HEADER PROTEIN FIBRIL 24-MAY-17 5O3O
TITLE PRONASE-TREATED PAIRED HELICAL FILAMENT IN ALZHEIMER'S DISEASE BRAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MICROTUBULE-ASSOCIATED PROTEIN TAU;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J;
COMPND 4 FRAGMENT: UNP RESIDUES 623-695;
COMPND 5 SYNONYM: NEUROFIBRILLARY TANGLE PROTEIN,PAIRED HELICAL FILAMENT-TAU,
COMPND 6 PHF-TAU
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS TAU, AMYLOID, CROSS-BETA, BETA-HELIX, PROTEIN FIBRIL
EXPDTA ELECTRON MICROSCOPY
AUTHOR A.W.P.FITZPATRICK,B.FALCON,S.HE,A.G.MURZIN,G.MURSHUDOV,H.G.GARRINGER,
AUTHOR 2 R.A.CROWTHER,B.GHETTI,M.GOEDERT,S.H.W.SCHERES
REVDAT 2 02-AUG-17 5O3O 1
REVDAT 1 26-JUL-17 5O3O 0
JRNL AUTH A.W.P.FITZPATRICK,B.FALCON,S.HE,A.G.MURZIN,G.MURSHUDOV,
JRNL AUTH 2 H.J.GARRINGER,R.A.CROWTHER,B.GHETTI,M.GOEDERT,S.H.W.SCHERES
JRNL TITL CRYO-EM STRUCTURES OF TAU FILAMENTS FROM ALZHEIMER'S
JRNL TITL 2 DISEASE.
JRNL REF NATURE V. 547 185 2017
JRNL REFN ESSN 1476-4687
JRNL PMID 28678775
JRNL DOI 10.1038/NATURE23002
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : RELION, GCTF, COOT, REFMAC, RELION,
REMARK 3 RELION, RELION
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 2RNM
REMARK 3 REFINEMENT SPACE : RECIPROCAL
REMARK 3 REFINEMENT PROTOCOL : AB INITIO MODEL
REMARK 3 REFINEMENT TARGET : FOURIER SHELL CORRELATION
REMARK 3 OVERALL ANISOTROPIC B VALUE : 106.000
REMARK 3
REMARK 3 FITTING PROCEDURE : FOURIER-SPACE REFINEMENT OF THE COMPLETE
REMARK 3 ATOMIC MODEL AGAINST THE PAIRED HELICAL FILAMENT AND STRAIGHT
REMARK 3 FILAMENT MAPS WAS PERFORMED IN REFMAC. A STACK OF THREE
REMARK 3 CONSECUTIVE MONOMERS FROM EACH OF THE PROTOFILAMENTS WAS REFINED
REMARK 3 TO PRESERVE NEAREST-NEIGHBOUR INTERACTIONS FOR THE MIDDLE CHAIN.
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.500
REMARK 3 NUMBER OF PARTICLES : 20778
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 5O3O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1200005138.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : HELICAL
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : TISSUE
REMARK 245 PARTICLE TYPE : HELICAL
REMARK 245 NAME OF SAMPLE : TAU FROM BRAIN
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.00
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.40
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 523
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K2 QUANTUM (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 900.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 3000.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 2.50
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 51350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -177.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J
