HEADER STRUCTURAL PROTEIN, PROTEIN TRANSPORT 06-AUG-09 3IKO TITLE CRYSTAL STRUCTURE OF THE HETEROTRIMERIC SEC13-NUP145C-NUP84 TITLE 2 NUCLEOPORIN COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN TRANSPORT PROTEIN SEC13; COMPND 3 CHAIN: A, D, G; COMPND 4 FRAGMENT: UNP RESIDUES 1-297; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: NUCLEOPORIN NUP145C; COMPND 8 CHAIN: B, E, H; COMPND 9 FRAGMENT: UNP RESIDUES 731-1158; COMPND 10 SYNONYM: NUCLEOPORIN NUP145C, C-NUP145; COMPND 11 EC: 3.4.21.-; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: NUCLEOPORIN NUP84; COMPND 15 CHAIN: C, F, I; COMPND 16 FRAGMENT: UNP RESIDUES 1-460; COMPND 17 SYNONYM: NUCLEAR PORE PROTEIN NUP84; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; SOURCE 3 ORGANISM_COMMON: YEAST; SOURCE 4 ORGANISM_TAXID: 4932; SOURCE 5 GENE: SEC13, ANU3, YLR208W, L8167.4; 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 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; SOURCE 12 ORGANISM_COMMON: YEAST; SOURCE 13 ORGANISM_TAXID: 4932; SOURCE 14 GENE: NUP145, RAT10, YGL092W; SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 17 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS (DE3)-RIL; SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PET; SOURCE 19 MOL_ID: 3; SOURCE 20 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; SOURCE 21 ORGANISM_COMMON: YEAST; SOURCE 22 ORGANISM_TAXID: 4932; SOURCE 23 GENE: NUP84, YDL116W; SOURCE 24 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 26 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS (DE3)-RIL; SOURCE 27 EXPRESSION_SYSTEM_VECTOR_TYPE: PET KEYWDS NPC, TRANSPORT, WD REPEAT, AUTOCATALYTIC CLEAVAGE, MRNA KEYWDS 2 TRANSPORT, NUCLEAR PORE COMPLEX, NUCLEUS, PHOSPHOPROTEIN, KEYWDS 3 TRANSLOCATION, PROTEIN TRANSPORT, COILED COIL, MEMBRANE, KEYWDS 4 HYDROLASE, RNA-BINDING, CYTOPLASMIC VESICLE, ENDOPLASMIC KEYWDS 5 RETICULUM, ER-GOLGI TRANSPORT, NUCLEAR PROTEIN, STRUCTURAL KEYWDS 6 PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR V.NAGY,K.-C.HSIA,E.W.DEBLER,A.DAVENPORT,G.BLOBEL,A.HOELZ REVDAT 2 24-NOV-09 3IKO 1 JRNL REVDAT 1 13-OCT-09 3IKO 0 JRNL AUTH V.NAGY,K.C.HSIA,E.W.DEBLER,M.KAMPMANN, JRNL AUTH 2 A.M.DAVENPORT,G.BLOBEL,A.HOELZ JRNL TITL STRUCTURE OF A TRIMERIC NUCLEOPORIN COMPLEX REVEALS JRNL TITL 2 ALTERNATE OLIGOMERIZATION STATES. JRNL REF PROC.NATL.ACAD.SCI.USA V. 106 17693 2009 JRNL REFN ISSN 0027-8424 JRNL PMID 19805193 JRNL DOI 10.1073/PNAS.0909373106 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 3.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.2 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) : 3.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.1 REMARK 3 NUMBER OF REFLECTIONS : 97899 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : 9.2 REMARK 3 R VALUE (WORKING SET) : 0.234 REMARK 3 FREE R VALUE : 0.273 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 9887 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 : 27032 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) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL 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) : 1.50 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 : NULL 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 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 3IKO COMPLIES WITH FORMAT V. 3.20, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-SEP-09. REMARK 100 THE RCSB ID CODE IS RCSB054531. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.14 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 105020 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5 REMARK 200 DATA REDUNDANCY : 7.500 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.11500 REMARK 200 FOR THE DATA SET : 16.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31 REMARK 200 COMPLETENESS FOR SHELL (%) : 75.9 REMARK 200 DATA REDUNDANCY IN SHELL : 4.90 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.52500 REMARK 200 FOR SHELL : 2.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD 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 (%): 68.66 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.92 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 20000, MES, PH 6.5, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 50.69850 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 163.90300 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 97.02500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 163.90300 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 50.69850 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 97.02500 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 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 8940 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 51440 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 9120 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 50140 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 9280 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 49410 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I 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 VAL A 3 REMARK 465 ILE A 4 REMARK 465 ALA A 5 REMARK 465 ASN A 6 REMARK 465 ALA A 7 REMARK 465 ILE A 158 REMARK 465 GLU A 159 REMARK 465 GLU A 160 REMARK 465 ASP A 161 REMARK 465 GLY A 162 REMARK 465 GLU A 163 REMARK 465 HIS A 164 REMARK 465 ASN A 165 REMARK 465 GLY A 166 REMARK 465 THR A 167 REMARK 465 LYS A 168 REMARK 465 GLU A 169 REMARK 465 GLU A 294 REMARK 465 VAL A 295 REMARK 465 HIS A 296 REMARK 465 GLN A 297 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 MET C 1 REMARK 465 GLU C 2 REMARK 465 LEU C 3 REMARK 465 SER C 4 REMARK 465 PRO C 5 REMARK 465 THR C 6 REMARK 465 ASN C 27 REMARK 465 ASN C 28 REMARK 465 GLU C 29 REMARK 465 GLN C 30 REMARK 465 ASN C 31 REMARK 465 PRO C 32 REMARK 465 ILE C 33 REMARK 465 ASP C 368 REMARK 465 VAL C 369 REMARK 465 VAL C 370 REMARK 465 LYS C 371 REMARK 465 GLY C 372 REMARK 465 THR C 373 REMARK 465 GLU C 374 REMARK 465 ALA C 375 REMARK 465 SER C 376 REMARK 465 ASN C 377 REMARK 465 GLU C 443 REMARK 465 ALA C 444 REMARK 465 CYS C 445 REMARK 465 SER C 446 REMARK 465 PHE C 447 REMARK 465 ILE C 448 REMARK 465 LEU C 449 REMARK 465 SER C 450 REMARK 465 SER C 451 REMARK 465 LEU C 452 REMARK 465 GLU C 453 REMARK 465 ASP C 454 REMARK 465 PRO C 455 REMARK 465 GLN C 456 REMARK 465 VAL C 457 REMARK 465 ARG C 458 REMARK 465 LYS C 459 REMARK 465 LYS C 460 REMARK 465 MET D 1 REMARK 465 VAL D 2 REMARK 465 VAL D 3 REMARK 465 ILE D 4 REMARK 465 ALA D 5 REMARK 465 ASN D 6 REMARK 465 ALA D 7 REMARK 465 ILE D 158 REMARK 465 GLU D 159 REMARK 465 GLU D 160 REMARK 465 ASP D 161 REMARK 465 GLY D 162 REMARK 465 GLU D 163 REMARK 465 HIS D 164 REMARK 465 ASN D 165 REMARK 465 GLY D 166 REMARK 465 THR D 167 REMARK 465 LYS D 168 REMARK 465 GLU D 169 REMARK 465 GLU D 294 REMARK 465 VAL D 295 REMARK 465 HIS D 296 REMARK 465 GLN D 297 REMARK 465 MET E 111 REMARK 465 GLY E 112 REMARK 465 SER E 113 REMARK 465 SER E 114 REMARK 465 HIS E 115 REMARK 465 HIS E 116 REMARK 465 HIS E 117 REMARK 465 HIS E 118 REMARK 465 HIS E 119 REMARK 465 HIS E 120 REMARK 465 SER E 121 REMARK 465 GLN E 122 REMARK 465 ASP E 123 REMARK 465 PRO E 124 REMARK 465 PHE E 125 REMARK 465 SER E 126 REMARK 465 GLU E 127 REMARK 465 CYS E 128 REMARK 465 ASN E 129 REMARK 465 MET F 1 REMARK 465 GLU F 2 REMARK 465 LEU F 3 REMARK 465 SER F 4 REMARK 465 PRO F 5 REMARK 465 THR F 6 REMARK 465 ASN F 28 REMARK 465 GLU F 29 REMARK 465 GLN F 30 REMARK 465 ASN F 31 REMARK 465 PRO F 32 REMARK 465 ILE F 33 REMARK 465 ASP F 368 REMARK 465 VAL F 369 REMARK 465 VAL F 370 REMARK 465 LYS F 371 REMARK 465 GLY F 372 REMARK 465 THR F 373 REMARK 465 GLU F 374 REMARK 465 ALA F 375 REMARK 465 SER F 376 REMARK 465 ASN F 377 REMARK 465 ASP F 378 REMARK 465 GLU F 443 REMARK 465 ALA F 444 REMARK 465 CYS F 445 REMARK 465 SER F 446 REMARK 465 PHE F 447 REMARK 465 ILE F 448 REMARK 465 LEU F 449 REMARK 465 SER F 450 REMARK 465 SER F 451 REMARK 465 LEU F 452 REMARK 465 GLU F 453 REMARK 465 ASP F 454 REMARK 465 PRO F 455 REMARK 465 GLN F 456 REMARK 465 VAL F 457 REMARK 465 ARG F 458 REMARK 465 LYS F 459 REMARK 465 LYS F 460 REMARK 465 MET G 1 REMARK 465 VAL G 2 REMARK 465 VAL G 3 REMARK 465 ILE G 4 REMARK 465 ALA G 5 REMARK 465 ASN G 6 REMARK 465 ALA G 7 REMARK 465 ILE G 158 REMARK 465 GLU G 159 REMARK 465 GLU G 160 REMARK 465 ASP G 161 REMARK 465 GLY G 162 REMARK 465 GLU G 163 REMARK 465 HIS G 164 REMARK 465 ASN G 165 REMARK 465 GLY G 166 REMARK 465 THR G 167 REMARK 465 LYS G 168 REMARK 465 GLU G 169 REMARK 465 GLU G 294 REMARK 465 VAL G 295 REMARK 465 HIS G 296 REMARK 465 GLN G 297 REMARK 465 MET H 111 REMARK 465 GLY H 112 REMARK 465 SER H 113 REMARK 465 SER H 114 REMARK 465 HIS H 115 REMARK 465 HIS H 116 REMARK 465 HIS H 117 REMARK 465 HIS H 118 REMARK 465 HIS H 119 REMARK 465 HIS H 120 REMARK 465 SER H 121 REMARK 465 GLN H 122 REMARK 465 ASP H 123 REMARK 465 PRO H 124 REMARK 465 PHE H 125 REMARK 465 SER H 126 REMARK 465 GLU H 127 REMARK 465 CYS H 128 REMARK 465 ASN H 129 REMARK 465 ASN H 550 REMARK 465 TYR H 551 REMARK 465 LEU H 552 REMARK 465 MET I 1 REMARK 465 GLU I 2 REMARK 465 LEU I 3 REMARK 465 SER I 4 REMARK 465 PRO I 5 REMARK 465 THR I 6 REMARK 465 ASN I 31 REMARK 465 PRO I 32 REMARK 465 ILE I 33 REMARK 465 ASP I 368 REMARK 465 VAL I 369 REMARK 465 VAL I 370 REMARK 465 LYS I 371 REMARK 465 GLY I 372 REMARK 465 THR I 373 REMARK 465 GLU I 374 REMARK 465 ALA I 375 REMARK 465 SER I 376 REMARK 465 ASN I 377 REMARK 465 ASP I 378 REMARK 465 ILE I 379 REMARK 465 ILE I 380 REMARK 465 ASN I 437 REMARK 465 GLU I 438 REMARK 465 SER I 439 REMARK 465 ASP I 440 REMARK 465 CYS I 441 REMARK 465 LEU I 442 REMARK 465 GLU I 443 REMARK 465 ALA I 444 REMARK 465 CYS I 445 REMARK 465 SER I 446 REMARK 465 PHE I 447 REMARK 465 ILE I 448 REMARK 465 LEU I 449 REMARK 465 SER I 450 REMARK 465 SER I 451 REMARK 465 LEU I 452 REMARK 465 GLU I 453 REMARK 465 ASP I 454 REMARK 465 PRO I 455 REMARK 465 GLN I 456 REMARK 465 VAL I 457 REMARK 465 ARG I 458 REMARK 465 LYS I 459 REMARK 465 LYS I 460 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 ARG E 441 CG CD NE CZ NH1 NH2 REMARK 480 GLU E 482 CD OE1 OE2 REMARK 480 ARG H 441 CG CD NE CZ NH1 NH2 REMARK 480 GLU H 482 CD OE1 OE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 PRO B 247 C - N - CA ANGL. DEV. = 10.4 DEGREES REMARK 500 PRO C 383 C - N - CA ANGL. DEV. = 16.7 DEGREES REMARK 500 PRO C 383 C - N - CD ANGL. DEV. = -16.4 DEGREES REMARK 500 PRO E 247 C - N - CA ANGL. DEV. = 10.4 DEGREES REMARK 500 PRO E 330 C - N - CA ANGL. DEV. = 10.0 DEGREES REMARK 500 PRO F 383 C - N - CA ANGL. DEV. = 9.3 DEGREES REMARK 500 PRO H 247 C - N - CA ANGL. DEV. = 10.5 DEGREES REMARK 500 PRO H 330 C - N - CA ANGL. DEV. = 10.3 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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 ASN A 9 88.24 168.48 REMARK 500 LEU A 11 94.41 -172.53 REMARK 500 TYR A 19 -36.95 -31.61 REMARK 500 SER A 28 -152.97 -105.74 REMARK 500 ASP A 30 12.29 -65.50 REMARK 500 LYS A 31 -2.88 73.09 REMARK 500 GLU A 39 109.94 -174.14 REMARK 500 GLU A 53 37.79 -98.46 REMARK 500 ASP A 60 112.45 -176.82 REMARK 500 PRO A 64 -1.60 -51.11 REMARK 500 ASP A 76 30.54 -72.41 REMARK 500 LYS A 83 129.03 177.49 REMARK 500 SER A 90 117.09 -163.74 REMARK 500 GLN A 91 101.38 -56.20 REMARK 500 VAL A 97 34.17 -69.09 REMARK 500 SER A 99 33.85 -83.73 REMARK 500 ALA A 100 -171.45 -172.25 REMARK 500 ASN A 103 -65.09 -93.32 REMARK 500 VAL A 105 101.71 -164.79 REMARK 500 TRP A 107 179.43 -59.87 REMARK 500 HIS A 110 -0.67 -48.08 REMARK 500 LEU A 115 162.33 -43.02 REMARK 500 ASP A 122 31.82 -75.33 REMARK 500 LYS A 131 -167.68 -68.49 REMARK 500 ALA A 151 114.15 -170.41 REMARK 500 GLN A 192 -16.57 62.38 REMARK 500 TYR A 194 124.64 -36.18 REMARK 500 TRP A 206 105.10 -22.30 REMARK 500 VAL A 207 86.60 -60.60 REMARK 500 ARG A 208 -77.29 -39.60 REMARK 500 PRO A 214 44.81 -82.81 REMARK 500 VAL A 216 48.64 -80.73 REMARK 500 LEU A 217 -166.45 -103.69 REMARK 500 ARG A 219 -165.96 -121.16 REMARK 500 ASP A 228 14.56 -69.61 REMARK 500 ASN A 238 -156.78 -153.41 REMARK 500 GLU A 239 2.58 -63.54 REMARK 500 GLN A 240 -85.24 -121.94 REMARK 500 THR A 246 78.80 -158.32 REMARK 500 LEU A 248 -81.54 -27.20 REMARK 500 PRO A 254 5.74 -45.27 REMARK 500 ASP A 255 145.92 177.65 REMARK 500 VAL A 256 142.86 -39.38 REMARK 500 TRP A 258 -76.09 -111.31 REMARK 500 LEU A 264 -78.13 -72.50 REMARK 500 ASN A 276 -2.47 97.15 REMARK 500 MET B 139 -82.50 -42.30 REMARK 500 ARG B 143 -3.09 96.86 REMARK 500 PHE B 144 100.40 -52.22 REMARK 500 ALA B 146 -6.62 -43.17 REMARK 500 REMARK 500 THIS ENTRY HAS 384 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 PHE C 435 17.39 REMARK 500 PHE F 435 -18.69 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 ASN A 276 24.5 L L OUTSIDE RANGE REMARK 500 ASN D 276 24.5 L L OUTSIDE RANGE REMARK 500 PHE F 435 23.4 L L OUTSIDE RANGE REMARK 500 LEU F 436 22.4 L L OUTSIDE RANGE REMARK 500 ASN G 276 24.5 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL DBREF 3IKO A 1 297 UNP Q04491 SEC13_YEAST 1 297 DBREF 3IKO B 125 552 UNP P49687 NU145_YEAST 731 1158 DBREF 3IKO C 1 460 UNP P52891 NUP84_YEAST 1 460 DBREF 3IKO D 1 297 UNP Q04491 SEC13_YEAST 1 297 DBREF 3IKO E 125 552 UNP P49687 NU145_YEAST 731 1158 DBREF 3IKO F 1 460 UNP P52891 NUP84_YEAST 1 460 DBREF 3IKO G 1 297 UNP Q04491 SEC13_YEAST 1 297 DBREF 3IKO H 125 552 UNP P49687 NU145_YEAST 731 1158 DBREF 3IKO I 1 460 UNP P52891 NUP84_YEAST 1 460 SEQADV 3IKO MET B 111 UNP P49687 EXPRESSION TAG SEQADV 3IKO GLY B 112 UNP P49687 EXPRESSION TAG SEQADV 3IKO SER B 113 UNP P49687 EXPRESSION TAG SEQADV 3IKO SER B 114 UNP P49687 EXPRESSION TAG SEQADV 3IKO HIS B 115 UNP P49687 EXPRESSION TAG SEQADV 3IKO HIS B 116 UNP P49687 EXPRESSION TAG SEQADV 3IKO HIS B 117 UNP P49687 EXPRESSION TAG SEQADV 3IKO HIS B 118 UNP P49687 EXPRESSION TAG SEQADV 3IKO HIS B 119 UNP P49687 EXPRESSION TAG SEQADV 3IKO HIS B 120 UNP P49687 EXPRESSION TAG SEQADV 3IKO SER B 121 UNP P49687 EXPRESSION TAG SEQADV 3IKO GLN B 122 UNP P49687 EXPRESSION TAG SEQADV 3IKO ASP B 123 UNP P49687 EXPRESSION TAG SEQADV 3IKO PRO B 124 UNP P49687 EXPRESSION TAG SEQADV 3IKO MET E 111 UNP P49687 EXPRESSION TAG SEQADV 3IKO GLY E 112 UNP P49687 EXPRESSION TAG SEQADV 3IKO SER E 113 UNP P49687 EXPRESSION TAG SEQADV 3IKO SER E 114 UNP P49687 EXPRESSION TAG SEQADV 3IKO HIS E 115 UNP P49687 EXPRESSION TAG SEQADV 3IKO HIS E 116 UNP P49687 EXPRESSION TAG SEQADV 3IKO HIS E 117 UNP P49687 EXPRESSION TAG SEQADV 3IKO HIS E 118 UNP P49687 EXPRESSION TAG SEQADV 3IKO HIS E 119 UNP P49687 EXPRESSION TAG SEQADV 3IKO HIS E 120 UNP P49687 EXPRESSION TAG SEQADV 3IKO SER E 121 UNP P49687 EXPRESSION TAG SEQADV 3IKO GLN E 122 UNP P49687 EXPRESSION TAG SEQADV 3IKO ASP E 123 UNP P49687 EXPRESSION TAG SEQADV 3IKO PRO E 124 UNP P49687 EXPRESSION TAG SEQADV 3IKO MET H 111 UNP P49687 EXPRESSION TAG SEQADV 3IKO GLY H 112 UNP P49687 EXPRESSION TAG SEQADV 3IKO SER H 113 UNP P49687 EXPRESSION TAG SEQADV 3IKO SER H 114 UNP P49687 EXPRESSION TAG SEQADV 3IKO HIS H 115 UNP P49687 EXPRESSION TAG SEQADV 3IKO HIS H 116 UNP P49687 EXPRESSION TAG SEQADV 3IKO HIS H 117 UNP P49687 EXPRESSION TAG SEQADV 3IKO HIS H 118 UNP P49687 EXPRESSION TAG SEQADV 3IKO HIS H 119 UNP P49687 EXPRESSION TAG SEQADV 3IKO HIS H 120 UNP P49687 EXPRESSION TAG SEQADV 3IKO SER H 121 UNP P49687 EXPRESSION TAG SEQADV 3IKO GLN H 122 UNP P49687 EXPRESSION TAG SEQADV 3IKO ASP H 123 UNP P49687 EXPRESSION TAG SEQADV 3IKO PRO H 124 UNP P49687 EXPRESSION TAG SEQRES 1 A 297 MET VAL VAL ILE ALA ASN ALA HIS ASN GLU LEU ILE HIS SEQRES 2 A 297 ASP ALA VAL LEU ASP TYR TYR GLY LYS ARG LEU ALA THR SEQRES 3 A 297 CYS SER SER ASP LYS THR ILE LYS ILE PHE GLU VAL GLU SEQRES 4 A 297 GLY GLU THR HIS LYS LEU ILE ASP THR LEU THR GLY HIS SEQRES 5 A 297 GLU GLY PRO VAL TRP ARG VAL ASP TRP ALA HIS PRO LYS SEQRES 6 A 297 PHE GLY THR ILE LEU ALA SER CYS SER TYR ASP GLY LYS SEQRES 7 A 297 VAL LEU ILE TRP LYS GLU GLU ASN GLY ARG TRP SER GLN SEQRES 8 A 297 ILE ALA VAL HIS ALA VAL HIS SER ALA SER VAL ASN SER SEQRES 9 A 297 VAL GLN TRP ALA PRO HIS GLU TYR GLY PRO LEU LEU LEU SEQRES 10 A 297 VAL ALA SER SER ASP GLY LYS VAL SER VAL VAL GLU PHE SEQRES 11 A 297 LYS GLU ASN GLY THR THR SER PRO ILE ILE ILE ASP ALA SEQRES 12 A 297 HIS ALA ILE GLY VAL ASN SER ALA SER TRP ALA PRO ALA SEQRES 13 A 297 THR ILE GLU GLU ASP GLY GLU HIS ASN GLY THR LYS GLU SEQRES 14 A 297 SER ARG LYS PHE VAL THR GLY GLY ALA ASP ASN LEU VAL SEQRES 15 A 297 LYS ILE TRP LYS TYR ASN SER ASP ALA GLN THR TYR VAL SEQRES 16 A 297 LEU GLU SER THR LEU GLU GLY HIS SER ASP TRP VAL ARG SEQRES 17 A 297 ASP VAL ALA TRP SER PRO THR VAL LEU LEU ARG SER TYR SEQRES 18 A 297 LEU ALA SER VAL SER GLN ASP ARG THR CYS ILE ILE TRP SEQRES 19 A 297 THR GLN ASP ASN GLU GLN GLY PRO TRP LYS LYS THR LEU SEQRES 20 A 297 LEU LYS GLU GLU LYS PHE PRO ASP VAL LEU TRP ARG ALA SEQRES 21 A 297 SER TRP SER LEU SER GLY ASN VAL LEU ALA LEU SER GLY SEQRES 22 A 297 GLY ASP ASN LYS VAL THR LEU TRP LYS GLU ASN LEU GLU SEQRES 23 A 297 GLY LYS TRP GLU PRO ALA GLY GLU VAL HIS GLN SEQRES 1 B 442 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN 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 460 MET GLU LEU SER PRO THR TYR GLN THR GLU ARG PHE THR SEQRES 2 C 460 LYS PHE SER ASP THR LEU LYS GLU PHE LYS ILE GLU GLN SEQRES 3 C 460 ASN ASN GLU GLN ASN PRO ILE ASP PRO PHE ASN ILE ILE SEQRES 4 C 460 ARG GLU PHE ARG SER ALA ALA GLY GLN LEU ALA LEU ASP SEQRES 5 C 460 LEU ALA ASN SER GLY ASP GLU SER ASN VAL ILE SER SER SEQRES 6 C 460 LYS ASP TRP GLU LEU GLU ALA ARG PHE TRP HIS LEU VAL SEQRES 7 C 460 GLU LEU LEU LEU VAL PHE ARG ASN ALA ASP LEU ASP LEU SEQRES 8 C 460 ASP GLU MET GLU LEU HIS PRO TYR ASN SER ARG GLY LEU SEQRES 9 C 460 PHE GLU LYS LYS LEU MET GLN ASP ASN LYS GLN LEU TYR SEQRES 10 C 460 GLN ILE TRP ILE VAL MET VAL TRP LEU LYS GLU ASN THR SEQRES 11 C 460 TYR VAL MET GLU ARG PRO LYS ASN VAL PRO THR SER LYS SEQRES 12 C 460 TRP LEU ASN SER ILE THR SER GLY GLY LEU LYS SER CYS SEQRES 13 C 460 ASP LEU ASP PHE PRO LEU ARG GLU ASN THR ASN VAL LEU SEQRES 14 C 460 ASP VAL LYS ASP LYS GLU GLU ASP HIS ILE PHE PHE LYS SEQRES 15 C 460 TYR ILE TYR GLU LEU ILE LEU ALA GLY ALA ILE ASP GLU SEQRES 16 C 460 ALA LEU GLU GLU ALA LYS LEU SER ASP ASN ILE SER ILE SEQRES 17 C 460 CYS MET ILE LEU CYS GLY ILE GLN GLU TYR LEU ASN PRO SEQRES 18 C 460 VAL ILE ASP THR GLN ILE ALA ASN GLU PHE ASN THR GLN SEQRES 19 C 460 GLN GLY ILE LYS LYS HIS SER LEU TRP ARG ARG THR VAL SEQRES 20 C 460 TYR SER LEU SER GLN GLN ALA GLY LEU ASP PRO TYR GLU SEQRES 21 C 460 ARG ALA ILE TYR SER TYR LEU SER GLY ALA ILE PRO ASN SEQRES 22 C 460 GLN GLU VAL LEU GLN TYR SER ASP TRP GLU SER ASP LEU SEQRES 23 C 460 HIS ILE HIS LEU ASN GLN ILE LEU GLN THR GLU ILE GLU SEQRES 24 C 460 ASN TYR LEU LEU GLU ASN ASN GLN VAL GLY THR ASP GLU SEQRES 25 C 460 LEU ILE LEU PRO LEU PRO SER HIS ALA LEU THR VAL GLN SEQRES 26 C 460 GLU VAL LEU ASN ARG VAL ALA SER ARG HIS PRO SER GLU SEQRES 27 C 460 SER GLU HIS PRO ILE ARG VAL LEU MET ALA SER VAL ILE SEQRES 28 C 460 LEU ASP SER LEU PRO SER VAL ILE HIS SER SER VAL GLU SEQRES 29 C 460 MET LEU LEU ASP VAL VAL LYS GLY THR GLU ALA SER ASN SEQRES 30 C 460 ASP ILE ILE ASP LYS PRO TYR LEU LEU ARG ILE VAL THR SEQRES 31 C 460 HIS LEU ALA ILE CYS LEU ASP ILE ILE ASN PRO GLY SER SEQRES 32 C 460 VAL GLU GLU VAL ASP LYS SER LYS LEU ILE THR THR TYR SEQRES 33 C 460 ILE SER LEU LEU LYS LEU GLN GLY LEU TYR GLU ASN ILE SEQRES 34 C 460 PRO ILE TYR ALA THR PHE LEU ASN GLU SER ASP CYS LEU SEQRES 35 C 460 GLU ALA CYS SER PHE ILE LEU SER SER LEU GLU ASP PRO SEQRES 36 C 460 GLN VAL ARG LYS LYS SEQRES 1 D 297 MET VAL VAL ILE ALA ASN ALA HIS ASN GLU LEU ILE HIS SEQRES 2 D 297 ASP ALA VAL LEU ASP TYR TYR GLY LYS ARG LEU ALA THR SEQRES 3 D 297 CYS SER SER ASP LYS THR ILE LYS ILE PHE GLU VAL GLU SEQRES 4 D 297 GLY GLU THR HIS LYS LEU ILE ASP THR LEU THR GLY HIS SEQRES 5 D 297 GLU GLY PRO VAL TRP ARG VAL ASP TRP ALA HIS PRO LYS SEQRES 6 D 297 PHE GLY THR ILE LEU ALA SER CYS SER TYR ASP GLY LYS SEQRES 7 D 297 VAL LEU ILE TRP LYS GLU GLU ASN GLY ARG TRP SER GLN