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HEADER CHAPERONE 16-MAR-01 1IOK TITLE CRYSTAL STRUCTURE OF CHAPERONIN-60 FROM PARACOCCUS TITLE 2 DENITRIFICANS COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHAPERONIN 60; COMPND 3 CHAIN: A, B, C, D, E, F, G SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PARACOCCUS DENITRIFICANS; SOURCE 3 ORGANISM_TAXID: 266 KEYWDS CHAPERONIN, CHAPERONE EXPDTA X-RAY DIFFRACTION AUTHOR T.A.FUKAMI,M.YOHDA,H.TAGUCHI,M.YOSHIDA,K.MIKI REVDAT 3 24-FEB-09 1IOK 1 VERSN REVDAT 2 21-JAN-03 1IOK 1 REMARK REVDAT 1 03-OCT-01 1IOK 0 JRNL AUTH T.A.FUKAMI,M.YOHDA,H.TAGUCHI,M.YOSHIDA,K.MIKI JRNL TITL CRYSTAL STRUCTURE OF CHAPERONIN-60 FROM PARACOCCUS JRNL TITL 2 DENITRIFICANS. JRNL REF J.MOL.BIOL. V. 312 501 2001 JRNL REFN ISSN 0022-2836 JRNL PMID 11563912 JRNL DOI 10.1006/JMBI.2001.4961 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH T.A.FUKAMI,Y.TAKASUGA,M.SUMI,M.YOHDA,M.YOSHIDA, REMARK 1 AUTH 2 K.MIKI REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY REMARK 1 TITL 2 CHARACTERIZATION OF CHAPERONIN-60 FROM PARACOCCUS REMARK 1 TITL 3 DENITRIFICANS REMARK 1 REF J.CRYST.GROWTH V. 168 297 1996 REMARK 1 REFN ISSN 0022-0248 REMARK 1 DOI 10.1016/0022-0248(96)00336-3 REMARK 2 REMARK 2 RESOLUTION. 3.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 86523 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.204 REMARK 3 FREE R VALUE : 0.235 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 4354 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 : 25102 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) : 73.20 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) : NULL REMARK 3 BOND ANGLES (DEGREES) : NULL REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 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 1IOK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAR-01. REMARK 100 THE RCSB ID CODE IS RCSB005122. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-NOV-97; 06-NOV-97 REMARK 200 TEMPERATURE (KELVIN) : 293; 293 REMARK 200 PH : 9.00 REMARK 200 NUMBER OF CRYSTALS USED : 13 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y REMARK 200 RADIATION SOURCE : PHOTON FACTORY; PHOTON FACTORY REMARK 200 BEAMLINE : BL-6B; BL-6A REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL REMARK 200 WAVELENGTH OR RANGE (A) : 1.000; 1.000 REMARK 200 MONOCHROMATOR : NULL; NULL REMARK 200 OPTICS : NULL; NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE; IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : FUJI; FUJI REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 582211 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 (%) : 98.5 REMARK 200 DATA REDUNDANCY : 5.600 REMARK 200 R MERGE (I) : 0.07300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 20.6000 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 (%) : 99.3 REMARK 200 DATA REDUNDANCY IN SHELL : 5.60 REMARK 200 R MERGE FOR SHELL (I) : 0.46400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.330 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: X-PLOR REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 68.36 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.89 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, LICL, BICINE-NA, PH 9.00, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -Y+1/2,X+1/2,Z+1/2 REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 143.17750 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 143.17750 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 76.73150 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 143.17750 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 143.17750 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 76.73150 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 143.17750 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 143.17750 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 76.73150 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 143.17750 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 143.17750 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 76.73150 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: HEPTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEPTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 16700 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 147820 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -111.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRADECAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 38440 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 290620 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -240.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G, C, 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 BIOMT1 2 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 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 MET A 233 REMARK 465 VAL A 234 REMARK 465 PRO A 235 REMARK 465 LEU A 236 REMARK 465 LEU A 237 REMARK 465 GLU A 238 REMARK 465 SER A 239 REMARK 465 VAL A 240 REMARK 465 ILE A 241 REMARK 465 GLN A 242 REMARK 465 SER A 243 REMARK 465 GLY A 256 REMARK 465 GLU A 257 REMARK 465 ALA A 258 REMARK 465 LEU A 259 REMARK 465 ALA A 260 REMARK 465 THR A 261 REMARK 465 LEU A 262 REMARK 465 VAL A 263 REMARK 465 VAL A 264 REMARK 465 ASN A 265 REMARK 465 LYS A 266 REMARK 465 LEU A 267 REMARK 465 ARG A 268 REMARK 465 GLY A 269 REMARK 465 GLY A 270 REMARK 465 LEU A 271 REMARK 465 LYS A 272 REMARK 465 GLN A 299 REMARK 465 VAL A 300 REMARK 465 ILE A 301 REMARK 465 SER A 302 REMARK 465 GLU A 303 REMARK 465 ASP A 304 REMARK 465 LEU A 305 REMARK 465 GLY A 306 REMARK 465 MET A 307 REMARK 465 LYS A 308 REMARK 465 LEU A 309 REMARK 465 GLU A 310 REMARK 465 ASN A 311 REMARK 465 VAL A 312 REMARK 465 THR A 313 REMARK 465 GLU A 527 REMARK 465 PRO A 528 REMARK 465 LYS A 529 REMARK 465 ALA A 530 REMARK 465 PRO A 531 REMARK 465 ALA A 532 REMARK 465 GLY A 533 REMARK 465 GLY A 534 REMARK 465 MET A 535 REMARK 465 PRO A 536 REMARK 465 ASP A 537 REMARK 465 MET A 538 REMARK 465 GLY A 539 REMARK 465 GLY A 540 REMARK 465 MET A 541 REMARK 465 GLY A 542 REMARK 465 GLY A 543 REMARK 465 MET A 544 REMARK 465 MET A 545 REMARK 465 MET B 1 REMARK 465 MET B 233 REMARK 465 VAL B 234 REMARK 465 PRO B 235 REMARK 465 LEU B 236 REMARK 465 LEU B 237 REMARK 465 GLU B 238 REMARK 465 SER B 239 REMARK 465 VAL B 240 REMARK 465 ILE B 241 REMARK 465 GLN B 242 REMARK 465 SER B 243 REMARK 465 GLY B 256 REMARK 465 GLU B 257 REMARK 465 ALA B 258 REMARK 465 LEU B 259 REMARK 465 ALA B 260 REMARK 465 THR B 261 REMARK 465 LEU B 262 REMARK 465 VAL B 263 REMARK 465 VAL B 264 REMARK 465 ASN B 265 REMARK 465 LYS B 266 REMARK 465 LEU B 267 REMARK 465 ARG B 268 REMARK 465 GLY B 269 REMARK 465 GLY B 270 REMARK 465 LEU B 271 REMARK 465 LYS B 272 REMARK 465 GLN B 299 REMARK 465 VAL B 300 REMARK 465 ILE B 301 REMARK 465 SER B 302 REMARK 465 GLU B 303 REMARK 465 ASP B 304 REMARK 465 LEU B 305 REMARK 465 GLY B 306 REMARK 465 MET B 307 REMARK 465 LYS B 308 REMARK 465 LEU B 309 REMARK 465 GLU B 310 REMARK 465 ASN B 311 REMARK 465 VAL B 312 REMARK 465 THR B 313 REMARK 465 GLU B 527 REMARK 465 PRO B 528 REMARK 465 LYS B 529 REMARK 465 ALA B 530 REMARK 465 PRO B 