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 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 ASP A 348 74.64 61.46
REMARK 500 ARG A 349 53.86 70.38
REMARK 500 VAL A 363 71.54 -116.30
REMARK 500 ASP B 348 74.59 61.50
REMARK 500 ARG B 349 53.88 70.29
REMARK 500 VAL B 363 71.54 -116.17
REMARK 500 ASP C 348 74.68 61.48
REMARK 500 ARG C 349 53.75 70.48
REMARK 500 VAL C 363 71.62 -116.27
REMARK 500 ASP D 348 74.66 61.35
REMARK 500 ARG D 349 53.89 70.32
REMARK 500 VAL D 363 71.65 -116.29
REMARK 500 ASP E 348 74.62 61.41
REMARK 500 ARG E 349 53.80 70.40
REMARK 500 VAL E 363 71.58 -116.15
REMARK 500 ASP F 348 74.48 61.46
REMARK 500 ARG F 349 53.87 70.37
REMARK 500 VAL F 363 71.60 -116.30
REMARK 500 ASP G 348 74.65 61.54
REMARK 500 ARG G 349 53.79 70.33
REMARK 500 VAL G 363 71.51 -116.20
REMARK 500 ASP H 348 74.45 61.49
REMARK 500 ARG H 349 53.83 70.40
REMARK 500 VAL H 363 71.68 -116.37
REMARK 500 ASP I 348 74.63 61.51
REMARK 500 ARG I 349 53.77 70.46
REMARK 500 VAL I 363 71.53 -116.17
REMARK 500 ASP J 348 74.39 61.55
REMARK 500 ARG J 349 53.81 70.47
REMARK 500 VAL J 363 71.63 -116.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-3742 RELATED DB: EMDB
REMARK 900 PRONASE-TREATED PAIRED HELICAL FILAMENTS IN ALZHEIMER'S DISEASE
REMARK 900 BRAIN
DBREF 5O3O A 306 378 UNP P10636 TAU_HUMAN 623 695
DBREF 5O3O B 306 378 UNP P10636 TAU_HUMAN 623 695
DBREF 5O3O C 306 378 UNP P10636 TAU_HUMAN 623 695
DBREF 5O3O D 306 378 UNP P10636 TAU_HUMAN 623 695
DBREF 5O3O E 306 378 UNP P10636 TAU_HUMAN 623 695
DBREF 5O3O F 306 378 UNP P10636 TAU_HUMAN 623 695
DBREF 5O3O G 306 378 UNP P10636 TAU_HUMAN 623 695
DBREF 5O3O H 306 378 UNP P10636 TAU_HUMAN 623 695
DBREF 5O3O I 306 378 UNP P10636 TAU_HUMAN 623 695
DBREF 5O3O J 306 378 UNP P10636 TAU_HUMAN 623 695
SEQRES 1 A 73 VAL GLN ILE VAL TYR LYS PRO VAL ASP LEU SER LYS VAL
SEQRES 2 A 73 THR SER LYS CYS GLY SER LEU GLY ASN ILE HIS HIS LYS
SEQRES 3 A 73 PRO GLY GLY GLY GLN VAL GLU VAL LYS SER GLU LYS LEU
SEQRES 4 A 73 ASP PHE LYS ASP ARG VAL GLN SER LYS ILE GLY SER LEU
SEQRES 5 A 73 ASP ASN ILE THR HIS VAL PRO GLY GLY GLY ASN LYS LYS
SEQRES 6 A 73 ILE GLU THR HIS LYS LEU THR PHE
SEQRES 1 B 73 VAL GLN ILE VAL TYR LYS PRO VAL ASP LEU SER LYS VAL
SEQRES 2 B 73 THR SER LYS CYS GLY SER LEU GLY ASN ILE HIS HIS LYS
SEQRES 3 B 73 PRO GLY GLY GLY GLN VAL GLU VAL LYS SER GLU LYS LEU
SEQRES 4 B 73 ASP PHE LYS ASP ARG VAL GLN SER LYS ILE GLY SER LEU
SEQRES 5 B 73 ASP ASN ILE THR HIS VAL PRO GLY GLY GLY ASN LYS LYS
SEQRES 6 B 73 ILE GLU THR HIS LYS LEU THR PHE
SEQRES 1 C 73 VAL GLN ILE VAL TYR LYS PRO VAL ASP LEU SER LYS VAL
SEQRES 2 C 73 THR SER LYS CYS GLY SER LEU GLY ASN ILE HIS HIS LYS
SEQRES 3 C 73 PRO GLY GLY GLY GLN VAL GLU VAL LYS SER GLU LYS LEU
SEQRES 4 C 73 ASP PHE LYS ASP ARG VAL GLN SER LYS ILE GLY SER LEU