SEQRES 8 D 297 ILE ALA VAL HIS ALA VAL HIS SER ALA SER VAL ASN SER SEQRES 9 D 297 VAL GLN TRP ALA PRO HIS GLU TYR GLY PRO LEU LEU LEU SEQRES 10 D 297 VAL ALA SER SER ASP GLY LYS VAL SER VAL VAL GLU PHE SEQRES 11 D 297 LYS GLU ASN GLY THR THR SER PRO ILE ILE ILE ASP ALA SEQRES 12 D 297 HIS ALA ILE GLY VAL ASN SER ALA SER TRP ALA PRO ALA SEQRES 13 D 297 THR ILE GLU GLU ASP GLY GLU HIS ASN GLY THR LYS GLU SEQRES 14 D 297 SER ARG LYS PHE VAL THR GLY GLY ALA ASP ASN LEU VAL SEQRES 15 D 297 LYS ILE TRP LYS TYR ASN SER ASP ALA GLN THR TYR VAL SEQRES 16 D 297 LEU GLU SER THR LEU GLU GLY HIS SER ASP TRP VAL ARG SEQRES 17 D 297 ASP VAL ALA TRP SER PRO THR VAL LEU LEU ARG SER TYR SEQRES 18 D 297 LEU ALA SER VAL SER GLN ASP ARG THR CYS ILE ILE TRP SEQRES 19 D 297 THR GLN ASP ASN GLU GLN GLY PRO TRP LYS LYS THR LEU SEQRES 20 D 297 LEU LYS GLU GLU LYS PHE PRO ASP VAL LEU TRP ARG ALA SEQRES 21 D 297 SER TRP SER LEU SER GLY ASN VAL LEU ALA LEU SER GLY SEQRES 22 D 297 GLY ASP ASN LYS VAL THR LEU TRP LYS GLU ASN LEU GLU SEQRES 23 D 297 GLY LYS TRP GLU PRO ALA GLY GLU VAL HIS GLN SEQRES 1 E 442 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP SEQRES 2 E 442 PRO PHE SER GLU CYS ASN ASP GLU ILE ASP ASN ALA LYS SEQRES 3 E 442 LEU ILE MET LYS GLU ARG ARG PHE THR ALA SER TYR THR SEQRES 4 E 442 PHE ALA LYS PHE SER THR GLY SER MET LEU LEU THR LYS SEQRES 5 E 442 ASP ILE VAL GLY LYS SER GLY VAL SER ILE LYS ARG LEU SEQRES 6 E 442 PRO THR GLU LEU GLN ARG LYS PHE LEU PHE ASP ASP VAL SEQRES 7 E 442 TYR LEU ASP LYS GLU ILE GLU LYS VAL THR ILE GLU ALA SEQRES 8 E 442 ARG LYS SER ASN PRO TYR PRO GLN ILE SER GLU SER SER SEQRES 9 E 442 LEU LEU PHE LYS ASP ALA LEU ASP TYR MET GLU LYS THR SEQRES 10 E 442 SER SER ASP TYR ASN LEU TRP LYS LEU SER SER ILE LEU SEQRES 11 E 442 PHE ASP PRO VAL SER TYR PRO TYR LYS THR ASP ASN ASP SEQRES 12 E 442 GLN VAL LYS MET ALA LEU LEU LYS LYS GLU ARG HIS CYS SEQRES 13 E 442 ARG LEU THR SER TRP ILE VAL SER GLN ILE GLY PRO GLU SEQRES 14 E 442 ILE GLU GLU LYS ILE ARG ASN SER SER ASN GLU ILE GLU SEQRES 15 E 442 GLN ILE PHE LEU TYR LEU LEU LEU ASN ASP VAL VAL ARG SEQRES 16 E 442 ALA SER LYS LEU ALA ILE GLU SER LYS ASN GLY HIS LEU SEQRES 17 E 442 SER VAL LEU ILE SER TYR LEU GLY SER ASN ASP PRO ARG SEQRES 18 E 442 ILE ARG ASP LEU ALA GLU LEU GLN LEU GLN LYS TRP SER SEQRES 19 E 442 THR GLY GLY CYS SER ILE ASP LYS ASN ILE SER LYS ILE SEQRES 20 E 442 TYR LYS LEU LEU SER GLY SER PRO PHE GLU GLY LEU PHE SEQRES 21 E 442 SER LEU LYS GLU LEU GLU SER GLU PHE SER TRP LEU CYS SEQRES 22 E 442 LEU LEU ASN LEU THR LEU CYS TYR GLY GLN ILE ASP GLU SEQRES 23 E 442 TYR SER LEU GLU SER LEU VAL GLN SER HIS LEU ASP LYS SEQRES 24 E 442 PHE SER LEU PRO TYR ASP ASP PRO ILE GLY VAL ILE PHE SEQRES 25 E 442 GLN LEU TYR ALA ALA ASN GLU ASN THR GLU LYS LEU TYR SEQRES 26 E 442 LYS GLU VAL ARG GLN ARG THR ASN ALA LEU ASP VAL GLN SEQRES 27 E 442 PHE CYS TRP TYR LEU ILE GLN THR LEU ARG PHE ASN GLY SEQRES 28 E 442 THR ARG VAL PHE SER LYS GLU THR SER ASP GLU ALA THR SEQRES 29 E 442 PHE ALA PHE ALA ALA GLN LEU GLU PHE ALA GLN LEU HIS SEQRES 30 E 442 GLY HIS SER LEU PHE VAL SER CYS PHE LEU ASN ASP ASP SEQRES 31 E 442 LYS ALA ALA GLU ASP THR ILE LYS ARG LEU VAL MET ARG SEQRES 32 E 442 GLU ILE THR LEU LEU ARG ALA SER THR ASN ASP HIS ILE SEQRES 33 E 442 LEU ASN ARG LEU LYS ILE PRO SER GLN LEU ILE PHE ASN SEQRES 34 E 442 ALA GLN ALA LEU LYS ASP ARG TYR GLU GLY ASN TYR LEU SEQRES 1 F 460 MET GLU LEU SER PRO THR TYR GLN THR GLU ARG PHE THR SEQRES 2 F 460 LYS PHE SER ASP THR LEU LYS GLU PHE LYS ILE GLU GLN SEQRES 3 F 460 ASN ASN GLU GLN ASN PRO ILE ASP PRO PHE ASN ILE ILE SEQRES 4 F 460 ARG GLU PHE ARG SER ALA ALA GLY GLN LEU ALA LEU ASP SEQRES 5 F 460 LEU ALA ASN SER GLY ASP GLU SER ASN VAL ILE SER SER SEQRES 6 F 460 LYS ASP TRP GLU LEU GLU ALA ARG PHE TRP HIS LEU VAL SEQRES 7 F 460 GLU LEU LEU LEU VAL PHE ARG ASN ALA ASP LEU ASP LEU SEQRES 8 F 460 ASP GLU MET GLU LEU HIS PRO TYR ASN SER ARG GLY LEU SEQRES 9 F 460 PHE GLU LYS LYS LEU MET GLN ASP ASN LYS GLN LEU TYR SEQRES 10 F 460 GLN ILE TRP ILE VAL MET VAL TRP LEU LYS GLU ASN THR SEQRES 11 F 460 TYR VAL MET GLU ARG PRO LYS ASN VAL PRO THR SER LYS SEQRES 12 F 460 TRP LEU ASN SER ILE THR SER GLY GLY LEU LYS SER CYS SEQRES 13 F 460 ASP LEU ASP PHE PRO LEU ARG GLU ASN THR ASN VAL LEU SEQRES 14 F 460 ASP VAL LYS ASP LYS GLU GLU ASP HIS ILE PHE PHE LYS SEQRES 15 F 460 TYR ILE TYR GLU LEU ILE LEU ALA GLY ALA ILE ASP GLU SEQRES 16 F 460 ALA LEU GLU GLU ALA LYS LEU SER ASP ASN ILE SER ILE SEQRES 17 F 460 CYS MET ILE LEU CYS GLY ILE GLN GLU TYR LEU ASN PRO SEQRES 18 F 460 VAL ILE ASP THR GLN ILE ALA ASN GLU PHE ASN THR GLN SEQRES 19 F 460 GLN GLY ILE LYS LYS HIS SER LEU TRP ARG ARG THR VAL SEQRES 20 F 460 TYR SER LEU SER GLN GLN ALA GLY LEU ASP PRO TYR GLU SEQRES 21 F 460 ARG ALA ILE TYR SER TYR LEU SER GLY ALA ILE PRO ASN SEQRES 22 F 460 GLN GLU VAL LEU GLN TYR SER ASP TRP GLU SER ASP LEU SEQRES 23 F 460 HIS ILE HIS LEU ASN GLN ILE LEU GLN THR GLU ILE GLU SEQRES 24 F 460 ASN TYR LEU LEU GLU ASN ASN GLN VAL GLY THR ASP GLU SEQRES 25 F 460 LEU ILE LEU PRO LEU PRO SER HIS ALA LEU THR VAL GLN SEQRES 26 F 460 GLU VAL LEU ASN ARG VAL ALA SER ARG HIS PRO SER GLU SEQRES 27 F 460 SER GLU HIS PRO ILE ARG VAL LEU MET ALA SER VAL ILE SEQRES 28 F 460 LEU ASP SER LEU PRO SER VAL ILE HIS SER SER VAL GLU SEQRES 29 F 460 MET LEU LEU ASP VAL VAL LYS GLY THR GLU ALA SER ASN SEQRES 30 F 460 ASP ILE ILE ASP LYS PRO TYR LEU LEU ARG ILE VAL THR SEQRES 31 F 460 HIS LEU ALA ILE CYS LEU ASP ILE ILE ASN PRO GLY SER SEQRES 32 F 460 VAL GLU GLU VAL ASP LYS SER LYS LEU ILE THR THR TYR SEQRES 33 F 460 ILE SER LEU LEU LYS LEU GLN GLY LEU TYR GLU ASN ILE SEQRES 34 F 460 PRO ILE TYR ALA THR PHE LEU ASN GLU SER ASP CYS LEU SEQRES 35 F 460 GLU ALA CYS SER PHE ILE LEU SER SER LEU GLU ASP PRO SEQRES 36 F 460 GLN VAL ARG LYS LYS SEQRES 1 G 297 MET VAL VAL ILE ALA ASN ALA HIS ASN GLU LEU ILE HIS SEQRES 2 G 297 ASP ALA VAL LEU ASP TYR TYR GLY LYS ARG LEU ALA THR SEQRES 3 G 297 CYS SER SER ASP LYS THR ILE LYS ILE PHE GLU VAL GLU SEQRES 4 G 297 GLY GLU THR HIS LYS LEU ILE ASP THR LEU THR GLY HIS SEQRES 5 G 297 GLU GLY PRO VAL TRP ARG VAL ASP TRP ALA HIS PRO LYS SEQRES 6 G 297 PHE GLY THR ILE LEU ALA SER CYS SER TYR ASP GLY LYS SEQRES 7 G 297 VAL LEU ILE TRP LYS GLU GLU ASN GLY ARG TRP SER GLN SEQRES 8 G 297 ILE ALA VAL HIS ALA VAL HIS SER ALA SER VAL ASN SER SEQRES 9 G 297 VAL GLN TRP ALA PRO HIS GLU TYR GLY PRO LEU LEU LEU SEQRES 10 G 297 VAL ALA SER SER ASP GLY LYS VAL SER VAL VAL GLU PHE SEQRES 11 G 297 LYS GLU ASN GLY THR THR SER PRO ILE ILE ILE ASP ALA SEQRES 12 G 297 HIS ALA ILE GLY VAL ASN SER ALA SER TRP ALA PRO ALA SEQRES 13 G 297 THR ILE GLU GLU ASP GLY GLU HIS ASN GLY THR LYS GLU SEQRES 14 G 297 SER ARG LYS PHE VAL THR GLY GLY ALA ASP ASN LEU VAL SEQRES 15 G 297 LYS ILE TRP LYS TYR ASN SER ASP ALA GLN THR TYR VAL SEQRES 16 G 297 LEU GLU SER THR LEU GLU GLY HIS SER ASP TRP VAL ARG SEQRES 17 G 297 ASP VAL ALA TRP SER PRO THR VAL LEU LEU ARG SER TYR SEQRES 18 G 297 LEU ALA SER VAL SER GLN ASP ARG THR CYS ILE ILE TRP SEQRES 19 G 297 THR GLN ASP ASN GLU GLN GLY PRO TRP LYS LYS THR LEU SEQRES 20 G 297 LEU LYS GLU GLU LYS PHE PRO ASP VAL LEU TRP ARG ALA SEQRES 21 G 297 SER TRP SER LEU SER GLY ASN VAL LEU ALA LEU SER GLY SEQRES 22 G 297 GLY ASP ASN LYS VAL THR LEU TRP LYS GLU ASN LEU GLU SEQRES 23 G 297 GLY LYS TRP GLU PRO ALA GLY GLU VAL HIS GLN SEQRES 1 H 442 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP SEQRES 2 H 442 PRO PHE SER GLU CYS ASN ASP GLU ILE ASP ASN ALA LYS SEQRES 3 H 442 LEU ILE MET LYS GLU ARG ARG PHE THR ALA SER TYR THR SEQRES 4 H 442 PHE ALA LYS PHE SER THR GLY SER MET LEU LEU THR LYS SEQRES 5 H 442 ASP ILE VAL GLY LYS SER GLY VAL SER ILE LYS ARG LEU SEQRES 6 H 442 PRO THR GLU LEU GLN ARG LYS PHE LEU PHE ASP ASP VAL SEQRES 7 H 442 TYR LEU ASP LYS GLU ILE GLU LYS VAL THR ILE GLU ALA SEQRES 8 H 442 ARG LYS SER ASN PRO TYR PRO GLN ILE SER GLU SER SER SEQRES 9 H 442 LEU LEU PHE LYS ASP ALA LEU ASP TYR MET GLU LYS THR SEQRES 10 H 442 SER SER ASP TYR ASN LEU TRP LYS LEU SER SER ILE LEU SEQRES 11 H 442 PHE ASP PRO VAL SER TYR PRO TYR LYS THR ASP ASN ASP SEQRES 12 H 442 GLN VAL LYS MET ALA LEU LEU LYS LYS GLU ARG HIS CYS SEQRES 13 H 442 ARG LEU THR SER TRP ILE VAL SER GLN ILE GLY PRO GLU SEQRES 14 H 442 ILE GLU GLU LYS ILE ARG ASN SER SER ASN GLU ILE GLU SEQRES 15 H 442 GLN ILE PHE LEU TYR LEU LEU LEU ASN ASP VAL VAL ARG SEQRES 16 H 442 ALA SER LYS LEU ALA ILE GLU SER LYS ASN GLY HIS LEU SEQRES 17 H 442 SER VAL LEU ILE SER TYR LEU GLY SER ASN ASP PRO ARG SEQRES 18 H 442 ILE ARG ASP LEU ALA GLU LEU GLN LEU GLN LYS TRP SER SEQRES 19 H 442 THR GLY GLY CYS SER ILE ASP LYS ASN ILE SER LYS ILE SEQRES 20 H 442 TYR LYS LEU LEU SER GLY SER PRO PHE GLU GLY LEU PHE SEQRES 21 H 442 SER LEU LYS GLU LEU GLU SER GLU PHE SER TRP LEU CYS SEQRES 22 H 442 LEU LEU ASN LEU THR LEU CYS TYR GLY GLN ILE ASP GLU SEQRES 23 H 442 TYR SER LEU GLU SER LEU VAL GLN SER HIS LEU ASP LYS SEQRES 24 H 442 PHE SER LEU PRO TYR ASP ASP PRO ILE GLY VAL ILE PHE SEQRES 25 H 442 GLN LEU TYR ALA ALA ASN GLU ASN THR GLU LYS LEU TYR SEQRES 26 H 442 LYS GLU VAL ARG GLN ARG THR ASN ALA LEU ASP VAL GLN SEQRES 27 H 442 PHE CYS TRP TYR LEU ILE GLN THR LEU ARG PHE ASN GLY SEQRES 28 H 442 THR ARG VAL PHE SER LYS GLU THR SER ASP GLU ALA THR SEQRES 29 H 442 PHE ALA PHE ALA ALA GLN LEU GLU PHE ALA GLN LEU HIS SEQRES 30 H 442 GLY HIS SER LEU PHE VAL SER CYS PHE LEU ASN ASP ASP SEQRES 31 H 442 LYS ALA ALA GLU ASP THR ILE LYS ARG LEU VAL MET ARG SEQRES 32 H 442 GLU ILE THR LEU LEU ARG ALA SER THR ASN ASP HIS ILE SEQRES 33 H 442 LEU ASN ARG LEU LYS ILE PRO SER GLN LEU ILE PHE ASN SEQRES 34 H 442 ALA GLN ALA LEU LYS ASP ARG TYR GLU GLY ASN TYR LEU SEQRES 1 I 460 MET GLU LEU SER PRO THR TYR GLN THR GLU ARG PHE THR SEQRES 2 I 460 LYS PHE SER ASP THR LEU LYS GLU PHE LYS ILE GLU GLN SEQRES 3 I 460 ASN ASN GLU GLN ASN PRO ILE ASP PRO PHE ASN ILE ILE SEQRES 4 I 460 ARG GLU PHE ARG SER ALA ALA GLY GLN LEU ALA LEU ASP SEQRES 5 I 460 LEU ALA ASN SER GLY ASP GLU SER ASN VAL ILE SER SER SEQRES 6 I 460 LYS ASP TRP GLU LEU GLU ALA ARG PHE TRP HIS LEU VAL SEQRES 7 I 460 GLU LEU LEU LEU VAL PHE ARG ASN ALA ASP LEU ASP LEU SEQRES 8 I 460 ASP GLU MET GLU LEU HIS PRO TYR ASN SER ARG GLY LEU SEQRES 9 I 460 PHE GLU LYS LYS LEU MET GLN ASP ASN LYS GLN LEU TYR SEQRES 10 I 460 GLN ILE TRP ILE VAL MET VAL TRP LEU LYS GLU ASN THR SEQRES 11 I 460 TYR VAL MET GLU ARG PRO LYS ASN VAL PRO THR SER LYS SEQRES 12 I 460 TRP LEU ASN SER ILE THR SER GLY GLY LEU LYS SER CYS SEQRES 13 I 460 ASP LEU ASP PHE PRO LEU ARG GLU ASN THR ASN VAL LEU SEQRES 14 I 460 ASP VAL LYS ASP LYS GLU GLU ASP HIS ILE PHE PHE LYS SEQRES 15 I 460 TYR ILE TYR GLU LEU ILE LEU ALA GLY ALA ILE ASP GLU SEQRES 16 I 460 ALA LEU GLU GLU ALA LYS LEU SER ASP ASN ILE SER ILE SEQRES 17 I 460 CYS MET ILE LEU CYS GLY ILE GLN GLU TYR LEU ASN PRO SEQRES 18 I 460 VAL ILE ASP THR GLN ILE ALA ASN GLU PHE ASN THR GLN SEQRES 19 I 460 GLN GLY ILE LYS LYS HIS SER LEU TRP ARG ARG THR VAL SEQRES 20 I 460 TYR SER LEU SER GLN GLN ALA GLY LEU ASP PRO TYR GLU SEQRES 21 I 460 ARG ALA ILE TYR SER TYR LEU SER GLY ALA ILE PRO ASN SEQRES 22 I 460 GLN GLU VAL LEU GLN TYR SER ASP TRP GLU SER ASP LEU SEQRES 23 I 460 HIS ILE HIS LEU ASN GLN ILE LEU GLN THR GLU ILE GLU SEQRES 24 I 460 ASN TYR LEU LEU GLU ASN ASN GLN VAL GLY THR ASP GLU SEQRES 25 I 460 LEU ILE LEU PRO LEU PRO SER HIS ALA LEU THR VAL GLN SEQRES 26 I 460 GLU VAL LEU ASN ARG VAL ALA SER ARG HIS PRO SER GLU SEQRES 27 I 460 SER GLU HIS PRO ILE ARG VAL LEU MET ALA SER VAL ILE SEQRES 28 I 460 LEU ASP SER LEU PRO SER VAL ILE HIS SER SER VAL GLU SEQRES 29 I 460 MET LEU LEU ASP VAL VAL LYS GLY THR GLU ALA SER ASN SEQRES 30 I 460 ASP ILE ILE ASP LYS PRO TYR LEU LEU ARG ILE VAL THR SEQRES 31 I 460 HIS LEU ALA ILE CYS LEU ASP ILE ILE ASN PRO GLY SER SEQRES 32 I 460 VAL GLU GLU VAL ASP LYS SER LYS LEU ILE THR THR TYR SEQRES 33 I 460 ILE SER LEU LEU LYS LEU GLN GLY LEU TYR GLU ASN ILE SEQRES 34 I 460 PRO ILE TYR ALA THR PHE LEU ASN GLU SER ASP CYS LEU SEQRES 35 I 460 GLU ALA CYS SER PHE ILE LEU SER SER LEU GLU ASP PRO SEQRES 36 I 460 GLN VAL ARG LYS LYS HELIX 44 44 HIS A 63 GLY A 67 1 5 SHEET 30 30 1 ILE A 12 LEU A 17 0 SHEET 31 31 1 ARG A 23 SER A 28 0 SHEET 32 32 1 THR A 32 GLU A 37 0 SHEET 33 33 1 LYS A 44 LEU A 45 0 SHEET 34 34 1 LEU A 49 THR A 50 0 SHEET 35 35 1 VAL A 56 ARG A 58 0 SHEET 36 36 1 ILE A 69 SER A 74 0 SHEET 37 37 1 VAL A 79 GLU A 85 0 SHEET 38 38 1 ARG A 88 TRP A 89 0 SHEET 39 39 1 ALA A 93 HIS A 95 0 SHEET 40 40 1 VAL A 102 VAL A 105 0 SHEET 41 41 1 VAL A 118 SER A 120 0 SHEET 42 42 1 LYS A 124 SER A 126 0 SHEET 43 43 1 GLU A 129 PHE A 130 0 SHEET 44 44 1 THR A 136 SER A 137 0 SHEET 45 45 1 ILE A 141 ASP A 142 0 SHEET 46 46 1 VAL A 148 TRP A 153 0 SHEET 47 47 1 LYS A 172 GLY A 177 0 SHEET 48 48 1 LEU A 181 LYS A 186 0 SHEET 49 49 1 VAL A 195 GLU A 201 0 SHEET 50 50 1 ALA A 223 VAL A 225 0 SHEET 51 51 1 CYS A 231 ILE A 233 0 SHEET 52 52 1 LEU A 257 TRP A 262 0 SHEET 53 53 1 LEU A 269 GLY A 273 0 SHEET 54 54 1 VAL A 278 GLU A 283 0 SHEET 55 55 1 TRP A 289 PRO A 291 0 CRYST1 101.397 194.050 327.806 90.00 90.00 90.00 P 21 21 21 12 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 0.009862 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005153 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003051 0.00000 ATOM 1 N HIS A 8 96.169 182.339 839.320 1.00192.53 N ATOM 2 CA HIS A 8 95.286 182.213 840.486 1.00197.76 C ATOM 3 CB HIS A 8 94.989 180.741 840.776 1.00201.57 C ATOM 4 CG HIS A 8 93.674 180.512 841.562 1.00201.57 C ATOM 5 CD2 HIS A 8 93.453 180.274 842.877 1.00201.57 C ATOM 6 NE2 HIS A 8 92.095 180.146 843.041 1.00201.57 N ATOM 7 CE1 HIS A 8 91.505 180.300 841.870 1.00201.57 C ATOM 8 ND1 HIS A 8 92.435 180.522 840.959 1.00201.57 N ATOM 9 C HIS A 8 95.875 182.848 841.712 1.00201.57 C ATOM 10 O HIS A 8 97.067 182.708 842.024 1.00200.66 O ATOM 11 N ASN A 9 95.028 183.533 842.408 1.00201.33 N ATOM 12 CA ASN A 9 95.349 184.131 843.680 1.00201.33 C ATOM 13 CB ASN A 9 96.733 184.781 843.633 1.00201.47 C ATOM 14 CG ASN A 9 97.591 184.411 844.828 1.00201.47 C ATOM 15 ND2 ASN A 9 97.174 183.386 845.561 1.00201.47 N ATOM 16 OD1 ASN A 9 98.606 185.053 845.097 1.00201.47 O ATOM 17 C ASN A 9 94.242 185.031 843.999 1.00201.33 C ATOM 18 O ASN A 9 94.166 186.239 843.722 1.00201.33 O ATOM 19 N GLU A 10 93.374 184.317 844.624 1.00201.40 N ATOM 20 CA GLU A 10 92.123 184.763 845.085 1.00201.40 C ATOM 21 CB GLU A 10 91.093 183.633 845.017 1.00201.57 C ATOM 22 CG GLU A 10 90.867 183.083 843.618 1.00201.57 C ATOM 23 CD GLU A 10 90.370 184.139 842.650 1.00201.57 C ATOM 24 OE1 GLU A 10 90.202 185.302 843.073 1.00201.57 O ATOM 25 OE2 GLU A 10 90.165 183.808 841.464 1.00201.57 O ATOM 26 C GLU A 10 92.220 185.302 846.492 1.00201.40 C ATOM 27 O GLU A 10 91.246 185.891 846.986 1.00201.40 O ATOM 28 N LEU A 11 93.355 185.136 847.168 1.00134.65 N ATOM 29 CA LEU A 11 93.383 185.655 848.526 1.00134.65 C ATOM 30 C LEU A 11 94.762 185.608 849.215 1.00134.65 C ATOM 31 O LEU A 11 95.139 184.589 849.807 1.00134.65 O ATOM 32 CB LEU A 11 92.418 184.873 849.418 1.00201.57 C ATOM 33 CG LEU A 11 92.162 185.452 850.811 1.00201.57 C ATOM 34 CD2 LEU A 11 91.455 184.434 851.695 1.00198.74 C ATOM 35 CD1 LEU A 11 91.351 186.735 850.720 1.00198.74 C ATOM 36 N ILE A 12 95.520 186.702 849.147 1.00135.80 N ATOM 37 CA ILE A 12 96.808 186.817 849.819 1.00136.11 C ATOM 38 CB ILE A 12 97.822 187.617 848.955 1.00106.33 C ATOM 39 CG2 ILE A 12 99.087 187.928 849.745 1.00107.93 C ATOM 40 CG1 ILE A 12 98.154 186.841 847.678 1.00107.91 C ATOM 41 CD1 ILE A 12 98.486 187.722 846.492 1.00136.93 C ATOM 42 C ILE A 12 96.568 187.528 851.142 1.00134.33 C ATOM 43 O ILE A 12 96.078 188.652 851.131 1.00126.90 O ATOM 44 N HIS A 13 96.911 186.925 852.274 1.00146.59 N ATOM 45 CA HIS A 13 96.625 187.525 853.606 1.00146.59 C ATOM 46 CB HIS A 13 96.621 186.444 854.681 1.00201.22 C ATOM 47 CG HIS A 13 95.242 186.157 855.268 1.00201.22 C ATOM 48 CD2 HIS A 13 94.459 185.057 855.166 1.00201.22 C ATOM 49 NE2 HIS A 13 93.313 185.311 855.881 1.00198.77 N ATOM 50 CE1 HIS A 13 93.391 186.523 856.402 1.00201.22 C ATOM 51 ND1 HIS A 13 94.547 187.056 856.048 1.00201.22 N ATOM 52 C HIS A 13 97.600 188.596 854.056 1.00146.59 C ATOM 53 O HIS A 13 97.233 189.434 854.884 1.00146.59 O ATOM 54 N ASP A 14 98.827 188.583 853.550 1.00167.17 N ATOM 55 CA ASP A 14 99.801 189.591 853.952 1.00167.17 C ATOM 56 CB ASP A 14 100.396 189.241 855.325 1.00133.34 C ATOM 57 CG ASP A 14 101.071 190.430 855.994 1.00133.34 C ATOM 58 OD2 ASP A 14 101.822 190.232 856.970 1.00133.34 O ATOM 59 OD1 ASP A 14 100.843 191.568 855.521 1.00133.34 O ATOM 60 C ASP A 14 100.907 189.724 852.916 1.00167.17 C ATOM 61 O ASP A 14 101.201 188.788 852.175 1.00167.17 O ATOM 62 N ALA A 15 101.501 190.911 852.862 1.00145.40 N ATOM 63 CA ALA A 15 102.589 191.210 851.939 1.00145.40 C ATOM 64 C ALA A 15 103.547 192.149 852.675 1.00145.40 C ATOM 65 O ALA A 15 103.122 192.886 853.563 1.00145.40 O ATOM 66 CB ALA A 15 102.037 191.885 850.679 1.00104.50 C ATOM 67 N VAL A 16 104.835 192.116 852.335 1.00131.22 N ATOM 68 CA VAL A 16 105.793 192.997 853.009 1.00129.37 C ATOM 69 CB VAL A 16 106.407 192.283 854.261 1.00 94.04 C ATOM 70 CG1 VAL A 16 107.528 193.122 854.872 1.00 94.04 C ATOM 71 CG2 VAL A 16 105.316 192.081 855.313 1.00 93.45 C ATOM 72 C VAL A 16 106.893 193.555 852.085 1.00133.77 C ATOM 73 O VAL A 16 107.236 192.954 851.070 1.00137.22 O ATOM 74 N LEU A 17 107.412 194.728 852.451 1.00150.42 N ATOM 75 CA LEU A 17 108.450 195.414 851.702 1.00150.25 C ATOM 76 CB LEU A 17 108.035 196.840 851.459 1.00201.57 C ATOM 77 CG LEU A 17 106.799 196.975 850.635 1.00201.57 C ATOM 78 CD2 LEU A 17 107.060 196.384 849.291 1.00107.58 C ATOM 79 CD1 LEU A 17 106.509 198.406 850.472 1.00107.58 C ATOM 80 C LEU A 17 109.766 195.431 852.448 1.00150.42 C ATOM 81 O LEU A 17 109.804 195.680 853.658 1.00150.42 O ATOM 82 N ASP A 18 110.843 195.163 851.715 1.00136.00 N ATOM 83 CA ASP A 18 112.187 195.148 852.278 1.00136.00 C ATOM 84 C ASP A 18 112.676 196.584 852.438 1.00136.00 C ATOM 85 O ASP A 18 112.261 197.471 851.692 1.00136.00 O ATOM 86 CB ASP A 18 113.126 194.353 851.361 1.00157.29 C ATOM 87 CG ASP A 18 112.941 194.702 849.893 1.00161.76 C ATOM 88 OD2 ASP A 18 113.942 194.957 849.195 1.00167.02 O ATOM 89 OD1 ASP A 18 111.783 194.716 849.433 1.00153.25 O ATOM 90 N TYR A 19 113.544 196.799 853.421 1.00146.33 N ATOM 91 CA TYR A 19 114.101 198.115 853.734 1.00149.45 C ATOM 92 CB TYR A 19 115.453 197.943 854.418 1.00127.57 C ATOM 93 CG TYR A 19 115.916 199.141 855.211 1.00134.42 C ATOM 94 CD2 TYR A 19 116.930 199.962 854.733 1.00136.79 C ATOM 95 CE2 TYR A 19 117.390 201.043 855.462 1.00139.28 C ATOM 96 CZ TYR A 19 116.838 201.316 856.696 1.00140.67 C ATOM 97 OH TYR A 19 117.304 202.387 857.419 1.00142.80 O ATOM 98 CE1 TYR A 19 115.820 200.518 857.202 1.00142.00 C ATOM 99 CD1 TYR A 19 115.365 199.432 856.455 1.00137.50 C ATOM 100 C TYR A 19 114.266 199.039 852.526 1.00146.83 C ATOM 101 O TYR A 19 114.057 200.253 852.634 1.00152.94 O ATOM 102 N TYR A 20 114.639 198.466 851.384 1.00101.31 N ATOM 103 CA TYR A 20 114.846 199.242 850.159 1.00102.80 C ATOM 104 C TYR A 20 113.735 199.028 849.140 1.00104.21 C ATOM 105 O TYR A 20 113.842 199.472 847.989 1.00 95.11 O ATOM 106 CB TYR A 20 116.197 198.886 849.513 1.00105.43 C ATOM 107 CG TYR A 20 117.405 199.221 850.362 1.00100.14 C ATOM 108 CD1 TYR A 20 117.461 198.848 851.711 1.00 99.22 C ATOM 109 CE1 TYR A 20 118.561 199.152 852.502 1.00102.16 C ATOM 110 CZ TYR A 20 119.627 199.838 851.958 1.00108.16 C ATOM 111 OH TYR A 20 120.705 200.152 852.764 1.00103.90 O ATOM 112 CE2 TYR A 20 119.601 200.221 850.621 1.00106.88 C ATOM 113 CD2 TYR A 20 118.493 199.910 849.829 1.00103.74 C ATOM 114 N GLY A 21 112.675 198.342 849.569 1.00148.15 N ATOM 115 CA GLY A 21 111.541 198.066 848.701 1.00148.15 C ATOM 116 C GLY A 21 111.880 197.693 847.267 1.00148.15 C ATOM 117 O GLY A 21 111.509 198.399 846.330 1.00148.15 O ATOM 118 N LYS A 22 112.588 196.585 847.087 1.00140.85 N ATOM 119 CA LYS A 22 112.952 196.128 845.754 1.00140.85 C ATOM 