531 REMARK 465 ALA B 532 REMARK 465 GLY B 533 REMARK 465 GLY B 534 REMARK 465 MET B 535 REMARK 465 PRO B 536 REMARK 465 ASP B 537 REMARK 465 MET B 538 REMARK 465 GLY B 539 REMARK 465 GLY B 540 REMARK 465 MET B 541 REMARK 465 GLY B 542 REMARK 465 GLY B 543 REMARK 465 MET B 544 REMARK 465 MET B 545 REMARK 465 MET C 1 REMARK 465 MET C 233 REMARK 465 VAL C 234 REMARK 465 PRO C 235 REMARK 465 LEU C 236 REMARK 465 LEU C 237 REMARK 465 GLU C 238 REMARK 465 SER C 239 REMARK 465 VAL C 240 REMARK 465 ILE C 241 REMARK 465 GLN C 242 REMARK 465 SER C 243 REMARK 465 GLY C 256 REMARK 465 GLU C 257 REMARK 465 ALA C 258 REMARK 465 LEU C 259 REMARK 465 ALA C 260 REMARK 465 THR C 261 REMARK 465 LEU C 262 REMARK 465 VAL C 263 REMARK 465 VAL C 264 REMARK 465 ASN C 265 REMARK 465 LYS C 266 REMARK 465 LEU C 267 REMARK 465 ARG C 268 REMARK 465 GLY C 269 REMARK 465 GLY C 270 REMARK 465 LEU C 271 REMARK 465 LYS C 272 REMARK 465 GLN C 299 REMARK 465 VAL C 300 REMARK 465 ILE C 301 REMARK 465 SER C 302 REMARK 465 GLU C 303 REMARK 465 ASP C 304 REMARK 465 LEU C 305 REMARK 465 GLY C 306 REMARK 465 MET C 307 REMARK 465 LYS C 308 REMARK 465 LEU C 309 REMARK 465 GLU C 310 REMARK 465 ASN C 311 REMARK 465 VAL C 312 REMARK 465 THR C 313 REMARK 465 GLU C 527 REMARK 465 PRO C 528 REMARK 465 LYS C 529 REMARK 465 ALA C 530 REMARK 465 PRO C 531 REMARK 465 ALA C 532 REMARK 465 GLY C 533 REMARK 465 GLY C 534 REMARK 465 MET C 535 REMARK 465 PRO C 536 REMARK 465 ASP C 537 REMARK 465 MET C 538 REMARK 465 GLY C 539 REMARK 465 GLY C 540 REMARK 465 MET C 541 REMARK 465 GLY C 542 REMARK 465 GLY C 543 REMARK 465 MET C 544 REMARK 465 MET C 545 REMARK 465 MET D 1 REMARK 465 MET D 233 REMARK 465 VAL D 234 REMARK 465 PRO D 235 REMARK 465 LEU D 236 REMARK 465 LEU D 237 REMARK 465 GLU D 238 REMARK 465 SER D 239 REMARK 465 VAL D 240 REMARK 465 ILE D 241 REMARK 465 GLN D 242 REMARK 465 SER D 243 REMARK 465 GLY D 256 REMARK 465 GLU D 257 REMARK 465 ALA D 258 REMARK 465 LEU D 259 REMARK 465 ALA D 260 REMARK 465 THR D 261 REMARK 465 LEU D 262 REMARK 465 VAL D 263 REMARK 465 VAL D 264 REMARK 465 ASN D 265 REMARK 465 LYS D 266 REMARK 465 LEU D 267 REMARK 465 ARG D 268 REMARK 465 GLY D 269 REMARK 465 GLY D 270 REMARK 465 LEU D 271 REMARK 465 LYS D 272 REMARK 465 GLN D 299 REMARK 465 VAL D 300 REMARK 465 ILE D 301 REMARK 465 SER D 302 REMARK 465 GLU D 303 REMARK 465 ASP D 304 REMARK 465 LEU D 305 REMARK 465 GLY D 306 REMARK 465 MET D 307 REMARK 465 LYS D 308 REMARK 465 LEU D 309 REMARK 465 GLU D 310 REMARK 465 ASN D 311 REMARK 465 VAL D 312 REMARK 465 THR D 313 REMARK 465 GLU D 527 REMARK 465 PRO D 528 REMARK 465 LYS D 529 REMARK 465 ALA D 530 REMARK 465 PRO D 531 REMARK 465 ALA D 532 REMARK 465 GLY D 533 REMARK 465 GLY D 534 REMARK 465 MET D 535 REMARK 465 PRO D 536 REMARK 465 ASP D 537 REMARK 465 MET D 538 REMARK 465 GLY D 539 REMARK 465 GLY D 540 REMARK 465 MET D 541 REMARK 465 GLY D 542 REMARK 465 GLY D 543 REMARK 465 MET D 544 REMARK 465 MET D 545 REMARK 465 MET E 1 REMARK 465 MET E 233 REMARK 465 VAL E 234 REMARK 465 PRO E 235 REMARK 465 LEU E 236 REMARK 465 LEU E 237 REMARK 465 GLU E 238 REMARK 465 SER E 239 REMARK 465 VAL E 240 REMARK 465 ILE E 241 REMARK 465 GLN E 242 REMARK 465 SER E 243 REMARK 465 GLY E 256 REMARK 465 GLU E 257 REMARK 465 ALA E 258 REMARK 465 LEU E 259 REMARK 465 ALA E 260 REMARK 465 THR E 261 REMARK 465 LEU E 262 REMARK 465 VAL E 263 REMARK 465 VAL E 264 REMARK 465 ASN E 265 REMARK 465 LYS E 266 REMARK 465 LEU E 267 REMARK 465 ARG E 268 REMARK 465 GLY E 269 REMARK 465 GLY E 270 REMARK 465 LEU E 271 REMARK 465 LYS E 272 REMARK 465 GLN E 299 REMARK 465 VAL E 300 REMARK 465 ILE E 301 REMARK 465 SER E 302 REMARK 465 GLU E 303 REMARK 465 ASP E 304 REMARK 465 LEU E 305 REMARK 465 GLY E 306 REMARK 465 MET E 307 REMARK 465 LYS E 308 REMARK 465 LEU E 309 REMARK 465 GLU E 310 REMARK 465 ASN E 311 REMARK 465 VAL E 312 REMARK 465 THR E 313 REMARK 465 GLU E 527 REMARK 465 PRO E 528 REMARK 465 LYS E 529 REMARK 465 ALA E 530 REMARK 465 PRO E 531 REMARK 465 ALA E 532 REMARK 465 GLY E 533 REMARK 465 GLY E 534 REMARK 465 MET E 535 REMARK 465 PRO E 536 REMARK 465 ASP E 537 REMARK 465 MET E 538 REMARK 465 GLY E 539 REMARK 465 GLY E 540 REMARK 465 MET E 541 REMARK 465 GLY E 542 REMARK 465 GLY E 543 REMARK 465 MET E 544 REMARK 465 MET E 545 REMARK 465 MET F 1 REMARK 465 MET F 233 REMARK 465 VAL F 234 REMARK 465 PRO F 235 REMARK 465 LEU F 236 REMARK 465 LEU F 237 REMARK 465 GLU F 238 REMARK 465 SER F 239 REMARK 465 VAL F 240 REMARK 465 ILE F 241 REMARK 465 GLN F 242 REMARK 465 SER F 243 REMARK 465 GLY F 256 REMARK 465 GLU F 257 REMARK 465 ALA F 258 REMARK 465 LEU F 259 REMARK 465 ALA F 260 REMARK 465 THR F 261 REMARK 465 LEU F 262 REMARK 465 VAL F 263 REMARK 465 VAL F 264 REMARK 465 ASN F 265 REMARK 465 LYS F 266 REMARK 465 LEU F 267 REMARK 465 ARG F 268 REMARK 465 GLY F 269 REMARK 465 GLY F 270 REMARK 465 LEU F 271 REMARK 465 LYS F 272 REMARK 465 GLN F 299 REMARK 465 VAL F 300 REMARK 465 ILE F 301 REMARK 465 SER F 302 REMARK 465 GLU F 303 REMARK 465 ASP F 304 REMARK 465 LEU F 305 REMARK 465 GLY F 306 REMARK 465 MET F 307 REMARK 465 LYS F 308 REMARK 465 LEU F 309 REMARK 465 GLU F 310 REMARK 465 ASN F 311 REMARK 465 VAL F 312 REMARK 465 THR F 313 REMARK 465 GLU F 527 REMARK 465 PRO F 528 REMARK 465 LYS F 529 REMARK 465 ALA F 530 REMARK 465 PRO F 531 REMARK 465 ALA F 532 REMARK 465 GLY F 533 REMARK 465 GLY F 534 REMARK 465 MET F 535 REMARK 465 PRO F 536 REMARK 465 ASP F 537 REMARK 465 MET F 538 REMARK 465 GLY F 539 REMARK 465 GLY F 540 REMARK 465 MET F 541 REMARK 465 GLY F 542 REMARK 465 GLY F 543 REMARK 465 MET F 544 REMARK 465 MET F 545 REMARK 465 MET G 1 REMARK 465 MET G 233 REMARK 465 VAL G 234 REMARK 465 PRO G 235 REMARK 465 LEU G 236 REMARK 465 LEU G 237 REMARK 465 GLU G 238 REMARK 465 SER G 239 REMARK 465 VAL G 240 REMARK 465 ILE G 241 REMARK 465 GLN G 242 REMARK 465 SER G 243 REMARK 465 GLY G 256 REMARK 465 GLU G 257 REMARK 465 ALA G 258 REMARK 465 LEU G 259 REMARK 465 ALA G 260 REMARK 465 THR G 261 REMARK 465 LEU G 262 REMARK 465 VAL G 263 REMARK 465 VAL G 264 REMARK 465 ASN G 265 REMARK 465 LYS G 266 REMARK 465 LEU G 267 REMARK 465 ARG G 268 REMARK 465 GLY G 269 REMARK 465 GLY G 270 REMARK 465 LEU G 271 REMARK 465 LYS G 272 REMARK 465 GLN G 299 REMARK 465 VAL G 300 REMARK 465 ILE G 301 REMARK 465 SER G 302 REMARK 465 GLU G 303 REMARK 465 ASP G 304 REMARK 465 LEU G 305 REMARK 465 GLY G 306 REMARK 465 MET G 307 REMARK 465 LYS G 308 REMARK 465 LEU G 309 REMARK 465 GLU G 310 REMARK 465 ASN G 311 REMARK 465 VAL G 312 REMARK 465 THR G 313 REMARK 465 GLU G 527 REMARK 465 PRO G 528 REMARK 465 LYS G 529 REMARK 465 ALA G 530 REMARK 465 PRO G 531 REMARK 465 ALA G 532 REMARK 465 GLY G 533 REMARK 465 GLY G 534 REMARK 465 MET G 535 REMARK 465 PRO G 536 REMARK 465 ASP G 537 REMARK 465 MET G 538 REMARK 465 GLY G 539 REMARK 465 GLY G 540 REMARK 465 MET G 541 REMARK 465 GLY G 542 REMARK 465 GLY G 543 REMARK 465 MET G 544 REMARK 465 MET G 545 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 ALA A 3 142.52 -34.98 REMARK 500 ASN A 9 -138.80 32.03 REMARK 500 THR A 30 53.29 -102.41 REMARK 500 SER A 43 -5.81 -56.06 REMARK 500 MET A 73 -71.70 -64.62 REMARK 500 ALA A 85 94.62 42.15 REMARK 500 ASP A 87 14.63 -64.93 REMARK 500 SER A 133 45.78 -72.47 REMARK 500 ALA A 134 5.47 -170.55 REMARK 500 ASN A 153 17.63 59.07 REMARK 500 THR A 176 86.56 -151.52 REMARK 500 ASN A 180 -149.15 -118.92 REMARK 500 LYS A 181 -85.12 -110.95 REMARK 500 PHE A 195 -173.64 -65.35 REMARK 500 THR A 206 36.31 -97.38 REMARK 500 ASN A 207 110.37 -29.71 REMARK 500 ASP A 209 -42.21 -148.05 REMARK 500 MET A 211 71.81 -68.40 REMARK 500 LEU A 222 135.69 -171.20 REMARK 500 LYS A 225 -143.69 -99.21 REMARK 500 LEU A 227 50.89 -115.14 REMARK 500 SER A 228 -86.82 -62.08 REMARK 500 PRO A 246 167.02 -46.89 REMARK 500 ASP A 253 171.15 178.99 REMARK 500 ASN A 326 -160.25 -125.81 REMARK 500 ASP A 334 80.49 51.30 REMARK 500 ALA A 336 -25.14 -164.90 REMARK 500 LYS A 339 -37.08 -36.20 REMARK 500 TYR A 360 -65.40 -101.90 REMARK 500 ASP A 361 2.53 -67.84 REMARK 500 ALA A 373 38.25 -89.64 REMARK 500 VAL A 378 99.28 -165.53 REMARK 500 LYS A 475 -6.98 -50.80 REMARK 500 GLU A 484 36.37 75.70 REMARK 500 ALA B 3 142.31 -35.66 REMARK 500 ASN B 9 -139.55 31.99 REMARK 500 THR B 30 52.74 -101.39 REMARK 500 SER B 43 -5.76 -56.04 REMARK 500 MET B 73 -71.75 -64.32 REMARK 500 ALA B 85 94.74 42.33 REMARK 500 ASP B 87 14.56 -65.00 REMARK 500 SER B 133 46.64 -72.46 REMARK 500 ALA B 134 5.36 -171.46 REMARK 500 ASN B 153 17.26 58.59 REMARK 500 THR B 176 86.70 -151.26 REMARK 500 ASN B 180 -149.22 -118.63 REMARK 500 LYS B 181 -84.95 -111.13 REMARK 500 PHE B 195 -173.84 -65.33 REMARK 500 THR B 206 36.48 -97.37 REMARK 500 ASN B 207 110.62 -29.95 REMARK 500 ASP B 209 -42.01 -147.94 REMARK 500 MET B 211 71.69 -68.62 REMARK 500 LEU B 222 135.56 -171.17 REMARK 500 LYS B 225 -144.07 -99.64 REMARK 500 LEU B 227 50.92 -115.13 REMARK 500 SER B 228 -87.21 -61.90 REMARK 500 PRO B 246 167.23 -46.88 REMARK 500 ASP B 253 171.41 179.35 REMARK 500 ASN B 326 -160.41 -125.67 REMARK 500 ASP B 334 80.51 51.14 REMARK 500 ALA B 336 -25.20 -164.97 REMARK 500 LYS B 339 -36.95 -36.18 REMARK 500 TYR B 360 -65.24 -101.90 REMARK 500 ASP B 361 2.52 -68.04 REMARK 500 ALA B 373 38.20 -89.92 REMARK 500 VAL B 378 99.22 -165.71 REMARK 500 LYS B 475 -6.57 -50.56 REMARK 500 GLU B 484 37.28 74.97 REMARK 500 ALA C 3 141.70 -34.85 REMARK 500 ASN C 9 -138.88 32.38 REMARK 500 THR C 30 53.07 -101.52 REMARK 500 SER C 43 -5.76 -55.76 REMARK 500 MET C 73 -71.18 -65.94 REMARK 500 ALA C 85 94.72 42.40 REMARK 500 ASP C 87 14.47 -64.99 REMARK 500 SER C 133 46.58 -72.72 REMARK 500 ALA C 134 6.01 -171.43 REMARK 500 ASN C 153 17.74 59.05 REMARK 500 THR C 176 86.36 -151.20 REMARK 500 ASN C 180 -149.19 -118.55 REMARK 500 LYS C 181 -84.96 -110.95 REMARK 500 PHE C 195 -173.74 -65.44 REMARK 500 THR C 206 36.54 -97.49 REMARK 500 ASN C 207 110.55 -30.12 REMARK 500 ASP C 209 -42.25 -148.06 REMARK 500 MET C 211 71.95 -68.51 REMARK 500 LEU C 222 135.76 -171.32 REMARK 500 LYS C 225 -143.85 -99.45 REMARK 500 LEU C 227 50.78 -115.11 REMARK 500 SER C 228 -87.41 -61.95 REMARK 500 PRO C 246 167.17 -46.81 REMARK 500 ASP C 253 171.03 179.75 REMARK 500 ASN C 326 -160.57 -125.83 REMARK 500 ASP C 334 80.38 51.30 REMARK 500 ALA C 336 -25.28 -164.75 REMARK 500 LYS C 339 -37.17 -36.19 REMARK 500 TYR C 360 -65.54 -101.88 REMARK 500 ASP C 361 2.50 -67.81 REMARK 500 ALA C 373 38.17 -89.77 REMARK 500 VAL C 378 99.14 -165.88 REMARK 500 LYS C 475 -7.27 -50.79 REMARK 500 GLU C 484 36.90 75.39 REMARK 500 ALA D 3 142.26 -35.52 REMARK 500 ASN D 9 -139.19 31.66 REMARK 500 THR D 30 54.24 -102.82 REMARK 500 SER D 43 -5.73 -55.76 REMARK 500 MET D 73 -71.08 -65.56 REMARK 500 ALA D 85 94.62 42.19 REMARK 500 ASP D 87 14.59 -64.89 REMARK 500 SER D 133 46.22 -72.00 REMARK 500 ALA D 134 5.94 -171.07 REMARK 500 ASN D 153 17.42 58.67 REMARK 500 THR D 176 86.45 -151.31 REMARK 500 ASN D 180 -149.32 -118.83 REMARK 500 LYS D 181 -85.07 -110.98 REMARK 500 PHE D 195 -173.92 -65.18 REMARK 500 THR D 206 36.54 -97.35 REMARK 500 ASN D 207 110.51 -29.84 REMARK 500 ASP D 209 -42.14 -148.12 REMARK 500 MET D 211 71.94 -68.35 REMARK 500 LEU D 222 135.44 -171.56 REMARK 500 LYS D 225 -143.63 -99.27 REMARK 500 LEU D 227 50.76 -114.98 REMARK 500 SER D 228 -87.08 -62.02 REMARK 500 PRO D 246 167.24 -46.94 REMARK 500 ASP D 253 171.34 179.55 REMARK 500 ASN D 326 -160.57 -125.45 REMARK 500 ASP D 334 80.24 51.53 REMARK 500 ALA D 336 -25.27 -164.98 REMARK 500 LYS D 339 -37.29 -35.96 REMARK 500 TYR D 360 -65.43 -101.74 REMARK 500 ASP D 361 2.88 -68.04 REMARK 500 ALA D 373 38.79 -89.98 REMARK 500 VAL D 378 98.51 -165.95 REMARK 500 LYS D 475 -6.89 -50.66 REMARK 500 GLU D 484 36.83 75.38 REMARK 500 ALA E 3 142.36 -35.11 REMARK 500 ASN E 9 -139.44 32.34 REMARK 500 THR E 30 54.23 -101.93 REMARK 500 SER E 43 -5.62 -55.98 REMARK 500 MET E 73 -71.18 -65.56 REMARK 500 ALA E 85 94.90 42.30 REMARK 500 ASP E 87 14.86 -65.34 REMARK 500 SER E 133 46.58 -72.24 REMARK 500 ALA E 134 5.17 -171.46 REMARK 500 ASN E 153 17.76 58.03 REMARK 500 THR E 176 86.47 -151.45 REMARK 500 ASN E 180 -149.11 -118.86 REMARK 500 LYS E 181 -84.99 -111.17 REMARK 500 PHE E 195 -173.77 -65.30 REMARK 500 THR E 206 36.41 -97.47 REMARK 500 ASN E 207 110.52 -29.91 REMARK 500 ASP E 209 -42.31 -148.05 REMARK 500 MET E 211 71.76 -68.44 REMARK 500 LEU E 222 135.63 -171.30 REMARK 500 LYS E 225 -143.81 -99.53 REMARK 500 LEU E 227 50.67 -115.15 REMARK 500 SER E 228 -87.14 -61.84 REMARK 500 PRO E 246 167.13 -47.04 REMARK 500 ASP E 253 171.46 179.56 REMARK 500 ASN E 326 -160.67 -125.57 REMARK 500 ASP E 334 80.22 51.16 REMARK 500 ALA E 336 -25.13 -165.00 REMARK 500 LYS E 339 -37.15 -36.28 REMARK 500 TYR E 360 -65.55 -101.94 REMARK 500 ASP E 361 2.69 -67.86 REMARK 500 ALA E 373 38.36 -90.00 REMARK 500 VAL E 378 99.45 -165.55 REMARK 500 LYS E 475 -6.70 -50.65 REMARK 500 GLU E 484 37.36 74.86 REMARK 500 ALA F 3 142.43 -34.22 REMARK 500 ASN F 9 -139.43 32.43 REMARK 500 THR F 30 53.49 -101.08 REMARK 500 SER F 43 -5.80 -56.08 REMARK 500 MET F 73 -71.87 -64.67 REMARK 500 ALA F 85 94.76 42.08 REMARK 500 ASP F 87 14.33 -64.86 REMARK 500 VAL F 122 -70.05 -61.49 REMARK 500 SER F 133 45.77 -72.55 REMARK 500 ALA F 134 4.94 -170.16 REMARK 500 ASN F 153 17.94 59.05 REMARK 500 THR F 176 86.60 -151.84 REMARK 500 ASN F 180 -149.43 -118.95 REMARK 500 LYS F 181 -85.12 -110.70 REMARK 500 PHE F 195 -173.86 -65.20 REMARK 500 THR F 206 36.63 -97.34 REMARK 500 ASN F 207 110.54 -30.08 REMARK 500 ASP F 209 -42.10 -148.15 REMARK 500 MET F 211 71.74 -68.33 REMARK 500 LEU F 222 135.68 -171.29 REMARK 500 LYS F 225 -143.85 -99.31 REMARK 500 LEU F 227 50.71 -114.98 REMARK 500 SER F 228 -87.21 -62.02 REMARK 500 PRO F 246 167.05 -46.92 REMARK 500 ASP F 253 171.22 179.52 REMARK 500 ASN F 326 -160.34 -125.57 REMARK 500 ASP F 334 80.38 51.05 REMARK 500 ALA F 336 -25.32 -164.72 REMARK 500 LYS F 339 -37.23 -36.28 REMARK 500 TYR F 360 -65.42 -101.65 REMARK 500 ASP F 361 2.80 -68.03 REMARK 500 ALA F 373 38.24 -89.64 REMARK 500 VAL F 378 98.99 -165.98 REMARK 500 LYS F 475 -7.26 -50.62 REMARK 500 GLU F 484 36.95 75.09 REMARK 500 ALA G 3 142.47 -35.21 REMARK 500 ASN G 9 -139.29 32.28 REMARK 500 THR G 30 53.88 -102.46 REMARK 500 SER G 43 -5.95 -56.01 REMARK 500 MET G 73 -71.22 -65.55 REMARK 500 ALA G 85 95.00 42.04 REMARK 500 ASP G 87 14.45 -65.04 REMARK 500 VAL G 122 -70.17 -61.17 REMARK 500 SER G 133 46.22 -72.51 REMARK 500 