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HEADER HYDROLASE 15-SEP-14 4WFK
TITLE CRYSTAL STRUCTURE OF PET-DEGRADING CUTINASE CUT190 S226P MUTANT IN
TITLE 2 CA(2+)-BOUND STATE AT 2.35 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 47-304;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMONOSPORA VIRIDIS;
SOURCE 3 ORGANISM_TAXID: 1852;
SOURCE 4 STRAIN: AHK190;
SOURCE 5 GENE: CUT190;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA-GAMI B (DE3)
KEYWDS CUTINASE, POLYESTERASE, ALPHA/BETA-HYDROLASE FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR T.MIYAKAWA,H.MIZUSHIMA,J.OHTSUKA,M.ODA,F.KAWAI,M.TANOKURA
REVDAT 1 24-DEC-14 4WFK 0
JRNL AUTH T.MIYAKAWA,H.MIZUSHIMA,J.OHTSUKA,M.ODA,F.KAWAI,M.TANOKURA
JRNL TITL STRUCTURAL BASIS FOR THE CA(2+)-ENHANCED THERMOSTABILITY AND
JRNL TITL 2 ACTIVITY OF PET-DEGRADING CUTINASE-LIKE ENZYME FROM
JRNL TITL 3 SACCHAROMONOSPORA VIRIDIS AHK190.
JRNL REF APPL.MICROBIOL.BIOTECHNOL. 2014
JRNL REFN ESSN 1432-0614
JRNL PMID 25492421
JRNL DOI 10.1007/S00253-014-6272-8
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.57
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 10973
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.790
REMARK 3 FREE R VALUE TEST SET COUNT : 526
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 19.5719 - 3.7239 1.00 2720 136 0.1431 0.1841
REMARK 3 2 3.7239 - 2.9591 1.00 2610 136 0.1749 0.2256
REMARK 3 3 2.9591 - 2.5860 1.00 2577 137 0.2002 0.2893
REMARK 3 4 2.5860 - 2.3500 0.99 2540 117 0.2040 0.2968
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.100
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 2065
REMARK 3 ANGLE : 1.092 2811
REMARK 3 CHIRALITY : 0.040 302
REMARK 3 PLANARITY : 0.006 372
REMARK 3 DIHEDRAL : 12.761 761
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4WFK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1000203666.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-FEB-14
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.900
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20285
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 29.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM FLUORIDE, 20% (W/V) PEG
REMARK 280 3350
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 27.31500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.07000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.95000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 35.07000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.31500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.95000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 35
REMARK 465 ARG A 36
REMARK 465 GLY A 37
REMARK 465 SER A 38
REMARK 465 HIS A 39
REMARK 465 HIS A 40
REMARK 465 HIS A 41
REMARK 465 HIS A 42
REMARK 465 HIS A 43
REMARK 465 HIS A 44
REMARK 465 GLY A 45
REMARK 465 SER A 46
REMARK 465 LYS A 305
REMARK 465 LEU A 306
REMARK 465 ASN A 307
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 SER A 176 -120.70 63.54
REMARK 500 THR A 199 58.31 35.56
REMARK 500 HIS A 230 -85.63 -122.80
REMARK 500 ASP A 292 148.12 -38.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 76 O
REMARK 620 2 ALA A 78 O 94.7
REMARK 620 3 PHE A 81 O 89.9 71.9
REMARK 620 4 HOH A 510 O 177.0 84.3 87.1
REMARK 620 5 HOH A 523 O 97.8 99.9 169.2 85.1
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4WFI RELATED DB: PDB
REMARK 900 RELATED ID: 4WFJ RELATED DB: PDB
DBREF 4WFK A 47 304 UNP W0TJ64 W0TJ64_9PSEU 47 304
SEQADV 4WFK MET A 35 UNP W0TJ64 EXPRESSION TAG
SEQADV 4WFK ARG A 36 UNP W0TJ64 EXPRESSION TAG
SEQADV 4WFK GLY A 37 UNP W0TJ64 EXPRESSION TAG
SEQADV 4WFK SER A 38 UNP W0TJ64 EXPRESSION TAG
SEQADV 4WFK HIS A 39 UNP W0TJ64 EXPRESSION TAG
SEQADV 4WFK HIS A 40 UNP W0TJ64 EXPRESSION TAG