120 CB LYS A 22 114.471 196.204 845.566 1.00124.57 C ATOM 121 CG LYS A 22 114.901 196.866 844.266 1.00129.82 C ATOM 122 CD LYS A 22 116.419 196.960 844.156 1.00132.58 C ATOM 123 CE LYS A 22 116.834 197.868 843.005 1.00132.39 C ATOM 124 NZ LYS A 22 116.150 197.514 841.727 1.00130.06 N ATOM 125 C LYS A 22 112.481 194.687 845.601 1.00140.85 C ATOM 126 O LYS A 22 112.290 194.192 844.488 1.00140.85 O ATOM 127 N ARG A 23 112.270 194.040 846.746 1.00177.70 N ATOM 128 CA ARG A 23 111.845 192.643 846.831 1.00177.70 C ATOM 129 C ARG A 23 110.540 192.490 847.642 1.00177.70 C ATOM 130 O ARG A 23 110.537 192.670 848.860 1.00177.70 O ATOM 131 CB ARG A 23 112.975 191.844 847.497 1.00142.26 C ATOM 132 CG ARG A 23 113.383 190.552 846.803 1.00148.20 C ATOM 133 CD ARG A 23 114.627 189.942 847.471 1.00152.53 C ATOM 134 NE ARG A 23 115.868 190.646 847.136 1.00154.43 N ATOM 135 CZ ARG A 23 117.050 190.434 847.723 1.00154.14 C ATOM 136 NH2 ARG A 23 118.118 191.127 847.335 1.00153.63 N ATOM 137 NH1 ARG A 23 117.175 189.535 848.691 1.00152.72 N ATOM 138 N LEU A 24 109.438 192.155 846.974 1.00150.16 N ATOM 139 CA LEU A 24 108.141 191.974 847.649 1.00143.70 C ATOM 140 CB LEU A 24 107.000 192.435 846.734 1.00102.19 C ATOM 141 CG LEU A 24 105.556 192.105 847.134 1.00102.19 C ATOM 142 CD1 LEU A 24 105.223 192.690 848.507 1.00102.19 C ATOM 143 CD2 LEU A 24 104.620 192.647 846.063 1.00102.19 C ATOM 144 C LEU A 24 107.896 190.520 848.064 1.00143.55 C ATOM 145 O LEU A 24 108.233 189.596 847.325 1.00146.65 O ATOM 146 N ALA A 25 107.295 190.319 849.238 1.00136.90 N ATOM 147 CA ALA A 25 107.020 188.967 849.725 1.00136.90 C ATOM 148 CB ALA A 25 107.934 188.637 850.904 1.00133.71 C ATOM 149 C ALA A 25 105.565 188.753 850.139 1.00136.90 C ATOM 150 O ALA A 25 105.220 188.982 851.296 1.00136.90 O ATOM 151 N THR A 26 104.726 188.301 849.202 1.00145.49 N ATOM 152 CA THR A 26 103.304 188.041 849.474 1.00145.49 C ATOM 153 C THR A 26 103.052 186.592 849.887 1.00145.49 C ATOM 154 O THR A 26 103.635 185.667 849.324 1.00138.15 O ATOM 155 CB THR A 26 102.387 188.347 848.238 1.00134.48 C ATOM 156 OG1 THR A 26 102.913 187.712 847.066 1.00136.55 O ATOM 157 CG2 THR A 26 102.268 189.852 848.003 1.00128.38 C ATOM 158 N CYS A 27 102.180 186.399 850.870 1.00118.20 N ATOM 159 CA CYS A 27 101.848 185.059 851.344 1.00116.90 C ATOM 160 C CYS A 27 100.331 184.875 851.442 1.00118.20 C ATOM 161 O CYS A 27 99.649 185.651 852.116 1.00118.20 O ATOM 162 CB CYS A 27 102.503 184.804 852.705 1.00103.46 C ATOM 163 SG CYS A 27 101.851 185.784 854.074 1.00109.14 S ATOM 164 N SER A 28 99.811 183.845 850.770 1.00140.03 N ATOM 165 CA SER A 28 98.370 183.575 850.757 1.00140.03 C ATOM 166 C SER A 28 97.902 182.384 851.605 1.00140.03 C ATOM 167 O SER A 28 98.534 182.026 852.606 1.00140.03 O ATOM 168 CB SER A 28 97.888 183.396 849.309 1.00181.07 C ATOM 169 OG SER A 28 98.613 182.377 848.642 1.00181.07 O ATOM 170 N SER A 29 96.780 181.790 851.196 1.00128.39 N ATOM 171 CA SER A 29 96.196 180.650 851.899 1.00133.36 C ATOM 172 CB SER A 29 94.672 180.672 851.776 1.00106.24 C ATOM 173 OG SER A 29 94.129 181.867 852.308 1.00106.40 O ATOM 174 C SER A 29 96.718 179.309 851.397 1.00133.88 C ATOM 175 O SER A 29 96.770 178.341 852.158 1.00135.49 O ATOM 176 N ASP A 30 97.102 179.245 850.121 1.00181.24 N ATOM 177 CA ASP A 30 97.619 178.000 849.563 1.00181.24 C ATOM 178 CB ASP A 30 97.755 178.089 848.029 1.00147.38 C ATOM 179 CG ASP A 30 98.018 179.501 847.532 1.00153.19 C ATOM 180 OD2 ASP A 30 97.167 180.037 846.789 1.00156.32 O ATOM 181 OD1 ASP A 30 99.074 180.074 847.874 1.00155.42 O ATOM 182 C ASP A 30 98.945 177.592 850.207 1.00181.24 C ATOM 183 O ASP A 30 99.637 176.695 849.720 1.00181.24 O ATOM 184 N LYS A 31 99.276 178.260 851.311 1.00167.73 N ATOM 185 CA LYS A 31 100.483 177.995 852.094 1.00167.73 C ATOM 186 CB LYS A 31 100.560 176.500 852.420 1.00161.32 C ATOM 187 CG LYS A 31 99.257 175.923 852.964 1.00165.18 C ATOM 188 CD LYS A 31 99.315 174.406 853.042 1.00172.92 C ATOM 189 CE LYS A 31 97.975 173.818 853.445 1.00179.22 C ATOM 190 NZ LYS A 31 98.021 172.332 853.441 1.00180.09 N ATOM 191 C LYS A 31 101.802 178.459 851.466 1.00167.73 C ATOM 192 O LYS A 31 102.863 178.328 852.088 1.00167.73 O ATOM 193 N THR A 32 101.740 179.002 850.249 1.00158.96 N ATOM 194 CA THR A 32 102.946 179.472 849.565 1.00158.96 C ATOM 195 CB THR A 32 102.911 179.209 848.017 1.00158.77 C ATOM 196 CG2 THR A 32 102.681 177.731 847.719 1.00158.77 C ATOM 197 OG1 THR A 32 101.878 179.996 847.406 1.00158.77 O ATOM 198 C THR A 32 103.221 180.959 849.772 1.00158.96 C ATOM 199 O THR A 32 102.302 181.776 849.860 1.00158.96 O ATOM 200 N ILE A 33 104.506 181.283 849.853 1.00148.17 N ATOM 201 CA ILE A 33 104.995 182.644 850.029 1.00146.48 C ATOM 202 CB ILE A 33 105.986 182.712 851.231 1.00125.65 C ATOM 203 CG2 ILE A 33 106.690 184.067 851.264 1.00124.28 C ATOM 204 CG1 ILE A 33 105.231 182.462 852.542 1.00120.18 C ATOM 205 CD1 ILE A 33 105.906 181.484 853.467 1.00158.23 C ATOM 206 C ILE A 33 105.716 182.986 848.719 1.00147.39 C ATOM 207 O ILE A 33 106.767 182.422 848.421 1.00144.64 O ATOM 208 N LYS A 34 105.146 183.894 847.932 1.00128.96 N ATOM 209 CA LYS A 34 105.741 184.278 846.651 1.00128.96 C ATOM 210 C LYS A 34 106.621 185.537 846.711 1.00128.96 C ATOM 211 O LYS A 34 106.146 186.620 847.055 1.00128.96 O ATOM 212 CB LYS A 34 104.633 184.484 845.607 1.00135.49 C ATOM 213 CG LYS A 34 103.742 183.272 845.362 1.00136.75 C ATOM 214 CD LYS A 34 102.594 183.626 844.425 1.00135.19 C ATOM 215 CE LYS A 34 101.755 182.411 844.100 1.00135.95 C ATOM 216 NZ LYS A 34 102.576 181.372 843.421 1.00136.22 N ATOM 217 N ILE A 35 107.900 185.389 846.362 1.00188.35 N ATOM 218 CA ILE A 35 108.856 186.501 846.353 1.00188.13 C ATOM 219 CB ILE A 35 110.272 186.025 846.820 1.00100.00 C ATOM 220 CG2 ILE A 35 111.355 186.869 846.151 1.00 95.03 C ATOM 221 CG1 ILE A 35 110.396 186.110 848.349 1.00 94.26 C ATOM 222 CD1 ILE A 35 109.437 185.239 849.128 1.00125.68 C ATOM 223 C ILE A 35 108.962 187.124 844.946 1.00188.35 C ATOM 224 O ILE A 35 109.133 186.415 843.953 1.00188.35 O ATOM 225 N PHE A 36 108.863 188.450 844.871 1.00138.93 N ATOM 226 CA PHE A 36 108.931 189.162 843.594 1.00140.12 C ATOM 227 C PHE A 36 110.064 190.191 843.552 1.00140.12 C ATOM 228 O PHE A 36 110.599 190.592 844.586 1.00140.12 O ATOM 229 CB PHE A 36 107.620 189.916 843.318 1.00173.54 C ATOM 230 CG PHE A 36 106.391 189.046 843.261 1.00173.54 C ATOM 231 CD1 PHE A 36 105.971 188.320 844.372 1.00173.54 C ATOM 232 CE1 PHE A 36 104.790 187.569 844.336 1.00173.54 C ATOM 233 CZ PHE A 36 104.021 187.540 843.180 1.00173.54 C ATOM 234 CE2 PHE A 36 104.433 188.259 842.062 1.00173.54 C ATOM 235 CD2 PHE A 36 105.614 189.006 842.107 1.00173.54 C ATOM 236 N GLU A 37 110.416 190.619 842.340 1.00153.63 N ATOM 237 CA GLU A 37 111.441 191.640 842.128 1.00153.63 C ATOM 238 C GLU A 37 110.699 192.861 841.597 1.00153.63 C ATOM 239 O GLU A 37 110.668 193.099 840.387 1.00153.63 O ATOM 240 CB GLU A 37 112.476 191.184 841.092 1.00201.43 C ATOM 241 CG GLU A 37 113.651 190.414 841.671 1.00201.43 C ATOM 242 CD GLU A 37 114.316 191.145 842.825 1.00201.43 C ATOM 243 OE1 GLU A 37 114.606 192.353 842.686 1.00201.43 O ATOM 244 OE2 GLU A 37 114.551 190.505 843.874 1.00201.43 O ATOM 245 N VAL A 38 110.111 193.635 842.506 1.00151.34 N ATOM 246 CA VAL A 38 109.321 194.800 842.122 1.00151.34 C ATOM 247 C VAL A 38 110.026 195.905 841.345 1.00151.34 C ATOM 248 O VAL A 38 111.219 196.156 841.522 1.00151.34 O ATOM 249 CB VAL A 38 108.626 195.423 843.348 1.00162.41 C ATOM 250 CG2 VAL A 38 107.892 194.336 844.128 1.00161.56 C ATOM 251 CG1 VAL A 38 107.641 196.504 842.896 1.00162.41 C ATOM 252 N GLU A 39 109.240 196.548 840.481 1.00183.94 N ATOM 253 CA GLU A 39 109.671 197.643 839.619 1.00183.94 C ATOM 254 C GLU A 39 108.478 198.227 838.874 1.00183.94 C ATOM 255 O GLU A 39 107.929 197.582 837.984 1.00183.94 O ATOM 256 CB GLU A 39 110.668 197.150 838.587 1.00154.55 C ATOM 257 CG GLU A 39 112.068 197.041 839.077 1.00154.55 C ATOM 258 CD GLU A 39 112.985 196.613 837.977 1.00154.55 C ATOM 259 OE2 GLU A 39 114.184 196.411 838.258 1.00154.55 O ATOM 260 OE1 GLU A 39 112.502 196.485 836.829 1.00154.55 O ATOM 261 N GLY A 40 108.086 199.444 839.232 1.00133.02 N ATOM 262 CA GLY A 40 106.963 200.089 838.571 1.00133.00 C ATOM 263 C GLY A 40 105.708 199.242 838.449 1.00133.36 C ATOM 264 O GLY A 40 105.050 198.944 839.449 1.00134.36 O ATOM 265 N GLU A 41 105.376 198.861 837.216 1.00201.57 N ATOM 266 CA GLU A 41 104.198 198.040 836.927 1.00201.57 C ATOM 267 C GLU A 41 104.571 196.553 836.803 1.00201.57 C ATOM 268 O GLU A 41 103.693 195.690 836.712 1.00201.57 O ATOM 269 CB GLU A 41 103.542 198.496 835.610 1.00201.57 C ATOM 270 CG GLU A 41 102.898 199.884 835.623 1.00201.57 C ATOM 271 CD GLU A 41 101.462 199.866 836.121 1.00201.57 C ATOM 272 OE2 GLU A 41 101.154 200.617 837.069 1.00201.57 O ATOM 273 OE1 GLU A 41 100.640 199.108 835.559 1.00201.57 O ATOM 274 N THR A 42 105.872 196.260 836.796 1.00201.57 N ATOM 275 CA THR A 42 106.346 194.884 836.657 1.00201.57 C ATOM 276 CB THR A 42 107.345 194.730 835.458 1.00170.75 C ATOM 277 CG2 THR A 42 106.608 194.754 834.119 1.00171.56 C ATOM 278 OG1 THR A 42 108.320 195.782 835.498 1.00167.10 O ATOM 279 C THR A 42 107.011 194.267 837.886 1.00201.57 C ATOM 280 O THR A 42 108.182 194.535 838.170 1.00201.57 O ATOM 281 N HIS A 43 106.257 193.445 838.614 1.00200.09 N ATOM 282 CA HIS A 43 106.803 192.746 839.771 1.00200.09 C ATOM 283 C HIS A 43 106.982 191.290 839.352 1.00200.09 C ATOM 284 O HIS A 43 106.094 190.458 839.535 1.00200.09 O ATOM 285 CB HIS A 43 105.903 192.827 841.024 1.00191.19 C ATOM 286 CG HIS A 43 104.585 193.508 840.817 1.00191.19 C ATOM 287 ND1 HIS A 43 103.881 193.786 839.693 1.00191.19 N ATOM 288 CE1 HIS A 43 102.711 194.388 840.089 1.00191.19 C ATOM 289 NE2 HIS A 43 102.699 194.477 841.405 1.00191.19 N ATOM 290 CD2 HIS A 43 103.818 193.954 841.870 1.00191.19 C ATOM 291 N LYS A 44 108.143 191.010 838.768 1.00186.48 N ATOM 292 CA LYS A 44 108.494 189.678 838.288 1.00186.48 C ATOM 293 CB LYS A 44 109.841 189.730 837.554 1.00193.82 C ATOM 294 CG LYS A 44 110.348 188.366 837.124 1.00192.06 C ATOM 295 CD LYS A 44 111.763 188.417 836.588 1.00188.31 C ATOM 296 CE LYS A 44 112.257 187.013 836.298 1.00187.64 C ATOM 297 NZ LYS A 44 113.618 187.018 835.718 1.00181.79 N ATOM 298 C LYS A 44 108.568 188.637 839.406 1.00186.48 C ATOM 299 O LYS A 44 109.212 188.854 840.435 1.00186.48 O ATOM 300 N LEU A 45 107.908 187.503 839.193 1.00197.92 N ATOM 301 CA LEU A 45 107.912 186.414 840.163 1.00197.92 C ATOM 302 CB LEU A 45 106.862 185.361 839.771 1.00148.84 C ATOM 303 CG LEU A 45 106.525 184.212 840.732 1.00153.21 C ATOM 304 CD2 LEU A 45 105.533 183.259 840.054 1.00150.51 C ATOM 305 CD1 LEU A 45 105.941 184.766 842.033 1.00155.67 C ATOM 306 C LEU A 45 109.314 185.806 840.132 1.00195.44 C ATOM 307 O LEU A 45 109.797 185.402 839.074 1.00197.92 O ATOM 308 N ILE A 46 109.979 185.765 841.282 1.00157.08 N ATOM 309 CA ILE A 46 111.319 185.192 841.343 1.00157.08 C ATOM 310 CB ILE A 46 112.374 186.246 841.840 1.00196.28 C ATOM 311 CG2 ILE A 46 113.425 185.591 842.745 1.00196.28 C ATOM 312 CG1 ILE A 46 113.013 186.931 840.620 1.00196.28 C ATOM 313 CD1 ILE A 46 114.437 187.445 840.838 1.00122.68 C ATOM 314 C ILE A 46 111.357 183.936 842.212 1.00157.08 C ATOM 315 O ILE A 46 112.242 183.095 842.056 1.00157.08 O ATOM 316 N ASP A 47 110.387 183.794 843.106 1.00183.84 N ATOM 317 CA ASP A 47 110.333 182.624 843.983 1.00183.84 C ATOM 318 CB ASP A 47 111.117 182.885 845.280 1.00194.21 C ATOM 319 CG ASP A 47 112.595 182.575 845.152 1.00194.21 C ATOM 320 OD1 ASP A 47 112.923 181.403 844.873 1.00194.21 O ATOM 321 OD2 ASP A 47 113.421 183.498 845.339 1.00194.21 O ATOM 322 C ASP A 47 108.915 182.210 844.360 1.00183.84 C ATOM 323 O ASP A 47 107.934 182.887 844.040 1.00183.84 O ATOM 324 N THR A 48 108.847 181.068 845.037 1.00152.48 N ATOM 325 CA THR A 48 107.625 180.471 845.573 1.00157.71 C ATOM 326 CB THR A 48 106.865 179.566 844.550 1.00111.40 C ATOM 327 CG2 THR A 48 105.649 178.916 845.222 1.00111.40 C ATOM 328 OG1 THR A 48 106.406 180.352 843.438 1.00111.40 O ATOM 329 C THR A 48 108.243 179.607 846.662 1.00162.66 C ATOM 330 O THR A 48 109.218 178.897 846.412 1.00160.61 O ATOM 331 N LEU A 49 107.705 179.677 847.870 1.00153.72 N ATOM 332 CA LEU A 49 108.274 178.916 848.973 1.00153.72 C ATOM 333 C LEU A 49 107.248 178.096 849.760 1.00153.72 C ATOM 334 O LEU A 49 106.520 178.640 850.595 1.00153.72 O ATOM 335 CB LEU A 49 108.997 179.878 849.921 1.00125.63 C ATOM 336 CG LEU A 49 109.980 180.898 849.336 1.00128.05 C ATOM 337 CD2 LEU A 49 111.049 180.216 848.493 1.00126.92 C ATOM 338 CD1 LEU A 49 110.614 181.662 850.488 1.00127.70 C ATOM 339 N THR A 50 107.211 176.785 849.501 1.00172.14 N ATOM 340 CA THR A 50 106.281 175.882 850.183 1.00172.14 C ATOM 341 C THR A 50 106.928 175.150 851.356 1.00172.14 C ATOM 342 O THR A 50 108.003 174.560 851.226 1.00172.14 O ATOM 343 CB THR A 50 105.690 174.826 849.221 1.00200.03 C ATOM 344 CG2 THR A 50 104.782 173.863 849.980 1.00200.03 C ATOM 345 OG1 THR A 50 104.926 175.480 848.198 1.00200.03 O ATOM 346 N GLY A 51 106.252 175.197 852.500 1.00138.56 N ATOM 347 CA GLY A 51 106.758 174.551 853.693 1.00141.31 C ATOM 348 C GLY A 51 105.842 174.796 854.876 1.00141.16 C ATOM 349 O GLY A 51 106.233 174.583 856.025 1.00136.86 O ATOM 350 N HIS A 52 104.620 175.247 854.600 1.00152.81 N ATOM 351 CA HIS A 52 103.647 175.514 855.656 1.00152.81 C ATOM 352 C HIS A 52 102.440 174.582 855.574 1.00152.81 C ATOM 353 O HIS A 52 101.964 174.265 854.484 1.00152.81 O ATOM 354 CB HIS A 52 103.185 176.976 855.598 1.00158.90 C ATOM 355 CG HIS A 52 104.078 177.922 856.338 1.00158.90 C ATOM 356 ND1 HIS A 52 104.353 177.786 857.684 1.00158.90 N ATOM 357 CE1 HIS A 52 105.159 178.763 858.069 1.00155.70 C ATOM 358 NE2 HIS A 52 105.414 179.524 857.023 1.00158.90 N ATOM 359 CD2 HIS A 52 104.752 179.023 855.927 1.00158.48 C ATOM 360 N GLU A 53 101.954 174.152 856.737 1.00175.84 N ATOM 361 CA GLU A 53 100.807 173.246 856.821 1.00175.84 C ATOM 362 CB GLU A 53 101.056 172.196 857.913 1.00201.57 C ATOM 363 CG GLU A 53 102.291 171.331 857.676 1.00201.57 C ATOM 364 CD GLU A 53 102.609 170.413 858.846 1.00201.57 C ATOM 365 OE2 GLU A 53 102.499 169.181 858.679 1.00201.57 O ATOM 366 OE1 GLU A 53 102.967 170.924 859.929 1.00201.57 O ATOM 367 C GLU A 53 99.504 173.995 857.108 1.00175.84 C ATOM 368 O GLU A 53 98.643 173.514 857.847 1.00175.84 O ATOM 369 N GLY A 54 99.372 175.174 856.507 1.00185.29 N ATOM 370 CA GLY A 54 98.187 175.995 856.687 1.00185.29 C ATOM 371 C GLY A 54 98.360 177.302 855.935 1.00185.29 C ATOM 372 O GLY A 54 99.454 177.576 855.440 1.00185.29 O ATOM 373 N PRO A 55 97.311 178.133 855.816 1.00129.28 N ATOM 374 CD PRO A 55 95.909 177.927 856.216 1.00126.26 C ATOM 375 CG PRO A 55 95.175 178.801 855.227 1.00128.67 C ATOM 376 CB PRO A 55 96.061 180.003 855.151 1.00135.51 C ATOM 377 CA PRO A 55 97.463 179.399 855.092 1.00128.96 C ATOM 378 C PRO A 55 98.510 180.292 855.762 1.00132.93 C ATOM 379 O PRO A 55 98.546 180.389 856.989 1.00138.88 O ATOM 380 N VAL A 56 99.364 180.930 854.967 1.00144.77 N ATOM 381 CA VAL A 56 100.397 181.799 855.523 1.00144.48 C ATOM 382 CB VAL A 56 101.567 182.016 854.523 1.00200.12 C ATOM 383 CG1 VAL A 56 102.751 182.656 855.238 1.00200.12 C ATOM 384 CG2 VAL A 56 101.985 180.688 853.906 1.00200.12 C ATOM 385 C VAL A 56 99.758 183.142 855.858 1.00144.77 C ATOM 386 O VAL A 56 99.375 183.898 854.963 1.00144.77 O ATOM 387 N TRP A 57 99.638 183.426 857.152 1.00182.80 N ATOM 388 CA TRP A 57 99.022 184.663 857.633 1.00182.80 C ATOM 389 CB TRP A 57 98.748 184.572 859.141 1.00175.69 C ATOM 390 CG TRP A 57 97.636 183.623 859.556 1.00175.69 C ATOM 391 CD1 TRP A 57 97.437 183.105 860.807 1.00175.69 C ATOM 392 NE1 TRP A 57 96.340 182.280 860.814 1.00174.99 N ATOM 393 CE2 TRP A 57 95.799 182.248 859.556 1.00175.69 C ATOM 394 CZ2 TRP A 57 94.686 181.555 859.074 1.00175.69 C ATOM 395 CH2 TRP A 57 94.369 181.710 857.749 1.00175.62 C ATOM 396 CZ3 TRP A 57 95.129 182.536 856.905 1.00175.69 C ATOM 397 CE3 TRP A 57 96.237 183.227 857.384 1.00175.69 C ATOM 398 CD2 TRP A 57 96.586 183.085 858.734 1.00175.69 C ATOM 399 C TRP A 57 99.831 185.925 857.365 1.00182.80 C ATOM 400 O TRP A 57 99.309 186.893 856.811 1.00182.80 O ATOM 401 N ARG A 58 101.099 185.917 857.768 1.00140.71 N ATOM 402 CA ARG A 58 101.955 187.080 857.581 1.00140.71 C ATOM 403 CB ARG A 58 101.901 187.969 858.828 1.00145.34 C ATOM 404 CG ARG A 58 100.535 188.527 859.161 1.00150.34 C ATOM 405 CD ARG A 58 100.671 189.681 860.137 1.00150.34 C ATOM 406 NE ARG A 58 99.381 190.240 860.529 1.00150.34 N ATOM 407 CZ ARG A 58 99.232 191.311 861.303 1.00149.13 C ATOM 408 NH1 ARG A 58 100.294 191.950 861.773 1.00146.48 N ATOM 409 NH2 ARG A 58 98.018 191.740 861.618 1.00150.34 N ATOM 410 C ARG A 58 103.421 186.767 857.273 1.00140.71 C ATOM 411 O ARG A 58 103.965 185.768 857.736 1.00140.71 O ATOM 412 N VAL A 59 104.045 187.637 856.480 1.00158.29 N ATOM 413 CA VAL A 59 105.460 187.528 856.126 1.00158.29 C ATOM 414 CB VAL A 59 105.671 187.399 854.595 1.00124.84 C ATOM 415 CG2 VAL A 59 104.761 188.361 853.869 1.00130.41 C ATOM 416 CG1 VAL A 59 105.401 185.961 854.146 1.00121.87 C ATOM 417 C VAL A 59 106.071 188.833 856.625 1.00158.29 C ATOM 418 O VAL A 59 105.340 189.783 856.895 1.00158.29 O ATOM 419 N ASP A 60 107.391 188.894 856.762 1.00185.99 N ATOM 420 CA ASP A 60 108.022 190.111 857.268 1.00185.99 C ATOM 421 CB ASP A 60 107.515 190.382 858.690 1.00129.58 C ATOM 422 CG ASP A 60 108.119 191.623 859.300 1.00129.52 C ATOM 423 OD2 ASP A 60 108.571 191.561 860.469 1.00123.88 O ATOM 424 OD1 ASP A 60 108.130 192.662 858.608 1.00121.05 O ATOM 425 C ASP A 60 109.543 190.001 857.272 1.00185.99 C ATOM 426 O ASP A 60 110.109 189.222 858.038 1.00185.99 O ATOM 427 N TRP A 61 110.205 190.783 856.426 1.00124.42 N ATOM 428 CA TRP A 61 111.664 190.740 856.361 1.00124.90 C ATOM 429 CB TRP A 61 112.174 191.525 855.160 1.00113.23 C ATOM 430 CG TRP A 61 111.451 191.238 853.910 1.00115.61 C ATOM 431 CD2 TRP A 61 112.003 190.690 852.715 1.00116.04 C ATOM 432 CE3 TRP A 61 113.274 190.218 852.359 1.00113.11 C ATOM 433 CZ3 TRP A 61 113.470 189.742 851.062 1.00112.34 C ATOM 434 CH2 TRP A 61 112.412 189.714 850.131 1.00113.47 C ATOM 435 CZ2 TRP A 61 111.160 190.168 850.455 1.00116.60 C ATOM 436 CE2 TRP A 61 110.966 190.645 851.756 1.00117.43 C ATOM 437 NE1 TRP A 61 109.840 191.154 852.351 1.00115.16 N ATOM 438 CD1 TRP A 61 110.142 191.502 853.645 1.00115.56 C ATOM 439 C TRP A 61 112.278 191.330 857.623 1.00126.15 C ATOM 440 O TRP A 61 111.583 191.948 858.426 1.00126.59 O ATOM 441 N ALA A 62 113.579 191.128 857.796 1.00128.06 N ATOM 442 CA ALA A 62 114.301 191.667 858.948 1.00123.15 C ATOM 443 CB ALA A 62 115.117 190.576 859.636 1.00111.43 C ATOM 444 C ALA A 62 115.221 192.755 858.417 1.00123.33 C ATOM 445 O ALA A 62 115.392 192.896 857.200 1.00113.25 O ATOM 446 N HIS A 63 115.808 193.529 859.316 1.00174.62 N ATOM 447 CA HIS A 63 116.694 194.591 858.883 1.00174.87 C ATOM 448 C HIS A 63 117.813 193.961 858.063 1.00174.87 C ATOM 449 O HIS A 63 118.446 193.017 858.527 1.00174.87 O ATOM 450 CB HIS A 63 117.188 195.400 860.085 1.00168.83 C ATOM 451 CG HIS A 63 117.939 196.698 859.697 1.00172.08 C ATOM 452 CD2 HIS A 63 119.264 196.974 859.630 1.00172.08 C ATOM 453 NE2 HIS A 63 119.384 198.282 859.232 1.00172.08 N ATOM 454 CE1 HIS A 63 118.178 198.792 859.060 1.00172.08 C ATOM 455 ND1 HIS A 63 117.286 197.856 859.334 1.00172.08 N ATOM 456 N PRO A 64 118.066 194.464 856.834 1.00116.66 N ATOM 457 CA PRO A 64 119.127 193.922 855.966 1.00118.07 C ATOM 458 C PRO A 64 120.493 193.805 856.657 1.00118.09 C ATOM 459 O PRO A 64 121.476 193.337 856.067 1.00116.33 O ATOM 460 CB PRO A 64 119.137 194.892 854.786 1.00133.00 C ATOM 461 CG PRO A 64 117.708 195.265 854.674 1.00130.87 C ATOM 462 CD PRO A 64 117.315 195.515 856.125 1.00131.68 C ATOM 463 N LYS A 65 120.534 194.236 857.916 1.00165.85 N ATOM 464 CA LYS A 65 121.729 194.174 858.752 1.00165.16 C ATOM 465 C LYS A 65 121.939 192.710 859.129 1.00166.26 C ATOM 466 O LYS A 