HEADER PROTEIN TRANSPORT, HYDROLASE 23-NOV-07 3BG0 TITLE ARCHITECTURE OF A COAT FOR THE NUCLEAR PORE MEMBRANE COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN SEC13 HOMOLOG; COMPND 3 CHAIN: A, D, E, H; COMPND 4 SYNONYM: SEC13-RELATED PROTEIN, SEC13-LIKE PROTEIN 1; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: NUCLEOPORIN NUP145; COMPND 8 CHAIN: B, C, F, G; COMPND 9 FRAGMENT: NUCLEOPORIN NUP145C; COMPND 10 SYNONYM: NUCLEAR PORE PROTEIN NUP145; COMPND 11 EC: 3.4.21.-; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: SEC13, D3S1231E, SEC13L1, SEC13R; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS (DE3)-RIL; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24B; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; SOURCE 13 ORGANISM_COMMON: BAKER'S YEAST; SOURCE 14 ORGANISM_TAXID: 4932; SOURCE 15 GENE: NUP145, RAT10; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS (DE3)-RIL; SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PET; SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET-DUET1 KEYWDS NPC, TRANSPORT, WD REPEAT, AUTOCATALYTIC CLEAVAGE, MRNA KEYWDS 2 TRANSPORT, NUCLEAR PORE COMPLEX, NUCLEUS, PHOSPHOPROTEIN, KEYWDS 3 RNA-BINDING, TRANSLOCATION, PROTEIN TRANSPORT, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR A.HOELZ REVDAT 4 24-FEB-09 3BG0 1 VERSN REVDAT 3 15-JAN-08 3BG0 1 TITLE REVDAT 2 08-JAN-08 3BG0 1 JRNL REVDAT 1 01-JAN-08 3BG0 0 JRNL AUTH K.C.HSIA,P.STAVROPOULOS,G.BLOBEL,A.HOELZ JRNL TITL ARCHITECTURE OF A COAT FOR THE NUCLEAR PORE JRNL TITL 2 MEMBRANE. JRNL REF CELL(CAMBRIDGE,MASS.) V. 131 1313 2007 JRNL REFN ISSN 0092-8674 JRNL PMID 18160040 JRNL DOI 10.1016/J.CELL.2007.11.038 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.15 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.15 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.7 REMARK 3 NUMBER OF REFLECTIONS : 55955 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING SET) : 0.252 REMARK 3 FREE R VALUE : 0.294 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.500 REMARK 3 FREE R VALUE TEST SET COUNT : 2837 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 22566 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 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) : 153.30 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -36.43800 REMARK 3 B22 (A**2) : -43.02000 REMARK 3 B33 (A**2) : 79.45800 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -1.65200 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : NULL REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : 87.62 REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : CNS_TOPPAR:PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3BG0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-NOV-07. REMARK 100 THE RCSB ID CODE IS RCSB045473. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-OCT-06 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.7 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ALS REMARK 200 BEAMLINE : 8.2.2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55955 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.150 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 10.800 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.15 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.26 REMARK 200 COMPLETENESS FOR SHELL (%) : 77.7 REMARK 200 DATA REDUNDANCY IN SHELL : 6.20 REMARK 200 R MERGE FOR SHELL (I) : 0.74600 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: N/A REMARK 200 SOFTWARE USED: SHARP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.73 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 16 % (W/V) PEG 3,350, 400 MM NACL, REMARK 280 100 MM NA-K TARTRATE, AND 100 MM BIS-TRIS, PH 7.7, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 294K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 90.90900 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 108.28750 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 90.90900 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 108.28750 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 13700 ANGSTROM**2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D 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 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 13780 ANGSTROM**2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H 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 350 REMARK 350 BIOMOLECULE: 4 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5380 ANGSTROM**2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 5 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5220 ANGSTROM**2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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 350 REMARK 350 BIOMOLECULE: 6 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5430 ANGSTROM**2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F 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 350 REMARK 350 BIOMOLECULE: 7 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5190 ANGSTROM**2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H 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 1 REMARK 465 VAL A 2 REMARK 465 SER A 3 REMARK 465 VAL A 4 REMARK 465 ILE A 5 REMARK 465 ASN A 6 REMARK 465 THR A 7 REMARK 465 VAL A 8 REMARK 465 ASP A 9 REMARK 465 THR A 10 REMARK 465 SER A 11 REMARK 465 HIS A 12 REMARK 465 GLU A 13 REMARK 465 GLY A 165 REMARK 465 SER A 166 REMARK 465 LEU A 167 REMARK 465 ILE A 168 REMARK 465 ASP A 169 REMARK 465 HIS A 170 REMARK 465 PRO A 171 REMARK 465 SER A 172 REMARK 465 LYS A 305 REMARK 465 GLY A 306 REMARK 465 GLN A 307 REMARK 465 GLY A 308 REMARK 465 SER A 309 REMARK 465 VAL A 310 REMARK 465 SER A 311 REMARK 465 ALA A 312 REMARK 465 SER A 313 REMARK 465 VAL A 314 REMARK 465 THR A 315 REMARK 465 GLU A 316 REMARK 465 MET B 111 REMARK 465 GLY B 112 REMARK 465 SER B 113 REMARK 465 SER B 114 REMARK 465 HIS B 115 REMARK 465 HIS B 116 REMARK 465 HIS B 117 REMARK 465 HIS B 118 REMARK 465 HIS B 119 REMARK 465 HIS B 120 REMARK 465 SER B 121 REMARK 465 GLY B 122 REMARK 465 ASP B 123 REMARK 465 PRO B 124 REMARK 465 PHE B 125 REMARK 465 SER B 126 REMARK 465 GLU B 127 REMARK 465 CYS B 128 REMARK 465 ASN B 129 REMARK 465 MET C 111 REMARK 465 GLY C 112 REMARK 465 SER C 113 REMARK 465 SER C 114 REMARK 465 HIS C 115 REMARK 465 HIS C 116 REMARK 465 HIS C 117 REMARK 465 HIS C 118 REMARK 465 HIS C 119 REMARK 465 HIS C 120 REMARK 465 SER C 121 REMARK 465 GLY C 122 REMARK 465 ASP C 123 REMARK 465 PRO C 124 REMARK 465 PHE C 125 REMARK 465 SER C 126 REMARK 465 GLU C 127 REMARK 465 CYS C 128 REMARK 465 ASN C 129 REMARK 465 VAL C 165 REMARK 465 GLY C 166 REMARK 465 LYS C 167 REMARK 465 MET D 1 REMARK 465 VAL D 2 REMARK 465 SER D 3 REMARK 465 VAL D 4 REMARK 465 ILE D 5 REMARK 465 ASN D 6 REMARK 465 THR D 7 REMARK 465 VAL D 8 REMARK 465 ASP D 9 REMARK 465 THR D 10 REMARK 465 SER D 11 REMARK 465 HIS D 12 REMARK 465 GLU D 13 REMARK 465 GLY D 165 REMARK 465 SER D 166 REMARK 465 LEU D 167 REMARK 465 ILE D 168 REMARK 465 ASP D 169 REMARK 465 HIS D 170 REMARK 465 PRO D 171 REMARK 465 SER D 172 REMARK 465 VAL D 303 REMARK 465 ASN D 304 REMARK 465 LYS D 305 REMARK 465 GLY D 306 REMARK 465 GLN D 307 REMARK 465 GLY D 308 REMARK 465 SER D 309 REMARK 465 VAL D 310 REMARK 465 SER D 311 REMARK 465 ALA D 312 REMARK 465 SER D 313 REMARK 465 VAL D 314 REMARK 465 THR D 315 REMARK 465 GLU D 316 REMARK 465 MET E 1 REMARK 465 VAL E 2 REMARK 465 SER E 3 REMARK 465 VAL E 4 REMARK 465 ILE E 5 REMARK 465 ASN E 6 REMARK 465 THR E 7 REMARK 465 VAL E 8 REMARK 465 ASP E 9 REMARK 465 THR E 10 REMARK 465 SER E 11 REMARK 465 HIS E 12 REMARK 465 GLU E 13 REMARK 465 GLY E 165 REMARK 465 SER E 166 REMARK 465 LEU E 167 REMARK 465 ILE E 168 REMARK 465 ASP E 169 REMARK 465 HIS E 170 REMARK 465 PRO E 171 REMARK 465 SER E 172 REMARK 465 LYS E 305 REMARK 465 GLY E 306 REMARK 465 GLN E 307 REMARK 465 GLY E 308 REMARK 465 SER E 309 REMARK 465 VAL E 310 REMARK 465 SER E 311 REMARK 465 ALA E 312 REMARK 465 SER E 313 REMARK 465 VAL E 314 REMARK 465 THR E 315 REMARK 465 GLU E 316 REMARK 465 MET F 111 REMARK 465 GLY F 112 REMARK 465 SER F 113 REMARK 465 SER F 114 REMARK 465 HIS F 115 REMARK 465 HIS F 116 REMARK 465 HIS F 117 REMARK 465 HIS F 118 REMARK 465 HIS F 119 REMARK 465 HIS F 120 REMARK 465 SER F 121 REMARK 465 GLY F 122 REMARK 465 ASP F 123 REMARK 465 PRO F 124 REMARK 465 PHE F 125 REMARK 465 SER F 126 REMARK 465 GLU F 127 REMARK 465 CYS F 128 REMARK 465 ASN F 129 REMARK 465 MET G 111 REMARK 465 GLY G 112 REMARK 465 SER G 113 REMARK 465 SER G 114 REMARK 465 HIS G 115 REMARK 465 HIS G 116 REMARK 465 HIS G 117 REMARK 465 HIS G 118 REMARK 465 HIS G 119 REMARK 465 HIS G 120 REMARK 465 SER G 121 REMARK 465 GLY G 122 REMARK 465 ASP G 123 REMARK 465 PRO G 124 REMARK 465 PHE G 125 REMARK 465 SER G 126 REMARK 465 GLU G 127 REMARK 465 CYS G 128 REMARK 465 ASN G 129 REMARK 465 VAL G 165 REMARK 465 GLY G 166 REMARK 465 LYS G 167 REMARK 465 MET H 1 REMARK 465 VAL H 2 REMARK 465 SER H 3 REMARK 465 VAL H 4 REMARK 465 ILE H 5 REMARK 465 ASN H 6 REMARK 465 THR H 7 REMARK 465 VAL H 8 REMARK 465 ASP H 9 REMARK 465 THR H 10 REMARK 465 SER H 11 REMARK 465 HIS H 12 REMARK 465 GLU H 13 REMARK 465 GLY H 165 REMARK 465 SER H 166 REMARK 465 LEU H 167 REMARK 465 ILE H 168 REMARK 465 ASP H 169 REMARK 465 HIS H 170 REMARK 465 PRO H 171 REMARK 465 SER H 172 REMARK 465 VAL H 303 REMARK 465 ASN H 304 REMARK 465 LYS H 305 REMARK 465 GLY H 306 REMARK 465 GLN H 307 REMARK 465 GLY H 308 REMARK 465 SER H 309 REMARK 465 VAL H 310 REMARK 465 SER H 311 REMARK 465 ALA H 312 REMARK 465 SER H 313 REMARK 465 VAL H 314 REMARK 465 THR H 315 REMARK 465 GLU H 316 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 ARG B 441 CG CD NE CZ NH1 NH2 REMARK 480 GLU B 482 CD OE1 OE2 REMARK 480 TYR B 551 CG CD1 CD2 CE1 CE2 CZ OH REMARK 480 LEU B 552 CG CD1 CD2 REMARK 480 ARG C 441 CG CD NE CZ NH1 NH2 REMARK 480 GLU C 482 CD OE1 OE2 REMARK 480 TYR C 551 CG CD1 CD2 CE1 CE2 CZ OH REMARK 480 LEU C 552 CG CD1 CD2 REMARK 480 ARG F 441 CG CD NE CZ NH1 NH2 REMARK 480 GLU F 482 CD OE1 OE2 REMARK 480 TYR F 551 CG CD1 CD2 CE1 CE2 CZ OH REMARK 480 LEU F 552 CG CD1 CD2 REMARK 480 ARG G 441 CG CD NE CZ NH1 NH2 REMARK 480 GLU G 482 CD OE1 OE2 REMARK 480 TYR G 551 CG CD1 CD2 CE1 CE2 CZ OH REMARK 480 LEU G 552 CG CD1 CD2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 HIS A 17 -75.83 -99.43 REMARK 500 THR A 26 -60.37 -134.33 REMARK 500 VAL A 42 66.96 -108.63 REMARK 500 ASN A 44 66.21 80.93 REMARK 500 ILE A 48 87.79 -155.12 REMARK 500 TRP A 61 -86.81 -93.63 REMARK 500 PRO A 68 -10.11 -43.78 REMARK 500 ASN A 90 80.18 75.15 REMARK 500 HIS A 97 159.38 177.84 REMARK 500 ALA A 100 53.35 -117.32 REMARK 500 HIS A 114 -9.01 -50.63 REMARK 500 GLU A 137 -169.21 -119.35 REMARK 500 PRO A 160 153.38 -48.97 REMARK 500 LYS A 175 55.29 86.08 REMARK 500 PRO A 176 155.31 -36.64 REMARK 500 LYS A 180 87.15 -53.00 REMARK 500 SER A 184 118.03 179.73 REMARK 500 ASN A 189 -0.55 83.88 REMARK 500 GLU A 198 3.04 -51.53 REMARK 500 ALA A 210 -25.10 167.97 REMARK 500 ASP A 247 -164.52 -121.59 REMARK 500 SER A 249 15.06 51.54 REMARK 500 ASN A 251 -5.02 55.24 REMARK 500 SER A 271 -170.25 -61.22 REMARK 500 ASP A 283 35.32 -98.90 REMARK 500 VAL A 293 -8.03 -43.06 REMARK 500 ARG B 143 6.96 81.80 REMARK 500 ILE B 164 6.01 -67.83 REMARK 500 SER B 171 100.22 -51.51 REMARK 500 ARG B 181 100.97 -167.29 REMARK 500 LYS B 203 30.96 -81.27 REMARK 500 SER B 204 11.43 -157.48 REMARK 500 ASN B 205 -177.69 175.12 REMARK 500 LYS B 226 -0.65 -58.49 REMARK 500 ASN B 232 -72.42 -65.55 REMARK 500 PRO B 247 -85.51 -42.22 REMARK 500 ARG B 267 -38.22 -37.58 REMARK 500 ASP B 302 76.35 -101.53 REMARK 500 LYS B 314 43.39 75.14 REMARK 500 THR B 345 -88.58 -67.44 REMARK 500 SER B 349 40.11 -88.86 REMARK 500 PHE B 370 36.01 -152.06 REMARK 500 SER B 371 157.52 -18.84 REMARK 500 GLU B 396 104.83 -56.93 REMARK 500 SER B 398 129.62 -33.83 REMARK 500 PRO B 413 127.23 -35.92 REMARK 500 THR B 442 36.57 -71.19 REMARK 500 LEU B 486 41.70 -107.03 REMARK 500 HIS B 487 -39.17 -39.66 REMARK 500 ARG B 519 -122.41 -105.71 REMARK 500 ALA B 520 -24.14 -30.12 REMARK 500 THR B 522 38.38 -68.67 REMARK 500 ASN B 523 6.79 88.77 REMARK 500 ASP B 524 73.29 50.73 REMARK 500 HIS B 525 -31.78 161.40 REMARK 500 ILE B 526 -57.17 -21.46 REMARK 500 LYS C 203 31.03 -81.21 REMARK 500 SER C 204 11.41 -157.57 REMARK 500 ASN C 205 -177.68 175.06 REMARK 500 LYS C 226 -0.53 -58.58 REMARK 500 ASN C 232 -72.40 -65.66 REMARK 500 ARG C 267 -38.13 -37.73 REMARK 500 SER C 288 -48.81 -132.48 REMARK 500 ASP C 302 62.95 -115.99 REMARK 500 LYS C 314 43.28 75.22 REMARK 500 THR C 345 -91.97 -67.24 REMARK 500 PHE C 370 35.91 -152.03 REMARK 500 SER C 371 157.52 -18.70 REMARK 500 GLN C 393 74.60 -39.79 REMARK 500 ASP C 395 -153.29 85.05 REMARK 500 THR C 442 36.52 -70.90 REMARK 500 LEU C 486 71.84 -104.09 REMARK 500 PHE C 496 8.30 -66.64 REMARK 500 ASP C 500 -28.55 -29.88 REMARK 500 ARG C 519 -122.64 -105.80 REMARK 500 ALA C 520 -24.06 -30.01 REMARK 500 THR C 522 38.45 -68.73 REMARK 500 ASN C 523 6.77 88.78 REMARK 500 ASP C 524 73.37 50.58 REMARK 500 HIS C 525 -31.72 161.40 REMARK 500 ILE C 526 -57.12 -21.42 REMARK 500 HIS D 17 -75.79 -99.39 REMARK 500 THR D 26 -60.14 -134.11 REMARK 500 VAL D 42 66.99 -108.47 REMARK 500 ASN D 44 66.22 81.00 REMARK 500 ILE D 48 87.97 -155.24 REMARK 500 TRP D 61 -86.98 -93.53 REMARK 500 PRO D 68 -10.16 -43.84 REMARK 500 ASN D 90 80.09 75.32 REMARK 500 HIS D 97 159.43 177.85 REMARK 500 ALA D 100 53.25 -117.23 REMARK 500 HIS D 114 -9.01 -50.55 REMARK 500 GLU D 137 -169.08 -119.31 REMARK 500 LYS D 175 55.28 86.13 REMARK 500 PRO D 176 155.34 -36.70 REMARK 500 LYS D 180 87.20 -53.03 REMARK 500 SER D 184 118.04 179.82 REMARK 500 ASN D 189 -0.39 83.67 REMARK 500 GLU D 196 114.46 -161.58 REMARK 500 ALA D 210 -25.23 167.91 REMARK 500 SER D 250 26.82 91.95 REMARK 500 ASN D 251 -173.73 51.14 REMARK 500 THR D 252 101.04 -160.92 REMARK 500 SER D 271 -170.12 -61.42 REMARK 500 ASP D 283 35.31 -98.86 REMARK 500 VAL D 293 -8.03 -42.93 REMARK 500 HIS E 17 -75.83 -99.56 REMARK 500 THR E 26 -60.32 -134.27 REMARK 500 VAL E 42 66.97 -108.62 REMARK 500 ASN E 44 66.15 80.92 REMARK 500 ILE E 48 87.87 -155.22 REMARK 500 TRP E 61 -86.82 -93.60 REMARK 500 PRO E 68 -10.13 -43.80 REMARK 500 ASN E 90 80.21 75.22 REMARK 500 HIS E 97 159.46 177.87 REMARK 500 ALA E 100 53.37 -117.28 REMARK 500 HIS E 114 -8.89 -50.43 REMARK 500 GLU E 137 -169.10 -119.32 REMARK 500 PRO E 160 150.81 -49.01 REMARK 500 LYS E 175 55.27 86.11 REMARK 500 PRO E 176 155.34 -36.68 REMARK 500 LYS E 180 87.10 -52.93 REMARK 500 SER E 184 117.40 179.74 REMARK 500 ASN E 189 -0.54 83.89 REMARK 500 GLU E 198 3.07 -51.43 REMARK 500 ALA E 210 -24.92 168.21 REMARK 500 SER E 249 -1.92 108.35 REMARK 500 THR E 252 79.64 -158.61 REMARK 500 SER E 271 -170.17 -60.85 REMARK 500 ASP E 283 35.38 -98.87 REMARK 500 VAL E 293 -8.12 -43.19 REMARK 500 ARG F 143 6.98 81.60 REMARK 500 ILE F 164 6.01 -67.97 REMARK 500 SER F 171 100.08 -51.57 REMARK 500 ARG F 181 100.54 -162.82 REMARK 500 LYS F 203 30.91 -81.21 REMARK 500 SER F 204 11.59 -157.51 REMARK 500 ASN F 205 -177.74 174.98 REMARK 500 LYS F 226 -0.56 -58.34 REMARK 500 ASN F 232 -72.47 -65.44 REMARK 500 ARG F 267 -38.08 -37.57 REMARK 500 SER F 288 28.73 -78.03 REMARK 500 LYS F 314 43.47 75.17 REMARK 500 THR F 345 -95.53 -67.37 REMARK 500 CYS F 348 -169.54 -115.32 REMARK 500 PHE F 370 36.08 -151.97 REMARK 500 SER F 371 157.47 -18.77 REMARK 500 TRP F 381 -36.08 -37.97 REMARK 500 GLN F 393 102.33 -52.68 REMARK 500 THR F 442 36.49 -70.95 REMARK 500 GLN F 485 30.81 36.17 REMARK 500 LEU F 486 66.46 -108.66 REMARK 500 HIS F 487 11.46 -64.20 REMARK 500 SER F 490 -76.95 -54.09 REMARK 500 ARG F 519 -122.44 -105.83 REMARK 500 ALA F 520 -24.06 -30.12 REMARK 500 THR F 522 38.45 -68.72 REMARK 500 ASN F 523 6.80 88.75 REMARK 500 ASP F 524 73.31 50.58 REMARK 500 HIS F 525 -31.81 161.50 REMARK 500 ILE F 526 -57.31 -21.37 REMARK 500 GLN G 180 55.61 -115.17 REMARK 500 LYS G 203 30.91 -81.10 REMARK 500 SER G 204 11.59 -157.57 REMARK 500 ASN G 205 -177.73 174.90 REMARK 500 LYS G 226 -0.66 -58.60 REMARK 500 ASN G 232 -72.46 -65.59 REMARK 500 PRO G 247 -19.25 -44.01 REMARK 500 ARG G 267 -38.27 -37.73 REMARK 500 SER G 287 135.35 -37.44 REMARK 500 SER G 288 -63.87 -142.50 REMARK 500 LYS G 314 43.38 75.19 REMARK 500 THR G 345 -91.80 -66.93 REMARK 500 PHE G 370 35.94 -151.99 REMARK 500 SER G 371 157.54 -18.79 REMARK 500 ASP G 395 126.09 -14.95 REMARK 500 SER G 398 145.16 -38.86 REMARK 500 THR G 442 36.48 -70.87 REMARK 500 GLN G 485 13.71 56.51 REMARK 500 LEU G 491 -72.45 -65.51 REMARK 500 PHE G 496 6.02 -60.88 REMARK 500 ASP G 499 98.76 -66.10 REMARK 500 ARG G 519 -122.48 -105.83 REMARK 500 ALA G 520 -24.10 -30.08 REMARK 500 THR G 522 38.39 -68.77 REMARK 500 ASN G 523 6.67 88.84 REMARK 500 ASP G 524 73.27 50.70 REMARK 500 HIS G 525 -31.82 161.49 REMARK 500 ILE G 526 -57.24 -21.31 REMARK 500 HIS H 17 -75.73 -99.46 REMARK 500 THR H 26 -60.15 -134.06 REMARK 500 VAL H 42 67.01 -108.48 REMARK 500 ASN H 44 66.11 81.03 REMARK 500 ILE H 48 88.05 -155.25 REMARK 500 TRP H 61 -86.94 -93.52 REMARK 500 PRO H 68 -10.03 -43.93 REMARK 500 ASN H 90 80.20 75.20 REMARK 500 HIS H 97 159.43 177.86 REMARK 500 ALA H 100 53.28 -117.18 REMARK 500 HIS H 114 -8.88 -50.54 REMARK 500 GLU H 137 -169.02 -119.28 REMARK 500 LYS H 175 55.28 86.10 REMARK 500 PRO H 176 155.29 -36.64 REMARK 500 LYS H 180 87.18 -53.09 REMARK 500 SER H 184 117.95 179.81 REMARK 500 ASN H 189 -0.43 83.72 REMARK 500 GLU H 198 134.95 -24.95 REMARK 500 ASP H 199 -18.71 99.06 REMARK 500 ALA H 210 -25.22 167.88 REMARK 500 SER H 249 155.36 177.88 REMARK 500 SER H 271 -170.22 -61.46 REMARK 500 ASP H 283 35.33 -98.97 REMARK 500 GLN H 296 107.71 -168.21 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3BG1 RELATED DB: PDB DBREF 3BG0 A 1 316 UNP P55735 SEC13_HUMAN 1 316 DBREF 3BG0 B 125 552 UNP P49687 NU145_YEAST 731 1158 DBREF 3BG0 C 125 552 UNP P49687 NU145_YEAST 731 1158 DBREF 3BG0 D 1 316 UNP P55735 SEC13_HUMAN 1 316 DBREF 3BG0 E 1 316 UNP P55735 SEC13_HUMAN 1 316 DBREF 3BG0 F 125 552 UNP P49687 NU145_YEAST 731 1158 DBREF 3BG0 G 125 552 UNP P49687 NU145_YEAST 731 1158 DBREF 3BG0 H 1 316 UNP P55735 SEC13_HUMAN 1 316 SEQADV 3BG0 MET B 111 UNP P49687 EXPRESSION TAG SEQADV 3BG0 GLY B 112 UNP P49687 EXPRESSION TAG SEQADV 3BG0 SER B 113 UNP P49687 EXPRESSION TAG SEQADV 3BG0 SER B 114 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS B 115 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS B 116 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS B 117 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS B 118 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS B 119 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS B 120 UNP P49687 EXPRESSION TAG SEQADV 3BG0 SER B 121 UNP P49687 EXPRESSION TAG SEQADV 3BG0 GLY B 122 UNP P49687 EXPRESSION TAG SEQADV 3BG0 ASP B 123 UNP P49687 EXPRESSION TAG SEQADV 3BG0 PRO B 124 UNP P49687 EXPRESSION TAG SEQADV 3BG0 MET C 111 UNP P49687 EXPRESSION TAG SEQADV 3BG0 GLY C 112 UNP P49687 EXPRESSION TAG SEQADV 3BG0 SER C 113 UNP P49687 EXPRESSION TAG SEQADV 3BG0 SER C 114 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS C 115 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS C 116 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS C 117 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS C 118 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS C 119 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS C 120 UNP P49687 EXPRESSION TAG SEQADV 3BG0 SER C 121 UNP P49687 EXPRESSION TAG SEQADV 3BG0 GLY C 122 UNP P49687 EXPRESSION TAG SEQADV 3BG0 ASP C 123 UNP P49687 EXPRESSION TAG SEQADV 3BG0 PRO C 124 UNP P49687 EXPRESSION TAG SEQADV 3BG0 MET F 111 UNP P49687 EXPRESSION TAG SEQADV 3BG0 GLY F 112 UNP P49687 EXPRESSION TAG SEQADV 3BG0 SER F 113 UNP P49687 EXPRESSION TAG SEQADV 3BG0 SER F 114 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS F 115 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS F 116 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS F 117 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS F 118 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS F 119 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS F 120 UNP P49687 EXPRESSION TAG SEQADV 3BG0 SER F 121 UNP P49687 EXPRESSION TAG SEQADV 3BG0 GLY F 122 UNP P49687 EXPRESSION TAG SEQADV 3BG0 ASP F 123 UNP P49687 EXPRESSION TAG SEQADV 3BG0 PRO F 124 UNP P49687 EXPRESSION TAG SEQADV 3BG0 MET G 111 UNP P49687 EXPRESSION TAG SEQADV 3BG0 GLY G 112 UNP P49687 EXPRESSION TAG SEQADV 3BG0 SER G 113 UNP P49687 EXPRESSION TAG SEQADV 3BG0 SER G 114 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS G 115 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS G 116 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS G 117 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS G 118 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS G 119 UNP P49687 EXPRESSION TAG SEQADV 3BG0 HIS G 120 UNP P49687 EXPRESSION TAG SEQADV 3BG0 SER G 121 UNP P49687 EXPRESSION TAG SEQADV 3BG0 GLY G 122 UNP P49687 EXPRESSION TAG SEQADV 3BG0 ASP G 123 UNP P49687 EXPRESSION TAG SEQADV 3BG0 PRO G 124 UNP P49687 EXPRESSION TAG SEQRES 1 A 316 MET VAL SER VAL ILE ASN THR VAL ASP