM 2428 CD1 PHE A1114 30.973 -5.313 -3.359 1.00102.40 C ANISOU 2428 CD1 PHE A1114 14225 13409 11275 -231 917 8 C ATOM 2429 CD2 PHE A1114 32.811 -5.097 -1.852 1.00103.54 C ANISOU 2429 CD2 PHE A1114 14105 13853 11381 -284 908 -84 C ATOM 2430 CE1 PHE A1114 30.683 -3.954 -3.202 1.00103.55 C ANISOU 2430 CE1 PHE A1114 14453 13488 11405 -371 940 5 C ATOM 2431 CE2 PHE A1114 32.517 -3.737 -1.689 1.00106.56 C ANISOU 2431 CE2 PHE A1114 14571 14164 11754 -449 936 -96 C ATOM 2432 CZ PHE A1114 31.454 -3.176 -2.365 1.00103.80 C ANISOU 2432 CZ PHE A1114 14403 13621 11415 -484 955 -46 C ATOM 2433 N THR A1115 34.509 -9.592 -5.019 1.00 99.13 N ANISOU 2433 N THR A1115 13408 13469 10786 219 997 -76 N ATOM 2434 CA THR A1115 34.957 -10.964 -5.288 1.00 99.56 C ANISOU 2434 CA THR A1115 13430 13574 10824 404 1006 -71 C ATOM 2435 C THR A1115 35.603 -11.650 -4.075 1.00104.29 C ANISOU 2435 C THR A1115 13916 14317 11393 561 962 -78 C ATOM 2436 O THR A1115 35.372 -12.844 -3.874 1.00103.86 O ANISOU 2436 O THR A1115 13920 14205 11335 740 951 -42 O ATOM 2437 CB THR A1115 35.915 -10.994 -6.489 1.00108.49 C ANISOU 2437 CB THR A1115 14490 14814 11918 377 1079 -115 C ATOM 2438 OG1 THR A1115 36.920 -9.989 -6.333 1.00109.92 O ANISOU 2438 OG1 THR A1115 14525 15177 12063 238 1107 -182 O ATOM 2439 CG2 THR A1115 35.190 -10.804 -7.818 1.00105.74 C ANISOU 2439 CG2 THR A1115 14284 14303 11588 299 1123 -92 C ATOM 2440 N ASN A1116 36.389 -10.911 -3.271 1.00102.00 N ANISOU 2440 N ASN A1116 13475 14209 11070 494 942 -129 N ATOM 2441 CA ASN A1116 37.067 -11.458 -2.090 1.00102.91 C ANISOU 2441 CA ASN A1116 13465 14497 11140 648 893 -144 C ATOM 2442 C ASN A1116 36.094 -11.620 -0.906 1.00105.23 C ANISOU 2442 C ASN A1116 13858 14660 11464 704 827 -87 C ATOM 2443 O ASN A1116 36.087 -12.679 -0.274 1.00104.99 O ANISOU 2443 O ASN A1116 13850 14630 11410 907 801 -52 O ATOM 2444 CB ASN A1116 38.271 -10.587 -1.690 1.00106.37 C ANISOU 2444 CB ASN A1116 13687 15206 11521 541 897 -236 C ATOM 2445 CG ASN A1116 39.267 -10.318 -2.804 1.00136.50 C ANISOU 2445 CG ASN A1116 17393 19169 15301 455 973 -305 C ATOM 2446 OD1 ASN A1116 39.616 -11.194 -3.607 1.00132.41 O ANISOU 2446 OD1 ASN A1116 16874 18671 14766 583 1008 -297 O ATOM 2447 ND2 ASN A1116 39.772 -9.095 -2.859 1.00130.10 N ANISOU 2447 ND2 ASN A1116 16491 18466 14474 230 1009 -379 N ATOM 2448 N SER A1117 35.270 -10.580 -0.624 1.00100.04 N ANISOU 2448 N SER A1117 13274 13885 10853 533 808 -77 N ATOM 2449 CA SER A1117 34.281 -10.553 0.462 1.00 98.48 C ANISOU 2449 CA SER A1117 13169 13562 10687 554 750 -29 C ATOM 2450 C SER A1117 33.208 -11.628 0.303 1.00100.43 C ANISOU 2450 C SER A1117 13588 13602 10970 677 749 40 C ATOM 2451 O SER A1117 32.860 -12.267 1.295 1.00 99.73 O ANISOU 2451 O SER A1117 13540 13476 10876 798 712 74 O ATOM 2452 CB SER A1117 33.609 -9.187 0.551 1.00101.45 C ANISOU 2452 CB SER A1117 13602 13846 11100 345 745 -36 C ATOM 2453 OG SER A1117 34.499 -8.198 1.040 1.00111.83 O ANISOU 2453 OG SER A1117 14776 15338 12377 221 746 -104 O ATOM 2454 N LEU A1118 32.686 -11.824 -0.935 1.00 95.99 N ANISOU 2454 N LEU A1118 13127 12909 10437 638 794 53 N ATOM 2455 CA LEU A1118 31.651 -12.820 -1.251 1.00 94.82 C ANISOU 2455 CA LEU A1118 13138 12571 10317 720 807 99 C ATOM 2456 C LEU A1118 32.149 -14.246 -0.986 1.00 99.06 C ANISOU 2456 C LEU A1118 13687 13138 10815 933 825 115 C ATOM 2457 O LEU A1118 31.370 -15.095 -0.541 1.00 98.58 O ANISOU 2457 O LEU A1118 13754 12938 10764 1020 827 153 O ATOM 2458 CB LEU A1118 31.182 -12.689 -2.713 1.00 94.27 C ANISOU 2458 CB LEU A1118 13147 12403 10269 633 852 94 C ATOM 2459 CG LEU A1118 30.228 -11.534 -3.046 1.00 97.49 C ANISOU 2459 CG LEU A1118 13623 12711 10710 467 839 98 C ATOM 2460 CD1 LEU A1118 30.287 -11.199 -4.522 1.00 97.37 C ANISOU 2460 CD1 LEU A1118 13635 12675 10686 390 889 82 C ATOM 2461 CD2 LEU A1118 28.793 -11.851 -2.635 1.00 98.69 C ANISOU 2461 CD2 LEU A1118 13902 12699 10897 477 809 131 C ATOM 2462 N ARG A1119 33.452 -14.490 -1.236 1.00 95.91 N ANISOU 2462 N ARG A1119 13158 12922 10363 1019 846 83 N ATOM 2463 CA ARG A1119 34.123 -15.769 -1.018 1.00 96.64 C ANISOU 2463 CA ARG A1119 13249 13073 10397 1249 868 96 C ATOM 2464 C ARG A1119 34.204 -16.084 0.486 1.00100.59 C ANISOU 2464 C ARG A1119 13737 13621 10860 1382 819 122 C ATOM 2465 O ARG A1119 33.966 -17.226 0.877 1.00101.07 O ANISOU 2465 O ARG A1119 13920 13589 10894 1558 840 165 O ATOM 2466 CB ARG A1119 35.519 -15.736 -1.656 1.00 98.74 C ANISOU 2466 CB ARG A1119 13349 13560 10607 1294 897 44 C ATOM 2467 CG ARG A1119 36.265 -17.067 -1.635 1.00112.57 C ANISOU 2467 CG ARG A1119 15105 15381 12287 1554 929 56 C ATOM 2468 CD ARG A1119 37.378 -17.142 -2.667 1.00127.74 C ANISOU 2468 CD ARG A1119 16901 17469 14165 1582 976 5 C ATOM 2469 NE ARG A1119 38.368 -16.069 -2.529 1.00138.28 N ANISOU 2469 NE ARG A1119 18005 19063 15472 1470 952 -65 N ATOM 2470 CZ ARG A1119 38.599 -15.141 -3.451 1.00152.75 C ANISOU 2470 CZ ARG A1119 19768 20941 17330 1266 984 -114 C ATOM 2471 NH1 ARG A1119 39.516 -14.206 -3.243 1.00142.36 N ANISOU 2471 NH1 ARG A1119 18252 19860 15980 1153 975 -188 N ATOM 2472 NH2 ARG A1119 37.920 -15.143 -4.592 1.00137.25 N ANISOU 2472 NH2 ARG A1119 17939 18792 15418 1170 1031 -95 N ATOM 2473 N MET A1120 34.516 -15.071 1.320 1.00 96.29 N ANISOU 2473 N MET A1120 13062 13215 10310 1294 761 95 N ATOM 2474 CA MET A1120 34.616 -15.202 2.781 1.00 96.05 C ANISOU 2474 CA MET A1120 13001 13254 10239 1403 706 113 C ATOM 2475 C MET A1120 33.237 -15.454 3.406 1.00 98.09 C ANISOU 2475 C MET A1120 13448 13275 10547 1387 694 172 C ATOM 2476 O MET A1120 33.146 -16.172 4.402 1.00 98.40 O ANISOU 2476 O MET A1120 13550 13293 10546 1546 680 211 O ATOM 2477 CB MET A1120 35.258 -13.953 3.414 1.00 98.63 C ANISOU 2477 CB MET A1120 13139 13789 10548 1274 653 54 C ATOM 2478 CG MET A1120 36.672 -13.666 2.946 1.00103.63 C ANISOU 2478 CG MET A1120 13562 14693 11120 1274 668 -22 C ATOM 2479 SD MET A1120 37.911 -14.790 3.624 1.00109.69 S ANISOU 2479 SD MET A1120 14205 15711 11762 1592 649 -31 S ATOM 2480 CE MET A1120 39.387 -14.084 2.933 1.00107.76 C ANISOU 2480 CE MET A1120 13688 15793 11462 1497 669 -146 C ATOM 2481 N LEU A1121 32.173 -14.871 2.819 1.00 92.45 N ANISOU 2481 N LEU A1121 12824 12391 9910 1202 704 177 N ATOM 2482 CA LEU A1121 30.794 -15.040 3.284 1.00 90.81 C ANISOU 2482 CA LEU A1121 12779 11974 9750 1162 698 218 C ATOM 2483 C LEU A1121 30.301 -16.452 2.995 1.00 95.16 C ANISOU 2483 C LEU A1121 13500 12365 10292 1291 759 253 C ATOM 2484 O LEU A1121 29.588 -17.036 3.816 1.00 95.19 O ANISOU 2484 O LEU A1121 13627 12247 10293 1351 764 289 O ATOM 2485 CB LEU A1121 29.861 -14.007 2.632 1.00 89.35 C ANISOU 2485 CB LEU A1121 12627 11688 9635 947 691 204 C ATOM 2486 CG LEU A1121 30.033 -12.556 3.075 1.00 93.14 C ANISOU 2486 CG LEU A1121 13001 12263 10126 800 643 177 C ATOM 2487 CD1 LEU A1121 29.261 -11.628 2.175 1.00 92.03 C ANISOU 2487 CD1 LEU A1121 12912 12023 10032 625 655 167 C ATOM 2488 CD2 LEU A1121 29.631 -12.362 4.526 1.00 95.25 C ANISOU 2488 CD2 LEU A1121 13278 12522 10390 820 591 197 C ATOM 2489 N GLN A1122 30.708 -17.003 1.835 1.00 91.57 N ANISOU 2489 N GLN A1122 13060 11908 9827 1330 815 238 N ATOM 2490 CA GLN A1122 30.379 -18.353 1.373 1.00 91.54 C ANISOU 2490 CA GLN A1122 13221 11754 9805 1443 890 259 C ATOM 2491 C GLN A1122 31.032 -19.422 2.265 1.00 96.41 C ANISOU 2491 C GLN A1122 13886 12403 10341 1688 911 294 C ATOM 2492 O GLN A1122 30.466 -20.502 2.427 1.00 96.70 O ANISOU 2492 O GLN A1122 14113 12269 10361 1776 974 324 O ATOM 2493 CB GLN A1122 30.841 -18.525 -0.078 1.00 93.08 C ANISOU 2493 CB GLN A1122 13392 11973 10000 1424 939 228 C ATOM 2494 CG GLN A1122 30.043 -19.552 -0.867 1.00109.43 C ANISOU 2494 CG GLN A1122 15649 13847 12082 1430 1018 229 C ATOM 2495 CD GLN A1122 30.792 -20.040 -2.081 1.00132.05 C ANISOU 2495 CD GLN A1122 18499 16756 14919 1488 1075 206 C ATOM 2496 OE1 GLN A1122 31.064 -21.234 -2.226 1.00129.87 O ANISOU 2496 OE1 GLN A1122 18334 16416 14595 1645 1144 218 O ATOM 2497 NE2 GLN A1122 31.150 -19.131 -2.981 1.00124.50 N ANISOU 2497 NE2 GLN A1122 17417 15902 13985 1367 1055 172 N ATOM 2498 N GLN A1123 32.218 -19.110 2.838 1.00 92.97 N ANISOU 2498 N GLN A1123 13284 12194 9848 1797 863 286 N ATOM 2499 CA GLN A1123 33.000 -19.980 3.728 1.00 93.59 C ANISOU 2499 CA GLN A1123 13374 12358 9826 2060 868 318 C ATOM 2500 C GLN A1123 32.647 -19.760 5.211 1.00 96.71 C ANISOU 2500 C GLN A1123 13787 12756 10205 2092 813 349 C ATOM 2501 O GLN A1123 33.329 -20.305 6.086 1.00 97.65 O ANISOU 2501 O GLN A1123 13894 12978 10230 2313 801 375 O ATOM 2502 CB GLN A1123 34.502 -19.732 3.522 1.00 95.90 C ANISOU 2502 CB GLN A1123 13447 12940 10051 2164 840 277 C ATOM 2503 CG GLN A1123 35.073 -20.300 2.233 1.00105.26 C ANISOU 2503 CG GLN A1123 14632 14141 11219 2224 907 256 C ATOM 2504 CD GLN A1123 36.416 -19.701 1.893 1.00118.70 C ANISOU 2504 CD GLN A1123 16080 16144 12876 2237 876 194 C ATOM 2505 OE1 GLN A1123 37.225 -19.373 2.762 1.00112.97 O ANISOU 2505 OE1 GLN A1123 15190 15648 12084 2323 818 172 O ATOM 2506 NE2 GLN A1123 36.692 -19.562 0.611 1.00110.02 N ANISOU 2506 NE2 GLN A1123 14937 15060 11803 2149 919 157 N ATOM 2507 N LYS A1124 31.587 -18.961 5.485 1.00 91.39 N ANISOU 2507 N LYS A1124 13140 11974 9612 1884 780 347 N ATOM 2508 CA LYS A1124 31.068 -18.614 6.815 1.00 90.90 C ANISOU 2508 CA LYS A1124 13098 11890 9548 1870 729 372 C ATOM 2509 C LYS A1124 32.147 -17.934 7.708 1.00 96.26 C ANISOU 2509 C LYS A1124 13571 12839 10165 1937 648 349 C ATOM 2510 O LYS A1124 32.179 -18.147 8.925 1.00 96.61 O ANISOU 2510 O LYS A1124 13639 12915 10155 2056 617 379 O ATOM 2511 CB LYS A1124 30.448 -19.842 7.513 1.00 93.72 C ANISOU 2511 CB LYS A1124 13685 12058 9864 2021 789 431 C ATOM 2512 N ARG A1125 33.002 -17.092 7.083 1.00 93.02 N ANISOU 2512 N ARG A1125 12959 12624 9760 1844 619 288 N ATOM 2513 CA ARG A1125 34.073 -16.309 7.719 1.00 93.65 C ANISOU 2513 CA ARG A1125 12812 12989 9782 1852 551 237 C ATOM 2514 C ARG A1125 33.612 -14.850 7.743 1.00 97.29 C ANISOU 2514 C ARG A1125 13197 13449 10319 1576 511 195 C ATOM 2515 O ARG A1125 33.816 -14.108 6.779 1.00 96.91 O ANISOU 2515 O ARG A1125 13073 13437 10313 1410 528 149 O ATOM 2516 CB ARG A1125 35.404 -16.496 6.958 1.00 94.29 C ANISOU 2516 CB ARG A1125 12731 13294 9802 1943 568 187 C ATOM 2517 CG ARG A1125 35.946 -17.926 7.002 1.00101.40 C ANISOU 2517 CG ARG A1125 13709 14212 10608 2251 607 229 C ATOM 2518 CD ARG A1125 36.933 -18.231 5.893 1.00105.57 C ANISOU 2518 CD ARG A1125 14133 14879 11100 2318 648 188 C ATOM 2519 NE ARG A1125 38.147 -17.417 5.975 1.00114.32 N ANISOU 2519 NE ARG A1125 14958 16325 12154 2281 600 101 N ATOM 2520 CZ ARG A1125 39.250 -17.634 5.266 1.00131.48 C ANISOU 2520 CZ ARG A1125 16984 18705 14266 2368 624 50 C ATOM 2521 NH1 ARG A1125 40.300 -16.836 5.401 1.00120.39 N ANISOU 2521 NH1 ARG A1125 15313 17619 12811 2303 584 -43 N ATOM 2522 NH2 ARG A1125 39.313 -18.652 4.417 1.00119.70 N ANISOU 2522 NH2 ARG A1125 15611 17109 12761 2515 693 84 N ATOM 2523 N TRP A1126 32.925 -14.466 8.825 1.00 93.84 N ANISOU 2523 N TRP A1126 12809 12949 9898 1531 468 217 N ATOM 2524 CA TRP A1126 32.275 -13.165 8.965 1.00 92.86 C ANISOU 2524 CA TRP A1126 12664 12775 9843 1291 438 191 C ATOM 2525 C TRP A1126 33.213 -11.999 9.295 1.00 98.50 C ANISOU 2525 C TRP A1126 13170 13732 10525 1175 395 113 C ATOM 2526 O TRP A1126 33.056 -10.935 8.692 1.00 97.62 O ANISOU 2526 O TRP A1126 13029 13598 10465 961 407 73 O ATOM 2527 CB TRP A1126 31.154 -13.234 10.013 1.00 90.76 C ANISOU 2527 CB TRP A1126 12534 12348 9601 1292 415 241 C ATOM 2528 CG TRP A1126 30.357 -14.510 9.994 1.00 91.53 C ANISOU 2528 CG TRP A1126 12833 12239 9704 1423 464 308 C ATOM 2529 CD1 TRP A1126 30.242 -15.413 11.008 1.00 95.09 C ANISOU 2529 CD1 TRP A1126 13382 12651 10097 1605 467 357 C ATOM 2530 CD2 TRP A1126 29.603 -15.043 8.893 1.00 90.62 C ANISOU 2530 CD2 TRP A1126 12854 11933 9646 1378 530 325 C ATOM 2531 NE1 TRP A1126 29.444 -16.464 10.619 1.00 94.38 N ANISOU 2531 NE1 TRP A1126 13492 12341 10026 1659 540 402 N ATOM 2532 CE2 TRP A1126 29.042 -16.266 9.323 1.00 94.88 C ANISOU 2532 CE2 TRP A1126 13573 12317 10160 1519 576 378 C ATOM 2533 CE3 TRP A1126 29.338 -14.602 7.585 1.00 91.09 C ANISOU 2533 CE3 TRP A1126 12907 11938 9766 1230 557 297 C ATOM 2534 CZ2 TRP A1126 28.225 -17.048 8.497 1.00 93.69 C ANISOU 2534 CZ2 TRP A1126 13584 11967 10047 1496 651 393 C ATOM 2535 CZ3 TRP A1126 28.554 -15.392 6.759 1.00 92.13 C ANISOU 2535 CZ3 TRP A1126 13187 11887 9930 1228 620 316 C ATOM 2536 CH2 TRP A1126 28.004 -16.597 7.216 1.00 93.06 C ANISOU 2536 CH2 TRP A1126 13472 11860 10025 1351 667 358 C ATOM 2537 N ASP A1127 34.150 -12.168 10.250 1.00 96.89 N ANISOU 2537 N ASP A1127 12831 13756 10227 1309 349 86 N ATOM 2538 CA ASP A1127 35.053 -11.083 10.659 1.00 97.68 C ANISOU 2538 CA ASP A1127 12721 14108 10284 1185 311 -7 C ATOM 2539 C ASP A1127 36.087 -10.719 9.571 1.00101.09 C ANISOU 2539 C ASP A1127 12997 14714 10699 1098 350 -85 C ATOM 2540 O ASP A1127 36.447 -9.546 9.457 1.00100.35 O ANISOU 2540 O ASP A1127 12794 14723 10612 881 355 -164 O ATOM 2541 CB ASP A1127 35.755 -11.418 11.983 1.00101.37 C ANISOU 2541 CB ASP A1127 13076 14798 10642 1364 248 -23 C ATOM 2542 CG ASP A1127 34.886 -11.163 13.203 1.00115.04 C ANISOU 2542 CG ASP A1127 14906 16418 12387 1348 203 17 C ATOM 2543 OD1 ASP A1127 33.854 -11.860 13.358 1.00115.40 O ANISOU 2543 OD1 ASP A1127 15154 16220 12474 1429 221 105 O ATOM 2544 OD2 ASP A1127 35.232 -10.266 14.001 1.00122.89 O ANISOU 2544 OD2 ASP A1127 15774 17571 13347 1244 157 -48 O ATOM 2545 N GLU A1128 36.533 -11.707 8.768 1.00 97.60 N ANISOU 2545 N GLU A1128 12561 14292 10233 1257 388 -65 N ATOM 2546 CA GLU A1128 37.502 -11.495 7.687 1.00 97.87 C ANISOU 2546 CA GLU A1128 12453 14486 10247 1193 432 -135 C ATOM 2547 C GLU A1128 36.839 -10.813 6.486 1.00100.20 C ANISOU 2547 C GLU A1128 12852 14580 10641 966 491 -131 C ATOM 2548 O GLU A1128 37.490 -10.020 5.802 1.00100.30 O ANISOU 2548 O GLU A1128 12749 14712 10648 799 527 -207 O ATOM 2549 CB GLU A1128 38.166 -12.813 7.281 1.00100.20 C ANISOU 2549 CB GLU A1128 12732 14865 10476 1461 453 -111 C ATOM 2550 CG GLU A1128 39.125 -13.321 8.343 1.00111.05 C ANISOU 2550 CG GLU A1128 13956 16517 11723 1692 398 -137 C ATOM 2551 CD GLU A1128 39.618 -14.740 8.166 1.00128.68 C ANISOU 2551 CD GLU A1128 16225 18793 13875 2014 418 -91 C ATOM 2552 OE1 GLU A1128 38.775 -15.663 8.098 1.00119.78 O ANISOU 2552 OE1 GLU A1128 15331 17400 12779 2140 449 7 O ATOM 2553 OE2 GLU A1128 40.853 -14.935 8.164 1.00122.37 O ANISOU 2553 OE2 GLU A1128 15222 18304 12971 2146 405 -157 O ATOM 2554 N ALA A1129 35.541 -11.100 6.247 1.00 94.67 N ANISOU 2554 N ALA A1129 12368 13584 10019 957 503 -49 N ATOM 2555 CA ALA A1129 34.753 -10.466 5.191 1.00 92.90 C ANISOU 2555 CA ALA A1129 12257 13163 9876 767 549 -38 C ATOM 2556 C ALA A1129 34.482 -9.017 5.565 1.00 97.03 C ANISOU 2556 C ALA A1129 12761 13679 10425 538 536 -77 C ATOM 2557 O ALA A1129 34.496 -8.149 4.693 1.00 96.94 O ANISOU 2557 O ALA A1129 12760 13634 10440 357 583 -109 O ATOM 2558 CB ALA A1129 33.441 -11.210 4.992 1.00 92.17 C ANISOU 2558 CB ALA A1129 12378 12798 9844 834 558 47 C ATOM 2559 N ALA A1130 34.270 -8.762 6.878 1.00 93.49 N ANISOU 2559 N ALA A1130 12297 13262 9960 552 479 -75 N ATOM 2560 CA ALA A1130 33.967 -7.459 7.473 1.00 93.01 C ANISOU 2560 CA ALA A1130 12235 13188 9915 357 464 -110 C ATOM 2561 C ALA A1130 35.087 -6.429 7.287 1.00 98.74 C ANISOU 2561 C ALA A1130 12796 14125 10595 180 495 -217 C ATOM 2562 O ALA A1130 34.786 -5.241 7.157 1.00 98.37 O ANISOU 2562 O ALA A1130 12800 14004 10573 -31 525 -246 O ATOM 2563 CB ALA A1130 33.674 -7.626 8.951 1.00 93.63 C ANISOU 2563 CB ALA A1130 12314 13291 9971 447 396 -89 C ATOM 2564 N VAL A1131 36.364 -6.868 7.284 1.00 96.86 N ANISOU 2564 N VAL A1131 12367 14154 10283 262 493 -280 N ATOM 2565 CA VAL A1131 37.525 -5.978 7.131 1.00 98.10 C ANISOU 2565 CA VAL A1131 12338 14551 10382 87 530 -402 C ATOM 2566 C VAL A1131 37.595 -5.442 5.683 1.00102.43 C ANISOU 2566 C VAL A1131 12940 15011 10965 -81 622 -421 C ATOM 2567 O VAL A1131 37.806 -4.239 5.496 1.00102.51 O ANISOU 2567 O VAL A1131 12943 15036 10971 -323 676 -490 O ATOM 2568 CB VAL A1131 38.857 -6.656 7.567 1.00103.58 C ANISOU 2568 CB VAL A1131 12793 15589 10973 245 497 -472 C ATOM 2569 CG1 VAL A1131 40.041 -5.697 7.452 1.00105.01 C ANISOU 2569 CG1 VAL A1131 12765 16047 11089 36 540 -618 C ATOM 2570 CG2 VAL A1131 38.761 -7.196 8.990 1.00103.60 C ANISOU 2570 CG2 VAL A1131 12763 15672 10927 432 408 -445 C ATOM 2571 N ASN A1132 37.402 -6.329 4.677 1.00 98.75 N ANISOU 2571 N ASN A1132 12546 14446 10529 45 646 -360 N ATOM 2572 CA ASN A1132 37.446 -5.983 3.250 1.00 98.46 C ANISOU 2572 CA ASN A1132 12569 14324 10518 -79 730 -368 C ATOM 2573 C ASN A1132 36.298 -5.058 2.844 1.00101.95 C ANISOU 2573 C ASN A1132 13220 14493 11025 -242 762 -321 C ATOM 2574 O ASN A1132 36.522 -4.146 2.045 1.00101.91 O ANISOU 2574 O ASN A1132 13244 14463 11014 -432 839 -363 O ATOM 2575 CB ASN A1132 37.437 -7.238 2.383 1.00 97.35 C ANISOU 2575 CB ASN A1132 12462 14137 10388 114 740 -313 C ATOM 2576 CG ASN A1132 38.704 -8.047 2.479 1.00118.18 C ANISOU 2576 CG ASN A1132 14899 17055 12949 271 733 -367 C ATOM 2577 OD1 ASN A1132 38.749 -9.092 3.132 1.00114.18 O ANISOU 2577 OD1 ASN A1132 14373 16596 12413 506 679 -327 O ATOM 2578 ND2 ASN A1132 39.761 -7.588 1.822 1.00108.92 N ANISOU 2578 ND2 ASN A1132 13577 16076 11730 153 793 -459 N ATOM 2579 N LEU A1133 35.082 -5.278 3.405 1.00 97.77 N ANISOU 2579 N LEU A1133 12838 13766 10546 -164 707 -239 N ATOM 2580 CA LEU A1133 33.884 -4.469 3.143 1.00 96.56 C ANISOU 2580 CA LEU A1133 12877 13366 10443 -277 724 -190 C ATOM 2581 C LEU A1133 34.062 -3.048 3.674 1.00102.41 C ANISOU 2581 C LEU A1133 13617 14133 11162 -489 751 -251 C ATOM 2582 O LEU A1133 33.536 -2.103 3.081 1.00101.62 O ANISOU 2582 O LEU A1133 13659 13877 11075 -628 806 -240 O ATOM 2583 CB LEU A1133 32.627 -5.109 3.755 1.00 95.07 C ANISOU 2583 CB LEU A1133 12812 13008 10303 -139 657 -104 C ATOM 2584 CG LEU A1133 32.122 -6.414 3.127 1.00 98.74 C ANISOU 2584 CG LEU A1133 13345 13375 10796 35 650 -40 C ATOM 2585 CD1 LEU A1133 31.156 -7.112 4.052 1.00 97.90 C ANISOU 2585 CD1 LEU A1133 13319 13161 10718 162 591 20 C ATOM 2586 CD2 LEU A1133 31.476 -6.178 1.768 1.00100.19 C ANISOU 2586 CD2 LEU A1133 13658 13401 11010 -29 700 -13 C ATOM 2587 N ALA A1134 34.823 -2.902 4.778 1.00101.32 N ANISOU 2587 N ALA A1134 13325 14194 10979 -507 717 -318 N ATOM 2588 CA ALA A1134 35.162 -1.619 5.388 1.00102.71 C ANISOU 2588 CA ALA A1134 13475 14431 11121 -719 749 -397 C ATOM 2589 C ALA A1134 36.158 -0.858 4.506 1.00110.20 C ANISOU 2589 C ALA A1134 14361 15485 12024 -921 854 -490 C ATOM 2590 O ALA A1134 36.133 0.374 4.479 1.00110.64 O ANISOU 2590 O ALA A1134 14500 15476 12064 -1137 924 -536 O ATOM 2591 CB ALA A1134 35.746 -1.839 6.773 1.00104.24 C ANISOU 2591 CB ALA A1134 13500 14840 11268 -663 678 -451 C ATOM 2592 N LYS A1135 37.021 -1.600 3.777 1.00108.74 N ANISOU 2592 N LYS A1135 14044 15457 11816 -849 874 -519 N ATOM 2593 CA LYS A1135 38.026 -1.053 2.867 1.00110.46 C ANISOU 2593 CA LYS A1135 14185 15798 11988 -1025 978 -610 C ATOM 2594 C LYS A1135 37.445 -0.967 1.440 1.00115.11 C ANISOU 2594 C LYS A1135 14960 16163 12615 -1047 1047 -541 C ATOM 2595 O LYS A1135 37.876 -1.695 0.539 1.00115.37 O ANISOU 2595 O LYS A1135 14936 16255 12644 -962 1068 -535 O ATOM 2596 CB LYS A1135 39.309 -1.905 2.917 1.00114.30 C ANISOU 2596 CB LYS A1135 14407 16605 12416 -922 958 -686 C ATOM 2597 N SER A1136 36.440 -0.081 1.255 1.00111.49 N ANISOU 2597 N SER A1136 14727 15449 12185 -1146 1080 -488 N ATOM 2598 CA SER A1136 35.745 0.150 -0.021 1.00110.94 C ANISOU 2598 CA SER A1136 14858 15157 12138 -1161 1141 -419 C ATOM 2599 C SER A1136 35.099 1.545 -0.071 1.00115.08 C ANISOU 2599 C SER A1136 15597 15479 12650 -1335 1211 -409 C ATOM 2600 O SER A1136 34.926 2.177 0.974 1.00114.68 O ANISOU 2600 O SER A1136 15561 15421 12592 -1409 1192 -434 O ATOM 2601 CB SER A1136 34.680 -0.922 -0.260 1.00113.04 C ANISOU 2601 CB SER A1136 15206 15280 12463 -929 1058 -307 C ATOM 2602 OG SER A1136 33.598 -0.827 0.655 1.00120.75 O ANISOU 2602 OG SER A1136 16279 16123 13476 -865 984 -249 O ATOM 2603 N ARG A1137 34.713 2.002 -1.288 1.00111.70 N ANISOU 2603 N ARG A1137 15349 14881 12211 -1384 1292 -367 N ATOM 2604 CA ARG A1137 34.054 3.294 -1.529 1.00111.49 C ANISOU 2604 CA ARG A1137 15567 14639 12157 -1514 1371 -342 C ATOM 2605 C ARG A1137 32.622 3.310 -0.957 1.00113.70 C ANISOU 2605 C ARG A1137 15989 14734 12477 -1377 1283 -248 C ATOM 2606 O ARG A1137 32.102 4.391 -0.671 1.00113.34 O ANISOU 2606 O ARG A1137 16115 14543 12406 -1468 1327 -238 O ATOM 2607 CB ARG A1137 34.035 3.626 -3.029 1.00111.92 C ANISOU 2607 CB ARG A1137 15772 14576 12177 -1559 1475 -315 C ATOM 2608 N TRP A1138 32.002 2.112 -0.784 1.00108.87 N ANISOU 2608 N TRP A1138 15311 14132 11924 -1164 1168 -186 N ATOM 2609 CA TRP A1138 30.660 1.904 -0.218 1.00107.07 C ANISOU 2609 CA TRP A1138 15179 13766 11737 -1025 1078 -107 C ATOM 2610 C TRP A1138 30.624 2.350 1.248 1.00112.00 C ANISOU 2610 C TRP A1138 15763 14426 12366 -1074 1037 -138 C ATOM 2611 O TRP A1138 29.690 3.044 1.656 1.00111.04 O ANISOU 2611 O TRP A1138 15791 14156 12243 -1076 1028 -100 O ATOM 2612 CB TRP A1138 30.237 0.420 -0.349 1.00104.26 C ANISOU 2612 CB TRP A1138 14739 13443 11434 -819 987 -57 C ATOM 2613 CG TRP A1138 28.963 0.054 0.365 1.00103.61 C ANISOU 2613 CG TRP A1138 14718 13257 11393 -689 896 5 C ATOM 2614 CD1 TRP A1138 27.725 0.591 0.163 1.00105.77 C ANISOU 2614 CD1 TRP A1138 15162 13360 11664 -658 888 59 C ATOM 2615 CD2 TRP A1138 28.800 -0.964 1.362 1.00102.60 C ANISOU 2615 CD2 TRP A1138 14480 13197 11305 -565 807 15 C ATOM 2616 NE1 TRP A1138 26.806 -0.011 0.990 1.00104.09 N ANISOU 2616 NE1 TRP A1138 14939 13116 11493 -540 801 95 N ATOM 2617 CE2 TRP A1138 27.438 -0.972 1.735 1.00105.35 C ANISOU 2617 CE2 TRP A1138 14939 13408 11680 -487 754 72 C ATOM 2618 CE3 TRP A1138 29.677 -1.870 1.984 1.00104.03 C ANISOU 2618 CE3 TRP A1138 14486 13547 11492 -504 771 -17 C ATOM 2619 CZ2 TRP A1138 26.930 -1.847 2.703 1.00103.83 C ANISOU 2619 CZ2 TRP A1138 14696 13229 11525 -371 676 94 C ATOM 2620 CZ3 TRP A1138 29.172 -2.740 2.938 1.00104.69 C ANISOU 2620 CZ3 TRP A1138 14536 13634 11607 -369 692 14 C ATOM 2621 CH2 TRP A1138 27.815 -2.719 3.293 1.00104.26 C ANISOU 2621 CH2 TRP A1138 14603 13428 11584 -315 649 68 C ATOM 2622 N TYR A1139 31.651 1.957 2.026 1.00110.17 N ANISOU 2622 N TYR A1139 15329 14403 12130 -1104 1012 -209 N ATOM 2623 CA TYR A1139 31.800 2.298 3.440 1.00110.70 C ANISOU 2623 CA TYR A1139 15326 14547 12190 -1153 971 -253 C ATOM 2624 C TYR A1139 32.084 3.790 3.621 1.00116.07 C ANISOU 2624 C TYR A1139 16107 15176 12817 -1383 1069 -316 C ATOM 2625 O TYR A1139 31.705 4.355 4.644 1.00115.73 O ANISOU 2625 O TYR A1139 16108 15093 12771 -1424 1046 -325 O ATOM 2626 CB TYR A1139 32.926 1.461 4.071 1.00112.91 C ANISOU 2626 CB TYR A1139 15351 15092 12457 -1111 923 -320 C ATOM 2627 CG TYR A1139 33.034 1.591 5.576 1.00115.18 C ANISOU 2627 CG TYR A1139 15548 15481 12733 -1117 860 -358 C ATOM 2628 CD1 TYR A1139 32.238 0.823 6.421 1.00116.01 C ANISOU 2628 CD1 TYR A1139 15656 15544 12879 -936 756 -290 C ATOM 2629 CD2 TYR A1139 33.959 2.455 6.156 1.00117.54 C ANISOU 2629 CD2 TYR A1139 15756 15929 12975 -1311 908 -470 C ATOM 2630 CE1 TYR A1139 32.342 0.929 7.807 1.00117.15 C ANISOU 2630 CE1 TYR A1139 15722 15784 13006 -934 698 -323 C ATOM 2631 CE2 TYR A1139 34.069 2.573 7.541 1.00118.84 C ANISOU 2631 CE2 TYR A1139 15832 16201 13121 -1315 846 -512 C ATOM 2632 CZ TYR A1139 33.261 1.804 8.363 1.00125.53 C ANISOU 2632 CZ TYR A1139 16688 16998 14008 -1118 739 -433 C ATOM 2633 OH TYR A1139 33.368 1.909 9.729 1.00127.41 O ANISOU 2633 OH TYR A1139 16845 17343 14222 -1115 678 -471 O ATOM 2634 N ASN A1140 32.763 4.417 2.646 1.00113.84 N ANISOU 2634 N ASN A1140 15871 14893 12490 -1540 1188 -363 N ATOM 2635 CA ASN A1140 33.105 5.838 2.696 1.00114.93 C ANISOU 2635 CA ASN A1140 16134 14967 12566 -1781 1311 -431 C ATOM 2636 C ASN A1140 31.916 6.720 2.291 1.00117.70 C ANISOU 2636 C ASN A1140 16785 15029 12907 -1769 1358 -347 C ATOM 2637 O ASN A1140 31.765 7.809 2.848 1.00117.92 O ANISOU 2637 O ASN A1140 16948 14961 12897 -1903 1418 -376 O ATOM 2638 CB ASN A1140 34.327 6.136 1.821 1.00118.09 C ANISOU 2638 CB ASN A1140 16472 15484 12914 -1962 1434 -521 C ATOM 2639 CG ASN A1140 35.581 5.374 2.210 1.00144.74 C ANISOU 2639 CG ASN A1140 19538 19176 16280 -1977 1397 -620 C ATOM 2640 OD1 ASN A1140 36.257 4.782 1.364 1.00141.74 O ANISOU 2640 OD1 ASN A1140 19048 18912 15893 -1954 1422 -640 O ATOM 2641 ND2 ASN A1140 35.937 5.378 3.491 1.00136.57 N ANISOU 2641 ND2 ASN A1140 18354 18300 15235 -2007 1338 -688 N ATOM 2642 N GLN A1141 31.066 6.248 1.350 1.00112.73 N ANISOU 2642 N GLN A1141 16261 14270 12302 -1602 1329 -246 N ATOM 2643 CA GLN A1141 29.882 6.974 0.877 1.00111.83 C ANISOU 2643 CA GLN A1141 16417 13908 12165 -1544 1360 -161 C ATOM 2644 C GLN A1141 28.806 7.029 1.970 1.00113.34 C ANISOU 2644 C GLN A1141 16654 14023 12388 -1434 1265 -115 C ATOM 2645 O GLN A1141 28.458 8.122 2.421 1.00113.44 O ANISOU 2645 O GLN A1141 16835 13909 12360 -1516 1320 -119 O ATOM 2646 CB GLN A1141 29.321 6.337 -0.405 1.00112.60 C ANISOU 2646 CB GLN A1141 16572 13937 12272 -1388 1342 -82 C ATOM 2647 CG GLN A1141 29.170 7.323 -1.563 1.00130.81 C ANISOU 2647 CG GLN A1141 19126 16075 14502 -1454 1471 -54 C ATOM 2648 CD GLN A1141 30.385 7.415 -2.463 1.00151.50 C ANISOU 2648 CD GLN A1141 21704 18776 17084 -1608 1585 -117 C ATOM 2649 OE1 GLN A1141 31.505 7.013 -2.114 1.00147.89 O ANISOU 2649 OE1 GLN A1141 21033 18514 16644 -1713 1589 -203 O ATOM 2650 NE2 GLN A1141 30.193 7.968 -3.651 1.00143.27 N ANISOU 2650 NE2 GLN A1141 20866 17592 15977 -1618 1683 -76 N ATOM 2651 N THR A1142 28.297 5.856 2.401 1.00107.58 N ANISOU 2651 N THR A1142 15786 13365 11726 -1254 1133 -74 N ATOM 2652 CA THR A1142 27.288 5.742 3.457 1.00105.93 C ANISOU 2652 CA THR A1142 15594 13103 11550 -1144 1040 -33 C ATOM 2653 C THR A1142 27.913 4.959 4.620 1.00108.70 C ANISOU 2653 C THR A1142 15719 13642 11941 -1136 960 -82 C ATOM 2654 O THR A1142 27.781 3.737 4.664 1.00107.17 O ANISOU 2654 O THR A1142 15399 13526 11794 -992 876 -53 O ATOM 2655 CB THR A1142 25.982 5.110 2.938 1.00111.51 C ANISOU 2655 CB THR A1142 16370 13712 12286 -941 969 58 C ATOM 2656 OG1 THR A1142 26.271 3.843 2.346 1.00109.65 O ANISOU 2656 OG1 THR A1142 15992 13579 12090 -851 924 66 O ATOM 2657 CG2 THR A1142 25.240 6.006 1.955 1.00110.54 C ANISOU 2657 CG2 THR A1142 16482 13413 12105 -922 1037 108 C ATOM 2658 N PRO A1143 28.636 5.637 5.544 1.00105.86 N ANISOU 2658 N PRO A1143 15309 13360 11551 -1290 991 -161 N ATOM 2659 CA PRO A1143 29.294 4.912 6.645 1.00105.31 C ANISOU 2659 CA PRO A1143 15017 13493 11501 -1269 913 -212 C ATOM 2660 C PRO A1143 28.320 4.354 7.679 1.00106.52 C ANISOU 2660 C PRO A1143 15162 13612 11698 -1112 802 -155 C ATOM 2661 O PRO A1143 28.501 3.215 8.102 1.00105.23 O ANISOU 2661 O PRO A1143 14847 13571 11565 -987 722 -145 O ATOM 2662 CB PRO A1143 30.218 5.968 7.270 1.00108.71 C ANISOU 2662 CB PRO A1143 15423 14007 11874 -1496 988 -320 C ATOM 2663 CG PRO A1143 30.268 7.099 6.278 1.00114.30 C ANISOU 2663 CG PRO A1143 16332 14564 12534 -1650 1125 -331 C ATOM 2664 CD PRO A1143 28.934 7.080 5.618 1.00108.73 C ANISOU 2664 CD PRO A1143 15821 13640 11852 -1493 1106 -215 C ATOM 2665 N ASN A1144 27.296 5.142 8.074 1.00102.12 N ANISOU 2665 N ASN A1144 14776 12887 11137 -1112 806 -118 N ATOM 2666 CA ASN A1144 26.284 4.766 9.072 1.00100.39 C ANISOU 2666 CA ASN A1144 14566 12623 10953 -982 714 -69 C ATOM 2667 C ASN A1144 25.447 3.555 8.613 1.00100.51 C ANISOU 2667 C ASN A1144 14563 12606 11021 -787 644 9 C ATOM 2668 O ASN A1144 25.146 2.681 9.432 1.00 99.49 O ANISOU 2668 O ASN A1144 14347 12529 10924 -679 565 28 O ATOM 2669 CB ASN A1144 25.367 5.953 9.394 1.00102.35 C ANISOU 2669 CB ASN A1144 15016 12696 11176 -1022 749 -48 C ATOM 2670 CG ASN A1144 26.094 7.150 9.953 1.00128.80 C ANISOU 2670 CG ASN A1144 18411 16056 14471 -1224 827 -130 C ATOM 2671 OD1 ASN A1144 26.296 7.271 11.165 1.00125.82 O ANISOU 2671 OD1 ASN A1144 17961 15755 14088 -1266 792 -173 O ATOM 2672 ND2 ASN A1144 26.504 8.060 9.081 1.00120.60 N ANISOU 2672 ND2 ASN A1144 17500 14940 13383 -1359 943 -156 N ATOM 2673 N ARG A1145 25.099 3.501 7.308 1.00 94.35 N ANISOU 2673 N ARG A1145 13867 11740 10240 -751 681 47 N ATOM 2674 CA ARG A1145 24.316 2.415 6.712 1.00 91.80 C ANISOU 2674 CA ARG A1145 13535 11387 9956 -593 629 105 C ATOM 2675 C ARG A1145 25.171 1.146 6.548 1.00 93.44 C ANISOU 2675 C ARG A1145 13576 11738 10190 -539 603 89 C ATOM 2676 O ARG A1145 24.696 0.060 6.887 1.00 91.93 O ANISOU 2676 O ARG A1145 13334 11561 10035 -413 542 120 O ATOM 2677 CB ARG A1145 23.726 2.855 5.365 1.00 90.24 C ANISOU 2677 CB ARG A1145 13482 11071 9735 -576 679 141 C ATOM 2678 CG ARG A1145 22.748 1.861 4.759 1.00 93.36 C ANISOU 2678 CG ARG A1145 13878 11435 10159 -426 628 189 C ATOM 2679 CD ARG A1145 22.760 1.967 3.254 1.00 97.53 C ANISOU 2679 CD ARG A1145 14477 11921 10657 -419 680 205 C ATOM 2680 NE ARG A1145 22.000 0.898 2.604 1.00 97.50 N ANISOU 2680 NE ARG A1145 14448 11918 10678 -294 636 232 N ATOM 2681 CZ ARG A1145 20.858 1.084 1.953 1.00104.74 C ANISOU 2681 CZ ARG A1145 15466 12761 11568 -215 625 263 C ATOM 2682 NH1 ARG A1145 20.328 2.296 1.864 1.00 87.34 N ANISOU 2682 NH1 ARG A1145 13408 10469 9310 -223 654 282 N ATOM 2683 NH2 ARG A1145 20.238 0.060 1.383 1.00 89.41 N ANISOU 2683 NH2 ARG A1145 13485 10842 9645 -124 590 270 N ATOM 2684 N ALA A1146 26.419 1.285 6.033 1.00 89.75 N ANISOU 2684 N ALA A1146 13031 11374 9697 -633 657 39 N ATOM 2685 CA ALA A1146 27.359 0.177 5.827 1.00 89.40 C ANISOU 2685 CA ALA A1146 12826 11481 9661 -576 641 17 C ATOM 2686 C ALA A1146 27.766 -0.462 7.150 1.00 92.89 C ANISOU 2686 C ALA A1146 13133 12054 10108 -514 575 -3 C ATOM 2687 O ALA A1146 27.898 -1.683 7.208 1.00 92.70 O ANISOU 2687 O ALA A1146 13030 12091 10100 -379 535 18 O ATOM 2688 CB ALA A1146 28.593 0.651 5.081 1.00 91.27 C ANISOU 2688 CB ALA A1146 13006 11815 9859 -707 720 -45 C ATOM 2689 N LYS A1147 27.933 0.351 8.213 1.00 88.84 N ANISOU 2689 N LYS A1147 12607 11575 9571 -604 567 -42 N ATOM 2690 CA LYS A1147 28.280 -0.119 9.557 1.00 88.48 C ANISOU 2690 CA LYS A1147 12443 11659 9516 -546 502 -63 C ATOM 2691 C LYS A1147 27.199 -1.089 10.067 1.00 89.73 C ANISOU 2691 C LYS A1147 12650 11727 9716 -376 435 12 C ATOM 2692 O LYS A1147 27.545 -2.126 10.627 1.00 89.15 O ANISOU 2692 O LYS A1147 12484 11753 9638 -253 391 20 O ATOM 2693 CB LYS A1147 28.455 1.078 10.514 1.00 92.07 C ANISOU 2693 CB LYS A1147 12910 12136 9936 -692 514 -119 C ATOM 2694 CG LYS A1147 29.018 0.742 11.899 1.00110.68 C ANISOU 2694 CG LYS A1147 15125 14665 12263 -654 451 -160 C ATOM 2695 CD LYS A1147 29.111 1.972 12.831 1.00122.92 C ANISOU 2695 CD LYS A1147 16701 16227 13777 -813 468 -222 C ATOM 2696 CE LYS A1147 27.788 2.629 13.196 1.00132.80 C ANISOU 2696 CE LYS A1147 18137 17265 15057 -818 465 -169 C ATOM 2697 NZ LYS A1147 26.889 1.732 13.974 1.00139.19 N ANISOU 2697 NZ LYS A1147 18957 18028 15900 -642 383 -98 N ATOM 2698 N ARG A1148 25.904 -0.771 9.820 1.00 84.56 N ANISOU 2698 N ARG A1148 12146 10891 9093 -365 437 63 N ATOM 2699 CA ARG A1148 24.746 -1.581 10.222 1.00 83.00 C ANISOU 2699 CA ARG A1148 12004 10600 8931 -235 389 121 C ATOM 2700 C ARG A1148 24.674 -2.907 9.463 1.00 86.24 C ANISOU 2700 C ARG A1148 12395 11007 9364 -117 387 153 C ATOM 2701 O ARG A1148 24.385 -3.936 10.076 1.00 85.83 O ANISOU 2701 O ARG A1148 12330 10958 9324 -4 354 179 O ATOM 2702 CB ARG A1148 23.431 -0.810 10.017 1.00 82.05 C ANISOU 2702 CB ARG A1148 12031 10319 8825 -261 397 152 C ATOM 2703 CG ARG A1148 23.159 0.251 11.077 1.00 90.74 C ANISOU 2703 CG ARG A1148 13179 11392 9908 -333 387 135 C ATOM 2704 CD ARG A1148 21.727 0.766 11.035 1.00 93.43 C ANISOU 2704 CD ARG A1148 13656 11587 10257 -305 383 173 C ATOM 2705 NE ARG A1148 21.440 1.525 9.815 1.00 96.78 N ANISOU 2705 NE ARG A1148 14186 11924 10661 -344 435 182 N ATOM 2706 CZ ARG A1148 21.564 2.843 9.698 1.00108.59 C ANISOU 2706 CZ ARG A1148 15782 13359 12116 -443 487 165 C ATOM 2707 NH1 ARG A1148 21.967 3.575 10.728 1.00 94.96 N ANISOU 2707 NH1 ARG A1148 14056 11654 10370 -531 494 129 N ATOM 2708 NH2 ARG A1148 21.283 3.440 8.547 1.00 95.65 N ANISOU 2708 NH2 ARG A1148 14258 11635 10449 -453 539 182 N ATOM 2709 N VAL A1149 24.926 -2.880 8.136 1.00 82.16 N ANISOU 2709 N VAL A1149 11893 10475 8848 -145 432 149 N ATOM 2710 CA VAL A1149 24.878 -4.056 7.255 1.00 81.31 C ANISOU 2710 CA VAL A1149 11779 10356 8757 -49 442 171 C ATOM 2711 C VAL A1149 26.057 -5.010 7.570 1.00 84.86 C ANISOU 2711 C VAL A1149 12104 10951 9188 32 435 154 C ATOM 2712 O VAL A1149 25.828 -6.214 7.696 1.00 84.17 O ANISOU 2712 O VAL A1149 12026 10845 9111 157 423 183 O ATOM 2713 CB