65 122.925 192.351 859.773 1.00165.19 O ATOM 467 CB LYS A 65 121.511 195.014 860.018 1.00114.96 C ATOM 468 CG LYS A 65 122.626 194.955 861.053 1.00112.57 C ATOM 469 CD LYS A 65 122.249 195.758 862.302 1.00113.38 C ATOM 470 CE LYS A 65 123.358 195.725 863.353 1.00113.97 C ATOM 471 NZ LYS A 65 123.012 196.487 864.592 1.00116.19 N ATOM 472 N PHE A 66 120.991 191.872 858.717 1.00138.02 N ATOM 473 CA PHE A 66 121.026 190.442 858.994 1.00142.15 C ATOM 474 C PHE A 66 120.786 189.666 857.692 1.00141.31 C ATOM 475 O PHE A 66 119.906 188.805 857.611 1.00142.68 O ATOM 476 CB PHE A 66 119.951 190.095 860.032 1.00116.34 C ATOM 477 CG PHE A 66 119.921 191.037 861.220 1.00117.32 C ATOM 478 CD2 PHE A 66 121.033 191.169 862.054 1.00117.30 C ATOM 479 CE2 PHE A 66 121.009 192.030 863.149 1.00113.77 C ATOM 480 CZ PHE A 66 119.866 192.772 863.419 1.00115.48 C ATOM 481 CE1 PHE A 66 118.747 192.652 862.596 1.00117.68 C ATOM 482 CD1 PHE A 66 118.778 191.789 861.503 1.00116.20 C ATOM 483 N GLY A 67 121.579 189.988 856.672 1.00153.63 N ATOM 484 CA GLY A 67 121.444 189.325 855.388 1.00152.89 C ATOM 485 C GLY A 67 120.080 189.547 854.774 1.00153.11 C ATOM 486 O GLY A 67 119.621 190.681 854.660 1.00154.53 O ATOM 487 N THR A 68 119.436 188.461 854.368 1.00139.87 N ATOM 488 CA THR A 68 118.109 188.525 853.769 1.00138.96 C ATOM 489 CB THR A 68 118.132 188.137 852.257 1.00120.15 C ATOM 490 CG2 THR A 68 116.730 188.194 851.667 1.00123.57 C ATOM 491 OG1 THR A 68 118.975 189.042 851.526 1.00112.98 O ATOM 492 C THR A 68 117.236 187.530 854.516 1.00138.08 C ATOM 493 O THR A 68 116.983 186.436 854.030 1.00139.99 O ATOM 494 N ILE A 69 116.776 187.908 855.700 1.00182.09 N ATOM 495 CA ILE A 69 115.947 187.027 856.514 1.00181.12 C ATOM 496 C ILE A 69 114.469 187.423 856.507 1.00182.09 C ATOM 497 O ILE A 69 114.133 188.599 856.620 1.00181.64 O ATOM 498 CB ILE A 69 116.492 186.996 857.955 1.00 92.47 C ATOM 499 CG1 ILE A 69 117.921 186.443 857.920 1.00 92.48 C ATOM 500 CD1 ILE A 69 118.640 186.478 859.249 1.00126.14 C ATOM 501 CG2 ILE A 69 115.579 186.177 858.861 1.00 88.13 C ATOM 502 N LEU A 70 113.596 186.429 856.371 1.00187.10 N ATOM 503 CA LEU A 70 112.150 186.652 856.324 1.00187.10 C ATOM 504 CB LEU A 70 111.678 186.499 854.859 1.00126.41 C ATOM 505 CG LEU A 70 110.265 186.047 854.450 1.00127.13 C ATOM 506 CD2 LEU A 70 110.098 186.180 852.919 1.00125.00 C ATOM 507 CD1 LEU A 70 109.210 186.855 855.189 1.00124.23 C ATOM 508 C LEU A 70 111.398 185.687 857.253 1.00187.10 C ATOM 509 O LEU A 70 111.230 184.525 856.917 1.00187.10 O ATOM 510 N ALA A 71 110.953 186.163 858.415 1.00187.85 N ATOM 511 CA ALA A 71 110.225 185.305 859.366 1.00187.85 C ATOM 512 CB ALA A 71 110.525 185.735 860.831 1.00 45.03 C ATOM 513 C ALA A 71 108.711 185.307 859.127 1.00187.85 C ATOM 514 O ALA A 71 108.046 186.313 859.366 1.00187.85 O ATOM 515 N SER A 72 108.163 184.177 858.672 1.00135.16 N ATOM 516 CA SER A 72 106.723 184.077 858.414 1.00135.16 C ATOM 517 C SER A 72 105.980 183.191 859.416 1.00135.16 C ATOM 518 O SER A 72 106.526 182.221 859.944 1.00135.16 O ATOM 519 CB SER A 72 106.448 183.561 856.988 1.00103.32 C ATOM 520 OG SER A 72 106.560 182.151 856.899 1.00105.80 O ATOM 521 N CYS A 73 104.722 183.554 859.664 1.00164.60 N ATOM 522 CA CYS A 73 103.838 182.838 860.578 1.00164.60 C ATOM 523 CB CYS A 73 103.324 183.785 861.671 1.00169.52 C ATOM 524 SG CYS A 73 102.353 185.209 861.070 1.00169.52 S ATOM 525 C CYS A 73 102.660 182.292 859.773 1.00164.60 C ATOM 526 O CYS A 73 102.022 183.022 859.011 1.00164.22 O ATOM 527 N SER A 74 102.373 181.008 859.938 1.00160.76 N ATOM 528 CA SER A 74 101.276 180.403 859.204 1.00160.76 C ATOM 529 CB SER A 74 101.812 179.337 858.246 1.00201.57 C ATOM 530 OG SER A 74 100.783 178.831 857.412 1.00201.57 O ATOM 531 C SER A 74 100.236 179.792 860.130 1.00160.76 C ATOM 532 O SER A 74 100.325 179.909 861.356 1.00160.76 O ATOM 533 N TYR A 75 99.248 179.138 859.528 1.00122.31 N ATOM 534 CA TYR A 75 98.177 178.506 860.277 1.00122.31 C ATOM 535 CB TYR A 75 97.005 178.213 859.338 1.00167.03 C ATOM 536 CG TYR A 75 95.875 177.491 860.014 1.00167.03 C ATOM 537 CD2 TYR A 75 95.409 176.272 859.526 1.00162.49 C ATOM 538 CE2 TYR A 75 94.393 175.581 860.179 1.00157.89 C ATOM 539 CZ TYR A 75 93.835 176.115 861.338 1.00157.13 C ATOM 540 OH TYR A 75 92.840 175.443 862.007 1.00167.03 O ATOM 541 CE1 TYR A 75 94.280 177.325 861.838 1.00159.84 C ATOM 542 CD1 TYR A 75 95.294 178.004 861.174 1.00167.03 C ATOM 543 C TYR A 75 98.619 177.221 860.991 1.00122.31 C ATOM 544 O TYR A 75 98.001 176.807 861.974 1.00122.31 O ATOM 545 N ASP A 76 99.698 176.603 860.510 1.00170.49 N ATOM 546 CA ASP A 76 100.197 175.367 861.109 1.00170.49 C ATOM 547 CB ASP A 76 101.148 174.643 860.132 1.00184.50 C ATOM 548 CG ASP A 76 102.446 175.407 859.866 1.00184.50 C ATOM 549 OD2 ASP A 76 103.534 174.806 860.011 1.00184.50 O ATOM 550 OD1 ASP A 76 102.380 176.597 859.496 1.00184.50 O ATOM 551 C ASP A 76 100.873 175.557 862.475 1.00170.49 C ATOM 552 O ASP A 76 101.773 174.803 862.839 1.00170.49 O ATOM 553 N GLY A 77 100.423 176.557 863.231 1.00138.38 N ATOM 554 CA GLY A 77 100.987 176.818 864.547 1.00140.14 C ATOM 555 C GLY A 77 102.493 177.007 864.594 1.00140.37 C ATOM 556 O GLY A 77 103.066 177.221 865.670 1.00138.36 O ATOM 557 N LYS A 78 103.129 176.942 863.424 1.00157.82 N ATOM 558 CA LYS A 78 104.578 177.084 863.302 1.00157.82 C ATOM 559 CB LYS A 78 105.173 175.892 862.536 1.00155.29 C ATOM 560 CG LYS A 78 104.923 174.521 863.137 1.00164.92 C ATOM 561 CD LYS A 78 105.433 173.440 862.193 1.00174.05 C ATOM 562 CE LYS A 78 105.072 172.051 862.686 1.00177.96 C ATOM 563 NZ LYS A 78 105.451 171.004 861.700 1.00179.86 N ATOM 564 C LYS A 78 105.031 178.363 862.599 1.00157.82 C ATOM 565 O LYS A 78 104.420 178.808 861.624 1.00157.82 O ATOM 566 N VAL A 79 106.123 178.934 863.104 1.00200.75 N ATOM 567 CA VAL A 79 106.724 180.136 862.535 1.00200.75 C ATOM 568 CB VAL A 79 107.088 181.171 863.632 1.00154.80 C ATOM 569 CG2 VAL A 79 105.839 181.567 864.410 1.00151.52 C ATOM 570 CG1 VAL A 79 107.731 182.399 863.002 1.00156.07 C ATOM 571 C VAL A 79 108.003 179.677 861.838 1.00200.75 C ATOM 572 O VAL A 79 108.894 179.113 862.471 1.00200.75 O ATOM 573 N LEU A 80 108.085 179.910 860.535 1.00133.66 N ATOM 574 CA LEU A 80 109.249 179.498 859.759 1.00133.66 C ATOM 575 C LEU A 80 110.137 180.645 859.282 1.00133.66 C ATOM 576 O LEU A 80 109.701 181.486 858.507 1.00133.66 O ATOM 577 CB LEU A 80 108.801 178.681 858.542 1.00166.41 C ATOM 578 CG LEU A 80 108.681 177.167 858.713 1.00166.41 C ATOM 579 CD1 LEU A 80 107.765 176.602 857.646 1.00166.41 C ATOM 580 CD2 LEU A 80 110.068 176.538 858.636 1.00166.41 C ATOM 581 N ILE A 81 111.379 180.669 859.755 1.00115.73 N ATOM 582 CA ILE A 81 112.359 181.678 859.350 1.00121.35 C ATOM 583 C ILE A 81 112.959 181.189 858.023 1.00121.65 C ATOM 584 O ILE A 81 113.268 180.006 857.882 1.00122.59 O ATOM 585 CB ILE A 81 113.509 181.813 860.407 1.00 84.03 C ATOM 586 CG1 ILE A 81 113.037 182.617 861.629 1.00 87.10 C ATOM 587 CD1 ILE A 81 111.837 182.038 862.346 1.00121.98 C ATOM 588 CG2 ILE A 81 114.739 182.453 859.759 1.00 84.34 C ATOM 589 N TRP A 82 113.111 182.077 857.049 1.00122.30 N ATOM 590 CA TRP A 82 113.681 181.687 855.758 1.00124.84 C ATOM 591 CB TRP A 82 112.665 181.901 854.625 1.00153.98 C ATOM 592 CG TRP A 82 111.337 181.192 854.841 1.00153.98 C ATOM 593 CD1 TRP A 82 110.455 181.400 855.864 1.00153.98 C ATOM 594 NE1 TRP A 82 109.357 180.584 855.725 1.00153.98 N ATOM 595 CE2 TRP A 82 109.511 179.828 854.595 1.00153.98 C ATOM 596 CZ2 TRP A 82 108.670 178.859 854.040 1.00153.98 C ATOM 597 CH2 TRP A 82 109.087 178.248 852.887 1.00153.73 C ATOM 598 CZ3 TRP A 82 110.317 178.578 852.283 1.00153.16 C ATOM 599 CE3 TRP A 82 111.152 179.540 852.834 1.00153.98 C ATOM 600 CD2 TRP A 82 110.753 180.182 854.010 1.00153.98 C ATOM 601 C TRP A 82 114.944 182.503 855.503 1.00128.22 C ATOM 602 O TRP A 82 115.408 183.212 856.395 1.00127.56 O ATOM 603 N LYS A 83 115.512 182.388 854.305 1.00195.52 N ATOM 604 CA LYS A 83 116.725 183.130 853.965 1.00195.52 C ATOM 605 C LYS A 83 117.254 182.822 852.578 1.00195.52 C ATOM 606 O LYS A 83 117.445 181.660 852.222 1.00195.52 O ATOM 607 CB LYS A 83 117.843 182.855 854.973 1.00126.05 C ATOM 608 CG LYS A 83 119.189 183.430 854.552 1.00126.05 C ATOM 609 CD LYS A 83 120.092 183.592 855.755 1.00126.05 C ATOM 610 CE LYS A 83 121.386 184.299 855.399 1.00126.05 C ATOM 611 NZ LYS A 83 122.155 184.626 856.634 1.00126.05 N ATOM 612 N GLU A 84 117.505 183.869 851.803 1.00166.97 N ATOM 613 CA GLU A 84 118.032 183.686 850.463 1.00166.97 C ATOM 614 CB GLU A 84 117.748 184.912 849.591 1.00201.57 C ATOM 615 CG GLU A 84 118.060 184.682 848.119 1.00201.57 C ATOM 616 CD GLU A 84 117.529 185.786 847.231 1.00201.57 C ATOM 617 OE2 GLU A 84 116.646 185.500 846.388 1.00201.57 O ATOM 618 OE1 GLU A 84 117.992 186.936 847.381 1.00201.57 O ATOM 619 C GLU A 84 119.529 183.463 850.583 1.00166.97 C ATOM 620 O GLU A 84 120.229 184.239 851.238 1.00166.97 O ATOM 621 N GLU A 85 120.008 182.383 849.968 1.00190.03 N ATOM 622 CA GLU A 85 121.421 182.042 850.006 1.00190.03 C ATOM 623 C GLU A 85 121.972 181.801 848.610 1.00190.03 C ATOM 624 O GLU A 85 121.670 180.791 847.974 1.00190.03 O ATOM 625 CB GLU A 85 121.647 180.792 850.860 1.00154.12 C ATOM 626 CG GLU A 85 123.021 180.744 851.506 1.00154.82 C ATOM 627 CD GLU A 85 123.154 181.729 852.657 1.00154.82 C ATOM 628 OE1 GLU A 85 122.865 182.925 852.456 1.00154.82 O ATOM 629 OE2 GLU A 85 123.550 181.311 853.766 1.00154.82 O ATOM 630 N ASN A 86 122.772 182.751 848.138 1.00180.96 N ATOM 631 CA ASN A 86 123.406 182.665 846.832 1.00181.02 C ATOM 632 C ASN A 86 122.425 182.492 845.676 1.00179.01 C ATOM 633 O ASN A 86 122.725 181.811 844.692 1.00178.72 O ATOM 634 CB ASN A 86 124.410 181.514 846.835 1.00197.41 C ATOM 635 CG ASN A 86 125.236 181.476 848.104 1.00197.41 C ATOM 636 OD1 ASN A 86 125.839 182.473 848.496 1.00197.41 O ATOM 637 ND2 ASN A 86 125.268 180.317 848.753 1.00197.41 N ATOM 638 N GLY A 87 121.254 183.108 845.796 1.00184.34 N ATOM 639 CA GLY A 87 120.263 183.019 844.740 1.00184.15 C ATOM 640 C GLY A 87 119.140 182.027 844.984 1.00181.98 C ATOM 641 O GLY A 87 118.173 181.983 844.219 1.00179.71 O ATOM 642 N ARG A 88 119.261 181.234 846.042 1.00200.20 N ATOM 643 CA ARG A 88 118.240 180.242 846.359 1.00200.20 C ATOM 644 CB ARG A 88 118.683 178.873 845.846 1.00190.82 C ATOM 645 CG ARG A 88 118.791 178.822 844.334 1.00190.82 C ATOM 646 CD ARG A 88 119.457 177.550 843.851 1.00190.82 C ATOM 647 NE ARG A 88 119.638 177.572 842.401 1.00190.82 N ATOM 648 CZ ARG A 88 120.311 176.656 841.714 1.00190.82 C ATOM 649 NH1 ARG A 88 120.875 175.635 842.343 1.00190.82 N ATOM 650 NH2 ARG A 88 120.426 176.765 840.396 1.00190.82 N ATOM 651 C ARG A 88 117.901 180.173 847.846 1.00200.20 C ATOM 652 O ARG A 88 118.786 180.020 848.699 1.00200.20 O ATOM 653 N TRP A 89 116.604 180.282 848.138 1.00164.31 N ATOM 654 CA TRP A 89 116.091 180.260 849.507 1.00156.49 C ATOM 655 C TRP A 89 116.230 178.918 850.207 1.00152.16 C ATOM 656 O TRP A 89 116.380 177.878 849.565 1.00151.44 O ATOM 657 CB TRP A 89 114.623 180.711 849.539 1.00170.47 C ATOM 658 CG TRP A 89 114.442 182.201 849.349 1.00170.47 C ATOM 659 CD1 TRP A 89 114.524 182.901 848.172 1.00170.47 C ATOM 660 NE1 TRP A 89 114.340 184.244 848.406 1.00170.47 N ATOM 661 CE2 TRP A 89 114.133 184.440 849.750 1.00170.47 C ATOM 662 CZ2 TRP A 89 113.900 185.621 850.465 1.00170.47 C ATOM 663 CH2 TRP A 89 113.723 185.517 851.825 1.00170.47 C ATOM 664 CZ3 TRP A 89 113.773 184.270 852.477 1.00170.47 C ATOM 665 CE3 TRP A 89 114.006 183.095 851.765 1.00170.47 C ATOM 666 CD2 TRP A 89 114.189 183.171 850.376 1.00170.47 C ATOM 667 N SER A 90 116.157 178.955 851.533 1.00110.06 N ATOM 668 CA SER A 90 116.308 177.759 852.350 1.00108.91 C ATOM 669 CB SER A 90 117.792 177.370 852.386 1.00115.42 C ATOM 670 OG SER A 90 118.618 178.488 852.705 1.00114.13 O ATOM 671 C SER A 90 115.800 177.969 853.776 1.00111.54 C ATOM 672 O SER A 90 116.339 178.798 854.506 1.00114.38 O ATOM 673 N GLN A 91 114.772 177.227 854.179 1.00151.60 N ATOM 674 CA GLN A 91 114.246 177.352 855.539 1.00147.85 C ATOM 675 C GLN A 91 115.393 177.101 856.516 1.00146.39 C ATOM 676 O GLN A 91 115.761 175.958 856.761 1.00147.30 O ATOM 677 CB GLN A 91 113.130 176.335 855.765 1.00152.90 C ATOM 678 CG GLN A 91 111.927 176.567 854.875 1.00158.06 C ATOM 679 CD GLN A 91 110.865 175.503 855.040 1.00163.18 C ATOM 680 OE1 GLN A 91 110.602 175.049 856.153 1.00163.15 O ATOM 681 NE2 GLN A 91 110.237 175.107 853.932 1.00160.96 N ATOM 682 N ILE A 92 115.948 178.176 857.070 1.00138.55 N ATOM 683 CA ILE A 92 117.089 178.091 857.980 1.00136.37 C ATOM 684 C ILE A 92 116.832 177.667 859.425 1.00133.15 C ATOM 685 O ILE A 92 117.718 177.116 860.077 1.00134.45 O ATOM 686 CB ILE A 92 117.887 179.424 857.963 1.00201.57 C ATOM 687 CG1 ILE A 92 118.855 179.410 856.773 1.00201.57 C ATOM 688 CD1 ILE A 92 119.798 180.590 856.715 1.00199.31 C ATOM 689 CG2 ILE A 92 118.618 179.638 859.287 1.00201.57 C ATOM 690 N ALA A 93 115.641 177.921 859.936 1.00119.03 N ATOM 691 CA ALA A 93 115.333 177.519 861.303 1.00117.78 C ATOM 692 C ALA A 93 113.823 177.558 861.474 1.00121.15 C ATOM 693 O ALA A 93 113.108 177.919 860.539 1.00122.39 O ATOM 694 CB ALA A 93 116.021 178.451 862.308 1.00 98.40 C ATOM 695 N VAL A 94 113.334 177.158 862.645 1.00158.22 N ATOM 696 CA VAL A 94 111.899 177.181 862.908 1.00159.58 C ATOM 697 C VAL A 94 111.626 177.281 864.407 1.00160.52 C ATOM 698 O VAL A 94 112.441 176.859 865.237 1.00155.86 O ATOM 699 CB VAL A 94 111.173 175.933 862.299 1.00142.94 C ATOM 700 CG1 VAL A 94 111.508 174.672 863.092 1.00145.03 C ATOM 701 CG2 VAL A 94 109.660 176.181 862.244 1.00139.72 C ATOM 702 N HIS A 95 110.482 177.869 864.739 1.00201.57 N ATOM 703 CA HIS A 95 110.078 178.062 866.125 1.00201.57 C ATOM 704 C HIS A 95 108.552 178.136 866.246 1.00201.57 C ATOM 705 O HIS A 95 107.930 179.127 865.845 1.00201.57 O ATOM 706 CB HIS A 95 110.696 179.347 866.669 1.00185.33 C ATOM 707 CG HIS A 95 110.310 179.644 868.082 1.00185.33 C ATOM 708 ND1 HIS A 95 109.365 180.470 868.592 1.00185.33 N ATOM 709 CE1 HIS A 95 109.410 180.340 869.957 1.00185.33 C ATOM 710 NE2 HIS A 95 110.346 179.464 870.276 1.00185.33 N ATOM 711 CD2 HIS A 95 110.907 179.027 869.161 1.00185.33 C ATOM 712 N ALA A 96 107.962 177.084 866.815 1.00201.57 N ATOM 713 CA ALA A 96 106.514 176.991 866.991 1.00201.57 C ATOM 714 C ALA A 96 106.105 176.483 868.376 1.00201.57 C ATOM 715 O ALA A 96 105.202 175.651 868.484 1.00201.57 O ATOM 716 CB ALA A 96 105.925 176.081 865.925 1.00201.57 C ATOM 717 N VAL A 97 106.763 176.975 869.426 1.00149.47 N ATOM 718 CA VAL A 97 106.439 176.565 870.793 1.00149.47 C ATOM 719 C VAL A 97 105.058 177.112 871.191 1.00149.47 C ATOM 720 O VAL A 97 104.815 177.462 872.354 1.00149.47 O ATOM 721 CB VAL A 97 107.520 177.057 871.813 1.00177.68 C ATOM 722 CG1 VAL A 97 108.898 176.534 871.406 1.00177.68 C ATOM 723 CG2 VAL A 97 107.520 178.582 871.904 1.00177.68 C ATOM 724 N HIS A 98 104.163 177.178 870.204 1.00201.57 N ATOM 725 CA HIS A 98 102.799 177.666 870.389 1.00201.57 C ATOM 726 CB HIS A 98 102.582 178.957 869.583 1.00195.59 C ATOM 727 CG HIS A 98 103.454 180.097 870.015 1.00195.59 C ATOM 728 ND1 HIS A 98 103.562 180.497 871.333 1.00195.59 N ATOM 729 CE1 HIS A 98 104.396 181.517 871.417 1.00195.59 C ATOM 730 NE2 HIS A 98 104.836 181.795 870.201 1.00195.59 N ATOM 731 CD2 HIS A 98 104.263 180.923 869.308 1.00195.59 C ATOM 732 C HIS A 98 101.784 176.594 869.967 1.00201.57 C ATOM 733 O HIS A 98 101.901 175.998 868.890 1.00201.57 O ATOM 734 N SER A 99 100.791 176.372 870.824 1.00172.53 N ATOM 735 CA SER A 99 99.754 175.362 870.613 1.00172.53 C ATOM 736 C SER A 99 98.557 175.744 869.740 1.00172.53 C ATOM 737 O SER A 99 97.439 175.278 869.974 1.00172.53 O ATOM 738 CB SER A 99 99.248 174.878 871.975 1.00105.04 C ATOM 739 OG SER A 99 98.916 175.965 872.818 1.00105.79 O ATOM 740 N ALA A 100 98.783 176.573 868.728 1.00183.98 N ATOM 741 CA ALA A 100 97.697 176.985 867.848 1.00183.98 C ATOM 742 C ALA A 100 98.214 177.777 866.658 1.00183.98 C ATOM 743 O ALA A 100 99.421 177.874 866.442 1.00183.98 O ATOM 744 CB ALA A 100 96.687 177.819 868.621 1.00103.66 C ATOM 745 N SER A 101 97.285 178.345 865.896 1.00147.09 N ATOM 746 CA SER A 101 97.618 179.130 864.716 1.00147.09 C ATOM 747 CB SER A 101 96.337 179.471 863.953 1.00181.85 C ATOM 748 OG SER A 101 96.625 180.233 862.795 1.00181.85 O ATOM 749 C SER A 101 98.362 180.418 865.070 1.00147.09 C ATOM 750 O SER A 101 97.877 181.221 865.871 1.00147.09 O ATOM 751 N VAL A 102 99.538 180.607 864.470 1.00178.72 N ATOM 752 CA VAL A 102 100.353 181.802 864.705 1.00178.72 C ATOM 753 CB VAL A 102 101.844 181.545 864.353 1.00110.40 C ATOM 754 CG1 VAL A 102 102.661 182.801 864.586 1.00110.40 C ATOM 755 CG2 VAL A 102 102.394 180.407 865.203 1.00110.40 C ATOM 756 C VAL A 102 99.811 182.954 863.851 1.00178.72 C ATOM 757 O VAL A 102 99.635 182.809 862.641 1.00178.72 O ATOM 758 N ASN A 103 99.557 184.095 864.491 1.00182.30 N ATOM 759 CA ASN A 103 98.992 185.268 863.821 1.00182.30 C ATOM 760 C ASN A 103 99.974 186.324 863.273 1.00182.30 C ATOM 761 O ASN A 103 100.046 186.539 862.059 1.00182.30 O ATOM 762 CB ASN A 103 97.987 185.945 864.764 1.00168.77 C ATOM 763 CG ASN A 103 96.817 185.036 865.128 1.00168.77 C ATOM 764 ND2 ASN A 103 96.768 184.602 866.384 1.00168.77 N ATOM 765 OD1 ASN A 103 95.973 184.728 864.285 1.00168.77 O ATOM 766 N SER A 104 100.713 186.989 864.159 1.00141.83 N ATOM 767 CA SER A 104 101.665 188.018 863.734 1.00141.83 C ATOM 768 C SER A 104 103.119 187.594 863.921 1.00141.83 C ATOM 769 O SER A 104 103.418 186.617 864.606 1.00141.83 O ATOM 770 CB SER A 104 101.428 189.318 864.507 1.00162.84 C ATOM 771 OG SER A 104 101.903 189.217 865.839 1.00162.84 O ATOM 772 N VAL A 105 104.016 188.350 863.304 1.00160.36 N ATOM 773 CA VAL A 105 105.448 188.096 863.380 1.00164.02 C ATOM 774 C VAL A 105 106.139 189.364 862.882 1.00166.67 C ATOM 775 O VAL A 105 106.214 189.624 861.682 1.00160.29 O ATOM 776 CB VAL A 105 105.848 186.875 862.502 1.00101.06 C ATOM 777 CG1 VAL A 105 105.466 187.123 861.045 1.00 94.95 C ATOM 778 CG2 VAL A 105 107.344 186.591 862.642 1.00107.24 C ATOM 779 N GLN A 106 106.635 190.163 863.815 1.00161.89 N ATOM 780 CA GLN A 106 107.277 191.417 863.449 1.00161.89 C ATOM 781 C GLN A 106 108.621 191.565 864.145 1.00161.89 C ATOM 782 O GLN A 106 108.697 191.529 865.374 1.00161.19 O ATOM 783 CB GLN A 106 106.353 192.569 863.837 1.00142.48 C ATOM 784 CG GLN A 106 106.667 193.903 863.204 1.00142.48 C ATOM 785 CD GLN A 106 105.768 194.996 863.738 1.00142.48 C ATOM 786 OE1 GLN A 106 105.864 195.376 864.910 1.00142.48 O ATOM 787 NE2 GLN A 106 104.875 195.499 862.890 1.00142.48 N ATOM 788 N TRP A 107 109.683 191.741 863.361 1.00142.90 N ATOM 789 CA TRP A 107 111.014 191.891 863.931 1.00144.39 C ATOM 790 CB TRP A 107 112.051 192.033 862.820 1.00139.65 C ATOM 791 CG TRP A 107 112.072 190.866 861.903 1.00142.28 C ATOM 792 CD1 TRP A 107 111.317 190.691 860.789 1.00142.85 C ATOM 793 NE1 TRP A 107 111.597 189.475 860.213 1.00141.82 N ATOM 794 CE2 TRP A 107 112.550 188.838 860.960 1.00137.65 C ATOM 795 CZ2 TRP A 107 113.154 187.586 860.783 1.00136.83 C ATOM 796 CH2 TRP A 107 114.090 187.197 861.707 1.00140.04 C ATOM 797 CZ3 TRP A 107 114.435 188.022 862.796 1.00133.89 C ATOM 798 CE3 TRP A 107 113.836 189.268 862.970 1.00134.36 C ATOM 799 CD2 TRP A 107 112.875 189.689 862.040 1.00135.51 C ATOM 800 C TRP A 107 111.085 193.096 864.852 1.00144.08 C ATOM 801 O TRP A 107 110.101 193.805 865.032 1.00134.80 O ATOM 802 N ALA A 108 112.255 193.323 865.438 1.00160.53 N ATOM 803 CA ALA A 108 112.447 194.448 866.345 1.00160.53 C ATOM 804 CB ALA A 108 113.030 193.949 867.682 1.00167.78 C ATOM 805 C ALA A 108 113.382 195.481 865.716 1.00160.53 C ATOM 806 O ALA A 108 113.919 195.272 864.624 1.00160.53 O ATOM 807 N PRO A 109 113.555 196.636 866.378 1.00152.39 N ATOM 808 CD PRO A 109 112.749 197.215 867.467 1.00179.21 C ATOM 809 CG PRO A 109 112.871 198.695 867.201 1.00179.21 C ATOM 810 CB PRO A 109 114.296 198.814 866.772 1.00179.21 