ALA G 134 5.41 -170.94 REMARK 500 ASN G 153 17.85 58.19 REMARK 500 THR G 176 86.57 -151.28 REMARK 500 ASN G 180 -149.23 -118.92 REMARK 500 LYS G 181 -85.09 -110.91 REMARK 500 VAL G 190 -179.79 -63.60 REMARK 500 PHE G 195 -173.78 -65.31 REMARK 500 THR G 206 36.41 -97.47 REMARK 500 ASN G 207 110.57 -29.81 REMARK 500 ASP G 209 -42.03 -148.06 REMARK 500 MET G 211 72.08 -68.54 REMARK 500 LEU G 222 135.80 -171.14 REMARK 500 LYS G 225 -143.70 -99.58 REMARK 500 LEU G 227 50.70 -115.14 REMARK 500 SER G 228 -87.08 -61.88 REMARK 500 PRO G 246 167.04 -47.12 REMARK 500 ASP G 253 171.45 179.72 REMARK 500 ASN G 326 -160.54 -125.64 REMARK 500 ASP G 334 80.68 51.39 REMARK 500 ALA G 336 -24.92 -165.29 REMARK 500 LYS G 339 -36.91 -36.22 REMARK 500 TYR G 360 -65.42 -101.85 REMARK 500 ASP G 361 2.46 -67.95 REMARK 500 ALA G 373 38.74 -89.84 REMARK 500 VAL G 378 98.62 -165.83 REMARK 500 LYS G 475 -6.95 -50.55 REMARK 500 GLU G 484 37.08 75.11 REMARK 500 REMARK 500 REMARK: NULL DBREF 1IOK A 1 545 UNP Q9Z462 CH60_PARDE 1 545 DBREF 1IOK B 1 545 UNP Q9Z462 CH60_PARDE 1 545 DBREF 1IOK C 1 545 UNP Q9Z462 CH60_PARDE 1 545 DBREF 1IOK D 1 545 UNP Q9Z462 CH60_PARDE 1 545 DBREF 1IOK E 1 545 UNP Q9Z462 CH60_PARDE 1 545 DBREF 1IOK F 1 545 UNP Q9Z462 CH60_PARDE 1 545 DBREF 1IOK G 1 545 UNP Q9Z462 CH60_PARDE 1 545 SEQRES 1 A 545 MET ALA ALA LYS GLU VAL LYS PHE ASN SER ASP ALA ARG SEQRES 2 A 545 ASP ARG MET LEU LYS GLY VAL ASN ILE LEU ALA ASP ALA SEQRES 3 A 545 VAL LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL SEQRES 4 A 545 ILE ASP LYS SER PHE GLY ALA PRO ARG ILE THR LYS ASP SEQRES 5 A 545 GLY VAL SER VAL ALA LYS GLU ILE GLU LEU SER ASP LYS SEQRES 6 A 545 PHE GLU ASN MET GLY ALA GLN MET VAL ARG GLU VAL ALA SEQRES 7 A 545 SER ARG THR ASN ASP GLU ALA GLY ASP GLY THR THR THR SEQRES 8 A 545 ALA THR VAL LEU ALA GLN ALA ILE VAL ARG GLU GLY LEU SEQRES 9 A 545 LYS ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS SEQRES 10 A 545 ARG GLY ILE ASP VAL ALA THR ALA LYS VAL VAL GLU ALA SEQRES 11 A 545 ILE LYS SER ALA ALA ARG PRO VAL ASN ASP SER SER GLU SEQRES 12 A 545 VAL ALA GLN VAL GLY THR ILE SER ALA ASN GLY GLU SER SEQRES 13 A 545 PHE ILE GLY GLN GLN ILE ALA GLU ALA MET GLN ARG VAL SEQRES 14 A 545 GLY ASN GLU GLY VAL ILE THR VAL GLU GLU ASN LYS GLY SEQRES 15 A 545 MET GLU THR GLU VAL GLU VAL VAL GLU GLY MET GLN PHE SEQRES 16 A 545 ASP ARG GLY TYR LEU SER PRO TYR PHE VAL THR ASN ALA SEQRES 17 A 545 ASP LYS MET ILE ALA GLU LEU GLU ASP ALA TYR ILE LEU SEQRES 18 A 545 LEU HIS GLU LYS LYS LEU SER SER LEU GLN PRO MET VAL SEQRES 19 A 545 PRO LEU LEU GLU SER VAL ILE GLN SER GLN LYS PRO LEU SEQRES 20 A 545 LEU ILE VAL ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA SEQRES 21 A 545 THR LEU VAL VAL ASN LYS LEU ARG GLY GLY LEU LYS ILE SEQRES 22 A 545 ALA ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS SEQRES 23 A 545 ALA MET LEU GLN ASP ILE ALA ILE LEU THR GLY GLY GLN SEQRES 24 A 545 VAL ILE SER GLU ASP LEU GLY MET LYS LEU GLU ASN VAL SEQRES 25 A 545 THR ILE ASP MET LEU GLY ARG ALA LYS LYS VAL SER ILE SEQRES 26 A 545 ASN LYS ASP ASN THR THR ILE VAL ASP GLY ALA GLY GLU SEQRES 27 A 545 LYS ALA GLU ILE GLU ALA ARG VAL SER GLN ILE ARG GLN SEQRES 28 A 545 GLN ILE GLU GLU THR THR SER ASP TYR ASP ARG GLU LYS SEQRES 29 A 545 LEU GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA SEQRES 30 A 545 VAL ILE ARG VAL GLY GLY MET THR GLU ILE GLU VAL LYS SEQRES 31 A 545 GLU ARG LYS ASP ARG VAL ASP ASP ALA LEU ASN ALA THR SEQRES 32 A 545 ARG ALA ALA VAL GLN GLU GLY ILE VAL VAL GLY GLY GLY SEQRES 33 A 545 VAL ALA LEU VAL GLN GLY ALA LYS VAL LEU GLU GLY LEU SEQRES 34 A 545 SER GLY ALA ASN SER ASP GLN ASP ALA GLY ILE ALA ILE SEQRES 35 A 545 ILE ARG ARG ALA LEU GLU ALA PRO MET ARG GLN ILE ALA SEQRES 36 A 545 GLU ASN ALA GLY VAL ASP GLY ALA VAL VAL ALA GLY LYS SEQRES 37 A 545 VAL ARG GLU SER SER ASP LYS ALA PHE GLY PHE ASN ALA SEQRES 38 A 545 GLN THR GLU GLU TYR GLY ASP MET PHE LYS PHE GLY VAL SEQRES 39 A 545 ILE ASP PRO ALA LYS VAL VAL ARG THR ALA LEU GLU ASP SEQRES 40 A 545 ALA ALA SER VAL ALA GLY LEU LEU ILE THR THR GLU ALA SEQRES 41 A 545 MET ILE ALA GLU LYS PRO GLU PRO LYS ALA PRO ALA GLY SEQRES 42 A 545 GLY MET PRO ASP MET GLY GLY MET GLY GLY MET MET SEQRES 1 B 545 MET ALA ALA LYS GLU VAL LYS PHE ASN SER ASP ALA ARG SEQRES 2 B 545 ASP ARG MET LEU LYS GLY VAL ASN ILE LEU ALA ASP ALA SEQRES 3 B 545 VAL LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL SEQRES 4 B 545 ILE ASP LYS SER PHE GLY ALA PRO ARG ILE THR LYS ASP SEQRES 5 B 545 GLY VAL SER VAL ALA LYS GLU ILE GLU LEU SER ASP LYS SEQRES 6 B 545 PHE GLU ASN MET GLY ALA GLN MET VAL ARG GLU VAL ALA SEQRES 7 B 545 SER ARG THR ASN ASP GLU ALA GLY ASP GLY THR THR THR SEQRES 8 B 545 ALA THR VAL LEU ALA GLN ALA ILE VAL ARG GLU GLY LEU SEQRES 9 B 545 LYS ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS SEQRES 10 B 545 ARG GLY ILE ASP VAL ALA THR ALA LYS VAL VAL GLU ALA SEQRES 11 B 545 ILE LYS SER ALA ALA ARG PRO VAL ASN ASP SER SER GLU SEQRES 12 B 545 VAL ALA GLN VAL GLY THR ILE SER ALA ASN GLY GLU SER SEQRES 13 B 545 PHE ILE GLY GLN GLN ILE ALA GLU ALA MET GLN ARG VAL SEQRES 14 B 545 GLY ASN GLU GLY VAL ILE THR VAL GLU GLU ASN LYS GLY SEQRES 15 B 545 MET GLU THR GLU VAL GLU VAL VAL GLU GLY MET GLN PHE SEQRES 16 B 545 ASP ARG GLY TYR LEU SER PRO TYR PHE VAL THR ASN ALA SEQRES 17 B 545 ASP LYS MET ILE ALA GLU LEU GLU ASP ALA TYR ILE LEU SEQRES 18 B 545 LEU HIS GLU LYS LYS LEU SER SER LEU GLN PRO MET VAL SEQRES 19 B 545 PRO LEU LEU GLU SER VAL ILE GLN SER GLN LYS PRO LEU SEQRES 20 B 545 LEU ILE VAL ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA SEQRES 21 B 545 THR LEU VAL VAL ASN LYS LEU ARG GLY GLY LEU LYS ILE SEQRES 22 B 545 ALA ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS SEQRES 23 B 545 ALA MET LEU GLN ASP ILE ALA ILE LEU THR GLY GLY GLN SEQRES 24 B 545 VAL ILE SER GLU ASP LEU GLY MET LYS LEU GLU ASN VAL SEQRES 25 B 545 THR ILE ASP MET LEU GLY ARG ALA LYS LYS VAL SER ILE SEQRES 26 B 545 ASN LYS ASP ASN THR THR ILE VAL ASP GLY ALA GLY GLU SEQRES 27 B 545 LYS ALA GLU ILE GLU ALA ARG VAL SER GLN ILE ARG GLN SEQRES 28 B 545 GLN ILE GLU GLU THR THR SER ASP TYR ASP ARG GLU LYS SEQRES 29 B 545 LEU GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA SEQRES 30 B 545 VAL ILE ARG VAL GLY GLY MET THR GLU ILE GLU VAL LYS SEQRES 31 B 545 GLU ARG LYS ASP ARG VAL ASP ASP ALA LEU ASN ALA THR SEQRES 32 B 545 ARG ALA ALA VAL GLN GLU GLY ILE VAL VAL GLY GLY GLY SEQRES 33 B 545 VAL ALA LEU VAL GLN GLY ALA LYS VAL LEU GLU GLY LEU SEQRES 34 B 545 SER GLY ALA ASN SER ASP GLN ASP ALA GLY ILE ALA ILE SEQRES 35 B 545 ILE ARG ARG ALA LEU GLU ALA PRO MET ARG GLN ILE ALA SEQRES 36 B 545 GLU ASN ALA GLY VAL ASP GLY ALA VAL VAL ALA GLY LYS SEQRES 37 B 545 VAL ARG GLU SER SER ASP LYS ALA PHE GLY PHE ASN ALA SEQRES 38 B 545 GLN THR GLU GLU TYR GLY ASP MET PHE LYS PHE GLY VAL SEQRES 39 B 545 ILE ASP PRO ALA LYS VAL VAL ARG THR ALA LEU GLU ASP SEQRES 40 B 545 ALA ALA SER VAL ALA GLY LEU LEU ILE THR THR GLU ALA SEQRES 41 B 545 MET ILE ALA GLU LYS PRO GLU PRO LYS ALA PRO ALA GLY SEQRES 42 B 545 GLY MET PRO ASP MET GLY GLY MET GLY GLY MET MET SEQRES 1 C 545 MET ALA ALA LYS GLU VAL LYS PHE ASN SER ASP ALA ARG SEQRES 2 C 545 ASP ARG MET LEU