VAL A1149 24.825 -3.652 5.750 1.00 85.20 C ANISOU 2713 CB VAL A1149 12328 10798 9247 -104 493 170 C ATOM 2714 CG1 VAL A1149 24.836 -4.873 4.835 1.00 84.88 C ANISOU 2714 CG1 VAL A1149 12278 10754 9220 -12 507 184 C ATOM 2715 CG2 VAL A1149 23.597 -2.793 5.455 1.00 84.50 C ANISOU 2715 CG2 VAL A1149 12370 10576 9160 -141 495 192 C ATOM 2716 N ILE A1150 27.291 -4.472 7.726 1.00 81.69 N ANISOU 2716 N ILE A1150 11591 10697 8749 -37 447 103 N ATOM 2717 CA ILE A1150 28.505 -5.247 8.026 1.00 82.25 C ANISOU 2717 CA ILE A1150 11521 10947 8782 49 437 75 C ATOM 2718 C ILE A1150 28.374 -5.946 9.412 1.00 86.66 C ANISOU 2718 C ILE A1150 12056 11544 9326 176 380 98 C ATOM 2719 O ILE A1150 28.730 -7.126 9.515 1.00 86.49 O ANISOU 2719 O ILE A1150 12004 11572 9285 331 372 118 O ATOM 2720 CB ILE A1150 29.790 -4.364 7.898 1.00 86.25 C ANISOU 2720 CB ILE A1150 11901 11627 9244 -81 466 -3 C ATOM 2721 CG1 ILE A1150 30.097 -4.061 6.411 1.00 86.73 C ANISOU 2721 CG1 ILE A1150 11982 11662 9308 -165 535 -19 C ATOM 2722 CG2 ILE A1150 31.016 -4.997 8.575 1.00 87.86 C ANISOU 2722 CG2 ILE A1150 11929 12063 9390 13 438 -46 C ATOM 2723 CD1 ILE A1150 30.933 -2.790 6.152 1.00 94.97 C ANISOU 2723 CD1 ILE A1150 12976 12794 10315 -364 592 -96 C ATOM 2724 N THR A1151 27.828 -5.244 10.445 1.00 83.37 N ANISOU 2724 N THR A1151 11674 11091 8912 120 347 98 N ATOM 2725 CA THR A1151 27.621 -5.792 11.801 1.00 83.27 C ANISOU 2725 CA THR A1151 11655 11103 8880 229 296 121 C ATOM 2726 C THR A1151 26.602 -6.950 11.746 1.00 86.74 C ANISOU 2726 C THR A1151 12214 11389 9353 357 299 188 C ATOM 2727 O THR A1151 26.785 -7.957 12.435 1.00 86.47 O ANISOU 2727 O THR A1151 12177 11389 9289 504 283 214 O ATOM 2728 CB THR A1151 27.204 -4.681 12.787 1.00 89.55 C ANISOU 2728 CB THR A1151 12471 11880 9674 121 270 101 C ATOM 2729 OG1 THR A1151 28.200 -3.657 12.769 1.00 90.38 O ANISOU 2729 OG1 THR A1151 12474 12124 9741 -17 284 26 O ATOM 2730 CG2 THR A1151 27.047 -5.183 14.221 1.00 87.18 C ANISOU 2730 CG2 THR A1151 12162 11617 9346 229 218 122 C ATOM 2731 N THR A1152 25.565 -6.815 10.891 1.00 83.04 N ANISOU 2731 N THR A1152 11854 10762 8935 301 327 210 N ATOM 2732 CA THR A1152 24.530 -7.828 10.662 1.00 82.54 C ANISOU 2732 CA THR A1152 11901 10558 8901 381 343 254 C ATOM 2733 C THR A1152 25.178 -9.073 10.019 1.00 87.37 C ANISOU 2733 C THR A1152 12500 11202 9497 499 376 264 C ATOM 2734 O THR A1152 24.782 -10.187 10.351 1.00 87.00 O ANISOU 2734 O THR A1152 12526 11085 9444 607 392 296 O ATOM 2735 CB THR A1152 23.381 -7.224 9.833 1.00 89.92 C ANISOU 2735 CB THR A1152 12924 11364 9879 285 360 256 C ATOM 2736 OG1 THR A1152 22.807 -6.147 10.579 1.00 90.36 O ANISOU 2736 OG1 THR A1152 13002 11391 9938 207 332 252 O ATOM 2737 CG2 THR A1152 22.290 -8.239 9.481 1.00 86.11 C ANISOU 2737 CG2 THR A1152 12538 10760 9421 339 383 280 C ATOM 2738 N PHE A1153 26.193 -8.889 9.147 1.00 84.94 N ANISOU 2738 N PHE A1153 12105 10995 9172 478 395 234 N ATOM 2739 CA PHE A1153 26.925 -10.003 8.534 1.00 85.70 C ANISOU 2739 CA PHE A1153 12179 11139 9244 599 428 240 C ATOM 2740 C PHE A1153 27.809 -10.710 9.566 1.00 92.21 C ANISOU 2740 C PHE A1153 12939 12091 10007 755 405 247 C ATOM 2741 O PHE A1153 28.035 -11.916 9.451 1.00 92.45 O ANISOU 2741 O PHE A1153 13013 12105 10009 907 433 273 O ATOM 2742 CB PHE A1153 27.792 -9.525 7.357 1.00 87.72 C ANISOU 2742 CB PHE A1153 12350 11484 9494 528 456 201 C ATOM 2743 CG PHE A1153 27.099 -9.437 6.018 1.00 88.46 C ANISOU 2743 CG PHE A1153 12527 11454 9628 456 496 205 C ATOM 2744 CD1 PHE A1153 26.650 -10.583 5.371 1.00 91.28 C ANISOU 2744 CD1 PHE A1153 12970 11717 9997 540 531 228 C ATOM 2745 CD2 PHE A1153 26.951 -8.217 5.374 1.00 90.15 C ANISOU 2745 CD2 PHE A1153 12742 11654 9857 307 505 183 C ATOM 2746 CE1 PHE A1153 26.029 -10.504 4.122 1.00 91.60 C ANISOU 2746 CE1 PHE A1153 13075 11666 10064 475 563 223 C ATOM 2747 CE2 PHE A1153 26.334 -8.139 4.124 1.00 92.43 C ANISOU 2747 CE2 PHE A1153 13108 11843 10167 260 538 189 C ATOM 2748 CZ PHE A1153 25.879 -9.283 3.505 1.00 90.30 C ANISOU 2748 CZ PHE A1153 12902 11499 9910 344 562 206 C ATOM 2749 N ARG A1154 28.313 -9.954 10.565 1.00 90.10 N ANISOU 2749 N ARG A1154 12573 11953 9706 723 357 220 N ATOM 2750 CA ARG A1154 29.185 -10.461 11.626 1.00 91.34 C ANISOU 2750 CA ARG A1154 12648 12270 9788 873 323 219 C ATOM 2751 C ARG A1154 28.426 -11.270 12.674 1.00 96.31 C ANISOU 2751 C ARG A1154 13402 12788 10404 997 313 277 C ATOM 2752 O ARG A1154 28.876 -12.356 13.038 1.00 96.80 O ANISOU 2752 O ARG A1154 13487 12886 10405 1190 323 307 O ATOM 2753 CB ARG A1154 29.925 -9.312 12.328 1.00 91.51 C ANISOU 2753 CB ARG A1154 12519 12478 9774 773 276 156 C ATOM 2754 CG ARG A1154 31.074 -8.705 11.533 1.00 99.82 C ANISOU 2754 CG ARG A1154 13416 13708 10802 682 294 84 C ATOM 2755 CD ARG A1154 32.226 -8.294 12.435 1.00105.86 C ANISOU 2755 CD ARG A1154 13998 14741 11484 692 250 15 C ATOM 2756 NE ARG A1154 31.856 -7.242 13.385 1.00110.95 N ANISOU 2756 NE ARG A1154 14639 15382 12133 556 216 -13 N ATOM 2757 CZ ARG A1154 32.389 -7.103 14.596 1.00126.31 C ANISOU 2757 CZ ARG A1154 16480 17503 14007 603 163 -49 C ATOM 2758 NH1 ARG A1154 33.316 -7.952 15.021 1.00113.92 N ANISOU 2758 NH1 ARG A1154 14797 16137 12349 798 133 -59 N ATOM 2759 NH2 ARG A1154 31.992 -6.122 15.393 1.00114.10 N ANISOU 2759 NH2 ARG A1154 14948 15936 12469 466 140 -76 N ATOM 2760 N THR A1155 27.301 -10.731 13.180 1.00 93.14 N ANISOU 2760 N THR A1155 13085 12253 10050 895 300 292 N ATOM 2761 CA THR A1155 26.508 -11.343 14.251 1.00 93.56 C ANISOU 2761 CA THR A1155 13256 12201 10091 980 296 339 C ATOM 2762 C THR A1155 25.392 -12.268 13.755 1.00 97.96 C ANISOU 2762 C THR A1155 13985 12545 10690 998 358 379 C ATOM 2763 O THR A1155 25.106 -13.277 14.406 1.00 97.74 O ANISOU 2763 O THR A1155 14068 12441 10627 1123 386 420 O ATOM 2764 CB THR A1155 25.893 -10.257 15.147 1.00103.00 C ANISOU 2764 CB THR A1155 14445 13384 11309 858 252 326 C ATOM 2765 OG1 THR A1155 25.080 -9.384 14.357 1.00102.07 O ANISOU 2765 OG1 THR A1155 14358 13161 11262 688 265 308 O ATOM 2766 CG2 THR A1155 26.941 -9.463 15.921 1.00103.13 C ANISOU 2766 CG2 THR A1155 14306 13610 11267 844 196 280 C ATOM 2767 N GLY A1156 24.748 -11.901 12.651 1.00 94.92 N ANISOU 2767 N GLY A1156 13627 12069 10369 870 383 362 N ATOM 2768 CA GLY A1156 23.627 -12.657 12.107 1.00 94.87 C ANISOU 2768 CA GLY A1156 13762 11885 10399 854 440 378 C ATOM 2769 C GLY A1156 22.354 -12.398 12.886 1.00 99.55 C ANISOU 2769 C GLY A1156 14435 12371 11019 784 433 386 C ATOM 2770 O GLY A1156 21.466 -13.253 12.925 1.00 99.17 O ANISOU 2770 O GLY A1156 14511 12191 10978 796 486 398 O ATOM 2771 N THR A1157 22.269 -11.209 13.526 1.00 96.58 N ANISOU 2771 N THR A1157 13990 12054 10653 703 375 373 N ATOM 2772 CA THR A1157 21.130 -10.758 14.336 1.00 96.05 C ANISOU 2772 CA THR A1157 13978 11909 10607 636 360 376 C ATOM 2773 C THR A1157 20.687 -9.346 13.924 1.00 99.75 C ANISOU 2773 C THR A1157 14399 12388 11114 495 327 346 C ATOM 2774 O THR A1157 21.343 -8.696 13.102 1.00 99.44 O ANISOU 2774 O THR A1157 14291 12413 11080 445 319 325 O ATOM 2775 CB THR A1157 21.471 -10.792 15.842 1.00104.10 C ANISOU 2775 CB THR A1157 14991 12984 11580 713 327 397 C ATOM 2776 OG1 THR A1157 22.667 -10.050 16.079 1.00103.37 O ANISOU 2776 OG1 THR A1157 14765 13055 11454 718 276 377 O ATOM 2777 CG2 THR A1157 21.593 -12.208 16.399 1.00103.56 C ANISOU 2777 CG2 THR A1157 15021 12865 11461 865 372 438 C ATOM 2778 N TRP A1158 19.576 -8.874 14.520 1.00 96.01 N ANISOU 2778 N TRP A1158 13974 11847 10658 438 315 345 N ATOM 2779 CA TRP A1158 19.002 -7.551 14.283 1.00 95.30 C ANISOU 2779 CA TRP A1158 13869 11750 10592 331 289 323 C ATOM 2780 C TRP A1158 19.497 -6.535 15.340 1.00100.20 C ANISOU 2780 C TRP A1158 14440 12440 11190 301 243 317 C ATOM 2781 O TRP A1158 18.876 -5.483 15.517 1.00 99.55 O ANISOU 2781 O TRP A1158 14377 12330 11118 227 227 305 O ATOM 2782 CB TRP A1158 17.465 -7.638 14.277 1.00 93.23 C ANISOU 2782 CB TRP A1158 13681 11390 10352 297 304 317 C ATOM 2783 CG TRP A1158 16.904 -8.520 13.199 1.00 93.89 C ANISOU 2783 CG TRP A1158 13805 11420 10451 299 351 304 C ATOM 2784 CD1 TRP A1158 16.355 -9.758 13.356 1.00 96.94 C ANISOU 2784 CD1 TRP A1158 14258 11740 10834 330 400 303 C ATOM 2785 CD2 TRP A1158 16.866 -8.239 11.792 1.00 93.48 C ANISOU 2785 CD2 TRP A1158 13736 11373 10410 261 360 284 C ATOM 2786 NE1 TRP A1158 15.951 -10.256 12.139 1.00 96.24 N ANISOU 2786 NE1 TRP A1158 14189 11623 10757 303 438 276 N ATOM 2787 CE2 TRP A1158 16.262 -9.349 11.159 1.00 97.38 C ANISOU 2787 CE2 TRP A1158 14277 11815 10909 270 409 267 C ATOM 2788 CE3 TRP A1158 17.287 -7.156 11.001 1.00 94.54 C ANISOU 2788 CE3 TRP A1158 13833 11546 10542 218 340 278 C ATOM 2789 CZ2 TRP A1158 16.075 -9.409 9.772 1.00 96.55 C ANISOU 2789 CZ2 TRP A1158 14167 11710 10807 243 427 242 C ATOM 2790 CZ3 TRP A1158 17.092 -7.214 9.629 1.00 95.85 C ANISOU 2790 CZ3 TRP A1158 14005 11703 10711 200 362 262 C ATOM 2791 CH2 TRP A1158 16.491 -8.329 9.029 1.00 96.46 C ANISOU 2791 CH2 TRP A1158 14115 11743 10793 216 399 243 C ATOM 2792 N ASP A1159 20.638 -6.843 16.009 1.00 97.85 N ANISOU 2792 N ASP A1159 14079 12245 10854 364 225 320 N ATOM 2793 CA ASP A1159 21.283 -6.020 17.042 1.00 98.27 C ANISOU 2793 CA ASP A1159 14068 12397 10872 337 183 301 C ATOM 2794 C ASP A1159 21.622 -4.605 16.546 1.00102.13 C ANISOU 2794 C ASP A1159 14515 12922 11367 205 178 260 C ATOM 2795 O ASP A1159 21.581 -3.664 17.340 1.00102.07 O ANISOU 2795 O ASP A1159 14503 12935 11344 140 156 239 O ATOM 2796 CB ASP A1159 22.568 -6.701 17.554 1.00101.32 C ANISOU 2796 CB ASP A1159 14371 12924 11203 443 166 301 C ATOM 2797 CG ASP A1159 22.364 -7.730 18.654 1.00113.37 C ANISOU 2797 CG ASP A1159 15951 14433 12692 577 161 341 C ATOM 2798 OD1 ASP A1159 21.745 -7.385 19.686 1.00113.73 O ANISOU 2798 OD1 ASP A1159 16036 14445 12732 559 141 347 O ATOM 2799 OD2 ASP A1159 22.899 -8.854 18.522 1.00120.37 O ANISOU 2799 OD2 ASP A1159 16846 15344 13546 708 182 365 O ATOM 2800 N ALA A1160 21.955 -4.456 15.245 1.00 98.28 N ANISOU 2800 N ALA A1160 14013 12433 10895 163 208 248 N ATOM 2801 CA ALA A1160 22.299 -3.169 14.634 1.00 98.00 C ANISOU 2801 CA ALA A1160 13968 12412 10857 35 224 212 C ATOM 2802 C ALA A1160 21.067 -2.286 14.412 1.00100.77 C ANISOU 2802 C ALA A1160 14427 12631 11229 -24 234 222 C ATOM 2803 O ALA A1160 21.181 -1.061 14.467 1.00100.31 O ANISOU 2803 O ALA A1160 14396 12564 11155 -122 246 197 O ATOM 2804 CB ALA A1160 23.015 -3.395 13.315 1.00 99.02 C ANISOU 2804 CB ALA A1160 14058 12576 10989 23 259 200 C ATOM 2805 N TYR A1161 19.898 -2.904 14.165 1.00 96.92 N ANISOU 2805 N TYR A1161 14006 12051 10771 36 235 253 N ATOM 2806 CA TYR A1161 18.635 -2.204 13.907 1.00 96.41 C ANISOU 2806 CA TYR A1161 14029 11886 10715 12 240 260 C ATOM 2807 C TYR A1161 17.757 -2.131 15.178 1.00101.49 C ANISOU 2807 C TYR A1161 14706 12497 11359 34 213 268 C ATOM 2808 O TYR A1161 16.532 -1.994 15.080 1.00101.19 O ANISOU 2808 O TYR A1161 14725 12393 11328 50 213 273 O ATOM 2809 CB TYR A1161 17.888 -2.879 12.738 1.00 96.82 C ANISOU 2809 CB TYR A1161 14112 11887 10786 52 260 271 C ATOM 2810 CG TYR A1161 18.631 -2.764 11.423 1.00 98.30 C ANISOU 2810 CG TYR A1161 14285 12097 10970 25 289 263 C ATOM 2811 CD1 TYR A1161 19.604 -3.693 11.064 1.00100.48 C ANISOU 2811 CD1 TYR A1161 14495 12433 11250 56 302 262 C ATOM 2812 CD2 TYR A1161 18.382 -1.710 10.550 1.00 98.90 C ANISOU 2812 CD2 TYR A1161 14421 12131 11027 -21 310 260 C ATOM 2813 CE1 TYR A1161 20.319 -3.569 9.875 1.00101.16 C ANISOU 2813 CE1 TYR A1161 14562 12546 11330 27 333 252 C ATOM 2814 CE2 TYR A1161 19.082 -1.584 9.351 1.00 99.96 C ANISOU 2814 CE2 TYR A1161 14550 12281 11150 -51 345 254 C ATOM 2815 CZ TYR A1161 20.051 -2.516 9.018 1.00106.92 C ANISOU 2815 CZ TYR A1161 15352 13230 12043 -33 355 247 C ATOM 2816 OH TYR A1161 20.749 -2.397 7.841 1.00108.38 O ANISOU 2816 OH TYR A1161 15528 13436 12217 -65 393 239 O ATOM 2817 N LYS A 263 18.403 -2.176 16.367 1.00 98.61 N ANISOU 2817 N LYS A 263 14297 12194 10977 37 189 262 N ATOM 2818 CA LYS A 263 17.775 -2.102 17.690 1.00 98.10 C ANISOU 2818 CA LYS A 263 14258 12112 10904 56 165 268 C ATOM 2819 C LYS A 263 17.219 -0.698 17.953 1.00101.63 C ANISOU 2819 C LYS A 263 14765 12510 11339 -12 164 253 C ATOM 2820 O LYS A 263 17.990 0.266 18.034 1.00101.46 O ANISOU 2820 O LYS A 263 14736 12520 11293 -90 170 226 O ATOM 2821 CB LYS A 263 18.789 -2.478 18.786 1.00100.94 C ANISOU 2821 CB LYS A 263 14548 12570 11233 84 138 263 C ATOM 2822 CG LYS A 263 18.591 -3.855 19.391 1.00110.51 C ANISOU 2822 CG LYS A 263 15767 13781 12443 193 136 295 C ATOM 2823 CD LYS A 263 19.618 -4.099 20.484 1.00118.83 C ANISOU 2823 CD LYS A 263 16756 14948 13445 243 104 291 C ATOM 2824 CE LYS A 263 19.409 -5.414 21.187 1.00128.67 C ANISOU 2824 CE LYS A 263 18041 16175 14673 366 111 331 C ATOM 2825 NZ LYS A 263 20.418 -5.629 22.256 1.00138.17 N ANISOU 2825 NZ LYS A 263 19182 17506 15809 441 75 329 N ATOM 2826 N PHE A 264 15.875 -0.598 18.085 1.00 97.55 N ANISOU 2826 N PHE A 264 14312 11920 10832 16 163 264 N ATOM 2827 CA PHE A 264 15.100 0.625 18.352 1.00 97.28 C ANISOU 2827 CA PHE A 264 14352 11830 10779 -12 165 255 C ATOM 2828 C PHE A 264 15.403 1.738 17.320 1.00101.46 C ANISOU 2828 C PHE A 264 14938 12325 11288 -65 196 246 C ATOM 2829 O PHE A 264 15.590 2.902 17.689 1.00101.45 O ANISOU 2829 O PHE A 264 14996 12293 11256 -122 211 231 O ATOM 2830 CB PHE A 264 15.325 1.140 19.795 1.00 99.27 C ANISOU 2830 CB PHE A 264 14607 12101 11009 -41 145 243 C ATOM 2831 CG PHE A 264 15.262 0.099 20.890 1.00100.48 C ANISOU 2831 CG PHE A 264 14716 12293 11167 12 120 255 C ATOM 2832 CD1 PHE A 264 14.045 -0.447 21.285 1.00102.81 C ANISOU 2832 CD1 PHE A 264 15042 12545 11475 64 121 269 C ATOM 2833 CD2 PHE A 264 16.413 -0.301 21.558 1.00102.78 C ANISOU 2833 CD2 PHE A 264 14940 12671 11439 12 101 249 C ATOM 2834 CE1 PHE A 264 13.987 -1.400 22.303 1.00103.57 C ANISOU 2834 CE1 PHE A 264 15124 12660 11567 109 113 283 C ATOM 2835 CE2 PHE A 264 16.352 -1.248 22.581 1.00105.54 C ANISOU 2835 CE2 PHE A 264 15272 13048 11779 81 84 268 C ATOM 2836 CZ PHE A 264 15.139 -1.791 22.946 1.00103.16 C ANISOU 2836 CZ PHE A 264 15024 12678 11492 125 95 288 C ATOM 2837 N CYS A 265 15.454 1.363 16.028 1.00 97.63 N ANISOU 2837 N CYS A 265 14446 11836 10814 -47 214 255 N ATOM 2838 CA CYS A 265 15.700 2.293 14.923 1.00 97.48 C ANISOU 2838 CA CYS A 265 14494 11776 10769 -85 251 252 C ATOM 2839 C CYS A 265 14.373 2.732 14.329 1.00 99.93 C ANISOU 2839 C CYS A 265 14887 12025 11056 -15 255 266 C ATOM 2840 O CYS A 265 14.186 3.920 14.061 1.00 99.98 O ANISOU 2840 O CYS A 265 15002 11970 11018 -24 284 269 O ATOM 2841 CB CYS A 265 16.603 1.664 13.867 1.00 98.05 C ANISOU 2841 CB CYS A 265 14509 11891 10855 -101 269 251 C ATOM 2842 SG CYS A 265 18.340 1.531 14.359 1.00102.68 S ANISOU 2842 SG CYS A 265 14997 12576 11440 -186 275 222 S ATOM 2843 N LEU A 266 13.446 1.770 14.141 1.00 95.10 N ANISOU 2843 N LEU A 266 14230 11438 10465 58 232 269 N ATOM 2844 CA LEU A 266 12.099 1.989 13.612 1.00 94.37 C ANISOU 2844 CA LEU A 266 14179 11334 10343 136 226 268 C ATOM 2845 C LEU A 266 11.305 2.891 14.565 1.00 97.30 C ANISOU 2845 C LEU A 266 14612 11673 10683 165 216 267 C ATOM 2846 O LEU A 266 11.486 2.793 15.782 1.00 97.05 O ANISOU 2846 O LEU A 266 14559 11645 10672 131 203 262 O ATOM 2847 CB LEU A 266 11.398 0.628 13.433 1.00 93.95 C ANISOU 2847 CB LEU A 266 14043 11334 10320 172 209 252 C ATOM 2848 CG LEU A 266 10.325 0.522 12.349 1.00 98.40 C ANISOU 2848 CG LEU A 266 14607 11930 10851 238 207 234 C ATOM 2849 CD1 LEU A 266 10.940 0.294 10.974 1.00 98.49 C ANISOU 2849 CD1 LEU A 266 14618 11947 10859 232 226 240 C ATOM 2850 CD2 LEU A 266 9.389 -0.620 12.645 1.00100.42 C ANISOU 2850 CD2 LEU A 266 14789 12239 11126 248 199 199 C ATOM 2851 N LYS A 267 10.460 3.787 14.013 1.00 92.89 N ANISOU 2851 N LYS A 267 14138 11088 10067 238 225 271 N ATOM 2852 CA LYS A 267 9.641 4.737 14.780 1.00 92.30 C ANISOU 2852 CA LYS A 267 14140 10982 9950 289 222 271 C ATOM 2853 C LYS A 267 8.677 4.024 15.738 1.00 94.32 C ANISOU 2853 C LYS A 267 14313 11297 10228 319 188 249 C ATOM 2854 O LYS A 267 8.448 4.511 16.845 1.00 94.09 O ANISOU 2854 O LYS A 267 14314 11244 10191 315 184 246 O ATOM 2855 CB LYS A 267 8.853 5.655 13.835 1.00 95.47 C ANISOU 2855 CB LYS A 267 14643 11360 10270 399 237 283 C ATOM 2856 N GLU A 268 8.145 2.863 15.320 1.00 89.55 N ANISOU 2856 N GLU A 268 13609 10766 9648 336 173 227 N ATOM 