THR SER HIS GLU SEQRES 2 A 316 ASP MET ILE HIS ASP ALA GLN MET ASP TYR TYR GLY THR SEQRES 3 A 316 ARG LEU ALA THR CYS SER SER ASP ARG SER VAL LYS ILE SEQRES 4 A 316 PHE ASP VAL ARG ASN GLY GLY GLN ILE LEU ILE ALA ASP SEQRES 5 A 316 LEU ARG GLY HIS GLU GLY PRO VAL TRP GLN VAL ALA TRP SEQRES 6 A 316 ALA HIS PRO MET TYR GLY ASN ILE LEU ALA SER CYS SER SEQRES 7 A 316 TYR ASP ARG LYS VAL ILE ILE TRP ARG GLU GLU ASN GLY SEQRES 8 A 316 THR TRP GLU LYS SER HIS GLU HIS ALA GLY HIS ASP SER SEQRES 9 A 316 SER VAL ASN SER VAL CYS TRP ALA PRO HIS ASP TYR GLY SEQRES 10 A 316 LEU ILE LEU ALA CYS GLY SER SER ASP GLY ALA ILE SER SEQRES 11 A 316 LEU LEU THR TYR THR GLY GLU GLY GLN TRP GLU VAL LYS SEQRES 12 A 316 LYS ILE ASN ASN ALA HIS THR ILE GLY CYS ASN ALA VAL SEQRES 13 A 316 SER TRP ALA PRO ALA VAL VAL PRO GLY SER LEU ILE ASP SEQRES 14 A 316 HIS PRO SER GLY GLN LYS PRO ASN TYR ILE LYS ARG PHE SEQRES 15 A 316 ALA SER GLY GLY CYS ASP ASN LEU ILE LYS LEU TRP LYS SEQRES 16 A 316 GLU GLU GLU ASP GLY GLN TRP LYS GLU GLU GLN LYS LEU SEQRES 17 A 316 GLU ALA HIS SER ASP TRP VAL ARG ASP VAL ALA TRP ALA SEQRES 18 A 316 PRO SER ILE GLY LEU PRO THR SER THR ILE ALA SER CYS SEQRES 19 A 316 SER GLN ASP GLY ARG VAL PHE ILE TRP THR CYS ASP ASP SEQRES 20 A 316 ALA SER SER ASN THR TRP SER PRO LYS LEU LEU HIS LYS SEQRES 21 A 316 PHE ASN ASP VAL VAL TRP HIS VAL SER TRP SER ILE THR SEQRES 22 A 316 ALA ASN ILE LEU ALA VAL SER GLY GLY ASP ASN LYS VAL SEQRES 23 A 316 THR LEU TRP LYS GLU SER VAL ASP GLY GLN TRP VAL CYS SEQRES 24 A 316 ILE SER ASP VAL ASN LYS GLY GLN GLY SER VAL SER ALA SEQRES 25 A 316 SER VAL THR GLU SEQRES 1 B 442 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLY ASP SEQRES 2 B 442 PRO PHE SER GLU CYS ASN ASP GLU ILE ASP ASN ALA LYS SEQRES 3 B 442 LEU ILE MET LYS GLU ARG ARG PHE THR ALA SER TYR THR SEQRES 4 B 442 PHE ALA LYS PHE SER THR GLY SER MET LEU LEU THR LYS SEQRES 5 B 442 ASP ILE VAL GLY LYS SER GLY VAL SER ILE LYS ARG LEU SEQRES 6 B 442 PRO THR GLU LEU GLN ARG LYS PHE LEU PHE ASP ASP VAL SEQRES 7 B 442 TYR LEU ASP LYS GLU ILE GLU LYS VAL THR ILE GLU ALA SEQRES 8 B 442 ARG LYS SER ASN PRO TYR PRO GLN ILE SER GLU SER SER SEQRES 9 B 442 LEU LEU PHE LYS ASP ALA LEU ASP TYR MET GLU LYS THR SEQRES 10 B 442 SER SER ASP TYR ASN LEU TRP LYS LEU SER SER ILE LEU SEQRES 11 B 442 PHE ASP PRO VAL SER TYR PRO TYR LYS THR ASP ASN ASP SEQRES 12 B 442 GLN VAL LYS MET ALA LEU LEU LYS LYS GLU ARG HIS CYS SEQRES 13 B 442 ARG LEU THR SER TRP ILE VAL SER GLN ILE GLY PRO GLU SEQRES 14 B 442 ILE GLU GLU LYS ILE ARG ASN SER SER ASN GLU ILE GLU SEQRES 15 B 442 GLN ILE PHE LEU TYR LEU LEU LEU ASN ASP VAL VAL ARG SEQRES 16 B 442 ALA SER LYS LEU ALA ILE GLU SER LYS ASN GLY HIS LEU SEQRES 17 B 442 SER VAL LEU ILE SER TYR LEU GLY SER ASN ASP PRO ARG SEQRES 18 B 442 ILE ARG ASP LEU ALA GLU LEU GLN LEU GLN LYS TRP SER SEQRES 19 B 442 THR GLY GLY CYS SER ILE ASP LYS ASN ILE SER LYS ILE SEQRES 20 B 442 TYR LYS LEU LEU SER GLY SER PRO PHE GLU GLY LEU PHE SEQRES 21 B 442 SER LEU LYS GLU LEU GLU SER GLU PHE SER TRP LEU CYS SEQRES 22 B 442 LEU LEU ASN LEU THR LEU CYS TYR GLY GLN ILE ASP GLU SEQRES 23 B 442 TYR SER LEU GLU SER LEU VAL GLN SER HIS LEU ASP LYS SEQRES 24 B 442 PHE SER LEU PRO TYR ASP ASP PRO ILE GLY VAL ILE PHE SEQRES 25 B 442 GLN LEU TYR ALA ALA ASN GLU ASN THR GLU LYS LEU TYR SEQRES 26 B 442 LYS GLU VAL ARG GLN ARG THR ASN ALA LEU ASP VAL GLN SEQRES 27 B 442 PHE CYS TRP TYR LEU ILE GLN THR LEU ARG PHE ASN GLY SEQRES 28 B 442 THR ARG VAL PHE SER LYS GLU THR SER ASP GLU ALA THR SEQRES 29 B 442 PHE ALA PHE ALA ALA GLN LEU GLU PHE ALA GLN LEU HIS SEQRES 30 B 442 GLY HIS SER LEU PHE VAL SER CYS PHE LEU ASN ASP ASP SEQRES 31 B 442 LYS ALA ALA GLU ASP THR ILE LYS ARG LEU VAL MET ARG SEQRES 32 B 442 GLU ILE THR LEU LEU ARG ALA SER THR ASN ASP HIS ILE SEQRES 33 B 442 LEU ASN ARG LEU LYS ILE PRO SER GLN LEU ILE PHE ASN SEQRES 34 B 442 ALA GLN ALA LEU LYS ASP ARG TYR GLU GLY ASN TYR LEU SEQRES 1 C 442 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLY ASP SEQRES 2 C 442 PRO PHE SER GLU CYS ASN ASP GLU ILE ASP ASN ALA LYS SEQRES 3 C 442 LEU ILE MET LYS GLU ARG ARG PHE THR ALA SER TYR THR SEQRES 4 C 442 PHE ALA LYS PHE SER THR GLY SER MET LEU LEU THR LYS SEQRES 5 C 442 ASP ILE VAL GLY LYS SER GLY VAL SER ILE LYS ARG LEU SEQRES 6 C 442 PRO THR GLU LEU GLN ARG LYS PHE LEU PHE ASP ASP VAL SEQRES 7 C 442 TYR LEU ASP LYS GLU ILE GLU LYS VAL THR ILE GLU ALA SEQRES 8 C 442 ARG LYS SER ASN PRO TYR PRO GLN ILE SER GLU SER SER SEQRES 9 C 442 LEU LEU PHE LYS ASP ALA LEU ASP TYR MET GLU LYS THR SEQRES 10 C 442 SER SER ASP TYR ASN LEU TRP LYS LEU SER SER ILE LEU SEQRES 11 C 442 PHE ASP PRO VAL SER TYR PRO TYR LYS THR ASP ASN ASP SEQRES 12 C 442 GLN VAL LYS MET ALA LEU LEU LYS LYS GLU ARG HIS CYS SEQRES 13 C 442 ARG LEU THR SER TRP ILE VAL SER GLN ILE GLY PRO GLU SEQRES 14 C 442 ILE GLU GLU LYS ILE ARG ASN SER SER ASN GLU ILE GLU SEQRES 15 C 442 GLN ILE PHE LEU TYR LEU LEU LEU ASN ASP VAL VAL ARG SEQRES 16 C 442 ALA SER LYS LEU ALA ILE GLU SER LYS ASN GLY HIS LEU SEQRES 17 C 442 SER VAL LEU ILE SER TYR LEU GLY SER ASN ASP PRO ARG SEQRES 18 C 442 ILE ARG ASP LEU ALA GLU LEU GLN LEU GLN LYS TRP SER SEQRES 19 C 442 THR GLY GLY CYS SER ILE ASP LYS ASN ILE SER LYS ILE SEQRES 20 C 442 TYR LYS LEU LEU SER GLY SER PRO PHE GLU GLY LEU PHE SEQRES 21 C 442 SER LEU LYS GLU LEU GLU SER GLU PHE SER TRP LEU CYS SEQRES 22 C 442 LEU LEU ASN LEU THR LEU CYS TYR GLY GLN ILE ASP GLU SEQRES 23 C 442 TYR SER LEU GLU SER LEU VAL GLN SER HIS LEU ASP LYS SEQRES 24 C 442 PHE SER LEU PRO TYR ASP ASP PRO ILE GLY VAL ILE PHE SEQRES 25 C 442 GLN LEU TYR ALA ALA ASN GLU ASN THR GLU LYS LEU TYR SEQRES 26 C 442 LYS GLU VAL ARG GLN ARG THR ASN ALA LEU ASP VAL GLN SEQRES 27 C 442 PHE CYS TRP TYR LEU ILE GLN THR LEU ARG PHE ASN GLY SEQRES 28 C 442 THR ARG VAL PHE SER LYS GLU THR SER ASP GLU ALA THR SEQRES 29 C 442 PHE ALA PHE ALA ALA GLN LEU GLU PHE ALA GLN LEU HIS SEQRES 30 C 442 GLY HIS SER LEU PHE VAL SER CYS PHE LEU ASN ASP ASP SEQRES 31 C 442 LYS ALA ALA GLU ASP THR ILE LYS ARG LEU VAL MET ARG SEQRES 32 C 442 GLU ILE THR LEU LEU ARG ALA SER THR ASN ASP HIS ILE SEQRES 33 C 442 LEU ASN ARG LEU LYS ILE PRO SER GLN LEU ILE PHE ASN SEQRES 34 C 442 ALA GLN ALA LEU LYS ASP ARG TYR GLU GLY ASN TYR LEU SEQRES 1 D 316 MET VAL SER VAL ILE ASN THR VAL ASP THR SER HIS GLU SEQRES 2 D 316 ASP MET ILE HIS ASP ALA GLN MET ASP TYR TYR GLY THR SEQRES 3 D 316 ARG LEU ALA THR CYS SER SER ASP ARG SER VAL LYS ILE SEQRES 4 D 316 PHE ASP VAL ARG ASN GLY GLY GLN ILE LEU ILE ALA ASP SEQRES 5 D 316 LEU ARG GLY HIS GLU GLY PRO VAL TRP GLN VAL ALA TRP SEQRES 6 D 316 ALA HIS PRO MET TYR GLY ASN ILE LEU ALA SER CYS SER SEQRES 7 D 316 TYR ASP ARG LYS VAL ILE ILE TRP ARG GLU GLU ASN GLY SEQRES 8 D 316 THR TRP GLU LYS SER HIS GLU HIS ALA GLY HIS ASP SER SEQRES 9 D 316 SER VAL ASN SER VAL CYS TRP ALA PRO HIS ASP TYR GLY SEQRES 10 D 316 LEU ILE LEU ALA CYS GLY SER SER ASP GLY ALA ILE SER SEQRES 11 D 316 LEU LEU THR TYR THR GLY GLU GLY GLN TRP GLU VAL LYS SEQRES 12 D 316 LYS ILE ASN ASN ALA HIS THR ILE GLY CYS ASN ALA VAL SEQRES 13 D 316 SER TRP ALA PRO ALA VAL VAL PRO GLY SER LEU ILE ASP SEQRES 14 D 316 HIS PRO SER GLY GLN LYS PRO ASN TYR ILE LYS ARG PHE SEQRES 15 D 316 ALA SER GLY GLY CYS ASP ASN LEU ILE LYS LEU TRP LYS SEQRES 16 D 316 GLU GLU GLU ASP GLY GLN TRP LYS GLU GLU GLN LYS LEU SEQRES 17 D 316 GLU ALA HIS SER ASP TRP VAL ARG ASP VAL ALA TRP ALA SEQRES 18 D 316 PRO SER ILE GLY LEU PRO THR SER THR ILE ALA SER CYS SEQRES 19 D 316 SER GLN ASP GLY ARG VAL PHE ILE TRP THR CYS ASP ASP SEQRES 20 D 316 ALA SER SER ASN THR TRP SER PRO LYS LEU LEU HIS LYS SEQRES 21 D 316 PHE ASN ASP VAL VAL TRP HIS VAL SER TRP SER ILE THR SEQRES 22 D 316 ALA ASN ILE LEU ALA VAL SER GLY GLY ASP ASN LYS VAL SEQRES 23 D 316 THR LEU TRP LYS GLU SER VAL ASP GLY GLN TRP VAL CYS SEQRES 24 D 316 ILE SER ASP VAL ASN LYS GLY GLN GLY SER VAL SER ALA SEQRES 25 D 316 SER VAL THR GLU SEQRES 1 E 316 MET VAL SER VAL ILE ASN THR VAL ASP THR SER HIS GLU SEQRES 2 E 316 ASP MET ILE HIS ASP ALA GLN MET ASP TYR TYR GLY THR SEQRES 3 E 316 ARG LEU ALA THR CYS SER SER ASP ARG SER VAL LYS ILE SEQRES 4 E 316 PHE ASP VAL ARG ASN GLY GLY GLN ILE LEU ILE ALA ASP SEQRES 5 E 316 LEU ARG GLY HIS GLU GLY PRO VAL TRP GLN VAL ALA TRP SEQRES 6 E 316 ALA HIS PRO MET TYR GLY ASN ILE LEU ALA SER CYS SER SEQRES 7 E 316 TYR ASP ARG LYS VAL ILE ILE TRP ARG GLU GLU ASN GLY SEQRES 8 E 316 THR TRP GLU LYS SER HIS GLU HIS ALA GLY HIS ASP SER SEQRES 9 E 316 SER VAL ASN SER VAL CYS TRP ALA PRO HIS ASP TYR GLY SEQRES 10 E 316 LEU ILE LEU ALA CYS GLY SER SER ASP GLY ALA ILE SER SEQRES 11 E 316 LEU LEU THR TYR THR GLY GLU GLY GLN TRP GLU VAL LYS SEQRES 12 E 316 LYS ILE ASN ASN ALA HIS THR ILE GLY CYS ASN ALA VAL SEQRES 13 E 316 SER TRP ALA PRO ALA VAL VAL PRO GLY SER LEU ILE ASP SEQRES 14 E 316 HIS PRO SER GLY GLN LYS PRO ASN TYR ILE LYS ARG PHE SEQRES 15 E 316 ALA SER GLY GLY CYS ASP ASN LEU ILE LYS LEU TRP LYS SEQRES 16 E 316 GLU GLU GLU ASP GLY GLN TRP LYS GLU GLU GLN LYS LEU SEQRES 17 E 316 GLU ALA HIS SER ASP TRP VAL ARG ASP VAL ALA TRP ALA SEQRES 18 E 316 PRO SER ILE GLY LEU PRO THR SER THR ILE ALA SER CYS SEQRES 19 E 316 SER GLN ASP GLY ARG VAL PHE ILE TRP THR CYS ASP ASP SEQRES 20 E 316 ALA SER SER ASN THR TRP SER PRO LYS LEU LEU HIS LYS SEQRES 21 E 316 PHE ASN ASP VAL VAL TRP HIS VAL SER TRP SER ILE THR SEQRES 22 E 316 ALA ASN ILE LEU ALA VAL SER GLY GLY ASP ASN LYS VAL SEQRES 23 E 316 THR LEU TRP LYS GLU SER VAL ASP GLY GLN TRP VAL CYS SEQRES 24 E 316 ILE SER ASP VAL ASN LYS GLY GLN GLY SER VAL SER ALA SEQRES 25 E 316 SER VAL THR GLU SEQRES 1 F 442 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLY ASP SEQRES 2 F 442 PRO PHE SER GLU CYS ASN ASP GLU ILE ASP ASN ALA LYS SEQRES 3 F 442 LEU ILE MET LYS GLU ARG ARG PHE THR ALA SER TYR THR SEQRES 4 F 442 PHE ALA LYS PHE SER THR GLY SER MET LEU LEU THR LYS SEQRES 5 F 442 ASP ILE VAL GLY LYS SER GLY VAL SER ILE LYS ARG LEU SEQRES 6 F 442 PRO THR GLU LEU GLN ARG LYS PHE LEU PHE ASP ASP VAL SEQRES 7 F 442 TYR LEU ASP LYS GLU ILE GLU LYS VAL THR ILE GLU ALA SEQRES 8 F 442 ARG LYS SER ASN PRO TYR PRO GLN ILE SER GLU SER SER SEQRES 9 F 442 LEU LEU PHE LYS ASP ALA LEU ASP TYR MET GLU LYS THR SEQRES 10 F 442 SER SER ASP TYR ASN LEU TRP LYS LEU SER SER ILE LEU SEQRES 11 F 442 PHE ASP PRO VAL SER TYR PRO TYR LYS THR ASP ASN ASP SEQRES 12 F 442 GLN VAL LYS MET ALA LEU LEU LYS LYS GLU ARG HIS CYS SEQRES 13 F 442 ARG LEU THR SER TRP ILE VAL SER GLN ILE GLY PRO GLU SEQRES 14 F 442 ILE GLU GLU LYS ILE ARG ASN SER SER ASN GLU ILE GLU SEQRES 15 F 442 GLN ILE PHE LEU TYR LEU LEU LEU ASN ASP VAL VAL ARG SEQRES 16 F 442 ALA SER LYS LEU ALA ILE GLU SER LYS ASN GLY HIS LEU SEQRES 17 F 442 SER VAL LEU ILE SER TYR LEU GLY SER ASN ASP PRO ARG SEQRES 18 F 442 ILE ARG ASP LEU ALA GLU LEU GLN LEU GLN LYS TRP SER SEQRES 19 F 442 THR GLY GLY CYS SER ILE ASP LYS ASN ILE SER LYS ILE SEQRES 20 F 442 TYR LYS LEU LEU SER GLY SER PRO PHE GLU GLY LEU PHE SEQRES 21 F 442 SER LEU LYS GLU LEU GLU SER GLU PHE SER TRP LEU CYS SEQRES 22 F 442 LEU LEU ASN LEU THR LEU CYS TYR GLY GLN ILE ASP GLU SEQRES 23 F 442 TYR SER LEU GLU SER LEU VAL GLN SER HIS LEU ASP LYS SEQRES 24 F 442 PHE SER LEU PRO TYR ASP ASP PRO ILE GLY VAL ILE PHE SEQRES 25 F 442 GLN LEU TYR ALA ALA ASN GLU ASN THR GLU LYS LEU TYR SEQRES 26 F 442 LYS GLU VAL ARG GLN ARG THR ASN ALA LEU ASP VAL GLN SEQRES 27 F 442 PHE CYS TRP TYR LEU ILE GLN THR LEU ARG PHE ASN GLY SEQRES 28 F 442 THR ARG VAL PHE SER LYS GLU THR SER ASP GLU ALA THR SEQRES 29 F 442 PHE ALA PHE ALA ALA GLN LEU GLU PHE ALA GLN LEU HIS SEQRES 30 F 442 GLY HIS SER LEU PHE VAL SER CYS PHE LEU ASN ASP ASP SEQRES 31 F 442 LYS ALA ALA GLU ASP THR ILE LYS ARG LEU VAL MET ARG SEQRES 32 F 442 GLU ILE THR LEU LEU ARG ALA SER THR ASN ASP HIS ILE SEQRES 33 F 442 LEU ASN ARG LEU LYS ILE PRO SER GLN LEU ILE PHE ASN SEQRES 34 F 442 ALA GLN ALA LEU LYS ASP ARG TYR GLU GLY ASN TYR LEU SEQRES 1 G 442 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLY ASP SEQRES 2 G 442 PRO PHE SER GLU CYS ASN ASP GLU ILE ASP ASN ALA LYS SEQRES 3 G 442 LEU ILE MET LYS GLU ARG ARG PHE THR ALA SER TYR THR SEQRES 4 G 442 PHE ALA LYS PHE SER THR GLY SER MET LEU LEU THR LYS SEQRES 5 G 442 ASP ILE VAL GLY LYS SER GLY VAL SER ILE LYS ARG LEU SEQRES 6 G 442 PRO THR GLU LEU GLN ARG LYS PHE LEU PHE ASP ASP VAL SEQRES 7 G 442 TYR LEU ASP LYS GLU ILE GLU LYS VAL THR ILE GLU ALA SEQRES 8 G 442 ARG LYS SER ASN PRO TYR PRO GLN ILE SER GLU SER SER SEQRES 9 G 442 LEU LEU PHE LYS ASP ALA LEU ASP TYR MET GLU LYS THR SEQRES 10 G 442 SER SER ASP TYR ASN LEU TRP LYS LEU SER SER ILE LEU SEQRES 11 G 442 PHE ASP PRO VAL SER TYR PRO TYR LYS THR ASP ASN ASP SEQRES 12 G 442 GLN VAL LYS MET ALA LEU LEU LYS LYS GLU ARG HIS CYS SEQRES 13 G 442 ARG LEU THR SER TRP ILE VAL SER GLN ILE GLY PRO GLU SEQRES 14 G 442 ILE GLU GLU LYS ILE ARG ASN SER SER ASN GLU ILE GLU SEQRES 15 G 442 GLN ILE PHE LEU TYR LEU LEU LEU ASN ASP VAL VAL ARG SEQRES 16 G 442 ALA SER LYS LEU ALA ILE GLU SER LYS ASN GLY HIS LEU SEQRES 17 G 442 SER VAL LEU ILE SER TYR LEU GLY SER ASN ASP PRO ARG SEQRES 18 G 442 ILE ARG ASP LEU ALA GLU LEU GLN LEU GLN LYS TRP SER SEQRES 19 G 442 THR GLY GLY CYS SER ILE ASP LYS ASN ILE SER LYS ILE SEQRES 20 G 442 TYR LYS LEU LEU SER GLY SER PRO PHE GLU GLY LEU PHE SEQRES 21 G 442 SER LEU LYS GLU LEU GLU SER GLU PHE SER TRP LEU CYS SEQRES 22 G 442 LEU LEU ASN LEU THR LEU CYS TYR GLY GLN ILE ASP GLU SEQRES 23 G 442 TYR SER LEU GLU SER LEU VAL GLN SER HIS LEU ASP LYS SEQRES 24 G 442 PHE SER LEU PRO TYR ASP ASP PRO ILE GLY VAL ILE PHE SEQRES 25 G 442 GLN LEU TYR ALA ALA ASN GLU ASN THR GLU LYS LEU TYR SEQRES 26 G 442 LYS GLU VAL ARG GLN ARG THR ASN ALA LEU ASP VAL GLN SEQRES 27 G 442 PHE CYS TRP TYR LEU ILE GLN THR LEU ARG PHE ASN GLY SEQRES 28 G 442 THR ARG VAL PHE SER LYS GLU THR SER ASP GLU ALA THR SEQRES 29 G 442 PHE ALA PHE ALA ALA GLN LEU GLU PHE ALA GLN LEU HIS SEQRES 30 G 442 GLY HIS SER LEU PHE VAL SER CYS PHE LEU ASN ASP ASP SEQRES 31 G 442 LYS ALA ALA GLU ASP THR ILE LYS ARG LEU VAL MET ARG SEQRES 32 G 442 GLU ILE THR LEU LEU ARG ALA SER THR ASN ASP HIS ILE SEQRES 33 G 442 LEU ASN ARG LEU LYS ILE PRO SER GLN LEU ILE PHE ASN SEQRES 34 G 442 ALA GLN ALA LEU LYS ASP ARG TYR GLU GLY ASN TYR LEU SEQRES 1 H 316 MET VAL SER VAL ILE ASN THR VAL ASP THR SER HIS GLU SEQRES 2 H 316 ASP MET ILE HIS ASP ALA GLN MET ASP TYR TYR GLY THR SEQRES 3 H 316 ARG LEU ALA THR CYS SER SER ASP ARG SER VAL LYS ILE SEQRES 4 H 316 PHE ASP VAL ARG ASN GLY GLY GLN ILE LEU ILE ALA ASP SEQRES 5 H 316 LEU ARG GLY HIS GLU GLY PRO VAL TRP GLN VAL ALA TRP SEQRES 6 H 316 ALA HIS PRO MET TYR GLY ASN ILE LEU ALA SER CYS SER SEQRES 7 H 316 TYR ASP ARG LYS VAL ILE ILE TRP ARG GLU GLU ASN GLY SEQRES 8 H 316 THR TRP GLU LYS SER HIS GLU HIS ALA GLY HIS ASP SER SEQRES 9 H 316 SER VAL ASN SER VAL CYS TRP ALA PRO HIS ASP TYR GLY SEQRES 10 H 316 LEU ILE LEU ALA CYS GLY SER SER ASP GLY ALA ILE SER SEQRES 11 H 316 LEU LEU THR TYR THR GLY GLU GLY GLN TRP GLU VAL LYS SEQRES 12 H 316 LYS ILE ASN ASN ALA HIS THR ILE GLY CYS ASN ALA VAL SEQRES 13 H 316 SER TRP ALA PRO ALA VAL VAL PRO GLY SER LEU ILE ASP SEQRES 14 H 316 HIS PRO SER GLY GLN LYS PRO ASN TYR ILE LYS ARG PHE SEQRES 15 H 316 ALA SER GLY GLY CYS ASP ASN LEU ILE LYS LEU TRP LYS SEQRES 16 H 316 GLU GLU GLU ASP GLY GLN TRP LYS GLU GLU GLN LYS LEU SEQRES 17 H 316 GLU ALA HIS SER ASP TRP VAL ARG ASP VAL ALA TRP ALA SEQRES 18 H 316 PRO SER ILE GLY LEU PRO THR SER THR ILE ALA SER CYS SEQRES 19 H 316 SER GLN ASP GLY ARG VAL PHE ILE TRP THR CYS ASP ASP SEQRES 20 H 316 ALA SER SER ASN THR TRP SER PRO LYS LEU LEU HIS LYS SEQRES 21 H 316 PHE ASN ASP VAL VAL TRP HIS VAL SER TRP SER ILE THR SEQRES 22 H 316 ALA ASN ILE LEU ALA VAL SER GLY GLY ASP ASN LYS VAL SEQRES 23 H 316 THR LEU TRP LYS GLU SER VAL ASP GLY GLN TRP VAL CYS SEQRES 24 H 316 ILE SER ASP VAL ASN LYS GLY GLN GLY SER VAL SER ALA SEQRES 25 H 316 SER VAL THR GLU HELIX 75 75 HIS A 67 GLY A 71 1 5 HELIX 76 76 PRO A 113 GLY A 117 1 5 SHEET 61 61 1 ILE A 16 MET A 21 0 SHEET 62 62 1 ARG A 27 SER A 32 0 SHEET 63 63 1 SER A 36 ASP A 41 0 SHEET 64 64 1 ALA A 51 ARG A 54 0 SHEET 65 65 1 VAL A 60 TRP A 65 0 SHEET 66 66 1 LEU A 74 SER A 78 0 SHEET 67 67 1 VAL A 83 TRP A 86 0 SHEET 68 68 1 LYS A 95 HIS A 99 0 SHEET 69 69 1 VAL A 106 TRP A 111 0 SHEET 70 70 1 LEU A 120 SER A 124 0 SHEET 71 71 1 ILE A 129 TYR A 134 0 SHEET 72 72 1 TRP A 140 VAL A 142 0 SHEET 73 73 1 SER A 157 TRP A 158 0 SHEET 74 74 1 PHE A 182 ALA A 183 0 SHEET 75 75 1 LEU A 193 GLU A 196 0 SHEET 76 76 1 TRP A 202 GLN A 206 0 SHEET 77 77 1 VAL A 215 ALA A 219 0 SHEET 78 78 1 THR A 230 SER A 235 0 SHEET 79 79 1 ARG A 239 THR A 244 0 SHEET 80 80 1 LEU A 257 LYS A 260 0 SHEET 81 81 1 VAL A 265 TRP A 270 0 SHEET 82 82 1 LEU A 277 GLY A 281 0 SHEET 83 83 1 VAL A 286 GLU A 291 0 SHEET 84 84 1 TRP A 297 ASP A 302 0 CRYST1 181.818 216.575 100.959 90.00 108.11 90.00 C 1 2 1 16 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 0.005500 0.000000 0.001799 0.00000 SCALE2 0.000000 0.004617 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010421 0.00000 ATOM 1 N ASP A 14 187.450 217.346 805.206 1.00202.38 N ATOM 2 CA ASP A 14 187.213 216.051 805.917 1.00202.38 C ATOM 3 C ASP A 14 186.559 216.264 807.289 1.00202.38 C ATOM 4 O ASP A 14 185.372 215.960 807.474 1.00202.38 O ATOM 5 CB ASP A 14 188.540 215.279 806.065 1.00182.60 C ATOM 6 CG ASP A 14 189.625 216.084 806.775 1.00182.60 C ATOM 7 OD1 ASP A 14 189.919 217.221 806.341 1.00182.60 O ATOM 8 OD2 ASP A 14 190.191 215.573 807.766 1.00182.60 O ATOM 9 N MET A 15 187.332 216.778 808.247 1.00152.50 N ATOM 10 CA MET A 15 186.809 217.039 809.583 1.00148.35 C ATOM 11 C MET A 15 187.006 218.498 809.975 1.00144.66 C ATOM 12 O MET A 15 188.120 219.027 809.959 1.00143.75 O ATOM 13 CB MET A 15 187.468 216.126 810.623 1.00201.98 C ATOM 14 CG MET A 15 186.760 216.152 811.981 1.00201.98 C ATOM 15 SD MET A 15 187.360 214.914 813.164 1.00201.98 S ATOM 16 CE MET A 15 186.035 213.655 813.098 1.00201.98 C ATOM 17 N ILE A 16 185.896 219.136 810.319 1.00145.71 N ATOM 18 CA ILE A 16 185.894 220.528 810.713 1.00141.11 C ATOM 19 CB ILE A 16 184.551 221.169 810.433 1.00148.29 C ATOM 20 CG1 ILE A 16 184.096 220.790 809.029 1.00149.35 C ATOM 21 CD1 ILE A 16 182.969 221.636 808.506 1.00149.23 C ATOM 22 CG2 ILE A 16 184.662 222.673 810.603 1.00147.90 C ATOM 23 C ILE A 16 186.161 220.655 812.194 1.00138.23 C ATOM 24 O ILE A 16 185.858 219.747 812.962 1.00138.16 O ATOM 25 N HIS A 17 186.707 221.797 812.593 1.00152.66 N ATOM 26 CA HIS A 17 187.022 222.028 813.992 1.00147.94 C ATOM 27 C HIS A 17 185.964 222.868 814.708 1.00144.79 C ATOM 28 O HIS A 17 185.166 222.349 815.483 1.00144.46 O ATOM 29 CB HIS A 17 188.387 222.700 814.114 1.00185.90 C ATOM 30 CG HIS A 17 189.097 222.373 815.386 1.00187.50 C ATOM 31 ND1 HIS A 17 189.705 221.155 815.605 1.00187.52 N ATOM 32 CE1 HIS A 17 190.199 221.126 816.829 1.00187.52 C ATOM 33 NE2 HIS A 17 189.935 222.282 817.413 1.00187.52 N ATOM 34 CD2 HIS A 17 189.250 223.080 816.530 1.00187.52 C ATOM 35 N ASP A 18 185.962 224.171 814.459 1.00152.56 N ATOM 36 CA ASP A 18 184.996 225.058 815.091 1.00148.59 C ATOM 37 C ASP A 18 184.255 225.752 813.964 1.00145.69 C ATOM 38 O ASP A 18 184.775 225.860 812.857 1.00145.81 O ATOM 39 CB ASP A 18 185.730 226.081 815.967 1.00187.62 C ATOM 40 CG ASP A 18 184.796 226.850 816.889 1.00187.62 C ATOM 41 OD1 ASP A 18 183.967 227.629 816.387 1.00187.62 O ATOM 42 OD2 ASP A 18 184.895 226.678 818.124 1.00187.62 O ATOM 43 N ALA A 19 183.031 226.196 814.224 1.00103.78 N ATOM 44 CA ALA A 19 182.247 226.893 813.208 1.00102.30 C ATOM 45 C ALA A 19 181.253 227.802 813.901 1.00100.40 C ATOM 46 O ALA A 19 180.360 227.322 814.581 1.00101.11 O ATOM 47 CB ALA A 19 181.516 225.899 812.346 1.00159.46 C ATOM 48 N GLN A 20 181.396 229.112 813.737 1.00135.46 N ATOM 49 CA GLN A 20 180.487 230.040 814.408 1.00132.26 C ATOM 50 C GLN A 20 179.674 230.928 813.486 1.00128.30 C ATOM 51 O GLN A 20 180.196 231.602 812.606 1.00126.50 O ATOM 52 CB GLN A 20 181.244 230.925 815.408 1.00148.20 C ATOM 53 CG GLN A 20 180.322 231.903 816.113 1.00147.60 C ATOM 54 CD GLN A 20 181.047 232.892 816.997 1.00148.80 C ATOM 55 OE1 GLN A 20 181.880 233.681 816.534 1.00148.63 O ATOM 56 NE2 GLN A 20 180.720 232.868 818.281 1.00148.30 N ATOM 57 N MET A 21 178.380 230.947 813.719 1.00110.64 N ATOM 58 CA MET A 21 177.524 231.759 812.905 1.00110.34 C ATOM 59 C MET A 21 177.810 233.222 813.121 1.00109.37 C ATOM 60 O MET A 21 178.362 233.582 814.138 1.00109.02 O ATOM 61 CB MET A 21 176.104 231.487 813.270 1.00117.33 C ATOM 62 CG MET A 21 175.166 232.081 812.292 1.00118.50 C ATOM 63 SD MET A 21 173.918 230.884 811.974 1.00121.94 S ATOM 64 CE MET A 21 174.722 229.337 812.611 1.00116.58 C ATOM 65 N ASP A 22 177.412 234.063 812.175 1.00118.17 N ATOM 66 CA ASP A 22 177.616 235.506 812.273 1.00117.47 C ATOM 67 C ASP A 22 176.534 236.164 813.159 1.00119.24 C ATOM 68 O ASP A 22 175.621 235.477 813.627 1.00119.55 O ATOM 69 CB ASP A 22 177.634 236.099 810.865 1.00120.11 C ATOM 70 CG ASP A 22 176.457 237.004 810.584 1.00120.11 C ATOM 71 OD1 ASP A 22 175.307 236.644 810.919 1.00120.11 O ATOM 72 OD2 ASP A 22 176.696 238.079 810.001 1.00120.11 O ATOM 73 N TYR A 23 176.625 237.478 813.382 1.00123.12 N ATOM 74 CA TYR A 23 175.676 238.181 