C ATOM 811 CA PRO A 109 114.457 197.638 865.813 1.00152.95 C ATOM 812 C PRO A 109 115.854 197.017 865.881 1.00156.98 C ATOM 813 O PRO A 109 116.263 196.543 866.941 1.00156.98 O ATOM 814 N HIS A 110 116.572 197.019 864.762 1.00135.45 N ATOM 815 CA HIS A 110 117.905 196.419 864.691 1.00139.34 C ATOM 816 CB HIS A 110 118.535 196.716 863.331 1.00142.77 C ATOM 817 CG HIS A 110 118.774 198.169 863.092 1.00145.43 C ATOM 818 ND1 HIS A 110 117.747 199.077 862.970 1.00146.11 N ATOM 819 CE1 HIS A 110 118.252 200.286 862.794 1.00146.87 C ATOM 820 NE2 HIS A 110 119.569 200.191 862.799 1.00149.19 N ATOM 821 CD2 HIS A 110 119.923 198.875 862.983 1.00146.92 C ATOM 822 C HIS A 110 118.913 196.774 865.799 1.00139.70 C ATOM 823 O HIS A 110 120.043 196.280 865.776 1.00143.01 O ATOM 824 N GLU A 111 118.526 197.617 866.754 1.00124.97 N ATOM 825 CA GLU A 111 119.427 197.986 867.853 1.00125.11 C ATOM 826 C GLU A 111 119.247 197.010 869.011 1.00126.77 C ATOM 827 O GLU A 111 119.949 197.080 870.023 1.00126.77 O ATOM 828 CB GLU A 111 119.139 199.407 868.348 1.00188.51 C ATOM 829 CG GLU A 111 119.367 200.509 867.321 1.00188.51 C ATOM 830 CD GLU A 111 118.243 200.618 866.300 1.00188.51 C ATOM 831 OE1 GLU A 111 118.312 201.517 865.434 1.00188.51 O ATOM 832 OE2 GLU A 111 117.291 199.813 866.366 1.00188.51 O ATOM 833 N TYR A 112 118.288 196.104 868.841 1.00192.41 N ATOM 834 CA TYR A 112 117.956 195.079 869.826 1.00194.39 C ATOM 835 C TYR A 112 118.619 193.755 869.440 1.00194.74 C ATOM 836 O TYR A 112 118.584 192.777 870.189 1.00194.19 O ATOM 837 CB TYR A 112 116.436 194.877 869.862 1.00152.31 C ATOM 838 CG TYR A 112 115.625 196.073 870.325 1.00157.94 C ATOM 839 CD1 TYR A 112 114.232 196.050 870.263 1.00158.94 C ATOM 840 CE1 TYR A 112 113.467 197.114 870.741 1.00161.57 C ATOM 841 CZ TYR A 112 114.092 198.217 871.287 1.00161.61 C ATOM 842 OH TYR A 112 113.328 199.248 871.789 1.00163.80 O ATOM 843 CE2 TYR A 112 115.477 198.270 871.355 1.00164.38 C ATOM 844 CD2 TYR A 112 116.236 197.200 870.873 1.00160.26 C ATOM 845 N GLY A 113 119.228 193.742 868.260 1.00132.07 N ATOM 846 CA GLY A 113 119.863 192.541 867.761 1.00132.86 C ATOM 847 C GLY A 113 118.979 192.019 866.644 1.00135.20 C ATOM 848 O GLY A 113 118.558 192.796 865.789 1.00132.29 O ATOM 849 N PRO A 114 118.687 190.710 866.608 1.00198.49 N ATOM 850 CA PRO A 114 117.831 190.172 865.548 1.00198.49 C ATOM 851 C PRO A 114 116.496 189.623 866.082 1.00198.49 C ATOM 852 O PRO A 114 115.849 188.800 865.425 1.00196.60 O ATOM 853 CB PRO A 114 118.703 189.083 864.953 1.00184.13 C ATOM 854 CG PRO A 114 119.295 188.469 866.199 1.00184.13 C ATOM 855 CD PRO A 114 119.580 189.658 867.131 1.00184.13 C ATOM 856 N LEU A 115 116.092 190.085 867.266 1.00158.03 N ATOM 857 CA LEU A 115 114.853 189.634 867.900 1.00150.64 C ATOM 858 C LEU A 115 113.679 189.530 866.932 1.00151.42 C ATOM 859 O LEU A 115 113.699 190.091 865.838 1.00152.99 O ATOM 860 CB LEU A 115 114.470 190.559 869.063 1.00151.81 C ATOM 861 CG LEU A 115 115.514 190.796 870.161 1.00150.69 C ATOM 862 CD1 LEU A 115 114.859 191.499 871.344 1.00150.32 C ATOM 863 CD2 LEU A 115 116.108 189.478 870.609 1.00149.38 C ATOM 864 N LEU A 116 112.656 188.796 867.352 1.00201.57 N ATOM 865 CA LEU A 116 111.457 188.596 866.550 1.00201.57 C ATOM 866 C LEU A 116 110.284 188.660 867.528 1.00201.57 C ATOM 867 O LEU A 116 110.499 188.620 868.743 1.00201.57 O ATOM 868 CB LEU A 116 111.515 187.219 865.868 1.00128.81 C ATOM 869 CG LEU A 116 110.479 186.810 864.811 1.00125.30 C ATOM 870 CD1 LEU A 116 110.604 187.687 863.581 1.00116.49 C ATOM 871 CD2 LEU A 116 110.704 185.363 864.414 1.00123.73 C ATOM 872 N LEU A 117 109.060 188.783 867.009 1.00168.12 N ATOM 873 CA LEU A 117 107.869 188.834 867.863 1.00168.12 C ATOM 874 C LEU A 117 106.702 188.061 867.249 1.00168.12 C ATOM 875 O LEU A 117 106.134 188.461 866.227 1.00168.12 O ATOM 876 CB LEU A 117 107.433 190.279 868.132 1.00118.26 C ATOM 877 CG LEU A 117 106.514 190.433 869.353 1.00118.26 C ATOM 878 CD1 LEU A 117 107.299 190.117 870.622 1.00118.26 C ATOM 879 CD2 LEU A 117 105.963 191.844 869.423 1.00118.26 C ATOM 880 N VAL A 118 106.352 186.953 867.899 1.00199.39 N ATOM 881 CA VAL A 118 105.270 186.084 867.454 1.00199.39 C ATOM 882 C VAL A 118 104.090 186.143 868.430 1.00199.39 C ATOM 883 O VAL A 118 104.282 186.266 869.641 1.00199.39 O ATOM 884 CB VAL A 118 105.768 184.614 867.337 1.00163.56 C ATOM 885 CG1 VAL A 118 104.620 183.691 866.962 1.00163.56 C ATOM 886 CG2 VAL A 118 106.875 184.521 866.299 1.00163.56 C ATOM 887 N ALA A 119 102.875 186.064 867.889 1.00127.78 N ATOM 888 CA ALA A 119 101.653 186.097 868.693 1.00122.35 C ATOM 889 C ALA A 119 100.687 185.022 868.201 1.00123.70 C ATOM 890 O ALA A 119 100.101 185.151 867.127 1.00124.39 O ATOM 891 CB ALA A 119 101.002 187.469 868.599 1.00198.12 C ATOM 892 N SER A 120 100.525 183.966 868.992 1.00162.36 N ATOM 893 CA SER A 120 99.646 182.864 868.620 1.00158.96 C ATOM 894 C SER A 120 98.370 182.827 869.455 1.00165.84 C ATOM 895 O SER A 120 98.257 183.520 870.465 1.00163.60 O ATOM 896 CB SER A 120 100.398 181.535 868.751 1.00200.79 C ATOM 897 OG SER A 120 99.608 180.450 868.299 1.00200.79 O ATOM 898 N SER A 121 97.418 182.005 869.019 1.00158.31 N ATOM 899 CA SER A 121 96.123 181.854 869.682 1.00158.31 C ATOM 900 C SER A 121 96.188 181.314 871.109 1.00158.31 C ATOM 901 O SER A 121 95.262 181.521 871.897 1.00158.31 O ATOM 902 CB SER A 121 95.217 180.948 868.847 1.00118.07 C ATOM 903 OG SER A 121 95.076 181.452 867.532 1.00114.70 O ATOM 904 N ASP A 122 97.267 180.615 871.442 1.00179.23 N ATOM 905 CA ASP A 122 97.416 180.065 872.786 1.00179.23 C ATOM 906 C ASP A 122 97.778 181.158 873.790 1.00179.23 C ATOM 907 O ASP A 122 98.484 180.911 874.772 1.00179.23 O ATOM 908 CB ASP A 122 98.477 178.958 872.796 1.00182.09 C ATOM 909 CG ASP A 122 99.813 179.419 872.245 1.00185.41 C ATOM 910 OD1 ASP A 122 99.849 179.858 871.076 1.00187.02 O ATOM 911 OD2 ASP A 122 100.822 179.336 872.978 1.00195.55 O ATOM 912 N GLY A 123 97.284 182.365 873.532 1.00184.89 N ATOM 913 CA GLY A 123 97.551 183.485 874.413 1.00184.89 C ATOM 914 C GLY A 123 99.014 183.647 874.774 1.00184.89 C ATOM 915 O GLY A 123 99.346 183.972 875.913 1.00184.89 O ATOM 916 N LYS A 124 99.892 183.414 873.808 1.00175.91 N ATOM 917 CA LYS A 124 101.318 183.555 874.047 1.00168.14 C ATOM 918 C LYS A 124 101.946 184.480 873.016 1.00166.92 C ATOM 919 O LYS A 124 101.379 184.716 871.946 1.00169.83 O ATOM 920 CB LYS A 124 102.020 182.188 874.010 1.00161.84 C ATOM 921 CG LYS A 124 101.800 181.304 875.240 1.00159.20 C ATOM 922 CD LYS A 124 102.734 180.094 875.199 1.00159.11 C ATOM 923 CE LYS A 124 102.669 179.271 876.475 1.00167.32 C ATOM 924 NZ LYS A 124 103.675 178.172 876.460 1.00179.30 N ATOM 925 N VAL A 125 103.117 185.008 873.366 1.00164.22 N ATOM 926 CA VAL A 125 103.890 185.905 872.510 1.00169.94 C ATOM 927 C VAL A 125 105.349 185.755 872.920 1.00169.94 C ATOM 928 O VAL A 125 105.708 186.055 874.060 1.00169.94 O ATOM 929 CB VAL A 125 103.474 187.383 872.696 1.00146.83 C ATOM 930 CG1 VAL A 125 104.396 188.285 871.884 1.00146.83 C ATOM 931 CG2 VAL A 125 102.020 187.580 872.265 1.00146.83 C ATOM 932 N SER A 126 106.187 185.290 872.000 1.00163.07 N ATOM 933 CA SER A 126 107.599 185.088 872.307 1.00163.07 C ATOM 934 C SER A 126 108.542 186.126 871.698 1.00163.07 C ATOM 935 O SER A 126 108.140 186.923 870.845 1.00163.07 O ATOM 936 CB SER A 126 108.030 183.674 871.878 1.00201.57 C ATOM 937 OG SER A 126 107.631 183.369 870.551 1.00201.57 O ATOM 938 N VAL A 127 109.790 186.112 872.169 1.00201.57 N ATOM 939 CA VAL A 127 110.847 187.008 871.692 1.00201.57 C ATOM 940 C VAL A 127 112.068 186.151 871.349 1.00201.57 C ATOM 941 O VAL A 127 113.074 186.151 872.064 1.00201.57 O ATOM 942 CB VAL A 127 111.250 188.044 872.764 1.00186.13 C ATOM 943 CG1 VAL A 127 112.279 189.011 872.185 1.00180.89 C ATOM 944 CG2 VAL A 127 110.022 188.798 873.249 1.00185.70 C ATOM 945 N VAL A 128 111.956 185.421 870.244 1.00195.46 N ATOM 946 CA VAL A 128 112.996 184.517 869.763 1.00195.46 C ATOM 947 C VAL A 128 114.253 185.181 869.221 1.00195.46 C ATOM 948 O VAL A 128 114.287 185.618 868.070 1.00195.46 O ATOM 949 CB VAL A 128 112.439 183.580 868.662 1.00201.57 C ATOM 950 CG1 VAL A 128 113.568 182.814 867.972 1.00201.57 C ATOM 951 CG2 VAL A 128 111.452 182.617 869.283 1.00201.57 C ATOM 952 N GLU A 129 115.287 185.242 870.054 1.00201.57 N ATOM 953 CA GLU A 129 116.548 185.824 869.630 1.00201.57 C ATOM 954 C GLU A 129 117.375 184.743 868.950 1.00201.57 C ATOM 955 O GLU A 129 117.135 183.556 869.150 1.00201.57 O ATOM 956 CB GLU A 129 117.332 186.366 870.819 1.00178.83 C ATOM 957 CG GLU A 129 118.689 186.896 870.409 1.00178.83 C ATOM 958 CD GLU A 129 119.472 187.442 871.564 1.00178.83 C ATOM 959 OE1 GLU A 129 119.806 186.655 872.476 1.00178.83 O ATOM 960 OE2 GLU A 129 119.750 188.659 871.556 1.00178.83 O ATOM 961 N PHE A 130 118.347 185.157 868.146 1.00201.57 N ATOM 962 CA PHE A 130 119.212 184.216 867.453 1.00201.57 C ATOM 963 C PHE A 130 120.639 184.342 867.997 1.00201.57 C ATOM 964 O PHE A 130 121.284 185.381 867.855 1.00201.57 O ATOM 965 CB PHE A 130 119.137 184.469 865.940 1.00150.88 C ATOM 966 CG PHE A 130 117.804 184.091 865.338 1.00150.07 C ATOM 967 CD1 PHE A 130 116.615 184.579 865.880 1.00149.35 C ATOM 968 CE1 PHE A 130 115.368 184.191 865.360 1.00149.39 C ATOM 969 CZ PHE A 130 115.306 183.307 864.284 1.00147.55 C ATOM 970 CE2 PHE A 130 116.489 182.815 863.729 1.00146.08 C ATOM 971 CD2 PHE A 130 117.734 183.210 864.260 1.00148.74 C ATOM 972 N LYS A 131 121.108 183.273 868.642 1.00201.57 N ATOM 973 CA LYS A 131 122.436 183.234 869.249 1.00201.57 C ATOM 974 C LYS A 131 123.590 183.243 868.253 1.00201.57 C ATOM 975 O LYS A 131 123.402 183.498 867.059 1.00201.57 O ATOM 976 CB LYS A 131 122.560 182.010 870.169 1.00157.95 C ATOM 977 CG LYS A 131 121.489 181.948 871.241 1.00159.69 C ATOM 978 CD LYS A 131 121.839 180.953 872.328 1.00160.85 C ATOM 979 CE LYS A 131 120.817 181.029 873.439 1.00161.18 C ATOM 980 NZ LYS A 131 121.193 180.251 874.643 1.00162.06 N ATOM 981 N GLU A 132 124.786 182.953 868.759 1.00195.20 N ATOM 982 CA GLU A 132 125.997 182.942 867.945 1.00195.20 C ATOM 983 C GLU A 132 126.027 181.821 866.906 1.00195.20 C ATOM 984 O GLU A 132 126.501 182.023 865.786 1.00195.20 O ATOM 985 CB GLU A 132 127.224 182.842 868.850 1.00200.56 C ATOM 986 CG GLU A 132 127.005 183.432 870.231 1.00201.26 C ATOM 987 CD GLU A 132 128.293 183.884 870.879 1.00201.32 C ATOM 988 OE1 GLU A 132 129.337 183.239 870.644 1.00201.57 O ATOM 989 OE2 GLU A 132 128.253 184.880 871.630 1.00200.91 O ATOM 990 N ASN A 133 125.525 180.643 867.275 1.00201.57 N ATOM 991 CA ASN A 133 125.498 179.499 866.359 1.00201.57 C ATOM 992 C ASN A 133 124.338 179.640 865.363 1.00201.57 C ATOM 993 O ASN A 133 124.152 178.791 864.484 1.00201.57 O ATOM 994 CB ASN A 133 125.334 178.178 867.134 1.00191.21 C ATOM 995 CG ASN A 133 126.360 178.011 868.250 1.00191.21 C ATOM 996 OD1 ASN A 133 127.368 178.713 868.301 1.00191.21 O ATOM 997 ND2 ASN A 133 126.105 177.059 869.142 1.00191.21 N ATOM 998 N GLY A 134 123.568 180.719 865.510 1.00199.74 N ATOM 999 CA GLY A 134 122.424 180.956 864.646 1.00199.74 C ATOM 1000 C GLY A 134 121.199 180.258 865.216 1.00199.74 C ATOM 1001 O GLY A 134 120.106 180.328 864.645 1.00199.74 O ATOM 1002 N THR A 135 121.399 179.591 866.355 1.00201.57 N ATOM 1003 CA THR A 135 120.353 178.842 867.063 1.00201.57 C ATOM 1004 C THR A 135 119.381 179.744 867.859 1.00201.57 C ATOM 1005 O THR A 135 119.746 180.852 868.259 1.00201.57 O ATOM 1006 CB THR A 135 120.997 177.776 868.021 1.00173.95 C ATOM 1007 OG1 THR A 135 121.900 178.420 868.936 1.00173.95 O ATOM 1008 CG2 THR A 135 121.767 176.721 867.215 1.00173.95 C ATOM 1009 N THR A 136 118.154 179.259 868.089 1.00201.57 N ATOM 1010 CA THR A 136 117.118 180.019 868.811 1.00201.57 C ATOM 1011 CB THR A 136 115.687 179.700 868.218 1.00172.80 C ATOM 1012 OG1 THR A 136 115.366 178.313 868.397 1.00172.80 O ATOM 1013 CG2 THR A 136 115.640 180.026 866.723 1.00172.80 C ATOM 1014 C THR A 136 117.084 179.878 870.360 1.00201.57 C ATOM 1015 O THR A 136 117.285 178.791 870.911 1.00201.57 O ATOM 1016 N SER A 137 116.827 181.000 871.044 1.00201.57 N ATOM 1017 CA SER A 137 116.752 181.070 872.515 1.00201.57 C ATOM 1018 C SER A 137 115.462 181.778 872.958 1.00201.57 C ATOM 1019 O SER A 137 115.500 182.933 873.394 1.00201.57 O ATOM 1020 CB SER A 137 117.954 181.850 873.068 1.00157.79 C ATOM 1021 OG SER A 137 117.843 182.066 874.466 1.00159.68 O ATOM 1022 N PRO A 138 114.308 181.087 872.870 1.00201.57 N ATOM 1023 CA PRO A 138 113.012 181.663 873.254 1.00201.57 C ATOM 1024 C PRO A 138 112.745 181.999 874.727 1.00201.57 C ATOM 1025 O PRO A 138 113.052 181.218 875.629 1.00201.57 O ATOM 1026 CB PRO A 138 112.012 180.640 872.715 1.00201.57 C ATOM 1027 CG PRO A 138 112.757 179.346 872.846 1.00201.57 C ATOM 1028 CD PRO A 138 114.137 179.718 872.343 1.00201.57 C ATOM 1029 N ILE A 139 112.171 183.182 874.942 1.00171.40 N ATOM 1030 CA ILE A 139 111.786 183.667 876.268 1.00171.40 C ATOM 1031 C ILE A 139 110.356 184.202 876.096 1.00171.40 C ATOM 1032 O ILE A 139 110.125 185.406 875.959 1.00171.40 O ATOM 1033 CB ILE A 139 112.744 184.789 876.792 1.00201.57 C ATOM 1034 CG1 ILE A 139 114.053 184.175 877.324 1.00201.57 C ATOM 1035 CD1 ILE A 139 115.007 183.616 876.268 1.00143.65 C ATOM 1036 CG2 ILE A 139 112.072 185.571 877.926 1.00201.57 C ATOM 1037 N ILE A 140 109.411 183.261 876.088 1.00162.46 N ATOM 1038 CA ILE A 140 107.981 183.520 875.904 1.00162.46 C ATOM 1039 C ILE A 140 107.284 184.101 877.149 1.00162.46 C ATOM 1040 O ILE A 140 107.860 184.135 878.241 1.00162.46 O ATOM 1041 CB ILE A 140 107.233 182.195 875.477 1.00168.01 C ATOM 1042 CG1 ILE A 140 107.882 181.572 874.233 1.00169.20 C ATOM 1043 CD1 ILE A 140 109.192 180.843 874.479 1.00150.32 C ATOM 1044 CG2 ILE A 140 105.777 182.480 875.136 1.00164.51 C ATOM 1045 N ILE A 141 106.049 184.567 876.953 1.00157.11 N ATOM 1046 CA ILE A 141 105.200 185.128 878.013 1.00157.11 C ATOM 1047 C ILE A 141 103.722 185.036 877.615 1.00157.11 C ATOM 1048 O ILE A 141 103.364 185.299 876.465 1.00157.11 O ATOM 1049 CB ILE A 141 105.496 186.624 878.294 1.00163.24 C ATOM 1050 CG1 ILE A 141 105.490 187.406 876.976 1.00162.39 C ATOM 1051 CD1 ILE A 141 105.575 188.906 877.145 1.00141.36 C ATOM 1052 CG2 ILE A 141 106.793 186.770 879.066 1.00168.63 C ATOM 1053 N ASP A 142 102.869 184.658 878.564 1.00201.57 N ATOM 1054 CA ASP A 142 101.436 184.569 878.300 1.00201.57 C ATOM 1055 CB ASP A 142 100.701 183.856 879.446 1.00165.68 C ATOM 1056 CG ASP A 142 101.109 182.398 879.596 1.00170.91 C ATOM 1057 OD1 ASP A 142 101.149 181.679 878.572 1.00176.09 O ATOM 1058 OD2 ASP A 142 101.377 181.969 880.740 1.00164.77 O ATOM 1059 C ASP A 142 100.936 186.004 878.178 1.00201.57 C ATOM 1060 O ASP A 142 101.171 186.826 879.069 1.00201.57 O ATOM 1061 N ALA A 143 100.248 186.302 877.079 1.00201.57 N ATOM 1062 CA ALA A 143 99.743 187.650 876.833 1.00201.57 C ATOM 1063 C ALA A 143 98.223 187.825 876.946 1.00201.57 C ATOM 1064 O ALA A 143 97.755 188.716 877.661 1.00201.57 O ATOM 1065 CB ALA A 143 100.225 188.136 875.460 1.00201.33 C ATOM 1066 N HIS A 144 97.452 186.992 876.244 1.00201.32 N ATOM 1067 CA HIS A 144 95.992 187.100 876.282 1.00201.32 C ATOM 1068 C HIS A 144 95.244 185.776 876.410 1.00201.32 C ATOM 1069 O HIS A 144 95.421 184.857 875.612 1.00201.32 O ATOM 1070 CB HIS A 144 95.494 187.860 875.050 1.00201.57 C ATOM 1071 CG HIS A 144 95.868 189.310 875.048 1.00201.57 C ATOM 1072 ND1 HIS A 144 96.647 190.028 874.204 1.00201.57 N ATOM 1073 CE1 HIS A 144 96.667 191.320 874.678 1.00201.57 C ATOM 1074 NE2 HIS A 144 95.931 191.390 875.769 1.00201.57 N ATOM 1075 CD2 HIS A 144 95.435 190.188 876.015 1.00201.57 C ATOM 1076 N ALA A 145 94.387 185.716 877.424 1.00184.26 N ATOM 1077 CA ALA A 145 93.588 184.541 877.739 1.00184.26 C ATOM 1078 C ALA A 145 92.939 183.811 876.565 1.00184.26 C ATOM 1079 O ALA A 145 93.247 182.645 876.314 1.00184.26 O ATOM 1080 CB ALA A 145 92.518 184.920 878.758 1.00121.36 C ATOM 1081 N ILE A 146 92.046 184.486 875.848 1.00137.77 N ATOM 1082 CA ILE A 146 91.328 183.853 874.738 1.00137.77 C ATOM 1083 C ILE A 146 92.022 183.886 873.368 1.00137.77 C ATOM 1084 O ILE A 146 91.386 183.685 872.330 1.00137.77 O ATOM 1085 CB ILE A 146 89.900 184.460 874.620 1.00123.56 C ATOM 1086 CG1 ILE A 146 89.268 184.533 876.017 1.00114.62 C ATOM 1087 CD1 ILE A 146 87.836 185.021 876.043 1.00143.19 C ATOM 1088 CG2 ILE A 146 89.027 183.598 873.696 1.00126.29 C ATOM 1089 N GLY A 147 93.332 184.111 873.373 1.00200.98 N ATOM 1090 CA GLY A 147 94.080 184.165 872.129 1.00200.98 C ATOM 1091 C GLY A 147 94.589 185.564 871.834 1.00200.98 C ATOM 1092 O GLY A 147 94.090 186.539 872.394 1.00200.98 O ATOM 1093 N VAL A 148 95.590 185.667 870.961 1.00179.74 N ATOM 1094 CA VAL A 148 96.159 186.961 870.589 1.00179.74 C ATOM 1095 C VAL A 148 96.112 187.114 869.069 1.00179.74 C ATOM 1096 O VAL A 148 96.579 186.238 868.336 1.00179.74 O ATOM 1097 CB VAL A 148 97.634 187.098 871.058 1.00114.01 C ATOM 1098 CG1 VAL A 148 98.124 188.514 870.807 1.00114.01 C ATOM 1099 CG2 VAL A 148 97.759 186.747 872.536 1.00114.01 C ATOM 1100 N ASN A 149 95.548 188.226 868.600 1.00115.46 N ATOM 1101 CA ASN A 149 95.431 188.485 867.164 1.00115.46 C ATOM 1102 CB ASN A 149 94.088 189.169 866.854 1.00152.89 C ATOM 1103 CG ASN A 149 92.895 188.224 866.975 1.00159.07 C ATOM 1104 OD1 ASN A 149 91.750 188.625 866.758 1.00165.26 O ATOM 1105 ND2 ASN A 149 93.161 186.968 867.315 1.00145.90 N ATOM 1106 C ASN A 149 96.582 189.320 866.582 1.00115.46 C ATOM 1107 O ASN A 149 96.770 189.340 865.362 1.00115.46 O ATOM 1108 N SER A 150 97.345 190.004 867.438 1.00177.92 N ATOM 1109 CA SER A 150 98.472 190.818 866.969 1.00177.92 C ATOM 1110 C SER A 150 99.386 191.367 868.068 1.00177.92 C ATOM 1111 O SER A 150 99.064 191.310 869.256 1.00177.92 O ATOM 1112 CB SER A 150 97.963 191.986 866.119 1.00161.76 C ATOM 1113 OG SER A 150 99.044 192.727 865.583 1.00161.76 O ATOM 1114 N ALA A 151 100.533 191.898 867.648 1.00165.29 N ATOM 1115 CA ALA A 151 101.519 192.470 868.561 1.00165.29 C ATOM 1116 C ALA A 151 102.621 193.216 867.791 1.00165.29 C ATOM 1117 O ALA A 151 103.393 192.600 867.054 1.00165.29 O ATOM 1118 CB ALA A 151 102.131 191.366 869.424 1.00108.12 C ATOM 1119 N SER A 152 102.687 194.541 867.966 1.00173.71 N ATOM 1120 CA SER A 152 103.683 195.388 867.294 1.00173.71 C ATOM 1121 C SER A 152 104.776 195.892 868.235 1.00173.71 C ATOM 1122 O SER A 152 104.550 196.040 869.434 1.00173.71 O ATOM 1123 CB SER A 152 103.008 196.604 866.640 1.00132.92 C ATOM 1124 OG SER A 152 102.306 196.249 865.461 1.00133.80 O ATOM 1125 N TRP A 153 105.955 196.163 867.678 1.00134.83 N ATOM 1126 CA TRP A 153 107.078 196.665 868.467 1.00134.94 C ATOM 1127 CB TRP A 153 108.414 196.297 867.819 1.00152.10 C ATOM 1128 CG TRP A 153 108.956 194.944 868.193 1.00152.10 C ATOM 1129 CD1 TRP A 153 108.786 193.775 867.513 1.00152.10 C ATOM 1130 NE1 TRP A 153 109.455 192.756 868.145 1.00152.10 N ATOM 1131 CE2 TRP A 153 110.073 193.253 869.263 1.00152.10 C ATOM 1132 CZ2 TRP A 153 110.862 192.608 870.221 1.00152.10 C ATOM 1133 CH2 TRP A 153 111.356 193.366 871.253 1.00149.45 C ATOM 1134 CZ3 TRP A 153 111.084 194.741 871.348 1.00152.10 C ATOM 1135 CE3 TRP A 153 110.297 195.384 870.392 1.00152.10 C ATOM 1136 CD2 TRP A 153 109.779 194.632 869.326 1.00152.10 C ATOM 1137 C TRP A 153 107.029 198.179 868.644 1.00137.30 C ATOM 1138 O TRP A 153 106.165 198.856 868.085 1.00133.32 O ATOM 1139 N ALA A 154 107.979 198.702 869.414 1.00201.57 N ATOM 1140 CA ALA A 154 108.051 200.133 869.681 1.00201.57 C ATOM 1141 C ALA A 154 109.458 200.681 869.524 1.00201.57 C ATOM 1142 O ALA A 154 110.383 200.246 870.213 1.00201.57 O ATOM 1143 CB ALA A 154 107.563 200.419 871.081 1.00 88.15 C ATOM 1144 N PRO A 155 109.644 201.646 868.612 1.00139.09 N ATOM 1145 CD PRO A 155 108.670 202.297 867.716 1.00157.04 C ATOM 1146 CG PRO A 155 109.390 203.560 867.326 1.00159.28 C ATOM 1147 CB PRO A 155 110.827 203.108 867.223 1.00159.28 C ATOM 1148 CA PRO A 155 110.988 202.204 868.441 1.00141.48 C ATOM 1149 C PRO A 