2857 CA GLU A 268 7.217 2.041 16.101 1.00 88.77 C ANISOU 2857 CA GLU A 268 13434 10727 9568 344 157 195 C ATOM 2858 C GLU A 268 7.940 1.334 17.251 1.00 91.70 C ANISOU 2858 C GLU A 268 13772 11076 9993 267 159 204 C ATOM 2859 O GLU A 268 7.319 1.045 18.274 1.00 91.41 O ANISOU 2859 O GLU A 268 13714 11055 9961 266 155 189 O ATOM 2860 CB GLU A 268 6.520 1.009 15.199 1.00 90.19 C ANISOU 2860 CB GLU A 268 13531 10988 9750 361 157 158 C ATOM 2861 CG GLU A 268 5.550 1.607 14.185 1.00102.75 C ANISOU 2861 CG GLU A 268 15130 12641 11269 461 146 137 C ATOM 2862 CD GLU A 268 6.118 2.227 12.918 1.00124.08 C ANISOU 2862 CD GLU A 268 17897 15311 13936 499 153 167 C ATOM 2863 OE1 GLU A 268 7.311 2.001 12.613 1.00117.01 O ANISOU 2863 OE1 GLU A 268 17019 14357 13081 428 170 195 O ATOM 2864 OE2 GLU A 268 5.358 2.938 12.221 1.00118.02 O ANISOU 2864 OE2 GLU A 268 17165 14585 13091 607 144 161 O ATOM 2865 N HIS A 269 9.247 1.055 17.075 1.00 87.55 N ANISOU 2865 N HIS A 269 13242 10524 9498 211 166 226 N ATOM 2866 CA HIS A 269 10.110 0.395 18.058 1.00 86.85 C ANISOU 2866 CA HIS A 269 13121 10433 9445 161 163 238 C ATOM 2867 C HIS A 269 10.611 1.387 19.108 1.00 90.39 C ANISOU 2867 C HIS A 269 13614 10853 9876 132 154 246 C ATOM 2868 O HIS A 269 10.806 0.997 20.262 1.00 90.12 O ANISOU 2868 O HIS A 269 13559 10830 9851 117 144 247 O ATOM 2869 CB HIS A 269 11.293 -0.292 17.357 1.00 87.63 C ANISOU 2869 CB HIS A 269 13185 10543 9570 132 173 250 C ATOM 2870 CG HIS A 269 10.922 -1.540 16.610 1.00 90.97 C ANISOU 2870 CG HIS A 269 13566 10987 10014 149 189 238 C ATOM 2871 ND1 HIS A 269 11.866 -2.506 16.317 1.00 92.81 N ANISOU 2871 ND1 HIS A 269 13766 11227 10270 138 202 250 N ATOM 2872 CD2 HIS A 269 9.721 -1.945 16.127 1.00 92.61 C ANISOU 2872 CD2 HIS A 269 13760 11215 10213 172 198 209 C ATOM 2873 CE1 HIS A 269 11.216 -3.457 15.665 1.00 92.15 C ANISOU 2873 CE1 HIS A 269 13667 11149 10195 149 225 229 C ATOM 2874 NE2 HIS A 269 9.923 -3.165 15.530 1.00 92.39 N ANISOU 2874 NE2 HIS A 269 13701 11196 10207 160 222 199 N ATOM 2875 N LYS A 270 10.806 2.670 18.710 1.00 86.47 N ANISOU 2875 N LYS A 270 13192 10316 9345 123 165 249 N ATOM 2876 CA LYS A 270 11.233 3.765 19.589 1.00 86.11 C ANISOU 2876 CA LYS A 270 13211 10233 9274 79 170 245 C ATOM 2877 C LYS A 270 10.132 4.091 20.599 1.00 89.68 C ANISOU 2877 C LYS A 270 13693 10674 9707 124 159 237 C ATOM 2878 O LYS A 270 10.437 4.506 21.719 1.00 89.52 O ANISOU 2878 O LYS A 270 13694 10644 9678 86 154 230 O ATOM 2879 CB LYS A 270 11.600 5.017 18.781 1.00 88.78 C ANISOU 2879 CB LYS A 270 13653 10509 9571 55 207 247 C ATOM 2880 CG LYS A 270 12.932 4.913 18.060 1.00100.02 C ANISOU 2880 CG LYS A 270 15051 11946 11007 -23 228 245 C ATOM 2881 CD LYS A 270 13.349 6.243 17.453 1.00109.00 C ANISOU 2881 CD LYS A 270 16315 13006 12095 -72 282 241 C ATOM 2882 CE LYS A 270 14.584 6.124 16.592 1.00120.05 C ANISOU 2882 CE LYS A 270 17685 14426 13502 -155 312 233 C ATOM 2883 NZ LYS A 270 15.813 5.886 17.396 1.00129.52 N ANISOU 2883 NZ LYS A 270 18795 15700 14719 -259 305 200 N ATOM 2884 N ALA A 271 8.853 3.889 20.198 1.00 85.74 N ANISOU 2884 N ALA A 271 13187 10194 9196 205 155 232 N ATOM 2885 CA ALA A 271 7.662 4.081 21.031 1.00 85.39 C ANISOU 2885 CA ALA A 271 13151 10164 9131 259 146 216 C ATOM 2886 C ALA A 271 7.594 3.011 22.124 1.00 88.95 C ANISOU 2886 C ALA A 271 13531 10651 9617 227 136 209 C ATOM 2887 O ALA A 271 7.071 3.276 23.208 1.00 88.69 O ANISOU 2887 O ALA A 271 13514 10615 9568 237 132 200 O ATOM 2888 CB ALA A 271 6.409 4.032 20.170 1.00 86.19 C ANISOU 2888 CB ALA A 271 13234 10312 9201 349 145 199 C ATOM 2889 N LEU A 272 8.130 1.806 21.835 1.00 85.09 N ANISOU 2889 N LEU A 272 12976 10186 9167 195 137 215 N ATOM 2890 CA LEU A 272 8.177 0.686 22.773 1.00 84.57 C ANISOU 2890 CA LEU A 272 12870 10138 9125 175 140 216 C ATOM 2891 C LEU A 272 9.280 0.899 23.804 1.00 88.78 C ANISOU 2891 C LEU A 272 13416 10661 9655 140 125 234 C ATOM 2892 O LEU A 272 9.126 0.478 24.950 1.00 89.09 O ANISOU 2892 O LEU A 272 13454 10706 9689 142 123 237 O ATOM 2893 CB LEU A 272 8.371 -0.656 22.048 1.00 84.40 C ANISOU 2893 CB LEU A 272 12801 10133 9134 167 159 217 C ATOM 2894 CG LEU A 272 7.216 -1.140 21.157 1.00 89.14 C ANISOU 2894 CG LEU A 272 13370 10767 9733 184 179 182 C ATOM 2895 CD1 LEU A 272 7.660 -2.290 20.282 1.00 89.20 C ANISOU 2895 CD1 LEU A 272 13348 10776 9766 164 202 181 C ATOM 2896 CD2 LEU A 272 5.991 -1.552 21.982 1.00 91.80 C ANISOU 2896 CD2 LEU A 272 13694 11130 10058 182 199 147 C ATOM 2897 N LYS A 273 10.383 1.562 23.407 1.00 84.75 N ANISOU 2897 N LYS A 273 12917 10146 9140 105 117 240 N ATOM 2898 CA LYS A 273 11.499 1.876 24.301 1.00 84.55 C ANISOU 2898 CA LYS A 273 12884 10141 9099 60 101 240 C ATOM 2899 C LYS A 273 11.088 2.988 25.274 1.00 88.96 C ANISOU 2899 C LYS A 273 13505 10671 9624 45 98 224 C ATOM 2900 O LYS A 273 11.460 2.928 26.445 1.00 88.81 O ANISOU 2900 O LYS A 273 13475 10680 9589 29 81 219 O ATOM 2901 CB LYS A 273 12.741 2.282 23.495 1.00 86.94 C ANISOU 2901 CB LYS A 273 13171 10461 9400 7 105 234 C ATOM 2902 CG LYS A 273 14.020 2.351 24.317 1.00 98.68 C ANISOU 2902 CG LYS A 273 14613 12014 10865 -43 86 219 C ATOM 2903 CD LYS A 273 15.150 2.947 23.505 1.00109.85 C ANISOU 2903 CD LYS A 273 16012 13455 12271 -118 102 196 C ATOM 2904 CE LYS A 273 16.456 2.954 24.257 1.00122.76 C ANISOU 2904 CE LYS A 273 17572 15196 13875 -170 82 164 C ATOM 2905 NZ LYS A 273 17.563 3.482 23.418 1.00133.12 N ANISOU 2905 NZ LYS A 273 18855 16549 15175 -260 107 130 N ATOM 2906 N THR A 274 10.303 3.983 24.790 1.00 85.61 N ANISOU 2906 N THR A 274 13152 10194 9182 63 115 216 N ATOM 2907 CA THR A 274 9.796 5.121 25.571 1.00 85.43 C ANISOU 2907 CA THR A 274 13212 10128 9120 63 122 202 C ATOM 2908 C THR A 274 8.904 4.607 26.717 1.00 88.69 C ANISOU 2908 C THR A 274 13603 10564 9533 104 110 199 C ATOM 2909 O THR A 274 9.107 5.012 27.861 1.00 88.90 O ANISOU 2909 O THR A 274 13653 10588 9535 76 103 189 O ATOM 2910 CB THR A 274 9.067 6.124 24.653 1.00 92.23 C ANISOU 2910 CB THR A 274 14163 10930 9950 112 149 202 C ATOM 2911 OG1 THR A 274 9.960 6.549 23.622 1.00 91.39 O ANISOU 2911 OG1 THR A 274 14090 10794 9840 66 171 206 O ATOM 2912 CG2 THR A 274 8.553 7.344 25.402 1.00 91.78 C ANISOU 2912 CG2 THR A 274 14215 10815 9844 128 167 189 C ATOM 2913 N LEU A 275 7.960 3.689 26.416 1.00 84.15 N ANISOU 2913 N LEU A 275 12980 10015 8978 156 113 203 N ATOM 2914 CA LEU A 275 7.068 3.085 27.411 1.00 83.58 C ANISOU 2914 CA LEU A 275 12887 9966 8903 179 116 195 C ATOM 2915 C LEU A 275 7.856 2.225 28.403 1.00 87.20 C ANISOU 2915 C LEU A 275 13319 10444 9371 149 107 210 C ATOM 2916 O LEU A 275 7.475 2.137 29.570 1.00 86.86 O ANISOU 2916 O LEU A 275 13290 10405 9308 154 108 207 O ATOM 2917 CB LEU A 275 5.967 2.240 26.744 1.00 83.44 C ANISOU 2917 CB LEU A 275 12819 9983 8900 215 135 180 C ATOM 2918 CG LEU A 275 4.911 2.969 25.904 1.00 88.15 C ANISOU 2918 CG LEU A 275 13426 10599 9470 277 139 156 C ATOM 2919 CD1 LEU A 275 4.073 1.978 25.135 1.00 88.24 C ANISOU 2919 CD1 LEU A 275 13361 10672 9493 289 155 128 C ATOM 2920 CD2 LEU A 275 4.000 3.842 26.766 1.00 90.41 C ANISOU 2920 CD2 LEU A 275 13752 10886 9713 323 141 138 C ATOM 2921 N GLY A 276 8.944 1.616 27.924 1.00 83.79 N ANISOU 2921 N GLY A 276 12850 10029 8957 129 98 228 N ATOM 2922 CA GLY A 276 9.848 0.790 28.718 1.00 83.68 C ANISOU 2922 CA GLY A 276 12810 10049 8935 128 86 246 C ATOM 2923 C GLY A 276 10.638 1.587 29.741 1.00 87.66 C ANISOU 2923 C GLY A 276 13325 10580 9401 98 58 235 C ATOM 2924 O GLY A 276 10.939 1.069 30.821 1.00 87.46 O ANISOU 2924 O GLY A 276 13293 10589 9349 118 45 245 O ATOM 2925 N ILE A 277 10.973 2.863 29.410 1.00 83.95 N ANISOU 2925 N ILE A 277 12882 10095 8919 47 53 210 N ATOM 2926 CA ILE A 277 11.702 3.790 30.294 1.00 84.10 C ANISOU 2926 CA ILE A 277 12919 10139 8896 -10 37 181 C ATOM 2927 C ILE A 277 10.757 4.232 31.448 1.00 88.24 C ANISOU 2927 C ILE A 277 13501 10633 9395 8 41 173 C ATOM 2928 O ILE A 277 11.196 4.306 32.598 1.00 88.00 O ANISOU 2928 O ILE A 277 13464 10645 9326 -8 21 160 O ATOM 2929 CB ILE A 277 12.317 4.996 29.503 1.00 87.17 C ANISOU 2929 CB ILE A 277 13345 10501 9276 -89 55 151 C ATOM 2930 CG1 ILE A 277 13.439 4.513 28.553 1.00 87.29 C ANISOU 2930 CG1 ILE A 277 13287 10571 9308 -118 51 152 C ATOM 2931 CG2 ILE A 277 12.868 6.080 30.451 1.00 88.51 C ANISOU 2931 CG2 ILE A 277 13554 10682 9394 -171 56 105 C ATOM 2932 CD1 ILE A 277 13.657 5.345 27.313 1.00 92.58 C ANISOU 2932 CD1 ILE A 277 14005 11187 9984 -171 87 140 C ATOM 2933 N ILE A 278 9.463 4.476 31.131 1.00 84.54 N ANISOU 2933 N ILE A 278 13078 10106 8939 50 65 177 N ATOM 2934 CA ILE A 278 8.400 4.873 32.067 1.00 84.45 C ANISOU 2934 CA ILE A 278 13115 10070 8903 80 75 167 C ATOM 2935 C ILE A 278 8.212 3.767 33.139 1.00 88.37 C ANISOU 2935 C ILE A 278 13577 10605 9394 106 68 183 C ATOM 2936 O ILE A 278 8.168 4.072 34.335 1.00 88.35 O ANISOU 2936 O ILE A 278 13603 10612 9356 101 61 172 O ATOM 2937 CB ILE A 278 7.089 5.179 31.267 1.00 87.42 C ANISOU 2937 CB ILE A 278 13518 10410 9289 138 100 164 C ATOM 2938 CG1 ILE A 278 7.211 6.472 30.412 1.00 88.32 C ANISOU 2938 CG1 ILE A 278 13708 10467 9382 134 115 154 C ATOM 2939 CG2 ILE A 278 5.833 5.202 32.147 1.00 88.13 C ANISOU 2939 CG2 ILE A 278 13624 10504 9358 185 113 151 C ATOM 2940 CD1 ILE A 278 7.068 7.830 31.174 1.00 99.66 C ANISOU 2940 CD1 ILE A 278 15253 11847 10767 124 132 130 C ATOM 2941 N MET A 279 8.142 2.495 32.698 1.00 84.51 N ANISOU 2941 N MET A 279 13042 10132 8935 133 78 207 N ATOM 2942 CA MET A 279 7.991 1.309 33.551 1.00 84.23 C ANISOU 2942 CA MET A 279 13002 10113 8888 162 92 229 C ATOM 2943 C MET A 279 9.251 1.059 34.399 1.00 88.11 C ANISOU 2943 C MET A 279 13482 10656 9341 167 58 243 C ATOM 2944 O MET A 279 9.142 0.623 35.548 1.00 87.65 O ANISOU 2944 O MET A 279 13449 10609 9244 195 61 256 O ATOM 2945 CB MET A 279 7.688 0.065 32.690 1.00 86.20 C ANISOU 2945 CB MET A 279 13228 10351 9173 179 125 245 C ATOM 2946 CG MET A 279 6.327 0.095 32.043 1.00 89.46 C ANISOU 2946 CG MET A 279 13634 10747 9608 177 160 218 C ATOM 2947 SD MET A 279 6.135 -1.175 30.780 1.00 93.34 S ANISOU 2947 SD MET A 279 14091 11234 10138 171 198 220 S ATOM 2948 CE MET A 279 4.615 -0.663 30.057 1.00 89.98 C ANISOU 2948 CE MET A 279 13634 10834 9718 170 218 168 C ATOM 2949 N GLY A 280 10.420 1.323 33.810 1.00 84.62 N ANISOU 2949 N GLY A 280 12997 10254 8900 143 28 238 N ATOM 2950 CA GLY A 280 11.723 1.139 34.438 1.00 84.90 C ANISOU 2950 CA GLY A 280 12992 10377 8890 152 -10 238 C ATOM 2951 C GLY A 280 12.002 2.126 35.549 1.00 89.27 C ANISOU 2951 C GLY A 280 13559 10970 9391 111 -37 202 C ATOM 2952 O GLY A 280 12.455 1.728 36.628 1.00 89.30 O ANISOU 2952 O GLY A 280 13551 11040 9338 150 -61 207 O ATOM 2953 N THR A 281 11.728 3.423 35.284 1.00 85.77 N ANISOU 2953 N THR A 281 13150 10483 8956 39 -28 163 N ATOM 2954 CA THR A 281 11.914 4.532 36.227 1.00 85.90 C ANISOU 2954 CA THR A 281 13200 10515 8923 -20 -39 117 C ATOM 2955 C THR A 281 11.005 4.330 37.447 1.00 89.39 C ANISOU 2955 C THR A 281 13690 10936 9338 29 -33 130 C ATOM 2956 O THR A 281 11.481 4.452 38.575 1.00 89.68 O ANISOU 2956 O THR A 281 13721 11039 9316 22 -59 111 O ATOM 2957 CB THR A 281 11.658 5.885 35.530 1.00 92.84 C ANISOU 2957 CB THR A 281 14144 11315 9816 -93 -8 82 C ATOM 2958 OG1 THR A 281 12.458 5.966 34.348 1.00 91.93 O ANISOU 2958 OG1 THR A 281 13991 11213 9724 -138 -4 75 O ATOM 2959 CG2 THR A 281 11.952 7.082 36.431 1.00 91.92 C ANISOU 2959 CG2 THR A 281 14080 11203 9643 -173 -6 26 C ATOM 2960 N PHE A 282 9.716 3.992 37.213 1.00 85.05 N ANISOU 2960 N PHE A 282 13178 10311 8825 74 2 156 N ATOM 2961 CA PHE A 282 8.712 3.747 38.255 1.00 84.66 C ANISOU 2961 CA PHE A 282 13173 10240 8754 114 22 165 C ATOM 2962 C PHE A 282 9.160 2.627 39.212 1.00 88.64 C ANISOU 2962 C PHE A 282 13663 10799 9216 164 9 196 C ATOM 2963 O PHE A 282 8.922 2.721 40.418 1.00 88.73 O ANISOU 2963 O PHE A 282 13711 10825 9179 179 8 192 O ATOM 2964 CB PHE A 282 7.352 3.401 37.622 1.00 85.77 C ANISOU 2964 CB PHE A 282 13328 10321 8939 145 66 177 C ATOM 2965 CG PHE A 282 6.224 3.226 38.611 1.00 87.25 C ANISOU 2965 CG PHE A 282 13553 10494 9103 172 97 173 C ATOM 2966 CD1 PHE A 282 5.445 4.308 39.000 1.00 90.53 C ANISOU 2966 CD1 PHE A 282 14012 10885 9501 170 108 141 C ATOM 2967 CD2 PHE A 282 5.929 1.975 39.141 1.00 89.24 C ANISOU 2967 CD2 PHE A 282 13809 10751 9346 200 126 201 C ATOM 2968 CE1 PHE A 282 4.400 4.145 39.912 1.00 91.59 C ANISOU 2968 CE1 PHE A 282 14171 11016 9611 193 140 133 C ATOM 2969 CE2 PHE A 282 4.896 1.817 40.066 1.00 92.30 C ANISOU 2969 CE2 PHE A 282 14235 11127 9709 211 166 193 C ATOM 2970 CZ PHE A 282 4.129 2.899 40.434 1.00 90.58 C ANISOU 2970 CZ PHE A 282 14038 10901 9477 206 170 157 C ATOM 2971 N THR A 283 9.798 1.580 38.665 1.00 84.77 N ANISOU 2971 N THR A 283 13134 10337 8738 202 5 230 N ATOM 2972 CA THR A 283 10.324 0.443 39.413 1.00 84.88 C ANISOU 2972 CA THR A 283 13152 10397 8701 278 -1 269 C ATOM 2973 C THR A 283 11.513 0.910 40.260 1.00 89.59 C ANISOU 2973 C THR A 283 13709 11109 9224 280 -61 244 C ATOM 2974 O THR A 283 11.554 0.616 41.448 1.00 89.73 O ANISOU 2974 O THR A 283 13758 11163 9173 331 -70 256 O ATOM 2975 CB THR A 283 10.697 -0.687 38.440 1.00 92.13 C ANISOU 2975 CB THR A 283 14050 11306 9650 323 17 307 C ATOM 2976 OG1 THR A 283 9.540 -1.050 37.686 1.00 92.13 O ANISOU 2976 OG1 THR A 283 14079 11214 9711 302 74 313 O ATOM 2977 CG2 THR A 283 11.256 -1.914 39.143 1.00 90.78 C ANISOU 2977 CG2 THR A 283 13910 11169 9414 426 22 355 C ATOM 2978 N LEU A 284 12.449 1.667 39.651 1.00 86.50 N ANISOU 2978 N LEU A 284 13249 10779 8838 218 -98 202 N ATOM 2979 CA LEU A 284 13.661 2.210 40.279 1.00 87.28 C ANISOU 2979 CA LEU A 284 13283 11015 8865 190 -152 154 C ATOM 2980 C LEU A 284 13.355 3.137 41.465 1.00 91.16 C ANISOU 2980 C LEU A 284 13816 11516 9306 142 -161 111 C ATOM 2981 O LEU A 284 14.129 3.170 42.424 1.00 91.91 O ANISOU 2981 O LEU A 284 13871 11735 9315 159 -205 83 O ATOM 2982 CB LEU A 284 14.474 2.992 39.221 1.00 87.56 C ANISOU 2982 CB LEU A 284 13252 11087 8930 91 -163 104 C ATOM 2983 CG LEU A 284 15.997 2.757 39.106 1.00 93.45 C ANISOU 2983 CG LEU A 284 13880 12003 9623 96 -211 72 C ATOM 2984 CD1 LEU A 284 16.775 3.410 40.246 1.00 94.81 C ANISOU 2984 CD1 LEU A 284 14003 12322 9700 51 -255 1 C ATOM 2985 CD2 LEU A 284 16.353 1.280 38.881 1.00 96.12 C ANISOU 2985 CD2 LEU A 284 14187 12384 9950 238 -220 138 C ATOM 2986 N CYS A 285 12.236 3.885 41.392 1.00 86.42 N ANISOU 2986 N CYS A 285 13292 10796 8748 92 -121 101 N ATOM 2987 CA CYS A 285 11.815 4.857 42.398 1.00 86.06 C ANISOU 2987 CA CYS A 285 13303 10734 8661 45 -118 59 C ATOM 2988 C CYS A 285 11.060 4.217 43.571 1.00 89.12 C ANISOU 2988 C CYS A 285 13743 11108 9010 126 -107 95 C ATOM 2989 O CYS A 285 11.323 4.592 44.714 1.00 89.28 O ANISOU 2989 O CYS A 285 13773 11191 8956 118 -131 65 O ATOM 2990 CB CYS A 285 10.981 5.961 41.753 1.00 85.81 C ANISOU 2990 CB CYS A 285 13339 10583 8681 -22 -75 34 C ATOM 2991 SG CYS A 285 11.901 7.008 40.595 1.00 89.80 S ANISOU 2991 SG CYS A 285 13826 11087 9207 -138 -71 -20 S ATOM 2992 N TRP A 286 10.127 3.280 43.302 1.00 85.01 N ANISOU 2992 N TRP A 286 13258 10510 8532 191 -65 153 N ATOM 2993 CA TRP A 286 9.287 2.669 44.339 1.00 85.20 C ANISOU 2993 CA TRP A 286 13347 10504 8521 250 -34 184 C ATOM 2994 C TRP A 286 9.827 1.359 44.960 1.00 89.75 C ANISOU 2994 C TRP A 286 13933 11134 9035 351 -40 237 C ATOM 2995 O TRP A 286 9.434 1.047 46.087 1.00 90.01 O ANISOU 2995 O TRP A 286 14026 11164 9008 395 -23 254 O ATOM 2996 CB TRP A 286 7.871 2.430 43.807 1.00 83.31 C ANISOU 2996 CB TRP A 286 13149 10157 8348 248 32 201 C ATOM 2997 CG TRP A 286 7.082 3.694 43.643 1.00 84.05 C ANISOU 2997 CG TRP A 286 13266 10203 8469 194 46 155 C ATOM 2998 CD1 TRP A 286 6.797 4.336 42.475 1.00 86.49 C ANISOU 2998 CD1 TRP A 286 13560 10468 8835 161 54 136 C ATOM 2999 CD2 TRP A 286 6.515 4.495 44.691 1.00 84.28 C ANISOU 2999 CD2 TRP A 286 13347 10221 8454 182 54 124 C ATOM 3000 NE1 TRP A 286 6.060 5.471 42.725 1.00 86.04 N ANISOU 3000 NE1 TRP A 286 13553 10370 8770 142 71 99 N ATOM 3001 CE2 TRP A 286 5.869 5.591 44.078 1.00 87.95 C ANISOU 3001 CE2 TRP A 286 13834 10629 8953 150 72 89 C ATOM 3002 CE3 TRP A 286 6.473 4.383 46.093 1.00 86.13 C ANISOU 3002 CE3 TRP A 286 13621 10487 8618 204 52 123 C ATOM 3003 CZ2 TRP A 286 5.182 6.564 44.816 1.00 87.61 C ANISOU 3003 CZ2 TRP A 286 13853 10558 8878 