LYS GLY VAL ASN ILE LEU ALA ASP ALA SEQRES 3 C 545 VAL LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL SEQRES 4 C 545 ILE ASP LYS SER PHE GLY ALA PRO ARG ILE THR LYS ASP SEQRES 5 C 545 GLY VAL SER VAL ALA LYS GLU ILE GLU LEU SER ASP LYS SEQRES 6 C 545 PHE GLU ASN MET GLY ALA GLN MET VAL ARG GLU VAL ALA SEQRES 7 C 545 SER ARG THR ASN ASP GLU ALA GLY ASP GLY THR THR THR SEQRES 8 C 545 ALA THR VAL LEU ALA GLN ALA ILE VAL ARG GLU GLY LEU SEQRES 9 C 545 LYS ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS SEQRES 10 C 545 ARG GLY ILE ASP VAL ALA THR ALA LYS VAL VAL GLU ALA SEQRES 11 C 545 ILE LYS SER ALA ALA ARG PRO VAL ASN ASP SER SER GLU SEQRES 12 C 545 VAL ALA GLN VAL GLY THR ILE SER ALA ASN GLY GLU SER SEQRES 13 C 545 PHE ILE GLY GLN GLN ILE ALA GLU ALA MET GLN ARG VAL SEQRES 14 C 545 GLY ASN GLU GLY VAL ILE THR VAL GLU GLU ASN LYS GLY SEQRES 15 C 545 MET GLU THR GLU VAL GLU VAL VAL GLU GLY MET GLN PHE SEQRES 16 C 545 ASP ARG GLY TYR LEU SER PRO TYR PHE VAL THR ASN ALA SEQRES 17 C 545 ASP LYS MET ILE ALA GLU LEU GLU ASP ALA TYR ILE LEU SEQRES 18 C 545 LEU HIS GLU LYS LYS LEU SER SER LEU GLN PRO MET VAL SEQRES 19 C 545 PRO LEU LEU GLU SER VAL ILE GLN SER GLN LYS PRO LEU SEQRES 20 C 545 LEU ILE VAL ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA SEQRES 21 C 545 THR LEU VAL VAL ASN LYS LEU ARG GLY GLY LEU LYS ILE SEQRES 22 C 545 ALA ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS SEQRES 23 C 545 ALA MET LEU GLN ASP ILE ALA ILE LEU THR GLY GLY GLN SEQRES 24 C 545 VAL ILE SER GLU ASP LEU GLY MET LYS LEU GLU ASN VAL SEQRES 25 C 545 THR ILE ASP MET LEU GLY ARG ALA LYS LYS VAL SER ILE SEQRES 26 C 545 ASN LYS ASP ASN THR THR ILE VAL ASP GLY ALA GLY GLU SEQRES 27 C 545 LYS ALA GLU ILE GLU ALA ARG VAL SER GLN ILE ARG GLN SEQRES 28 C 545 GLN ILE GLU GLU THR THR SER ASP TYR ASP ARG GLU LYS SEQRES 29 C 545 LEU GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA SEQRES 30 C 545 VAL ILE ARG VAL GLY GLY MET THR GLU ILE GLU VAL LYS SEQRES 31 C 545 GLU ARG LYS ASP ARG VAL ASP ASP ALA LEU ASN ALA THR SEQRES 32 C 545 ARG ALA ALA VAL GLN GLU GLY ILE VAL VAL GLY GLY GLY SEQRES 33 C 545 VAL ALA LEU VAL GLN GLY ALA LYS VAL LEU GLU GLY LEU SEQRES 34 C 545 SER GLY ALA ASN SER ASP GLN ASP ALA GLY ILE ALA ILE SEQRES 35 C 545 ILE ARG ARG ALA LEU GLU ALA PRO MET ARG GLN ILE ALA SEQRES 36 C 545 GLU ASN ALA GLY VAL ASP GLY ALA VAL VAL ALA GLY LYS SEQRES 37 C 545 VAL ARG GLU SER SER ASP LYS ALA PHE GLY PHE ASN ALA SEQRES 38 C 545 GLN THR GLU GLU TYR GLY ASP MET PHE LYS PHE GLY VAL SEQRES 39 C 545 ILE ASP PRO ALA LYS VAL VAL ARG THR ALA LEU GLU ASP SEQRES 40 C 545 ALA ALA SER VAL ALA GLY LEU LEU ILE THR THR GLU ALA SEQRES 41 C 545 MET ILE ALA GLU LYS PRO GLU PRO LYS ALA PRO ALA GLY SEQRES 42 C 545 GLY MET PRO ASP MET GLY GLY MET GLY GLY MET MET SEQRES 1 D 545 MET ALA ALA LYS GLU VAL LYS PHE ASN SER ASP ALA ARG SEQRES 2 D 545 ASP ARG MET LEU LYS GLY VAL ASN ILE LEU ALA ASP ALA SEQRES 3 D 545 VAL LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL SEQRES 4 D 545 ILE ASP LYS SER PHE GLY ALA PRO ARG ILE THR LYS ASP SEQRES 5 D 545 GLY VAL SER VAL ALA LYS GLU ILE GLU LEU SER ASP LYS SEQRES 6 D 545 PHE GLU ASN MET GLY ALA GLN MET VAL ARG GLU VAL ALA SEQRES 7 D 545 SER ARG THR ASN ASP GLU ALA GLY ASP GLY THR THR THR SEQRES 8 D 545 ALA THR VAL LEU ALA GLN ALA ILE VAL ARG GLU GLY LEU SEQRES 9 D 545 LYS ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS SEQRES 10 D 545 ARG GLY ILE ASP VAL ALA THR ALA LYS VAL VAL GLU ALA SEQRES 11 D 545 ILE LYS SER ALA ALA ARG PRO VAL ASN ASP SER SER GLU SEQRES 12 D 545 VAL ALA GLN VAL GLY THR ILE SER ALA ASN GLY GLU SER SEQRES 13 D 545 PHE ILE GLY GLN GLN ILE ALA GLU ALA MET GLN ARG VAL SEQRES 14 D 545 GLY ASN GLU GLY VAL ILE THR VAL GLU GLU ASN LYS GLY SEQRES 15 D 545 MET GLU THR GLU VAL GLU VAL VAL GLU GLY MET GLN PHE SEQRES 16 D 545 ASP ARG GLY TYR LEU SER PRO TYR PHE VAL THR ASN ALA SEQRES 17 D 545 ASP LYS MET ILE ALA GLU LEU GLU ASP ALA TYR ILE LEU SEQRES 18 D 545 LEU HIS GLU LYS LYS LEU SER SER LEU GLN PRO MET VAL SEQRES 19 D 545 PRO LEU LEU GLU SER VAL ILE GLN SER GLN LYS PRO LEU SEQRES 20 D 545 LEU ILE VAL ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA SEQRES 21 D 545 THR LEU VAL VAL ASN LYS LEU ARG GLY GLY LEU LYS ILE SEQRES 22 D 545 ALA ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS SEQRES 23 D 545 ALA MET LEU GLN ASP ILE ALA ILE LEU THR GLY GLY GLN SEQRES 24 D 545 VAL ILE SER GLU ASP LEU GLY MET LYS LEU GLU ASN VAL SEQRES 25 D 545 THR ILE ASP MET LEU GLY ARG ALA LYS LYS VAL SER ILE SEQRES 26 D 545 ASN LYS ASP ASN THR THR ILE VAL ASP GLY ALA GLY GLU SEQRES 27 D 545 LYS ALA GLU ILE GLU ALA ARG VAL SER GLN ILE ARG GLN SEQRES 28 D 545 GLN ILE GLU GLU THR THR SER ASP TYR ASP ARG GLU LYS SEQRES 29 D 545 LEU GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA SEQRES 30 D 545 VAL ILE ARG VAL GLY GLY MET THR GLU ILE GLU VAL LYS SEQRES 31 D 545 GLU ARG LYS ASP ARG VAL ASP ASP ALA LEU ASN ALA THR SEQRES 32 D 545 ARG ALA ALA VAL GLN GLU GLY ILE VAL VAL GLY GLY GLY SEQRES 33 D 545 VAL ALA LEU VAL GLN GLY ALA LYS VAL LEU GLU GLY LEU SEQRES 34 D 545 SER GLY ALA ASN SER ASP GLN ASP ALA GLY ILE ALA ILE SEQRES 35 D 545 ILE ARG ARG ALA LEU GLU ALA PRO MET ARG GLN ILE ALA SEQRES 36 D 545 GLU ASN ALA GLY VAL ASP GLY ALA VAL VAL ALA GLY LYS SEQRES 37 D 545 VAL ARG GLU SER SER ASP LYS ALA PHE GLY PHE ASN ALA SEQRES 38 D 545 GLN THR GLU GLU TYR GLY ASP MET PHE LYS PHE GLY VAL SEQRES 39 D 545 ILE ASP PRO ALA LYS VAL VAL ARG THR ALA LEU GLU ASP SEQRES 40 D 545 ALA ALA SER VAL ALA GLY LEU LEU ILE THR THR GLU ALA SEQRES 41 D 545 MET ILE ALA GLU LYS PRO GLU PRO LYS ALA PRO ALA GLY SEQRES 42 D 545 GLY MET PRO ASP MET GLY GLY MET GLY GLY MET MET SEQRES 1 E 545 MET ALA ALA LYS GLU VAL LYS PHE ASN SER ASP ALA ARG SEQRES 2 E 545 ASP ARG MET LEU LYS GLY VAL ASN ILE LEU ALA ASP ALA SEQRES 3 E 545 VAL LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL SEQRES 4 E 545 ILE ASP LYS SER PHE GLY ALA PRO ARG ILE THR LYS ASP SEQRES 5 E 545 GLY VAL SER VAL ALA LYS GLU ILE GLU LEU SER ASP LYS SEQRES 6 E 545 PHE GLU ASN MET GLY ALA GLN MET VAL ARG GLU VAL ALA SEQRES 7 E 545 SER ARG THR ASN ASP GLU ALA GLY ASP GLY THR THR THR SEQRES 8 E 545 ALA THR VAL LEU ALA GLN ALA ILE VAL ARG GLU GLY LEU SEQRES 9 E 545 LYS ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS SEQRES 10 E 545 ARG GLY ILE ASP VAL ALA THR ALA LYS VAL VAL GLU ALA SEQRES 11 E 545 ILE LYS SER ALA ALA ARG PRO VAL ASN ASP SER SER GLU SEQRES 12 E 545 VAL ALA GLN VAL GLY THR ILE SER ALA ASN GLY GLU SER SEQRES 13 E 545 PHE ILE GLY GLN GLN ILE ALA GLU ALA MET GLN ARG VAL SEQRES 14 E 545 GLY ASN GLU GLY VAL ILE THR VAL GLU GLU ASN LYS GLY SEQRES 15 E 545 MET GLU THR GLU VAL GLU VAL VAL GLU GLY MET GLN PHE SEQRES 16 E 545 ASP ARG GLY TYR LEU SER PRO TYR PHE VAL THR ASN ALA SEQRES 17 E 545 ASP LYS MET ILE ALA GLU LEU GLU ASP ALA TYR ILE LEU SEQRES 18 E 545 LEU HIS GLU LYS LYS LEU SER SER LEU GLN PRO MET VAL SEQRES 19 E 545 PRO LEU LEU GLU SER VAL ILE GLN SER GLN LYS PRO LEU SEQRES 20 E 545 LEU ILE VAL ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA SEQRES 21 E 545 THR LEU VAL VAL ASN LYS LEU ARG GLY GLY LEU LYS ILE SEQRES 22 E 545 ALA ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS SEQRES 23 E 545 ALA MET LEU GLN ASP ILE ALA ILE LEU THR GLY GLY GLN SEQRES 24 E 545 VAL ILE SER GLU ASP LEU GLY MET LYS LEU GLU ASN VAL SEQRES 25 E 545 THR ILE ASP MET LEU GLY ARG ALA LYS LYS VAL SER ILE SEQRES 26 E 545 ASN LYS ASP ASN THR THR ILE VAL ASP GLY ALA GLY GLU SEQRES 27 E 545 LYS ALA GLU ILE GLU ALA ARG VAL SER GLN ILE ARG GLN SEQRES 28 E 545 GLN ILE GLU GLU THR THR SER ASP TYR ASP ARG GLU LYS SEQRES 29 E 545 LEU GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA SEQRES 30 E 545 VAL ILE ARG VAL GLY GLY MET THR GLU ILE GLU VAL LYS SEQRES 31 E 545 GLU ARG LYS ASP ARG VAL ASP ASP ALA LEU ASN ALA THR SEQRES 32 E 545 ARG ALA ALA VAL GLN GLU GLY ILE VAL VAL GLY GLY GLY SEQRES 33 E 545 VAL ALA LEU VAL GLN GLY ALA LYS VAL LEU GLU GLY LEU SEQRES 34 E 545 SER GLY ALA ASN SER ASP GLN ASP ALA GLY ILE ALA ILE SEQRES 35 E 545 ILE ARG ARG ALA LEU GLU ALA PRO MET ARG GLN ILE ALA SEQRES 36 E 545 GLU ASN ALA GLY VAL ASP GLY ALA VAL VAL ALA GLY LYS SEQRES 37 E 545 VAL ARG GLU SER SER ASP LYS ALA PHE GLY PHE ASN ALA SEQRES 38 E 545 GLN THR GLU GLU TYR GLY ASP MET PHE LYS PHE GLY VAL SEQRES 39 E 545 ILE ASP PRO ALA LYS VAL VAL ARG THR ALA LEU GLU ASP SEQRES 40 E 545 ALA ALA SER VAL ALA GLY LEU LEU ILE THR THR GLU ALA SEQRES 41 E 545 MET ILE ALA GLU LYS PRO GLU PRO LYS ALA PRO ALA GLY SEQRES 42 E 545 GLY MET PRO ASP MET GLY GLY MET GLY GLY MET MET SEQRES 1 F 545 MET ALA ALA LYS GLU VAL LYS PHE ASN SER ASP ALA ARG SEQRES 2 F 545 ASP ARG MET LEU LYS GLY VAL ASN ILE LEU ALA ASP ALA SEQRES 3 F 545 VAL LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL SEQRES 4 F 545 ILE ASP LYS SER PHE GLY ALA PRO ARG ILE THR LYS ASP SEQRES 5 F 545 GLY VAL SER VAL ALA LYS GLU ILE GLU LEU SER ASP LYS SEQRES 6 F 545 PHE GLU ASN MET GLY ALA GLN MET VAL ARG GLU VAL ALA SEQRES 7 F 545 SER ARG THR ASN ASP GLU ALA GLY ASP GLY THR THR THR SEQRES 8 F 545 ALA THR VAL LEU ALA GLN ALA ILE VAL ARG GLU GLY LEU SEQRES 9 F 545 LYS ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS SEQRES 10 F 545 ARG GLY ILE ASP VAL ALA THR ALA LYS VAL VAL GLU ALA SEQRES 11 F 545 ILE LYS SER ALA ALA ARG PRO VAL ASN ASP SER SER GLU SEQRES 12 F 545 VAL ALA GLN VAL GLY THR ILE SER ALA ASN GLY GLU SER SEQRES 13 F 545 PHE ILE GLY GLN GLN ILE ALA GLU ALA MET GLN ARG VAL SEQRES 14 F 545 GLY ASN GLU GLY VAL ILE THR VAL GLU GLU ASN LYS GLY SEQRES 15 F 545 MET GLU THR GLU VAL GLU VAL VAL GLU GLY MET GLN PHE SEQRES 16 F 545 ASP ARG GLY TYR LEU SER PRO TYR PHE VAL THR ASN ALA SEQRES 17 F 545 ASP LYS MET ILE ALA GLU LEU GLU ASP ALA TYR ILE LEU SEQRES 18 F 545 LEU HIS GLU LYS LYS LEU SER SER LEU GLN PRO MET VAL SEQRES 19 F 545 PRO LEU LEU GLU SER VAL ILE GLN SER GLN LYS PRO LEU SEQRES 20 F 545 LEU ILE VAL ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA SEQRES 21 F 545 THR LEU VAL VAL ASN LYS LEU ARG GLY GLY LEU LYS ILE SEQRES 22 F 545 ALA ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS SEQRES 23 F 545 ALA MET LEU GLN ASP ILE ALA ILE LEU THR GLY GLY GLN SEQRES 24 F 545 VAL ILE SER GLU ASP LEU GLY MET LYS LEU GLU ASN VAL SEQRES 25 F 545 THR ILE ASP MET LEU GLY ARG ALA LYS LYS VAL SER ILE SEQRES 26 F 545 ASN LYS ASP ASN THR THR ILE VAL ASP GLY ALA GLY GLU SEQRES 27 F 545 LYS ALA GLU ILE GLU ALA ARG VAL SER GLN ILE ARG GLN SEQRES 28 F 545 GLN ILE GLU GLU THR THR SER ASP TYR ASP ARG GLU LYS SEQRES 29 F 545 LEU GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA SEQRES 30 F 545 VAL ILE ARG VAL GLY GLY MET THR GLU ILE GLU VAL LYS SEQRES 31 F 545 GLU ARG LYS ASP ARG VAL ASP ASP ALA LEU ASN ALA THR SEQRES 32 F 545 ARG ALA ALA VAL GLN GLU GLY ILE VAL VAL GLY GLY GLY SEQRES 33 F 545 VAL ALA LEU VAL GLN GLY ALA LYS VAL LEU GLU GLY LEU SEQRES 34 F 545 SER GLY ALA ASN SER ASP GLN ASP ALA GLY ILE ALA ILE SEQRES 35 F 545 ILE ARG ARG ALA LEU GLU ALA PRO MET ARG GLN ILE ALA SEQRES 36 F 545 GLU ASN ALA GLY VAL ASP GLY ALA VAL VAL ALA GLY LYS SEQRES 37 F 545 VAL ARG GLU SER SER ASP LYS ALA PHE GLY PHE ASN ALA SEQRES 38 F 545 GLN THR GLU GLU TYR GLY ASP MET PHE LYS PHE GLY VAL SEQRES 39 F 545 ILE ASP PRO ALA LYS VAL VAL ARG THR ALA LEU GLU ASP SEQRES 40 F 545 ALA ALA SER VAL ALA GLY LEU LEU ILE THR THR GLU ALA SEQRES 41 F 545 MET ILE ALA GLU LYS PRO GLU PRO LYS ALA PRO ALA GLY SEQRES 42 F 545 GLY MET PRO ASP MET GLY GLY MET GLY GLY MET MET SEQRES 1 G 545 MET ALA ALA LYS GLU VAL LYS PHE ASN SER ASP ALA ARG SEQRES 2 G 545 ASP ARG MET LEU LYS GLY VAL ASN ILE LEU ALA ASP ALA SEQRES 3 G 545 VAL LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL SEQRES 4 G 545 ILE ASP LYS SER PHE GLY ALA PRO ARG ILE THR LYS ASP SEQRES 5 G 545 GLY VAL SER VAL ALA LYS GLU ILE GLU LEU SER ASP LYS SEQRES 6 G 545 PHE GLU ASN MET GLY ALA GLN MET VAL ARG GLU VAL ALA SEQRES 7 G 545 SER ARG THR ASN ASP GLU ALA GLY ASP GLY THR THR THR SEQRES 8 G 545 ALA THR VAL LEU ALA GLN ALA ILE VAL ARG GLU GLY LEU SEQRES 9 G 545 LYS ALA VAL ALA ALA GLY MET ASN PRO MET ASP LEU LYS SEQRES 10 G 545 ARG GLY ILE ASP VAL ALA THR ALA LYS VAL VAL GLU ALA SEQRES 11 G 545 ILE LYS SER ALA ALA ARG PRO VAL ASN ASP SER SER GLU SEQRES 12 G 545 VAL ALA GLN VAL GLY THR ILE SER ALA ASN GLY GLU SER SEQRES 13 G 545 PHE ILE GLY GLN GLN ILE ALA GLU ALA MET GLN ARG VAL SEQRES 14 G 545 GLY ASN GLU GLY VAL ILE THR VAL GLU GLU ASN LYS GLY SEQRES 15 G 545 MET GLU THR GLU VAL GLU VAL VAL GLU GLY MET GLN PHE SEQRES 16 G 545 ASP ARG GLY TYR LEU SER PRO TYR PHE VAL THR ASN ALA SEQRES 17 G 545 ASP LYS MET ILE ALA GLU LEU GLU ASP ALA TYR ILE LEU SEQRES 18 G 545 LEU HIS GLU LYS LYS LEU SER SER LEU GLN PRO MET VAL SEQRES 19 G 545 PRO LEU LEU GLU SER VAL ILE GLN SER GLN LYS PRO LEU SEQRES 20 G 545 LEU ILE VAL ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA SEQRES 21 G 545 THR LEU VAL VAL ASN LYS LEU ARG GLY GLY LEU LYS ILE SEQRES 22 G 545 ALA ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS SEQRES 23 G 545 ALA MET LEU GLN ASP ILE ALA ILE LEU THR GLY GLY GLN SEQRES 24 G 545 VAL ILE SER GLU ASP LEU GLY MET LYS LEU GLU ASN VAL SEQRES 25 G 545 THR ILE ASP MET LEU GLY ARG ALA LYS LYS VAL SER ILE SEQRES 26 G 545 ASN LYS ASP ASN THR THR ILE VAL ASP GLY ALA GLY GLU SEQRES 27 G 545 LYS ALA GLU ILE GLU ALA ARG VAL SER GLN ILE ARG GLN SEQRES 28 G 545 GLN ILE GLU GLU THR THR SER ASP TYR ASP ARG GLU LYS SEQRES 29 G 545 LEU GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA SEQRES 30 G 545 VAL ILE ARG VAL GLY GLY MET THR GLU ILE GLU VAL LYS SEQRES 31 G 545 GLU ARG LYS ASP ARG VAL ASP ASP ALA LEU ASN ALA THR SEQRES 32 G 545 ARG ALA ALA VAL GLN GLU GLY ILE VAL VAL GLY GLY GLY SEQRES 33 G 545 VAL ALA LEU VAL GLN GLY ALA LYS VAL LEU GLU GLY LEU SEQRES 34 G 545 SER GLY ALA ASN SER ASP GLN ASP ALA GLY ILE ALA ILE SEQRES 35 G 545 ILE ARG ARG ALA LEU GLU ALA PRO MET ARG GLN ILE ALA SEQRES 36 G 545 GLU ASN ALA GLY VAL ASP GLY ALA VAL VAL ALA GLY LYS SEQRES 37 G 545 VAL ARG GLU SER SER ASP LYS ALA PHE GLY PHE ASN ALA SEQRES 38 G 545 GLN THR GLU GLU TYR GLY ASP MET PHE LYS PHE GLY VAL SEQRES 39 G 545 ILE ASP PRO ALA LYS VAL VAL ARG THR ALA LEU GLU ASP SEQRES 40 G 545 ALA ALA SER VAL ALA GLY LEU LEU ILE THR THR GLU ALA SEQRES 41 G 545 MET ILE ALA GLU LYS PRO GLU PRO LYS ALA PRO ALA GLY SEQRES 42 G 545 GLY MET PRO ASP MET GLY GLY MET GLY GLY MET MET