814.250 1.00122.51 C ATOM 75 C TYR A 23 174.193 238.085 813.927 1.00123.07 C ATOM 76 O TYR A 23 173.429 237.493 814.689 1.00125.41 O ATOM 77 CB TYR A 23 176.046 239.655 814.362 1.00121.26 C ATOM 78 CG TYR A 23 175.189 240.431 815.354 1.00122.48 C ATOM 79 CD1 TYR A 23 175.083 240.036 816.692 1.00121.30 C ATOM 80 CE1 TYR A 23 174.358 240.808 817.620 1.00121.38 C ATOM 81 CZ TYR A 23 173.735 241.980 817.200 1.00120.70 C ATOM 82 OH TYR A 23 173.049 242.789 818.078 1.00121.94 O ATOM 83 CE2 TYR A 23 173.821 242.375 815.886 1.00119.79 C ATOM 84 CD2 TYR A 23 174.543 241.602 814.973 1.00122.26 C ATOM 85 N TYR A 24 173.766 238.687 812.825 1.00113.16 N ATOM 86 CA TYR A 24 172.356 238.636 812.471 1.00113.71 C ATOM 87 C TYR A 24 171.880 237.251 812.019 1.00115.78 C ATOM 88 O TYR A 24 170.719 237.084 811.628 1.00115.25 O ATOM 89 CB TYR A 24 172.046 239.644 811.374 1.00115.45 C ATOM 90 CG TYR A 24 172.135 241.083 811.799 1.00112.92 C ATOM 91 CD1 TYR A 24 173.359 241.695 812.018 1.00113.52 C ATOM 92 CE1 TYR A 24 173.434 243.041 812.381 1.00113.20 C ATOM 93 CZ TYR A 24 172.277 243.775 812.530 1.00111.64 C ATOM 94 OH TYR A 24 172.319 245.110 812.868 1.00109.56 O ATOM 95 CE2 TYR A 24 171.055 243.179 812.323 1.00111.65 C ATOM 96 CD2 TYR A 24 170.987 241.843 811.958 1.00112.44 C ATOM 97 N GLY A 25 172.768 236.260 812.072 1.00105.39 N ATOM 98 CA GLY A 25 172.402 234.918 811.658 1.00108.51 C ATOM 99 C GLY A 25 172.147 234.884 810.171 1.00109.51 C ATOM 100 O GLY A 25 171.021 234.675 809.733 1.00110.92 O ATOM 101 N THR A 26 173.207 235.109 809.402 1.00119.13 N ATOM 102 CA THR A 26 173.152 235.128 807.943 1.00118.44 C ATOM 103 C THR A 26 174.302 234.333 807.366 1.00118.57 C ATOM 104 O THR A 26 174.089 233.376 806.636 1.00119.61 O ATOM 105 CB THR A 26 173.245 236.548 807.411 1.00107.24 C ATOM 106 OG1 THR A 26 172.045 237.247 807.752 1.00107.24 O ATOM 107 CG2 THR A 26 173.438 236.548 805.900 1.00107.24 C ATOM 108 N ARG A 27 175.527 234.745 807.668 1.00 95.72 N ATOM 109 CA ARG A 27 176.679 234.012 807.193 1.00 96.53 C ATOM 110 C ARG A 27 177.047 232.976 808.243 1.00 95.24 C ATOM 111 O ARG A 27 176.420 232.894 809.293 1.00 94.86 O ATOM 112 CB ARG A 27 177.854 234.945 806.937 1.00186.99 C ATOM 113 CG ARG A 27 177.710 235.798 805.700 1.00186.99 C ATOM 114 CD ARG A 27 176.780 236.970 805.905 1.00186.99 C ATOM 115 NE ARG A 27 177.087 238.008 804.928 1.00186.99 N ATOM 116 CZ ARG A 27 178.272 238.608 804.836 1.00186.99 C ATOM 117 NH1 ARG A 27 179.256 238.276 805.663 1.00186.99 N ATOM 118 NH2 ARG A 27 178.478 239.533 803.906 1.00186.99 N ATOM 119 N LEU A 28 178.059 232.174 807.968 1.00 96.29 N ATOM 120 CA LEU A 28 178.455 231.167 808.916 1.00 95.99 C ATOM 121 C LEU A 28 179.875 230.791 808.603 1.00 97.65 C ATOM 122 O LEU A 28 180.115 230.094 807.648 1.00 96.29 O ATOM 123 CB LEU A 28 177.558 229.955 808.782 1.00 95.54 C ATOM 124 CG LEU A 28 177.859 228.848 809.786 1.00 96.09 C ATOM 125 CD1 LEU A 28 176.667 227.932 809.854 1.00 95.90 C ATOM 126 CD2 LEU A 28 179.126 228.078 809.421 1.00100.30 C ATOM 127 N ALA A 29 180.825 231.242 809.402 1.00 97.74 N ATOM 128 CA ALA A 29 182.215 230.908 809.138 1.00101.61 C ATOM 129 C ALA A 29 182.563 229.506 809.634 1.00103.28 C ATOM 130 O ALA A 29 182.044 229.048 810.654 1.00103.12 O ATOM 131 CB ALA A 29 183.121 231.946 809.781 1.00149.19 C ATOM 132 N THR A 30 183.441 228.829 808.894 1.00117.30 N ATOM 133 CA THR A 30 183.890 227.482 809.237 1.00120.64 C ATOM 134 C THR A 30 185.373 227.327 808.994 1.00125.52 C ATOM 135 O THR A 30 185.978 228.120 808.278 1.00126.20 O ATOM 136 CB THR A 30 183.208 226.432 808.390 1.00 88.06 C ATOM 137 OG1 THR A 30 181.802 226.491 808.610 1.00 86.49 O ATOM 138 CG2 THR A 30 183.706 225.063 808.760 1.00 88.45 C ATOM 139 N CYS A 31 185.962 226.297 809.593 1.00143.40 N ATOM 140 CA CYS A 31 187.380 226.029 809.407 1.00147.62 C ATOM 141 C CYS A 31 187.674 224.604 809.845 1.00149.31 C ATOM 142 O CYS A 31 187.087 224.118 810.814 1.00149.59 O ATOM 143 CB CYS A 31 188.235 227.017 810.211 1.00145.22 C ATOM 144 SG CYS A 31 188.334 226.703 811.989 1.00150.31 S ATOM 145 N SER A 32 188.569 223.937 809.116 1.00122.93 N ATOM 146 CA SER A 32 188.944 222.557 809.423 1.00125.48 C ATOM 147 C SER A 32 190.443 222.354 809.250 1.00127.31 C ATOM 148 O SER A 32 191.160 223.262 808.823 1.00127.54 O ATOM 149 CB SER A 32 188.162 221.564 808.546 1.00202.38 C ATOM 150 OG SER A 32 188.237 221.892 807.169 1.00202.38 O ATOM 151 N SER A 33 190.899 221.152 809.585 1.00141.07 N ATOM 152 CA SER A 33 192.311 220.787 809.518 1.00144.27 C ATOM 153 C SER A 33 193.044 221.063 808.196 1.00146.59 C ATOM 154 O SER A 33 194.277 221.105 808.171 1.00147.11 O ATOM 155 CB SER A 33 192.454 219.310 809.877 1.00141.54 C ATOM 156 OG SER A 33 191.347 218.887 810.655 1.00141.54 O ATOM 157 N ASP A 34 192.308 221.246 807.100 1.00181.21 N ATOM 158 CA ASP A 34 192.954 221.503 805.816 1.00181.21 C ATOM 159 C ASP A 34 193.443 222.936 805.632 1.00181.21 C ATOM 160 O ASP A 34 193.745 223.351 804.517 1.00181.21 O ATOM 161 CB ASP A 34 192.038 221.118 804.644 1.00139.34 C ATOM 162 CG ASP A 34 190.659 221.746 804.735 1.00140.66 C ATOM 163 OD1 ASP A 34 189.822 221.221 805.495 1.00141.68 O ATOM 164 OD2 ASP A 34 190.405 222.760 804.045 1.00141.71 O ATOM 165 N ARG A 35 193.524 223.685 806.728 1.00126.46 N ATOM 166 CA ARG A 35 193.999 225.071 806.708 1.00124.78 C ATOM 167 C ARG A 35 193.093 226.037 805.927 1.00123.01 C ATOM 168 O ARG A 35 193.544 227.117 805.503 1.00122.78 O ATOM 169 CB ARG A 35 195.414 225.148 806.114 1.00149.29 C ATOM 170 CG ARG A 35 196.329 223.959 806.389 1.00151.85 C ATOM 171 CD ARG A 35 197.646 224.166 805.654 1.00154.56 C ATOM 172 NE ARG A 35 198.439 222.949 805.525 1.00154.71 N ATOM 173 CZ ARG A 35 199.615 222.892 804.905 1.00154.71 C ATOM 174 NH1 ARG A 35 200.134 223.986 804.356 1.00154.71 N ATOM 175 NH2 ARG A 35 200.271 221.741 804.824 1.00154.71 N ATOM 176 N SER A 36 191.824 225.671 805.748 1.00114.14 N ATOM 177 CA SER A 36 190.907 226.524 804.989 1.00112.59 C ATOM 178 C SER A 36 189.689 227.061 805.752 1.00110.06 C ATOM 179 O SER A 36 188.867 226.290 806.253 1.00109.81 O ATOM 180 CB SER A 36 190.431 225.778 803.729 1.00202.38 C ATOM 181 OG SER A 36 191.472 225.629 802.773 1.00202.38 O ATOM 182 N VAL A 37 189.577 228.389 805.810 1.00118.70 N ATOM 183 CA VAL A 37 188.471 229.065 806.497 1.00116.90 C ATOM 184 C VAL A 37 187.347 229.440 805.526 1.00116.98 C ATOM 185 O VAL A 37 187.401 230.498 804.898 1.00116.75 O ATOM 186 CB VAL A 37 188.953 230.371 807.187 1.00121.23 C ATOM 187 CG1 VAL A 37 187.792 231.036 807.893 1.00120.92 C ATOM 188 CG2 VAL A 37 190.078 230.076 808.173 1.00120.63 C ATOM 189 N LYS A 38 186.328 228.586 805.422 1.00131.62 N ATOM 190 CA LYS A 38 185.195 228.814 804.514 1.00130.77 C ATOM 191 C LYS A 38 184.071 229.633 805.156 1.00129.22 C ATOM 192 O LYS A 38 183.772 229.456 806.333 1.00129.92 O ATOM 193 CB LYS A 38 184.616 227.470 804.047 1.00145.54 C ATOM 194 CG LYS A 38 185.603 226.511 803.392 1.00145.54 C ATOM 195 CD LYS A 38 184.938 225.172 803.095 1.00145.54 C ATOM 196 CE LYS A 38 185.926 224.162 802.521 1.00145.54 C ATOM 197 NZ LYS A 38 185.286 222.828 802.304 1.00145.54 N ATOM 198 N ILE A 39 183.447 230.516 804.380 1.00121.51 N ATOM 199 CA ILE A 39 182.344 231.341 804.873 1.00120.00 C ATOM 200 C ILE A 39 181.042 231.142 804.092 1.00120.39 C ATOM 201 O ILE A 39 180.771 231.868 803.141 1.00121.16 O ATOM 202 CB ILE A 39 182.658 232.846 804.810 1.00129.42 C ATOM 203 CG1 ILE A 39 183.860 233.180 805.683 1.00128.93 C ATOM 204 CD1 ILE A 39 184.175 234.671 805.719 1.00128.06 C ATOM 205 CG2 ILE A 39 181.439 233.642 805.275 1.00128.04 C ATOM 206 N PHE A 40 180.229 230.175 804.505 1.00 99.23 N ATOM 207 CA PHE A 40 178.954 229.907 803.858 1.00100.03 C ATOM 208 C PHE A 40 177.999 231.042 804.193 1.00101.50 C ATOM 209 O PHE A 40 178.416 232.062 804.725 1.00102.64 O ATOM 210 CB PHE A 40 178.412 228.582 804.357 1.00109.19 C ATOM 211 CG PHE A 40 179.372 227.452 804.192 1.00110.80 C ATOM 212 CD1 PHE A 40 180.745 227.695 804.122 1.00111.93 C ATOM 213 CE1 PHE A 40 181.663 226.654 804.014 1.00113.40 C ATOM 214 CZ PHE A 40 181.217 225.344 803.976 1.00113.76 C ATOM 215 CE2 PHE A 40 179.839 225.077 804.045 1.00113.92 C ATOM 216 CD2 PHE A 40 178.924 226.137 804.150 1.00112.72 C ATOM 217 N ASP A 41 176.734 230.894 803.854 1.00116.31 N ATOM 218 CA ASP A 41 175.759 231.920 804.161 1.00119.39 C ATOM 219 C ASP A 41 174.449 231.132 804.128 1.00121.67 C ATOM 220 O ASP A 41 174.178 230.397 803.187 1.00121.12 O ATOM 221 CB ASP A 41 175.905 233.081 803.150 1.00166.06 C ATOM 222 CG ASP A 41 174.825 233.120 802.109 1.00166.06 C ATOM 223 OD1 ASP A 41 174.350 232.042 801.701 1.00166.06 O ATOM 224 OD2 ASP A 41 174.469 234.248 801.678 1.00166.06 O ATOM 225 N VAL A 42 173.669 231.224 805.197 1.00178.36 N ATOM 226 CA VAL A 42 172.452 230.427 805.312 1.00182.36 C ATOM 227 C VAL A 42 171.116 231.145 805.188 1.00184.68 C ATOM 228 O VAL A 42 170.361 231.210 806.152 1.00185.35 O ATOM 229 CB VAL A 42 172.453 229.659 806.664 1.00155.78 C ATOM 230 CG1 VAL A 42 171.400 228.563 806.657 1.00154.98 C ATOM 231 CG2 VAL A 42 173.837 229.081 806.933 1.00156.65 C ATOM 232 N ARG A 43 170.803 231.667 804.011 1.00151.68 N ATOM 233 CA ARG A 43 169.525 232.345 803.854 1.00155.27 C ATOM 234 C ARG A 43 168.415 231.313 803.610 1.00156.59 C ATOM 235 O ARG A 43 168.239 230.828 802.500 1.00157.08 O ATOM 236 CB ARG A 43 169.600 233.356 802.705 1.00184.05 C ATOM 237 CG ARG A 43 170.632 234.453 802.925 1.00184.05 C ATOM 238 CD ARG A 43 170.365 235.651 802.039 1.00184.05 C ATOM 239 NE ARG A 43 171.216 236.790 802.374 1.00184.05 N ATOM 240 CZ ARG A 43 171.000 238.033 801.949 1.00184.05 C ATOM 241 NH1 ARG A 43 169.963 238.300 801.164 1.00184.05 N ATOM 242 NH2 ARG A 43 171.799 239.019 802.329 1.00184.05 N ATOM 243 N ASN A 44 167.685 230.974 804.670 1.00164.14 N ATOM 244 CA ASN A 44 166.586 230.000 804.629 1.00164.14 C ATOM 245 C ASN A 44 167.010 228.529 804.682 1.00164.14 C ATOM 246 O ASN A 44 166.821 227.784 803.717 1.00164.14 O ATOM 247 CB ASN A 44 165.691 230.219 803.401 1.00155.61 C ATOM 248 CG ASN A 44 164.827 231.463 803.517 1.00155.95 C ATOM 249 OD1 ASN A 44 164.124 231.661 804.513 1.00155.66 O ATOM 250 ND2 ASN A 44 164.866 232.305 802.492 1.00155.82 N ATOM 251 N GLY A 45 167.575 228.128 805.823 1.00202.38 N ATOM 252 CA GLY A 45 168.002 226.754 806.039 1.00202.38 C ATOM 253 C GLY A 45 169.017 226.129 805.096 1.00202.38 C ATOM 254 O GLY A 45 169.604 225.097 805.434 1.00202.38 O ATOM 255 N GLY A 46 169.239 226.735 803.931 1.00178.39 N ATOM 256 CA GLY A 46 170.185 226.174 802.980 1.00176.71 C ATOM 257 C GLY A 46 171.580 226.777 802.985 1.00175.01 C ATOM 258 O GLY A 46 171.727 228.000 802.994 1.00175.99 O ATOM 259 N GLN A 47 172.603 225.916 802.967 1.00165.93 N ATOM 260 CA GLN A 47 174.011 226.342 802.963 1.00162.83 C ATOM 261 C GLN A 47 174.485 226.734 801.546 1.00159.37 C ATOM 262 O GLN A 47 174.053 226.147 800.553 1.00158.91 O ATOM 263 CB GLN A 47 174.918 225.224 803.524 1.00177.66 C ATOM 264 CG GLN A 47 174.574 224.721 804.946 1.00178.57 C ATOM 265 CD GLN A 47 175.677 223.852 805.567 1.00179.36 C ATOM 266 OE1 GLN A 47 176.137 222.881 804.971 1.00179.08 O ATOM 267 NE2 GLN A 47 176.097 224.206 806.770 1.00179.87 N ATOM 268 N ILE A 48 175.378 227.722 801.468 1.00121.30 N ATOM 269 CA ILE A 48 175.914 228.235 800.194 1.00117.77 C ATOM 270 C ILE A 48 177.297 228.894 800.339 1.00116.58 C ATOM 271 O ILE A 48 177.382 230.106 800.516 1.00118.56 O ATOM 272 CB ILE A 48 174.981 229.335 799.579 1.00124.17 C ATOM 273 CG1 ILE A 48 173.624 228.746 799.151 1.00122.89 C ATOM 274 CD1 ILE A 48 172.624 229.790 798.568 1.00119.75 C ATOM 275 CG2 ILE A 48 175.705 230.031 798.417 1.00123.37 C ATOM 276 N LEU A 49 178.373 228.122 800.240 1.00119.43 N ATOM 277 CA LEU A 49 179.726 228.685 800.366 1.00118.34 C ATOM 278 C LEU A 49 179.915 230.009 799.604 1.00117.05 C ATOM 279 O LEU A 49 179.275 230.210 798.581 1.00117.73 O ATOM 280 CB LEU A 49 180.745 227.648 799.880 1.00129.77 C ATOM 281 CG LEU A 49 182.163 228.049 799.464 1.00129.77 C ATOM 282 CD1 LEU A 49 182.858 228.840 800.565 1.00129.77 C ATOM 283 CD2 LEU A 49 182.941 226.773 799.127 1.00129.77 C ATOM 284 N ILE A 50 180.762 230.914 800.112 1.00127.81 N ATOM 285 CA ILE A 50 181.019 232.194 799.438 1.00126.11 C ATOM 286 C ILE A 50 182.495 232.455 799.228 1.00125.92 C ATOM 287 O ILE A 50 182.901 232.868 798.148 1.00125.94 O ATOM 288 CB ILE A 50 180.500 233.425 800.196 1.00 89.18 C ATOM 289 CG1 ILE A 50 178.980 233.364 800.365 1.00 90.74 C ATOM 290 CD1 ILE A 50 178.395 234.549 801.171 1.00 92.21 C ATOM 291 CG2 ILE A 50 180.916 234.695 799.439 1.00 87.69 C ATOM 292 N ALA A 51 183.305 232.266 800.257 1.00121.76 N ATOM 293 CA ALA A 51 184.738 232.487 800.097 1.00125.32 C ATOM 294 C ALA A 51 185.526 231.388 800.806 1.00129.06 C ATOM 295 O ALA A 51 185.014 230.752 801.724 1.00130.05 O ATOM 296 CB ALA A 51 185.128 233.879 800.619 1.00 57.68 C ATOM 297 N ASP A 52 186.748 231.138 800.346 1.00170.58 N ATOM 298 CA ASP A 52 187.623 230.120 800.930 1.00175.04 C ATOM 299 C ASP A 52 188.933 230.851 801.197 1.00175.04 C ATOM 300 O ASP A 52 189.793 230.945 800.322 1.00175.04 O ATOM 301 CB ASP A 52 187.836 228.947 799.942 1.00163.97 C ATOM 302 CG ASP A 52 188.642 227.768 800.542 1.00164.89 C ATOM 303 OD1 ASP A 52 189.874 227.901 800.749 1.00165.91 O ATOM 304 OD2 ASP A 52 188.039 226.694 800.798 1.00163.90 O ATOM 305 N LEU A 53 189.065 231.392 802.403 1.00182.78 N ATOM 306 CA LEU A 53 190.264 232.131 802.763 1.00185.05 C ATOM 307 C LEU A 53 191.375 231.198 803.253 1.00187.38 C ATOM 308 O LEU A 53 191.326 230.672 804.368 1.00188.14 O ATOM 309 CB LEU A 53 189.931 233.184 803.828 1.00127.57 C ATOM 310 CG LEU A 53 188.530 233.829 803.804 1.00127.08 C ATOM 311 CD1 LEU A 53 188.570 235.102 804.617 1.00126.35 C ATOM 312 CD2 LEU A 53 188.079 234.153 802.388 1.00128.61 C ATOM 313 N ARG A 54 192.367 230.978 802.394 1.00182.55 N ATOM 314 CA ARG A 54 193.505 230.132 802.721 1.00184.06 C ATOM 315 C ARG A 54 194.630 231.025 803.211 1.00183.94 C ATOM 316 O ARG A 54 194.923 232.044 802.593 1.00184.63 O ATOM 317 CB ARG A 54 193.982 229.372 801.488 1.00164.10 C ATOM 318 CG ARG A 54 193.430 227.979 801.351 1.00167.48 C ATOM 319 CD ARG A 54 194.378 227.165 800.496 1.00170.66 C ATOM 320 NE ARG A 54 194.210 225.726 800.674 1.00173.16 N ATOM 321 CZ ARG A 54 195.115 224.820 800.302 1.00174.76 C ATOM 322 NH1 ARG A 54 196.248 225.206 799.731 1.00174.79 N ATOM 323 NH2 ARG A 54 194.884 223.529 800.499 1.00174.79 N ATOM 324 N GLY A 55 195.262 230.656 804.317 1.00129.06 N ATOM 325 CA GLY A 55 196.344 231.488 804.815 1.00128.67 C ATOM 326 C GLY A 55 197.048 230.998 806.066 1.00128.45 C ATOM 327 O GLY A 55 197.766 231.763 806.717 1.00128.25 O ATOM 328 N HIS A 56 196.859 229.728 806.409 1.00134.14 N ATOM 329 CA HIS A 56 197.496 229.179 807.599 1.00133.77 C ATOM 330 C HIS A 56 198.345 227.962 807.250 1.00134.31 C ATOM 331 O HIS A 56 197.875 227.041 806.580 1.00133.52 O ATOM 332 CB HIS A 56 196.430 228.801 808.638 1.00139.18 C ATOM 333 CG HIS A 56 195.637 229.968 809.155 1.00137.14 C ATOM 334 ND1 HIS A 56 196.189 230.952 809.947 1.00136.55 N ATOM 335 CE1 HIS A 56 195.256 231.830 810.270 1.00136.17 C ATOM 336 NE2 HIS A 56 194.119 231.453 809.713 1.00136.95 N ATOM 337 CD2 HIS A 56 194.330 230.292 809.010 1.00137.21 C ATOM 338 N GLU A 57 199.596 227.969 807.708 1.00202.22 N ATOM 339 CA GLU A 57 200.517 226.866 807.443 1.00202.22 C ATOM 340 C GLU A 57 200.184 225.622 808.282 1.00202.22 C ATOM 341 O GLU A 57 200.944 224.652 808.308 1.00202.22 O ATOM 342 CB GLU A 57 201.979 227.313 807.695 1.00201.87 C ATOM 343 CG GLU A 57 202.586 228.214 806.592 1.00201.87 C ATOM 344 CD GLU A 57 204.076 228.535 806.801 1.00201.87 C ATOM 345 OE1 GLU A 57 204.890 227.596 806.956 1.00201.87 O ATOM 346 OE2 GLU A 57 204.431 229.736 806.797 1.00201.87 O ATOM 347 N GLY A 58 199.041 225.653 808.957 1.00142.87 N ATOM 348 CA GLY A 58 198.623 224.526 809.774 1.00142.71 C ATOM 349 C GLY A 58 197.120 224.576 809.983 1.00140.10 C ATOM 350 O GLY A 58 196.511 225.616 809.746 1.00140.87 O ATOM 351 N PRO A 59 196.489 223.485 810.441 1.00129.39 N ATOM 352 CA PRO A 59 195.035 223.497 810.652 1.00127.18 C ATOM 353 C PRO A 59 194.540 224.708 811.444 1.00125.33 C ATOM 354 O PRO A 59 195.261 225.238 812.281 1.00126.08 O ATOM 355 CB PRO A 59 194.779 222.172 811.383 1.00112.63 C ATOM 356 CG PRO A 59 196.076 221.913 812.096 1.00112.81 C ATOM 357 CD PRO A 59 197.100 222.292 811.053 1.00114.39 C ATOM 358 N VAL A 60 193.320 225.156 811.164 1.00126.87 N ATOM 359 CA VAL A 60 192.745 226.292 811.876 1.00125.91 C ATOM 360 C VAL A 60 191.949 225.741 813.047 1.00125.81 C ATOM 361 O VAL A 60 191.233 224.751 812.907 1.00127.00 O ATOM 362 CB VAL A 60 191.798 227.107 810.986 1.00125.52 C ATOM 363 CG1 VAL A 60 191.224 228.273 811.772 1.00125.06 C ATOM 364 CG2 VAL A 60 192.540 227.611 809.779 1.00126.86 C ATOM 365 N TRP A 61 192.064 226.378 814.204 1.00160.08 N ATOM 366 CA TRP A 61 191.361 225.882 815.374 1.00158.92 C ATOM 367 C TRP A 61 189.991 226.519 815.606 1.00157.53 C ATOM 368 O TRP A 61 188.979 225.980 815.157 1.00157.13 O ATOM 369 CB TRP A 61 192.257 226.030 816.609 1.00134.80 C ATOM 370 CG TRP A 61 193.548 225.220 816.540 1.00137.29 C ATOM 371 CD1 TRP A 61 194.809 225.673 816.797 1.00138.09 C ATOM 372 NE1 TRP A 61 195.719 224.655 816.664 1.00138.56 N ATOM 373 CE2 TRP A 61 195.058 223.509 816.318 1.00138.36 C ATOM 374 CZ2 TRP A 61 195.550 222.229 816.072 1.00138.73 C ATOM 375 CH2 TRP A 61 194.647 221.257 815.738 1.00138.65 C ATOM 376 CZ3 TRP A 61 193.278 221.536 815.636 1.00138.22 C ATOM 377 CE3 TRP A 61 192.785 222.813 815.879 1.00138.38 C ATOM 378 CD2 TRP A 61 193.687 223.825 816.224 1.00138.18 C ATOM 379 N GLN A 62 189.942 227.649 816.300 1.00125.42 N ATOM 380 CA GLN A 62 188.661 228.293 816.560 1.00121.73 C ATOM 381 C GLN A 62 188.531 229.494 815.642 1.00118.61 C ATOM 382 O GLN A 62 189.525 229.966 815.089 1.00117.63 O ATOM 383 CB GLN A 62 188.556 228.719 818.040 1.00165.01 C ATOM 384 CG GLN A 62 187.142 229.128 818.495 1.00167.82 C ATOM 385 CD GLN A 62 187.000 229.257 820.013 1.00170.17 C ATOM 386 OE1 GLN A 62 187.332 228.335 820.761 1.00170.69 O ATOM 387 NE2 GLN A 62 186.487 230.396 820.467 1.00171.30 N ATOM 388 N VAL A 63 187.302 229.976 815.475 1.00144.71 N ATOM 389 CA VAL A 63 187.018 231.128 814.627 1.00144.71 C ATOM 390 C VAL A 63 186.016 232.046 815.315 1.00144.71 C ATOM 391 O VAL A 63 185.162 231.567 816.063 1.00144.71 O ATOM 392 CB VAL A 63 186.438 230.667 813.304 1.00104.24 C ATOM 393 CG1 VAL A 63 186.012 231.855 812.476 1.00104.24 C ATOM 394 CG2 VAL A 63 187.465 229.853 812.574 1.00104.24 C ATOM 395 N ALA A 64 186.104 233.355 815.067 1.00 84.15 N ATOM 396 CA ALA A 64 185.179 234.289 815.714 1.00 81.96 C ATOM 397 C ALA A 64 184.783 235.542 814.930 1.00 80.03 C ATOM 398 O ALA A 64 185.639 236.283 814.447 1.00 80.17 O ATOM 399 CB ALA A 64 185.743 234.694 817.072 1.00202.38 C ATOM 400 N TRP A 65 183.476 235.780 814.835 1.00105.45 N ATOM 401 CA TRP A 65 182.944 236.941 814.127 1.00103.71 C ATOM 402 C TRP A 65 182.919 238.142 815.047 1.00101.92 C ATOM 403 O TRP A 65 182.590 238.004 816.221 1.00103.24 O ATOM 404 CB TRP A 65 181.503 236.685 813.673 1.00137.07 C ATOM 405 CG TRP A 65 181.353 235.913 812.409 1.00139.10 C ATOM 406 CD1 TRP A 65 181.422 234.564 812.258 1.00139.83 C ATOM 407 NE1 TRP A 65 181.267 234.226 810.938 1.00140.89 N ATOM 408 CE2 TRP A 65 181.090 235.368 810.207 1.00140.64 C ATOM 409 CZ2 TRP A 65 180.894 235.540 808.838 1.00142.31 C ATOM 410 CH2 TRP A 65 180.740 236.821 808.376 1.00142.39 C ATOM 411 CZ3 TRP A 65 180.777 237.922 809.246 1.00140.85 C ATOM 412 CE3 TRP A 65 180.976 237.751 810.609 1.00140.60 C ATOM 413 CD2 TRP A 65 181.136 236.454 811.105 1.00140.20 C ATOM 414 N ALA A 66 183.242 239.322 814.527 1.00 97.22 N ATOM 415 CA ALA A 66 183.201 240.534 815.346 1.00 95.45 C ATOM 416 C ALA A 66 181.822 241.192 815.237 1.00 95.44 C ATOM 417 O ALA A 66 181.040 240.857 814.357 1.00 93.67 O ATOM 418 CB ALA A 66 184.290 241.514 814.918 1.00 64.19 C ATOM 419 N HIS A 67 181.530 242.122 816.137 1.00104.87 N ATOM 420 CA HIS A 67 180.239 242.813 816.152 1.00107.41 C ATOM 421 C HIS A 67 180.060 243.683 814.902 1.00107.40 C ATOM 422 O HIS A 67 180.857 244.563 814.645 1.00108.35 O ATOM 423 CB HIS A 67 180.159 243.668 817.423 1.00121.91 C ATOM 424 CG HIS A 67 178.803 244.240 817.691 1.00123.03 C ATOM 425 ND1 HIS A 67 178.359 245.407 817.110 1.00123.43 N ATOM 426 CE1 HIS A 67 177.129 245.661 817.525 1.00124.29 C ATOM 427 NE2 HIS A 67 176.759 244.700 818.353 1.00124.53 N ATOM 428 CD2 HIS A 67 177.790 243.798 818.475 1.00124.58 C ATOM 429 N PRO A 68 178.992 243.467 814.129 1.00152.35 N ATOM 430 CA PRO A 68 178.731 244.235 812.907 1.00153.30 C ATOM 431 C PRO A 68 178.946 245.734 813.009 1.00153.74 C ATOM 432 O PRO A 68 178.920 246.442 812.004 1.00155.46 O ATOM 433 CB PRO A 68 177.281 243.908 812.608 1.00104.12 C ATOM 434 CG PRO A 68 176.722 243.764 813.950 1.00104.22 C ATOM 435 CD PRO A 68 177.741 242.867 814.604 1.00103.67 C ATOM 436 N MET A 69 179.141 246.215 814.224 1.00121.79 N ATOM 437 CA MET A 69 179.367 247.630 814.472 1.00122.33 C ATOM 438 C MET A 69 180.625 248.168 813.778 1.00121.60 C ATOM 439 O MET A 69 180.762 249.373 813.585 1.00120.56 O ATOM 440 CB MET A 69 179.456 247.837 