144 90 53 C ATOM 3004 CZ3 TRP A 286 5.804 5.356 46.823 1.00 87.78 C ANISOU 3004 CZ3 TRP A 286 13882 10671 8799 183 67 85 C ATOM 3005 CH2 TRP A 286 5.182 6.438 46.188 1.00 88.11 C ANISOU 3005 CH2 TRP A 286 13946 10653 8878 154 87 49 C ATOM 3006 N LEU A 287 10.707 0.607 44.257 1.00 86.12 N ANISOU 3006 N LEU A 287 13424 10718 8580 397 -59 265 N ATOM 3007 CA LEU A 287 11.290 -0.650 44.761 1.00 86.40 C ANISOU 3007 CA LEU A 287 13483 10801 8543 520 -61 321 C ATOM 3008 C LEU A 287 12.081 -0.475 46.081 1.00 90.51 C ANISOU 3008 C LEU A 287 13993 11452 8944 578 -118 307 C ATOM 3009 O LEU A 287 11.882 -1.317 46.959 1.00 90.34 O ANISOU 3009 O LEU A 287 14053 11419 8851 679 -92 357 O ATOM 3010 CB LEU A 287 12.206 -1.320 43.723 1.00 86.57 C ANISOU 3010 CB LEU A 287 13446 10865 8584 566 -78 343 C ATOM 3011 CG LEU A 287 11.997 -2.802 43.377 1.00 91.67 C ANISOU 3011 CG LEU A 287 14166 11434 9230 663 -18 415 C ATOM 3012 CD1 LEU A 287 13.330 -3.479 43.145 1.00 92.77 C ANISOU 3012 CD1 LEU A 287 14255 11683 9312 774 -60 440 C ATOM 3013 CD2 LEU A 287 11.194 -3.562 44.443 1.00 94.60 C ANISOU 3013 CD2 LEU A 287 14669 11728 9545 724 47 460 C ATOM 3014 N PRO A 288 12.959 0.560 46.275 1.00 87.41 N ANISOU 3014 N PRO A 288 13508 11186 8518 517 -187 237 N ATOM 3015 CA PRO A 288 13.680 0.670 47.558 1.00 88.43 C ANISOU 3015 CA PRO A 288 13616 11461 8521 573 -242 214 C ATOM 3016 C PRO A 288 12.752 0.863 48.758 1.00 92.77 C ANISOU 3016 C PRO A 288 14267 11952 9031 578 -213 221 C ATOM 3017 O PRO A 288 13.081 0.408 49.853 1.00 93.46 O ANISOU 3017 O PRO A 288 14382 12122 9007 679 -235 240 O ATOM 3018 CB PRO A 288 14.572 1.903 47.363 1.00 90.47 C ANISOU 3018 CB PRO A 288 13761 11843 8770 452 -300 115 C ATOM 3019 CG PRO A 288 14.684 2.075 45.903 1.00 94.15 C ANISOU 3019 CG PRO A 288 14182 12252 9338 380 -283 108 C ATOM 3020 CD PRO A 288 13.355 1.660 45.370 1.00 88.63 C ANISOU 3020 CD PRO A 288 13582 11360 8733 388 -210 169 C ATOM 3021 N PHE A 289 11.593 1.516 48.546 1.00 88.65 N ANISOU 3021 N PHE A 289 13798 11293 8590 481 -162 205 N ATOM 3022 CA PHE A 289 10.596 1.764 49.584 1.00 88.51 C ANISOU 3022 CA PHE A 289 13871 11213 8546 475 -124 205 C ATOM 3023 C PHE A 289 9.866 0.471 49.968 1.00 92.98 C ANISOU 3023 C PHE A 289 14540 11696 9093 574 -57 285 C ATOM 3024 O PHE A 289 9.740 0.192 51.160 1.00 93.07 O ANISOU 3024 O PHE A 289 14618 11730 9014 636 -50 304 O ATOM 3025 CB PHE A 289 9.594 2.850 49.137 1.00 89.30 C ANISOU 3025 CB PHE A 289 13991 11208 8733 360 -88 161 C ATOM 3026 CG PHE A 289 8.417 3.061 50.064 1.00 90.56 C ANISOU 3026 CG PHE A 289 14237 11296 8875 358 -39 161 C ATOM 3027 CD1 PHE A 289 8.577 3.708 51.285 1.00 94.13 C ANISOU 3027 CD1 PHE A 289 14714 11808 9243 348 -65 122 C ATOM 3028 CD2 PHE A 289 7.145 2.627 49.710 1.00 91.74 C ANISOU 3028 CD2 PHE A 289 14438 11332 9087 359 37 191 C ATOM 3029 CE1 PHE A 289 7.491 3.895 52.144 1.00 94.90 C ANISOU 3029 CE1 PHE A 289 14893 11844 9323 349 -16 122 C ATOM 3030 CE2 PHE A 289 6.060 2.814 50.571 1.00 94.56 C ANISOU 3030 CE2 PHE A 289 14864 11641 9423 355 87 183 C ATOM 3031 CZ PHE A 289 6.239 3.450 51.780 1.00 93.25 C ANISOU 3031 CZ PHE A 289 14728 11526 9177 354 60 153 C ATOM 3032 N PHE A 290 9.388 -0.307 48.972 1.00 89.55 N ANISOU 3032 N PHE A 290 14125 11163 8735 579 -1 327 N ATOM 3033 CA PHE A 290 8.644 -1.548 49.200 1.00 89.77 C ANISOU 3033 CA PHE A 290 14266 11093 8750 642 86 392 C ATOM 3034 C PHE A 290 9.522 -2.688 49.727 1.00 96.62 C ANISOU 3034 C PHE A 290 15189 12011 9512 790 80 456 C ATOM 3035 O PHE A 290 8.998 -3.561 50.424 1.00 97.18 O ANISOU 3035 O PHE A 290 15389 12010 9526 853 153 507 O ATOM 3036 CB PHE A 290 7.902 -1.994 47.934 1.00 90.35 C ANISOU 3036 CB PHE A 290 14339 11059 8932 587 151 401 C ATOM 3037 CG PHE A 290 6.593 -1.271 47.728 1.00 90.78 C ANISOU 3037 CG PHE A 290 14388 11045 9058 484 195 355 C ATOM 3038 CD1 PHE A 290 5.436 -1.691 48.375 1.00 93.51 C ANISOU 3038 CD1 PHE A 290 14820 11322 9388 471 281 362 C ATOM 3039 CD2 PHE A 290 6.516 -0.165 46.890 1.00 91.99 C ANISOU 3039 CD2 PHE A 290 14458 11210 9285 409 156 304 C ATOM 3040 CE1 PHE A 290 4.228 -1.014 48.191 1.00 93.64 C ANISOU 3040 CE1 PHE A 290 14814 11305 9460 391 317 312 C ATOM 3041 CE2 PHE A 290 5.306 0.510 46.705 1.00 94.10 C ANISOU 3041 CE2 PHE A 290 14724 11428 9602 345 194 264 C ATOM 3042 CZ PHE A 290 4.171 0.077 47.353 1.00 92.15 C ANISOU 3042 CZ PHE A 290 14540 11136 9338 340 270 266 C ATOM 3043 N ILE A 291 10.839 -2.689 49.408 1.00 94.47 N ANISOU 3043 N ILE A 291 14827 11864 9203 852 0 452 N ATOM 3044 CA ILE A 291 11.772 -3.713 49.895 1.00 95.77 C ANISOU 3044 CA ILE A 291 15034 12106 9250 1025 -18 510 C ATOM 3045 C ILE A 291 11.997 -3.475 51.398 1.00101.35 C ANISOU 3045 C ILE A 291 15776 12909 9825 1095 -55 506 C ATOM 3046 O ILE A 291 11.797 -4.398 52.185 1.00101.92 O ANISOU 3046 O ILE A 291 15984 12935 9804 1216 -2 572 O ATOM 3047 CB ILE A 291 13.095 -3.774 49.066 1.00 99.11 C ANISOU 3047 CB ILE A 291 15330 12660 9667 1075 -93 498 C ATOM 3048 CG1 ILE A 291 12.866 -4.562 47.755 1.00 98.86 C ANISOU 3048 CG1 ILE A 291 15324 12510 9728 1069 -32 536 C ATOM 3049 CG2 ILE A 291 14.262 -4.389 49.874 1.00101.40 C ANISOU 3049 CG2 ILE A 291 15617 13114 9798 1267 -150 529 C ATOM 3050 CD1 ILE A 291 14.028 -4.540 46.729 1.00107.76 C ANISOU 3050 CD1 ILE A 291 16320 13749 10876 1092 -95 517 C ATOM 3051 N VAL A 292 12.335 -2.228 51.789 1.00 98.75 N ANISOU 3051 N VAL A 292 15340 12696 9484 1011 -132 425 N ATOM 3052 CA VAL A 292 12.558 -1.810 53.180 1.00100.32 C ANISOU 3052 CA VAL A 292 15551 13004 9562 1052 -176 400 C ATOM 3053 C VAL A 292 11.256 -2.011 54.014 1.00106.37 C ANISOU 3053 C VAL A 292 16470 13624 10322 1039 -88 435 C ATOM 3054 O VAL A 292 11.333 -2.351 55.200 1.00106.61 O ANISOU 3054 O VAL A 292 16580 13700 10228 1142 -87 463 O ATOM 3055 CB VAL A 292 13.102 -0.354 53.205 1.00103.85 C ANISOU 3055 CB VAL A 292 15857 13581 10019 919 -259 290 C ATOM 3056 CG1 VAL A 292 12.696 0.415 54.460 1.00103.87 C ANISOU 3056 CG1 VAL A 292 15897 13611 9956 876 -269 246 C ATOM 3057 CG2 VAL A 292 14.616 -0.346 53.028 1.00104.62 C ANISOU 3057 CG2 VAL A 292 15813 13897 10040 978 -354 251 C ATOM 3058 N ASN A 293 10.081 -1.869 53.359 1.00103.63 N ANISOU 3058 N ASN A 293 16160 13114 10101 923 -9 432 N ATOM 3059 CA ASN A 293 8.751 -2.066 53.939 1.00104.00 C ANISOU 3059 CA ASN A 293 16329 13027 10159 887 87 452 C ATOM 3060 C ASN A 293 8.541 -3.534 54.370 1.00110.04 C ANISOU 3060 C ASN A 293 17253 13709 10848 1010 176 542 C ATOM 3061 O ASN A 293 7.925 -3.774 55.408 1.00109.90 O ANISOU 3061 O ASN A 293 17351 13645 10760 1035 234 564 O ATOM 3062 CB ASN A 293 7.675 -1.640 52.932 1.00103.94 C ANISOU 3062 CB ASN A 293 16292 12902 10297 748 143 419 C ATOM 3063 CG ASN A 293 6.258 -1.731 53.438 1.00126.29 C ANISOU 3063 CG ASN A 293 19216 15625 13145 694 241 418 C ATOM 3064 OD1 ASN A 293 5.825 -0.957 54.302 1.00119.11 O ANISOU 3064 OD1 ASN A 293 18317 14735 12204 660 234 381 O ATOM 3065 ND2 ASN A 293 5.498 -2.668 52.885 1.00117.66 N ANISOU 3065 ND2 ASN A 293 18187 14420 12098 676 341 451 N ATOM 3066 N ILE A 294 9.061 -4.500 53.581 1.00108.31 N ANISOU 3066 N ILE A 294 17054 13464 10636 1087 194 593 N ATOM 3067 CA ILE A 294 8.967 -5.948 53.835 1.00109.71 C ANISOU 3067 CA ILE A 294 17406 13543 10736 1210 291 682 C ATOM 3068 C ILE A 294 10.029 -6.375 54.886 1.00117.24 C ANISOU 3068 C ILE A 294 18414 14619 11512 1412 235 731 C ATOM 3069 O ILE A 294 9.753 -7.264 55.697 1.00117.76 O ANISOU 3069 O ILE A 294 18663 14607 11473 1517 318 798 O ATOM 3070 CB ILE A 294 9.084 -6.733 52.486 1.00112.17 C ANISOU 3070 CB ILE A 294 17719 13773 11128 1206 335 709 C ATOM 3071 CG1 ILE A 294 7.821 -6.539 51.591 1.00111.28 C ANISOU 3071 CG1 ILE A 294 17588 13532 11163 1023 415 666 C ATOM 3072 CG2 ILE A 294 9.433 -8.221 52.658 1.00113.97 C ANISOU 3072 CG2 ILE A 294 18127 13923 11252 1372 416 802 C ATOM 3073 CD1 ILE A 294 6.429 -7.110 52.128 1.00118.75 C ANISOU 3073 CD1 ILE A 294 18688 14328 12103 952 563 676 C ATOM 3074 N VAL A 295 11.216 -5.722 54.884 1.00116.01 N ANISOU 3074 N VAL A 295 18101 14662 11316 1462 100 690 N ATOM 3075 CA VAL A 295 12.323 -5.976 55.819 1.00118.42 C ANISOU 3075 CA VAL A 295 18407 15142 11444 1656 22 714 C ATOM 3076 C VAL A 295 11.905 -5.549 57.248 1.00125.79 C ANISOU 3076 C VAL A 295 19408 16107 12282 1662 21 702 C ATOM 3077 O VAL A 295 12.262 -6.228 58.210 1.00126.50 O ANISOU 3077 O VAL A 295 19614 16242 12210 1844 28 761 O ATOM 3078 CB VAL A 295 13.643 -5.289 55.355 1.00122.45 C ANISOU 3078 CB VAL A 295 18698 15881 11945 1667 -118 646 C ATOM 3079 CG1 VAL A 295 14.763 -5.454 56.383 1.00124.09 C ANISOU 3079 CG1 VAL A 295 18877 16315 11956 1864 -208 651 C ATOM 3080 CG2 VAL A 295 14.098 -5.833 54.004 1.00121.74 C ANISOU 3080 CG2 VAL A 295 18559 15764 11934 1685 -110 667 C ATOM 3081 N HIS A 296 11.110 -4.461 57.368 1.00124.24 N ANISOU 3081 N HIS A 296 19154 15875 12177 1476 21 629 N ATOM 3082 CA HIS A 296 10.583 -3.923 58.632 1.00125.82 C ANISOU 3082 CA HIS A 296 19409 16090 12307 1452 27 606 C ATOM 3083 C HIS A 296 9.629 -4.920 59.327 1.00131.52 C ANISOU 3083 C HIS A 296 20357 16643 12972 1512 163 688 C ATOM 3084 O HIS A 296 9.523 -4.903 60.556 1.00132.15 O ANISOU 3084 O HIS A 296 20522 16758 12930 1580 168 702 O ATOM 3085 CB HIS A 296 9.869 -2.581 58.381 1.00125.88 C ANISOU 3085 CB HIS A 296 19317 16069 12442 1240 14 513 C ATOM 3086 CG HIS A 296 9.346 -1.923 59.622 1.00130.14 C ANISOU 3086 CG HIS A 296 19902 16628 12916 1206 17 479 C ATOM 3087 ND1 HIS A 296 10.183 -1.229 60.480 1.00133.02 N ANISOU 3087 ND1 HIS A 296 20193 17180 13170 1241 -86 424 N ATOM 3088 CD2 HIS A 296 8.086 -1.885 60.115 1.00131.89 C ANISOU 3088 CD2 HIS A 296 20232 16715 13165 1139 113 486 C ATOM 3089 CE1 HIS A 296 9.408 -0.792 61.460 1.00132.70 C ANISOU 3089 CE1 HIS A 296 20227 17098 13094 1199 -49 406 C ATOM 3090 NE2 HIS A 296 8.138 -1.161 61.282 1.00132.37 N ANISOU 3090 NE2 HIS A 296 20294 16867 13134 1139 70 443 N ATOM 3091 N VAL A 297 8.951 -5.781 58.542 1.00128.41 N ANISOU 3091 N VAL A 297 20062 16069 12660 1479 278 737 N ATOM 3092 CA VAL A 297 8.023 -6.806 59.035 1.00129.25 C ANISOU 3092 CA VAL A 297 20392 15996 12719 1504 433 806 C ATOM 3093 C VAL A 297 8.826 -7.950 59.696 1.00135.01 C ANISOU 3093 C VAL A 297 21287 16744 13267 1747 452 904 C ATOM 3094 O VAL A 297 8.424 -8.452 60.750 1.00135.41 O ANISOU 3094 O VAL A 297 21520 16728 13200 1820 533 954 O ATOM 3095 CB VAL A 297 7.092 -7.330 57.904 1.00132.51 C ANISOU 3095 CB VAL A 297 20843 16230 13274 1370 552 807 C ATOM 3096 CG1 VAL A 297 6.092 -8.350 58.435 1.00133.19 C ANISOU 3096 CG1 VAL A 297 21162 16135 13310 1361 729 859 C ATOM 3097 CG2 VAL A 297 6.360 -6.185 57.207 1.00130.79 C ANISOU 3097 CG2 VAL A 297 20457 16019 13219 1167 522 713 C ATOM 3098 N ILE A 298 9.962 -8.341 59.074 1.00132.41 N ANISOU 3098 N ILE A 298 20896 16507 12906 1880 380 931 N ATOM 3099 CA ILE A 298 10.862 -9.399 59.550 1.00134.25 C ANISOU 3099 CA ILE A 298 21268 16782 12959 2145 384 1023 C ATOM 3100 C ILE A 298 11.558 -8.931 60.851 1.00140.77 C ANISOU 3100 C ILE A 298 22059 17813 13614 2287 277 1013 C ATOM 3101 O ILE A 298 11.456 -9.621 61.867 1.00141.83 O ANISOU 3101 O ILE A 298 22396 17902 13591 2440 342 1087 O ATOM 3102 CB ILE A 298 11.887 -9.828 58.447 1.00137.23 C ANISOU 3102 CB ILE A 298 21555 17228 13358 2244 327 1039 C ATOM 3103 CG1 ILE A 298 11.228 -10.026 57.039 1.00136.00 C ANISOU 3103 CG1 ILE A 298 21379 16902 13392 2067 407 1022 C ATOM 3104 CG2 ILE A 298 12.699 -11.061 58.870 1.00139.96 C ANISOU 3104 CG2 ILE A 298 22079 17588 13511 2542 355 1145 C ATOM 3105 CD1 ILE A 298 10.149 -11.174 56.863 1.00142.67 C ANISOU 3105 CD1 ILE A 298 22479 17471 14258 2023 608 1086 C ATOM 3106 N GLN A 299 12.239 -7.760 60.819 1.00138.13 N ANISOU 3106 N GLN A 299 21478 17699 13304 2226 121 917 N ATOM 3107 CA GLN A 299 12.923 -7.153 61.970 1.00139.61 C ANISOU 3107 CA GLN A 299 21591 18114 13340 2322 7 878 C ATOM 3108 C GLN A 299 12.584 -5.664 62.038 1.00143.37 C ANISOU 3108 C GLN A 299 21890 18660 13925 2090 -62 757 C ATOM 3109 O GLN A 299 12.844 -4.917 61.092 1.00142.00 O ANISOU 3109 O GLN A 299 21534 18538 13881 1947 -123 682 O ATOM 3110 CB GLN A 299 14.440 -7.376 61.912 1.00142.32 C ANISOU 3110 CB GLN A 299 21813 18711 13550 2531 -119 877 C ATOM 3111 CG GLN A 299 15.057 -7.583 63.292 1.00161.54 C ANISOU 3111 CG GLN A 299 24306 21326 15744 2758 -178 902 C ATOM 3112 CD GLN A 299 16.554 -7.799 63.272 1.00183.89 C ANISOU 3112 CD GLN A 299 26998 24448 18425 2981 -308 890 C ATOM 3113 OE1 GLN A 299 17.136 -8.311 62.305 1.00179.69 O ANISOU 3113 OE1 GLN A 299 26416 23933 17927 3054 -317 914 O ATOM 3114 NE2 GLN A 299 17.210 -7.449 64.368 1.00177.44 N ANISOU 3114 NE2 GLN A 299 26113 23880 17425 3106 -410 851 N ATOM 3115 N ASP A 300 11.990 -5.248 63.160 1.00141.01 N ANISOU 3115 N ASP A 300 21663 18350 13565 2057 -42 742 N ATOM 3116 CA ASP A 300 11.475 -3.900 63.400 1.00140.34 C ANISOU 3116 CA ASP A 300 21467 18291 13565 1849 -78 637 C ATOM 3117 C ASP A 300 12.546 -2.825 63.690 1.00144.98 C ANISOU 3117 C ASP A 300 21846 19148 14092 1827 -233 529 C ATOM 3118 O ASP A 300 12.337 -1.667 63.318 1.00143.36 O ANISOU 3118 O ASP A 300 21516 18951 14002 1627 -266 432 O ATOM 3119 CB ASP A 300 10.472 -3.933 64.574 1.00142.84 C ANISOU 3119 CB ASP A 300 21950 18502 13819 1839 9 663 C ATOM 3120 CG ASP A 300 9.423 -5.046 64.542 1.00153.68 C ANISOU 3120 CG ASP A 300 23551 19629 15213 1859 178 761 C ATOM 3121 OD1 ASP A 300 9.246 -5.674 63.471 1.00153.63 O ANISOU 3121 OD1 ASP A 300 23566 19499 15307 1832 240 797 O ATOM 3122 OD2 ASP A 300 8.769 -5.274 65.582 1.00159.92 O ANISOU 3122 OD2 ASP A 300 24498 20350 15916 1888 255 793 O ATOM 3123 N ASN A 301 13.655 -3.186 64.368 1.00143.60 N ANISOU 3123 N ASN A 301 21641 19192 13728 2027 -320 539 N ATOM 3124 CA ASN A 301 14.701 -2.242 64.797 1.00144.34 C ANISOU 3124 CA ASN A 301 21536 19575 13731 2009 -463 423 C ATOM 3125 C ASN A 301 15.634 -1.738 63.674 1.00146.81 C ANISOU 3125 C ASN A 301 21627 20028 14125 1920 -548 340 C ATOM 3126 O ASN A 301 16.173 -0.635 63.801 1.00146.75 O ANISOU 3126 O ASN A 301 21452 20197 14110 1789 -634 213 O ATOM 3127 CB ASN A 301 15.556 -2.854 65.929 1.00148.87 C ANISOU 3127 CB ASN A 301 22144 20366 14054 2272 -529 457 C ATOM 3128 CG ASN A 301 16.536 -3.945 65.531 1.00176.99 C ANISOU 3128 CG ASN A 301 25698 24038 17510 2520 -562 529 C ATOM 3129 OD1 ASN A 301 16.293 -4.761 64.632 1.00172.45 O ANISOU 3129 OD1 ASN A 301 25210 23287 17024 2558 -484 614 O ATOM 3130 ND2 ASN A 301 17.668 -3.993 66.219 1.00170.07 N ANISOU 3130 ND2 ASN A 301 24720 23468 16431 2703 -678 493 N ATOM 3131 N LEU A 302 15.842 -2.541 62.613 1.00141.81 N ANISOU 3131 N LEU A 302 21000 19320 13560 1987 -518 406 N ATOM 3132 CA LEU A 302 16.754 -2.245 61.502 1.00140.85 C ANISOU 3132 CA LEU A 302 20683 19326 13506 1929 -588 343 C ATOM 3133 C LEU A 302 16.441 -0.942 60.734 1.00142.17 C ANISOU 3133 C LEU A 302 20728 19438 13851 1638 -592 234 C ATOM 3134 O LEU A 302 17.380 -0.275 60.290 1.00142.25 O ANISOU 3134 O LEU A 302 20548 19637 13862 1557 -675 133 O ATOM 3135 CB LEU A 302 16.769 -3.416 60.515 1.00140.50 C ANISOU 3135 CB LEU A 302 20716 19152 13517 2047 -527 449 C ATOM 3136 N ILE A 303 15.148 -0.582 60.573 1.00135.97 N ANISOU 3136 N ILE A 303 20053 18405 13205 1488 -500 250 N ATOM 3137 CA ILE A 303 14.740 0.607 59.810 1.00133.62 C ANISOU 3137 CA ILE A 303 19674 18026 13068 1242 -489 163 C ATOM 3138 C ILE A 303 14.309 1.760 60.740 1.00136.24 C ANISOU 3138 C ILE A 303 20014 18374 13375 1111 -498 77 C ATOM 3139 O ILE A 303 13.439 1.586 61.600 1.00135.97 O ANISOU 3139 O ILE A 303 20118 18238 13308 1146 -443 121 O ATOM 3140 CB ILE A 303 13.628 0.245 58.773 1.00134.79 C ANISOU 3140 CB ILE A 303 19918 17904 13392 1172 -383 231 C ATOM 3141 CG1 ILE A 303 14.168 -0.718 57.697 1.00134.87 C ANISOU 3141 CG1 ILE A 303 19900 17906 13439 1267 -379 293 C ATOM 3142 CG2 ILE A 303 13.010 1.487 58.111 1.00133.85 C ANISOU 3142 CG2 ILE A 303 19752 17682 13423 947 -362 153 C ATOM 3143 CD1 ILE A 303 13.726 -2.125 57.844 1.00140.80 C ANISOU 3143 CD1 ILE A 303 20817 18529 14150 1434 -299 417 C ATOM 3144 N ARG A 304 14.922 2.943 60.527 1.00131.47 N ANISOU 3144 N ARG A 304 19271 17894 12787 951 -558 -50 N ATOM 3145 CA ARG A 304 14.642 4.185 61.248 1.00130.73 C ANISOU 3145 CA ARG A 304 19179 17818 12676 799 -564 -152 C ATOM 3146 C ARG A 304 13.569 4.988 60.510 1.00131.40 C ANISOU 3146 C ARG A 304 19326 17667 12933 625 -483 -166 C ATOM 