SEQRES 5 C 73 ASP ASN ILE THR HIS VAL PRO GLY GLY GLY ASN LYS LYS
SEQRES 6 C 73 ILE GLU THR HIS LYS LEU THR PHE
SEQRES 1 D 73 VAL GLN ILE VAL TYR LYS PRO VAL ASP LEU SER LYS VAL
SEQRES 2 D 73 THR SER LYS CYS GLY SER LEU GLY ASN ILE HIS HIS LYS
SEQRES 3 D 73 PRO GLY GLY GLY GLN VAL GLU VAL LYS SER GLU LYS LEU
SEQRES 4 D 73 ASP PHE LYS ASP ARG VAL GLN SER LYS ILE GLY SER LEU
SEQRES 5 D 73 ASP ASN ILE THR HIS VAL PRO GLY GLY GLY ASN LYS LYS
SEQRES 6 D 73 ILE GLU THR HIS LYS LEU THR PHE
SEQRES 1 E 73 VAL GLN ILE VAL TYR LYS PRO VAL ASP LEU SER LYS VAL
SEQRES 2 E 73 THR SER LYS CYS GLY SER LEU GLY ASN ILE HIS HIS LYS
SEQRES 3 E 73 PRO GLY GLY GLY GLN VAL GLU VAL LYS SER GLU LYS LEU
SEQRES 4 E 73 ASP PHE LYS ASP ARG VAL GLN SER LYS ILE GLY SER LEU
SEQRES 5 E 73 ASP ASN ILE THR HIS VAL PRO GLY GLY GLY ASN LYS LYS
SEQRES 6 E 73 ILE GLU THR HIS LYS LEU THR PHE
SEQRES 1 F 73 VAL GLN ILE VAL TYR LYS PRO VAL ASP LEU SER LYS VAL
SEQRES 2 F 73 THR SER LYS CYS GLY SER LEU GLY ASN ILE HIS HIS LYS
SEQRES 3 F 73 PRO GLY GLY GLY GLN VAL GLU VAL LYS SER GLU LYS LEU
SEQRES 4 F 73 ASP PHE LYS ASP ARG VAL GLN SER LYS ILE GLY SER LEU
SEQRES 5 F 73 ASP ASN ILE THR HIS VAL PRO GLY GLY GLY ASN LYS LYS
SEQRES 6 F 73 ILE GLU THR HIS LYS LEU THR PHE
SEQRES 1 G 73 VAL GLN ILE VAL TYR LYS PRO VAL ASP LEU SER LYS VAL
SEQRES 2 G 73 THR SER LYS CYS GLY SER LEU GLY ASN ILE HIS HIS LYS
SEQRES 3 G 73 PRO GLY GLY GLY GLN VAL GLU VAL LYS SER GLU LYS LEU
SEQRES 4 G 73 ASP PHE LYS ASP ARG VAL GLN SER LYS ILE GLY SER LEU
SEQRES 5 G 73 ASP ASN ILE THR HIS VAL PRO GLY GLY GLY ASN LYS LYS
SEQRES 6 G 73 ILE GLU THR HIS LYS LEU THR PHE
SEQRES 1 H 73 VAL GLN ILE VAL TYR LYS PRO VAL ASP LEU SER LYS VAL
SEQRES 2 H 73 THR SER LYS CYS GLY SER LEU GLY ASN ILE HIS HIS LYS
SEQRES 3 H 73 PRO GLY GLY GLY GLN VAL GLU VAL LYS SER GLU LYS LEU
SEQRES 4 H 73 ASP PHE LYS ASP ARG VAL GLN SER LYS ILE GLY SER LEU
SEQRES 5 H 73 ASP ASN ILE THR HIS VAL PRO GLY GLY GLY ASN LYS LYS
SEQRES 6 H 73 ILE GLU THR HIS LYS LEU THR PHE
SEQRES 1 I 73 VAL GLN ILE VAL TYR LYS PRO VAL ASP LEU SER LYS VAL
SEQRES 2 I 73 THR SER LYS CYS GLY SER LEU GLY ASN ILE HIS HIS LYS
SEQRES 3 I 73 PRO GLY GLY GLY GLN VAL GLU VAL LYS SER GLU LYS LEU
SEQRES 4 I 73 ASP PHE LYS ASP ARG VAL GLN SER LYS ILE GLY SER LEU
SEQRES 5 I 73 ASP ASN ILE THR HIS VAL PRO GLY GLY GLY ASN LYS LYS
SEQRES 6 I 73 ILE GLU THR HIS LYS LEU THR PHE
SEQRES 1 J 73 VAL GLN ILE VAL TYR LYS PRO VAL ASP LEU SER LYS VAL
SEQRES 2 J 73 THR SER LYS CYS GLY SER LEU GLY ASN ILE HIS HIS LYS
SEQRES 3 J 73 PRO GLY GLY GLY GLN VAL GLU VAL LYS SER GLU LYS LEU
SEQRES 4 J 73 ASP PHE LYS ASP ARG VAL GLN SER LYS ILE GLY SER LEU
SEQRES 5 J 73 ASP ASN ILE THR HIS VAL PRO GLY GLY GLY ASN LYS LYS
SEQRES 6 J 73 ILE GLU THR HIS LYS LEU THR PHE
SHEET 1 1 1 VAL A 306 LYS A 311 0
SHEET 1 2 1 VAL A 313 CYS A 322 0