815.977 1.00151.63 C ATOM 441 CG MET A 69 179.791 249.222 816.422 1.00151.32 C ATOM 442 SD MET A 69 179.396 249.358 818.168 1.00150.63 S ATOM 443 CE MET A 69 180.642 248.393 818.922 1.00147.51 C ATOM 444 N TYR A 70 181.531 247.261 813.404 1.00120.41 N ATOM 445 CA TYR A 70 182.793 247.599 812.730 1.00122.31 C ATOM 446 C TYR A 70 182.836 246.902 811.371 1.00122.64 C ATOM 447 O TYR A 70 183.730 246.091 811.110 1.00120.38 O ATOM 448 CB TYR A 70 183.989 247.093 813.537 1.00136.78 C ATOM 449 CG TYR A 70 183.914 247.358 815.016 1.00137.99 C ATOM 450 CD1 TYR A 70 182.812 246.961 815.759 1.00141.48 C ATOM 451 CE1 TYR A 70 182.737 247.209 817.115 1.00142.72 C ATOM 452 CZ TYR A 70 183.772 247.867 817.755 1.00140.64 C ATOM 453 OH TYR A 70 183.698 248.147 819.103 1.00141.00 O ATOM 454 CE2 TYR A 70 184.879 248.266 817.038 1.00139.44 C ATOM 455 CD2 TYR A 70 184.945 248.010 815.673 1.00137.84 C ATOM 456 N GLY A 71 181.880 247.216 810.507 1.00143.81 N ATOM 457 CA GLY A 71 181.842 246.567 809.213 1.00143.81 C ATOM 458 C GLY A 71 181.694 245.091 809.497 1.00143.81 C ATOM 459 O GLY A 71 181.125 244.709 810.515 1.00143.81 O ATOM 460 N ASN A 72 182.208 244.247 808.619 1.00117.34 N ATOM 461 CA ASN A 72 182.090 242.829 808.865 1.00116.64 C ATOM 462 C ASN A 72 183.431 242.165 808.971 1.00115.32 C ATOM 463 O ASN A 72 184.138 241.990 807.983 1.00115.53 O ATOM 464 CB ASN A 72 181.241 242.168 807.790 1.00145.95 C ATOM 465 CG ASN A 72 179.769 242.400 808.012 1.00147.09 C ATOM 466 OD1 ASN A 72 179.109 243.071 807.221 1.00146.87 O ATOM 467 ND2 ASN A 72 179.243 241.860 809.110 1.00147.33 N ATOM 468 N ILE A 73 183.758 241.782 810.197 1.00124.96 N ATOM 469 CA ILE A 73 185.027 241.156 810.483 1.00122.56 C ATOM 470 C ILE A 73 184.954 239.731 810.998 1.00123.66 C ATOM 471 O ILE A 73 184.098 239.373 811.806 1.00124.51 O ATOM 472 CB ILE A 73 185.793 241.984 811.505 1.00 79.19 C ATOM 473 CG1 ILE A 73 186.128 243.342 810.912 1.00 78.84 C ATOM 474 CD1 ILE A 73 185.982 244.483 811.891 1.00 78.22 C ATOM 475 CG2 ILE A 73 187.043 241.248 811.934 1.00 77.22 C ATOM 476 N LEU A 74 185.879 238.925 810.513 1.00106.56 N ATOM 477 CA LEU A 74 185.990 237.541 810.926 1.00108.64 C ATOM 478 C LEU A 74 187.453 237.361 811.276 1.00110.66 C ATOM 479 O LEU A 74 188.326 237.923 810.615 1.00110.98 O ATOM 480 CB LEU A 74 185.640 236.598 809.788 1.00118.17 C ATOM 481 CG LEU A 74 185.771 235.122 810.153 1.00116.49 C ATOM 482 CD1 LEU A 74 184.596 234.736 811.019 1.00115.18 C ATOM 483 CD2 LEU A 74 185.795 234.269 808.908 1.00117.22 C ATOM 484 N ALA A 75 187.732 236.583 812.313 1.00116.24 N ATOM 485 CA ALA A 75 189.102 236.353 812.723 1.00118.21 C ATOM 486 C ALA A 75 189.299 234.862 812.947 1.00119.93 C ATOM 487 O ALA A 75 188.447 234.210 813.554 1.00120.55 O ATOM 488 CB ALA A 75 189.385 237.129 813.995 1.00140.90 C ATOM 489 N SER A 76 190.400 234.315 812.439 1.00105.96 N ATOM 490 CA SER A 76 190.676 232.888 812.621 1.00107.71 C ATOM 491 C SER A 76 192.098 232.710 813.115 1.00109.17 C ATOM 492 O SER A 76 192.997 233.410 812.665 1.00108.32 O ATOM 493 CB SER A 76 190.487 232.110 811.312 1.00135.37 C ATOM 494 OG SER A 76 191.437 232.465 810.321 1.00136.06 O ATOM 495 N CYS A 77 192.296 231.791 814.054 1.00140.94 N ATOM 496 CA CYS A 77 193.628 231.533 814.593 1.00144.96 C ATOM 497 C CYS A 77 194.047 230.172 814.069 1.00147.73 C ATOM 498 O CYS A 77 193.221 229.467 813.487 1.00148.28 O ATOM 499 CB CYS A 77 193.599 231.517 816.121 1.00140.12 C ATOM 500 SG CYS A 77 192.639 230.168 816.805 1.00144.51 S ATOM 501 N SER A 78 195.305 229.787 814.273 1.00137.79 N ATOM 502 CA SER A 78 195.758 228.493 813.758 1.00140.50 C ATOM 503 C SER A 78 197.014 227.916 814.417 1.00141.32 C ATOM 504 O SER A 78 197.666 228.578 815.226 1.00142.11 O ATOM 505 CB SER A 78 195.989 228.609 812.249 1.00171.64 C ATOM 506 OG SER A 78 196.238 227.349 811.654 1.00173.78 O ATOM 507 N TYR A 79 197.332 226.669 814.057 1.00121.01 N ATOM 508 CA TYR A 79 198.505 225.976 814.581 1.00121.54 C ATOM 509 C TYR A 79 199.746 226.544 813.917 1.00122.01 C ATOM 510 O TYR A 79 200.874 226.183 814.251 1.00122.40 O ATOM 511 CB TYR A 79 198.426 224.469 814.308 1.00157.26 C ATOM 512 CG TYR A 79 199.665 223.721 814.752 1.00158.71 C ATOM 513 CD1 TYR A 79 200.214 223.931 816.020 1.00159.62 C ATOM 514 CE1 TYR A 79 201.375 223.275 816.439 1.00159.62 C ATOM 515 CZ TYR A 79 202.003 222.393 815.584 1.00159.70 C ATOM 516 OH TYR A 79 203.159 221.765 815.997 1.00160.28 O ATOM 517 CE2 TYR A 79 201.479 222.158 814.317 1.00159.60 C ATOM 518 CD2 TYR A 79 200.312 222.824 813.907 1.00159.29 C ATOM 519 N ASP A 80 199.533 227.449 812.972 1.00129.16 N ATOM 520 CA ASP A 80 200.639 228.056 812.266 1.00130.33 C ATOM 521 C ASP A 80 201.231 229.218 813.056 1.00130.43 C ATOM 522 O ASP A 80 201.962 230.032 812.497 1.00130.98 O ATOM 523 CB ASP A 80 200.182 228.536 810.887 1.00165.75 C ATOM 524 CG ASP A 80 199.427 229.841 810.948 1.00167.46 C ATOM 525 OD1 ASP A 80 198.576 229.988 811.851 1.00168.26 O ATOM 526 OD2 ASP A 80 199.682 230.716 810.089 1.00168.96 O ATOM 527 N ARG A 81 200.907 229.298 814.346 1.00149.10 N ATOM 528 CA ARG A 81 201.430 230.350 815.233 1.00148.23 C ATOM 529 C ARG A 81 200.967 231.770 814.867 1.00146.96 C ATOM 530 O ARG A 81 201.410 232.752 815.479 1.00145.98 O ATOM 531 CB ARG A 81 202.972 230.312 815.239 1.00150.18 C ATOM 532 CG ARG A 81 203.591 228.929 815.490 1.00153.74 C ATOM 533 CD ARG A 81 204.903 228.760 814.722 1.00156.74 C ATOM 534 NE ARG A 81 205.412 227.391 814.781 1.00157.70 N ATOM 535 CZ ARG A 81 206.205 226.844 813.862 1.00157.70 C ATOM 536 NH1 ARG A 81 206.586 227.550 812.800 1.00157.70 N ATOM 537 NH2 ARG A 81 206.619 225.589 814.002 1.00157.70 N ATOM 538 N LYS A 82 200.078 231.872 813.881 1.00131.23 N ATOM 539 CA LYS A 82 199.577 233.169 813.416 1.00129.25 C ATOM 540 C LYS A 82 198.055 233.328 813.528 1.00126.57 C ATOM 541 O LYS A 82 197.310 232.348 813.497 1.00126.16 O ATOM 542 CB LYS A 82 200.006 233.406 811.951 1.00185.04 C ATOM 543 CG LYS A 82 201.528 233.531 811.721 1.00186.65 C ATOM 544 CD LYS A 82 201.912 233.701 810.233 1.00186.65 C ATOM 545 CE LYS A 82 203.436 233.813 810.049 1.00186.65 C ATOM 546 NZ LYS A 82 203.876 233.853 808.619 1.00186.65 N ATOM 547 N VAL A 83 197.611 234.572 813.680 1.00145.36 N ATOM 548 CA VAL A 83 196.191 234.899 813.765 1.00143.89 C ATOM 549 C VAL A 83 195.893 235.868 812.633 1.00141.56 C ATOM 550 O VAL A 83 196.626 236.840 812.429 1.00141.47 O ATOM 551 CB VAL A 83 195.823 235.577 815.106 1.00134.74 C ATOM 552 CG1 VAL A 83 194.892 236.767 814.861 1.00134.02 C ATOM 553 CG2 VAL A 83 195.133 234.564 816.030 1.00136.67 C ATOM 554 N ILE A 84 194.813 235.608 811.904 1.00134.20 N ATOM 555 CA ILE A 84 194.428 236.442 810.774 1.00131.89 C ATOM 556 C ILE A 84 193.092 237.109 810.987 1.00131.08 C ATOM 557 O ILE A 84 192.149 236.497 811.495 1.00131.82 O ATOM 558 CB ILE A 84 194.313 235.616 809.493 1.00107.55 C ATOM 559 CG1 ILE A 84 195.660 234.978 809.153 1.00105.42 C ATOM 560 CD1 ILE A 84 195.559 233.878 808.138 1.00103.33 C ATOM 561 CG2 ILE A 84 193.812 236.498 808.379 1.00108.23 C ATOM 562 N ILE A 85 193.007 238.365 810.583 1.00115.32 N ATOM 563 CA ILE A 85 191.764 239.086 810.714 1.00117.74 C ATOM 564 C ILE A 85 191.320 239.445 809.311 1.00119.20 C ATOM 565 O ILE A 85 192.002 240.190 808.615 1.00119.61 O ATOM 566 CB ILE A 85 191.939 240.362 811.551 1.00116.52 C ATOM 567 CG1 ILE A 85 192.654 240.035 812.864 1.00114.53 C ATOM 568 CD1 ILE A 85 192.826 241.225 813.789 1.00111.78 C ATOM 569 CG2 ILE A 85 190.585 240.939 811.880 1.00117.89 C ATOM 570 N TRP A 86 190.186 238.900 808.889 1.00114.64 N ATOM 571 CA TRP A 86 189.676 239.170 807.556 1.00118.64 C ATOM 572 C TRP A 86 188.551 240.211 807.533 1.00121.17 C ATOM 573 O TRP A 86 187.482 239.996 808.114 1.00122.44 O ATOM 574 CB TRP A 86 189.160 237.885 806.920 1.00128.65 C ATOM 575 CG TRP A 86 189.912 236.664 807.282 1.00130.23 C ATOM 576 CD1 TRP A 86 189.673 235.845 808.340 1.00131.75 C ATOM 577 NE1 TRP A 86 190.511 234.759 808.301 1.00129.93 N ATOM 578 CE2 TRP A 86 191.321 234.870 807.205 1.00129.88 C ATOM 579 CZ2 TRP A 86 192.326 234.024 806.741 1.00129.94 C ATOM 580 CH2 TRP A 86 192.982 234.389 805.595 1.00130.88 C ATOM 581 CZ3 TRP A 86 192.657 235.575 804.911 1.00130.44 C ATOM 582 CE3 TRP A 86 191.659 236.419 805.373 1.00129.81 C ATOM 583 CD2 TRP A 86 190.972 236.066 806.541 1.00129.66 C ATOM 584 N ARG A 87 188.796 241.323 806.839 1.00128.12 N ATOM 585 CA ARG A 87 187.826 242.415 806.713 1.00132.62 C ATOM 586 C ARG A 87 186.917 242.158 805.517 1.00135.22 C ATOM 587 O ARG A 87 186.951 241.093 804.910 1.00134.69 O ATOM 588 CB ARG A 87 188.567 243.749 806.513 1.00162.27 C ATOM 589 CG ARG A 87 187.727 244.993 806.737 1.00164.58 C ATOM 590 CD ARG A 87 188.186 245.719 807.982 1.00167.56 C ATOM 591 NE ARG A 87 187.185 246.664 808.466 1.00171.79 N ATOM 592 CZ ARG A 87 187.312 247.376 809.583 1.00173.38 C ATOM 593 NH1 ARG A 87 188.406 247.244 810.326 1.00173.84 N ATOM 594 NH2 ARG A 87 186.347 248.208 809.965 1.00172.94 N ATOM 595 N GLU A 88 186.103 243.146 805.182 1.00182.53 N ATOM 596 CA GLU A 88 185.205 243.039 804.046 1.00182.53 C ATOM 597 C GLU A 88 184.895 244.445 803.563 1.00182.53 C ATOM 598 O GLU A 88 184.582 245.327 804.363 1.00182.53 O ATOM 599 CB GLU A 88 183.918 242.329 804.445 1.00172.05 C ATOM 600 CG GLU A 88 182.936 242.183 803.303 1.00173.22 C ATOM 601 CD GLU A 88 181.655 241.491 803.725 1.00173.78 C ATOM 602 OE1 GLU A 88 180.953 242.029 804.608 1.00173.19 O ATOM 603 OE2 GLU A 88 181.354 240.407 803.179 1.00173.09 O ATOM 604 N GLU A 89 184.994 244.655 802.254 1.00202.35 N ATOM 605 CA GLU A 89 184.736 245.965 801.672 1.00202.35 C ATOM 606 C GLU A 89 184.013 245.828 800.330 1.00202.35 C ATOM 607 O GLU A 89 184.555 246.148 799.271 1.00202.35 O ATOM 608 CB GLU A 89 186.061 246.733 801.541 1.00202.38 C ATOM 609 CG GLU A 89 186.653 247.120 802.919 1.00202.38 C ATOM 610 CD GLU A 89 188.099 247.608 802.876 1.00202.38 C ATOM 611 OE1 GLU A 89 188.397 248.551 802.113 1.00202.38 O ATOM 612 OE2 GLU A 89 188.939 247.050 803.624 1.00202.38 O ATOM 613 N ASN A 90 182.773 245.345 800.420 1.00202.38 N ATOM 614 CA ASN A 90 181.879 245.109 799.286 1.00202.38 C ATOM 615 C ASN A 90 182.318 243.854 798.535 1.00202.38 C ATOM 616 O ASN A 90 182.983 243.942 797.505 1.00202.38 O ATOM 617 CB ASN A 90 181.861 246.313 798.332 1.00181.75 C ATOM 618 CG ASN A 90 180.518 246.482 797.622 1.00181.75 C ATOM 619 OD1 ASN A 90 179.950 245.525 797.089 1.00181.75 O ATOM 620 ND2 ASN A 90 180.012 247.709 797.608 1.00181.75 N ATOM 621 N GLY A 91 181.943 242.691 799.063 1.00134.68 N ATOM 622 CA GLY A 91 182.314 241.426 798.448 1.00133.80 C ATOM 623 C GLY A 91 183.803 241.158 798.565 1.00132.44 C ATOM 624 O GLY A 91 184.271 240.032 798.353 1.00132.23 O ATOM 625 N THR A 92 184.546 242.206 798.910 1.00202.25 N ATOM 626 CA THR A 92 185.994 242.131 799.066 1.00202.25 C ATOM 627 C THR A 92 186.372 241.512 800.398 1.00202.25 C ATOM 628 O THR A 92 186.346 242.189 801.421 1.00202.25 O ATOM 629 CB THR A 92 186.664 243.534 799.035 1.00195.70 C ATOM 630 OG1 THR A 92 186.306 244.224 797.835 1.00195.70 O ATOM 631 CG2 THR A 92 188.181 243.404 799.099 1.00195.70 C ATOM 632 N TRP A 93 186.697 240.228 800.401 1.00131.13 N ATOM 633 CA TRP A 93 187.137 239.611 801.639 1.00127.96 C ATOM 634 C TRP A 93 188.657 239.531 801.556 1.00125.80 C ATOM 635 O TRP A 93 189.214 238.692 800.842 1.00124.91 O ATOM 636 CB TRP A 93 186.540 238.208 801.828 1.00171.48 C ATOM 637 CG TRP A 93 185.193 238.205 802.500 1.00170.51 C ATOM 638 CD1 TRP A 93 183.983 238.071 801.895 1.00169.95 C ATOM 639 NE1 TRP A 93 182.976 238.150 802.825 1.00169.23 N ATOM 640 CE2 TRP A 93 183.524 238.341 804.064 1.00170.03 C ATOM 641 CZ2 TRP A 93 182.908 238.481 805.312 1.00170.60 C ATOM 642 CH2 TRP A 93 183.719 238.668 806.402 1.00170.60 C ATOM 643 CZ3 TRP A 93 185.117 238.712 806.274 1.00170.10 C ATOM 644 CE3 TRP A 93 185.731 238.569 805.031 1.00170.87 C ATOM 645 CD2 TRP A 93 184.925 238.380 803.901 1.00170.53 C ATOM 646 N GLU A 94 189.327 240.437 802.257 1.00158.28 N ATOM 647 CA GLU A 94 190.777 240.449 802.261 1.00158.21 C ATOM 648 C GLU A 94 191.260 240.438 803.694 1.00156.57 C ATOM 649 O GLU A 94 190.478 240.311 804.629 1.00155.89 O ATOM 650 CB GLU A 94 191.321 241.693 801.546 1.00202.04 C ATOM 651 CG GLU A 94 190.960 241.794 800.071 1.00202.04 C ATOM 652 CD GLU A 94 191.699 242.918 799.358 1.00202.04 C ATOM 653 OE1 GLU A 94 191.733 244.048 799.889 1.00202.04 O ATOM 654 OE2 GLU A 94 192.242 242.671 798.260 1.00202.04 O ATOM 655 N LYS A 95 192.561 240.595 803.854 1.00169.91 N ATOM 656 CA LYS A 95 193.199 240.603 805.154 1.00169.91 C ATOM 657 C LYS A 95 193.572 242.057 805.497 1.00169.91 C ATOM 658 O LYS A 95 194.383 242.667 804.800 1.00169.91 O ATOM 659 CB LYS A 95 194.425 239.717 805.023 1.00166.76 C ATOM 660 CG LYS A 95 195.132 239.352 806.268 1.00164.98 C ATOM 661 CD LYS A 95 196.232 238.398 805.858 1.00162.41 C ATOM 662 CE LYS A 95 197.450 238.547 806.731 1.00161.33 C ATOM 663 NZ LYS A 95 198.645 237.937 806.093 1.00160.73 N ATOM 664 N SER A 96 192.972 242.628 806.541 1.00202.38 N ATOM 665 CA SER A 96 193.297 244.008 806.907 1.00202.38 C ATOM 666 C SER A 96 194.338 244.055 808.018 1.00202.38 C ATOM 667 O SER A 96 194.723 245.132 808.482 1.00202.38 O ATOM 668 CB SER A 96 192.042 244.800 807.311 1.00171.80 C ATOM 669 OG SER A 96 191.303 244.144 808.317 1.00172.14 O ATOM 670 N HIS A 97 194.783 242.869 808.435 1.00155.89 N ATOM 671 CA HIS A 97 195.823 242.719 809.450 1.00155.63 C ATOM 672 C HIS A 97 196.104 241.258 809.778 1.00155.17 C ATOM 673 O HIS A 97 195.282 240.372 809.527 1.00154.89 O ATOM 674 CB HIS A 97 195.479 243.454 810.752 1.00161.71 C ATOM 675 CG HIS A 97 196.624 243.519 811.715 1.00161.13 C ATOM 676 ND1 HIS A 97 197.778 244.228 811.449 1.00161.84 N ATOM 677 CE1 HIS A 97 198.634 244.059 812.441 1.00161.40 C ATOM 678 NE2 HIS A 97 198.079 243.269 813.343 1.00160.73 N ATOM 679 CD2 HIS A 97 196.821 242.919 812.913 1.00160.62 C ATOM 680 N GLU A 98 197.286 241.030 810.341 1.00128.76 N ATOM 681 CA GLU A 98 197.740 239.705 810.737 1.00128.80 C ATOM 682 C GLU A 98 198.660 239.859 811.946 1.00128.32 C ATOM 683 O GLU A 98 199.348 240.872 812.092 1.00127.66 O ATOM 684 CB GLU A 98 198.496 239.051 809.589 1.00170.03 C ATOM 685 CG GLU A 98 199.163 237.749 809.946 1.00170.06 C ATOM 686 CD GLU A 98 200.122 237.284 808.869 1.00169.55 C ATOM 687 OE1 GLU A 98 200.860 238.139 808.323 1.00168.66 O ATOM 688 OE2 GLU A 98 200.158 236.067 808.578 1.00168.45 O ATOM 689 N HIS A 99 198.673 238.859 812.818 1.00120.72 N ATOM 690 CA HIS A 99 199.507 238.930 814.005 1.00121.82 C ATOM 691 C HIS A 99 200.127 237.589 814.358 1.00122.08 C ATOM 692 O HIS A 99 199.423 236.638 814.705 1.00121.45 O ATOM 693 CB HIS A 99 198.688 239.449 815.186 1.00161.41 C ATOM 694 CG HIS A 99 199.492 239.661 816.424 1.00161.75 C ATOM 695 ND1 HIS A 99 199.301 238.919 817.569 1.00161.33 N ATOM 696 CE1 HIS A 99 200.173 239.303 818.486 1.00161.48 C ATOM 697 NE2 HIS A 99 200.918 240.268 817.976 1.00161.29 N ATOM 698 CD2 HIS A 99 200.512 240.512 816.688 1.00161.31 C ATOM 699 N ALA A 100 201.453 237.527 814.275 1.00160.40 N ATOM 700 CA ALA A 100 202.202 236.312 814.571 1.00161.14 C ATOM 701 C ALA A 100 203.117 236.564 815.760 1.00161.86 C ATOM 702 O ALA A 100 204.323 236.318 815.691 1.00162.84 O ATOM 703 CB ALA A 100 203.029 235.902 813.352 1.00202.38 C ATOM 704 N GLY A 101 202.537 237.047 816.853 1.00170.61 N ATOM 705 CA GLY A 101 203.319 237.346 818.038 1.00169.55 C ATOM 706 C GLY A 101 203.554 236.219 819.033 1.00169.14 C ATOM 707 O GLY A 101 204.125 236.464 820.100 1.00168.88 O ATOM 708 N HIS A 102 203.119 235.000 818.704 1.00137.44 N ATOM 709 CA HIS A 102 203.303 233.844 819.592 1.00137.46 C ATOM 710 C HIS A 102 204.140 232.736 818.948 1.00138.20 C ATOM 711 O HIS A 102 204.045 232.483 817.743 1.00139.39 O ATOM 712 CB HIS A 102 201.952 233.283 820.050 1.00103.97 C ATOM 713 CG HIS A 102 201.109 234.272 820.796 1.00103.74 C ATOM 714 ND1 HIS A 102 200.030 233.900 821.568 1.00104.71 N ATOM 715 CE1 HIS A 102 199.460 234.981 822.073 1.00105.19 C ATOM 716 NE2 HIS A 102 200.131 236.041 821.658 1.00103.53 N ATOM 717 CD2 HIS A 102 201.167 235.626 820.858 1.00103.32 C ATOM 718 N ASP A 103 204.947 232.077 819.780 1.00142.56 N ATOM 719 CA ASP A 103 205.869 231.026 819.352 1.00142.64 C ATOM 720 C ASP A 103 205.298 229.647 819.044 1.00141.22 C ATOM 721 O ASP A 103 205.993 228.814 818.468 1.00141.17 O ATOM 722 CB ASP A 103 206.980 230.861 820.397 1.00202.36 C ATOM 723 CG ASP A 103 207.669 232.176 820.737 1.00202.36 C ATOM 724 OD1 ASP A 103 208.192 232.845 819.818 1.00202.36 O ATOM 725 OD2 ASP A 103 207.689 232.540 821.932 1.00202.36 O ATOM 726 N SER A 104 204.052 229.393 819.426 1.00143.59 N ATOM 727 CA SER A 104 203.447 228.090 819.167 1.00143.59 C ATOM 728 C SER A 104 202.038 228.192 818.618 1.00143.59 C ATOM 729 O SER A 104 201.611 229.247 818.158 1.00143.59 O ATOM 730 CB SER A 104 203.424 227.244 820.443 1.00138.42 C ATOM 731 OG SER A 104 204.733 226.854 820.833 1.00140.28 O ATOM 732 N SER A 105 201.320 227.079 818.664 1.00135.91 N ATOM 733 CA SER A 105 199.955 227.044 818.176 1.00131.51 C ATOM 734 C SER A 105 199.106 228.066 818.908 1.00129.33 C ATOM 735 O SER A 105 199.438 228.466 820.012 1.00130.68 O ATOM 736 CB SER A 105 199.365 225.662 818.404 1.00142.65 C ATOM 737 OG SER A 105 197.964 225.688 818.205 1.00139.69 O ATOM 738 N VAL A 106 198.014 228.490 818.291 1.00127.96 N ATOM 739 CA VAL A 106 197.108 229.436 818.924 1.00126.23 C ATOM 740 C VAL A 106 195.767 228.729 818.975 1.00125.76 C ATOM 741 O VAL A 106 195.030 228.748 817.997 1.00125.86 O ATOM 742 CB VAL A 106 196.959 230.694 818.092 1.00 75.59 C ATOM 743 CG1 VAL A 106 195.958 231.643 818.740 1.00 75.67 C ATOM 744 CG2 VAL A 106 198.306 231.346 817.926 1.00 75.35 C ATOM 745 N ASN A 107 195.443 228.122 820.114 1.00122.07 N ATOM 746 CA ASN A 107 194.205 227.361 820.267 1.00120.62 C ATOM 747 C ASN A 107 192.853 228.031 820.207 1.00119.40 C ATOM 748 O ASN A 107 191.871 227.390 819.819 1.00120.45 O ATOM 749 CB ASN A 107 194.248 226.568 821.554 1.00147.20 C ATOM 750 CG ASN A 107 195.323 225.544 821.547 1.00147.20 C ATOM 751 OD1 ASN A 107 195.398 224.727 820.632 1.00147.20 O ATOM 752 ND2 ASN A 107 196.176 225.572 822.567 1.00147.20 N ATOM 753 N SER A 108 192.769 229.294 820.604 1.00117.05 N ATOM 754 CA SER A 108 191.466 229.926 820.588 1.00114.27 C ATOM 755 C SER A 108 191.504 231.435 820.445 1.00112.50 C ATOM 756 O SER A 108 192.530 232.078 820.674 1.00112.58 O ATOM 757 CB SER A 108 190.695 229.538 821.858 1.00112.44 C ATOM 758 OG SER A 108 189.336 229.941 821.780 1.00112.51 O ATOM 759 N VAL A 109 190.360 231.982 820.049 1.00114.89 N ATOM 760 CA VAL A 109 190.193 233.406 819.859 1.00114.38 C ATOM 761 C VAL A 109 188.801 233.786 820.302 1.00115.35 C ATOM 762 O VAL A 109 187.897 232.949 820.313 1.00115.28 O ATOM 763 CB VAL A 109 190.362 233.796 818.400 1.00 73.10 C ATOM 764 CG1 VAL A 109 189.857 235.200 818.183 1.00 72.34 C ATOM 765 CG2 VAL A 109 191.832 233.709 818.007 1.00 73.82 C ATOM 766 N CYS A 110 188.627 235.051 820.660 1.00101.08 N ATOM 767 CA CYS A 110 187.336 235.514 821.125 1.00101.74 C ATOM 768 C CYS A 110 187.317 237.032 821.086 1.00101.59 C ATOM 769 O CYS A 110 188.350 237.657 821.302 1.00101.08 O ATOM 770 CB CYS A 110 187.131 235.010 822.546 1.00155.17 C ATOM 771 SG CYS A 110 185.443 235.025 823.097 1.00155.23 S ATOM 772 N TRP A 111 186.166 237.633 820.788 1.00116.48 N ATOM 773 CA TRP A 111 186.091 239.091 820.753 1.00117.17 C ATOM 774 C TRP A 111 185.516 239.611 822.052 1.00117.35 C ATOM 775 O TRP A 111 184.633 238.995 822.645 1.00118.06 O ATOM 776 CB TRP A 111 185.226 239.590 819.593 1.00127.58 C ATOM 777 CG TRP A 111 185.785 239.273 818.260 1.00127.62 C ATOM 778 CD1 TRP A 111 185.537 238.165 817.519 1.00128.72 C ATOM 779 NE1 TRP A 111 186.277 238.190 816.362 1.00129.14 N ATOM 780 CE2 TRP A 111 187.025 239.334 816.340 1.00127.51 C ATOM 781 CZ2 TRP A 111 187.930 239.800 815.386 1.00127.87 C ATOM 782 CH2 TRP A 111 188.546 241.000 815.632 1.00126.32 C ATOM 783 CZ3 TRP A 111 188.284 241.733 816.797 1.00126.01 C ATOM 784 CE3 TRP A 111 187.384 241.266 817.747 1.00126.77 C ATOM 785 CD2 TRP A 111 186.740 240.044 817.522 1.00127.27 C ATOM 786 N ALA A 112 186.021 240.750 822.499 1.00 98.88 N ATOM 787 CA ALA A 112 185.542 241.334 823.733 1.00 99.26 C ATOM 788 C ALA A 112 184.211 241.985 823.454 1.00100.26 C ATOM 789 O ALA A 112 183.974 242.427 822.337 1.00 99.12 O ATOM 790 CB ALA A 112 186.518 242.367 824.215 1.00172.72 C ATOM 791 N PRO A 113 183.320 242.048 824.457 1.00 99.57 N ATOM 792 CA PRO A 113 182.004 242.673 824.274 1.00100.78 C ATOM 793 C PRO A 113 182.202 243.985 823.529 1.00100.25 C ATOM 794 O PRO A 113 183.103 244.738 823.851 1.00100.33 O ATOM 795 CB PRO A 113 181.522 242.869 825.702 1.00105.93 C ATOM 796 CG PRO A 113 182.052 241.642 826.370 1.00108.09 C ATOM 797 CD PRO A 113 183.471 241.541 825.828 1.00106.58 C ATOM 798 N HIS A 114 181.364 244.255 822.534 1.00136.73 N ATOM 799 CA HIS A 114 181.525 245.456 821.725 1.00135.51 C ATOM 800 C HIS A 114 181.680 246.803 822.408 1.00136.05 C ATOM 801 O HIS A 114 181.978 247.791 821.736 1.00136.10 O ATOM 802 CB HIS A 114 180.400 245.571 820.721 1.00111.11 C ATOM 803 CG HIS A 114 179.055 245.715 821.343 1.00110.18 C ATOM 804 ND1 HIS A 