3147 O ARG A 304 13.395 4.806 59.302 1.00130.10 O ANISOU 3147 O ARG A 304 19145 17392 12894 590 -450 -132 O ATOM 3148 CB ARG A 304 15.925 5.015 61.398 1.00132.04 C ANISOU 3148 CB ARG A 304 19172 18246 12752 708 -657 -292 C ATOM 3149 N LYS A 305 12.860 5.881 61.233 1.00126.41 N ANISOU 3149 N LYS A 305 18766 16967 12297 529 -451 -217 N ATOM 3150 CA LYS A 305 11.794 6.725 60.683 1.00124.34 C ANISOU 3150 CA LYS A 305 18575 16497 12173 391 -375 -234 C ATOM 3151 C LYS A 305 12.311 7.634 59.550 1.00126.24 C ANISOU 3151 C LYS A 305 18731 16734 12502 235 -384 -314 C ATOM 3152 O LYS A 305 11.677 7.687 58.497 1.00124.65 O ANISOU 3152 O LYS A 305 18559 16371 12432 196 -330 -277 O ATOM 3153 CB LYS A 305 11.134 7.567 61.788 1.00127.38 C ANISOU 3153 CB LYS A 305 19046 16847 12507 333 -348 -287 C ATOM 3154 CG LYS A 305 9.781 8.149 61.387 1.00142.35 C ANISOU 3154 CG LYS A 305 21044 18519 14526 259 -257 -275 C ATOM 3155 CD LYS A 305 9.237 9.114 62.429 1.00153.91 C ANISOU 3155 CD LYS A 305 22587 19957 15935 195 -231 -342 C ATOM 3156 CE LYS A 305 7.941 9.745 61.984 1.00163.79 C ANISOU 3156 CE LYS A 305 23929 21006 17297 141 -144 -335 C ATOM 3157 NZ LYS A 305 7.405 10.679 63.007 1.00173.19 N ANISOU 3157 NZ LYS A 305 25206 22169 18429 92 -115 -399 N ATOM 3158 N GLU A 306 13.470 8.306 59.751 1.00122.60 N ANISOU 3158 N GLU A 306 18164 16461 11959 145 -449 -427 N ATOM 3159 CA GLU A 306 14.098 9.221 58.779 1.00121.62 C ANISOU 3159 CA GLU A 306 17965 16350 11894 -25 -449 -519 C ATOM 3160 C GLU A 306 14.470 8.528 57.449 1.00122.40 C ANISOU 3160 C GLU A 306 17992 16433 12084 14 -454 -460 C ATOM 3161 O GLU A 306 14.496 9.195 56.412 1.00121.42 O ANISOU 3161 O GLU A 306 17860 16220 12053 -112 -420 -497 O ATOM 3162 CB GLU A 306 15.338 9.935 59.367 1.00124.71 C ANISOU 3162 CB GLU A 306 18244 16983 12158 -135 -513 -664 C ATOM 3163 CG GLU A 306 16.300 9.060 60.165 1.00137.29 C ANISOU 3163 CG GLU A 306 19721 18845 13597 9 -607 -663 C ATOM 3164 CD GLU A 306 16.058 8.963 61.663 1.00158.81 C ANISOU 3164 CD GLU A 306 22501 21650 16190 94 -632 -667 C ATOM 3165 OE1 GLU A 306 15.180 9.688 62.186 1.00153.65 O ANISOU 3165 OE1 GLU A 306 21969 20852 15558 17 -577 -687 O ATOM 3166 OE2 GLU A 306 16.763 8.163 62.318 1.00152.48 O ANISOU 3166 OE2 GLU A 306 21623 21060 15252 249 -707 -650 O ATOM 3167 N VAL A 307 14.734 7.204 57.479 1.00117.18 N ANISOU 3167 N VAL A 307 17293 15844 11387 193 -489 -368 N ATOM 3168 CA VAL A 307 15.081 6.405 56.295 1.00115.39 C ANISOU 3168 CA VAL A 307 17007 15604 11234 253 -492 -305 C ATOM 3169 C VAL A 307 13.799 6.081 55.503 1.00115.59 C ANISOU 3169 C VAL A 307 17145 15371 11404 268 -408 -209 C ATOM 3170 O VAL A 307 13.827 6.080 54.271 1.00114.04 O ANISOU 3170 O VAL A 307 16918 15101 11311 222 -387 -196 O ATOM 3171 CB VAL A 307 15.871 5.114 56.656 1.00120.03 C ANISOU 3171 CB VAL A 307 17530 16363 11713 453 -553 -244 C ATOM 3172 CG1 VAL A 307 16.544 4.516 55.424 1.00119.38 C ANISOU 3172 CG1 VAL A 307 17356 16316 11687 488 -568 -215 C ATOM 3173 CG2 VAL A 307 16.908 5.379 57.745 1.00121.67 C ANISOU 3173 CG2 VAL A 307 17638 16844 11747 474 -638 -335 C ATOM 3174 N TYR A 308 12.683 5.821 56.217 1.00110.65 N ANISOU 3174 N TYR A 308 16642 14624 10778 327 -359 -152 N ATOM 3175 CA TYR A 308 11.370 5.482 55.659 1.00108.85 C ANISOU 3175 CA TYR A 308 16511 14182 10664 343 -277 -76 C ATOM 3176 C TYR A 308 10.768 6.642 54.848 1.00110.65 C ANISOU 3176 C TYR A 308 16760 14280 11001 200 -233 -127 C ATOM 3177 O TYR A 308 10.257 6.407 53.753 1.00109.28 O ANISOU 3177 O TYR A 308 16594 13993 10934 195 -194 -86 O ATOM 3178 CB TYR A 308 10.409 5.064 56.791 1.00110.47 C ANISOU 3178 CB TYR A 308 16830 14324 10818 421 -233 -27 C ATOM 3179 CG TYR A 308 9.061 4.550 56.327 1.00111.52 C ANISOU 3179 CG TYR A 308 17051 14273 11050 439 -143 43 C ATOM 3180 CD1 TYR A 308 8.890 3.218 55.957 1.00113.34 C ANISOU 3180 CD1 TYR A 308 17311 14456 11297 540 -108 132 C ATOM 3181 CD2 TYR A 308 7.943 5.379 56.315 1.00111.84 C ANISOU 3181 CD2 TYR A 308 17147 14195 11152 361 -87 12 C ATOM 3182 CE1 TYR A 308 7.649 2.734 55.547 1.00113.60 C ANISOU 3182 CE1 TYR A 308 17414 14337 11411 535 -18 178 C ATOM 3183 CE2 TYR A 308 6.696 4.907 55.903 1.00112.10 C ANISOU 3183 CE2 TYR A 308 17236 14094 11264 376 -6 61 C ATOM 3184 CZ TYR A 308 6.553 3.582 55.523 1.00120.29 C ANISOU 3184 CZ TYR A 308 18290 15096 12319 451 29 139 C ATOM 3185 OH TYR A 308 5.326 3.112 55.120 1.00121.98 O ANISOU 3185 OH TYR A 308 18549 15194 12603 444 115 169 O ATOM 3186 N ILE A 309 10.820 7.878 55.389 1.00106.77 N ANISOU 3186 N ILE A 309 16291 13805 10473 92 -237 -218 N ATOM 3187 CA ILE A 309 10.283 9.099 54.767 1.00105.47 C ANISOU 3187 CA ILE A 309 16180 13511 10384 -30 -187 -270 C ATOM 3188 C ILE A 309 11.094 9.465 53.499 1.00107.60 C ANISOU 3188 C ILE A 309 16378 13794 10710 -118 -199 -305 C ATOM 3189 O ILE A 309 10.496 9.846 52.490 1.00106.63 O ANISOU 3189 O ILE A 309 16298 13534 10683 -151 -151 -290 O ATOM 3190 CB ILE A 309 10.241 10.274 55.793 1.00109.32 C ANISOU 3190 CB ILE A 309 16729 14013 10795 -119 -180 -362 C ATOM 3191 CG1 ILE A 309 9.488 9.864 57.079 1.00109.93 C ANISOU 3191 CG1 ILE A 309 16873 14088 10809 -27 -169 -326 C ATOM 3192 CG2 ILE A 309 9.619 11.544 55.184 1.00109.75 C ANISOU 3192 CG2 ILE A 309 16875 13911 10915 -222 -115 -408 C ATOM 3193 CD1 ILE A 309 9.996 10.503 58.362 1.00119.36 C ANISOU 3193 CD1 ILE A 309 18077 15398 11878 -77 -202 -411 C ATOM 3194 N LEU A 310 12.439 9.339 53.559 1.00103.26 N ANISOU 3194 N LEU A 310 15717 13422 10095 -149 -263 -355 N ATOM 3195 CA LEU A 310 13.363 9.635 52.456 1.00102.30 C ANISOU 3195 CA LEU A 310 15513 13347 10010 -242 -275 -399 C ATOM 3196 C LEU A 310 13.112 8.718 51.242 1.00103.77 C ANISOU 3196 C LEU A 310 15674 13457 10297 -160 -262 -306 C ATOM 3197 O LEU A 310 13.113 9.206 50.108 1.00102.87 O ANISOU 3197 O LEU A 310 15566 13258 10261 -237 -229 -318 O ATOM 3198 CB LEU A 310 14.825 9.507 52.940 1.00103.49 C ANISOU 3198 CB LEU A 310 15525 13748 10049 -268 -351 -475 C ATOM 3199 CG LEU A 310 15.938 9.695 51.898 1.00108.08 C ANISOU 3199 CG LEU A 310 15993 14425 10649 -364 -367 -532 C ATOM 3200 CD1 LEU A 310 16.236 11.163 51.663 1.00108.80 C ANISOU 3200 CD1 LEU A 310 16121 14482 10738 -581 -321 -654 C ATOM 3201 CD2 LEU A 310 17.199 8.967 52.314 1.00111.28 C ANISOU 3201 CD2 LEU A 310 16235 15100 10946 -296 -453 -561 C ATOM 3202 N LEU A 311 12.899 7.404 51.481 1.00 98.87 N ANISOU 3202 N LEU A 311 15040 12860 9668 -6 -279 -214 N ATOM 3203 CA LEU A 311 12.645 6.420 50.421 1.00 97.16 C ANISOU 3203 CA LEU A 311 14808 12571 9536 73 -261 -128 C ATOM 3204 C LEU A 311 11.246 6.589 49.825 1.00 98.44 C ANISOU 3204 C LEU A 311 15066 12536 9802 66 -189 -85 C ATOM 3205 O LEU A 311 11.044 6.274 48.649 1.00 97.13 O ANISOU 3205 O LEU A 311 14885 12299 9721 71 -166 -50 O ATOM 3206 CB LEU A 311 12.833 4.980 50.924 1.00 97.38 C ANISOU 3206 CB LEU A 311 14823 12669 9508 236 -285 -48 C ATOM 3207 CG LEU A 311 14.258 4.553 51.284 1.00103.14 C ANISOU 3207 CG LEU A 311 15441 13618 10130 295 -362 -74 C ATOM 3208 CD1 LEU A 311 14.249 3.214 51.959 1.00103.78 C ANISOU 3208 CD1 LEU A 311 15559 13737 10136 480 -370 13 C ATOM 3209 CD2 LEU A 311 15.165 4.505 50.062 1.00105.39 C ANISOU 3209 CD2 LEU A 311 15617 13965 10460 256 -384 -95 C ATOM 3210 N ASN A 312 10.289 7.093 50.635 1.00 93.64 N ANISOU 3210 N ASN A 312 14547 11853 9177 59 -154 -95 N ATOM 3211 CA ASN A 312 8.910 7.364 50.223 1.00 91.86 C ANISOU 3211 CA ASN A 312 14401 11473 9029 61 -88 -71 C ATOM 3212 C ASN A 312 8.873 8.585 49.304 1.00 95.09 C ANISOU 3212 C ASN A 312 14833 11806 9490 -36 -65 -122 C ATOM 3213 O ASN A 312 8.041 8.642 48.398 1.00 94.17 O ANISOU 3213 O ASN A 312 14744 11586 9449 -18 -24 -95 O ATOM 3214 CB ASN A 312 8.019 7.592 51.453 1.00 89.99 C ANISOU 3214 CB ASN A 312 14245 11205 8743 87 -60 -76 C ATOM 3215 CG ASN A 312 6.534 7.392 51.232 1.00 99.27 C ANISOU 3215 CG ASN A 312 15477 12264 9978 130 7 -38 C ATOM 3216 OD1 ASN A 312 5.818 6.788 52.038 1.00 86.24 O ANISOU 3216 OD1 ASN A 312 13834 10533 8400 112 39 -42 O ATOM 3217 ND2 ASN A 312 6.049 7.839 50.086 1.00 91.11 N ANISOU 3217 ND2 ASN A 312 14486 11230 8903 188 34 -9 N ATOM 3218 N TRP A 313 9.784 9.554 49.534 1.00 91.73 N ANISOU 3218 N TRP A 313 14403 11437 9014 -140 -86 -202 N ATOM 3219 CA TRP A 313 9.868 10.784 48.752 1.00 91.07 C ANISOU 3219 CA TRP A 313 14373 11270 8960 -245 -50 -257 C ATOM 3220 C TRP A 313 10.573 10.569 47.409 1.00 94.24 C ANISOU 3220 C TRP A 313 14707 11681 9418 -278 -58 -248 C ATOM 3221 O TRP A 313 10.308 11.335 46.484 1.00 93.85 O ANISOU 3221 O TRP A 313 14722 11525 9414 -325 -12 -260 O ATOM 3222 CB TRP A 313 10.504 11.924 49.557 1.00 90.70 C ANISOU 3222 CB TRP A 313 14368 11265 8830 -366 -49 -358 C ATOM 3223 CG TRP A 313 9.462 12.764 50.233 1.00 91.61 C ANISOU 3223 CG TRP A 313 14615 11268 8925 -360 3 -376 C ATOM 3224 CD1 TRP A 313 8.741 12.436 51.344 1.00 94.47 C ANISOU 3224 CD1 TRP A 313 15003 11640 9249 -283 -1 -354 C ATOM 3225 CD2 TRP A 313 8.943 14.020 49.774 1.00 91.59 C ANISOU 3225 CD2 TRP A 313 14748 11117 8937 -414 73 -412 C ATOM 3226 NE1 TRP A 313 7.813 13.414 51.612 1.00 94.01 N ANISOU 3226 NE1 TRP A 313 15074 11461 9185 -288 59 -378 N ATOM 3227 CE2 TRP A 313 7.928 14.409 50.675 1.00 95.54 C ANISOU 3227 CE2 TRP A 313 15342 11553 9405 -360 105 -413 C ATOM 3228 CE3 TRP A 313 9.255 14.871 48.698 1.00 92.92 C ANISOU 3228 CE3 TRP A 313 14980 11195 9132 -497 119 -443 C ATOM 3229 CZ2 TRP A 313 7.225 15.613 50.538 1.00 95.13 C ANISOU 3229 CZ2 TRP A 313 15444 11356 9345 -372 177 -444 C ATOM 3230 CZ3 TRP A 313 8.553 16.059 48.559 1.00 94.63 C ANISOU 3230 CZ3 TRP A 313 15364 11255 9337 -510 196 -469 C ATOM 3231 CH2 TRP A 313 7.558 16.423 49.476 1.00 95.44 C ANISOU 3231 CH2 TRP A 313 15557 11302 9405 -442 223 -469 C ATOM 3232 N ILE A 314 11.405 9.507 47.273 1.00 90.15 N ANISOU 3232 N ILE A 314 14073 11287 8894 -237 -110 -219 N ATOM 3233 CA ILE A 314 12.055 9.153 46.000 1.00 89.47 C ANISOU 3233 CA ILE A 314 13915 11219 8862 -254 -118 -204 C ATOM 3234 C ILE A 314 10.935 8.724 45.027 1.00 92.79 C ANISOU 3234 C ILE A 314 14377 11503 9375 -178 -78 -129 C ATOM 3235 O ILE A 314 10.946 9.120 43.859 1.00 92.26 O ANISOU 3235 O ILE A 314 14324 11370 9363 -217 -52 -131 O ATOM 3236 CB ILE A 314 13.166 8.075 46.192 1.00 92.75 C ANISOU 3236 CB ILE A 314 14201 11807 9234 -200 -183 -190 C ATOM 3237 CG1 ILE A 314 14.362 8.665 46.970 1.00 94.46 C ANISOU 3237 CG1 ILE A 314 14351 12192 9350 -293 -225 -289 C ATOM 3238 CG2 ILE A 314 13.633 7.479 44.851 1.00 92.61 C ANISOU 3238 CG2 ILE A 314 14113 11793 9280 -185 -186 -156 C ATOM 3239 CD1 ILE A 314 15.169 7.657 47.792 1.00102.96 C ANISOU 3239 CD1 ILE A 314 15321 13460 10337 -191 -296 -277 C ATOM 3240 N GLY A 315 9.947 7.999 45.556 1.00 89.11 N ANISOU 3240 N GLY A 315 13938 11002 8917 -79 -67 -74 N ATOM 3241 CA GLY A 315 8.764 7.571 44.822 1.00 88.20 C ANISOU 3241 CA GLY A 315 13853 10786 8875 -15 -25 -21 C ATOM 3242 C GLY A 315 7.851 8.729 44.461 1.00 92.52 C ANISOU 3242 C GLY A 315 14488 11222 9444 -38 22 -47 C ATOM 3243 O GLY A 315 7.185 8.684 43.423 1.00 92.13 O ANISOU 3243 O GLY A 315 14446 11108 9452 -5 49 -22 O ATOM 3244 N TYR A 316 7.820 9.784 45.311 1.00 89.19 N ANISOU 3244 N TYR A 316 14140 10783 8966 -86 33 -100 N ATOM 3245 CA TYR A 316 7.011 10.991 45.103 1.00 89.01 C ANISOU 3245 CA TYR A 316 14228 10649 8943 -93 84 -127 C ATOM 3246 C TYR A 316 7.513 11.847 43.932 1.00 93.91 C ANISOU 3246 C TYR A 316 14893 11206 9584 -157 108 -152 C ATOM 3247 O TYR A 316 6.689 12.406 43.204 1.00 93.47 O ANISOU 3247 O TYR A 316 14912 11053 9550 -109 151 -140 O ATOM 3248 CB TYR A 316 6.987 11.864 46.368 1.00 90.64 C ANISOU 3248 CB TYR A 316 14514 10850 9074 -135 95 -182 C ATOM 3249 CG TYR A 316 6.104 11.390 47.504 1.00 91.66 C ANISOU 3249 CG TYR A 316 14650 11001 9177 -60 97 -163 C ATOM 3250 CD1 TYR A 316 4.915 10.707 47.252 1.00 92.91 C ANISOU 3250 CD1 TYR A 316 14789 11133 9377 37 121 -113 C ATOM 3251 CD2 TYR A 316 6.385 11.738 48.820 1.00 92.75 C ANISOU 3251 CD2 TYR A 316 14820 11182 9240 -97 85 -204 C ATOM 3252 CE1 TYR A 316 4.075 10.312 48.292 1.00 93.12 C ANISOU 3252 CE1 TYR A 316 14828 11178 9376 90 136 -103 C ATOM 3253 CE2 TYR A 316 5.551 11.353 49.866 1.00 93.33 C ANISOU 3253 CE2 TYR A 316 14911 11268 9284 -31 95 -187 C ATOM 3254 CZ TYR A 316 4.396 10.640 49.598 1.00 98.45 C ANISOU 3254 CZ TYR A 316 15542 11887 9978 60 124 -135 C ATOM 3255 OH TYR A 316 3.574 10.259 50.628 1.00 98.72 O ANISOU 3255 OH TYR A 316 15595 11936 9979 111 146 -124 O ATOM 3256 N VAL A 317 8.856 11.974 43.772 1.00 91.28 N ANISOU 3256 N VAL A 317 14516 10935 9233 -263 85 -190 N ATOM 3257 CA VAL A 317 9.510 12.771 42.718 1.00 91.49 C ANISOU 3257 CA VAL A 317 14587 10907 9269 -353 117 -222 C ATOM 3258 C VAL A 317 9.179 12.174 41.325 1.00 95.54 C ANISOU 3258 C VAL A 317 15060 11385 9856 -283 120 -160 C ATOM 3259 O VAL A 317 9.040 12.930 40.359 1.00 95.51 O ANISOU 3259 O VAL A 317 15143 11283 9864 -297 167 -164 O ATOM 3260 CB VAL A 317 11.050 12.926 42.941 1.00 95.85 C ANISOU 3260 CB VAL A 317 15071 11570 9778 -494 92 -291 C ATOM 3261 CG1 VAL A 317 11.666 13.902 41.941 1.00 96.21 C ANISOU 3261 CG1 VAL A 317 15189 11543 9822 -613 149 -337 C ATOM 3262 CG2 VAL A 317 11.364 13.389 44.361 1.00 96.41 C ANISOU 3262 CG2 VAL A 317 15159 11704 9767 -559 81 -358 C ATOM 3263 N ASN A 318 8.992 10.830 41.249 1.00 92.05 N ANISOU 3263 N ASN A 318 14505 11014 9456 -201 78 -104 N ATOM 3264 CA ASN A 318 8.649 10.066 40.037 1.00 91.26 C ANISOU 3264 CA ASN A 318 14354 10899 9423 -136 78 -50 C ATOM 3265 C ASN A 318 7.378 10.606 39.332 1.00 95.37 C ANISOU 3265 C ASN A 318 14956 11315 9963 -61 122 -32 C ATOM 3266 O ASN A 318 7.272 10.492 38.107 1.00 95.06 O ANISOU 3266 O ASN A 318 14908 11249 9964 -35 133 -9 O ATOM 3267 CB ASN A 318 8.477 8.579 40.376 1.00 90.17 C ANISOU 3267 CB ASN A 318 14116 10837 9308 -64 43 -2 C ATOM 3268 CG ASN A 318 8.096 7.707 39.208 1.00108.74 C ANISOU 3268 CG ASN A 318 16417 13176 11724 -9 49 44 C ATOM 3269 OD1 ASN A 318 6.958 7.247 39.104 1.00101.04 O ANISOU 3269 OD1 ASN A 318 15443 12175 10772 60 70 69 O ATOM 3270 ND2 ASN A 318 9.017 7.508 38.274 1.00100.96 N ANISOU 3270 ND2 ASN A 318 15382 12215 10763 -45 35 48 N ATOM 3271 N SER A 319 6.451 11.228 40.097 1.00 91.62 N ANISOU 3271 N SER A 319 14562 10795 9453 -17 148 -47 N ATOM 3272 CA SER A 319 5.212 11.825 39.589 1.00 91.30 C ANISOU 3272 CA SER A 319 14600 10681 9410 78 188 -37 C ATOM 3273 C SER A 319 5.481 13.034 38.664 1.00 95.94 C ANISOU 3273 C SER A 319 15312 11166 9976 58 232 -53 C ATOM 3274 O SER A 319 4.588 13.442 37.922 1.00 95.69 O ANISOU 3274 O SER A 319 15338 11081 9937 159 261 -36 O ATOM 3275 CB SER A 319 4.315 12.250 40.746 1.00 95.27 C ANISOU 3275 CB SER A 319 15161 11171 9868 127 207 -56 C ATOM 3276 OG SER A 319 4.053 11.168 41.624 1.00104.53 O ANISOU 3276 OG SER A 319 16239 12426 11051 141 179 -42 O ATOM 3277 N GLY A 320 6.702 13.572 38.712 1.00 93.14 N ANISOU 3277 N GLY A 320 14997 10791 9600 -71 242 -89 N ATOM 3278 CA GLY A 320 7.132 14.698 37.890 1.00 93.82 C ANISOU 3278 CA GLY A 320 15220 10770 9658 -124 300 -110 C ATOM 3279 C GLY A 320 8.128 14.343 36.802 1.00 98.67 C ANISOU 3279 C GLY A 320 15772 11408 10309 -198 292 -103 C ATOM 3280 O GLY A 320 8.497 15.207 36.002 1.00 99.11 O ANISOU 3280 O GLY A 320 15945 11370 10341 -246 349 -117 O ATOM 3281 N PHE A 321 8.573 13.073 36.757 1.00 95.30 N ANISOU 3281 N PHE A 321 15175 11101 9934 -203 229 -80 N ATOM 3282 CA PHE A 321 9.532 12.590 35.764 1.00 95.18 C ANISOU 3282 CA PHE A 321 15081 11129 9955 -262 216 -73 C ATOM 3283 C PHE A 321 8.857 12.165 34.469 1.00 99.84 C ANISOU 3283 C PHE A 321 15657 11688 10589 -159 220 -19 C ATOM 3284 O PHE A 321 9.419 12.413 33.402 1.00100.19 O ANISOU 3284 O PHE A 321 15726 11699 10642 -200 244 -17 O ATOM 3285 CB PHE A 321 10.361 11.418 36.313 1.00 96.52 C ANISOU 3285 CB PHE A 321 15085 11442 10145 -296 151 -73 C ATOM 3286 CG PHE A 321 11.443 11.779 37.305 1.00 98.80 C ANISOU 3286 CG PHE A 321 15352 11806 10381 -418 139 -139 C ATOM 3287 CD1 PHE A 321 12.104 13.002 37.228 1.00102.69 C ANISOU 3287 CD1 PHE A 321 15942 12247 10826 -553 193 -207 C ATOM 3288 CD2 PHE A 321 11.843 10.875 38.280 1.00100.86 C ANISOU 3288 CD2 PHE A 321 15496 12196 10629 -402 79 -139 C ATOM 3289 CE1 PHE A 321 13.109 13.329 38.139 1.00104.49 C ANISOU 3289 CE1 PHE A 321 16134 12571 10998 -682 183 -286 C ATOM 3290 CE2 PHE A 321 12.855 11.200 39.186 1.00104.49 C ANISOU 3290 CE2 PHE A 