155 111.309 202.972 869.719 1.00145.31 C ATOM 1150 O PRO A 155 110.444 203.658 870.259 1.00149.10 O ATOM 1151 N ALA A 156 112.531 202.849 870.219 1.00120.86 N ATOM 1152 CA ALA A 156 112.894 203.544 871.453 1.00127.73 C ATOM 1153 C ALA A 156 114.364 203.973 871.487 1.00128.76 C ATOM 1154 O ALA A 156 115.112 203.711 870.545 1.00132.85 O ATOM 1155 CB ALA A 156 112.571 202.652 872.662 1.00130.47 C ATOM 1156 N THR A 157 114.763 204.647 872.566 1.00153.74 N ATOM 1157 CA THR A 157 116.145 205.109 872.743 1.00159.88 C ATOM 1158 C THR A 157 116.536 205.051 874.221 1.00164.93 C ATOM 1159 O THR A 157 116.775 206.079 874.859 1.00166.90 O ATOM 1160 CB THR A 157 116.347 206.570 872.233 1.00173.65 C ATOM 1161 OG1 THR A 157 115.954 206.661 870.859 1.00173.50 O ATOM 1162 CG2 THR A 157 117.820 206.989 872.350 1.00169.53 C ATOM 1163 N SER A 170 114.653 199.369 878.341 1.00190.15 N ATOM 1164 CA SER A 170 113.439 200.174 878.251 1.00190.15 C ATOM 1165 C SER A 170 112.709 199.948 876.927 1.00190.15 C ATOM 1166 O SER A 170 112.174 200.887 876.331 1.00190.15 O ATOM 1167 CB SER A 170 113.778 201.659 878.407 1.00201.57 C ATOM 1168 OG SER A 170 114.736 202.074 877.450 1.00201.57 O ATOM 1169 N ARG A 171 112.697 198.698 876.470 1.00201.51 N ATOM 1170 CA ARG A 171 112.032 198.329 875.223 1.00201.51 C ATOM 1171 C ARG A 171 110.567 198.051 875.511 1.00201.51 C ATOM 1172 O ARG A 171 110.186 197.845 876.663 1.00201.51 O ATOM 1173 CB ARG A 171 112.666 197.069 874.636 1.00162.15 C ATOM 1174 CG ARG A 171 114.160 197.162 874.434 1.00162.15 C ATOM 1175 CD ARG A 171 114.720 195.838 873.959 1.00162.15 C ATOM 1176 NE ARG A 171 116.141 195.937 873.639 1.00162.15 N ATOM 1177 CZ ARG A 171 116.875 194.933 873.172 1.00162.15 C ATOM 1178 NH1 ARG A 171 116.322 193.742 872.969 1.00162.15 N ATOM 1179 NH2 ARG A 171 118.160 195.122 872.899 1.00162.15 N ATOM 1180 N LYS A 172 109.749 198.040 874.466 1.00152.25 N ATOM 1181 CA LYS A 172 108.322 197.780 874.624 1.00151.50 C ATOM 1182 C LYS A 172 107.680 197.331 873.317 1.00152.68 C ATOM 1183 O LYS A 172 108.258 197.486 872.235 1.00150.81 O ATOM 1184 CB LYS A 172 107.587 199.036 875.117 1.00149.46 C ATOM 1185 CG LYS A 172 107.938 199.476 876.525 1.00149.46 C ATOM 1186 CD LYS A 172 107.286 200.805 876.876 1.00149.46 C ATOM 1187 CE LYS A 172 107.789 201.303 878.229 1.00149.46 C ATOM 1188 NZ LYS A 172 107.251 202.645 878.600 1.00149.46 N ATOM 1189 N PHE A 173 106.479 196.765 873.444 1.00131.02 N ATOM 1190 CA PHE A 173 105.679 196.310 872.311 1.00131.02 C ATOM 1191 C PHE A 173 104.212 196.244 872.733 1.00131.02 C ATOM 1192 O PHE A 173 103.902 196.088 873.915 1.00131.02 O ATOM 1193 CB PHE A 173 106.170 194.946 871.766 1.00176.82 C ATOM 1194 CG PHE A 173 106.129 193.799 872.762 1.00176.82 C ATOM 1195 CD1 PHE A 173 104.921 193.321 873.261 1.00176.82 C ATOM 1196 CE1 PHE A 173 104.888 192.231 874.137 1.00176.82 C ATOM 1197 CZ PHE A 173 106.072 191.611 874.520 1.00176.82 C ATOM 1198 CE2 PHE A 173 107.284 192.077 874.031 1.00176.82 C ATOM 1199 CD2 PHE A 173 107.308 193.165 873.157 1.00176.82 C ATOM 1200 N VAL A 174 103.316 196.397 871.768 1.00201.57 N ATOM 1201 CA VAL A 174 101.885 196.355 872.040 1.00201.57 C ATOM 1202 C VAL A 174 101.317 195.002 871.604 1.00201.57 C ATOM 1203 O VAL A 174 101.870 194.341 870.723 1.00201.57 O ATOM 1204 CB VAL A 174 101.156 197.509 871.302 1.00120.70 C ATOM 1205 CG1 VAL A 174 101.548 197.521 869.835 1.00115.84 C ATOM 1206 CG2 VAL A 174 99.650 197.360 871.441 1.00119.99 C ATOM 1207 N THR A 175 100.225 194.583 872.241 1.00179.85 N ATOM 1208 CA THR A 175 99.589 193.311 871.917 1.00179.85 C ATOM 1209 C THR A 175 98.063 193.408 871.857 1.00179.85 C ATOM 1210 O THR A 175 97.412 193.775 872.837 1.00179.85 O ATOM 1211 CB THR A 175 99.988 192.211 872.939 1.00184.62 C ATOM 1212 OG1 THR A 175 99.873 192.723 874.275 1.00184.62 O ATOM 1213 CG2 THR A 175 101.416 191.747 872.692 1.00184.62 C ATOM 1214 N GLY A 176 97.505 193.090 870.691 1.00187.03 N ATOM 1215 CA GLY A 176 96.063 193.125 870.510 1.00187.03 C ATOM 1216 C GLY A 176 95.511 191.738 870.773 1.00187.03 C ATOM 1217 O GLY A 176 95.935 190.772 870.136 1.00187.03 O ATOM 1218 N GLY A 177 94.561 191.633 871.701 1.00175.87 N ATOM 1219 CA GLY A 177 94.014 190.329 872.043 1.00175.87 C ATOM 1220 C GLY A 177 92.622 189.945 871.573 1.00175.87 C ATOM 1221 O GLY A 177 92.060 190.549 870.659 1.00175.87 O ATOM 1222 N ALA A 178 92.082 188.910 872.215 1.00157.01 N ATOM 1223 CA ALA A 178 90.754 188.375 871.917 1.00157.01 C ATOM 1224 C ALA A 178 89.779 188.762 873.018 1.00157.01 C ATOM 1225 O ALA A 178 88.562 188.735 872.826 1.00157.01 O ATOM 1226 CB ALA A 178 90.821 186.863 871.806 1.00160.81 C ATOM 1227 N ASP A 179 90.331 189.102 874.180 1.00189.09 N ATOM 1228 CA ASP A 179 89.536 189.521 875.325 1.00189.09 C ATOM 1229 C ASP A 179 89.404 191.048 875.298 1.00189.09 C ATOM 1230 O ASP A 179 89.143 191.690 876.318 1.00189.09 O ATOM 1231 CB ASP A 179 90.201 189.048 876.621 1.00164.23 C ATOM 1232 CG ASP A 179 91.618 189.556 876.767 1.00164.23 C ATOM 1233 OD1 ASP A 179 92.412 189.378 875.817 1.00164.23 O ATOM 1234 OD2 ASP A 179 91.942 190.126 877.832 1.00164.23 O ATOM 1235 N ASN A 180 89.603 191.610 874.106 1.00201.33 N ATOM 1236 CA ASN A 180 89.497 193.047 873.847 1.00201.33 C ATOM 1237 C ASN A 180 90.414 193.947 874.660 1.00201.33 C ATOM 1238 O ASN A 180 89.989 194.987 875.173 1.00200.46 O ATOM 1239 CB ASN A 180 88.051 193.493 874.030 1.00124.90 C ATOM 1240 CG ASN A 180 87.085 192.663 873.220 1.00124.90 C ATOM 1241 OD1 ASN A 180 87.616 191.744 872.423 1.00124.90 O ATOM 1242 ND2 ASN A 180 85.874 192.844 873.308 1.00124.90 N ATOM 1243 N LEU A 181 91.674 193.543 874.773 1.00201.57 N ATOM 1244 CA LEU A 181 92.659 194.326 875.502 1.00201.57 C ATOM 1245 C LEU A 181 93.730 194.819 874.538 1.00201.57 C ATOM 1246 O LEU A 181 93.752 194.457 873.357 1.00201.57 O ATOM 1247 CB LEU A 181 93.330 193.493 876.608 1.00143.31 C ATOM 1248 CG LEU A 181 92.639 193.218 877.949 1.00143.31 C ATOM 1249 CD1 LEU A 181 93.546 192.349 878.813 1.00143.31 C ATOM 1250 CD2 LEU A 181 92.347 194.518 878.660 1.00143.31 C ATOM 1251 N VAL A 182 94.610 195.659 875.068 1.00201.57 N ATOM 1252 CA VAL A 182 95.722 196.223 874.325 1.00201.57 C ATOM 1253 C VAL A 182 96.792 196.426 875.395 1.00201.57 C ATOM 1254 O VAL A 182 96.766 197.414 876.131 1.00201.57 O ATOM 1255 CB VAL A 182 95.338 197.584 873.679 1.00119.37 C ATOM 1256 CG1 VAL A 182 96.458 198.058 872.766 1.00119.37 C ATOM 1257 CG2 VAL A 182 94.037 197.452 872.886 1.00119.37 C ATOM 1258 N LYS A 183 97.712 195.473 875.496 1.00159.92 N ATOM 1259 CA LYS A 183 98.772 195.528 876.502 1.00159.85 C ATOM 1260 C LYS A 183 100.084 196.155 876.037 1.00159.92 C ATOM 1261 O LYS A 183 100.412 196.140 874.848 1.00159.92 O ATOM 1262 CB LYS A 183 99.067 194.121 877.028 1.00166.19 C ATOM 1263 CG LYS A 183 97.908 193.441 877.735 1.00172.96 C ATOM 1264 CD LYS A 183 98.357 192.107 878.306 1.00167.23 C ATOM 1265 CE LYS A 183 97.252 191.431 879.091 1.00172.96 C ATOM 1266 NZ LYS A 183 97.763 190.198 879.747 1.00172.96 N ATOM 1267 N ILE A 184 100.829 196.698 876.999 1.00183.22 N ATOM 1268 CA ILE A 184 102.129 197.318 876.748 1.00183.22 C ATOM 1269 C ILE A 184 103.165 196.680 877.674 1.00183.22 C ATOM 1270 O ILE A 184 103.242 197.000 878.865 1.00183.22 O ATOM 1271 CB ILE A 184 102.097 198.852 876.996 1.00173.17 C ATOM 1272 CG1 ILE A 184 101.195 199.529 875.961 1.00173.17 C ATOM 1273 CD1 ILE A 184 101.590 199.258 874.508 1.00138.66 C ATOM 1274 CG2 ILE A 184 103.509 199.431 876.915 1.00173.17 C ATOM 1275 N TRP A 185 103.958 195.774 877.114 1.00201.57 N ATOM 1276 CA TRP A 185 104.981 195.069 877.875 1.00201.57 C ATOM 1277 C TRP A 185 106.323 195.795 877.818 1.00201.57 C ATOM 1278 O TRP A 185 106.621 196.486 876.840 1.00201.57 O ATOM 1279 CB TRP A 185 105.130 193.642 877.338 1.00201.57 C ATOM 1280 CG TRP A 185 103.835 192.869 877.321 1.00201.57 C ATOM 1281 CD1 TRP A 185 102.740 193.112 876.535 1.00201.57 C ATOM 1282 NE1 TRP A 185 101.747 192.202 876.809 1.00201.57 N ATOM 1283 CE2 TRP A 185 102.186 191.345 877.789 1.00201.57 C ATOM 1284 CZ2 TRP A 185 101.539 190.263 878.400 1.00201.57 C ATOM 1285 CH2 TRP A 185 102.232 189.569 879.366 1.00201.57 C ATOM 1286 CZ3 TRP A 185 103.542 189.936 879.735 1.00201.57 C ATOM 1287 CE3 TRP A 185 104.183 191.016 879.127 1.00201.57 C ATOM 1288 CD2 TRP A 185 103.502 191.742 878.137 1.00201.57 C ATOM 1289 N LYS A 186 107.120 195.634 878.872 1.00201.57 N ATOM 1290 CA LYS A 186 108.439 196.266 878.963 1.00201.57 C ATOM 1291 C LYS A 186 109.508 195.288 879.476 1.00201.57 C ATOM 1292 O LYS A 186 109.324 194.645 880.512 1.00201.57 O ATOM 1293 CB LYS A 186 108.377 197.491 879.891 1.00184.37 C ATOM 1294 CG LYS A 186 109.709 198.221 880.034 1.00184.37 C ATOM 1295 CD LYS A 186 109.600 199.469 880.894 1.00184.37 C ATOM 1296 CE LYS A 186 110.944 200.180 880.977 1.00184.37 C ATOM 1297 NZ LYS A 186 110.876 201.438 881.768 1.00184.37 N ATOM 1298 N TYR A 187 110.620 195.183 878.750 1.00154.51 N ATOM 1299 CA TYR A 187 111.702 194.290 879.158 1.00154.51 C ATOM 1300 C TYR A 187 112.245 194.721 880.518 1.00154.51 C ATOM 1301 O TYR A 187 112.264 195.912 880.847 1.00154.51 O ATOM 1302 CB TYR A 187 112.830 194.301 878.115 1.00187.95 C ATOM 1303 CG TYR A 187 114.063 193.515 878.528 1.00187.95 C ATOM 1304 CD1 TYR A 187 113.975 192.165 878.881 1.00187.95 C ATOM 1305 CE1 TYR A 187 115.110 191.441 879.279 1.00187.95 C ATOM 1306 CZ TYR A 187 116.349 192.072 879.328 1.00187.95 C ATOM 1307 OH TYR A 187 117.466 191.371 879.728 1.00187.95 O ATOM 1308 CE2 TYR A 187 116.462 193.411 878.978 1.00187.95 C ATOM 1309 CD2 TYR A 187 115.319 194.125 878.582 1.00187.95 C ATOM 1310 N ASN A 188 112.676 193.747 881.313 1.00200.57 N ATOM 1311 CA ASN A 188 113.219 194.026 882.635 1.00200.57 C ATOM 1312 C ASN A 188 114.304 193.008 882.970 1.00200.57 C ATOM 1313 O ASN A 188 114.079 191.799 882.866 1.00200.57 O ATOM 1314 CB ASN A 188 112.098 193.968 883.674 1.00193.02 C ATOM 1315 CG ASN A 188 112.122 195.146 884.616 1.00193.02 C ATOM 1316 OD1 ASN A 188 113.068 195.323 885.383 1.00193.02 O ATOM 1317 ND2 ASN A 188 111.081 195.971 884.561 1.00193.02 N ATOM 1318 N SER A 189 115.480 193.500 883.365 1.00201.57 N ATOM 1319 CA SER A 189 116.614 192.634 883.714 1.00201.57 C ATOM 1320 C SER A 189 116.309 191.719 884.906 1.00201.57 C ATOM 1321 O SER A 189 116.669 190.538 884.907 1.00201.57 O ATOM 1322 CB SER A 189 117.862 193.482 884.025 1.00159.38 C ATOM 1323 OG SER A 189 118.398 194.085 882.858 1.00161.39 O ATOM 1324 N ASP A 190 115.641 192.275 885.912 1.00193.21 N ATOM 1325 CA ASP A 190 115.283 191.538 887.120 1.00193.21 C ATOM 1326 C ASP A 190 114.330 190.378 886.843 1.00193.21 C ATOM 1327 O ASP A 190 114.211 189.456 887.651 1.00193.21 O ATOM 1328 CB ASP A 190 114.650 192.494 888.136 1.00191.02 C ATOM 1329 CG ASP A 190 115.573 193.643 888.508 1.00191.02 C ATOM 1330 OD1 ASP A 190 116.029 194.361 887.593 1.00191.02 O ATOM 1331 OD2 ASP A 190 115.841 193.831 889.715 1.00191.02 O ATOM 1332 N ALA A 191 113.652 190.423 885.701 1.00201.57 N ATOM 1333 CA ALA A 191 112.711 189.372 885.336 1.00201.57 C ATOM 1334 C ALA A 191 113.175 188.551 884.126 1.00201.57 C ATOM 1335 O ALA A 191 112.698 187.435 883.919 1.00201.57 O ATOM 1336 CB ALA A 191 111.329 189.981 885.065 1.00121.22 C ATOM 1337 N GLN A 192 114.100 189.102 883.338 1.00194.49 N ATOM 1338 CA GLN A 192 114.631 188.429 882.143 1.00194.49 C ATOM 1339 C GLN A 192 113.557 188.162 881.080 1.00194.49 C ATOM 1340 O GLN A 192 113.866 187.884 879.918 1.00194.49 O ATOM 1341 CB GLN A 192 115.316 187.112 882.532 1.00201.57 C ATOM 1342 CG GLN A 192 116.665 187.279 883.232 1.00201.57 C ATOM 1343 CD GLN A 192 117.752 187.792 882.302 1.00201.57 C ATOM 1344 OE1 GLN A 192 117.656 188.892 881.753 1.00201.57 O ATOM 1345 NE2 GLN A 192 118.796 186.990 882.118 1.00201.57 N ATOM 1346 N THR A 193 112.296 188.243 881.496 1.00201.57 N ATOM 1347 CA THR A 193 111.154 188.040 880.611 1.00201.57 C ATOM 1348 C THR A 193 110.311 189.320 880.718 1.00201.57 C ATOM 1349 O THR A 193 110.001 189.775 881.824 1.00201.57 O ATOM 1350 CB THR A 193 110.324 186.780 881.041 1.00199.67 C ATOM 1351 OG1 THR A 193 109.395 186.435 880.007 1.00200.96 O ATOM 1352 CG2 THR A 193 109.564 187.035 882.345 1.00190.51 C ATOM 1353 N TYR A 194 109.972 189.912 879.573 1.00201.57 N ATOM 1354 CA TYR A 194 109.188 191.150 879.539 1.00201.57 C ATOM 1355 C TYR A 194 108.122 191.237 880.626 1.00201.57 C ATOM 1356 O TYR A 194 107.264 190.359 880.750 1.00201.57 O ATOM 1357 CB TYR A 194 108.521 191.334 878.169 1.00201.37 C ATOM 1358 CG TYR A 194 109.481 191.663 877.045 1.00201.37 C ATOM 1359 CD1 TYR A 194 110.342 190.696 876.528 1.00201.37 C ATOM 1360 CE1 TYR A 194 111.239 191.004 875.498 1.00201.37 C ATOM 1361 CZ TYR A 194 111.278 192.293 874.980 1.00201.37 C ATOM 1362 OH TYR A 194 112.164 192.612 873.972 1.00201.37 O ATOM 1363 CE2 TYR A 194 110.431 193.269 875.481 1.00201.37 C ATOM 1364 CD2 TYR A 194 109.537 192.949 876.507 1.00201.37 C ATOM 1365 N VAL A 195 108.185 192.314 881.405 1.00201.57 N ATOM 1366 CA VAL A 195 107.240 192.557 882.493 1.00201.57 C ATOM 1367 C VAL A 195 106.064 193.413 882.004 1.00201.57 C ATOM 1368 O VAL A 195 106.259 194.509 881.476 1.00201.57 O ATOM 1369 CB VAL A 195 107.940 193.282 883.685 1.00182.30 C ATOM 1370 CG1 VAL A 195 106.943 193.529 884.823 1.00182.30 C ATOM 1371 CG2 VAL A 195 109.124 192.454 884.175 1.00182.30 C ATOM 1372 N LEU A 196 104.846 192.904 882.172 1.00201.57 N ATOM 1373 CA LEU A 196 103.649 193.635 881.761 1.00201.57 C ATOM 1374 C LEU A 196 103.524 194.875 882.648 1.00201.57 C ATOM 1375 O LEU A 196 103.514 194.766 883.875 1.00201.57 O ATOM 1376 CB LEU A 196 102.414 192.737 881.909 1.00146.68 C ATOM 1377 CG LEU A 196 101.038 193.271 881.497 1.00146.68 C ATOM 1378 CD1 LEU A 196 101.079 193.773 880.056 1.00146.68 C ATOM 1379 CD2 LEU A 196 100.003 192.154 881.669 1.00142.75 C ATOM 1380 N GLU A 197 103.440 196.051 882.034 1.00201.12 N ATOM 1381 CA GLU A 197 103.337 197.280 882.807 1.00201.12 C ATOM 1382 C GLU A 197 101.995 198.002 882.674 1.00201.12 C ATOM 1383 O GLU A 197 101.452 198.488 883.669 1.00201.12 O ATOM 1384 CB GLU A 197 104.474 198.231 882.433 1.00198.92 C ATOM 1385 CG GLU A 197 104.532 199.466 883.311 1.00198.92 C ATOM 1386 CD GLU A 197 105.684 200.377 882.959 1.00198.92 C ATOM 1387 OE1 GLU A 197 106.302 200.158 881.894 1.00198.92 O ATOM 1388 OE2 GLU A 197 105.964 201.314 883.738 1.00198.92 O ATOM 1389 N SER A 198 101.462 198.080 881.456 1.00201.57 N ATOM 1390 CA SER A 198 100.177 198.749 881.231 1.00201.57 C ATOM 1391 C SER A 198 99.262 198.004 880.264 1.00201.57 C ATOM 1392 O SER A 198 99.712 197.450 879.260 1.00201.57 O ATOM 1393 CB SER A 198 100.392 200.174 880.701 1.00146.06 C ATOM 1394 OG SER A 198 100.997 201.001 881.675 1.00146.06 O ATOM 1395 N THR A 199 97.971 197.995 880.583 1.00154.93 N ATOM 1396 CA THR A 199 96.968 197.353 879.743 1.00154.93 C ATOM 1397 C THR A 199 95.841 198.367 879.622 1.00154.93 C ATOM 1398 O THR A 199 95.584 199.123 880.560 1.00154.93 O ATOM 1399 CB THR A 199 96.423 196.051 880.377 1.00201.57 C ATOM 1400 OG1 THR A 199 97.502 195.133 880.597 1.00201.57 O ATOM 1401 CG2 THR A 199 95.403 195.399 879.453 1.00201.57 C ATOM 1402 N LEU A 200 95.180 198.391 878.467 1.00180.51 N ATOM 1403 CA LEU A 200 94.093 199.335 878.235 1.00180.51 C ATOM 1404 C LEU A 200 92.863 198.653 877.631 1.00180.51 C ATOM 1405 O LEU A 200 92.988 197.748 876.805 1.00180.51 O ATOM 1406 CB LEU A 200 94.583 200.460 877.317 1.00201.56 C ATOM 1407 CG LEU A 200 95.859 201.188 877.771 1.00201.56 C ATOM 1408 CD1 LEU A 200 96.332 202.118 876.668 1.00201.56 C ATOM 1409 CD2 LEU A 200 95.606 201.959 879.063 1.00201.56 C ATOM 1410 N GLU A 201 91.679 199.097 878.055 1.00164.98 N ATOM 1411 CA GLU A 201 90.409 198.535 877.584 1.00164.98 C ATOM 1412 C GLU A 201 89.530 199.556 876.864 1.00164.98 C ATOM 1413 O GLU A 201 89.439 200.710 877.285 1.00164.98 O ATOM 1414 CB GLU A 201 89.624 197.946 878.764 1.00201.57 C ATOM 1415 CG GLU A 201 90.162 196.617 879.278 1.00201.57 C ATOM 1416 CD GLU A 201 89.379 196.070 880.462 1.00201.57 C ATOM 1417 OE1 GLU A 201 88.130 196.048 880.396 1.00201.57 O ATOM 1418 OE2 GLU A 201 90.014 195.651 881.455 1.00201.57 O ATOM 1419 N GLY A 202 88.875 199.127 875.787 1.00145.22 N ATOM 1420 CA GLY A 202 88.018 200.037 875.048 1.00147.16 C ATOM 1421 C GLY A 202 87.308 199.445 873.846 1.00144.27 C ATOM 1422 O GLY A 202 86.551 200.142 873.163 1.00150.49 O ATOM 1423 N HIS A 203 87.547 198.167 873.578 1.00170.02 N ATOM 1424 CA HIS A 203 86.907 197.505 872.448 1.00170.02 C ATOM 1425 C HIS A 203 85.904 196.456 872.919 1.00170.02 C ATOM 1426 O HIS A 203 86.032 195.912 874.018 1.00170.02 O ATOM 1427 CB HIS A 203 87.963 196.858 871.550 1.00172.72 C ATOM 1428 CG HIS A 203 88.851 197.847 870.856 1.00172.72 C ATOM 1429 ND1 HIS A 203 88.366 198.776 869.961 1.00172.72 N ATOM 1430 CE1 HIS A 203 89.368 199.514 869.512 1.00172.72 C ATOM 1431 NE2 HIS A 203 90.482 199.093 870.084 1.00172.72 N ATOM 1432 CD2 HIS A 203 90.187 198.051 870.928 1.00172.72 C ATOM 1433 N SER A 204 84.902 196.180 872.089 1.00172.86 N ATOM 1434 CA SER A 204 83.875 195.200 872.429 1.00172.86 C ATOM 1435 C SER A 204 83.953 193.907 871.608 1.00172.86 C ATOM 1436 O SER A 204 82.989 193.140 871.552 1.00172.86 O ATOM 1437 CB SER A 204 82.486 195.830 872.286 1.00150.80 C ATOM 1438 OG SER A 204 82.347 196.489 871.041 1.00150.80 O ATOM 1439 N ASP A 205 85.103 193.671 870.978 1.00168.71 N ATOM 1440 CA ASP A 205 85.325 192.468 870.178 1.00168.71 C ATOM 1441 C ASP A 205 86.814 192.323 869.857 1.00168.71 C ATOM 1442 O ASP A 205 87.549 193.312 869.811 1.00168.71 O ATOM 1443 CB ASP A 205 84.518 192.522 868.875 1.00186.00 C ATOM 1444 CG ASP A 205 84.326 191.148 868.245 1.00184.81 C ATOM 1445 OD1 ASP A 205 85.325 190.415 868.076 1.00191.86 O ATOM 1446 OD2 ASP A 205 83.173 190.804 867.913 1.00191.61 O ATOM 1447 N TRP A 206 87.246 191.082 869.655 1.00201.57 N ATOM 1448 CA TRP A 206 88.634 190.752 869.336 1.00201.57 C ATOM 1449 C TRP A 206 89.442 191.903 868.730 1.00201.57 C ATOM 1450 O TRP A 206 89.262 192.238 867.558 1.00201.57 O ATOM 1451 CB TRP A 206 88.656 189.551 868.379 1.00194.67 C ATOM 1452 CG TRP A 206 88.193 188.281 869.014 1.00194.67 C ATOM 1453 CD1 TRP A 206 87.029 188.085 869.698 1.00194.67 C ATOM 1454 NE1 TRP A 206 86.978 186.805 870.187 1.00194.67 N ATOM 1455 CE2 TRP A 206 88.116 186.141 869.818 1.00194.67 C ATOM 1456 CZ2 TRP A 206 88.521 184.823 870.079 1.00194.67 C ATOM 1457 CH2 TRP A 206 89.734 184.418 869.575 1.00194.67 C ATOM 1458 CZ3 TRP A 206 90.546 185.294 868.828 1.00194.67 C ATOM 1459 CE3 TRP A 206 90.142 186.605 868.569 1.00194.67 C ATOM 1460 CD2 TRP A 206 88.908 187.041 869.075 1.00194.67 C ATOM 1461 N VAL A 207 90.330 192.502 869.524 1.00160.84 N ATOM 1462 CA VAL A 207 91.169 193.604 869.043 1.00160.84 C ATOM 1463 C VAL A 207 92.031 193.108 867.880 1.00160.84 C ATOM 1464 O VAL A 207 93.169 192.683 868.080 1.00160.84 O ATOM 1465 CB VAL A 207 92.115 194.142 870.151 1.00185.80 C ATOM 1466 CG1 VAL A 207 92.894 195.333 869.623 1.00185.80 C ATOM 1467 CG2 VAL A 207 91.324 194.537 871.386 1.00185.80 C ATOM 1468 N ARG A 208 91.475 193.169 866.671 1.00180.46 N ATOM 1469 CA ARG A 208 92.149 192.719 865.453 1.00180.46 C ATOM 1470 C ARG A 208 93.635 193.034 865.341 1.00180.46 C ATOM 1471 O ARG A 208 94.481 192.163 865.536 1.00180.46 O ATOM 1472 CB ARG A 208 91.431 193.271 864.213 1.00147.58 C ATOM 1473 CG ARG A 208 90.347 192.360 863.684 1.00147.58 C ATOM 1474 CD ARG A 208 90.937 190.990 863.418 1.00147.58 C ATOM 1475 NE ARG A 208 89.930 189.991 863.085 1.00147.58 N ATOM 1476 CZ ARG A 208 90.190 188.697 862.944 1.00147.58 C ATOM 1477 NH1 ARG A 208 91.426 188.242 863.107 1.00147.58 N ATOM 1478 NH2 ARG A 208 89.217 187.855 862.636 1.00147.58 N ATOM 1479 N ASP A 209 93.946 194.284 865.018 1.00154.99 N ATOM 1480 CA ASP A 209 95.330 194.707 864.845 1.00154.99 C ATOM 1481 C ASP A 209 95.662 195.895 865.753 1.00154.99 C ATOM 1482 O ASP A 209 94.802 196.726 866.037 1.00153.21 O ATOM 1483 CB ASP A 209 95.543 195.085 863.371 1.00125.47 C ATOM 1484 CG ASP A 209 96.993 194.991 862.937 1.00127.05 C ATOM 1485 OD1 ASP A 209 97.258 