114 178.445 244.688 822.032 1.00110.45 N ATOM 805 CE1 HIS A 114 177.247 245.080 822.428 1.00111.53 C ATOM 806 NE2 HIS A 114 177.062 246.327 822.026 1.00110.76 N ATOM 807 CD2 HIS A 114 178.180 246.747 821.349 1.00110.34 C ATOM 808 N ASP A 115 181.481 246.872 823.719 1.00121.06 N ATOM 809 CA ASP A 115 181.626 248.151 824.415 1.00120.21 C ATOM 810 C ASP A 115 183.096 248.534 824.670 1.00119.09 C ATOM 811 O ASP A 115 183.461 249.707 824.589 1.00118.27 O ATOM 812 CB ASP A 115 180.836 248.129 825.724 1.00158.62 C ATOM 813 CG ASP A 115 179.334 248.005 825.498 1.00158.62 C ATOM 814 OD1 ASP A 115 178.784 248.802 824.705 1.00158.62 O ATOM 815 OD2 ASP A 115 178.699 247.122 826.116 1.00158.62 O ATOM 816 N TYR A 116 183.938 247.542 824.960 1.00106.33 N ATOM 817 CA TYR A 116 185.365 247.766 825.205 1.00104.80 C ATOM 818 C TYR A 116 186.073 248.131 823.890 1.00105.97 C ATOM 819 O TYR A 116 187.303 248.054 823.800 1.00105.99 O ATOM 820 CB TYR A 116 186.039 246.492 825.748 1.00111.93 C ATOM 821 CG TYR A 116 185.375 245.779 826.913 1.00109.38 C ATOM 822 CD1 TYR A 116 185.776 244.482 827.265 1.00108.73 C ATOM 823 CE1 TYR A 116 185.176 243.788 828.320 1.00108.95 C ATOM 824 CZ TYR A 116 184.158 244.394 829.039 1.00109.75 C ATOM 825 OH TYR A 116 183.537 243.694 830.053 1.00109.67 O ATOM 826 CE2 TYR A 116 183.744 245.688 828.713 1.00110.11 C ATOM 827 CD2 TYR A 116 184.357 246.375 827.652 1.00109.40 C ATOM 828 N GLY A 117 185.303 248.512 822.870 1.00177.73 N ATOM 829 CA GLY A 117 185.892 248.830 821.577 1.00178.57 C ATOM 830 C GLY A 117 185.934 247.555 820.745 1.00178.53 C ATOM 831 O GLY A 117 184.964 246.808 820.741 1.00179.24 O ATOM 832 N LEU A 118 187.029 247.300 820.034 1.00107.86 N ATOM 833 CA LEU A 118 187.158 246.074 819.247 1.00105.64 C ATOM 834 C LEU A 118 188.432 245.390 819.701 1.00106.24 C ATOM 835 O LEU A 118 189.512 245.740 819.238 1.00106.92 O ATOM 836 CB LEU A 118 187.278 246.369 817.744 1.00107.51 C ATOM 837 CG LEU A 118 187.459 245.164 816.798 1.00105.55 C ATOM 838 CD1 LEU A 118 186.117 244.603 816.397 1.00104.33 C ATOM 839 CD2 LEU A 118 188.186 245.596 815.558 1.00105.18 C ATOM 840 N ILE A 119 188.316 244.416 820.593 1.00110.86 N ATOM 841 CA ILE A 119 189.502 243.732 821.086 1.00109.11 C ATOM 842 C ILE A 119 189.447 242.235 820.887 1.00110.25 C ATOM 843 O ILE A 119 188.426 241.601 821.169 1.00112.83 O ATOM 844 CB ILE A 119 189.698 244.026 822.570 1.00116.69 C ATOM 845 CG1 ILE A 119 189.926 245.530 822.748 1.00115.33 C ATOM 846 CD1 ILE A 119 189.639 246.050 824.122 1.00111.14 C ATOM 847 CG2 ILE A 119 190.846 243.172 823.127 1.00116.02 C ATOM 848 N LEU A 120 190.547 241.667 820.404 1.00 95.85 N ATOM 849 CA LEU A 120 190.615 240.228 820.175 1.00 96.46 C ATOM 850 C LEU A 120 191.539 239.598 821.217 1.00 97.10 C ATOM 851 O LEU A 120 192.615 240.109 821.493 1.00 96.80 O ATOM 852 CB LEU A 120 191.129 239.936 818.758 1.00111.55 C ATOM 853 CG LEU A 120 190.923 238.519 818.219 1.00110.50 C ATOM 854 CD1 LEU A 120 189.441 238.254 818.145 1.00108.75 C ATOM 855 CD2 LEU A 120 191.561 238.366 816.851 1.00109.51 C ATOM 856 N ALA A 121 191.107 238.488 821.796 1.00102.27 N ATOM 857 CA ALA A 121 191.890 237.809 822.812 1.00104.97 C ATOM 858 C ALA A 121 192.322 236.439 822.317 1.00106.54 C ATOM 859 O ALA A 121 191.485 235.558 822.112 1.00107.81 O ATOM 860 CB ALA A 121 191.069 237.666 824.082 1.00174.55 C ATOM 861 N CYS A 122 193.626 236.249 822.145 1.00 98.50 N ATOM 862 CA CYS A 122 194.127 234.978 821.648 1.00100.54 C ATOM 863 C CYS A 122 195.096 234.297 822.595 1.00101.33 C ATOM 864 O CYS A 122 196.039 234.922 823.050 1.00100.97 O ATOM 865 CB CYS A 122 194.821 235.199 820.307 1.00198.03 C ATOM 866 SG CYS A 122 193.855 236.171 819.135 1.00199.77 S ATOM 867 N GLY A 123 194.867 233.016 822.878 1.00102.07 N ATOM 868 CA GLY A 123 195.753 232.264 823.754 1.00103.53 C ATOM 869 C GLY A 123 196.520 231.227 822.952 1.00104.22 C ATOM 870 O GLY A 123 195.921 230.488 822.185 1.00105.16 O ATOM 871 N SER A 124 197.836 231.155 823.118 1.00115.52 N ATOM 872 CA SER A 124 198.639 230.192 822.367 1.00116.20 C ATOM 873 C SER A 124 199.056 228.953 823.166 1.00117.16 C ATOM 874 O SER A 124 198.883 228.896 824.375 1.00118.42 O ATOM 875 CB SER A 124 199.887 230.873 821.806 1.00127.42 C ATOM 876 OG SER A 124 200.790 231.223 822.839 1.00127.48 O ATOM 877 N SER A 125 199.614 227.968 822.466 1.00116.27 N ATOM 878 CA SER A 125 200.048 226.706 823.056 1.00117.94 C ATOM 879 C SER A 125 201.392 226.796 823.757 1.00119.90 C ATOM 880 O SER A 125 201.905 225.790 824.258 1.00120.93 O ATOM 881 CB SER A 125 200.125 225.628 821.974 1.00126.06 C ATOM 882 OG SER A 125 200.788 224.466 822.445 1.00123.94 O ATOM 883 N ASP A 126 201.970 227.993 823.787 1.00151.70 N ATOM 884 CA ASP A 126 203.259 228.184 824.446 1.00152.95 C ATOM 885 C ASP A 126 203.062 228.659 825.886 1.00151.83 C ATOM 886 O ASP A 126 204.005 228.672 826.684 1.00151.77 O ATOM 887 CB ASP A 126 204.120 229.189 823.669 1.00171.47 C ATOM 888 CG ASP A 126 203.479 230.560 823.567 1.00172.47 C ATOM 889 OD1 ASP A 126 203.111 231.127 824.617 1.00173.53 O ATOM 890 OD2 ASP A 126 203.353 231.074 822.434 1.00174.03 O ATOM 891 N GLY A 127 201.831 229.047 826.204 1.00137.17 N ATOM 892 CA GLY A 127 201.513 229.502 827.542 1.00135.27 C ATOM 893 C GLY A 127 201.269 230.990 827.660 1.00134.76 C ATOM 894 O GLY A 127 201.124 231.495 828.769 1.00136.16 O ATOM 895 N ALA A 128 201.221 231.695 826.532 1.00132.95 N ATOM 896 CA ALA A 128 200.994 233.142 826.543 1.00131.33 C ATOM 897 C ALA A 128 199.585 233.528 826.082 1.00130.24 C ATOM 898 O ALA A 128 198.758 232.665 825.795 1.00130.80 O ATOM 899 CB ALA A 128 202.037 233.846 825.660 1.00115.96 C ATOM 900 N ILE A 129 199.323 234.827 826.023 1.00172.25 N ATOM 901 CA ILE A 129 198.034 235.357 825.578 1.00170.52 C ATOM 902 C ILE A 129 198.259 236.763 825.028 1.00171.17 C ATOM 903 O ILE A 129 198.985 237.550 825.626 1.00172.68 O ATOM 904 CB ILE A 129 197.021 235.425 826.732 1.00 82.98 C ATOM 905 CG1 ILE A 129 196.757 234.010 827.260 1.00 81.14 C ATOM 906 CD1 ILE A 129 195.898 233.956 828.526 1.00 80.00 C ATOM 907 CG2 ILE A 129 195.726 236.055 826.262 1.00 83.21 C ATOM 908 N SER A 130 197.679 237.078 823.876 1.00106.83 N ATOM 909 CA SER A 130 197.851 238.410 823.307 1.00105.07 C ATOM 910 C SER A 130 196.495 239.099 823.288 1.00103.64 C ATOM 911 O SER A 130 195.460 238.444 823.371 1.00103.50 O ATOM 912 CB SER A 130 198.460 238.336 821.893 1.00202.38 C ATOM 913 OG SER A 130 197.641 237.601 820.999 1.00202.38 O ATOM 914 N LEU A 131 196.503 240.422 823.203 1.00112.84 N ATOM 915 CA LEU A 131 195.267 241.184 823.182 1.00113.65 C ATOM 916 C LEU A 131 195.314 242.317 822.172 1.00114.87 C ATOM 917 O LEU A 131 195.723 243.445 822.482 1.00112.62 O ATOM 918 CB LEU A 131 194.965 241.722 824.575 1.00112.82 C ATOM 919 CG LEU A 131 194.375 240.620 825.448 1.00111.68 C ATOM 920 CD1 LEU A 131 194.659 240.864 826.922 1.00113.71 C ATOM 921 CD2 LEU A 131 192.885 240.552 825.174 1.00110.97 C ATOM 922 N LEU A 132 194.884 242.001 820.952 1.00142.12 N ATOM 923 CA LEU A 132 194.866 242.967 819.869 1.00143.32 C ATOM 924 C LEU A 132 193.770 243.997 820.059 1.00145.40 C ATOM 925 O LEU A 132 192.586 243.668 820.016 1.00146.79 O ATOM 926 CB LEU A 132 194.623 242.278 818.533 1.00119.59 C ATOM 927 CG LEU A 132 195.440 241.063 818.125 1.00117.91 C ATOM 928 CD1 LEU A 132 195.224 240.884 816.641 1.00117.32 C ATOM 929 CD2 LEU A 132 196.918 241.243 818.414 1.00117.66 C ATOM 930 N THR A 133 194.166 245.242 820.276 1.00107.29 N ATOM 931 CA THR A 133 193.201 246.321 820.428 1.00109.81 C ATOM 932 C THR A 133 193.275 247.017 819.069 1.00112.48 C ATOM 933 O THR A 133 194.234 246.808 818.330 1.00111.83 O ATOM 934 CB THR A 133 193.608 247.289 821.582 1.00153.58 C ATOM 935 OG1 THR A 133 193.877 246.533 822.779 1.00153.05 O ATOM 936 CG2 THR A 133 192.487 248.300 821.859 1.00152.52 C ATOM 937 N TYR A 134 192.286 247.831 818.723 1.00139.92 N ATOM 938 CA TYR A 134 192.288 248.491 817.420 1.00144.98 C ATOM 939 C TYR A 134 192.427 250.016 817.536 1.00148.25 C ATOM 940 O TYR A 134 191.752 250.633 818.358 1.00148.89 O ATOM 941 CB TYR A 134 190.998 248.113 816.696 1.00157.96 C ATOM 942 CG TYR A 134 190.874 248.591 815.269 1.00160.59 C ATOM 943 CD1 TYR A 134 191.842 248.278 814.320 1.00161.50 C ATOM 944 CE1 TYR A 134 191.689 248.656 812.991 1.00161.50 C ATOM 945 CZ TYR A 134 190.557 249.362 812.602 1.00161.50 C ATOM 946 OH TYR A 134 190.386 249.728 811.283 1.00161.50 O ATOM 947 CE2 TYR A 134 189.585 249.692 813.530 1.00161.50 C ATOM 948 CD2 TYR A 134 189.747 249.306 814.853 1.00161.41 C ATOM 949 N THR A 135 193.290 250.622 816.713 1.00172.14 N ATOM 950 CA THR A 135 193.506 252.077 816.749 1.00175.13 C ATOM 951 C THR A 135 193.379 252.800 815.413 1.00178.07 C ATOM 952 O THR A 135 194.325 252.819 814.626 1.00177.99 O ATOM 953 CB THR A 135 194.907 252.434 817.276 1.00168.82 C ATOM 954 OG1 THR A 135 195.075 251.903 818.592 1.00168.82 O ATOM 955 CG2 THR A 135 195.097 253.959 817.305 1.00168.82 C ATOM 956 N GLY A 136 192.218 253.409 815.172 1.00202.07 N ATOM 957 CA GLY A 136 191.993 254.165 813.948 1.00202.07 C ATOM 958 C GLY A 136 192.153 253.515 812.577 1.00202.07 C ATOM 959 O GLY A 136 191.158 253.286 811.888 1.00202.07 O ATOM 960 N GLU A 137 193.398 253.239 812.175 1.00170.81 N ATOM 961 CA GLU A 137 193.690 252.637 810.868 1.00170.81 C ATOM 962 C GLU A 137 194.395 251.289 810.992 1.00170.81 C ATOM 963 O GLU A 137 194.476 250.737 812.084 1.00170.81 O ATOM 964 CB GLU A 137 194.563 253.584 810.047 1.00200.29 C ATOM 965 CG GLU A 137 193.962 254.960 809.862 1.00200.29 C ATOM 966 CD GLU A 137 192.979 255.034 808.698 1.00200.29 C ATOM 967 OE1 GLU A 137 192.019 254.233 808.645 1.00200.29 O ATOM 968 OE2 GLU A 137 193.175 255.908 807.833 1.00200.29 O ATOM 969 N GLY A 138 194.896 250.774 809.867 1.00171.33 N ATOM 970 CA GLY A 138 195.589 249.493 809.855 1.00171.33 C ATOM 971 C GLY A 138 196.720 249.404 810.867 1.00171.33 C ATOM 972 O GLY A 138 197.886 249.226 810.507 1.00171.33 O ATOM 973 N GLN A 139 196.364 249.522 812.144 1.00202.38 N ATOM 974 CA GLN A 139 197.324 249.475 813.241 1.00202.38 C ATOM 975 C GLN A 139 196.736 248.740 814.434 1.00202.38 C ATOM 976 O GLN A 139 195.602 249.003 814.846 1.00202.38 O ATOM 977 CB GLN A 139 197.696 250.882 813.685 1.00188.26 C ATOM 978 CG GLN A 139 197.620 251.921 812.600 1.00188.26 C ATOM 979 CD GLN A 139 198.264 253.212 813.030 1.00188.26 C ATOM 980 OE1 GLN A 139 198.127 253.628 814.180 1.00188.26 O ATOM 981 NE2 GLN A 139 198.967 253.861 812.110 1.00188.26 N ATOM 982 N TRP A 140 197.527 247.836 814.997 1.00154.71 N ATOM 983 CA TRP A 140 197.089 247.051 816.136 1.00152.61 C ATOM 984 C TRP A 140 198.180 246.859 817.185 1.00151.41 C ATOM 985 O TRP A 140 199.248 246.306 816.893 1.00151.72 O ATOM 986 CB TRP A 140 196.617 245.675 815.670 1.00169.59 C ATOM 987 CG TRP A 140 195.423 245.685 814.747 1.00167.02 C ATOM 988 CD1 TRP A 140 195.398 246.041 813.427 1.00165.89 C ATOM 989 NE1 TRP A 140 194.128 245.887 812.918 1.00164.35 N ATOM 990 CE2 TRP A 140 193.308 245.429 813.913 1.00164.47 C ATOM 991 CZ2 TRP A 140 191.955 245.127 813.887 1.00164.29 C ATOM 992 CH2 TRP A 140 191.389 244.680 815.049 1.00164.21 C ATOM 993 CZ3 TRP A 140 192.143 244.532 816.224 1.00164.15 C ATOM 994 CE3 TRP A 140 193.483 244.831 816.250 1.00164.25 C ATOM 995 CD2 TRP A 140 194.091 245.290 815.078 1.00165.30 C ATOM 996 N GLU A 141 197.898 247.313 818.406 1.00152.86 N ATOM 997 CA GLU A 141 198.837 247.178 819.512 1.00151.40 C ATOM 998 C GLU A 141 198.632 245.813 820.123 1.00149.29 C ATOM 999 O GLU A 141 197.557 245.231 819.999 1.00149.93 O ATOM 1000 CB GLU A 141 198.583 248.247 820.555 1.00192.52 C ATOM 1001 CG GLU A 141 198.721 249.627 820.000 1.00194.71 C ATOM 1002 CD GLU A 141 198.226 250.657 820.964 1.00195.00 C ATOM 1003 OE1 GLU A 141 198.746 250.691 822.098 1.00195.00 O ATOM 1004 OE2 GLU A 141 197.318 251.426 820.594 1.00195.00 O ATOM 1005 N VAL A 142 199.645 245.297 820.799 1.00145.03 N ATOM 1006 CA VAL A 142 199.506 243.968 821.359 1.00141.74 C ATOM 1007 C VAL A 142 199.969 243.820 822.803 1.00141.69 C ATOM 1008 O VAL A 142 201.061 243.319 823.051 1.00141.77 O ATOM 1009 CB VAL A 142 200.272 242.937 820.494 1.00132.00 C ATOM 1010 CG1 VAL A 142 199.864 241.525 820.887 1.00129.72 C ATOM 1011 CG2 VAL A 142 200.026 243.207 819.001 1.00130.60 C ATOM 1012 N LYS A 143 199.149 244.251 823.757 1.00142.17 N ATOM 1013 CA LYS A 143 199.500 244.099 825.173 1.00140.10 C ATOM 1014 C LYS A 143 199.373 242.593 825.479 1.00138.67 C ATOM 1015 O LYS A 143 198.269 242.076 825.646 1.00139.11 O ATOM 1016 CB LYS A 143 198.549 244.939 826.046 1.00162.97 C ATOM 1017 CG LYS A 143 198.672 246.453 825.816 1.00162.56 C ATOM 1018 CD LYS A 143 197.602 247.254 826.560 1.00161.53 C ATOM 1019 CE LYS A 143 196.204 247.063 825.959 1.00161.05 C ATOM 1020 NZ LYS A 143 195.137 247.814 826.698 1.00158.14 N ATOM 1021 N LYS A 144 200.520 241.907 825.546 1.00106.40 N ATOM 1022 CA LYS A 144 200.611 240.453 825.767 1.00105.17 C ATOM 1023 C LYS A 144 200.928 239.963 827.207 1.00105.72 C ATOM 1024 O LYS A 144 201.672 240.598 827.951 1.00104.87 O ATOM 1025 CB LYS A 144 201.643 239.897 824.760 1.00114.91 C ATOM 1026 CG LYS A 144 201.918 238.388 824.759 1.00113.37 C ATOM 1027 CD LYS A 144 203.022 238.070 823.744 1.00111.19 C ATOM 1028 CE LYS A 144 203.685 236.722 823.983 1.00110.52 C ATOM 1029 NZ LYS A 144 204.919 236.587 823.153 1.00106.72 N ATOM 1030 N ILE A 145 200.351 238.811 827.563 1.00136.90 N ATOM 1031 CA ILE A 145 200.479 238.151 828.878 1.00136.77 C ATOM 1032 C ILE A 145 201.411 236.916 828.863 1.00139.09 C ATOM 1033 O ILE A 145 200.950 235.774 828.729 1.00138.46 O ATOM 1034 CB ILE A 145 199.074 237.680 829.365 1.00 91.22 C ATOM 1035 CG1 ILE A 145 198.215 238.878 829.735 1.00 88.91 C ATOM 1036 CD1 ILE A 145 196.772 238.494 830.015 1.00 88.57 C ATOM 1037 CG2 ILE A 145 199.192 236.702 830.510 1.00 90.70 C ATOM 1038 N ASN A 146 202.713 237.130 829.020 1.00139.32 N ATOM 1039 CA ASN A 146 203.647 236.007 829.010 1.00141.46 C ATOM 1040 C ASN A 146 203.455 235.029 830.170 1.00142.95 C ATOM 1041 O ASN A 146 203.116 235.426 831.289 1.00144.49 O ATOM 1042 CB ASN A 146 205.081 236.530 828.989 1.00154.91 C ATOM 1043 CG ASN A 146 205.607 236.717 827.581 1.00154.91 C ATOM 1044 OD1 ASN A 146 205.885 235.742 826.879 1.00154.91 O ATOM 1045 ND2 ASN A 146 205.737 237.968 827.153 1.00154.91 N ATOM 1046 N ASN A 147 203.671 233.745 829.891 1.00133.30 N ATOM 1047 CA ASN A 147 203.524 232.697 830.897 1.00133.96 C ATOM 1048 C ASN A 147 202.265 232.879 831.743 1.00134.50 C ATOM 1049 O ASN A 147 202.339 233.113 832.955 1.00136.28 O ATOM 1050 CB ASN A 147 204.763 232.655 831.798 1.00160.29 C ATOM 1051 CG ASN A 147 205.907 231.854 831.188 1.00162.50 C ATOM 1052 OD1 ASN A 147 206.178 231.946 829.989 1.00162.88 O ATOM 1053 ND2 ASN A 147 206.592 231.070 832.016 1.00164.93 N ATOM 1054 N ALA A 148 201.110 232.775 831.093 1.00132.84 N ATOM 1055 CA ALA A 148 199.829 232.915 831.776 1.00131.27 C ATOM 1056 C ALA A 148 199.365 231.545 832.242 1.00130.14 C ATOM 1057 O ALA A 148 198.613 231.421 833.206 1.00130.89 O ATOM 1058 CB ALA A 148 198.815 233.524 830.848 1.00 60.76 C ATOM 1059 N HIS A 149 199.820 230.520 831.537 1.00142.93 N ATOM 1060 CA HIS A 149 199.496 229.144 831.870 1.00140.94 C ATOM 1061 C HIS A 149 200.796 228.357 831.811 1.00140.56 C ATOM 1062 O HIS A 149 201.748 228.772 831.152 1.00141.12 O ATOM 1063 CB HIS A 149 198.465 228.600 830.891 1.00116.57 C ATOM 1064 CG HIS A 149 197.059 228.993 831.224 1.00114.89 C ATOM 1065 ND1 HIS A 149 196.329 228.373 832.214 1.00114.36 N ATOM 1066 CE1 HIS A 149 195.139 228.940 832.304 1.00114.61 C ATOM 1067 NE2 HIS A 149 195.069 229.907 831.407 1.00114.74 N ATOM 1068 CD2 HIS A 149 196.257 229.961 830.719 1.00114.89 C ATOM 1069 N THR A 150 200.844 227.227 832.499 1.00148.52 N ATOM 1070 CA THR A 150 202.069 226.445 832.546 1.00147.76 C ATOM 1071 C THR A 150 202.477 225.742 831.245 1.00147.16 C ATOM 1072 O THR A 150 203.511 226.084 830.666 1.00146.36 O ATOM 1073 CB THR A 150 202.015 225.434 833.731 1.00176.48 C ATOM 1074 OG1 THR A 150 201.763 226.150 834.950 1.00176.29 O ATOM 1075 CG2 THR A 150 203.332 224.693 833.876 1.00177.03 C ATOM 1076 N ILE A 151 201.682 224.785 830.769 1.00152.08 N ATOM 1077 CA ILE A 151 202.031 224.058 829.541 1.00152.19 C ATOM 1078 C ILE A 151 201.465 224.703 828.276 1.00152.04 C ATOM 1079 O ILE A 151 201.979 224.498 827.169 1.00151.92 O ATOM 1080 CB ILE A 151 201.524 222.605 829.595 1.00162.07 C ATOM 1081 CG1 ILE A 151 201.913 221.964 830.933 1.00162.25 C ATOM 1082 CD1 ILE A 151 201.244 220.624 831.194 1.00162.10 C ATOM 1083 CG2 ILE A 151 202.093 221.816 828.416 1.00162.03 C ATOM 1084 N GLY A 152 200.394 225.475 828.459 1.00140.12 N ATOM 1085 CA GLY A 152 199.745 226.146 827.351 1.00138.96 C ATOM 1086 C GLY A 152 198.334 226.606 827.687 1.00137.24 C ATOM 1087 O GLY A 152 197.816 226.338 828.773 1.00138.41 O ATOM 1088 N CYS A 153 197.711 227.299 826.738 1.00146.03 N ATOM 1089 CA CYS A 153 196.359 227.821 826.891 1.00142.57 C ATOM 1090 C CYS A 153 195.465 227.219 825.803 1.00140.72 C ATOM 1091 O CYS A 153 195.903 227.062 824.664 1.00139.34 O ATOM 1092 CB CYS A 153 196.393 229.346 826.770 1.00130.67 C ATOM 1093 SG CYS A 153 194.798 230.160 826.864 1.00130.74 S ATOM 1094 N ASN A 154 194.226 226.879 826.154 1.00120.86 N ATOM 1095 CA ASN A 154 193.288 226.287 825.198 1.00119.25 C ATOM 1096 C ASN A 154 192.052 227.148 824.960 1.00116.33 C ATOM 1097 O ASN A 154 191.646 227.390 823.819 1.00117.11 O ATOM 1098 CB ASN A 154 192.824 224.918 825.686 1.00125.97 C ATOM 1099 CG ASN A 154 193.967 223.964 825.908 1.00125.97 C ATOM 1100 OD1 ASN A 154 194.896 223.890 825.103 1.00125.97 O ATOM 1101 ND2 ASN A 154 193.901 223.208 826.999 1.00125.97 N ATOM 1102 N ALA A 155 191.451 227.599 826.049 1.00123.05 N ATOM 1103 CA ALA A 155 190.253 228.404 825.954 1.00119.36 C ATOM 1104 C ALA A 155 190.384 229.801 826.493 1.00116.91 C ATOM 1105 O ALA A 155 191.062 230.062 827.478 1.00116.93 O ATOM 1106 CB ALA A 155 189.096 227.696 826.648 1.00202.38 C ATOM 1107 N VAL A 156 189.688 230.692 825.816 1.00108.19 N ATOM 1108 CA VAL A 156 189.627 232.081 826.174 1.00105.39 C ATOM 1109 C VAL A 156 188.153 232.478 826.031 1.00104.66 C ATOM 1110 O VAL A 156 187.532 232.201 824.997 1.00103.52 O ATOM 1111 CB VAL A 156 190.490 232.894 825.218 1.00134.95 C ATOM 1112 CG1 VAL A 156 190.296 234.376 825.458 1.00134.77 C ATOM 1113 CG2 VAL A 156 191.951 232.501 825.408 1.00134.37 C ATOM 1114 N SER A 157 187.579 233.086 827.072 1.00 99.92 N ATOM 1115 CA SER A 157 186.178 233.517 827.028 1.00 98.99 C ATOM 1116 C SER A 157 186.100 234.875 827.699 1.00 98.92 C ATOM 1117 O SER A 157 186.709 235.079 828.723 1.00 99.76 O ATOM 1118 CB SER A 157 185.268 232.503 827.747 1.00109.24 C ATOM 1119 OG SER A 157 183.904 232.888 827.694 1.00109.71 O ATOM 1120 N TRP A 158 185.379 235.813 827.110 1.00 89.27 N ATOM 1121 CA TRP A 158 185.249 237.142 827.691 1.00 93.65 C ATOM 1122 C TRP A 158 184.077 237.276 828.651 1.00 96.25 C ATOM 1123 O TRP A 158 182.979 236.819 828.343 1.00 97.14 O ATOM 1124 CB TRP A 158 185.069 238.176 826.600 1.00110.71 C ATOM 1125 CG TRP A 158 186.325 238.555 825.998 1.00111.62 C ATOM 1126 CD1 TRP A 158 187.051 237.849 825.093 1.00111.77 C ATOM 1127 NE1 TRP A 158 188.206 238.515 824.780 1.00110.30 N ATOM 1128 CE2 TRP A 158 188.247 239.679 825.517 1.00110.44 C ATOM 1129 CZ2 TRP A 158 189.184 240.691 825.511 1.00111.51 C ATOM 1130 CH2 TRP A 158 188.953 241.745 826.358 1.00112.82 C ATOM 1131 CZ3 TRP A 158 187.772 241.838 827.124 1.00112.05 C ATOM 1132 CE3 TRP A 158 186.845 240.833 827.112 1.00111.14 C ATOM 1133 CD2 TRP A 158 187.049 239.744 826.249 1.00110.87 C ATOM 1134 N ALA A 159 184.303 237.915 829.801 1.00100.79 N ATOM 1135 CA ALA A 159 183.247 238.120 830.791 1.00103.82 C ATOM 1136 C ALA A 159 182.223 239.109 830.216 1.00105.71 C ATOM 1137 O ALA A 159 182.593 240.042 829.502 1.00106.15 O ATOM 1138 CB ALA A 159 183.847 238.661 832.085 1.00169.46 C ATOM 1139 N PRO A 160 180.929 238.933 830.543 1.00120.56 N ATOM 1140 CA PRO A 160 179.862 239.813 830.047 1.00123.81 C ATOM 1141 C PRO A 160 180.137 241.303 830.205 1.00128.03 C ATOM 1142 O PRO A 160 180.848 241.711 831.132 1.00127.81 O ATOM 1143 CB PRO A 160 178.649 239.372 830.857 1.00150.14 C ATOM 1144 CG PRO A 160 179.252 238.970 832.161 1.00150.31 C ATOM 1145 CD PRO A 160 180.439 238.148 831.692 1.00149.49 C ATOM 1146 N ALA A 161 179.505 242.112 829.301 1.00104.93 N ATOM 1147 CA ALA A 161 179.689 243.557 829.341 1.00110.40 C ATOM 1148 C ALA A 161 178.785 244.176 830.412 1.00115.34 C ATOM 1149 O ALA A 161 177.637 244.552 830.129 1.00115.24 O ATOM 1150 CB ALA A 161 179.382 244.164 827.977 1.00202.38 C ATOM 1151 N VAL A 162 179.306 244.277 831.639 1.00148.22 N ATOM 1152 CA VAL A 162 178.562 244.850 832.770 1.00152.77 C ATOM 1153 C VAL A 162 178.995 246.303 833.040 1.00156.07 C ATOM 1154 O VAL A 162 180.183 246.579 833.202 1.00155.89 O ATOM 1155 CB VAL A 162 178.765 243.998 834.065 1.00147.38 C ATOM 1156 CG1 VAL A 162 178.076 244.663 835.244 1.00147.66 C ATOM 1157 CG2 VAL A 162 178.203 242.580 833.867 1.00148.25 C ATOM 1158 N VAL A 163 178.017 247.213 833.080 1.00186.38 N ATOM 1159 CA VAL A 163 178.236 248.653 833.316 1.00186.38 C ATOM 1160 C VAL A 163 178.432 248.994 834.810 1.00186.38 C ATOM 1161 