321 15918 12756 11027 -506 60 -209 C ATOM 3291 CZ PHE A 321 13.484 12.422 39.105 1.00103.53 C ANISOU 3291 CZ PHE A 321 15875 12601 10862 -653 110 -287 C ATOM 3292 N ASN A 322 7.673 11.506 34.562 1.00 96.02 N ANISOU 3292 N ASN A 322 15128 11226 10129 -34 199 18 N ATOM 3293 CA ASN A 322 6.882 11.007 33.426 1.00 95.14 C ANISOU 3293 CA ASN A 322 14982 11116 10052 68 197 57 C ATOM 3294 C ASN A 322 6.671 12.078 32.331 1.00 98.56 C ANISOU 3294 C ASN A 322 15547 11449 10453 106 247 61 C ATOM 3295 O ASN A 322 6.962 11.744 31.180 1.00 98.19 O ANISOU 3295 O ASN A 322 15467 11408 10433 110 245 82 O ATOM 3296 CB ASN A 322 5.536 10.438 33.887 1.00 96.43 C ANISOU 3296 CB ASN A 322 15096 11321 10220 177 184 70 C ATOM 3297 CG ASN A 322 5.638 9.119 34.614 1.00123.26 C ANISOU 3297 CG ASN A 322 18371 14807 13654 157 148 79 C ATOM 3298 OD1 ASN A 322 6.578 8.853 35.372 1.00118.44 O ANISOU 3298 OD1 ASN A 322 17733 14229 13040 83 126 72 O ATOM 3299 ND2 ASN A 322 4.652 8.266 34.416 1.00116.57 N ANISOU 3299 ND2 ASN A 322 17455 14007 12831 226 146 92 N ATOM 3300 N PRO A 323 6.270 13.358 32.628 1.00 94.68 N ANISOU 3300 N PRO A 323 15220 10858 9897 133 298 44 N ATOM 3301 CA PRO A 323 6.108 14.349 31.539 1.00 94.49 C ANISOU 3301 CA PRO A 323 15349 10725 9827 186 356 57 C ATOM 3302 C PRO A 323 7.397 14.668 30.768 1.00 96.77 C ANISOU 3302 C PRO A 323 15685 10964 10120 54 390 46 C ATOM 3303 O PRO A 323 7.317 15.047 29.600 1.00 96.53 O ANISOU 3303 O PRO A 323 15736 10870 10070 104 426 70 O ATOM 3304 CB PRO A 323 5.595 15.597 32.267 1.00 97.30 C ANISOU 3304 CB PRO A 323 15885 10977 10106 226 411 35 C ATOM 3305 CG PRO A 323 4.978 15.081 33.516 1.00101.66 C ANISOU 3305 CG PRO A 323 16344 11611 10672 255 369 23 C ATOM 3306 CD PRO A 323 5.869 13.950 33.924 1.00 96.50 C ANISOU 3306 CD PRO A 323 15520 11062 10083 136 312 16 C ATOM 3307 N LEU A 324 8.570 14.508 31.406 1.00 92.34 N ANISOU 3307 N LEU A 324 15066 10443 9574 -108 380 6 N ATOM 3308 CA LEU A 324 9.870 14.756 30.779 1.00 92.24 C ANISOU 3308 CA LEU A 324 15069 10415 9562 -256 414 -21 C ATOM 3309 C LEU A 324 10.252 13.618 29.833 1.00 94.39 C ANISOU 3309 C LEU A 324 15184 10779 9899 -243 366 12 C ATOM 3310 O LEU A 324 10.935 13.857 28.836 1.00 93.74 O ANISOU 3310 O LEU A 324 15137 10664 9814 -304 404 10 O ATOM 3311 CB LEU A 324 10.968 14.952 31.839 1.00 92.88 C ANISOU 3311 CB LEU A 324 15116 10549 9626 -429 414 -90 C ATOM 3312 CG LEU A 324 10.806 16.136 32.798 1.00 98.86 C ANISOU 3312 CG LEU A 324 16037 11213 10313 -482 472 -138 C ATOM 3313 CD1 LEU A 324 11.701 15.974 34.008 1.00 99.54 C ANISOU 3313 CD1 LEU A 324 16026 11409 10386 -623 440 -206 C ATOM 3314 CD2 LEU A 324 11.080 17.471 32.103 1.00102.63 C ANISOU 3314 CD2 LEU A 324 16743 11525 10727 -555 586 -163 C ATOM 3315 N ILE A 325 9.805 12.386 30.140 1.00 90.15 N ANISOU 3315 N ILE A 325 14489 10350 9415 -167 294 40 N ATOM 3316 CA ILE A 325 10.086 11.189 29.337 1.00 89.33 C ANISOU 3316 CA ILE A 325 14241 10330 9370 -146 251 70 C ATOM 3317 C ILE A 325 9.186 11.184 28.070 1.00 94.33 C ANISOU 3317 C ILE A 325 14915 10919 10008 -26 266 110 C ATOM 3318 O ILE A 325 9.579 10.596 27.058 1.00 93.77 O ANISOU 3318 O ILE A 325 14780 10878 9970 -30 257 128 O ATOM 3319 CB ILE A 325 9.960 9.881 30.184 1.00 91.21 C ANISOU 3319 CB ILE A 325 14326 10681 9649 -116 187 81 C ATOM 3320 CG1 ILE A 325 10.826 9.961 31.469 1.00 91.60 C ANISOU 3320 CG1 ILE A 325 14342 10787 9674 -212 168 40 C ATOM 3321 CG2 ILE A 325 10.333 8.632 29.364 1.00 91.00 C ANISOU 3321 CG2 ILE A 325 14173 10727 9677 -98 155 109 C ATOM 3322 CD1 ILE A 325 10.325 9.165 32.658 1.00 96.27 C ANISOU 3322 CD1 ILE A 325 14865 11442 10271 -157 126 51 C ATOM 3323 N TYR A 326 8.023 11.883 28.099 1.00 91.75 N ANISOU 3323 N TYR A 326 14694 10529 9638 87 289 121 N ATOM 3324 CA TYR A 326 7.128 11.969 26.936 1.00 91.95 C ANISOU 3324 CA TYR A 326 14756 10536 9646 221 299 152 C ATOM 3325 C TYR A 326 7.712 12.882 25.840 1.00 97.32 C ANISOU 3325 C TYR A 326 15581 11113 10285 195 361 161 C ATOM 3326 O TYR A 326 7.240 12.845 24.704 1.00 96.52 O ANISOU 3326 O TYR A 326 15498 11007 10167 295 366 189 O ATOM 3327 CB TYR A 326 5.710 12.430 27.329 1.00 93.55 C ANISOU 3327 CB TYR A 326 15015 10730 9799 369 303 154 C ATOM 3328 CG TYR A 326 5.014 11.546 28.344 1.00 95.10 C ANISOU 3328 CG TYR A 326 15078 11026 10028 394 255 142 C ATOM 3329 CD1 TYR A 326 5.054 10.157 28.235 1.00 96.28 C ANISOU 3329 CD1 TYR A 326 15061 11278 10244 368 211 147 C ATOM 3330 CD2 TYR A 326 4.263 12.094 29.375 1.00 96.53 C ANISOU 3330 CD2 TYR A 326 15316 11193 10170 447 265 126 C ATOM 3331 CE1 TYR A 326 4.412 9.339 29.165 1.00 96.62 C ANISOU 3331 CE1 TYR A 326 15005 11397 10309 381 185 135 C ATOM 3332 CE2 TYR A 326 3.626 11.287 30.318 1.00 97.17 C ANISOU 3332 CE2 TYR A 326 15282 11362 10276 460 232 113 C ATOM 3333 CZ TYR A 326 3.703 9.909 30.209 1.00103.66 C ANISOU 3333 CZ TYR A 326 15948 12277 11162 423 195 117 C ATOM 3334 OH TYR A 326 3.059 9.118 31.128 1.00104.76 O ANISOU 3334 OH TYR A 326 15998 12488 11317 429 179 104 O ATOM 3335 N CYS A 327 8.776 13.647 26.165 1.00 95.72 N ANISOU 3335 N CYS A 327 15474 10836 10060 51 412 131 N ATOM 3336 CA CYS A 327 9.476 14.527 25.229 1.00 97.00 C ANISOU 3336 CA CYS A 327 15788 10890 10178 -13 490 129 C ATOM 3337 C CYS A 327 10.339 13.722 24.246 1.00100.62 C ANISOU 3337 C CYS A 327 16128 11415 10689 -81 471 137 C ATOM 3338 O CYS A 327 10.928 14.304 23.334 1.00100.77 O ANISOU 3338 O CYS A 327 16255 11356 10676 -136 536 138 O ATOM 3339 CB CYS A 327 10.304 15.562 25.980 1.00 98.74 C ANISOU 3339 CB CYS A 327 16140 11022 10353 -171 560 76 C ATOM 3340 SG CYS A 327 9.322 16.909 26.683 1.00103.98 S ANISOU 3340 SG CYS A 327 17043 11541 10925 -78 625 74 S ATOM 3341 N ARG A 328 10.400 12.388 24.423 1.00 96.37 N ANISOU 3341 N ARG A 328 15382 11011 10223 -74 392 143 N ATOM 3342 CA ARG A 328 11.103 11.473 23.529 1.00 95.59 C ANISOU 3342 CA ARG A 328 15160 10984 10175 -112 368 154 C ATOM 3343 C ARG A 328 10.293 11.309 22.241 1.00 99.72 C ANISOU 3343 C ARG A 328 15709 11491 10690 22 369 196 C ATOM 3344 O ARG A 328 10.871 11.252 21.154 1.00 99.66 O ANISOU 3344 O ARG A 328 15711 11472 10684 -8 394 206 O ATOM 3345 CB ARG A 328 11.326 10.117 24.207 1.00 94.24 C ANISOU 3345 CB ARG A 328 14792 10945 10070 -124 294 150 C ATOM 3346 CG ARG A 328 12.500 10.094 25.175 1.00103.10 C ANISOU 3346 CG ARG A 328 15854 12124 11195 -262 286 106 C ATOM 3347 CD ARG A 328 12.716 8.719 25.793 1.00110.20 C ANISOU 3347 CD ARG A 328 16581 13147 12143 -242 218 113 C ATOM 3348 NE ARG A 328 12.706 7.639 24.801 1.00117.28 N ANISOU 3348 NE ARG A 328 17387 14089 13086 -186 196 145 N ATOM 3349 CZ ARG A 328 13.758 7.258 24.083 1.00132.60 C ANISOU 3349 CZ ARG A 328 19262 16077 15043 -244 200 139 C ATOM 3350 NH1 ARG A 328 14.931 7.863 24.236 1.00121.28 N ANISOU 3350 NH1 ARG A 328 17829 14668 13581 -367 225 94 N ATOM 3351 NH2 ARG A 328 13.646 6.271 23.205 1.00118.54 N ANISOU 3351 NH2 ARG A 328 17411 14327 13301 -185 184 168 N ATOM 3352 N SER A 329 8.949 11.254 22.370 1.00 96.18 N ANISOU 3352 N SER A 329 15266 11055 10222 171 343 214 N ATOM 3353 CA SER A 329 8.023 11.131 21.246 1.00 95.97 C ANISOU 3353 CA SER A 329 15250 11044 10170 317 336 242 C ATOM 3354 C SER A 329 7.907 12.470 20.514 1.00100.65 C ANISOU 3354 C SER A 329 16060 11510 10672 379 409 262 C ATOM 3355 O SER A 329 7.631 13.487 21.159 1.00101.29 O ANISOU 3355 O SER A 329 16287 11502 10695 402 450 256 O ATOM 3356 CB SER A 329 6.651 10.654 21.719 1.00 99.27 C ANISOU 3356 CB SER A 329 15587 11545 10587 445 289 238 C ATOM 3357 OG SER A 329 5.724 10.573 20.647 1.00108.23 O ANISOU 3357 OG SER A 329 16716 12725 11682 589 279 251 O ATOM 3358 N PRO A 330 8.112 12.496 19.173 1.00 96.86 N ANISOU 3358 N PRO A 330 15620 11011 10171 411 431 286 N ATOM 3359 CA PRO A 330 8.015 13.768 18.432 1.00 97.69 C ANISOU 3359 CA PRO A 330 15960 10981 10175 482 512 311 C ATOM 3360 C PRO A 330 6.603 14.350 18.434 1.00101.65 C ANISOU 3360 C PRO A 330 16554 11478 10592 701 508 331 C ATOM 3361 O PRO A 330 6.462 15.569 18.391 1.00102.06 O ANISOU 3361 O PRO A 330 16834 11394 10549 763 582 349 O ATOM 3362 CB PRO A 330 8.457 13.390 17.015 1.00 99.41 C ANISOU 3362 CB PRO A 330 16160 11216 10397 482 521 333 C ATOM 3363 CG PRO A 330 9.178 12.083 17.163 1.00102.75 C ANISOU 3363 CG PRO A 330 16358 11754 10928 355 463 310 C ATOM 3364 CD PRO A 330 8.463 11.386 18.267 1.00 97.55 C ANISOU 3364 CD PRO A 330 15559 11190 10316 388 393 291 C ATOM 3365 N ASP A 331 5.568 13.486 18.518 1.00 97.89 N ANISOU 3365 N ASP A 331 15904 11151 10137 814 428 323 N ATOM 3366 CA ASP A 331 4.156 13.879 18.567 1.00 98.40 C ANISOU 3366 CA ASP A 331 16002 11265 10120 1029 410 327 C ATOM 3367 C ASP A 331 3.855 14.729 19.812 1.00102.33 C ANISOU 3367 C ASP A 331 16613 11685 10582 1044 440 317 C ATOM 3368 O ASP A 331 3.104 15.700 19.710 1.00103.56 O ANISOU 3368 O ASP A 331 16931 11787 10631 1215 476 335 O ATOM 3369 CB ASP A 331 3.241 12.643 18.532 1.00 99.63 C ANISOU 3369 CB ASP A 331 15915 11619 10319 1090 324 297 C ATOM 3370 CG ASP A 331 3.169 11.953 17.182 1.00110.49 C ANISOU 3370 CG ASP A 331 17202 13085 11696 1133 297 302 C ATOM 3371 OD1 ASP A 331 2.991 12.658 16.161 1.00111.40 O ANISOU 3371 OD1 ASP A 331 17450 13160 11718 1262 327 332 O ATOM 3372 OD2 ASP A 331 3.227 10.704 17.152 1.00116.38 O ANISOU 3372 OD2 ASP A 331 17753 13940 12524 1050 249 274 O ATOM 3373 N PHE A 332 4.456 14.380 20.969 1.00 96.92 N ANISOU 3373 N PHE A 332 15852 10996 9977 876 428 288 N ATOM 3374 CA PHE A 332 4.285 15.123 22.220 1.00 96.49 C ANISOU 3374 CA PHE A 332 15896 10871 9896 862 456 272 C ATOM 3375 C PHE A 332 5.104 16.404 22.215 1.00 99.82 C ANISOU 3375 C PHE A 332 16571 11098 10257 786 556 279 C ATOM 3376 O PHE A 332 4.664 17.388 22.806 1.00100.75 O ANISOU 3376 O PHE A 332 16858 11122 10301 856 605 278 O ATOM 3377 CB PHE A 332 4.671 14.270 23.435 1.00 97.32 C ANISOU 3377 CB PHE A 332 15832 11048 10096 713 408 237 C ATOM 3378 CG PHE A 332 3.596 13.330 23.914 1.00 98.38 C ANISOU 3378 CG PHE A 332 15782 11336 10262 796 338 220 C ATOM 3379 CD1 PHE A 332 3.445 12.071 23.343 1.00100.86 C ANISOU 3379 CD1 PHE A 332 15908 11778 10637 788 285 215 C ATOM 3380 CD2 PHE A 332 2.742 13.694 24.947 1.00101.04 C ANISOU 3380 CD2 PHE A 332 16139 11688 10565 870 336 202 C ATOM 3381 CE1 PHE A 332 2.449 11.198 23.789 1.00101.45 C ANISOU 3381 CE1 PHE A 332 15823 11989 10734 839 238 188 C ATOM 3382 CE2 PHE A 332 1.747 12.819 25.394 1.00103.54 C ANISOU 3382 CE2 PHE A 332 16284 12151 10907 928 284 178 C ATOM 3383 CZ PHE A 332 1.607 11.578 24.811 1.00100.94 C ANISOU 3383 CZ PHE A 332 15774 11944 10634 905 239 168 C ATOM 3384 N ARG A 333 6.296 16.389 21.569 1.00 94.53 N ANISOU 3384 N ARG A 333 15932 10370 9614 635 595 281 N ATOM 3385 CA ARG A 333 7.208 17.536 21.463 1.00 94.71 C ANISOU 3385 CA ARG A 333 16192 10213 9581 517 706 275 C ATOM 3386 C ARG A 333 6.537 18.713 20.757 1.00 99.05 C ANISOU 3386 C ARG A 333 17013 10621 9999 700 789 316 C ATOM 3387 O ARG A 333 6.631 19.845 21.233 1.00 99.57 O ANISOU 3387 O ARG A 333 17313 10529 9990 681 881 308 O ATOM 3388 CB ARG A 333 8.486 17.143 20.711 1.00 94.24 C ANISOU 3388 CB ARG A 333 16080 10156 9572 341 727 265 C ATOM 3389 CG ARG A 333 9.679 16.876 21.613 1.00102.05 C ANISOU 3389 CG ARG A 333 16969 11178 10629 99 725 207 C ATOM 3390 CD ARG A 333 10.961 16.666 20.820 1.00110.75 C ANISOU 3390 CD ARG A 333 18038 12282 11759 -69 761 190 C ATOM 3391 NE ARG A 333 10.950 15.415 20.055 1.00117.64 N ANISOU 3391 NE ARG A 333 18703 13291 12702 -19 679 216 N ATOM 3392 CZ ARG A 333 11.910 15.039 19.215 1.00133.09 C ANISOU 3392 CZ ARG A 333 20604 15276 14688 -123 696 210 C ATOM 3393 NH1 ARG A 333 12.973 15.807 19.018 1.00125.03 N ANISOU 3393 NH1 ARG A 333 19706 14167 13632 -293 793 174 N ATOM 3394 NH2 ARG A 333 11.812 13.887 18.564 1.00116.81 N ANISOU 3394 NH2 ARG A 333 18363 13331 12687 -65 624 232 N ATOM 3395 N ILE A 334 5.845 18.426 19.634 1.00 95.40 N ANISOU 3395 N ILE A 334 16526 10222 9500 886 757 359 N ATOM 3396 CA ILE A 334 5.117 19.385 18.802 1.00 96.59 C ANISOU 3396 CA ILE A 334 16914 10275 9512 1111 820 408 C ATOM 3397 C ILE A 334 3.886 19.919 19.571 1.00100.85 C ANISOU 3397 C ILE A 334 17518 10825 9977 1314 808 410 C ATOM 3398 O ILE A 334 3.543 21.094 19.429 1.00102.09 O ANISOU 3398 O ILE A 334 17953 10830 10007 1453 898 439 O ATOM 3399 CB ILE A 334 4.764 18.717 17.430 1.00 99.46 C ANISOU 3399 CB ILE A 334 17172 10753 9865 1242 767 441 C ATOM 3400 CG1 ILE A 334 5.844 19.021 16.368 1.00100.39 C ANISOU 3400 CG1 ILE A 334 17429 10749 9965 1128 850 463 C ATOM 3401 CG2 ILE A 334 3.379 19.090 16.897 1.00101.15 C ANISOU 3401 CG2 ILE A 334 17452 11024 9954 1561 746 475 C ATOM 3402 CD1 ILE A 334 7.026 18.058 16.312 1.00106.40 C ANISOU 3402 CD1 ILE A 334 17992 11578 10859 876 818 429 C ATOM 3403 N ALA A 335 3.252 19.065 20.396 1.00 96.09 N ANISOU 3403 N ALA A 335 16670 10393 9447 1329 708 378 N ATOM 3404 CA ALA A 335 2.086 19.434 21.196 1.00 96.21 C ANISOU 3404 CA ALA A 335 16702 10451 9402 1507 689 370 C ATOM 3405 C ALA A 335 2.474 20.305 22.386 1.00100.30 C ANISOU 3405 C ALA A 335 17391 10813 9905 1399 762 348 C ATOM 3406 O ALA A 335 1.752 21.253 22.692 1.00100.78 O ANISOU 3406 O ALA A 335 17641 10794 9858 1570 813 361 O ATOM 3407 CB ALA A 335 1.363 18.189 21.678 1.00 95.68 C ANISOU 3407 CB ALA A 335 16319 10615 9419 1522 572 334 C ATOM 3408 N PHE A 336 3.604 19.983 23.056 1.00 96.63 N ANISOU 3408 N PHE A 336 16860 10317 9540 1127 767 311 N ATOM 3409 CA PHE A 336 4.102 20.717 24.224 1.00 97.38 C ANISOU 3409 CA PHE A 336 17088 10285 9626 985 831 274 C ATOM 3410 C PHE A 336 4.561 22.124 23.847 1.00103.34 C ANISOU 3410 C PHE A 336 18197 10797 10269 971 977 288 C ATOM 3411 O PHE A 336 4.257 23.069 24.579 1.00104.09 O ANISOU 3411 O PHE A 336 18491 10770 10289 1013 1047 276 O ATOM 3412 CB PHE A 336 5.247 19.962 24.933 1.00 98.17 C ANISOU 3412 CB PHE A 336 17008 10447 9847 706 794 225 C ATOM 3413 CG PHE A 336 4.886 18.696 25.684 1.00 98.45 C ANISOU 3413 CG PHE A 336 16746 10679 9982 692 675 205 C ATOM 3414 CD1 PHE A 336 3.601 18.502 26.186 1.00101.48 C ANISOU 3414 CD1 PHE A 336 17058 11155 10346 871 624 209 C ATOM 3415 CD2 PHE A 336 5.840 17.713 25.921 1.00 99.84 C ANISOU 3415 CD2 PHE A 336 16724 10948 10262 501 622 179 C ATOM 3416 CE1 PHE A 336 3.273 17.337 26.887 1.00101.37 C ANISOU 3416 CE1 PHE A 336 16791 11307 10417 841 533 188 C ATOM 3417 CE2 PHE A 336 5.512 16.549 26.625 1.00101.65 C ANISOU 3417 CE2 PHE A 336 16714 11337 10571 495 528 167 C ATOM 3418 CZ PHE A 336 4.231 16.369 27.103 1.00 99.58 C ANISOU 3418 CZ PHE A 336 16397 11149 10291 655 489 171 C ATOM 3419 N GLN A 337 5.268 22.267 22.705 1.00100.29 N ANISOU 3419 N GLN A 337 17904 10335 9865 913 1033 311 N ATOM 3420 CA GLN A 337 5.762 23.562 22.234 1.00101.99 C ANISOU 3420 CA GLN A 337 18477 10307 9969 882 1191 323 C ATOM 3421 C GLN A 337 4.609 24.461 21.752 1.00107.58 C ANISOU 3421 C GLN A 337 19437 10916 10524 1202 1245 385 C ATOM 3422 O GLN A 337 4.745 25.685 21.798 1.00109.28 O ANISOU 3422 O GLN A 337 19992 10904 10626 1213 1386 392 O ATOM 3423 CB GLN A 337 6.844 23.404 21.147 1.00103.51 C ANISOU 3423 CB GLN A 337 18689 10456 10183 724 1238 328 C ATOM 3424 CG GLN A 337 6.369 22.832 19.811 1.00119.61 C ANISOU 3424 CG GLN A 337 20647 12590 12211 910 1181 389 C ATOM 3425 CD GLN A 337 7.483 22.584 18.823 1.00141.34 C ANISOU 3425 CD GLN A 337 23392 15315 14996 737 1223 389 C ATOM 3426 OE1 GLN A 337 8.633 22.295 19.181 1.00136.93 O ANISOU 3426 OE1 GLN A 337 22738 14770 14521 462 1237 332 O ATOM 3427 NE2 GLN A 337 7.147 22.641 17.544 1.00134.82 N ANISOU 3427 NE2 GLN A 337 22649 14473 14102 906 1238 448 N ATOM 3428 N GLU A 338 3.480 23.855 21.323 1.00103.50 N ANISOU 3428 N GLU A 338 18754 10575 9996 1459 1138 421 N ATOM 3429 CA GLU A 338 2.286 24.569 20.869 1.00104.86 C ANISOU 3429 CA GLU A 338 19110 10717 10016 1802 1164 474 C ATOM 3430 C GLU A 338 1.518 25.150 22.063 1.00109.99 C ANISOU 3430 C GLU A 338 19837 11338 10614 1910 1177 454 C ATOM 3431 O GLU A 338 1.053 26.290 21.996 1.00111.26 O ANISOU 3431 O GLU A 338 20311 11337 10628 2099 1278 487 O ATOM 3432 CB GLU A 338 1.376 23.641 20.040 1.00105.50 C ANISOU 3432 CB GLU A 338 18941 11040 10102 2016 1037 499 C ATOM 3433 CG GLU A 338 0.253 24.359 19.302 1.00117.81 C ANISOU 3433 CG GLU A 338 20682 12596 11483 2388 1062 554 C ATOM 3434 CD GLU A 338 0.686 25.447 18.336 1.00138.25 C ANISOU 3434 CD GLU A 338 23651 14944 13935 2464 1204 614 C