195.186 861.731 1.00127.05 O ATOM 1486 OD2 ASP A 209 97.865 194.724 863.790 1.00127.05 O ATOM 1487 N VAL A 210 96.906 195.958 866.219 1.00148.90 N ATOM 1488 CA VAL A 210 97.361 197.061 867.065 1.00148.90 C ATOM 1489 C VAL A 210 98.707 197.547 866.534 1.00148.90 C ATOM 1490 O VAL A 210 99.517 196.747 866.064 1.00148.90 O ATOM 1491 CB VAL A 210 97.519 196.641 868.542 1.00137.54 C ATOM 1492 CG1 VAL A 210 96.155 196.368 869.150 1.00135.48 C ATOM 1493 CG2 VAL A 210 98.407 195.419 868.639 1.00130.11 C ATOM 1494 N ALA A 211 98.948 198.852 866.609 1.00158.57 N ATOM 1495 CA ALA A 211 100.193 199.399 866.090 1.00158.57 C ATOM 1496 C ALA A 211 100.772 200.565 866.869 1.00158.57 C ATOM 1497 O ALA A 211 100.041 201.452 867.334 1.00158.57 O ATOM 1498 CB ALA A 211 100.005 199.802 864.621 1.00 77.92 C ATOM 1499 N TRP A 212 102.101 200.554 867.009 1.00161.81 N ATOM 1500 CA TRP A 212 102.824 201.625 867.704 1.00161.81 C ATOM 1501 C TRP A 212 103.365 202.484 866.547 1.00161.81 C ATOM 1502 O TRP A 212 103.554 201.983 865.434 1.00161.81 O ATOM 1503 CB TRP A 212 103.975 201.077 868.574 1.00193.71 C ATOM 1504 CG TRP A 212 104.459 202.076 869.662 1.00193.71 C ATOM 1505 CD1 TRP A 212 104.906 203.352 869.454 1.00193.71 C ATOM 1506 NE1 TRP A 212 105.316 203.922 870.640 1.00193.71 N ATOM 1507 CE2 TRP A 212 105.138 203.021 871.657 1.00193.71 C ATOM 1508 CZ2 TRP A 212 105.403 203.147 873.032 1.00193.71 C ATOM 1509 CH2 TRP A 212 105.126 202.069 873.834 1.00193.71 C ATOM 1510 CZ3 TRP A 212 104.582 200.884 873.305 1.00193.71 C ATOM 1511 CE3 TRP A 212 104.313 200.758 871.932 1.00193.71 C ATOM 1512 CD2 TRP A 212 104.589 201.844 871.087 1.00193.71 C ATOM 1513 N SER A 213 103.570 203.779 866.773 1.00158.56 N ATOM 1514 CA SER A 213 104.042 204.654 865.700 1.00158.56 C ATOM 1515 C SER A 213 105.519 205.040 865.747 1.00158.56 C ATOM 1516 O SER A 213 106.086 205.268 866.812 1.00158.56 O ATOM 1517 CB SER A 213 103.189 205.925 865.634 1.00145.92 C ATOM 1518 OG SER A 213 103.535 206.688 864.489 1.00144.98 O ATOM 1519 N PRO A 214 106.161 205.117 864.568 1.00170.85 N ATOM 1520 CA PRO A 214 107.575 205.470 864.408 1.00176.27 C ATOM 1521 C PRO A 214 107.798 206.981 864.421 1.00179.75 C ATOM 1522 O PRO A 214 108.533 207.520 863.590 1.00179.86 O ATOM 1523 CB PRO A 214 107.918 204.856 863.062 1.00155.19 C ATOM 1524 CG PRO A 214 106.674 205.133 862.280 1.00153.59 C ATOM 1525 CD PRO A 214 105.571 204.758 863.262 1.00157.17 C ATOM 1526 N THR A 215 107.153 207.663 865.361 1.00201.57 N ATOM 1527 CA THR A 215 107.282 209.110 865.475 1.00201.57 C ATOM 1528 C THR A 215 107.965 209.503 866.785 1.00201.57 C ATOM 1529 O THR A 215 107.327 209.556 867.837 1.00201.57 O ATOM 1530 CB THR A 215 105.898 209.798 865.397 1.00163.62 C ATOM 1531 OG1 THR A 215 106.034 211.192 865.697 1.00160.29 O ATOM 1532 CG2 THR A 215 104.928 209.160 866.377 1.00163.91 C ATOM 1533 N VAL A 216 109.266 209.775 866.711 1.00201.25 N ATOM 1534 CA VAL A 216 110.043 210.168 867.888 1.00201.25 C ATOM 1535 C VAL A 216 109.824 211.658 868.174 1.00201.25 C ATOM 1536 O VAL A 216 110.778 212.414 868.372 1.00201.25 O ATOM 1537 CB VAL A 216 111.566 209.907 867.677 1.00185.04 C ATOM 1538 CG1 VAL A 216 112.307 209.988 869.007 1.00185.34 C ATOM 1539 CG2 VAL A 216 111.780 208.546 867.033 1.00181.10 C ATOM 1540 N LEU A 217 108.558 212.071 868.191 1.00201.31 N ATOM 1541 CA LEU A 217 108.194 213.461 868.447 1.00201.31 C ATOM 1542 C LEU A 217 107.660 213.615 869.879 1.00201.31 C ATOM 1543 O LEU A 217 107.821 212.716 870.705 1.00201.31 O ATOM 1544 CB LEU A 217 107.147 213.921 867.415 1.00185.48 C ATOM 1545 CG LEU A 217 106.671 215.381 867.311 1.00190.36 C ATOM 1546 CD1 LEU A 217 105.337 215.544 868.025 1.00188.38 C ATOM 1547 CD2 LEU A 217 107.734 216.337 867.860 1.00188.00 C ATOM 1548 N LEU A 218 107.036 214.757 870.159 1.00201.29 N ATOM 1549 CA LEU A 218 106.483 215.066 871.479 1.00201.29 C ATOM 1550 C LEU A 218 105.936 213.873 872.271 1.00201.29 C ATOM 1551 O LEU A 218 106.416 213.584 873.371 1.00201.29 O ATOM 1552 CB LEU A 218 105.390 216.140 871.349 1.00201.57 C ATOM 1553 CG LEU A 218 105.796 217.538 870.854 1.00201.57 C ATOM 1554 CD1 LEU A 218 104.553 218.407 870.696 1.00201.57 C ATOM 1555 CD2 LEU A 218 106.773 218.180 871.831 1.00201.57 C ATOM 1556 N ARG A 219 104.943 213.178 871.720 1.00201.57 N ATOM 1557 CA ARG A 219 104.334 212.044 872.417 1.00201.57 C ATOM 1558 C ARG A 219 104.415 210.710 871.659 1.00201.57 C ATOM 1559 O ARG A 219 105.170 210.575 870.691 1.00201.57 O ATOM 1560 CB ARG A 219 102.870 212.368 872.713 1.00176.62 C ATOM 1561 CG ARG A 219 102.024 212.445 871.462 1.00176.62 C ATOM 1562 CD ARG A 219 100.689 213.091 871.717 1.00176.62 C ATOM 1563 NE ARG A 219 100.843 214.494 872.076 1.00176.62 N ATOM 1564 CZ ARG A 219 99.841 215.360 872.122 1.00176.62 C ATOM 1565 NH1 ARG A 219 98.607 214.966 871.829 1.00176.62 N ATOM 1566 NH2 ARG A 219 100.071 216.622 872.456 1.00176.62 N ATOM 1567 N SER A 220 103.630 209.731 872.117 1.00181.77 N ATOM 1568 CA SER A 220 103.581 208.398 871.507 1.00181.77 C ATOM 1569 C SER A 220 102.151 208.060 871.059 1.00181.77 C ATOM 1570 O SER A 220 101.201 208.211 871.828 1.00181.77 O ATOM 1571 CB SER A 220 104.083 207.344 872.506 1.00108.93 C ATOM 1572 OG SER A 220 105.448 207.551 872.845 1.00122.78 O ATOM 1573 N TYR A 221 102.004 207.592 869.819 1.00201.57 N ATOM 1574 CA TYR A 221 100.683 207.265 869.275 1.00201.57 C ATOM 1575 C TYR A 221 100.492 205.776 869.001 1.00201.57 C ATOM 1576 O TYR A 221 101.430 205.099 868.606 1.00201.57 O ATOM 1577 CB TYR A 221 100.445 208.027 867.970 1.00201.12 C ATOM 1578 CG TYR A 221 100.711 209.511 868.061 1.00201.12 C ATOM 1579 CD1 TYR A 221 102.015 209.999 868.156 1.00201.12 C ATOM 1580 CE1 TYR A 221 102.268 211.362 868.261 1.00201.12 C ATOM 1581 CZ TYR A 221 101.211 212.258 868.269 1.00201.12 C ATOM 1582 OH TYR A 221 101.463 213.604 868.389 1.00201.12 O ATOM 1583 CE2 TYR A 221 99.904 211.798 868.174 1.00201.12 C ATOM 1584 CD2 TYR A 221 99.661 210.429 868.069 1.00201.12 C ATOM 1585 N LEU A 222 99.264 205.286 869.186 1.00154.89 N ATOM 1586 CA LEU A 222 98.926 203.880 868.963 1.00154.89 C ATOM 1587 C LEU A 222 97.483 203.737 868.498 1.00154.89 C ATOM 1588 O LEU A 222 96.560 204.028 869.256 1.00154.89 O ATOM 1589 CB LEU A 222 99.099 203.087 870.255 1.00201.57 C ATOM 1590 CG LEU A 222 100.441 203.097 870.933 1.00201.57 C ATOM 1591 CD1 LEU A 222 100.564 202.208 872.108 1.00169.73 C ATOM 1592 CD2 LEU A 222 101.312 202.557 869.954 1.00169.73 C ATOM 1593 N ALA A 223 97.298 203.277 867.257 1.00201.26 N ATOM 1594 CA ALA A 223 95.960 203.096 866.684 1.00201.26 C ATOM 1595 C ALA A 223 95.559 201.619 866.683 1.00201.26 C ATOM 1596 O ALA A 223 96.082 200.827 865.896 1.00201.26 O ATOM 1597 CB ALA A 223 95.922 203.643 865.258 1.00201.57 C ATOM 1598 N SER A 224 94.622 201.262 867.558 1.00168.83 N ATOM 1599 CA SER A 224 94.158 199.884 867.662 1.00168.83 C ATOM 1600 C SER A 224 92.801 199.647 867.001 1.00168.83 C ATOM 1601 O SER A 224 91.763 200.058 867.517 1.00168.83 O ATOM 1602 CB SER A 224 94.105 199.449 869.137 1.00118.41 C ATOM 1603 OG SER A 224 93.269 200.288 869.918 1.00118.41 O ATOM 1604 N VAL A 225 92.827 198.985 865.849 1.00201.57 N ATOM 1605 CA VAL A 225 91.614 198.655 865.105 1.00201.57 C ATOM 1606 C VAL A 225 90.999 197.397 865.716 1.00201.57 C ATOM 1607 O VAL A 225 91.708 196.599 866.334 1.00201.57 O ATOM 1608 CB VAL A 225 91.940 198.415 863.609 1.00136.84 C ATOM 1609 CG1 VAL A 225 90.989 197.403 863.011 1.00136.84 C ATOM 1610 CG2 VAL A 225 91.848 199.727 862.850 1.00136.84 C ATOM 1611 N SER A 226 89.691 197.213 865.545 1.00159.52 N ATOM 1612 CA SER A 226 89.020 196.046 866.116 1.00159.52 C ATOM 1613 C SER A 226 87.909 195.445 865.251 1.00159.52 C ATOM 1614 O SER A 226 87.714 195.832 864.095 1.00159.52 O ATOM 1615 CB SER A 226 88.457 196.406 867.500 1.00201.50 C ATOM 1616 OG SER A 226 87.904 195.275 868.155 1.00201.50 O ATOM 1617 N GLN A 227 87.196 194.483 865.834 1.00146.64 N ATOM 1618 CA GLN A 227 86.101 193.792 865.166 1.00146.64 C ATOM 1619 C GLN A 227 84.822 194.603 865.341 1.00146.64 C ATOM 1620 O GLN A 227 83.975 194.640 864.446 1.00146.64 O ATOM 1621 CB GLN A 227 85.916 192.397 865.776 1.00181.53 C ATOM 1622 CG GLN A 227 85.057 191.421 864.964 1.00181.53 C ATOM 1623 CD GLN A 227 85.856 190.653 863.917 1.00181.53 C ATOM 1624 OE1 GLN A 227 85.357 190.631 862.686 1.00181.53 O ATOM 1625 NE2 GLN A 227 86.902 190.074 864.217 1.00181.53 N ATOM 1626 N ASP A 228 84.696 195.255 866.498 1.00158.94 N ATOM 1627 CA ASP A 228 83.519 196.068 866.804 1.00158.94 C ATOM 1628 C ASP A 228 83.450 197.338 865.953 1.00158.94 C ATOM 1629 O ASP A 228 82.684 198.258 866.246 1.00158.94 O ATOM 1630 CB ASP A 228 83.476 196.412 868.304 1.00145.52 C ATOM 1631 CG ASP A 228 84.670 197.234 868.770 1.00145.52 C ATOM 1632 OD1 ASP A 228 85.815 196.839 868.482 1.00145.52 O ATOM 1633 OD2 ASP A 228 84.464 198.271 869.444 1.00145.52 O ATOM 1634 N ARG A 229 84.256 197.366 864.895 1.00180.77 N ATOM 1635 CA ARG A 229 84.313 198.481 863.953 1.00180.77 C ATOM 1636 C ARG A 229 84.675 199.857 864.524 1.00180.77 C ATOM 1637 O ARG A 229 84.070 200.866 864.160 1.00180.77 O ATOM 1638 CB ARG A 229 82.995 198.556 863.173 1.00189.59 C ATOM 1639 CG ARG A 229 82.787 197.383 862.217 1.00189.59 C ATOM 1640 CD ARG A 229 81.357 197.269 861.695 1.00189.59 C ATOM 1641 NE ARG A 229 80.469 196.566 862.623 1.00189.59 N ATOM 1642 CZ ARG A 229 80.064 197.046 863.794 1.00189.59 C ATOM 1643 NH1 ARG A 229 80.460 198.244 864.196 1.00189.59 N ATOM 1644 NH2 ARG A 229 79.264 196.327 864.571 1.00189.59 N ATOM 1645 N THR A 230 85.667 199.890 865.412 1.00179.37 N ATOM 1646 CA THR A 230 86.145 201.138 866.008 1.00179.37 C ATOM 1647 C THR A 230 87.666 201.198 865.928 1.00179.37 C ATOM 1648 O THR A 230 88.325 200.178 865.724 1.00179.37 O ATOM 1649 CB THR A 230 85.742 201.283 867.509 1.00154.32 C ATOM 1650 OG1 THR A 230 85.865 200.019 868.171 1.00148.44 O ATOM 1651 CG2 THR A 230 84.322 201.816 867.642 1.00153.51 C ATOM 1652 N CYS A 231 88.219 202.399 866.073 1.00201.57 N ATOM 1653 CA CYS A 231 89.668 202.594 866.051 1.00201.57 C ATOM 1654 C CYS A 231 90.035 203.540 867.186 1.00201.57 C ATOM 1655 O CYS A 231 89.839 204.748 867.080 1.00201.57 O ATOM 1656 CB CYS A 231 90.130 203.192 864.715 1.00184.48 C ATOM 1657 SG CYS A 231 91.918 203.555 864.622 1.00189.95 S ATOM 1658 N ILE A 232 90.560 202.991 868.275 1.00136.22 N ATOM 1659 CA ILE A 232 90.938 203.810 869.417 1.00130.57 C ATOM 1660 C ILE A 232 92.388 204.246 869.320 1.00135.65 C ATOM 1661 O ILE A 232 93.264 203.450 868.995 1.00136.30 O ATOM 1662 CB ILE A 232 90.737 203.053 870.742 1.00149.33 C ATOM 1663 CG1 ILE A 232 89.270 202.646 870.886 1.00147.38 C ATOM 1664 CD1 ILE A 232 88.958 201.918 872.170 1.00139.64 C ATOM 1665 CG2 ILE A 232 91.160 203.931 871.908 1.00144.32 C ATOM 1666 N ILE A 233 92.637 205.516 869.613 1.00138.34 N ATOM 1667 CA ILE A 233 93.983 206.053 869.547 1.00139.17 C ATOM 1668 C ILE A 233 94.520 206.359 870.936 1.00138.42 C ATOM 1669 O ILE A 233 94.033 207.250 871.630 1.00133.95 O ATOM 1670 CB ILE A 233 94.012 207.309 868.667 1.00150.22 C ATOM 1671 CG1 ILE A 233 93.597 206.918 867.245 1.00151.05 C ATOM 1672 CD1 ILE A 233 93.325 208.078 866.335 1.00137.50 C ATOM 1673 CG2 ILE A 233 95.404 207.934 868.672 1.00149.89 C ATOM 1674 N TRP A 234 95.533 205.600 871.328 1.00158.24 N ATOM 1675 CA TRP A 234 96.150 205.756 872.632 1.00158.24 C ATOM 1676 C TRP A 234 97.349 206.681 872.562 1.00158.24 C ATOM 1677 O TRP A 234 98.469 206.238 872.307 1.00158.24 O ATOM 1678 CB TRP A 234 96.573 204.386 873.156 1.00189.47 C ATOM 1679 CG TRP A 234 95.458 203.396 873.092 1.00189.47 C ATOM 1680 CD1 TRP A 234 95.214 202.492 872.100 1.00189.47 C ATOM 1681 NE1 TRP A 234 94.053 201.805 872.362 1.00189.47 N ATOM 1682 CE2 TRP A 234 93.524 202.261 873.540 1.00189.47 C ATOM 1683 CZ2 TRP A 234 92.363 201.880 874.215 1.00189.47 C ATOM 1684 CH2 TRP A 234 92.077 202.521 875.394 1.00189.47 C ATOM 1685 CZ3 TRP A 234 92.916 203.527 875.905 1.00189.47 C ATOM 1686 CE3 TRP A 234 94.070 203.907 875.234 1.00189.47 C ATOM 1687 CD2 TRP A 234 94.386 203.268 874.028 1.00189.47 C ATOM 1688 N THR A 235 97.108 207.972 872.782 1.00160.54 N ATOM 1689 CA THR A 235 98.178 208.960 872.746 1.00157.90 C ATOM 1690 C THR A 235 98.629 209.258 874.173 1.00163.60 C ATOM 1691 O THR A 235 97.876 209.809 874.976 1.00163.60 O ATOM 1692 CB THR A 235 97.720 210.280 872.076 1.00182.18 C ATOM 1693 OG1 THR A 235 96.919 211.032 872.994 1.00182.18 O ATOM 1694 CG2 THR A 235 96.898 209.990 870.827 1.00182.18 C ATOM 1695 N GLN A 236 99.864 208.880 874.482 1.00201.57 N ATOM 1696 CA GLN A 236 100.414 209.100 875.809 1.00201.57 C ATOM 1697 C GLN A 236 101.313 210.330 875.806 1.00201.57 C ATOM 1698 O GLN A 236 102.287 210.397 875.053 1.00201.57 O ATOM 1699 CB GLN A 236 101.207 207.871 876.258 1.00181.95 C ATOM 1700 CG GLN A 236 101.771 207.953 877.669 1.00181.95 C ATOM 1701 CD GLN A 236 102.466 206.674 878.088 1.00181.95 C ATOM 1702 OE1 GLN A 236 103.335 206.171 877.378 1.00181.95 O ATOM 1703 NE2 GLN A 236 102.091 206.145 879.246 1.00181.95 N ATOM 1704 N ASP A 237 100.971 211.301 876.647 1.00201.57 N ATOM 1705 CA ASP A 237 101.729 212.541 876.765 1.00201.57 C ATOM 1706 C ASP A 237 103.223 212.229 876.715 1.00201.57 C ATOM 1707 O ASP A 237 103.918 212.613 875.772 1.00201.57 O ATOM 1708 CB ASP A 237 101.382 213.231 878.086 1.00189.99 C ATOM 1709 CG ASP A 237 99.933 213.007 878.499 1.00189.99 C ATOM 1710 OD1 ASP A 237 99.026 213.262 877.676 1.00189.99 O ATOM 1711 OD2 ASP A 237 99.702 212.576 879.649 1.00189.99 O ATOM 1712 N ASN A 238 103.704 211.530 877.739 1.00197.05 N ATOM 1713 CA ASN A 238 105.107 211.133 877.821 1.00197.05 C ATOM 1714 C ASN A 238 105.270 209.864 878.662 1.00197.05 C ATOM 1715 O ASN A 238 104.329 209.082 878.814 1.00197.05 O ATOM 1716 CB ASN A 238 105.975 212.268 878.394 1.00201.57 C ATOM 1717 CG ASN A 238 105.514 212.734 879.767 1.00201.57 C ATOM 1718 OD1 ASN A 238 104.201 212.804 879.966 1.00201.57 O ATOM 1719 ND2 ASN A 238 106.334 213.047 880.634 1.00201.57 N ATOM 1720 N GLU A 239 106.466 209.665 879.209 1.00190.01 N ATOM 1721 CA GLU A 239 106.759 208.486 880.017 1.00190.01 C ATOM 1722 C GLU A 239 105.945 208.380 881.300 1.00190.01 C ATOM 1723 O GLU A 239 106.143 207.450 882.085 1.00190.01 O ATOM 1724 CB GLU A 239 108.239 208.462 880.383 1.00201.57 C ATOM 1725 CG GLU A 239 109.178 208.565 879.205 1.00201.57 C ATOM 1726 CD GLU A 239 110.621 208.402 879.622 1.00201.57 C ATOM 1727 OE1 GLU A 239 111.091 209.197 880.462 1.00201.57 O ATOM 1728 OE2 GLU A 239 111.282 207.472 879.115 1.00201.57 O ATOM 1729 N GLN A 240 105.035 209.322 881.522 1.00201.57 N ATOM 1730 CA GLN A 240 104.229 209.314 882.739 1.00201.57 C ATOM 1731 C GLN A 240 102.713 209.260 882.524 1.00201.57 C ATOM 1732 O GLN A 240 102.117 208.180 882.552 1.00201.57 O ATOM 1733 CB GLN A 240 104.598 210.527 883.598 1.00201.57 C ATOM 1734 CG GLN A 240 106.027 210.503 884.113 1.00201.57 C ATOM 1735 CD GLN A 240 106.357 211.692 884.994 1.00201.57 C ATOM 1736 OE1 GLN A 240 105.433 212.645 885.083 1.00201.57 O ATOM 1737 NE2 GLN A 240 107.432 211.751 885.592 1.00201.57 N ATOM 1738 N GLY A 241 102.096 210.426 882.326 1.00201.57 N ATOM 1739 CA GLY A 241 100.658 210.489 882.117 1.00201.57 C ATOM 1740 C GLY A 241 100.136 209.341 881.274 1.00201.57 C ATOM 1741 O GLY A 241 100.489 209.228 880.099 1.00201.57 O ATOM 1742 N PRO A 242 99.296 208.464 881.849 1.00188.73 N ATOM 1743 CA PRO A 242 98.760 207.337 881.084 1.00188.73 C ATOM 1744 C PRO A 242 98.093 207.764 879.777 1.00188.73 C ATOM 1745 O PRO A 242 97.762 208.935 879.582 1.00188.73 O ATOM 1746 CB PRO A 242 97.793 206.672 882.071 1.00152.52 C ATOM 1747 CG PRO A 242 97.401 207.791 882.993 1.00152.52 C ATOM 1748 CD PRO A 242 98.706 208.516 883.195 1.00152.52 C ATOM 1749 N TRP A 243 97.909 206.800 878.884 1.00201.57 N ATOM 1750 CA TRP A 243 97.313 207.038 877.574 1.00201.57 C ATOM 1751 C TRP A 243 95.999 207.815 877.600 1.00201.57 C ATOM 1752 O TRP A 243 95.397 208.018 878.655 1.00201.57 O ATOM 1753 CB TRP A 243 97.119 205.695 876.861 1.00197.14 C ATOM 1754 CG TRP A 243 98.340 204.825 876.961 1.00197.14 C ATOM 1755 CD1 TRP A 243 98.698 204.025 878.013 1.00197.14 C ATOM 1756 NE1 TRP A 243 99.937 203.474 877.787 1.00197.14 N ATOM 1757 CE2 TRP A 243 100.402 203.907 876.575 1.00197.14 C ATOM 1758 CZ2 TRP A 243 101.604 203.622 875.910 1.00197.14 C ATOM 1759 CH2 TRP A 243 101.811 204.209 874.686 1.00197.14 C ATOM 1760 CZ3 TRP A 243 100.853 205.058 874.109 1.00197.14 C ATOM 1761 CE3 TRP A 243 99.656 205.342 874.767 1.00197.14 C ATOM 1762 CD2 TRP A 243 99.419 204.758 876.019 1.00197.14 C ATOM 1763 N LYS A 244 95.568 208.259 876.423 1.00196.50 N ATOM 1764 CA LYS A 244 94.325 209.008 876.288 1.00196.50 C ATOM 1765 C LYS A 244 93.456 208.384 875.198 1.00196.50 C ATOM 1766 O LYS A 244 93.820 208.379 874.021 1.00196.50 O ATOM 1767 CB LYS A 244 94.624 210.473 875.950 1.00166.15 C ATOM 1768 CG LYS A 244 95.372 211.217 877.051 1.00168.89 C ATOM 1769 CD LYS A 244 95.521 212.694 876.721 1.00175.56 C ATOM 1770 CE LYS A 244 96.114 213.457 877.891 1.00177.54 C ATOM 1771 NZ LYS A 244 96.163 214.917 877.623 1.00176.22 N ATOM 1772 N LYS A 245 92.309 207.852 875.606 1.00193.14 N ATOM 1773 CA LYS A 245 91.373 207.207 874.691 1.00193.14 C ATOM 1774 C LYS A 245 90.781 208.245 873.742 1.00193.14 C ATOM 1775 O LYS A 245 90.432 209.345 874.168 1.00193.14 O ATOM 1776 CB LYS A 245 90.260 206.536 875.499 1.00183.83 C ATOM 1777 CG LYS A 245 89.654 205.299 874.865 1.00191.76 C ATOM 1778 CD LYS A 245 88.710 204.623 875.848 1.00186.07 C ATOM 1779 CE LYS A 245 88.250 203.265 875.351 1.00194.92 C ATOM 1780 NZ LYS A 245 87.392 202.568 876.360 1.00186.82 N ATOM 1781 N THR A 246 90.671 207.898 872.460 1.00154.75 N ATOM 1782 CA THR A 246 90.126 208.821 871.463 1.00154.75 C ATOM 1783 C THR A 246 89.603 208.094 870.229 1.00154.75 C ATOM 1784 O THR A 246 90.280 208.061 869.204 1.00154.75 O ATOM 1785 CB THR A 246 91.197 209.828 870.983 1.00129.72 C ATOM 1786 OG1 THR A 246 91.788 210.482 872.111 1.00139.03 O ATOM 1787 CG2 THR A 246 90.571 210.870 870.051 1.00125.47 C ATOM 1788 N LEU A 247 88.410 207.517 870.315 1.00146.14 N ATOM 1789 CA LEU A 247 87.832 206.815 869.169 1.00142.02 C ATOM 1790 C LEU A 247 87.969 207.701 867.929 1.00141.00 C ATOM 1791 O LEU A 247 87.319 208.744 867.853 1.00142.22 O ATOM 1792 CB LEU A 247 86.349 206.519 869.414 1.00183.58 C ATOM 1793 CG LEU A 247 85.967 205.690 870.644 1.00184.08 C ATOM 1794 CD1 LEU A 247 84.452 205.682 870.791 1.00184.00 C ATOM 1795 CD2 LEU A 247 86.509 204.272 870.511 1.00175.89 C ATOM 1796 N LEU A 248 88.815 207.292 866.978 1.00201.49 N ATOM 1797 CA LEU A 248 89.045 208.046 865.736 1.00201.49 C ATOM 1798 C LEU A 248 87.782 208.850 865.437 1.00201.49 C ATOM 1799 O LEU A 248 87.718 210.041 865.741 1.00201.49 O ATOM 1800 CB LEU A 248 89.361 207.081 864.580 1.00182.27 C ATOM 1801 CG LEU A 248 90.034 207.622 863.312 1.00182.27 C ATOM 1802 CD1 LEU A 248 91.440 208.118 863.627 1.00182.27 C ATOM 1803 CD2 LEU A 248 90.096 206.518 862.271 1.00182.27 C ATOM 1804 N LYS A 249 86.783 208.208 864.840 1.00163.26 N ATOM 1805 CA LYS A 249 85.514 208.879 864.597 1.00173.25 C ATOM 1806 C LYS A 249 84.537 208.139 865.502 1.00175.18 C ATOM 1807 O LYS A 249 84.768 206.975 865.827 1.00178.39 O ATOM 1808 CB LYS A 249 85.096 208.809 863.123 1.00114.83 C ATOM 1809 CG LYS A 249 84.789 207.446 862.543 1.00123.25 C ATOM 1810 CD LYS A 249 84.281 207.654 861.122 1.00127.83 C ATOM 1811 CE LYS A 249 84.101 206.364 860.366 1.00131.27 C ATOM 1812 NZ LYS A 249 83.750 206.661 858.947 1.00134.90 N ATOM 1813 N GLU A 250 83.463 208.802 865.929 1.00146.37 N ATOM 1814 CA GLU A 250 82.514 208.173 866.845 1.00146.37 C ATOM 1815 C GLU A 250 81.377 207.356 866.241 1.00146.37 C ATOM 1816 O GLU A 250 80.323 207.192 866.856 1.00146.37 O ATOM 1817 CB GLU A 250 81.943 209.221 867.793 1.00190.27 C ATOM 1818 CG GLU A 250 83.003 209.935 868.601 1.00190.27 C ATOM 1819 CD GLU A 250 82.409 210.813 869.673 1.00190.27 C ATOM 1820 OE1 GLU A 250 81.469 211.573 869.361 1.00188.84 O ATOM 1821 OE2 GLU A 250 82.881 210.747 870.827 1.00190.27 O ATOM 1822 N GLU A 251 