SEQADV 4WFK HIS A 41 UNP W0TJ64 EXPRESSION TAG
SEQADV 4WFK HIS A 42 UNP W0TJ64 EXPRESSION TAG
SEQADV 4WFK HIS A 43 UNP W0TJ64 EXPRESSION TAG
SEQADV 4WFK HIS A 44 UNP W0TJ64 EXPRESSION TAG
SEQADV 4WFK GLY A 45 UNP W0TJ64 EXPRESSION TAG
SEQADV 4WFK SER A 46 UNP W0TJ64 EXPRESSION TAG
SEQADV 4WFK PRO A 226 UNP W0TJ64 SER 226 ENGINEERED MUTATION
SEQADV 4WFK LYS A 305 UNP W0TJ64 EXPRESSION TAG
SEQADV 4WFK LEU A 306 UNP W0TJ64 EXPRESSION TAG
SEQADV 4WFK ASN A 307 UNP W0TJ64 EXPRESSION TAG
SEQRES 1 A 273 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASN
SEQRES 2 A 273 PRO TYR GLU ARG GLY PRO ASP PRO THR GLU ASP SER ILE
SEQRES 3 A 273 GLU ALA ILE ARG GLY PRO PHE SER VAL ALA THR GLU ARG
SEQRES 4 A 273 VAL SER SER PHE ALA SER GLY PHE GLY GLY GLY THR ILE
SEQRES 5 A 273 TYR TYR PRO ARG GLU THR ASP GLU GLY THR PHE GLY ALA
SEQRES 6 A 273 VAL ALA VAL ALA PRO GLY PHE THR ALA SER GLN GLY SER
SEQRES 7 A 273 MET SER TRP TYR GLY GLU ARG VAL ALA SER GLN GLY PHE
SEQRES 8 A 273 ILE VAL PHE THR ILE ASP THR ASN THR ARG LEU ASP GLN
SEQRES 9 A 273 PRO GLY GLN ARG GLY ARG GLN LEU LEU ALA ALA LEU ASP
SEQRES 10 A 273 TYR LEU VAL GLU ARG SER ASP ARG LYS VAL ARG GLU ARG
SEQRES 11 A 273 LEU ASP PRO ASN ARG LEU ALA VAL MET GLY HIS SER MET
SEQRES 12 A 273 GLY GLY GLY GLY SER LEU GLU ALA THR VAL MET ARG PRO
SEQRES 13 A 273 SER LEU LYS ALA SER ILE PRO LEU THR PRO TRP ASN LEU
SEQRES 14 A 273 ASP LYS THR TRP GLY GLN VAL GLN VAL PRO THR PHE ILE
SEQRES 15 A 273 ILE GLY ALA GLU LEU ASP THR ILE ALA PRO VAL ARG THR
SEQRES 16 A 273 HIS ALA LYS PRO PHE TYR GLU SER LEU PRO SER SER LEU
SEQRES 17 A 273 PRO LYS ALA TYR MET GLU LEU ASP GLY ALA THR HIS PHE
SEQRES 18 A 273 ALA PRO ASN ILE PRO ASN THR THR ILE ALA LYS TYR VAL
SEQRES 19 A 273 ILE SER TRP LEU LYS ARG PHE VAL ASP GLU ASP THR ARG
SEQRES 20 A 273 TYR SER GLN PHE LEU CYS PRO ASN PRO THR ASP ARG ALA
SEQRES 21 A 273 ILE GLU GLU TYR ARG SER THR CYS PRO TYR LYS LEU ASN
HET CA A 401 1
HET CL A 402 1
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
FORMUL 2 CA CA 2+
FORMUL 3 CL CL 1-
FORMUL 4 HOH *65(H2 O)
HELIX 1 AA1 ASP A 58 ALA A 62 5 5
HELIX 2 AA2 SER A 109 SER A 114 5 6
HELIX 3 AA3 TRP A 115 SER A 122 1 8
HELIX 4 AA4 GLN A 138 SER A 157 1 20
HELIX 5 AA5 ASP A 158 GLU A 163 1 6
HELIX 6 AA6 SER A 176 ARG A 189 1 14
HELIX 7 AA7 HIS A 230 LEU A 238 1 9
HELIX 8 AA8 PHE A 255 ILE A 259 5 5
HELIX 9 AA9 ASN A 261 ASP A 277 1 17
HELIX 10 AB1 ASP A 279 ARG A 281 5 3
HELIX 11 AB2 TYR A 282 CYS A 287 1 6
SHEET 1 AA1 6 VAL A 69 VAL A 74 0
SHEET 2 AA1 6 GLY A 84 PRO A 89 -1 O GLY A 84 N VAL A 74
SHEET 3 AA1 6 ILE A 126 ILE A 130 -1 O VAL A 127 N TYR A 87
SHEET 4 AA1 6 PHE A 97 ALA A 103 1 N VAL A 102 O PHE A 128
SHEET 5 AA1 6 LEU A 165 HIS A 175 1 O HIS A 175 N ALA A 103
SHEET 6 AA1 6 ALA A 194 LEU A 198 1 O LEU A 198 N GLY A 174
SHEET 1 AA2 3 THR A 214 ALA A 219 0
SHEET 2 AA2 3 LYS A 244 LEU A 249 1 O LEU A 249 N GLY A 218
SHEET 3 AA2 3 ILE A 295 SER A 300 -1 O GLU A 297 N GLU A 248
SSBOND 1 CYS A 287 CYS A 302 1555 1555 2.06
LINK O SER A 76 CA CA A 401 1555 1555 2.96
LINK O ALA A 78 CA CA A 401 1555 1555 2.56
LINK O PHE A 81 CA CA A 401 1555 1555 2.93
LINK CA CA A 401 O HOH A 510 1555 1555 2.72
LINK CA CA A 401 O HOH A 523 1555 4455 2.86
CISPEP 1 CYS A 287 PRO A 288 0 3.00
CISPEP 2 CYS A 302 PRO A 303 0 -0.88
SITE 1 AC1 6 SER A 76 ALA A 78 PHE A 81 ASN A 133
SITE 2 AC1 6 HOH A 510 HOH A 523
SITE 1 AC2 2 THR A 223 HIS A 254
CRYST1 54.630 65.900 70.140 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.018305 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015175 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014257 0.00000
TER 2011 TYR A 304
MASTER 260 0 2 11 9 0 3 6 2077 1 7 21
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