ATOM 3435 OE1 GLU A 338 1.446 25.141 17.389 1.00129.17 O ANISOU 3435 OE1 GLU A 338 22495 13768 12816 2348 1220 631 O ATOM 3436 OE2 GLU A 338 0.251 26.607 18.521 1.00132.62 O ANISOU 3436 OE2 GLU A 338 23254 14062 13074 2647 1306 645 O ATOM 3437 N LEU A 339 1.382 24.362 23.147 1.00105.56 N ANISOU 3437 N LEU A 339 19007 10933 10170 1799 1080 403 N ATOM 3438 CA LEU A 339 0.681 24.770 24.363 1.00105.75 C ANISOU 3438 CA LEU A 339 19063 10955 10162 1877 1081 376 C ATOM 3439 C LEU A 339 1.497 25.795 25.149 1.00111.40 C ANISOU 3439 C LEU A 339 20053 11428 10848 1690 1211 347 C ATOM 3440 O LEU A 339 0.912 26.678 25.777 1.00112.47 O ANISOU 3440 O LEU A 339 20390 11459 10886 1821 1275 346 O ATOM 3441 CB LEU A 339 0.343 23.557 25.245 1.00103.93 C ANISOU 3441 CB LEU A 339 18466 10961 10062 1799 946 330 C ATOM 3442 CG LEU A 339 -0.657 22.542 24.669 1.00107.69 C ANISOU 3442 CG LEU A 339 18664 11695 10559 1980 825 338 C ATOM 3443 CD1 LEU A 339 -0.784 21.343 25.574 1.00106.24 C ANISOU 3443 CD1 LEU A 339 18157 11702 10508 1846 720 289 C ATOM 3444 CD2 LEU A 339 -2.029 23.166 24.428 1.00111.41 C ANISOU 3444 CD2 LEU A 339 19230 12219 10882 2331 830 362 C ATOM 3445 N LEU A 340 2.840 25.702 25.086 1.00107.94 N ANISOU 3445 N LEU A 340 19625 10905 10482 1385 1256 316 N ATOM 3446 CA LEU A 340 3.733 26.646 25.762 1.00108.98 C ANISOU 3446 CA LEU A 340 20003 10821 10583 1162 1388 268 C ATOM 3447 C LEU A 340 4.021 27.874 24.870 1.00115.53 C ANISOU 3447 C LEU A 340 21241 11385 11272 1211 1560 305 C ATOM 3448 O LEU A 340 4.684 28.812 25.321 1.00116.35 O ANISOU 3448 O LEU A 340 21607 11278 11322 1037 1699 263 O ATOM 3449 CB LEU A 340 5.041 25.960 26.204 1.00107.73 C ANISOU 3449 CB LEU A 340 19643 10732 10559 807 1355 201 C ATOM 3450 CG LEU A 340 4.934 25.006 27.406 1.00110.64 C ANISOU 3450 CG LEU A 340 19696 11299 11042 721 1226 155 C ATOM 3451 CD1 LEU A 340 6.157 24.127 27.511 1.00109.52 C ANISOU 3451 CD1 LEU A 340 19323 11268 11022 439 1173 107 C ATOM 3452 CD2 LEU A 340 4.721 25.763 28.715 1.00113.58 C ANISOU 3452 CD2 LEU A 340 20207 11581 11367 689 1279 108 C ATOM 3453 N CYS A 341 3.471 27.879 23.628 1.00113.17 N ANISOU 3453 N CYS A 341 21004 11096 10900 1453 1555 380 N ATOM 3454 CA CYS A 341 3.574 28.937 22.610 1.00115.45 C ANISOU 3454 CA CYS A 341 21680 11149 11038 1565 1709 434 C ATOM 3455 C CYS A 341 5.053 29.305 22.347 1.00119.27 C ANISOU 3455 C CYS A 341 22317 11456 11544 1218 1839 391 C ATOM 3456 O CYS A 341 5.456 30.462 22.521 1.00120.71 O ANISOU 3456 O CYS A 341 22864 11376 11623 1131 2016 374 O ATOM 3457 CB CYS A 341 2.741 30.162 22.992 1.00118.15 C ANISOU 3457 CB CYS A 341 22373 11306 11213 1807 1819 462 C ATOM 3458 SG CYS A 341 1.033 29.786 23.477 1.00121.78 S ANISOU 3458 SG CYS A 341 22634 11998 11640 2193 1673 490 S ATOM 3459 N LEU A 342 5.853 28.299 21.938 1.00113.43 N ANISOU 3459 N LEU A 342 21293 10868 10935 1016 1757 368 N ATOM 3460 CA LEU A 342 7.281 28.453 21.652 1.00129.94 C ANISOU 3460 CA LEU A 342 23452 12857 13062 679 1857 315 C ATOM 3461 C LEU A 342 7.537 28.512 20.143 1.00157.06 C ANISOU 3461 C LEU A 342 27007 16227 16443 742 1914 376 C ATOM 3462 O LEU A 342 6.998 27.706 19.384 1.00115.03 O ANISOU 3462 O LEU A 342 21485 11072 11151 929 1794 431 O ATOM 3463 CB LEU A 342 8.100 27.307 22.281 1.00127.88 C ANISOU 3463 CB LEU A 342 22796 12817 12976 407 1733 241 C ATOM 3464 CG LEU A 342 7.899 27.015 23.774 1.00131.52 C ANISOU 3464 CG LEU A 342 23080 13387 13506 339 1651 182 C ATOM 3465 CD1 LEU A 342 8.375 25.625 24.114 1.00129.54 C ANISOU 3465 CD1 LEU A 342 22410 13396 13415 197 1493 146 C ATOM 3466 CD2 LEU A 342 8.616 28.031 24.648 1.00135.40 C ANISOU 3466 CD2 LEU A 342 23803 13697 13945 100 1794 100 C TER 3467 LEU A 342 HETATM 3468 C1 SNP A1201 1.915 1.723 49.718 1.00 96.76 C HETATM 3469 C2 SNP A1201 1.201 1.509 48.522 1.00 97.68 C HETATM 3470 C3 SNP A1201 0.399 0.383 48.364 1.00 97.62 C HETATM 3471 C4 SNP A1201 0.291 -0.545 49.390 1.00 97.42 C HETATM 3472 C5 SNP A1201 0.883 -1.310 51.606 1.00 97.51 C HETATM 3473 C6 SNP A1201 1.573 -1.157 52.800 1.00 97.52 C HETATM 3474 C7 SNP A1201 2.389 -0.053 52.985 1.00 97.71 C HETATM 3475 C8 SNP A1201 2.514 0.902 51.980 1.00 97.81 C HETATM 3476 C9 SNP A1201 1.823 0.770 50.759 1.00 97.61 C HETATM 3477 C10 SNP A1201 0.994 -0.364 50.584 1.00 97.52 C HETATM 3478 O1 SNP A1201 2.774 2.815 49.938 1.00 93.98 O HETATM 3479 C11 SNP A1201 2.346 4.131 49.559 1.00 92.89 C HETATM 3480 C12 SNP A1201 3.108 5.112 50.437 1.00 92.62 C HETATM 3481 O2 SNP A1201 3.566 6.201 49.632 1.00 92.80 O HETATM 3482 C13 SNP A1201 2.211 5.572 51.603 1.00 91.95 C HETATM 3483 N1 SNP A1201 2.676 6.816 52.244 1.00 91.04 N HETATM 3484 C14 SNP A1201 2.261 6.933 53.660 1.00 91.13 C HETATM 3485 C15 SNP A1201 3.347 7.709 54.403 1.00 91.36 C HETATM 3486 C16 SNP A1201 0.916 7.640 53.881 1.00 91.15 C HETATM 3487 S SO4 A1202 -2.770 2.393 19.485 1.00110.56 S HETATM 3488 O1 SO4 A1202 -1.964 3.117 18.501 1.00110.84 O HETATM 3489 O2 SO4 A1202 -4.196 2.513 19.159 1.00109.86 O HETATM 3490 O3 SO4 A1202 -2.379 0.988 19.479 1.00111.02 O HETATM 3491 O4 SO4 A1202 -2.530 2.950 20.812 1.00110.75 O HETATM 3492 S SO4 A1203 16.605 5.906 21.233 1.00170.79 S HETATM 3493 O1 SO4 A1203 16.946 7.062 20.410 1.00170.95 O HETATM 3494 O2 SO4 A1203 17.473 4.784 20.882 1.00170.84 O HETATM 3495 O3 SO4 A1203 15.211 5.537 20.994 1.00170.90 O HETATM 3496 O4 SO4 A1203 16.792 6.243 22.643 1.00170.95 O HETATM 3497 S SO4 A1204 36.854 -7.136 -2.404 1.00152.78 S HETATM 3498 O1 SO4 A1204 36.236 -5.881 -2.828 1.00153.00 O HETATM 3499 O2 SO4 A1204 37.302 -7.874 -3.585 1.00152.78 O HETATM 3500 O3 SO4 A1204 35.874 -7.937 -1.677 1.00152.92 O HETATM 3501 O4 SO4 A1204 37.995 -6.850 -1.531 1.00152.87 O HETATM 3502 S SO4 A1205 24.366 7.670 5.874 1.00178.29 S HETATM 3503 O1 SO4 A1205 24.755 9.045 5.570 1.00178.32 O HETATM 3504 O2 SO4 A1205 23.662 7.094 4.731 1.00178.48 O HETATM 3505 O3 SO4 A1205 25.563 6.885 6.151 1.00178.41 O HETATM 3506 O4 SO4 A1205 23.484 7.654 7.043 1.00178.24 O HETATM 3507 C1 CLR A1206 -12.145 9.374 30.361 1.00114.56 C HETATM 3508 C2 CLR A1206 -12.190 9.205 28.835 1.00115.27 C HETATM 3509 C3 CLR A1206 -10.821 9.347 28.164 1.00115.92 C HETATM 3510 C4 CLR A1206 -9.762 8.448 28.818 1.00115.42 C HETATM 3511 C5 CLR A1206 -9.803 8.489 30.343 1.00114.40 C HETATM 3512 C6 CLR A1206 -8.604 8.494 30.971 1.00113.77 C HETATM 3513 C7 CLR A1206 -8.420 8.826 32.442 1.00112.93 C HETATM 3514 C8 CLR A1206 -9.678 8.513 33.266 1.00111.75 C HETATM 3515 C9 CLR A1206 -10.920 9.086 32.539 1.00111.90 C HETATM 3516 C10 CLR A1206 -11.134 8.485 31.119 1.00113.56 C HETATM 3517 C11 CLR A1206 -12.185 9.016 33.437 1.00110.72 C HETATM 3518 C12 CLR A1206 -11.998 9.482 34.898 1.00109.70 C HETATM 3519 C13 CLR A1206 -10.812 8.817 35.625 1.00109.04 C HETATM 3520 C14 CLR A1206 -9.605 9.066 34.704 1.00110.17 C HETATM 3521 C15 CLR A1206 -8.390 8.701 35.552 1.00109.29 C HETATM 3522 C16 CLR A1206 -8.798 9.217 36.928 1.00108.59 C HETATM 3523 C17 CLR A1206 -10.294 9.581 36.881 1.00107.98 C HETATM 3524 C18 CLR A1206 -11.135 7.323 35.890 1.00108.40 C HETATM 3525 C19 CLR A1206 -11.634 7.029 31.166 1.00113.17 C HETATM 3526 C20 CLR A1206 -10.983 9.429 38.267 1.00105.87 C HETATM 3527 C21 CLR A1206 -12.486 9.731 38.281 1.00106.24 C HETATM 3528 C22 CLR A1206 -10.330 10.371 39.293 1.00103.31 C HETATM 3529 C23 CLR A1206 -10.231 9.817 40.714 1.00101.19 C HETATM 3530 C24 CLR A1206 -10.403 10.942 41.733 1.00 99.17 C HETATM 3531 C25 CLR A1206 -10.292 10.445 43.172 1.00 97.04 C HETATM 3532 C26 CLR A1206 -9.133 11.114 43.901 1.00 95.64 C HETATM 3533 C27 CLR A1206 -11.599 10.657 43.927 1.00 96.66 C HETATM 3534 O1 CLR A1206 -10.957 8.979 26.785 1.00116.39 O HETATM 3535 C1 OLA A1207 13.416 13.358 57.580 1.00123.56 C HETATM 3536 O1 OLA A1207 13.980 14.356 58.087 1.00124.22 O HETATM 3537 O2 OLA A1207 12.500 12.804 58.229 1.00124.00 O HETATM 3538 C2 OLA A1207 13.832 12.812 56.228 1.00121.97 C HETATM 3539 C3 OLA A1207 13.906 13.913 55.175 1.00120.40 C HETATM 3540 C4 OLA A1207 12.941 13.645 54.029 1.00119.56 C HETATM 3541 C5 OLA A1207 12.781 14.887 53.162 1.00118.94 C HETATM 3542 C6 OLA A1207 12.188 14.526 51.808 1.00118.68 C HETATM 3543 C7 OLA A1207 12.840 15.330 50.692 1.00119.05 C HETATM 3544 C8 OLA A1207 13.624 14.412 49.761 1.00119.56 C HETATM 3545 C9 OLA A1207 13.581 14.947 48.343 1.00119.85 C HETATM 3546 C10 OLA A1207 13.837 14.219 47.246 1.00120.02 C HETATM 3547 C11 OLA A1207 14.205 12.747 47.254 1.00120.14 C HETATM 3548 C12 OLA A1207 14.677 12.325 45.868 1.00120.20 C HETATM 3549 C1 OLA A1208 -6.471 24.834 30.926 1.00118.93 C HETATM 3550 O1 OLA A1208 -5.665 25.361 30.131 1.00119.13 O HETATM 3551 O2 OLA A1208 -7.026 23.766 30.580 1.00119.25 O HETATM 3552 C2 OLA A1208 -6.771 25.487 32.259 1.00118.14 C HETATM 3553 C3 OLA A1208 -6.497 24.524 33.411 1.00117.90 C HETATM 3554 C4 OLA A1208 -5.156 24.815 34.073 1.00117.85 C HETATM 3555 C5 OLA A1208 -5.346 25.124 35.555 1.00117.54 C HETATM 3556 C6 OLA A1208 -4.729 24.044 36.441 1.00116.73 C HETATM 3557 C7 OLA A1208 -5.436 23.977 37.794 1.00115.51 C HETATM 3558 C8 OLA A1208 -4.508 23.544 38.927 1.00114.86 C HETATM 3559 C9 OLA A1208 -3.779 24.748 39.497 1.00114.91 C HETATM 3560 C10 OLA A1208 -3.904 25.243 40.738 1.00114.78 C HETATM 3561 C11 OLA A1208 -4.804 24.698 41.829 1.00113.87 C HETATM 3562 C12 OLA A1208 -4.699 25.591 43.061 1.00112.84 C HETATM 3563 C10 OLC A1209 6.245 27.354 33.182 1.00106.37 C HETATM 3564 C9 OLC A1209 5.524 26.566 32.389 1.00106.64 C HETATM 3565 C8 OLC A1209 4.708 25.442 32.980 1.00107.26 C HETATM 3566 C24 OLC A1209 -5.488 26.423 25.363 1.00121.20 C HETATM 3567 C7 OLC A1209 3.265 25.907 33.139 1.00108.21 C HETATM 3568 C6 OLC A1209 2.325 25.118 32.238 1.00109.13 C HETATM 3569 C5 OLC A1209 0.873 25.461 32.544 1.00110.00 C HETATM 3570 C4 OLC A1209 -0.071 24.603 31.712 1.00111.50 C HETATM 3571 C3 OLC A1209 -0.915 25.457 30.776 1.00113.12 C HETATM 3572 C2 OLC A1209 -1.174 24.742 29.451 1.00114.82 C HETATM 3573 C21 OLC A1209 -3.545 25.717 26.787 1.00119.73 C HETATM 3574 C1 OLC A1209 -1.758 25.714 28.449 1.00117.03 C HETATM 3575 C22 OLC A1209 -5.032 26.067 26.778 1.00120.67 C HETATM 3576 O19 OLC A1209 -1.044 26.574 27.945 1.00117.36 O HETATM 3577 O25 OLC A1209 -5.841 25.252 24.616 1.00121.48 O HETATM 3578 O23 OLC A1209 -5.804 24.977 27.301 1.00120.84 O HETATM 3579 O20 OLC A1209 -3.060 25.647 28.135 1.00118.65 O HETATM 3580 C9 OLC A1210 -9.434 16.930 41.588 1.00111.84 C HETATM 3581 C8 OLC A1210 -9.603 15.878 40.517 1.00112.26 C HETATM 3582 C24 OLC A1210 -9.556 13.014 27.792 1.00121.31 C HETATM 3583 C7 OLC A1210 -8.907 16.325 39.235 1.00112.47 C HETATM 3584 C6 OLC A1210 -8.931 15.235 38.168 1.00112.60 C HETATM 3585 C5 OLC A1210 -9.943 15.562 37.076 1.00113.61 C HETATM 3586 C4 OLC A1210 -9.380 15.273 35.692 1.00114.50 C HETATM 3587 C3 OLC A1210 -10.169 14.165 35.001 1.00115.50 C HETATM 3588 C2 OLC A1210 -10.646 14.601 33.616 1.00117.10 C HETATM 3589 C21 OLC A1210 -9.797 13.383 30.254 1.00120.79 C HETATM 3590 C1 OLC A1210 -9.649 14.297 32.510 1.00119.03 C HETATM 3591 C22 OLC A1210 -10.201 13.886 28.869 1.00121.25 C HETATM 3592 O19 OLC A1210 -8.484 13.997 32.753 1.00119.48 O HETATM 3593 O25 OLC A1210 -10.179 13.242 26.520 1.00121.58 O HETATM 3594 O23 OLC A1210 -11.629 13.845 28.743 1.00121.68 O HETATM 3595 O20 OLC A1210 -10.048 14.396 31.236 1.00120.12 O HETATM 3596 C8 OLC A1211 -4.028 -9.692 34.306 1.00105.92 C HETATM 3597 C24 OLC A1211 -8.366 -8.425 23.847 1.00113.17 C HETATM 3598 C7 OLC A1211 -3.940 -8.337 33.612 1.00106.94 C HETATM 3599 C6 OLC A1211 -5.050 -8.172 32.577 1.00108.18 C HETATM 3600 C5 OLC A1211 -5.128 -6.740 32.057 1.00108.81 C HETATM 3601 C4 OLC A1211 -6.318 -6.559 31.122 1.00109.53 C HETATM 3602 C3 OLC A1211 -5.862 -6.090 29.746 1.00110.69 C HETATM 3603 C2 OLC A1211 -6.791 -6.610 28.649 1.00112.17 C HETATM 3604 C21 OLC A1211 -6.585 -8.274 25.606 1.00113.25 C HETATM 3605 C1 OLC A1211 -6.188 -6.538 27.255 1.00113.73 C HETATM 3606 C22 OLC A1211 -6.875 -8.232 24.108 1.00113.24 C HETATM 3607 O19 OLC A1211 -5.091 -6.033 27.045 1.00114.80 O HETATM 3608 O25 OLC A1211 -8.543 -9.294 22.721 1.00113.04 O HETATM 3609 O23 OLC A1211 -6.433 -6.992 23.541 1.00113.46 O HETATM 3610 O20 OLC A1211 -6.881 -7.013 26.214 1.00113.67 O HETATM 3611 C24 OLC A1212 -8.846 21.588 59.504 1.00138.23 C HETATM 3612 C5 OLC A1212 -11.475 19.229 51.775 1.00136.43 C HETATM 3613 C4 OLC A1212 -11.737 18.939 53.250 1.00136.70 C HETATM 3614 C3 OLC A1212 -10.717 19.636 54.146 1.00137.06 C HETATM 3615 C2 OLC A1212 -9.655 18.660 54.650 1.00137.24 C HETATM 3616 C21 OLC A1212 -8.586 20.645 57.208 1.00137.96 C HETATM 3617 C1 OLC A1212 -8.433 19.405 55.145 1.00137.13 C HETATM 3618 C22 OLC A1212 -8.350 20.397 58.693 1.00138.33 C HETATM 3619 O19 OLC A1212 -7.645 19.907 54.355 1.00136.77 O HETATM 3620 O25 OLC A1212 -8.702 21.317 60.904 1.00138.18 O HETATM 3621 O23 OLC A1212 -9.051 19.215 59.101 1.00138.83 O HETATM 3622 O20 OLC A1212 -8.188 19.497 56.453 1.00137.54 O CONECT 591 1282 CONECT 1228 1276 CONECT 1276 1228 CONECT 1282 591 CONECT 3468 3469 3476 3478 CONECT 3469 3468 3470 CONECT 3470 3469 3471 CONECT 3471 3470 3477 CONECT 3472 3473 3477 CONECT 3473 3472 3474 CONECT 3474 3473 3475 CONECT 3475 3474 3476 CONECT 3476 3468 3475 3477 CONECT 3477 3471 3472 3476 CONECT 3478 3468 3479 CONECT 3479 3478 3480 CONECT 3480 3479 3481 3482 CONECT 3481 3480 CONECT 3482 3480 3483 CONECT 3483 3482 3484 CONECT 3484 3483 3485 3486 CONECT 3485 3484 CONECT 3486 3484 CONECT 3487 3488 3489 3490 3491 CONECT 3488 3487 CONECT 3489 3487 CONECT 3490 3487 CONECT 3491 3487 CONECT 3492 3493 3494 3495 3496 CONECT 3493 3492 CONECT 3494 3492 CONECT 3495 3492 CONECT 3496 3492 CONECT 3497 3498 3499 3500 3501 CONECT 3498 3497 CONECT 3499 3497 CONECT 3500 3497 CONECT 3501 3497 CONECT 3502 3503 3504 3505 3506 CONECT 3503 3502 CONECT 3504 3502 CONECT 3505 3502 CONECT 3506 3502 CONECT 3507 3508 3516 CONECT 3508 3507 3509 CONECT 3509 3508 3510 3534 CONECT 3510 3509 3511 CONECT 3511 3510 3512 3516 CONECT 3512 3511 3513 CONECT 3513 3512 3514 CONECT 3514 3513 3515 3520 CONECT 3515 3514 3516 3517 CONECT 3516 3507 3511 3515 3525 CONECT 3517 3515 3518 CONECT 3518 3517 3519 CONECT 3519 3518 3520 3523 3524 CONECT 3520 3514 3519 3521 CONECT 3521 3520 3522 CONECT 3522 3521 3523 CONECT 3523 3519 3522 3526 CONECT 3524 3519 CONECT 3525 3516 CONECT 3526 3523 3527 3528 CONECT 3527 3526 CONECT 3528 3526 3529 CONECT 3529 3528 3530 CONECT 3530 3529 3531 CONECT 3531 3530 3532 3533 CONECT 3532 3531 CONECT 3533 3531 CONECT 3534 3509 CONECT 3535 3536 3537 3538 CONECT 3536 3535 CONECT 3537 3535 CONECT 3538 3535 3539 CONECT 3539 3538 3540 CONECT 3540 3539 3541 CONECT 3541 3540 3542 CONECT 3542 3541 3543 CONECT 3543 3542 3544 CONECT 3544 3543 3545 CONECT 3545 3544 3546 CONECT 3546 3545 3547 CONECT 3547 3546 3548 CONECT 3548 3547 CONECT 3549 3550 3551 3552 CONECT 3550 3549 CONECT 3551 3549 CONECT 3552 3549 3553 CONECT 3553 3552 3554 CONECT 3554 3553 3555 CONECT 3555 3554 3556 CONECT 3556 3555 3557 CONECT 3557 3556 3558 CONECT 3558 3557 3559 CONECT 3559 3558 3560 CONECT 3560 3559 3561 CONECT 3561 3560 3562 CONECT 3562 3561 CONECT 3563 3564 CONECT 3564 3563 3565 CONECT 3565 3564 3567 CONECT 3566 3575 3577 CONECT 3567 3565 3568 CONECT 3568 3567 3569 CONECT 3569 3568 3570 CONECT 3570 3569 3571 CONECT 3571 3570 3572 CONECT 3572 3571 3574 CONECT 3573 3575 3579 CONECT 3574 3572 3576 3579 CONECT 3575 3566 3573 3578 CONECT 3576 3574 CONECT 3577 3566 CONECT 3578 3575 CONECT 3579 3573 3574 CONECT 3580 3581 CONECT 3581 3580 3583 CONECT 3582 3591 3593 CONECT 3583 3581 3584 CONECT 3584 3583 3585 CONECT 3585 3584 3586 CONECT 3586 3585 3587 CONECT 3587 3586 3588 CONECT 3588 3587 3590 CONECT 3589 3591 3595 CONECT 3590 3588 3592 3595 CONECT 3591 3582 3589 3594 CONECT 3592 3590 CONECT 3593 3582 CONECT 3594 3591 CONECT 3595 3589 3590 CONECT 3596 3598 CONECT 3597 3606 3608 CONECT 3598 3596 3599 CONECT 3599 3598 3600 CONECT 3600 3599 3601 CONECT 3601 3600 3602 CONECT 3602 3601 3603 CONECT 3603 3602 3605 CONECT 3604 3606 3610 CONECT 3605 3603 3607 3610 CONECT 3606 3597 3604 3609 CONECT 3607 3605 CONECT 3608 3597 CONECT 3609 3606 CONECT 3610 3604 3605 CONECT 3611 3618 3620 CONECT 3612 3613 CONECT 3613 3612 3614 CONECT 3614 3613 3615 CONECT 3615 3614 3617 CONECT 3616 3618 3622 CONECT 3617 3615 3619 3622 CONECT 3618 3611 3616 3621 CONECT 3619 3617 CONECT 3620 3611 CONECT 3621 3618 CONECT 3622 3616 3617 MASTER 408 0 12 23 3 0 14 6 3621 1 159 39 END