81.595 206.836 865.042 1.00201.57 N ATOM 1823 CA GLU A 251 80.603 206.005 864.383 1.00201.57 C ATOM 1824 C GLU A 251 81.305 204.748 863.907 1.00201.57 C ATOM 1825 O GLU A 251 82.520 204.743 863.702 1.00201.57 O ATOM 1826 CB GLU A 251 79.991 206.738 863.199 1.00201.57 C ATOM 1827 CG GLU A 251 79.093 207.877 863.595 1.00201.57 C ATOM 1828 CD GLU A 251 79.140 208.996 862.589 1.00201.57 C ATOM 1829 OE1 GLU A 251 79.599 208.743 861.454 1.00201.57 O ATOM 1830 OE2 GLU A 251 78.722 210.121 862.928 1.00201.57 O ATOM 1831 N LYS A 252 80.541 203.679 863.736 1.00181.32 N ATOM 1832 CA LYS A 252 81.106 202.416 863.292 1.00181.32 C ATOM 1833 C LYS A 252 81.357 202.426 861.789 1.00181.32 C ATOM 1834 O LYS A 252 80.609 203.046 861.030 1.00181.32 O ATOM 1835 CB LYS A 252 80.152 201.276 863.655 1.00192.67 C ATOM 1836 CG LYS A 252 79.830 201.198 865.143 1.00192.67 C ATOM 1837 CD LYS A 252 78.847 200.081 865.442 1.00192.67 C ATOM 1838 CE LYS A 252 78.845 199.742 866.921 1.00192.67 C ATOM 1839 NZ LYS A 252 78.058 198.510 867.201 1.00192.67 N ATOM 1840 N PHE A 253 82.422 201.758 861.365 1.00167.37 N ATOM 1841 CA PHE A 253 82.735 201.682 859.946 1.00167.37 C ATOM 1842 C PHE A 253 81.792 200.595 859.407 1.00167.37 C ATOM 1843 O PHE A 253 81.543 199.595 860.084 1.00167.37 O ATOM 1844 CB PHE A 253 84.220 201.320 859.737 1.00167.60 C ATOM 1845 CG PHE A 253 85.189 202.303 860.378 1.00165.66 C ATOM 1846 CD1 PHE A 253 85.413 202.290 861.757 1.00165.56 C ATOM 1847 CE1 PHE A 253 86.283 203.210 862.358 1.00161.22 C ATOM 1848 CZ PHE A 253 86.940 204.150 861.575 1.00164.05 C ATOM 1849 CE2 PHE A 253 86.727 204.173 860.199 1.00165.81 C ATOM 1850 CD2 PHE A 253 85.857 203.251 859.606 1.00165.05 C ATOM 1851 N PRO A 254 81.236 200.795 858.195 1.00174.68 N ATOM 1852 CA PRO A 254 80.306 199.878 857.518 1.00174.68 C ATOM 1853 C PRO A 254 80.631 198.380 857.500 1.00174.68 C ATOM 1854 O PRO A 254 79.925 197.599 856.860 1.00174.68 O ATOM 1855 CB PRO A 254 80.186 200.476 856.108 1.00171.88 C ATOM 1856 CG PRO A 254 81.409 201.335 855.964 1.00172.66 C ATOM 1857 CD PRO A 254 81.537 201.944 857.330 1.00170.78 C ATOM 1858 N ASP A 255 81.687 197.987 858.208 1.00176.12 N ATOM 1859 CA ASP A 255 82.094 196.586 858.298 1.00176.12 C ATOM 1860 C ASP A 255 83.369 196.486 859.134 1.00176.12 C ATOM 1861 O ASP A 255 84.216 197.382 859.102 1.00176.12 O ATOM 1862 CB ASP A 255 82.335 195.995 856.901 1.00201.57 C ATOM 1863 CG ASP A 255 82.291 194.473 856.894 1.00201.57 C ATOM 1864 OD1 ASP A 255 81.259 193.903 857.313 1.00201.57 O ATOM 1865 OD2 ASP A 255 83.283 193.847 856.467 1.00201.57 O ATOM 1866 N VAL A 256 83.491 195.395 859.883 1.00160.99 N ATOM 1867 CA VAL A 256 84.645 195.151 860.747 1.00159.68 C ATOM 1868 C VAL A 256 85.986 195.575 860.134 1.00160.99 C ATOM 1869 O VAL A 256 86.205 195.422 858.931 1.00160.99 O ATOM 1870 CB VAL A 256 84.716 193.658 861.136 1.00201.57 C ATOM 1871 CG1 VAL A 256 85.943 193.404 861.988 1.00201.57 C ATOM 1872 CG2 VAL A 256 83.446 193.255 861.879 1.00201.57 C ATOM 1873 N LEU A 257 86.876 196.104 860.975 1.00153.29 N ATOM 1874 CA LEU A 257 88.199 196.558 860.536 1.00153.29 C ATOM 1875 C LEU A 257 89.283 195.502 860.808 1.00152.43 C ATOM 1876 O LEU A 257 89.207 194.752 861.787 1.00153.29 O ATOM 1877 CB LEU A 257 88.569 197.871 861.238 1.00122.63 C ATOM 1878 CG LEU A 257 87.654 199.093 861.136 1.00127.90 C ATOM 1879 CD1 LEU A 257 88.237 200.206 862.003 1.00127.48 C ATOM 1880 CD2 LEU A 257 87.509 199.542 859.680 1.00128.93 C ATOM 1881 N TRP A 258 90.299 195.464 859.943 1.00152.20 N ATOM 1882 CA TRP A 258 91.391 194.490 860.051 1.00152.20 C ATOM 1883 C TRP A 258 92.757 195.084 860.433 1.00152.20 C ATOM 1884 O TRP A 258 93.206 194.955 861.572 1.00152.20 O ATOM 1885 CB TRP A 258 91.542 193.725 858.721 1.00151.21 C ATOM 1886 CG TRP A 258 90.272 193.055 858.211 1.00151.89 C ATOM 1887 CD1 TRP A 258 89.693 193.220 856.977 1.00151.89 C ATOM 1888 NE1 TRP A 258 88.555 192.453 856.880 1.00151.89 N ATOM 1889 CE2 TRP A 258 88.376 191.771 858.056 1.00151.89 C ATOM 1890 CZ2 TRP A 258 87.372 190.874 858.431 1.00151.89 C ATOM 1891 CH2 TRP A 258 87.443 190.332 859.691 1.00151.89 C ATOM 1892 CZ3 TRP A 258 88.485 190.660 860.574 1.00151.89 C ATOM 1893 CE3 TRP A 258 89.486 191.553 860.201 1.00148.53 C ATOM 1894 CD2 TRP A 258 89.438 192.121 858.917 1.00151.89 C ATOM 1895 N ARG A 259 93.406 195.724 859.460 1.00158.72 N ATOM 1896 CA ARG A 259 94.731 196.322 859.633 1.00158.72 C ATOM 1897 C ARG A 259 94.764 197.796 860.071 1.00158.72 C ATOM 1898 O ARG A 259 93.801 198.541 859.881 1.00158.72 O ATOM 1899 CB ARG A 259 95.527 196.164 858.330 1.00139.00 C ATOM 1900 CG ARG A 259 95.914 194.727 858.004 1.00139.00 C ATOM 1901 CD ARG A 259 97.044 194.256 858.911 1.00139.00 C ATOM 1902 NE ARG A 259 97.242 192.806 858.881 1.00139.00 N ATOM 1903 CZ ARG A 259 97.500 192.102 857.784 1.00139.00 C ATOM 1904 NH1 ARG A 259 97.594 192.707 856.612 1.00139.00 N ATOM 1905 NH2 ARG A 259 97.664 190.788 857.864 1.00139.00 N ATOM 1906 N ALA A 260 95.894 198.203 860.653 1.00150.96 N ATOM 1907 CA ALA A 260 96.114 199.572 861.125 1.00150.96 C ATOM 1908 C ALA A 260 97.617 199.869 861.133 1.00150.96 C ATOM 1909 O ALA A 260 98.320 199.551 862.096 1.00150.96 O ATOM 1910 CB ALA A 260 95.540 199.742 862.530 1.00201.57 C ATOM 1911 N SER A 261 98.098 200.495 860.062 1.00201.26 N ATOM 1912 CA SER A 261 99.518 200.805 859.926 1.00201.26 C ATOM 1913 C SER A 261 99.839 202.306 859.900 1.00201.26 C ATOM 1914 O SER A 261 99.143 203.093 859.255 1.00201.26 O ATOM 1915 CB SER A 261 100.051 200.145 858.649 1.00126.79 C ATOM 1916 OG SER A 261 101.463 200.247 858.526 1.00126.79 O ATOM 1917 N TRP A 262 100.900 202.684 860.614 1.00122.11 N ATOM 1918 CA TRP A 262 101.361 204.069 860.672 1.00122.11 C ATOM 1919 C TRP A 262 102.354 204.304 859.544 1.00122.11 C ATOM 1920 O TRP A 262 102.918 203.356 859.008 1.00122.11 O ATOM 1921 CB TRP A 262 102.085 204.345 861.989 1.00143.20 C ATOM 1922 CG TRP A 262 101.211 204.332 863.179 1.00141.50 C ATOM 1923 CD1 TRP A 262 101.251 203.444 864.211 1.00139.79 C ATOM 1924 NE1 TRP A 262 100.317 203.782 865.162 1.00140.05 N ATOM 1925 CE2 TRP A 262 99.650 204.909 864.749 1.00143.19 C ATOM 1926 CZ2 TRP A 262 98.620 205.627 865.366 1.00143.20 C ATOM 1927 CH2 TRP A 262 98.136 206.728 864.710 1.00139.34 C ATOM 1928 CZ3 TRP A 262 98.647 207.124 863.466 1.00136.01 C ATOM 1929 CE3 TRP A 262 99.670 206.412 862.852 1.00131.24 C ATOM 1930 CD2 TRP A 262 100.187 205.280 863.500 1.00139.80 C ATOM 1931 N SER A 263 102.569 205.564 859.181 1.00128.15 N ATOM 1932 CA SER A 263 103.541 205.878 858.140 1.00128.15 C ATOM 1933 C SER A 263 104.773 206.367 858.881 1.00128.15 C ATOM 1934 O SER A 263 104.690 206.763 860.047 1.00128.15 O ATOM 1935 CB SER A 263 103.027 206.964 857.182 1.00136.33 C ATOM 1936 OG SER A 263 103.258 208.270 857.676 1.00136.33 O ATOM 1937 N LEU A 264 105.916 206.320 858.215 1.00113.60 N ATOM 1938 CA LEU A 264 107.159 206.751 858.830 1.00124.85 C ATOM 1939 C LEU A 264 107.185 208.263 858.960 1.00128.47 C ATOM 1940 O LEU A 264 106.957 208.825 860.037 1.00129.35 O ATOM 1941 CB LEU A 264 108.331 206.272 857.980 1.00106.30 C ATOM 1942 CG LEU A 264 108.477 204.757 857.996 1.00108.45 C ATOM 1943 CD1 LEU A 264 109.455 204.294 856.922 1.00105.74 C ATOM 1944 CD2 LEU A 264 108.923 204.335 859.394 1.00111.41 C ATOM 1945 N SER A 265 107.468 208.914 857.842 1.00177.75 N ATOM 1946 CA SER A 265 107.523 210.358 857.787 1.00181.07 C ATOM 1947 C SER A 265 106.086 210.842 857.613 1.00181.38 C ATOM 1948 O SER A 265 105.512 210.691 856.539 1.00186.27 O ATOM 1949 CB SER A 265 108.385 210.784 856.592 1.00196.91 C ATOM 1950 OG SER A 265 108.652 212.174 856.583 1.00196.91 O ATOM 1951 N GLY A 266 105.494 211.387 858.673 1.00122.16 N ATOM 1952 CA GLY A 266 104.134 211.887 858.556 1.00122.16 C ATOM 1953 C GLY A 266 103.106 211.485 859.599 1.00122.16 C ATOM 1954 O GLY A 266 102.002 212.027 859.618 1.00122.16 O ATOM 1955 N ASN A 267 103.452 210.542 860.466 1.00122.42 N ATOM 1956 CA ASN A 267 102.532 210.079 861.507 1.00116.09 C ATOM 1957 C ASN A 267 101.085 209.901 861.011 1.00116.39 C ATOM 1958 O ASN A 267 100.135 210.063 861.769 1.00115.08 O ATOM 1959 CB ASN A 267 102.559 211.043 862.689 1.00144.18 C ATOM 1960 CG ASN A 267 101.998 210.424 863.948 1.00144.98 C ATOM 1961 OD1 ASN A 267 102.520 209.425 864.444 1.00141.85 O ATOM 1962 ND2 ASN A 267 100.927 211.010 864.474 1.00143.53 N ATOM 1963 N VAL A 268 100.935 209.563 859.735 1.00157.80 N ATOM 1964 CA VAL A 268 99.625 209.339 859.129 1.00157.80 C ATOM 1965 C VAL A 268 99.145 207.937 859.477 1.00157.62 C ATOM 1966 O VAL A 268 99.948 207.067 859.793 1.00157.80 O ATOM 1967 CB VAL A 268 99.712 209.421 857.604 1.00 94.73 C ATOM 1968 CG1 VAL A 268 98.357 209.139 856.983 1.00 94.74 C ATOM 1969 CG2 VAL A 268 100.240 210.772 857.195 1.00 96.27 C ATOM 1970 N LEU A 269 97.840 207.709 859.409 1.00135.29 N ATOM 1971 CA LEU A 269 97.312 206.383 859.708 1.00138.26 C ATOM 1972 C LEU A 269 96.479 205.847 858.560 1.00138.26 C ATOM 1973 O LEU A 269 95.643 206.556 857.996 1.00138.26 O ATOM 1974 CB LEU A 269 96.455 206.411 860.975 1.00134.32 C ATOM 1975 CG LEU A 269 95.853 205.059 861.357 1.00134.32 C ATOM 1976 CD1 LEU A 269 96.969 204.108 861.740 1.00134.32 C ATOM 1977 CD2 LEU A 269 94.880 205.228 862.512 1.00134.32 C ATOM 1978 N ALA A 270 96.720 204.589 858.214 1.00194.89 N ATOM 1979 CA ALA A 270 95.976 203.940 857.147 1.00194.89 C ATOM 1980 C ALA A 270 95.155 202.830 857.788 1.00194.89 C ATOM 1981 O ALA A 270 95.662 202.084 858.629 1.00194.89 O ATOM 1982 CB ALA A 270 96.932 203.361 856.107 1.00 57.32 C ATOM 1983 N LEU A 271 93.884 202.735 857.405 1.00120.95 N ATOM 1984 CA LEU A 271 93.007 201.711 857.948 1.00120.95 C ATOM 1985 C LEU A 271 92.401 200.826 856.865 1.00120.95 C ATOM 1986 O LEU A 271 91.624 201.283 856.013 1.00120.95 O ATOM 1987 CB LEU A 271 91.889 202.342 858.789 1.00106.99 C ATOM 1988 CG LEU A 271 92.292 203.009 860.104 1.00109.41 C ATOM 1989 CD1 LEU A 271 91.037 203.481 860.833 1.00110.40 C ATOM 1990 CD2 LEU A 271 93.093 202.033 860.967 1.00108.92 C ATOM 1991 N SER A 272 92.790 199.554 856.903 1.00180.83 N ATOM 1992 CA SER A 272 92.297 198.553 855.970 1.00180.83 C ATOM 1993 C SER A 272 91.006 198.004 856.559 1.00180.83 C ATOM 1994 O SER A 272 90.999 196.927 857.158 1.00180.83 O ATOM 1995 CB SER A 272 93.305 197.407 855.819 1.00164.73 C ATOM 1996 OG SER A 272 94.584 197.869 855.427 1.00164.73 O ATOM 1997 N GLY A 273 89.925 198.765 856.418 1.00175.88 N ATOM 1998 CA GLY A 273 88.643 198.327 856.934 1.00176.15 C ATOM 1999 C GLY A 273 88.130 197.233 856.024 1.00176.15 C ATOM 2000 O GLY A 273 88.327 197.304 854.809 1.00176.15 O ATOM 2001 N GLY A 274 87.487 196.216 856.592 1.00201.57 N ATOM 2002 CA GLY A 274 86.972 195.131 855.774 1.00201.57 C ATOM 2003 C GLY A 274 85.864 195.574 854.830 1.00201.57 C ATOM 2004 O GLY A 274 84.923 194.812 854.583 1.00201.57 O ATOM 2005 N ASP A 275 85.967 196.801 854.308 1.00201.57 N ATOM 2006 CA ASP A 275 84.956 197.332 853.391 1.00201.57 C ATOM 2007 C ASP A 275 85.370 197.726 851.956 1.00201.57 C ATOM 2008 O ASP A 275 84.601 198.394 851.262 1.00201.57 O ATOM 2009 CB ASP A 275 84.159 198.498 854.043 1.00155.64 C ATOM 2010 CG ASP A 275 84.932 199.248 855.134 1.00155.64 C ATOM 2011 OD1 ASP A 275 85.323 198.640 856.157 1.00155.64 O ATOM 2012 OD2 ASP A 275 85.120 200.472 854.976 1.00155.64 O ATOM 2013 N ASN A 276 86.565 197.315 851.523 1.00201.57 N ATOM 2014 CA ASN A 276 87.072 197.545 850.153 1.00201.57 C ATOM 2015 C ASN A 276 88.015 198.703 849.782 1.00201.57 C ATOM 2016 O ASN A 276 88.426 198.807 848.624 1.00201.57 O ATOM 2017 CB ASN A 276 85.911 197.513 849.141 1.00201.57 C ATOM 2018 CG ASN A 276 85.585 196.097 848.664 1.00201.57 C ATOM 2019 OD1 ASN A 276 85.330 195.197 849.471 1.00201.57 O ATOM 2020 ND2 ASN A 276 85.594 195.897 847.346 1.00201.57 N ATOM 2021 N LYS A 277 88.354 199.570 850.733 1.00167.72 N ATOM 2022 CA LYS A 277 89.295 200.668 850.474 1.00166.59 C ATOM 2023 C LYS A 277 89.955 200.996 851.799 1.00163.43 C ATOM 2024 O LYS A 277 89.440 200.652 852.866 1.00160.87 O ATOM 2025 CB LYS A 277 88.590 201.917 849.901 1.00170.15 C ATOM 2026 CG LYS A 277 89.374 203.268 850.006 1.00170.15 C ATOM 2027 CD LYS A 277 90.554 203.464 849.019 1.00170.15 C ATOM 2028 CE LYS A 277 91.205 204.856 849.218 1.00170.15 C ATOM 2029 NZ LYS A 277 92.313 205.189 848.275 1.00170.15 N ATOM 2030 N VAL A 278 91.107 201.642 851.732 1.00178.57 N ATOM 2031 CA VAL A 278 91.804 201.997 852.945 1.00178.57 C ATOM 2032 C VAL A 278 91.667 203.492 853.204 1.00178.57 C ATOM 2033 O VAL A 278 92.061 204.325 852.383 1.00178.57 O ATOM 2034 CB VAL A 278 93.285 201.614 852.846 1.00149.74 C ATOM 2035 CG1 VAL A 278 93.912 201.634 854.230 1.00149.74 C ATOM 2036 CG2 VAL A 278 93.423 200.243 852.196 1.00149.74 C ATOM 2037 N THR A 279 91.080 203.828 854.345 1.00150.45 N ATOM 2038 CA THR A 279 90.909 205.219 854.719 1.00150.45 C ATOM 2039 C THR A 279 92.254 205.744 855.210 1.00150.45 C ATOM 2040 O THR A 279 93.152 204.965 855.521 1.00150.45 O ATOM 2041 CB THR A 279 89.865 205.357 855.838 1.00177.30 C ATOM 2042 OG1 THR A 279 90.221 204.505 856.936 1.00177.30 O ATOM 2043 CG2 THR A 279 88.497 204.957 855.327 1.00177.30 C ATOM 2044 N LEU A 280 92.401 207.061 855.275 1.00143.44 N ATOM 2045 CA LEU A 280 93.651 207.653 855.739 1.00143.44 C ATOM 2046 C LEU A 280 93.345 208.816 856.676 1.00143.44 C ATOM 2047 O LEU A 280 92.731 209.808 856.283 1.00143.44 O ATOM 2048 CB LEU A 280 94.488 208.105 854.533 1.00115.78 C ATOM 2049 CG LEU A 280 95.087 206.965 853.694 1.00115.78 C ATOM 2050 CD1 LEU A 280 95.502 207.451 852.302 1.00115.78 C ATOM 2051 CD2 LEU A 280 96.272 206.385 854.455 1.00115.78 C ATOM 2052 N TRP A 281 93.781 208.687 857.922 1.00162.55 N ATOM 2053 CA TRP A 281 93.505 209.705 858.918 1.00162.55 C ATOM 2054 C TRP A 281 94.742 210.388 859.488 1.00162.55 C ATOM 2055 O TRP A 281 95.687 209.731 859.918 1.00162.55 O ATOM 2056 CB TRP A 281 92.667 209.079 860.039 1.00161.88 C ATOM 2057 CG TRP A 281 91.459 208.358 859.496 1.00161.88 C ATOM 2058 CD1 TRP A 281 91.456 207.233 858.717 1.00161.88 C ATOM 2059 NE1 TRP A 281 90.172 206.915 858.348 1.00161.88 N ATOM 2060 CE2 TRP A 281 89.313 207.831 858.889 1.00161.88 C ATOM 2061 CZ2 TRP A 281 87.920 207.926 858.796 1.00161.88 C ATOM 2062 CH2 TRP A 281 87.312 208.966 859.451 1.00161.88 C ATOM 2063 CZ3 TRP A 281 88.055 209.906 860.193 1.00161.88 C ATOM 2064 CE3 TRP A 281 89.440 209.813 860.286 1.00161.88 C ATOM 2065 CD2 TRP A 281 90.088 208.760 859.626 1.00161.88 C ATOM 2066 N LYS A 282 94.719 211.719 859.486 1.00133.14 N ATOM 2067 CA LYS A 282 95.824 212.523 859.994 1.00133.14 C ATOM 2068 C LYS A 282 95.391 213.361 861.194 1.00133.14 C ATOM 2069 O LYS A 282 94.221 213.715 861.328 1.00133.14 O ATOM 2070 CB LYS A 282 96.352 213.436 858.881 1.00164.17 C ATOM 2071 CG LYS A 282 95.272 214.256 858.195 1.00170.99 C ATOM 2072 CD LYS A 282 95.814 214.974 856.974 1.00171.31 C ATOM 2073 CE LYS A 282 94.727 215.789 856.294 1.00171.31 C ATOM 2074 NZ LYS A 282 95.174 216.329 854.975 1.00171.31 N ATOM 2075 N GLU A 283 96.341 213.672 862.064 1.00166.45 N ATOM 2076 CA GLU A 283 96.046 214.464 863.250 1.00166.45 C ATOM 2077 C GLU A 283 96.189 215.958 862.968 1.00166.45 C ATOM 2078 O GLU A 283 97.145 216.382 862.312 1.00166.45 O ATOM 2079 CB GLU A 283 96.988 214.063 864.392 1.00169.10 C ATOM 2080 CG GLU A 283 96.762 214.838 865.686 1.00169.10 C ATOM 2081 CD GLU A 283 97.733 214.447 866.787 1.00169.10 C ATOM 2082 OE1 GLU A 283 98.957 214.506 866.543 1.00169.10 O ATOM 2083 OE2 GLU A 283 97.274 214.085 867.894 1.00169.10 O ATOM 2084 N ASN A 284 95.231 216.750 863.454 1.00201.57 N ATOM 2085 CA ASN A 284 95.262 218.208 863.288 1.00201.57 C ATOM 2086 C ASN A 284 95.564 218.882 864.631 1.00201.57 C ATOM 2087 O ASN A 284 95.786 218.203 865.637 1.00201.57 O ATOM 2088 CB ASN A 284 93.938 218.731 862.694 1.00159.59 C ATOM 2089 CG ASN A 284 92.709 218.216 863.426 1.00159.59 C ATOM 2090 OD1 ASN A 284 92.541 218.442 864.626 1.00159.59 O ATOM 2091 ND2 ASN A 284 91.835 217.524 862.700 1.00159.59 N ATOM 2092 N LEU A 285 95.575 220.211 864.653 1.00191.70 N ATOM 2093 CA LEU A 285 95.888 220.939 865.878 1.00191.70 C ATOM 2094 C LEU A 285 94.847 220.789 866.983 1.00191.70 C ATOM 2095 O LEU A 285 95.060 221.227 868.115 1.00191.70 O ATOM 2096 CB LEU A 285 96.125 222.414 865.554 1.00126.71 C ATOM 2097 CG LEU A 285 97.254 222.608 864.536 1.00130.25 C ATOM 2098 CD1 LEU A 285 96.728 222.345 863.120 1.00130.25 C ATOM 2099 CD2 LEU A 285 97.813 224.021 864.659 1.00130.25 C ATOM 2100 N GLU A 286 93.724 220.163 866.647 1.00201.48 N ATOM 2101 CA GLU A 286 92.655 219.918 867.608 1.00201.48 C ATOM 2102 C GLU A 286 92.997 218.647 868.385 1.00201.48 C ATOM 2103 O GLU A 286 92.335 218.304 869.369 1.00201.48 O ATOM 2104 CB GLU A 286 91.321 219.720 866.878 1.00201.57 C ATOM 2105 CG GLU A 286 90.444 220.957 866.790 1.00201.57 C ATOM 2106 CD GLU A 286 89.833 221.327 868.129 1.00201.57 C ATOM 2107 OE1 GLU A 286 89.153 220.467 868.732 1.00201.57 O ATOM 2108 OE2 GLU A 286 90.029 222.477 868.577 1.00201.57 O ATOM 2109 N GLY A 287 94.042 217.957 867.934 1.00183.31 N ATOM 2110 CA GLY A 287 94.452 216.720 868.573 1.00183.31 C ATOM 2111 C GLY A 287 93.607 215.575 868.046 1.00183.31 C ATOM 2112 O GLY A 287 93.954 214.404 868.201 1.00183.31 O ATOM 2113 N LYS A 288 92.492 215.932 867.414 1.00201.57 N ATOM 2114 CA LYS A 288 91.560 214.967 866.841 1.00201.57 C ATOM 2115 C LYS A 288 91.996 214.631 865.416 1.00201.57 C ATOM 2116 O LYS A 288 92.712 215.408 864.786 1.00201.57 O ATOM 2117 CB LYS A 288 90.154 215.565 866.862 1.00143.26 C ATOM 2118 CG LYS A 288 89.760 216.054 868.250 1.00146.48 C ATOM 2119 CD LYS A 288 88.500 216.895 868.231 1.00150.15 C ATOM 2120 CE LYS A 288 88.246 217.514 869.597 1.00150.87 C ATOM 2121 NZ LYS A 288 87.013 218.345 869.603 1.00149.65 N ATOM 2122 N TRP A 289 91.556 213.482 864.905 1.00135.22 N ATOM 2123 CA TRP A 289 91.959 213.039 863.574 1.00135.22 C ATOM 2124 C TRP A 289 90.946 213.303 862.470 1.00135.22 C ATOM 2125 O TRP A 289 89.738 213.261 862.689 1.00135.22 O ATOM 2126 CB TRP A 289 92.342 211.556 863.636 1.00159.76 C ATOM 2127 CG TRP A 289 93.303 211.295 864.767 1.00159.76 C ATOM 2128 CD1 TRP A 289 93.021 211.329 866.105 1.00159.76 C ATOM 2129 NE1 TRP A 289 94.169 211.164 866.840 1.00159.76 N ATOM 2130 CE2 TRP A 289 95.225 211.015 865.985 1.00159.76 C ATOM 2131 CZ2 TRP A 289 96.585 210.818 866.256 1.00159.76 C ATOM 2132 CH2 TRP A 289 97.434 210.698 865.186 1.00159.76 C ATOM 2133 CZ3 TRP A 289 96.959 210.767 863.859 1.00159.76 C ATOM 2134 CE3 TRP A 289 95.605 210.960 863.587 1.00159.76 C ATOM 2135 CD2 TRP A 289 94.719 211.087 864.665 1.00159.76 C ATOM 2136 N GLU A 290 91.467 213.569 861.275 1.00139.03 N ATOM 2137 CA GLU A 290 90.655 213.899 860.111 1.00139.03 C ATOM 2138 C GLU A 290 91.100 213.136 858.865 1.00139.03 C ATOM 2139 O GLU A 290 92.284 212.853 858.689 1.00139.03 O ATOM 2140 CB GLU A 290 90.770 215.401 859.869 1.00188.86 C ATOM 2141 CG GLU A 290 89.841 215.972 858.832 1.00188.86 C ATOM 2142 CD GLU A 290 89.907 217.485 858.800 1.00188.86 C ATOM 2143 OE1 GLU A 290 90.590 218.063 859.673 1.00188.86 O ATOM 2144 OE2 GLU A 290 89.276 218.091 857.910 1.00188.86 O ATOM 2145 N PRO A 291 90.157 212.809 857.967 1.00152.11 N ATOM 2146 CA PRO A 291 90.506 212.075 856.746 1.00152.11 C ATOM 2147 C PRO A 291 91.305 212.847 855.697 1.00152.11 C ATOM 2148 O PRO A 291 91.036 214.014 855.422 1.00151.37 O ATOM 2149 CB PRO A 291 89.145 211.628 856.214 1.00101.01 C ATOM 2150 CG PRO A 291 88.258 212.753 856.618 1.00101.01 C ATOM 2151 CD PRO A 291 88.699 213.009 858.051 1.00101.01 C ATOM 2152 N ALA A 292 92.288 212.170 855.119 1.00168.84 N ATOM 2153 CA ALA A 292 93.124 212.740 854.074 1.00168.84 C ATOM 2154 C ALA A 292 93.236 211.685 852.976 1.00168.84 C ATOM 2155 O ALA A 292 93.096 210.494 853.247 1.00113.44 O ATOM 2156 CB ALA A 292 94.493 213.059 854.619 1.00134.30 C ATOM 2157 N GLY A 293 93.478 212.107 851.743 1.00155.03 N ATOM 2158 CA GLY A 293 93.603 211.138 850.670 1.00155.03 C ATOM 2159 C GLY A 293 93.085 211.619 849.332 1.00155.03 C ATOM 2160 O GLY A 293 93.800 212.404 848.677 1.00155.03 O END