HELIX 1 1 ASN A 9 LYS A 28 1 20 HELIX 2 2 VAL A 29 LEU A 31 5 3 HELIX 3 3 ASP A 52 ILE A 60 1 9 HELIX 4 4 ASP A 64 THR A 81 1 18 HELIX 5 5 ASN A 82 ALA A 85 5 4 HELIX 6 6 ASP A 87 ALA A 109 1 23 HELIX 7 7 ASN A 112 SER A 133 1 22 HELIX 8 8 ALA A 145 SER A 151 1 7 HELIX 9 9 GLU A 155 GLY A 170 1 16 HELIX 10 10 SER A 201 VAL A 205 5 5 HELIX 11 11 ASP A 283 GLY A 297 1 15 HELIX 12 12 GLU A 338 GLU A 354 1 17 HELIX 13 13 TYR A 360 LYS A 371 1 12 HELIX 14 14 THR A 385 GLY A 410 1 26 HELIX 15 15 GLY A 416 ALA A 423 1 8 HELIX 16 16 LYS A 424 GLY A 428 5 5 HELIX 17 17 ASN A 433 LEU A 447 1 15 HELIX 18 18 GLU A 448 GLY A 459 1 12 HELIX 19 19 ASP A 461 GLU A 471 1 11 HELIX 20 20 MET A 489 GLY A 493 1 5 HELIX 21 21 ALA A 498 THR A 517 1 20 HELIX 22 22 ASN B 9 LYS B 28 1 20 HELIX 23 23 VAL B 29 LEU B 31 5 3 HELIX 24 24 ASP B 52 ILE B 60 1 9 HELIX 25 25 ASP B 64 THR B 81 1 18 HELIX 26 26 ASN B 82 ALA B 85 5 4 HELIX 27 27 ASP B 87 ALA B 109 1 23 HELIX 28 28 ASN B 112 SER B 133 1 22 HELIX 29 29 ALA B 145 SER B 151 1 7 HELIX 30 30 GLU B 155 GLY B 170 1 16 HELIX 31 31 SER B 201 VAL B 205 5 5 HELIX 32 32 ASP B 283 GLY B 297 1 15 HELIX 33 33 GLU B 338 GLU B 354 1 17 HELIX 34 34 TYR B 360 LYS B 371 1 12 HELIX 35 35 THR B 385 GLY B 410 1 26 HELIX 36 36 GLY B 416 ALA B 423 1 8 HELIX 37 37 LYS B 424 GLY B 428 5 5 HELIX 38 38 ASN B 433 LEU B 447 1 15 HELIX 39 39 GLU B 448 GLY B 459 1 12 HELIX 40 40 ASP B 461 GLU B 471 1 11 HELIX 41 41 MET B 489 GLY B 493 1 5 HELIX 42 42 ALA B 498 THR B 517 1 20 HELIX 43 43 ASN C 9 LYS C 28 1 20 HELIX 44 44 VAL C 29 LEU C 31 5 3 HELIX 45 45 ASP C 52 ILE C 60 1 9 HELIX 46 46 ASP C 64 THR C 81 1 18 HELIX 47 47 ASN C 82 ALA C 85 5 4 HELIX 48 48 ASP C 87 ALA C 109 1 23 HELIX 49 49 ASN C 112 SER C 133 1 22 HELIX 50 50 ALA C 145 SER C 151 1 7 HELIX 51 51 GLU C 155 GLY C 170 1 16 HELIX 52 52 SER C 201 VAL C 205 5 5 HELIX 53 53 ASP C 283 GLY C 297 1 15 HELIX 54 54 GLU C 338 GLU C 354 1 17 HELIX 55 55 TYR C 360 LYS C 371 1 12 HELIX 56 56 THR C 385 GLY C 410 1 26 HELIX 57 57 GLY C 416 ALA C 423 1 8 HELIX 58 58 LYS C 424 GLY C 428 5 5 HELIX 59 59 ASN C 433 LEU C 447 1 15 HELIX 60 60 GLU C 448 GLY C 459 1 12 HELIX 61 61 ASP C 461 GLU C 471 1 11 HELIX 62 62 MET C 489 GLY C 493 1 5 HELIX 63 63 ALA C 498 THR C 517 1 20 HELIX 64 64 ASN D 9 LYS D 28 1 20 HELIX 65 65 VAL D 29 LEU D 31 5 3 HELIX 66 66 ASP D 52 ILE D 60 1 9 HELIX 67 67 ASP D 64 THR D 81 1 18 HELIX 68 68 ASN D 82 ALA D 85 5 4 HELIX 69 69 ASP D 87 ALA D 109 1 23 HELIX 70 70 ASN D 112 SER D 133 1 22 HELIX 71 71 ALA D 145 SER D 151 1 7 HELIX 72 72 GLU D 155 GLY D 170 1 16 HELIX 73 73 SER D 201 VAL D 205 5 5 HELIX 74 74 ASP D 283 GLY D 297 1 15 HELIX 75 75 GLU D 338 GLU D 354 1 17 HELIX 76 76 TYR D 360 LYS D 371 1 12 HELIX 77 77 THR D 385 GLY D 410 1 26 HELIX 78 78 GLY D 416 ALA D 423 1 8 HELIX 79 79 LYS D 424 GLY D 428 5 5 HELIX 80 80 ASN D 433 LEU D 447 1 15 HELIX 81 81 GLU D 448 GLY D 459 1 12 HELIX 82 82 ASP D 461 GLU D 471 1 11 HELIX 83 83 MET D 489 GLY D 493 1 5 HELIX 84 84 ALA D 498 THR D 517 1 20 HELIX 85 85 ASN E 9 LYS E 28 1 20 HELIX 86 86 VAL E 29 LEU E 31 5 3 HELIX 87 87 ASP E 52 ILE E 60 1 9 HELIX 88 88 ASP E 64 THR E 81 1 18 HELIX 89 89 ASN E 82 ALA E 85 5 4 HELIX 90 90 ASP E 87 ALA E 109 1 23 HELIX 91 91 ASN E 112 SER E 133 1 22 HELIX 92 92 ALA E 145 SER E 151 1 7 HELIX 93 93 GLU E 155 GLY E 170 1 16 HELIX 94 94 SER E 201 VAL E 205 5 5 HELIX 95 95 ASP E 283 GLY E 297 1 15 HELIX 96 96 GLU E 338 GLU E 354 1 17 HELIX 97 97 TYR E 360 LYS E 371 1 12 HELIX 98 98 THR E 385 GLY E 410 1 26 HELIX 99 99 GLY E 416 ALA E 423 1 8 HELIX 100 100 LYS E 424 GLY E 428 5 5 HELIX 101 101 ASN E 433 LEU E 447 1 15 HELIX 102 102 GLU E 448 GLY E 459 1 12 HELIX 103 103 ASP E 461 GLU E 471 1 11 HELIX 104 104 MET E 489 GLY E 493 1 5 HELIX 105 105 ALA E 498 THR E 517 1 20 HELIX 106 106 ASN F 9 LYS F 28 1 20 HELIX 107 107 VAL F 29 LEU F 31 5 3 HELIX 108 108 ASP F 52 ILE F 60 1 9 HELIX 109 109 ASP F 64 THR F 81 1 18 HELIX 110 110 ASN F 82 ALA F 85 5 4 HELIX 111 111 ASP F 87 ALA F 109 1 23 HELIX 112 112 ASN F 112 SER F 133 1 22 HELIX 113 113 ALA F 145 SER F 151 1 7 HELIX 114 114 GLU F 155 GLY F 170 1 16 HELIX 115 115 SER F 201 VAL F 205 5 5 HELIX 116 116 ASP F 283 GLY F 297 1 15 HELIX 117 117 GLU F 338 GLU F 354 1 17 HELIX 118 118 TYR F 360 LYS F 371 1 12 HELIX 119 119 THR F 385 GLY F 410 1 26 HELIX 120 120 GLY F 416 ALA F 423 1 8 HELIX 121 121 LYS F 424 GLY F 428 5 5 HELIX 122 122 ASN F 433 LEU F 447 1 15 HELIX 123 123 GLU F 448 GLY F 459 1 12 HELIX 124 124 ASP F 461 GLU F 471 1 11 HELIX 125 125 MET F 489 GLY F 493 1 5 HELIX 126 126 ALA F 498 THR F 517 1 20 HELIX 127 127 ASN G 9 LYS G 28 1 20 HELIX 128 128 VAL G 29 LEU G 31 5 3 HELIX 129 129 ASP G 52 ILE G 60 1 9 HELIX 130 130 ASP G 64 THR G 81 1 18 HELIX 131 131 ASN G 82 ALA G 85 5 4 HELIX 132 132 ASP G 87 ALA G 109 1 23 HELIX 133 133 ASN G 112 SER G 133 1 22 HELIX 134 134 ALA G 145 SER G 151 1 7 HELIX 135 135 GLU G 155 GLY G 170 1 16 HELIX 136 136 SER G 201 VAL G 205 5 5 HELIX 137 137 ASP G 283 GLY G 297 1 15 HELIX 138 138 GLU G 338 GLU G 354 1 17 HELIX 139 139 TYR G 360 LYS G 371 1 12 HELIX 140 140 THR G 385 GLY G 410 1 26 HELIX 141 141 GLY G 416 ALA G 423 1 8 HELIX 142 142 LYS G 424 GLY G 428 5 5 HELIX 143 143 ASN G 433 LEU G 447 1 15 HELIX 144 144 GLU G 448 GLY G 459 1 12 HELIX 145 145 ASP G 461 GLU G 471 1 11 HELIX 146 146 MET G 489 GLY G 493 1 5 HELIX 147 147 ALA G 498 THR G 517 1 20 SHEET 1 A 4 LYS A 4 PHE A 8 0 SHEET 2 A 4 THR A 518 GLU A 524 -1 N MET A 521 O LYS A 7 SHEET 3 A 4 ASN B 37 ILE B 40 1 O ASN B 37 N GLU A 519 SHEET 4 A 4 ARG B 48 THR B 50 -1 O ARG B 48 N ILE B 40 SHEET 1 B 4 ARG A 48 THR A 50 0 SHEET 2 B 4 ASN A 37 ILE A 40 -1 N VAL A 38 O THR A 50 SHEET 3 B 4 THR G 518 GLU G 524 1 N GLU G 519 O ASN A 37 SHEET 4 B 4 LYS G 4 PHE G 8 -1 N GLU G 5 O ALA G 523 SHEET 1 C 3 GLU A 178 GLU A 179 0 SHEET 2 C 3 VAL A 376 VAL A 381 1 O ILE A 379 N GLU A 178 SHEET 3 C 3 GLU A 186 VAL A 190 -1 O GLU A 186 N ARG A 380 SHEET 1 D 6 MET A 193 GLN A 194 0 SHEET 2 D 6 THR A 330 VAL A 333 -1 N ILE A 332 O MET A 193 SHEET 3 D 6 GLY A 318 ILE A 325 -1 N LYS A 322 O VAL A 333 SHEET 4 D 6 ALA A 213 LEU A 222 -1 N ALA A 213 O ILE A 325 SHEET 5 D 6 LEU A 248 ALA A 251 1 N LEU A 248 O TYR A 219 SHEET 6 D 6 ALA A 274 LYS A 277 1 O ALA A 274 N ILE A 249 SHEET 1 E 2 ILE A 411 VAL A 413 0 SHEET 2 E 2 ILE A 495 PRO A 497 -1 N ASP A 496 O VAL A 412 SHEET 1 F 2 PHE A 477 ASN A 480 0 SHEET 2 F 2 GLU A 485 ASP A 488 -1 O GLU A 485 N ASN A 480 SHEET 1 G 4 LYS B 4 PHE B 8 0 SHEET 2 G 4 THR B 518 GLU B 524 -1 N MET B 521 O LYS B 7 SHEET 3 G 4 ASN C 37 ILE C 40 1 O ASN C 37 N GLU B 519 SHEET 4 G 4 ARG C 48 THR C 50 -1 O ARG C 48 N ILE C 40 SHEET 1 H 3 GLU B 178 GLU B 179 0 SHEET 2 H 3 VAL B 376 VAL B 381 1 O ILE B 379 N GLU B 178 SHEET 3 H 3 GLU B 186 VAL B 190 -1 O GLU B 186 N ARG B 380 SHEET 1 I 6 MET B 193 GLN B 194 0 SHEET 2 I 6 THR B 330 VAL B 333 -1 N ILE B 332 O MET B 193 SHEET 3 I 6 GLY B 318 ILE B 325 -1 N LYS B 322 O VAL B 333 SHEET 4 I 6 ALA B 213 LEU B 222 -1 N ALA B 213 O ILE B 325 SHEET 5 I 6 LEU B 248 ALA B 251 1 N LEU B 248 O TYR B 219 SHEET 6 I 6 ALA B 274 LYS B 277 1 O ALA B 274 N ILE B 249 SHEET 1 J 2 ILE B 411 VAL B 413 0 SHEET 2 J 2 ILE B 495 PRO