SHEET 1 3 1 ASN A 327 LYS A 331 0
SHEET 1 4 1 GLN A 336 SER A 341 0
SHEET 1 5 1 LYS A 343 LYS A 347 0
SHEET 1 6 1 ARG A 349 ILE A 354 0
SHEET 1 7 1 SER A 356 VAL A 363 0
SHEET 1 8 1 ASN A 368 PHE A 378 0
SHEET 1 9 1 VAL B 306 LYS B 311 0
SHEET 1 10 1 VAL B 313 CYS B 322 0
SHEET 1 11 1 ASN B 327 LYS B 331 0
SHEET 1 12 1 GLN B 336 SER B 341 0
SHEET 1 13 1 LYS B 343 LYS B 347 0
SHEET 1 14 1 ARG B 349 ILE B 354 0
SHEET 1 15 1 SER B 356 VAL B 363 0
SHEET 1 16 1 ASN B 368 PHE B 378 0
SHEET 1 17 1 VAL C 306 LYS C 311 0
SHEET 1 18 1 VAL C 313 CYS C 322 0
SHEET 1 19 1 ASN C 327 LYS C 331 0
SHEET 1 20 1 GLN C 336 SER C 341 0
SHEET 1 21 1 LYS C 343 LYS C 347 0
SHEET 1 22 1 ARG C 349 ILE C 354 0
SHEET 1 23 1 SER C 356 VAL C 363 0
SHEET 1 24 1 ASN C 368 PHE C 378 0
SHEET 1 25 1 VAL D 306 LYS D 311 0
SHEET 1 26 1 VAL D 313 CYS D 322 0
SHEET 1 27 1 ASN D 327 LYS D 331 0
SHEET 1 28 1 GLN D 336 SER D 341 0
SHEET 1 29 1 LYS D 343 LYS D 347 0
SHEET 1 30 1 ARG D 349 ILE D 354 0
SHEET 1 31 1 SER D 356 VAL D 363 0
SHEET 1 32 1 ASN D 368 PHE D 378 0
SHEET 1 33 1 VAL E 306 LYS E 311 0
SHEET 1 34 1 VAL E 313 CYS E 322 0
SHEET 1 35 1 ASN E 327 LYS E 331 0
SHEET 1 36 1 GLN E 336 SER E 341 0
SHEET 1 37 1 LYS E 343 LYS E 347 0
SHEET 1 38 1 ARG E 349 ILE E 354 0
SHEET 1 39 1 SER E 356 VAL E 363 0
SHEET 1 40 1 ASN E 368 PHE E 378 0
SHEET 1 41 1 VAL F 306 LYS F 311 0
SHEET 1 42 1 VAL F 313 CYS F 322 0
SHEET 1 43 1 ASN F 327 LYS F 331 0
SHEET 1 44 1 GLN F 336 SER F 341 0
SHEET 1 45 1 LYS F 343 LYS F 347 0
SHEET 1 46 1 ARG F 349 ILE F 354 0
SHEET 1 47 1 SER F 356 VAL F 363 0
SHEET 1 48 1 ASN F 368 PHE F 378 0
SHEET 1 49 1 VAL G 306 LYS G 311 0
SHEET 1 50 1 VAL G 313 CYS G 322 0
SHEET 1 51 1 ASN G 327 LYS G 331 0
SHEET 1 52 1 GLN G 336 SER G 341 0
SHEET 1 53 1 LYS G 343 LYS G 347 0
SHEET 1 54 1 ARG G 349 ILE G 354 0
SHEET 1 55 1 SER G 356 VAL G 363 0
SHEET 1 56 1 ASN G 368 PHE G 378 0
SHEET 1 57 1 VAL H 306 LYS H 311 0
SHEET 1 58 1 VAL H 313 CYS H 322 0
SHEET 1 59 1 ASN H 327 LYS H 331 0
SHEET 1 60 1 GLN H 336 SER H 341 0
SHEET 1 61 1 LYS H 343 LYS H 347 0
SHEET 1 62 1 ARG H 349 ILE H 354 0
SHEET 1 63 1 SER H 356 VAL H 363 0
SHEET 1 64 1 ASN H 368 PHE H 378 0
SHEET 1 65 1 VAL I 306 LYS I 311 0
SHEET 1 66 1 VAL I 313 CYS I 322 0
SHEET 1 67 1 ASN I 327 LYS I 331 0
SHEET 1 68 1 GLN I 336 SER I 341 0
SHEET 1 69 1 LYS I 343 LYS I 347 0
SHEET 1 70 1 ARG I 349 ILE I 354 0
SHEET 1 71 1 SER I 356 VAL I 363 0
SHEET 1 72 1 ASN I 368 PHE I 378 0
SHEET 1 73 1 VAL J 306 LYS J 311 0
SHEET 1 74 1 VAL J 313 CYS J 322 0
SHEET 1 75 1 ASN J 327 LYS J 331 0
SHEET 1 76 1 GLN J 336 SER J 341 0
SHEET 1 77 1 LYS J 343 LYS J 347 0
SHEET 1 78 1 ARG J 349 ILE J 354 0
SHEET 1 79 1 SER J 356 VAL J 363 0
SHEET 1 80 1 ASN J 368 PHE J 378 0
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