O VAL A 163 177.834 248.360 835.682 1.00186.38 O ATOM 1162 CB VAL A 163 177.037 249.486 832.742 1.00142.15 C ATOM 1163 CG1 VAL A 163 177.142 250.951 833.156 1.00140.99 C ATOM 1164 CG2 VAL A 163 177.011 249.378 831.219 1.00143.38 C ATOM 1165 N PRO A 164 179.275 250.004 835.119 1.00196.71 N ATOM 1166 CA PRO A 164 179.539 250.409 836.505 1.00196.71 C ATOM 1167 C PRO A 164 178.447 251.276 837.118 1.00196.71 C ATOM 1168 O PRO A 164 178.724 252.109 837.984 1.00196.71 O ATOM 1169 CB PRO A 164 180.855 251.162 836.389 1.00196.49 C ATOM 1170 CG PRO A 164 180.682 251.875 835.091 1.00196.49 C ATOM 1171 CD PRO A 164 180.122 250.782 834.193 1.00196.49 C ATOM 1172 N GLY A 173 180.810 263.335 832.096 1.00184.07 N ATOM 1173 CA GLY A 173 181.431 262.327 831.261 1.00185.03 C ATOM 1174 C GLY A 173 180.540 261.121 831.004 1.00185.11 C ATOM 1175 O GLY A 173 179.758 260.719 831.879 1.00185.11 O ATOM 1176 N GLN A 174 180.663 260.549 829.801 1.00202.38 N ATOM 1177 CA GLN A 174 179.886 259.371 829.377 1.00202.38 C ATOM 1178 C GLN A 174 180.760 258.277 828.700 1.00202.38 C ATOM 1179 O GLN A 174 181.848 258.568 828.181 1.00202.38 O ATOM 1180 CB GLN A 174 178.735 259.803 828.438 1.00174.02 C ATOM 1181 CG GLN A 174 177.713 260.759 829.085 1.00174.02 C ATOM 1182 CD GLN A 174 176.440 260.925 828.270 1.00174.02 C ATOM 1183 OE1 GLN A 174 176.480 261.286 827.092 1.00174.02 O ATOM 1184 NE2 GLN A 174 175.298 260.667 828.902 1.00174.02 N ATOM 1185 N LYS A 175 180.257 257.035 828.710 1.00202.36 N ATOM 1186 CA LYS A 175 180.924 255.826 828.173 1.00202.36 C ATOM 1187 C LYS A 175 181.839 255.237 829.261 1.00202.36 C ATOM 1188 O LYS A 175 183.032 255.011 829.026 1.00202.36 O ATOM 1189 CB LYS A 175 181.758 256.130 826.909 1.00184.48 C ATOM 1190 CG LYS A 175 180.965 256.141 825.601 1.00183.31 C ATOM 1191 CD LYS A 175 181.881 256.239 824.383 1.00182.04 C ATOM 1192 CE LYS A 175 181.080 256.226 823.089 1.00181.51 C ATOM 1193 NZ LYS A 175 181.959 256.312 821.896 1.00181.69 N ATOM 1194 N PRO A 176 181.270 254.941 830.456 1.00202.21 N ATOM 1195 CA PRO A 176 181.940 254.390 831.648 1.00202.21 C ATOM 1196 C PRO A 176 183.062 253.358 831.491 1.00202.21 C ATOM 1197 O PRO A 176 183.148 252.652 830.484 1.00202.21 O ATOM 1198 CB PRO A 176 180.772 253.860 832.495 1.00178.55 C ATOM 1199 CG PRO A 176 179.704 253.582 831.493 1.00178.55 C ATOM 1200 CD PRO A 176 179.809 254.783 830.590 1.00178.55 C ATOM 1201 N ASN A 177 183.927 253.303 832.505 1.00169.17 N ATOM 1202 CA ASN A 177 185.046 252.360 832.540 1.00169.17 C ATOM 1203 C ASN A 177 184.499 251.019 832.999 1.00169.17 C ATOM 1204 O ASN A 177 183.735 250.947 833.966 1.00169.17 O ATOM 1205 CB ASN A 177 186.135 252.839 833.508 1.00191.59 C ATOM 1206 CG ASN A 177 187.180 253.706 832.830 1.00191.31 C ATOM 1207 OD1 ASN A 177 187.933 253.236 831.974 1.00191.61 O ATOM 1208 ND2 ASN A 177 187.229 254.981 833.206 1.00191.29 N ATOM 1209 N TYR A 178 184.892 249.958 832.301 1.00134.01 N ATOM 1210 CA TYR A 178 184.399 248.627 832.620 1.00130.14 C ATOM 1211 C TYR A 178 185.426 247.732 833.300 1.00127.32 C ATOM 1212 O TYR A 178 186.629 247.856 833.062 1.00125.30 O ATOM 1213 CB TYR A 178 183.907 247.929 831.341 1.00135.75 C ATOM 1214 CG TYR A 178 182.812 248.665 830.572 1.00135.14 C ATOM 1215 CD1 TYR A 178 183.119 249.523 829.506 1.00134.81 C ATOM 1216 CE1 TYR A 178 182.111 250.217 828.825 1.00134.34 C ATOM 1217 CZ TYR A 178 180.782 250.052 829.212 1.00134.25 C ATOM 1218 OH TYR A 178 179.768 250.744 828.586 1.00134.06 O ATOM 1219 CE2 TYR A 178 180.455 249.204 830.257 1.00134.84 C ATOM 1220 CD2 TYR A 178 181.468 248.516 830.932 1.00135.07 C ATOM 1221 N ILE A 179 184.936 246.840 834.156 1.00183.31 N ATOM 1222 CA ILE A 179 185.801 245.885 834.829 1.00181.29 C ATOM 1223 C ILE A 179 186.066 244.838 833.732 1.00179.00 C ATOM 1224 O ILE A 179 185.592 243.702 833.819 1.00179.77 O ATOM 1225 CB ILE A 179 185.086 245.199 836.038 1.00142.03 C ATOM 1226 CG1 ILE A 179 184.529 246.240 837.009 1.00142.49 C ATOM 1227 CD1 ILE A 179 183.845 245.632 838.243 1.00142.70 C ATOM 1228 CG2 ILE A 179 186.067 244.309 836.794 1.00141.70 C ATOM 1229 N LYS A 180 186.797 245.243 832.690 1.00136.68 N ATOM 1230 CA LYS A 180 187.124 244.366 831.563 1.00132.95 C ATOM 1231 C LYS A 180 187.764 243.052 831.994 1.00131.58 C ATOM 1232 O LYS A 180 188.987 242.943 832.045 1.00131.70 O ATOM 1233 CB LYS A 180 188.074 245.072 830.583 1.00102.82 C ATOM 1234 CG LYS A 180 187.499 246.310 829.919 1.00101.19 C ATOM 1235 CD LYS A 180 188.508 246.976 828.989 1.00 98.55 C ATOM 1236 CE LYS A 180 188.003 248.357 828.559 1.00 98.15 C ATOM 1237 NZ LYS A 180 189.002 249.152 827.773 1.00 98.29 N ATOM 1238 N ARG A 181 186.936 242.053 832.296 1.00128.60 N ATOM 1239 CA ARG A 181 187.434 240.740 832.699 1.00125.54 C ATOM 1240 C ARG A 181 187.225 239.724 831.580 1.00121.45 C ATOM 1241 O ARG A 181 186.439 239.945 830.658 1.00122.35 O ATOM 1242 CB ARG A 181 186.708 240.241 833.945 1.00145.54 C ATOM 1243 CG ARG A 181 186.816 241.132 835.147 1.00148.26 C ATOM 1244 CD ARG A 181 186.189 240.448 836.333 1.00152.43 C ATOM 1245 NE ARG A 181 185.953 241.370 837.429 1.00156.37 N ATOM 1246 CZ ARG A 181 185.414 241.020 838.590 1.00158.04 C ATOM 1247 NH1 ARG A 181 185.055 239.756 838.807 1.00157.59 N ATOM 1248 NH2 ARG A 181 185.219 241.941 839.524 1.00158.98 N ATOM 1249 N PHE A 182 187.927 238.605 831.681 1.00 93.63 N ATOM 1250 CA PHE A 182 187.843 237.537 830.706 1.00 88.96 C ATOM 1251 C PHE A 182 188.534 236.303 831.265 1.00 87.75 C ATOM 1252 O PHE A 182 189.653 236.391 831.722 1.00 89.10 O ATOM 1253 CB PHE A 182 188.505 237.977 829.385 1.00 95.28 C ATOM 1254 CG PHE A 182 190.027 237.877 829.355 1.00 90.50 C ATOM 1255 CD1 PHE A 182 190.682 236.632 829.352 1.00 88.17 C ATOM 1256 CE1 PHE A 182 192.082 236.546 829.247 1.00 86.39 C ATOM 1257 CZ PHE A 182 192.845 237.712 829.141 1.00 86.15 C ATOM 1258 CE2 PHE A 182 192.208 238.963 829.143 1.00 87.27 C ATOM 1259 CD2 PHE A 182 190.803 239.038 829.251 1.00 88.96 C ATOM 1260 N ALA A 183 187.895 235.149 831.242 1.00 87.96 N ATOM 1261 CA ALA A 183 188.560 233.968 831.785 1.00 87.65 C ATOM 1262 C ALA A 183 189.357 233.173 830.749 1.00 88.38 C ATOM 1263 O ALA A 183 189.426 233.561 829.581 1.00 89.06 O ATOM 1264 CB ALA A 183 187.525 233.085 832.447 1.00 54.13 C ATOM 1265 N SER A 184 189.968 232.072 831.179 1.00 93.99 N ATOM 1266 CA SER A 184 190.710 231.222 830.255 1.00 96.27 C ATOM 1267 C SER A 184 191.354 230.006 830.911 1.00 97.44 C ATOM 1268 O SER A 184 192.210 230.149 831.766 1.00 98.60 O ATOM 1269 CB SER A 184 191.787 232.029 829.529 1.00 97.14 C ATOM 1270 OG SER A 184 192.957 232.143 830.307 1.00 97.24 O ATOM 1271 N GLY A 185 190.953 228.806 830.498 1.00103.21 N ATOM 1272 CA GLY A 185 191.524 227.588 831.058 1.00107.29 C ATOM 1273 C GLY A 185 192.736 227.149 830.257 1.00110.59 C ATOM 1274 O GLY A 185 192.941 227.621 829.141 1.00110.61 O ATOM 1275 N GLY A 186 193.542 226.248 830.810 1.00109.52 N ATOM 1276 CA GLY A 186 194.732 225.800 830.103 1.00112.68 C ATOM 1277 C GLY A 186 195.118 224.345 830.322 1.00114.57 C ATOM 1278 O GLY A 186 194.301 223.526 830.758 1.00115.76 O ATOM 1279 N CYS A 187 196.372 224.021 830.010 1.00134.53 N ATOM 1280 CA CYS A 187 196.882 222.659 830.165 1.00134.33 C ATOM 1281 C CYS A 187 197.375 222.402 831.584 1.00134.70 C ATOM 1282 O CYS A 187 197.658 221.266 831.959 1.00133.64 O ATOM 1283 CB CYS A 187 198.036 222.421 829.199 1.00151.71 C ATOM 1284 SG CYS A 187 197.729 222.957 827.519 1.00149.02 S ATOM 1285 N ASP A 188 197.500 223.466 832.366 1.00142.82 N ATOM 1286 CA ASP A 188 197.957 223.340 833.733 1.00144.17 C ATOM 1287 C ASP A 188 196.828 222.951 834.672 1.00144.13 C ATOM 1288 O ASP A 188 197.057 222.798 835.865 1.00145.12 O ATOM 1289 CB ASP A 188 198.599 224.644 834.207 1.00145.48 C ATOM 1290 CG ASP A 188 197.849 225.875 833.739 1.00147.88 C ATOM 1291 OD1 ASP A 188 198.149 226.366 832.632 1.00148.85 O ATOM 1292 OD2 ASP A 188 196.954 226.352 834.469 1.00148.79 O ATOM 1293 N ASN A 189 195.618 222.794 834.131 1.00120.57 N ATOM 1294 CA ASN A 189 194.425 222.398 834.900 1.00119.47 C ATOM 1295 C ASN A 189 193.719 223.576 835.598 1.00117.20 C ATOM 1296 O ASN A 189 192.685 223.409 836.266 1.00117.87 O ATOM 1297 CB ASN A 189 194.789 221.330 835.947 1.00141.75 C ATOM 1298 CG ASN A 189 195.529 220.134 835.349 1.00142.56 C ATOM 1299 OD1 ASN A 189 196.116 219.331 836.075 1.00143.03 O ATOM 1300 ND2 ASN A 189 195.496 220.008 834.032 1.00143.88 N ATOM 1301 N LEU A 190 194.271 224.768 835.432 1.00128.38 N ATOM 1302 CA LEU A 190 193.691 225.929 836.072 1.00124.58 C ATOM 1303 C LEU A 190 192.898 226.806 835.122 1.00120.83 C ATOM 1304 O LEU A 190 193.249 226.971 833.966 1.00119.70 O ATOM 1305 CB LEU A 190 194.797 226.755 836.738 1.00196.05 C ATOM 1306 CG LEU A 190 195.475 226.109 837.950 1.00196.05 C ATOM 1307 CD1 LEU A 190 196.743 226.867 838.328 1.00196.05 C ATOM 1308 CD2 LEU A 190 194.489 226.086 839.105 1.00196.05 C ATOM 1309 N ILE A 191 191.823 227.377 835.624 1.00107.84 N ATOM 1310 CA ILE A 191 191.018 228.255 834.816 1.00103.61 C ATOM 1311 C ILE A 191 191.214 229.653 835.391 1.00101.76 C ATOM 1312 O ILE A 191 190.462 230.082 836.254 1.00104.42 O ATOM 1313 CB ILE A 191 189.538 227.869 834.905 1.00 75.85 C ATOM 1314 CG1 ILE A 191 189.390 226.352 834.822 1.00 76.64 C ATOM 1315 CD1 ILE A 191 187.982 225.881 835.183 1.00 79.18 C ATOM 1316 CG2 ILE A 191 188.764 228.526 833.787 1.00 76.78 C ATOM 1317 N LYS A 192 192.225 230.363 834.913 1.00 88.90 N ATOM 1318 CA LYS A 192 192.509 231.709 835.397 1.00 84.42 C ATOM 1319 C LYS A 192 191.630 232.859 834.857 1.00 84.50 C ATOM 1320 O LYS A 192 191.560 233.042 833.659 1.00 87.71 O ATOM 1321 CB LYS A 192 193.975 232.023 835.099 1.00 88.94 C ATOM 1322 CG LYS A 192 194.924 230.949 835.593 1.00 84.98 C ATOM 1323 CD LYS A 192 196.380 231.395 835.550 1.00 83.52 C ATOM 1324 CE LYS A 192 197.312 230.253 835.968 1.00 82.36 C ATOM 1325 NZ LYS A 192 198.775 230.611 835.967 1.00 82.38 N ATOM 1326 N LEU A 193 190.962 233.626 835.728 1.00 71.35 N ATOM 1327 CA LEU A 193 190.161 234.798 835.301 1.00 73.61 C ATOM 1328 C LEU A 193 191.163 235.928 835.115 1.00 75.13 C ATOM 1329 O LEU A 193 192.286 235.784 835.575 1.00 76.15 O ATOM 1330 CB LEU A 193 189.195 235.217 836.382 1.00 78.23 C ATOM 1331 CG LEU A 193 188.076 234.261 836.779 1.00 80.62 C ATOM 1332 CD1 LEU A 193 186.766 234.669 836.064 1.00 82.50 C ATOM 1333 CD2 LEU A 193 188.504 232.818 836.478 1.00 83.00 C ATOM 1334 N TRP A 194 190.812 237.040 834.460 1.00 83.87 N ATOM 1335 CA TRP A 194 191.785 238.151 834.279 1.00 88.82 C ATOM 1336 C TRP A 194 191.127 239.524 834.361 1.00 94.42 C ATOM 1337 O TRP A 194 189.913 239.641 834.190 1.00 96.49 O ATOM 1338 CB TRP A 194 192.563 238.034 832.951 1.00103.26 C ATOM 1339 CG TRP A 194 193.267 236.723 832.797 1.00101.50 C ATOM 1340 CD1 TRP A 194 192.687 235.492 832.690 1.00103.05 C ATOM 1341 NE1 TRP A 194 193.635 234.503 832.693 1.00101.46 N ATOM 1342 CE2 TRP A 194 194.867 235.084 832.789 1.00 99.83 C ATOM 1343 CZ2 TRP A 194 196.136 234.493 832.825 1.00 99.38 C ATOM 1344 CH2 TRP A 194 197.217 235.332 832.930 1.00 99.60 C ATOM 1345 CZ3 TRP A 194 197.057 236.740 832.996 1.00 99.79 C ATOM 1346 CE3 TRP A 194 195.784 237.326 832.958 1.00 99.78 C ATOM 1347 CD2 TRP A 194 194.670 236.491 832.854 1.00 99.99 C ATOM 1348 N LYS A 195 191.911 240.584 834.599 1.00129.34 N ATOM 1349 CA LYS A 195 191.345 241.921 834.716 1.00136.70 C ATOM 1350 C LYS A 195 192.311 242.970 834.227 1.00141.29 C ATOM 1351 O LYS A 195 193.508 242.893 834.494 1.00141.54 O ATOM 1352 CB LYS A 195 190.973 242.188 836.180 1.00139.62 C ATOM 1353 CG LYS A 195 190.401 243.565 836.472 1.00142.47 C ATOM 1354 CD LYS A 195 190.054 243.702 837.952 1.00143.76 C ATOM 1355 CE LYS A 195 189.566 245.112 838.284 1.00145.28 C ATOM 1356 NZ LYS A 195 189.187 245.276 839.720 1.00145.98 N ATOM 1357 N GLU A 196 191.786 243.951 833.505 1.00151.58 N ATOM 1358 CA GLU A 196 192.615 245.017 832.986 1.00157.99 C ATOM 1359 C GLU A 196 192.806 246.066 834.075 1.00162.04 C ATOM 1360 O GLU A 196 191.853 246.744 834.469 1.00162.83 O ATOM 1361 CB GLU A 196 191.955 245.646 831.764 1.00165.43 C ATOM 1362 CG GLU A 196 192.865 246.588 831.023 1.00168.55 C ATOM 1363 CD GLU A 196 192.204 247.171 829.808 1.00169.33 C ATOM 1364 OE1 GLU A 196 191.104 247.741 829.974 1.00169.47 O ATOM 1365 OE2 GLU A 196 192.783 247.059 828.701 1.00169.47 O ATOM 1366 N GLU A 197 194.035 246.178 834.577 1.00202.38 N ATOM 1367 CA GLU A 197 194.355 247.154 835.618 1.00202.38 C ATOM 1368 C GLU A 197 194.165 248.509 834.951 1.00202.38 C ATOM 1369 O GLU A 197 194.672 248.722 833.848 1.00202.38 O ATOM 1370 CB GLU A 197 195.810 246.984 836.071 1.00202.38 C ATOM 1371 CG GLU A 197 196.147 247.649 837.401 1.00202.38 C ATOM 1372 CD GLU A 197 195.368 247.058 838.565 1.00202.38 C ATOM 1373 OE1 GLU A 197 195.429 245.823 838.749 1.00202.38 O ATOM 1374 OE2 GLU A 197 194.703 247.828 839.297 1.00202.38 O ATOM 1375 N GLU A 198 193.451 249.422 835.607 1.00139.72 N ATOM 1376 CA GLU A 198 193.180 250.730 835.004 1.00141.21 C ATOM 1377 C GLU A 198 194.361 251.542 834.452 1.00140.96 C ATOM 1378 O GLU A 198 194.176 252.668 833.972 1.00140.95 O ATOM 1379 CB GLU A 198 192.398 251.606 835.967 1.00168.62 C ATOM 1380 CG GLU A 198 191.701 252.721 835.241 1.00169.96 C ATOM 1381 CD GLU A 198 190.780 253.489 836.130 1.00169.96 C ATOM 1382 OE1 GLU A 198 190.426 252.964 837.205 1.00169.96 O ATOM 1383 OE2 GLU A 198 190.398 254.609 835.750 1.00169.96 O ATOM 1384 N ASP A 199 195.560 250.963 834.504 1.00148.45 N ATOM 1385 CA ASP A 199 196.768 251.617 834.013 1.00147.92 C ATOM 1386 C ASP A 199 197.126 251.197 832.586 1.00146.50 C ATOM 1387 O ASP A 199 197.438 252.037 831.740 1.00146.33 O ATOM 1388 CB ASP A 199 197.954 251.318 834.944 1.00164.44 C ATOM 1389 CG ASP A 199 198.142 249.830 835.207 1.00165.11 C ATOM 1390 OD1 ASP A 199 197.522 249.006 834.504 1.00165.52 O ATOM 1391 OD2 ASP A 199 198.922 249.482 836.120 1.00165.54 O ATOM 1392 N GLY A 200 197.083 249.898 832.320 1.00178.95 N ATOM 1393 CA GLY A 200 197.419 249.426 830.993 1.00176.21 C ATOM 1394 C GLY A 200 197.485 247.921 830.831 1.00173.57 C ATOM 1395 O GLY A 200 197.089 247.412 829.781 1.00173.34 O ATOM 1396 N GLN A 201 197.971 247.200 831.841 1.00139.99 N ATOM 1397 CA GLN A 201 198.067 245.745 831.717 1.00137.14 C ATOM 1398 C GLN A 201 197.097 244.904 832.567 1.00134.68 C ATOM 1399 O GLN A 201 196.479 245.367 833.532 1.00133.09 O ATOM 1400 CB GLN A 201 199.519 245.261 831.928 1.00164.17 C ATOM 1401 CG GLN A 201 199.953 245.062 833.378 1.00164.13 C ATOM 1402 CD GLN A 201 200.946 246.114 833.877 1.00164.20 C ATOM 1403 OE1 GLN A 201 202.046 246.265 833.334 1.00164.11 O ATOM 1404 NE2 GLN A 201 200.557 246.837 834.921 1.00164.43 N ATOM 1405 N TRP A 202 196.941 243.667 832.112 1.00154.94 N ATOM 1406 CA TRP A 202 196.074 242.646 832.693 1.00151.95 C ATOM 1407 C TRP A 202 196.822 241.853 833.762 1.00151.39 C ATOM 1408 O TRP A 202 197.971 241.452 833.560 1.00150.06 O ATOM 1409 CB TRP A 202 195.590 241.673 831.585 1.00151.07 C ATOM 1410 CG TRP A 202 194.343 242.099 830.811 1.00149.93 C ATOM 1411 CD1 TRP A 202 193.037 241.785 831.105 1.00148.48 C ATOM 1412 NE1 TRP A 202 192.189 242.422 830.234 1.00146.89 N ATOM 1413 CE2 TRP A 202 192.935 243.163 829.353 1.00148.07 C ATOM 1414 CZ2 TRP A 202 192.529 243.980 828.295 1.00148.84 C ATOM 1415 CH2 TRP A 202 193.508 244.616 827.567 1.00149.75 C ATOM 1416 CZ3 TRP A 202 194.867 244.450 827.868 1.00150.77 C ATOM 1417 CE3 TRP A 202 195.273 243.634 828.922 1.00151.54 C ATOM 1418 CD2 TRP A 202 194.296 242.977 829.683 1.00149.88 C ATOM 1419 N LYS A 203 196.170 241.637 834.900 1.00133.04 N ATOM 1420 CA LYS A 203 196.743 240.856 835.996 1.00132.12 C ATOM 1421 C LYS A 203 195.716 239.782 836.356 1.00131.72 C ATOM 1422 O LYS A 203 194.539 240.094 836.563 1.00131.54 O ATOM 1423 CB LYS A 203 197.050 241.765 837.195 1.00154.12 C ATOM 1424 CG LYS A 203 198.385 242.514 837.055 1.00152.79 C ATOM 1425 CD LYS A 203 198.421 243.816 837.851 1.00151.38 C ATOM 1426 CE LYS A 203 199.699 244.596 837.568 1.00150.04 C ATOM 1427 NZ LYS A 203 199.679 245.934 838.214 1.00147.88 N ATOM 1428 N GLU A 204 196.145 238.522 836.418 1.00116.85 N ATOM 1429 CA GLU A 204 195.200 237.457 836.709 1.00117.13 C ATOM 1430 C GLU A 204 194.530 237.608 838.054 1.00116.48 C ATOM 1431 O GLU A 204 195.151 237.411 839.086 1.00115.94 O ATOM 1432 CB GLU A 204 195.857 236.084 836.600 1.00121.57 C ATOM 1433 CG GLU A 204 196.877 235.748 837.634 1.00124.44 C ATOM 1434 CD GLU A 204 197.375 234.324 837.471 1.00125.79 C ATOM 1435 OE1 GLU A 204 198.094 234.044 836.478 1.00125.42 O ATOM 1436 OE2 GLU A 204 197.038 233.475 838.326 1.00126.66 O ATOM 1437 N GLU A 205 193.248 237.958 838.022 1.00128.68 N ATOM 1438 CA GLU A 205 192.451 238.161 839.224 1.00129.32 C ATOM 1439 C GLU A 205 192.310 236.905 840.083 1.00129.18 C ATOM 1440 O GLU A 205 192.204 237.007 841.298 1.00129.27 O ATOM 1441 CB GLU A 205 191.062 238.692 838.843 1.00171.59 C ATOM 1442 CG GLU A 205 190.240 239.260 840.008 1.00171.59 C ATOM 1443 CD GLU A 205 188.868 239.792 839.580 1.00171.59 C ATOM 1444 OE1 GLU A 205 187.945 238.975 839.348 1.00171.59 O ATOM 1445 OE2 GLU A 205 188.715 241.030 839.472 1.00171.59 O ATOM 1446 N GLN A 206 192.313 235.724 839.472 1.00135.76 N ATOM 1447 CA GLN A 206 192.177 234.487 840.241 1.00136.49 C ATOM 1448 C GLN A 206 192.419 233.216 839.424 1.00135.90 C ATOM 1449 O GLN A 206 192.377 233.247 838.203 1.00137.21 O ATOM 1450 CB GLN A 206 190.785 234.433 840.885 1.00152.56 C ATOM 1451 CG GLN A 206 190.421 233.088 841.496 1.00154.71 C ATOM 1452 CD GLN A 206 189.759 233.218 842.858 1.00157.05 C ATOM 1453 OE1 GLN A 206 188.997 234.159 843.103 1.00158.93 O ATOM 1454 NE2 GLN A 206 190.035 232.260 843.749 1.00158.29 N ATOM 1455 N LYS A 207 192.701 232.111 840.116 1.00 93.30 N ATOM 1456 CA LYS A 207 192.926 230.800 839.501 1.00 93.01 C ATOM 1457 C LYS A 207 191.753 229.934 839.962 1.00 92.78 C ATOM 1458 O LYS A 207 191.199 230.149 841.042 1.00 92.33 O ATOM 1459 CB LYS A 207 194.255 230.164 839.970 1.00144.74 C ATOM 1460 CG LYS A 207 195.541 230.819 839.430 1.00147.25 C ATOM 1461 CD LYS A 207 196.806 230.004 839.790 1.00148.27 C ATOM 1462 CE LYS A 207 198.088 230.606 839.178 1.00148.00 C ATOM 1463 NZ LYS A 207 199.291 229.702 839.231 1.00148.31 N ATOM 1464 N LEU A 208 191.352 228.971 839.139 1.00151.67 N ATOM 1465 CA LEU A 208 190.240 228.096 839.497 1.00152.06 C ATOM 1466 C LEU A 208 190.666 226.651 839.357 1.00153.06 C ATOM 1467 O LEU A 208 190.856 226.152 838.248 1.00153.99 O ATOM 1468 CB LEU A 208 189.032 228.375 838.603 1.00111.52 C ATOM 1469 CG LEU A 208 188.437 229.780 838.738 1.00110.58 C ATOM 1470 CD1 LEU A 208 187.368 230.006 837.702 1.00112.75 C ATOM 1471 CD2 LEU A 208 187.860 229.955 840.120 1.00108.88 C ATOM 1472 N GLU A 209 190.833 225.981 840.490 1.00148.90 N ATOM 1473 CA GLU A 209 191.250 224.594 840.465 1.00148.90 C ATOM 1474 C GLU A 209 190.133 223.660 840.856 1.00146.62 C ATOM 1475 O GLU A 209 189.322 223.971 841.732 1.00146.77 O ATOM 1476 CB GLU A 209 192.425 224.354 841.408 1.00202.38 C ATOM 1477 CG GLU A 209 192.966 222.931 841.298 1.00202.38 C ATOM 1478 CD GLU A 209 193.784 222.499 842.503 1.00202.38 C ATOM 1479 OE1 GLU A 209 194.702 223.246 842.900 1.00202.38 O ATOM 1480 OE2 GLU A 209 193.512 221.404 843.045 1.00202.38 O ATOM 1481 N ALA A 210 190.118 222.501 840.202 1.00128.96 N ATOM 1482 CA ALA A 210 189.131 221.455 840.442 1.00125.23 C ATOM 1483 C ALA A 210 189.264 220.446 839.313 1.00122.76 C ATOM 1484 O ALA A 210 188.922 219.273 839.454 1.00122.51 O ATOM 1485 CB ALA A 210 187.712 222.037 840.469 1.00 64.21 C ATOM 1486 N HIS A 211 189.771 220.919 838.184 1.00127.15 N ATOM 1487 CA HIS A 211 189.945 220.056 837.032 1.00126.41 C ATOM 1488 C HIS A 211 191.202 219.256 837.247 1.00126.73 C ATOM 1489 O HIS A 211 192.255 219.825 837.535 1.00127.09 O ATOM 1490 CB HIS A 211 190.060 220.887 835.748 1.00117.77 C ATOM 1491 CG HIS A 211 188.741 221.327 835.191 1.00114.78 C ATOM 1492 ND1 HIS A 211 187.797 220.436 834.730 1.00113.39 N ATOM 1493 CE1 HIS A 211 186.738 221.102 834.305 1.00113.70 C ATOM 1494 NE2 HIS A 211 186.960 222.392 834.474 1.00112.95 N ATOM 1495 CD2 HIS A 211 188.207 222.561 835.026 1.00113.75 C ATOM 1496 N SER A 212 191.088 217.938 837.121 1.00114.90 N ATOM 1497 CA SER A 212 192.232 217.052 837.305 1.00115.93 C ATOM 1498 C SER A 212 193.097 216.840 836.056 1.00116.58 C ATOM 1499 O SER A 212 194.062 216.072 836.102 1.00116.63 O ATOM 1500 CB SER A 212 191.778 215.689 837.868 1.00115.93 C ATOM 1501 OG SER A 212 190.655 215.160 837.189 1.00117.87 O ATOM 1502 N ASP A 213 192.767 217.527 834.956 1.00141.88 N ATOM 1503 CA ASP A 213 193.519 217.415 833.698 1.00142.53 C ATOM 1504 C ASP A 213 193.339 218.678 832.848 1.00142.61 C ATOM 1505 O ASP A 213 192.716 219.638 833.288 1.00143.68 O ATOM 1506 CB ASP A 213 193.043 216.192 832.905 1.00155.71 C ATOM 1507 CG ASP A 213 194.157 215.542 832.096 1.00155.15 C ATOM 1508 OD1 ASP A 213 194.825 216.254 831.313 1.00154.99 O ATOM 1509 OD2 ASP A 213 194.360 214.313 832.248 1.00155.02 O ATOM 1510 N TRP A 214 193.884 218.672 831.634 1.00128.69 N ATOM 1511 CA TRP A 214 193.789 219.816 830.710 1.00127.51 C ATOM 1512 C TRP A 214 192.405 220.460 830.605 1.00125.79 C ATOM 1513 O TRP A 214 191.423 219.776 830.319 1.00125.68 O ATOM 1514 CB TRP A 214 194.197 