B 497 -1 N ASP B 496 O VAL B 412 SHEET 1 K 2 PHE B 477 ASN B 480 0 SHEET 2 K 2 GLU B 485 ASP B 488 -1 O GLU B 485 N ASN B 480 SHEET 1 L 4 LYS C 4 PHE C 8 0 SHEET 2 L 4 THR C 518 GLU C 524 -1 N MET C 521 O LYS C 7 SHEET 3 L 4 ASN D 37 ILE D 40 1 O ASN D 37 N GLU C 519 SHEET 4 L 4 ARG D 48 THR D 50 -1 O ARG D 48 N ILE D 40 SHEET 1 M 3 GLU C 178 GLU C 179 0 SHEET 2 M 3 VAL C 376 VAL C 381 1 O ILE C 379 N GLU C 178 SHEET 3 M 3 GLU C 186 VAL C 190 -1 O GLU C 186 N ARG C 380 SHEET 1 N 6 MET C 193 GLN C 194 0 SHEET 2 N 6 THR C 330 VAL C 333 -1 N ILE C 332 O MET C 193 SHEET 3 N 6 GLY C 318 ILE C 325 -1 N LYS C 322 O VAL C 333 SHEET 4 N 6 ALA C 213 LEU C 222 -1 N ALA C 213 O ILE C 325 SHEET 5 N 6 LEU C 248 ALA C 251 1 N LEU C 248 O TYR C 219 SHEET 6 N 6 ALA C 274 LYS C 277 1 O ALA C 274 N ILE C 249 SHEET 1 O 2 ILE C 411 VAL C 413 0 SHEET 2 O 2 ILE C 495 PRO C 497 -1 N ASP C 496 O VAL C 412 SHEET 1 P 2 PHE C 477 ASN C 480 0 SHEET 2 P 2 GLU C 485 ASP C 488 -1 O GLU C 485 N ASN C 480 SHEET 1 Q 4 LYS D 4 PHE D 8 0 SHEET 2 Q 4 THR D 518 GLU D 524 -1 N MET D 521 O LYS D 7 SHEET 3 Q 4 ASN E 37 ILE E 40 1 O ASN E 37 N GLU D 519 SHEET 4 Q 4 ARG E 48 THR E 50 -1 O ARG E 48 N ILE E 40 SHEET 1 R 3 GLU D 178 GLU D 179 0 SHEET 2 R 3 VAL D 376 VAL D 381 1 O ILE D 379 N GLU D 178 SHEET 3 R 3 GLU D 186 VAL D 190 -1 O GLU D 186 N ARG D 380 SHEET 1 S 6 MET D 193 GLN D 194 0 SHEET 2 S 6 THR D 330 VAL D 333 -1 N ILE D 332 O MET D 193 SHEET 3 S 6 GLY D 318 ILE D 325 -1 N LYS D 322 O VAL D 333 SHEET 4 S 6 ALA D 213 LEU D 222 -1 N ALA D 213 O ILE D 325 SHEET 5 S 6 LEU D 248 ALA D 251 1 N LEU D 248 O TYR D 219 SHEET 6 S 6 ALA D 274 LYS D 277 1 O ALA D 274 N ILE D 249 SHEET 1 T 2 ILE D 411 VAL D 413 0 SHEET 2 T 2 ILE D 495 PRO D 497 -1 N ASP D 496 O VAL D 412 SHEET 1 U 2 PHE D 477 ASN D 480 0 SHEET 2 U 2 GLU D 485 ASP D 488 -1 O GLU D 485 N ASN D 480 SHEET 1 V 4 LYS E 4 PHE E 8 0 SHEET 2 V 4 THR E 518 GLU E 524 -1 N MET E 521 O LYS E 7 SHEET 3 V 4 ASN F 37 ILE F 40 1 O ASN F 37 N GLU E 519 SHEET 4 V 4 ARG F 48 THR F 50 -1 O ARG F 48 N ILE F 40 SHEET 1 W 3 GLU E 178 GLU E 179 0 SHEET 2 W 3 VAL E 376 VAL E 381 1 O ILE E 379 N GLU E 178 SHEET 3 W 3 GLU E 186 VAL E 190 -1 O GLU E 186 N ARG E 380 SHEET 1 X 6 MET E 193 GLN E 194 0 SHEET 2 X 6 THR E 330 VAL E 333 -1 N ILE E 332 O MET E 193 SHEET 3 X 6 GLY E 318 ILE E 325 -1 N LYS E 322 O VAL E 333 SHEET 4 X 6 ALA E 213 LEU E 222 -1 N ALA E 213 O ILE E 325 SHEET 5 X 6 LEU E 248 ALA E 251 1 N LEU E 248 O TYR E 219 SHEET 6 X 6 ALA E 274 LYS E 277 1 O ALA E 274 N ILE E 249 SHEET 1 Y 2 ILE E 411 VAL E 413 0 SHEET 2 Y 2 ILE E 495 PRO E 497 -1 N ASP E 496 O VAL E 412 SHEET 1 Z 2 PHE E 477 ASN E 480 0 SHEET 2 Z 2 GLU E 485 ASP E 488 -1 O GLU E 485 N ASN E 480 SHEET 1 AA 4 LYS F 4 PHE F 8 0 SHEET 2 AA 4 THR F 518 GLU F 524 -1 N MET F 521 O LYS F 7 SHEET 3 AA 4 ASN G 37 ILE G 40 1 O ASN G 37 N GLU F 519 SHEET 4 AA 4 ARG G 48 THR G 50 -1 O ARG G 48 N ILE G 40 SHEET 1 AB 3 GLU F 178 GLU F 179 0 SHEET 2 AB 3 VAL F 376 VAL F 381 1 O ILE F 379 N GLU F 178 SHEET 3 AB 3 GLU F 186 VAL F 190 -1 O GLU F 186 N ARG F 380 SHEET 1 AC 6 MET F 193 GLN F 194 0 SHEET 2 AC 6 THR F 330 VAL F 333 -1 N ILE F 332 O MET F 193 SHEET 3 AC 6 GLY F 318 ILE F 325 -1 N LYS F 322 O VAL F 333 SHEET 4 AC 6 ALA F 213 LEU F 222 -1 N ALA F 213 O ILE F 325 SHEET 5 AC 6 LEU F 248 ALA F 251 1 N LEU F 248 O TYR F 219 SHEET 6 AC 6 ALA F 274 LYS F 277 1 O ALA F 274 N ILE F 249 SHEET 1 AD 2 ILE F 411 VAL F 413 0 SHEET 2 AD 2 ILE F 495 PRO F 497 -1 N ASP F 496 O VAL F 412 SHEET 1 AE 2 PHE F 477 ASN F 480 0 SHEET 2 AE 2 GLU F 485 ASP F 488 -1 O GLU F 485 N ASN F 480 SHEET 1 AF 3 GLU G 178 GLU G 179 0 SHEET 2 AF 3 VAL G 376 VAL G 381 1 O ILE G 379 N GLU G 178 SHEET 3 AF 3 GLU G 186 VAL G 190 -1 O GLU G 186 N ARG G 380 SHEET 1 AG 6 MET G 193 GLN G 194 0 SHEET 2 AG 6 THR G 330 VAL G 333 -1 N ILE G 332 O MET G 193 SHEET 3 AG 6 GLY G 318 ILE G 325 -1 N LYS G 322 O VAL G 333 SHEET 4 AG 6 ALA G 213 LEU G 222 -1 N ALA G 213 O ILE G 325 SHEET 5 AG 6 LEU G 248 ALA G 251 1 N LEU G 248 O TYR G 219 SHEET 6 AG 6 ALA G 274 LYS G 277 1 O ALA G 274 N ILE G 249 SHEET 1 AH 2 ILE G 411 VAL G 413 0 SHEET 2 AH 2 ILE G 495 PRO G 497 -1 N ASP G 496 O VAL G 412 SHEET 1 AI 2 PHE G 477 ASN G 480 0 SHEET 2 AI 2 GLU G 485 ASP G 488 -1 O GLU G 485 N ASN G 480 CRYST1 286.355 286.355 153.463 90.00 90.00 90.00 P 42 21 2 56 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 0.003492 0.000000 0.000000 0.00000 SCALE2 0.000000 0.003492 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006516 0.00000 MTRIX1 1 0.626133 0.779704 0.004449 -35.93260 1 MTRIX2 1 -0.779714 0.626109 0.005741 101.26306 1 MTRIX3 1 0.001691 -0.007064 0.999974 0.37255 1 MTRIX1 2 -0.215883 0.976347 0.011879 20.59499 1 MTRIX2 2 -0.976413 -0.215909 0.000920 192.73811 1 MTRIX3 2 0.003463 -0.011400 0.999929 0.73311 1 MTRIX1 3 -0.900039 0.435695 0.009930 128.63876 1 MTRIX2 3 -0.435765 -0.900038 -0.006327 205.54558 1 MTRIX3 3 0.006181 -0.010022 0.999931 0.38737 1 MTRIX1 4 -0.901533 -0.432677 0.005391 205.42465 1 MTRIX2 4 0.432606 -0.901519 -0.010797 129.40227 1 MTRIX3 4 0.009532 -0.007401 0.999927 -0.19825 1 MTRIX1 5 -0.228419 -0.973561 -0.001897 194.07994 1 MTRIX2 5 0.973502 -0.228382 -0.011628 22.70074 1 MTRIX3 5 0.010887 -0.004503 0.999931 -0.52396 1 MTRIX1 6 0.619200 -0.785213 -0.005763 102.96165 1 MTRIX2 6 0.785204 0.619223 -0.004092 -35.53516 1 MTRIX3 6 0.006781 -0.001991 0.999975 -0.33774 1 MTRIX1 7 0.622075 0.782952 0.002779 -35.86661 1 MTRIX2 7 -0.782950 0.622051 0.006503 102.22952 1 MTRIX3 7 0.003363 -0.006221 0.999975 -0.01005 1 MTRIX1 8 -0.204779 0.978807 -0.001244 19.06610 1 MTRIX2 8 -0.978783 -0.204765 0.007428 191.41692 1 MTRIX3 8 0.007015 0.002739 0.999972 -1.60970 1 MTRIX1 9 -0.887431 0.460712 0.014524 123.47654 1 MTRIX2 9 -0.460909 -0.887303 -0.016043 207.60902 1 MTRIX3 9 0.005496 -0.020932 0.999766 1.83574 1 MTRIX1 10 -0.897571 -0.440857 0.003310 206.07983 1 MTRIX2 10 0.440809 -0.897547 -0.009809 127.71628 1 MTRIX3 10 0.007296 -0.007345 0.999946 0.06883 1 MTRIX1 11 -0.233327 -0.972361 0.008476 194.36040 1 MTRIX2 11 0.972276 -0.233427 -0.013807 23.63896 1 MTRIX3 11 0.015403 0.005019 0.999869 -2.39584 1 MTRIX1 12 0.592870 -0.805202 -0.012447 109.35307 1 MTRIX2 12 0.805281 0.592888 0.002576 -35.08474 1 MTRIX3 12 0.005305 -0.011551 0.999919 1.03147 1 MTRIX1 13 0.623724 0.781643 0.001666 -35.91305 1 MTRIX2 13 -0.781603 0.623667 0.011651 101.56383 1 MTRIX3 13 0.008068 -0.008569 0.999931 -0.41253 1 MTRIX1 14 -0.219093 0.975637 0.011445 20.60262 1 MTRIX2 14 -0.975626 -0.219209 0.010065 192.77765 1 MTRIX3 14 0.012328 -0.008961 0.999884 -0.86837 1 MTRIX1 15 -0.894498 0.446379 0.024875 125.66047 1 MTRIX2 15 -0.446610 -0.894718 -0.004399 206.15771 1 MTRIX3 15 0.020293 -0.015044 0.999681 -0.88984 1 MTRIX1 16 -0.903372 -0.428764 0.009010 205.04071 1 MTRIX2 16 0.428708 -0.903412 -0.007540 129.94191 1 MTRIX3 16 0.011373 -0.002949 0.999931 -1.11375 1 MTRIX1 17 -0.220294 -0.975398 0.008350 192.99123 1 MTRIX2 17 0.975219 -0.220417 -0.019075 21.88970 1 MTRIX3 17 0.020446 0.003941 0.999783 -2.90347 1 MTRIX1 18 0.611836 -0.790519 -0.027136 105.92568 1 MTRIX2 18 0.790682 0.612191 -0.006638 -35.21476 1 MTRIX3 18 0.021860 -0.017394 0.999610 -0.60083 1