219.375 829.301 1.00150.26 C ATOM 1515 CG TRP A 214 195.657 219.379 829.020 1.00149.64 C ATOM 1516 CD1 TRP A 214 196.668 219.333 829.927 1.00150.61 C ATOM 1517 NE1 TRP A 214 197.880 219.317 829.283 1.00151.20 N ATOM 1518 CE2 TRP A 214 197.665 219.350 827.931 1.00149.14 C ATOM 1519 CZ2 TRP A 214 198.577 219.348 826.870 1.00149.48 C ATOM 1520 CH2 TRP A 214 198.071 219.387 825.602 1.00149.01 C ATOM 1521 CZ3 TRP A 214 196.688 219.426 825.371 1.00149.05 C ATOM 1522 CE3 TRP A 214 195.784 219.427 826.422 1.00148.01 C ATOM 1523 CD2 TRP A 214 196.274 219.389 827.729 1.00148.20 C ATOM 1524 N VAL A 215 192.320 221.770 830.816 1.00122.27 N ATOM 1525 CA VAL A 215 191.033 222.449 830.681 1.00120.40 C ATOM 1526 C VAL A 215 190.843 222.622 829.173 1.00119.29 C ATOM 1527 O VAL A 215 191.586 223.362 828.529 1.00118.79 O ATOM 1528 CB VAL A 215 191.026 223.849 831.362 1.00111.94 C ATOM 1529 CG1 VAL A 215 189.690 224.526 831.154 1.00111.13 C ATOM 1530 CG2 VAL A 215 191.282 223.712 832.848 1.00115.43 C ATOM 1531 N ARG A 216 189.860 221.929 828.606 1.00120.90 N ATOM 1532 CA ARG A 216 189.610 222.019 827.177 1.00118.05 C ATOM 1533 C ARG A 216 188.962 223.309 826.683 1.00117.11 C ATOM 1534 O ARG A 216 189.463 223.917 825.745 1.00118.16 O ATOM 1535 CB ARG A 216 188.787 220.823 826.718 1.00108.71 C ATOM 1536 CG ARG A 216 189.635 219.732 826.129 1.00108.45 C ATOM 1537 CD ARG A 216 190.346 220.283 824.920 1.00107.25 C ATOM 1538 NE ARG A 216 191.508 219.482 824.567 1.00105.21 N ATOM 1539 CZ ARG A 216 192.480 219.914 823.773 1.00103.61 C ATOM 1540 NH1 ARG A 216 192.431 221.136 823.243 1.00101.46 N ATOM 1541 NH2 ARG A 216 193.517 219.134 823.532 1.00105.14 N ATOM 1542 N ASP A 217 187.859 223.730 827.294 1.00117.83 N ATOM 1543 CA ASP A 217 187.183 224.960 826.874 1.00116.56 C ATOM 1544 C ASP A 217 186.585 225.653 828.113 1.00115.91 C ATOM 1545 O ASP A 217 186.268 224.996 829.109 1.00117.57 O ATOM 1546 CB ASP A 217 186.085 224.622 825.836 1.00132.58 C ATOM 1547 CG ASP A 217 185.808 225.767 824.841 1.00133.43 C ATOM 1548 OD1 ASP A 217 186.771 226.287 824.232 1.00131.71 O ATOM 1549 OD2 ASP A 217 184.624 226.135 824.648 1.00134.66 O ATOM 1550 N VAL A 218 186.443 226.976 828.054 1.00 95.53 N ATOM 1551 CA VAL A 218 185.888 227.754 829.157 1.00 92.89 C ATOM 1552 C VAL A 218 184.849 228.724 828.606 1.00 91.18 C ATOM 1553 O VAL A 218 185.157 229.518 827.717 1.00 90.00 O ATOM 1554 CB VAL A 218 186.979 228.560 829.827 1.00130.61 C ATOM 1555 CG1 VAL A 218 186.408 229.314 830.986 1.00132.46 C ATOM 1556 CG2 VAL A 218 188.077 227.645 830.287 1.00132.89 C ATOM 1557 N ALA A 219 183.624 228.698 829.129 1.00 74.69 N ATOM 1558 CA ALA A 219 182.620 229.599 828.583 1.00 76.01 C ATOM 1559 C ALA A 219 181.866 230.468 829.578 1.00 76.93 C ATOM 1560 O ALA A 219 181.035 229.979 830.339 1.00 75.82 O ATOM 1561 CB ALA A 219 181.636 228.808 827.744 1.00202.38 C ATOM 1562 N TRP A 220 182.145 231.768 829.515 1.00 70.71 N ATOM 1563 CA TRP A 220 181.531 232.778 830.376 1.00 75.08 C ATOM 1564 C TRP A 220 180.047 233.028 830.035 1.00 76.96 C ATOM 1565 O TRP A 220 179.729 233.915 829.240 1.00 78.48 O ATOM 1566 CB TRP A 220 182.317 234.110 830.250 1.00131.76 C ATOM 1567 CG TRP A 220 182.952 234.726 831.536 1.00134.52 C ATOM 1568 CD1 TRP A 220 184.296 234.962 831.769 1.00136.06 C ATOM 1569 NE1 TRP A 220 184.468 235.627 832.957 1.00134.19 N ATOM 1570 CE2 TRP A 220 183.240 235.832 833.524 1.00135.23 C ATOM 1571 CZ2 TRP A 220 182.907 236.458 834.718 1.00136.88 C ATOM 1572 CH2 TRP A 220 181.578 236.523 835.044 1.00138.57 C ATOM 1573 CZ3 TRP A 220 180.586 235.978 834.205 1.00137.54 C ATOM 1574 CE3 TRP A 220 180.916 235.357 833.023 1.00136.36 C ATOM 1575 CD2 TRP A 220 182.263 235.276 832.661 1.00135.09 C ATOM 1576 N ALA A 221 179.145 232.263 830.645 1.00 93.72 N ATOM 1577 CA ALA A 221 177.699 232.427 830.435 1.00 96.36 C ATOM 1578 C ALA A 221 177.252 233.889 830.574 1.00 98.89 C ATOM 1579 O ALA A 221 177.304 234.442 831.666 1.00 97.83 O ATOM 1580 CB ALA A 221 176.941 231.565 831.436 1.00140.21 C ATOM 1581 N PRO A 222 176.761 234.507 829.480 1.00 93.04 N ATOM 1582 CA PRO A 222 176.293 235.903 829.406 1.00 97.12 C ATOM 1583 C PRO A 222 175.111 236.298 830.286 1.00100.78 C ATOM 1584 O PRO A 222 173.969 235.982 829.990 1.00101.61 O ATOM 1585 CB PRO A 222 175.979 236.081 827.927 1.00180.35 C ATOM 1586 CG PRO A 222 175.440 234.752 827.571 1.00180.35 C ATOM 1587 CD PRO A 222 176.446 233.812 828.222 1.00180.35 C ATOM 1588 N SER A 223 175.411 237.031 831.353 1.00165.77 N ATOM 1589 CA SER A 223 174.410 237.479 832.313 1.00170.47 C ATOM 1590 C SER A 223 173.128 238.023 831.695 1.00173.24 C ATOM 1591 O SER A 223 173.126 239.078 831.051 1.00173.05 O ATOM 1592 CB SER A 223 175.010 238.541 833.249 1.00202.38 C ATOM 1593 OG SER A 223 175.299 239.753 832.564 1.00202.38 O ATOM 1594 N ILE A 224 172.040 237.281 831.893 1.00202.38 N ATOM 1595 CA ILE A 224 170.724 237.689 831.414 1.00202.38 C ATOM 1596 C ILE A 224 170.310 238.816 832.350 1.00202.38 C ATOM 1597 O ILE A 224 169.386 238.654 833.147 1.00202.38 O ATOM 1598 CB ILE A 224 169.676 236.536 831.530 1.00141.20 C ATOM 1599 CG1 ILE A 224 169.912 235.733 832.827 1.00141.20 C ATOM 1600 CD1 ILE A 224 168.915 234.608 833.072 1.00140.40 C ATOM 1601 CG2 ILE A 224 169.698 235.683 830.259 1.00141.20 C ATOM 1602 N GLY A 225 171.015 239.945 832.268 1.00193.23 N ATOM 1603 CA GLY A 225 170.722 241.080 833.133 1.00194.93 C ATOM 1604 C GLY A 225 170.977 240.794 834.609 1.00195.24 C ATOM 1605 O GLY A 225 171.395 241.685 835.356 1.00195.24 O ATOM 1606 N LEU A 226 170.726 239.545 835.015 1.00202.38 N ATOM 1607 CA LEU A 226 170.900 239.050 836.387 1.00202.38 C ATOM 1608 C LEU A 226 172.371 239.174 836.831 1.00202.38 C ATOM 1609 O LEU A 226 173.282 238.866 836.059 1.00202.38 O ATOM 1610 CB LEU A 226 170.436 237.584 836.448 1.00146.23 C ATOM 1611 CG LEU A 226 169.599 237.146 837.652 1.00144.93 C ATOM 1612 CD1 LEU A 226 170.458 237.125 838.903 1.00145.02 C ATOM 1613 CD2 LEU A 226 168.404 238.096 837.817 1.00144.15 C ATOM 1614 N PRO A 227 172.623 239.621 838.082 1.00202.38 N ATOM 1615 CA PRO A 227 173.998 239.780 838.590 1.00202.38 C ATOM 1616 C PRO A 227 174.789 238.512 838.971 1.00202.38 C ATOM 1617 O PRO A 227 175.979 238.597 839.285 1.00202.38 O ATOM 1618 CB PRO A 227 173.807 240.718 839.779 1.00148.00 C ATOM 1619 CG PRO A 227 172.470 240.275 840.318 1.00148.00 C ATOM 1620 CD PRO A 227 171.638 240.130 839.061 1.00148.00 C ATOM 1621 N THR A 228 174.134 237.351 838.923 1.00158.85 N ATOM 1622 CA THR A 228 174.735 236.051 839.276 1.00152.04 C ATOM 1623 C THR A 228 175.708 235.471 838.231 1.00148.72 C ATOM 1624 O THR A 228 175.580 234.303 837.864 1.00149.16 O ATOM 1625 CB THR A 228 173.623 234.976 839.490 1.00115.87 C ATOM 1626 OG1 THR A 228 172.392 235.620 839.864 1.00114.73 O ATOM 1627 CG2 THR A 228 174.043 233.950 840.558 1.00114.07 C ATOM 1628 N SER A 229 176.683 236.247 837.768 1.00122.81 N ATOM 1629 CA SER A 229 177.610 235.754 836.739 1.00117.43 C ATOM 1630 C SER A 229 178.151 234.314 836.924 1.00113.48 C ATOM 1631 O SER A 229 178.665 233.946 837.980 1.00111.98 O ATOM 1632 CB SER A 229 178.765 236.751 836.563 1.00159.57 C ATOM 1633 OG SER A 229 179.474 236.953 837.768 1.00161.13 O ATOM 1634 N THR A 230 178.020 233.503 835.872 1.00107.69 N ATOM 1635 CA THR A 230 178.464 232.105 835.881 1.00104.79 C ATOM 1636 C THR A 230 179.556 231.824 834.836 1.00101.40 C ATOM 1637 O THR A 230 179.888 232.678 834.016 1.00101.95 O ATOM 1638 CB THR A 230 177.288 231.149 835.590 1.00130.18 C ATOM 1639 OG1 THR A 230 176.203 231.432 836.483 1.00133.86 O ATOM 1640 CG2 THR A 230 177.719 229.702 835.764 1.00130.02 C ATOM 1641 N ILE A 231 180.112 230.621 834.884 1.00 92.72 N ATOM 1642 CA ILE A 231 181.155 230.195 833.960 1.00 90.99 C ATOM 1643 C ILE A 231 181.183 228.677 833.972 1.00 91.49 C ATOM 1644 O ILE A 231 181.053 228.070 835.036 1.00 93.75 O ATOM 1645 CB ILE A 231 182.575 230.701 834.364 1.00 65.56 C ATOM 1646 CG1 ILE A 231 182.700 232.203 834.119 1.00 66.17 C ATOM 1647 CD1 ILE A 231 184.142 232.721 834.313 1.00 65.91 C ATOM 1648 CG2 ILE A 231 183.647 229.988 833.540 1.00 63.84 C ATOM 1649 N ALA A 232 181.354 228.072 832.790 1.00107.20 N ATOM 1650 CA ALA A 232 181.397 226.619 832.664 1.00104.31 C ATOM 1651 C ALA A 232 182.670 226.171 831.969 1.00104.12 C ATOM 1652 O ALA A 232 183.190 226.865 831.096 1.00104.20 O ATOM 1653 CB ALA A 232 180.175 226.132 831.912 1.00 73.92 C ATOM 1654 N SER A 233 183.171 225.010 832.375 1.00 97.27 N ATOM 1655 CA SER A 233 184.403 224.465 831.824 1.00 99.20 C ATOM 1656 C SER A 233 184.362 222.947 831.731 1.00100.82 C ATOM 1657 O SER A 233 183.734 222.280 832.559 1.00100.30 O ATOM 1658 CB SER A 233 185.586 224.854 832.700 1.00116.11 C ATOM 1659 OG SER A 233 185.500 224.235 833.975 1.00115.41 O ATOM 1660 N CYS A 234 185.062 222.409 830.731 1.00110.85 N ATOM 1661 CA CYS A 234 185.137 220.968 830.484 1.00113.49 C ATOM 1662 C CYS A 234 186.588 220.581 830.235 1.00114.30 C ATOM 1663 O CYS A 234 187.342 221.353 829.652 1.00115.86 O ATOM 1664 CB CYS A 234 184.301 220.626 829.266 1.00124.67 C ATOM 1665 SG CYS A 234 184.699 221.665 827.858 1.00126.44 S ATOM 1666 N SER A 235 186.981 219.384 830.654 1.00 94.44 N ATOM 1667 CA SER A 235 188.371 218.956 830.488 1.00 97.66 C ATOM 1668 C SER A 235 188.559 217.454 830.280 1.00 98.93 C ATOM 1669 O SER A 235 187.646 216.659 830.542 1.00 99.90 O ATOM 1670 CB SER A 235 189.187 219.397 831.707 1.00140.80 C ATOM 1671 OG SER A 235 188.688 218.817 832.904 1.00140.80 O ATOM 1672 N GLN A 236 189.757 217.081 829.827 1.00104.73 N ATOM 1673 CA GLN A 236 190.115 215.686 829.555 1.00107.14 C ATOM 1674 C GLN A 236 189.650 214.657 830.605 1.00107.87 C ATOM 1675 O GLN A 236 189.484 213.477 830.283 1.00106.69 O ATOM 1676 CB GLN A 236 191.634 215.557 829.357 1.00133.18 C ATOM 1677 CG GLN A 236 192.218 216.479 828.288 1.00133.85 C ATOM 1678 CD GLN A 236 191.988 215.997 826.862 1.00133.63 C ATOM 1679 OE1 GLN A 236 191.666 216.791 825.971 1.00133.73 O ATOM 1680 NE2 GLN A 236 192.172 214.698 826.635 1.00134.79 N ATOM 1681 N ASP A 237 189.449 215.083 831.850 1.00135.25 N ATOM 1682 CA ASP A 237 188.999 214.153 832.888 1.00136.84 C ATOM 1683 C ASP A 237 187.564 213.707 832.606 1.00136.15 C ATOM 1684 O ASP A 237 187.158 212.599 832.981 1.00136.05 O ATOM 1685 CB ASP A 237 189.089 214.807 834.269 1.00138.26 C ATOM 1686 CG ASP A 237 188.525 216.214 834.286 1.00141.80 C ATOM 1687 OD1 ASP A 237 187.362 216.396 833.876 1.00144.85 O ATOM 1688 OD2 ASP A 237 189.246 217.140 834.713 1.00144.95 O ATOM 1689 N GLY A 238 186.814 214.584 831.942 1.00108.74 N ATOM 1690 CA GLY A 238 185.440 214.286 831.590 1.00108.36 C ATOM 1691 C GLY A 238 184.407 214.926 832.487 1.00107.80 C ATOM 1692 O GLY A 238 183.279 214.437 832.596 1.00109.46 O ATOM 1693 N ARG A 239 184.782 216.029 833.124 1.00112.04 N ATOM 1694 CA ARG A 239 183.876 216.730 834.032 1.00111.21 C ATOM 1695 C ARG A 239 183.538 218.120 833.512 1.00109.66 C ATOM 1696 O ARG A 239 184.348 218.763 832.855 1.00110.64 O ATOM 1697 CB ARG A 239 184.518 216.906 835.424 1.00101.38 C ATOM 1698 CG ARG A 239 185.074 215.673 836.135 1.00102.93 C ATOM 1699 CD ARG A 239 185.852 216.097 837.379 1.00103.07 C ATOM 1700 NE ARG A 239 186.911 215.151 837.691 1.00105.00 N ATOM 1701 CZ ARG A 239 186.707 213.952 838.225 1.00106.21 C ATOM 1702 NH1 ARG A 239 185.474 213.552 838.519 1.00105.56 N ATOM 1703 NH2 ARG A 239 187.736 213.141 838.441 1.00106.58 N ATOM 1704 N VAL A 240 182.340 218.589 833.817 1.00108.91 N ATOM 1705 CA VAL A 240 181.947 219.930 833.422 1.00108.08 C ATOM 1706 C VAL A 240 181.493 220.603 834.714 1.00109.37 C ATOM 1707 O VAL A 240 180.570 220.122 835.385 1.00110.40 O ATOM 1708 CB VAL A 240 180.797 219.907 832.383 1.00119.03 C ATOM 1709 CG1 VAL A 240 180.287 221.316 832.129 1.00119.62 C ATOM 1710 CG2 VAL A 240 181.298 219.302 831.083 1.00119.06 C ATOM 1711 N PHE A 241 182.174 221.690 835.079 1.00107.70 N ATOM 1712 CA PHE A 241 181.859 222.427 836.300 1.00106.64 C ATOM 1713 C PHE A 241 181.275 223.769 835.978 1.00106.66 C ATOM 1714 O PHE A 241 181.662 224.414 835.008 1.00108.16 O ATOM 1715 CB PHE A 241 183.108 222.661 837.146 1.00 88.80 C ATOM 1716 CG PHE A 241 183.753 221.404 837.629 1.00 89.28 C ATOM 1717 CD1 PHE A 241 185.086 221.131 837.321 1.00 89.69 C ATOM 1718 CE1 PHE A 241 185.690 219.943 837.729 1.00 91.57 C ATOM 1719 CZ PHE A 241 184.954 219.008 838.459 1.00 92.20 C ATOM 1720 CE2 PHE A 241 183.611 219.275 838.781 1.00 92.95 C ATOM 1721 CD2 PHE A 241 183.021 220.473 838.363 1.00 91.69 C ATOM 1722 N ILE A 242 180.353 224.212 836.791 1.00116.06 N ATOM 1723 CA ILE A 242 179.828 225.501 836.505 1.00115.43 C ATOM 1724 C ILE A 242 180.150 226.389 837.680 1.00116.37 C ATOM 1725 O ILE A 242 179.494 226.371 838.710 1.00117.29 O ATOM 1726 CB ILE A 242 178.367 225.387 836.175 1.00112.78 C ATOM 1727 CG1 ILE A 242 178.254 224.728 834.798 1.00110.69 C ATOM 1728 CD1 ILE A 242 176.894 224.190 834.451 1.00111.38 C ATOM 1729 CG2 ILE A 242 177.740 226.741 836.136 1.00113.44 C ATOM 1730 N TRP A 243 181.229 227.139 837.506 1.00 92.43 N ATOM 1731 CA TRP A 243 181.759 228.042 838.509 1.00 94.09 C ATOM 1732 C TRP A 243 180.874 229.255 838.789 1.00 97.63 C ATOM 1733 O TRP A 243 180.280 229.821 837.891 1.00 99.89 O ATOM 1734 CB TRP A 243 183.151 228.455 838.054 1.00121.55 C ATOM 1735 CG TRP A 243 183.989 227.254 837.748 1.00118.87 C ATOM 1736 CD1 TRP A 243 183.798 226.346 836.735 1.00119.51 C ATOM 1737 NE1 TRP A 243 184.712 225.320 836.836 1.00118.30 N ATOM 1738 CE2 TRP A 243 185.518 225.552 837.920 1.00116.94 C ATOM 1739 CZ2 TRP A 243 186.583 224.801 838.428 1.00116.80 C ATOM 1740 CH2 TRP A 243 187.224 225.284 839.545 1.00118.36 C ATOM 1741 CZ3 TRP A 243 186.824 226.492 840.162 1.00119.13 C ATOM 1742 CE3 TRP A 243 185.764 227.237 839.657 1.00118.62 C ATOM 1743 CD2 TRP A 243 185.092 226.767 838.517 1.00117.93 C ATOM 1744 N THR A 244 180.762 229.662 840.041 1.00170.09 N ATOM 1745 CA THR A 244 179.913 230.805 840.294 1.00174.85 C ATOM 1746 C THR A 244 180.353 231.806 841.340 1.00180.08 C ATOM 1747 O THR A 244 180.965 231.468 842.363 1.00180.08 O ATOM 1748 CB THR A 244 178.532 230.370 840.663 1.00 85.42 C ATOM 1749 OG1 THR A 244 178.292 229.056 840.146 1.00 83.11 O ATOM 1750 CG2 THR A 244 177.539 231.344 840.115 1.00 86.38 C ATOM 1751 N CYS A 245 179.984 233.049 841.051 1.00129.59 N ATOM 1752 CA CYS A 245 180.264 234.226 841.864 1.00135.20 C ATOM 1753 C CYS A 245 178.871 234.566 842.389 1.00137.99 C ATOM 1754 O CYS A 245 178.051 235.089 841.635 1.00137.28 O ATOM 1755 CB CYS A 245 180.780 235.331 840.930 1.00190.63 C ATOM 1756 SG CYS A 245 181.703 236.715 841.630 1.00190.63 S ATOM 1757 N ASP A 246 178.580 234.257 843.653 1.00161.53 N ATOM 1758 CA ASP A 246 177.239 234.537 844.165 1.00161.53 C ATOM 1759 C ASP A 246 176.888 236.007 843.893 1.00161.53 C ATOM 1760 O ASP A 246 175.851 236.309 843.292 1.00161.53 O ATOM 1761 CB ASP A 246 177.127 234.221 845.675 1.00177.87 C ATOM 1762 CG ASP A 246 175.759 233.573 846.072 1.00177.87 C ATOM 1763 OD1 ASP A 246 174.680 233.988 845.575 1.00177.87 O ATOM 1764 OD2 ASP A 246 175.764 232.644 846.910 1.00177.87 O ATOM 1765 N ASP A 247 177.763 236.917 844.318 1.00202.26 N ATOM 1766 CA ASP A 247 177.531 238.349 844.120 1.00202.26 C ATOM 1767 C ASP A 247 178.653 239.014 843.319 1.00202.26 C ATOM 1768 O ASP A 247 179.459 238.350 842.669 1.00202.26 O ATOM 1769 CB ASP A 247 177.391 239.079 845.474 1.00202.38 C ATOM 1770 CG ASP A 247 176.101 238.721 846.229 1.00202.38 C ATOM 1771 OD1 ASP A 247 175.019 238.700 845.590 1.00202.38 O ATOM 1772 OD2 ASP A 247 176.173 238.484 847.465 1.00202.38 O ATOM 1773 N ALA A 248 178.682 240.339 843.371 1.00202.38 N ATOM 1774 CA ALA A 248 179.700 241.119 842.688 1.00202.38 C ATOM 1775 C ALA A 248 180.799 241.356 843.725 1.00202.38 C ATOM 1776 O ALA A 248 180.505 241.493 844.914 1.00202.38 O ATOM 1777 CB ALA A 248 179.099 242.448 842.203 1.00 87.89 C ATOM 1778 N SER A 249 182.055 241.399 843.277 1.00202.38 N ATOM 1779 CA SER A 249 183.229 241.591 844.147 1.00202.38 C ATOM 1780 C SER A 249 183.290 240.624 845.351 1.00202.38 C ATOM 1781 O SER A 249 184.069 240.826 846.294 1.00202.38 O ATOM 1782 CB SER A 249 183.365 243.074 844.612 1.00195.12 C ATOM 1783 OG SER A 249 182.276 243.560 845.387 1.00195.12 O ATOM 1784 N SER A 250 182.485 239.558 845.299 1.00177.38 N ATOM 1785 CA SER A 250 182.462 238.560 846.363 1.00177.38 C ATOM 1786 C SER A 250 183.763 237.747 846.278 1.00177.38 C ATOM 1787 O SER A 250 183.994 236.870 847.103 1.00177.38 O ATOM 1788 CB SER A 250 181.234 237.636 846.221 1.00138.68 C ATOM 1789 OG SER A 250 180.537 237.434 847.450 1.00138.68 O ATOM 1790 N ASN A 251 184.596 238.033 845.271 1.00162.14 N ATOM 1791 CA ASN A 251 185.899 237.357 845.097 1.00162.14 C ATOM 1792 C ASN A 251 185.808 235.841 845.030 1.00162.14 C ATOM 1793 O ASN A 251 186.796 235.146 844.777 1.00162.14 O ATOM 1794 CB ASN A 251 186.817 237.690 846.279 1.00178.66 C ATOM 1795 CG ASN A 251 187.714 238.871 846.019 1.00178.66 C ATOM 1796 OD1 ASN A 251 188.494 238.864 845.068 1.00178.66 O ATOM 1797 ND2 ASN A 251 187.622 239.889 846.869 1.00178.66 N ATOM 1798 N THR A 252 184.604 235.346 845.239 1.00163.85 N ATOM 1799 CA THR A 252 184.351 233.931 845.332 1.00161.23 C ATOM 1800 C THR A 252 183.798 233.123 844.172 1.00159.02 C ATOM 1801 O THR A 252 182.715 233.414 843.661 1.00158.96 O ATOM 1802 CB THR A 252 183.421 233.727 846.499 1.00133.31 C ATOM 1803 OG1 THR A 252 182.297 234.616 846.361 1.00133.31 O ATOM 1804 CG2 THR A 252 184.132 234.047 847.788 1.00133.31 C ATOM 1805 N TRP A 253 184.532 232.095 843.753 1.00152.96 N ATOM 1806 CA TRP A 253 183.981 231.231 842.713 1.00147.71 C ATOM 1807 C TRP A 253 183.884 229.775 843.188 1.00145.90 C ATOM 1808 O TRP A 253 184.896 229.070 843.263 1.00143.76 O ATOM 1809 CB TRP A 253 184.821 231.300 841.434 1.00141.68 C ATOM 1810 CG TRP A 253 184.757 232.621 840.694 1.00137.42 C ATOM 1811 CD1 TRP A 253 185.587 233.695 840.851 1.00136.96 C ATOM 1812 NE1 TRP A 253 185.217 234.716 840.004 1.00134.39 N ATOM 1813 CE2 TRP A 253 184.125 234.313 839.281 1.00133.84 C ATOM 1814 CZ2 TRP A 253 183.392 234.990 838.303 1.00132.92 C ATOM 1815 CH2 TRP A 253 182.332 234.334 837.736 1.00132.32 C ATOM 1816 CZ3 TRP A 253 181.989 233.027 838.118 1.00133.95 C ATOM 1817 CE3 TRP A 253 182.718 232.351 839.088 1.00134.55 C ATOM 1818 CD2 TRP A 253 183.808 232.997 839.687 1.00135.18 C ATOM 1819 N SER A 254 182.665 229.330 843.502 1.00149.37 N ATOM 1820 CA SER A 254 182.440 227.964 843.973 1.00148.81 C ATOM 1821 C SER A 254 182.002 227.034 842.841 1.00146.79 C ATOM 1822 O SER A 254 180.884 227.139 842.331 1.00146.48 O ATOM 1823 CB SER A 254 181.383 227.957 845.085 1.00171.22 C ATOM 1824 OG SER A 254 180.167 228.533 844.640 1.00172.49 O ATOM 1825 N PRO A 255 182.884 226.102 842.440 1.00119.07 N ATOM 1826 CA PRO A 255 182.598 225.150 841.367 1.00117.61 C ATOM 1827 C PRO A 255 181.596 224.101 841.793 1.00116.10 C ATOM 1828 O PRO A 255 181.582 223.677 842.948 1.00117.83 O ATOM 1829 CB PRO A 255 183.962 224.547 841.082 1.00141.98 C ATOM 1830 CG PRO A 255 184.546 224.467 842.430 1.00143.55 C ATOM 1831 CD PRO A 255 184.216 225.838 843.009 1.00143.62 C ATOM 1832 N LYS A 256 180.772 223.687 840.839 1.00134.87 N ATOM 1833 CA LYS A 256 179.732 222.683 841.047 1.00133.89 C ATOM 1834 C LYS A 256 179.784 221.715 839.866 1.00131.33 C ATOM 1835 O LYS A 256 179.875 222.140 838.713 1.00131.92 O ATOM 1836 CB LYS A 256 178.380 223.375 841.098 1.00124.89 C ATOM 1837 CG LYS A 256 177.212 222.505 841.488 1.00128.50 C ATOM 1838 CD LYS A 256 175.974 223.373 841.511 1.00130.35 C ATOM 1839 CE LYS A 256 174.800 222.662 842.103 1.00132.31 C ATOM 1840 NZ LYS A 256 173.727 223.666 842.290 1.00133.94 N ATOM 1841 N LEU A 257 179.730 220.418 840.146 1.00130.69 N ATOM 1842 CA LEU A 257 179.799 219.436 839.069 1.00129.76 C ATOM 1843 C LEU A 257 178.503 219.190 838.327 1.00128.45 C ATOM 1844 O LEU A 257 177.458 218.921 838.928 1.00128.97 O ATOM 1845 CB LEU A 257 180.323 218.091 839.579 1.00 94.36 C ATOM 1846 CG LEU A 257 180.336 216.970 838.533 1.00 94.01 C ATOM 1847 CD1 LEU A 257 180.883 217.516 837.238 1.00 94.73 C ATOM 1848 CD2 LEU A 257 181.181 215.801 839.006 1.00 94.02 C ATOM 1849 N LEU A 258 178.600 219.267 837.002 1.00143.54 N ATOM 1850 CA LEU A 258 177.468 219.049 836.113 1.00143.59 C ATOM 1851 C LEU A 258 177.378 217.565 835.858 1.00144.69 C ATOM 1852 O LEU A 258 176.353 216.946 836.125 1.00145.39 O ATOM 1853 CB LEU A 258 177.676 219.790 834.796 1.00104.46 C ATOM 1854 CG LEU A 258 176.601 219.708 833.713 1.00102.82 C ATOM 1855 CD1 LEU A 258 175.247 219.804 834.320 1.00101.77 C ATOM 1856 CD2 LEU A 258 176.809 220.832 832.713 1.00100.93 C ATOM 1857 N HIS A 259 178.458 216.994 835.341 1.00 95.29 N ATOM 1858 CA HIS A 259 178.494 215.557 835.073 1.00 94.02 C ATOM 1859 C HIS A 259 179.881 215.107 834.646 1.00 93.31 C ATOM 1860 O HIS A 259 180.663 215.892 834.104 1.00 92.74 O ATOM 1861 CB HIS A 259 177.487 215.194 833.978 1.00119.85 C ATOM 1862 CG HIS A 259 177.144 213.740 833.931 1.00119.98 C ATOM 1863 ND1 HIS A 259 176.855 213.083 832.757 1.00120.04 N ATOM 1864 CE1 HIS A 259 176.595 211.814 833.018 1.00120.44 C ATOM 1865 NE2 HIS A 259 176.701 211.627 834.320 1.00120.49 N ATOM 1866 CD2 HIS A 259 177.044 212.819 834.914 1.00120.11 C ATOM 1867 N LYS A 260 180.193 213.849 834.917 1.00136.90 N ATOM 1868 CA LYS A 260 181.474 213.304 834.514 1.00138.56 C ATOM 1869 C LYS A 260 181.154 212.150 833.571 1.00140.26 C ATOM 1870 O LYS A 260 180.341 211.286 833.898 1.00140.96 O ATOM 1871 CB LYS A 260 182.274 212.775 835.711 1.00118.18 C ATOM 1872 CG LYS A 260 183.721 212.443 835.344 1.00117.96 C ATOM 1873 CD LYS A 260 184.283 211.219 836.065 1.00117.23 C ATOM 1874 CE LYS A 260 185.677 210.871 835.505 1.00117.90 C ATOM 1875 NZ LYS A 260 186.266 209.607 836.056 1.00116.96 N ATOM 1876 N PHE A 261 181.774 212.145 832.394 1.00121.98 N ATOM 1877 CA PHE A 261 181.555 211.079 831.420 1.00124.67 C ATOM 1878 C PHE A 261 182.829 210.244 831.430 1.00127.36 C ATOM 1879 O PHE A 261 183.848 210.710 831.940 1.00128.80 O ATOM 1880 CB PHE A 261 181.290 211.673 830.039 1.00110.19 C ATOM 1881 CG PHE A 261 180.513 212.963 830.072 1.00108.12 C ATOM 1882 CD1 PHE A 261 181.171 214.181 830.191 1.00107.34 C ATOM 1883 CE1 PHE A 261 180.462 215.373 830.245 1.00107.54 C ATOM 1884 CZ PHE A 261 179.076 215.354 830.178 1.00107.49 C ATOM 1885 CE2 PHE A 261 178.408 214.143 830.061 1.00108.31 C ATOM 1886 CD2 PHE A 261 179.128 212.954 830.006 1.00108.02 C ATOM 1887 N ASN A 262 182.820 209.039 830.870 1.00187.49 N ATOM 1888 CA ASN A 262 184.055 208.243 830.997 1.00188.32 C ATOM 1889 C ASN A 262 185.070 208.667 829.816 1.00188.32 C ATOM 1890 O ASN A 262 186.147 208.063 829.650 1.00188.32 O ATOM 1891 CB ASN A 262 183.678 206.761 830.943 1.00197.56 C ATOM 1892 CG ASN A 262 183.513 206.368 829.487 1.00199.99 C ATOM 1893 OD1 ASN A 262 183.457 207.330 828.615 1.00201.41 O ATOM 1894 ND2 ASN A 262 183.504 205.061 829.198 1.00202.18 N ATOM 1895 N ASP A 263 184.763 209.740 829.066 1.00139.31 N ATOM 1896 CA ASP A 263 185.660 210.275 828.016 1.00138.25 C ATOM 1897 C ASP A 263 185.747 211.823 828.058 1.00136.34 C ATOM 1898 O ASP A 263 184.949 212.485 828.713 1.00136.52 O ATOM 1899 CB ASP A 263 185.195 209.832 826.627 1.00174.29 C ATOM 1900 CG ASP A 263 186.225 210.124 825.538 1.00175.80 C ATOM 1901 OD1 ASP A 263 187.097 210.989 825.740 1.00176.16 O ATOM 1902 OD2 ASP A 263 186.157 209.497 824.461 1.00176.91 O ATOM 1903 N VAL A 264 186.718 212.377 827.341 1.00112.85 N ATOM 1904 CA VAL A 264 186.972 213.812 827.255 1.00108.70 C ATOM 1905 C VAL A 264 185.837 214.659 826.713 1.00106.45 C ATOM 1906 O VAL A 264 185.096 214.214 825.840 1.00106.72 O ATOM 1907 CB VAL A 264 188.181 214.095 826.346 1.00 92.33 C ATOM 1908 CG1 VAL A 264 188.381 215.607 826.210 1.00 92.66 C ATOM 1909 CG2 VAL A 264 189.434 213.409 826.897 1.00 92.82 C ATOM 1910 N VAL A 265 185.722 215.888 827.221 1.00 92.20 N ATOM 1911 CA VAL A 265 184.712 216.854 826.748 1.00 89.81 C ATOM 1912 C VAL A 265 185.506 217.930 825.980 1.00 89.84 C ATOM 1913 O VAL A 265 186.537 218.401 826.448 1.00 89.94 O ATOM 1914 CB VAL A 265 183.912 217.458 827.915 1.00 87.50 C ATOM 1915 CG1 VAL A 265 182.962 218.520 827.410 1.00 86.54 C ATOM 1916 CG2 VAL A 265 183.116 216.354 828.605 1.00 85.75 C ATOM 1917 N TRP A 266 185.037 218.296 824.791 1.00132.55 N ATOM 1918 CA TRP A 266 185.776 219.224 823.937 1.00129.80 C ATOM 1919 C TRP A 266 185.390 220.673 823.921 1.00128.77 C ATOM 1920 O TRP A 266 186.244 221.551 823.991 1.00129.93 O ATOM 1921 CB TRP A 266 185.756 218.699 822.504 1.00 93.29 C ATOM 1922 CG TRP A 266 186.137 217.282 822.459 1.00 91.70 C ATOM 1923 CD1 TRP A 266 185.314 216.208 822.628 1.00 91.87 C ATOM 1924 NE1 TRP A 266 186.054 215.051 822.730 1.00 91.81 N ATOM 1925 CE2 TRP A 266 187.379 215.373 822.618 1.00 91.56 C ATOM 1926 CZ2 TRP A 266 188.504 214.553 822.665 1.00 92.92 C ATOM 1927 CH2 TRP A 266 189.731 215.155 822.530 1.00 92.91 C ATOM 1928 CZ3 TRP A 266 189.850 216.546 822.347 1.00 92.68 C ATOM 1929 CE3 TRP A 266 188.720 217.361 822.297 1.00 92.23 C ATOM 1930 CD2 TRP A 266 187.465 216.772 822.438 1.00 91.40 C ATOM 1931 N HIS A 267 184.103 220.927 823.797 1.00106.93 N ATOM 1932 CA HIS A 267 183.622 222.288 823.754 1.00106.27 C ATOM 1933 C HIS A 267 182.397 222.459 824.630 1.00105.23 C ATOM 1934 O HIS A 267 181.730 221.494 825.017 1.00105.20 O ATOM 1935 CB HIS A 267 183.294 222.671 822.310 1.00112.01 C ATOM 1936 CG HIS A 267 184.498 222.959 821.473 1.00114.67 C ATOM 1937 ND1 HIS A 267 184.881 224.242 821.141 1.00116.54 N ATOM 1938 CE1 HIS A 267 185.989 224.196 820.422 1.00117.55 C ATOM 1939 NE2 HIS A 267 186.336 222.929 820.274 1.00117.84 N ATOM 1940 CD2 HIS A 267 185.416 222.136 820.920 1.00116.55 C ATOM 1941 N VAL A 268 182.104 223.710 824.938 1.00146.22 N ATOM 1942 CA VAL A 268 180.959 224.040 825.755 1.00142.59 C ATOM 1943 C VAL A 268 180.473 225.416 825.364 1.00141.41 C ATOM 1944 O VAL A 268 181.216 226.394 825.485 1.00141.95 O ATOM 1945 CB VAL A 268 181.334 224.069 827.241 1.00 61.98 C ATOM 1946 CG1 VAL A 268 180.226 224.701 828.032 1.00 60.82 C ATOM 1947 CG2 VAL A 268 181.579 222.663 827.745 1.00 62.20 C ATOM 1948 N SER A 269 179.252 225.508 824.855 1.00 87.91 N ATOM 1949 CA SER A 269 178.761 226.828 824.538 1.00 86.29 C ATOM 1950 C SER A 269 177.427 227.042 825.200 1.00 85.12 C ATOM 1951 O SER A 269 176.650 226.102 825.404 1.00 83.95 O ATOM 1952 CB SER A 269 178.645 227.068 823.050 1.00126.34 C ATOM 1953 OG SER A 269 178.518 228.465 822.834 1.00126.34 O ATOM 1954 N TRP A 270 177.181 228.294 825.564 1.00100.04 N ATOM 1955 CA TRP A 270 175.963 228.651 826.251 1.00100.95 C ATOM 1956 C TRP A 270 174.877 229.059 825.304 1.00102.25 C ATOM 1957 O TRP A 270 175.110 229.828 824.369 1.00102.48 O ATOM 1958 CB TRP A 270 176.209 229.811 827.238 1.00113.46 C ATOM 1959 CG TRP A 270 176.903 229.429 828.524 1.00109.65 C ATOM 1960 CD1 TRP A 270 178.226 229.606 828.833 1.00107.88 C ATOM 1961 NE1 TRP A 270 178.501 229.076 830.071 1.00105.04 N ATOM 1962 CE2 TRP A 270 177.349 228.541 830.589 1.00105.50 C ATOM 1963 CZ2 TRP A 270 177.125 227.895 831.802 1.00106.63 C ATOM 1964 CH2 TRP A 270 175.851 227.459 832.060 1.00105.63 C ATOM 1965 CZ3 TRP A 270 174.811 227.658 831.143 1.00105.16 C ATOM 1966 CE3 TRP A 270 175.029 228.296 829.939 1.00107.02 C ATOM 1967 CD2 TRP A 270 176.320 228.750 829.644 1.00107.08 C ATOM 1968 N SER A 271 173.684 228.540 825.550 1.00 93.71 N ATOM 1969 CA SER A 271 172.544 228.934 824.752 1.00 95.05 C ATOM 1970 C SER A 271 172.430 230.450 825.008 1.00 95.60 C ATOM 1971 O SER A 271 173.327 231.027 825.599 1.00 95.26 O ATOM 1972 CB SER A 271 171.300 228.183 825.235 1.00 78.31 C ATOM 1973 OG SER A 271 170.834 228.648 826.475 1.00 75.59 O ATOM 1974 N ILE A 272 171.375 231.122 824.587 1.00108.89 N ATOM 1975 CA ILE A 272 171.379 232.534 824.892 1.00112.61 C ATOM 1976 C ILE A 272 170.331 232.998 825.877 1.00115.14 C ATOM 1977 O ILE A 272 170.433 234.107 826.387 1.00115.79 O ATOM 1978 CB ILE A 272 171.270 233.386 823.644 1.00 91.89 C ATOM 1979 CG1 ILE A 272 172.326 234.486 823.695 1.00 91.40 C ATOM 1980 CD1 ILE A 272 172.184 235.518 822.588 1.00 91.06 C ATOM 1981 CG2 ILE A 272 169.874 233.998 823.544 1.00 92.90 C ATOM 1982 N THR A 273 169.326 232.193 826.177 1.00151.01 N ATOM 1983 CA THR A 273 168.360 232.704 827.124 1.00153.12 C ATOM 1984 C THR A 273 168.062 231.849 828.351 1.00153.94 C ATOM 1985 O THR A 273 168.009 232.381 829.462 1.00156.21 O ATOM 1986 CB THR A 273 167.045 233.081 826.419 1.00150.85 C ATOM 1987 OG1 THR A 273 167.327 233.952 825.314 1.00149.21 O ATOM 1988 CG2 THR A 273 166.129 233.822 827.380 1.00152.94 C ATOM 1989 N ALA A 274 167.876 230.543 828.181 1.00130.31 N ATOM 1990 CA ALA A 274 167.584 229.691 829.334 1.00129.86 C ATOM 1991 C ALA A 274 168.858 229.111 829.933 1.00130.17 C ATOM 1992 O ALA A 274 168.814 228.118 830.673 1.00130.66 O ATOM 1993 CB ALA A 274 166.646 228.564 828.932 1.00111.97 C ATOM 1994 N ASN A 275 169.989 229.743 829.629 1.00119.63 N ATOM 1995 CA ASN A 275 171.272 229.256 830.116 1.00118.66 C ATOM 1996 C ASN A 275 171.238 227.738 829.912 1.00116.44 C ATOM 1997 O ASN A 275 171.217 226.961 830.858 1.00116.74 O ATOM 1998 CB ASN A 275 171.453 229.606 831.600 1.00155.82 C ATOM 1999 CG ASN A 275 171.554 231.107 831.851 1.00158.10 C ATOM 2000 OD1 ASN A 275 170.638 231.870 831.539 1.00158.22 O ATOM 2001 ND2 ASN A 275 172.671 231.532 832.430 1.00157.94 N ATOM 2002 N ILE A 276 171.169 227.329 828.652 1.00115.41 N ATOM 2003 CA ILE A 276 171.144 225.923 828.295 1.00111.12 C ATOM 2004 C ILE A 276 172.550 225.649 827.839 1.00111.31 C ATOM 2005 O ILE A 276 173.054 226.270 826.893 1.00110.98 O ATOM 2006 CB ILE A 276 170.154 225.649 827.146 1.00 99.28 C ATOM 2007 CG1 ILE A 276 168.773 226.165 827.533 1.00 97.00 C ATOM 2008 CD1 ILE A 276 167.748 225.992 826.484 1.00 95.31 C ATOM 2009 CG2 ILE A 276 170.064 224.161 826.876 1.00 98.52 C ATOM 2010 N LEU A 277 173.199 224.735 828.533 1.00111.38 N ATOM 2011 CA LEU A 277 174.564 224.432 828.194 1.00112.38 C ATOM 2012 C LEU A 277 174.621 223.329 827.184 1.00114.24 C ATOM 2013 O LEU A 277 174.051 222.255 827.387 1.00117.06 O ATOM 2014 CB LEU A 277 175.356 224.018 829.430 1.00100.54 C ATOM 2015 CG LEU A 277 176.863 224.046 829.190 1.00 99.16 C ATOM 2016 CD1 LEU A 277 177.268 225.478 828.914 1.00101.03 C ATOM 2017 CD2 LEU A 277 177.606 223.490 830.380 1.00 99.52 C ATOM 2018 N ALA A 278 175.301 223.605 826.084 1.00 87.95 N ATOM 2019 CA ALA A 278 175.452 222.607 825.065 1.00 88.03 C ATOM 2020 C ALA A 278 176.790 221.962 825.375 1.00 88.90 C ATOM 2021 O ALA A 278 177.827 222.634 825.316 1.00 88.67 O ATOM 2022 CB ALA A 278 175.472 223.261 823.714 1.00112.71 C ATOM 2023 N VAL A 279 176.763 220.676 825.723 1.00 93.62 N ATOM 2024 CA VAL A 279 177.978 219.940 826.050 1.00 99.09 C ATOM 2025 C VAL A 279 178.417 219.063 824.903 1.00104.56 C ATOM 2026 O VAL A 279 177.789 218.041 824.614 1.00105.94 O ATOM 2027 CB VAL A 279 177.784 219.030 827.258 1.00102.72 C ATOM 2028 CG1 VAL A 279 179.006 218.147 827.437 1.00102.72 C ATOM 2029 CG2 VAL A 279 177.545 219.864 828.490 1.00102.72 C ATOM 2030 N SER A 280 179.507 219.463 824.265 1.00108.78 N ATOM 2031 CA SER A 280 180.050 218.726 823.139 1.00114.09 C ATOM 2032 C SER A 280 181.287 217.936 823.542 1.00117.44 C ATOM 2033 O SER A 280 182.402 218.460 823.584 1.00117.73 O ATOM 2034 CB SER A 280 180.367 219.695 821.988 1.00127.33 C ATOM 2035 OG SER A 280 180.803 220.958 822.471 1.00127.33 O ATOM 2036 N GLY A 281 181.081 216.665 823.851 1.00106.98 N ATOM 2037 CA GLY A 281 182.195 215.825 824.245 1.00112.34 C ATOM 2038 C GLY A 281 181.720 214.457 824.692 1.00115.94 C ATOM 2039 O GLY A 281 180.537 214.261 824.993 1.00116.35 O ATOM 2040 N GLY A 282 182.637 213.498 824.733 1.00160.36 N ATOM 2041 CA GLY A 282 182.260 212.167 825.161 1.00162.15 C ATOM 2042 C GLY A 282 182.180 211.144 824.045 1.00162.15 C ATOM 2043 O GLY A 282 183.213 210.707 823.529 1.00162.15 O ATOM 2044 N ASP A 283 180.952 210.774 823.664 1.00202.38 N ATOM 2045 CA ASP A 283 180.710 209.758 822.627 1.00202.38 C ATOM 2046 C ASP A 283 180.390 210.270 821.217 1.00202.38 C ATOM 2047 O ASP A 283 179.611 209.628 820.509 1.00202.38 O ATOM 2048 CB ASP A 283 179.549 208.838 823.039 1.00202.38 C ATOM 2049 CG ASP A 283 179.480 208.591 824.534 1.00202.38 C ATOM 2050 OD1 ASP A 283 180.546 208.456 825.171 1.00202.38 O ATOM 2051 OD2 ASP A 283 178.350 208.514 825.065 1.00202.38 O ATOM 2052 N ASN A 284 180.994 211.379 820.791 1.00166.80 N ATOM 2053 CA ASN A 284 180.695 211.949 819.471 1.00166.80 C ATOM 2054 C ASN A 284 179.300 212.584 819.543 1.00166.80 C ATOM 2055 O ASN A 284 178.788 213.125 818.550 1.00166.80 O ATOM 2056 CB ASN A 284 180.703 210.877 818.362 1.00172.34 C ATOM 2057 CG ASN A 284 182.095 210.592 817.816 1.00172.34 C ATOM 2058 OD1 ASN A 284 183.010 211.386 817.992 1.00172.34 O ATOM 2059 ND2 ASN A 284 182.249 209.464 817.127 1.00172.34 N ATOM 2060 N LYS A 285 178.696 212.500 820.730 1.00160.20 N ATOM 2061 CA LYS A 285 177.369 213.046 820.997 1.00154.73 C ATOM 2062 C LYS A 285 177.442 214.476 821.496 1.00149.88 C ATOM 2063 O LYS A 285 178.512 215.019 821.759 1.00150.06 O ATOM 2064 CB LYS A 285 176.634 212.201 822.047 1.00135.02 C ATOM 2065 CG LYS A 285 175.890 211.008 821.486 1.00137.01 C ATOM 2066 CD LYS A 285 175.018 210.358 822.547 1.00138.54 C ATOM 2067 CE LYS A 285 174.031 209.375 821.926 1.00139.44 C ATOM 2068 NZ LYS A 285 173.151 208.757 822.954 1.00140.19 N ATOM 2069 N VAL A 286 176.277 215.079 821.622 1.00121.65 N ATOM 2070 CA VAL A 286 176.173 216.432 822.107 1.00115.43 C ATOM 2071 C VAL A 286 174.941 216.449 822.980 1.00113.04 C ATOM 2072 O VAL A 286 173.871 216.001 822.567 1.00113.59 O ATOM 2073 CB VAL A 286 176.047 217.415 820.948 1.00 84.29 C ATOM 2074 CG1 VAL A 286 175.449 218.726 821.423 1.00 84.38 C ATOM 2075 CG2 VAL A 286 177.427 217.654 820.352 1.00 84.24 C ATOM 2076 N THR A 287 175.102 216.951 824.197 1.00110.40 N ATOM 2077 CA THR A 287 174.016 216.988 825.157 1.00105.96 C ATOM 2078 C THR A 287 173.632 218.385 825.547 1.00105.72 C ATOM 2079 O THR A 287 174.403 219.326 825.384 1.00106.85 O ATOM 2080 CB THR A 287 174.422 216.269 826.410 1.00 91.79 C ATOM 2081 OG1 THR A 287 175.843 216.397 826.562 1.00 89.18 O ATOM 2082 CG2 THR A 287 174.038 214.816 826.332 1.00 91.71 C ATOM 2083 N LEU A 288 172.432 218.514 826.077 1.00118.68 N ATOM 2084 CA LEU A 288 171.968 219.803 826.508 1.00117.50 C ATOM 2085 C LEU A 288 171.631 219.727 827.979 1.00119.18 C ATOM 2086 O LEU A 288 171.176 218.686 828.453 1.00119.79 O ATOM 2087 CB LEU A 288 170.747 220.221 825.697 1.00 82.19 C ATOM 2088 CG LEU A 288 171.032 220.637 824.251 1.00 78.13 C ATOM 2089 CD1 LEU A 288 169.973 221.650 823.813 1.00 76.75 C ATOM 2090 CD2 LEU A 288 172.411 221.278 824.128 1.00 76.24 C ATOM 2091 N TRP A 289 171.875 220.821 828.707 1.00 85.20 N ATOM 2092 CA TRP A 289 171.581 220.861 830.133 1.00 86.12 C ATOM 2093 C TRP A 289 170.929 222.141 830.535 1.00 88.13 C ATOM 2094 O TRP A 289 171.250 223.204 829.992 1.00 88.42 O ATOM 2095 CB TRP A 289 172.848 220.716 830.939 1.00100.24 C ATOM 2096 CG TRP A 289 173.610 219.534 830.578 1.00 99.63 C ATOM 2097 CD1 TRP A 289 174.381 219.360 829.469 1.00100.15 C ATOM 2098 NE1 TRP A 289 174.959 218.122 829.490 1.00 99.26 N ATOM 2099 CE2 TRP A 289 174.559 217.470 830.627 1.00 99.19 C ATOM 2100 CZ2 TRP A 289 174.877 216.190 831.095 1.00 99.75 C ATOM 2101 CH2 TRP A 289 174.315 215.790 832.283 1.00100.44 C ATOM 2102 CZ3 TRP A 289 173.451 216.635 833.004 1.00101.35 C ATOM 2103 CE3 TRP A 289 173.142 217.907 832.539 1.00 99.94 C ATOM 2104 CD2 TRP A 289 173.703 218.337 831.332 1.00 99.24 C ATOM 2105 N LYS A 290 169.973 222.003 831.462 1.00122.45 N ATOM 2106 CA LYS A 290 169.258 223.132 832.045 1.00125.98 C ATOM 2107 C LYS A 290 169.282 223.027 833.571 1.00128.84 C ATOM 2108 O LYS A 290 169.114 221.939 834.130 1.00129.76 O ATOM 2109 CB LYS A 290 167.802 223.169 831.578 1.00121.32 C ATOM 2110 CG LYS A 290 167.107 224.475 831.921 1.00120.80 C ATOM 2111 CD LYS A 290 165.768 224.635 831.230 1.00121.51 C ATOM 2112 CE LYS A 290 165.309 226.085 831.320 1.00122.13 C ATOM 2113 NZ LYS A 290 163.970 226.273 830.725 1.00121.82 N ATOM 2114 N GLU A 291 169.506 224.147 834.246 1.00125.32 N ATOM 2115 CA GLU A 291 169.501 224.133 835.700 1.00128.40 C ATOM 2116 C GLU A 291 168.043 224.082 836.123 1.00130.10 C ATOM 2117 O GLU A 291 167.256 224.975 835.796 1.00129.36 O ATOM 2118 CB GLU A 291 170.161 225.392 836.280 1.00139.54 C ATOM 2119 CG GLU A 291 170.420 225.309 837.799 1.00139.54 C ATOM 2120 CD GLU A 291 171.499 226.264 838.260 1.00139.54 C ATOM 2121 OE1 GLU A 291 171.321 227.487 838.095 1.00139.54 O ATOM 2122 OE2 GLU A 291 172.528 225.785 838.782 1.00139.54 O ATOM 2123 N SER A 292 167.686 223.024 836.842 1.00192.99 N ATOM 2124 CA SER A 292 166.316 222.839 837.305 1.00192.99 C ATOM 2125 C SER A 292 166.033 223.649 838.558 1.00192.99 C ATOM 2126 O SER A 292 166.946 223.945 839.334 1.00192.99 O ATOM 2127 CB SER A 292 166.036 221.358 837.586 1.00149.34 C ATOM 2128 OG SER A 292 166.859 220.856 838.626 1.00146.86 O ATOM 2129 N VAL A 293 164.757 224.001 838.732 1.00190.02 N ATOM 2130 CA VAL A 293 164.255 224.773 839.871 1.00190.02 C ATOM 2131 C VAL A 293 164.840 224.316 841.207 1.00190.02 C ATOM 2132 O VAL A 293 164.633 224.948 842.253 1.00190.02 O ATOM 2133 CB VAL A 293 162.731 224.620 839.971 1.00140.39 C ATOM 2134 CG1 VAL A 293 162.217 225.297 841.220 1.00139.91 C ATOM 2135 CG2 VAL A 293 162.066 225.190 838.741 1.00139.70 C ATOM 2136 N ASP A 294 165.567 223.208 841.161 1.00147.86 N ATOM 2137 CA ASP A 294 166.159 222.609 842.348 1.00147.93 C ATOM 2138 C ASP A 294 167.688 222.711 842.520 1.00145.84 C ATOM 2139 O ASP A 294 168.247 222.083 843.407 1.00144.97 O ATOM 2140 CB ASP A 294 165.735 221.134 842.392 1.00202.38 C ATOM 2141 CG ASP A 294 166.056 220.466 843.715 1.00202.38 C ATOM 2142 OD1 ASP A 294 166.885 221.004 844.475 1.00202.38 O ATOM 2143 OD2 ASP A 294 165.485 219.391 843.999 1.00202.38 O ATOM 2144 N GLY A 295 168.380 223.480 841.689 1.00120.39 N ATOM 2145 CA GLY A 295 169.825 223.578 841.848 1.00118.49 C ATOM 2146 C GLY A 295 170.698 222.588 841.091 1.00116.74 C ATOM 2147 O GLY A 295 171.826 222.916 840.720 1.00118.44 O ATOM 2148 N GLN A 296 170.159 221.390 840.909 1.00158.85 N ATOM 2149 CA GLN A 296 170.790 220.275 840.220 1.00154.96 C ATOM 2150 C GLN A 296 170.673 220.498 838.693 1.00151.01 C ATOM 2151 O GLN A 296 169.731 221.143 838.230 1.00150.57 O ATOM 2152 CB GLN A 296 170.053 219.007 840.673 1.00139.54 C ATOM 2153 CG GLN A 296 170.611 217.672 840.226 1.00141.17 C ATOM 2154 CD GLN A 296 172.034 217.407 840.704 1.00142.16 C ATOM 2155 OE1 GLN A 296 173.010 217.864 840.093 1.00142.16 O ATOM 2156 NE2 GLN A 296 172.161 216.664 841.803 1.00141.61 N ATOM 2157 N TRP A 297 171.634 219.999 837.915 1.00118.42 N ATOM 2158 CA TRP A 297 171.580 220.158 836.457 1.00113.64 C ATOM 2159 C TRP A 297 171.139 218.859 835.763 1.00112.86 C ATOM 2160 O TRP A 297 171.611 217.766 836.104 1.00111.49 O ATOM 2161 CB TRP A 297 172.943 220.532 835.885 1.00119.67 C ATOM 2162 CG TRP A 297 173.390 221.941 836.063 1.00116.74 C ATOM 2163 CD1 TRP A 297 174.175 222.424 837.065 1.00117.80 C ATOM 2164 NE1 TRP A 297 174.429 223.764 836.875 1.00116.44 N ATOM 2165 CE2 TRP A 297 173.799 224.171 835.729 1.00115.35 C ATOM 2166 CZ2 TRP A 297 173.759 225.426 835.123 1.00115.88 C ATOM 2167 CH2 TRP A 297 173.046 225.546 833.972 1.00114.76 C ATOM 2168 CZ3 TRP A 297 172.379 224.458 833.416 1.00112.92 C ATOM 2169 CE3 TRP A 297 172.413 223.208 834.011 1.00113.13 C ATOM 2170 CD2 TRP A 297 173.136 223.049 835.190 1.00114.93 C ATOM 2171 N VAL A 298 170.249 218.982 834.783 1.00106.84 N ATOM 2172 CA VAL A 298 169.779 217.817 834.055 1.00105.89 C ATOM 2173 C VAL A 298 170.000 217.909 832.578 1.00105.20 C ATOM 2174 O VAL A 298 170.180 218.992 832.017 1.00105.58 O ATOM 2175 CB VAL A 298 168.310 217.609 834.204 1.00 97.55 C ATOM 2176 CG1 VAL A 298 167.977 217.488 835.647 1.00101.27 C ATOM 2177 CG2 VAL A 298 167.567 218.744 833.551 1.00 99.14 C ATOM 2178 N CYS A 299 169.938 216.744 831.956 1.00127.58 N ATOM 2179 CA CYS A 299 170.113 216.595 830.529 1.00128.14 C ATOM 2180 C CYS A 299 168.723 216.730 829.900 1.00127.36 C ATOM 2181 O CYS A 299 167.847 215.951 830.232 1.00126.96 O ATOM 2182 CB CYS A 299 170.692 215.208 830.278 1.00134.73 C ATOM 2183 SG CYS A 299 171.288 214.933 828.629 1.00135.93 S ATOM 2184 N ILE A 300 168.505 217.704 829.017 1.00123.20 N ATOM 2185 CA ILE A 300 167.180 217.868 828.393 1.00123.28 C ATOM 2186 C ILE A 300 167.002 217.047 827.134 1.00128.06 C ATOM 2187 O ILE A 300 165.885 216.656 826.788 1.00127.75 O ATOM 2188 CB ILE A 300 166.879 219.308 827.944 1.00 82.90 C ATOM 2189 CG1 ILE A 300 168.173 219.953 827.477 1.00 81.28 C ATOM 2190 CD1 ILE A 300 167.990 221.408 827.150 1.00 79.50 C ATOM 2191 CG2 ILE A 300 166.103 220.074 829.012 1.00 80.49 C ATOM 2192 N SER A 301 168.092 216.821 826.419 1.00166.37 N ATOM 2193 CA SER A 301 168.007 216.048 825.198 1.00171.40 C ATOM 2194 C SER A 301 169.395 215.764 824.686 1.00174.68 C ATOM 2195 O SER A 301 170.341 216.499 824.966 1.00173.83 O ATOM 2196 CB SER A 301 167.222 216.810 824.127 1.00142.89 C ATOM 2197 OG SER A 301 167.925 217.969 823.706 1.00141.24 O ATOM 2198 N ASP A 302 169.502 214.681 823.933 1.00184.82 N ATOM 2199 CA ASP A 302 170.762 214.281 823.341 1.00184.82 C ATOM 2200 C ASP A 302 170.614 214.638 821.847 1.00184.82 C ATOM 2201 O ASP A 302 169.544 214.454 821.260 1.00184.82 O ATOM 2202 CB ASP A 302 170.985 212.788 823.661 1.00198.91 C ATOM 2203 CG ASP A 302 170.924 211.889 822.456 1.00198.91 C ATOM 2204 OD1 ASP A 302 170.210 212.197 821.482 1.00198.91 O ATOM 2205 OD2 ASP A 302 171.589 210.834 822.506 1.00198.91 O ATOM 2206 N VAL A 303 171.676 215.179 821.250 1.00170.55 N ATOM 2207 CA VAL A 303 171.647 215.661 819.857 1.00170.55 C ATOM 2208 C VAL A 303 172.276 214.858 818.689 1.00170.55 C ATOM 2209 O VAL A 303 173.505 214.761 818.551 1.00170.55 O ATOM 2210 CB VAL A 303 172.240 217.108 819.801 1.00135.67 C ATOM 2211 CG1 VAL A 303 172.140 217.676 818.389 1.00135.67 C ATOM 2212 CG2 VAL A 303 171.520 218.010 820.790 1.00135.67 C ATOM 2213 N ASN A 304 171.410 214.312 817.832 1.00202.38 N ATOM 2214 CA ASN A 304 171.822 213.560 816.640 1.00202.38 C ATOM 2215 C ASN A 304 170.604 213.367 815.737 1.00202.38 C ATOM 2216 O ASN A 304 170.650 213.819 814.571 1.00202.38 O ATOM 2217 CB ASN A 304 172.397 212.173 816.981 1.00202.38 C ATOM 2218 CG ASN A 304 172.749 212.017 818.444 1.00202.38 C ATOM 2219 OD1 ASN A 304 171.895 212.163 819.312 1.00202.38 O ATOM 2220 ND2 ASN A 304 174.009 211.706 818.723 1.00202.38 N END