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HEADER HYDROLASE 11-MAR-25 9M8H
TITLE CRYSTAL STRUCTURE OF WILD-TYPE PETASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PET HYDROLASE,PETASE,PET-DIGESTING ENZYME;
COMPND 5 EC: 3.1.1.101;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PISCINIBACTER SAKAIENSIS;
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 GENE: ISF6_4831;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PET-DEGRADING HYDROLASE, IDEONELLA SAKAIENSIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.F.CHEK,S.YOSHIDA,T.HAKOSHIMA
REVDAT 1 21-JAN-26 9M8H 0
JRNL AUTH M.F.CHEK,E.KAWANO,R.SANUKI,K.NISHIMURA,S.I.HACHISUKA,
JRNL AUTH 2 T.HAKOSHIMA,S.YOSHIDA
JRNL TITL ENHANCING THE SPECIFICITY OF A THERMOSTABLE PET HYDROLASE
JRNL TITL 2 TOWARD AROMATIC POLYESTERS VIA PISCINIBACTER SAKAIENSIS
JRNL TITL 3 PETASE-INSPIRED MUTATIONS.
JRNL REF INT.J.BIOL.MACROMOL. V. 338 49745 2025
JRNL REFN ISSN 0141-8130
JRNL PMID 41418965
JRNL DOI 10.1016/J.IJBIOMAC.2025.149745
REMARK 2
REMARK 2 RESOLUTION. 1.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.21_5207
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.46
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.460
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 3 NUMBER OF REFLECTIONS : 54214
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.117
REMARK 3 R VALUE (WORKING SET) : 0.116
REMARK 3 FREE R VALUE : 0.140
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.670
REMARK 3 FREE R VALUE TEST SET COUNT : 3800
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 47.4600 - 3.9100 1.00 3928 139 0.1406 0.1551
REMARK 3 2 3.9000 - 3.1000 1.00 3897 155 0.1305 0.1365
REMARK 3 3 3.1000 - 2.7100 1.00 3912 155 0.1317 0.1738
REMARK 3 4 2.7100 - 2.4600 1.00 3906 147 0.1296 0.1422
REMARK 3 5 2.4600 - 2.2800 1.00 3940 143 0.1186 0.1325
REMARK 3 6 2.2800 - 2.1500 1.00 3903 148 0.1112 0.1361
REMARK 3 7 2.1500 - 2.0400 1.00 3909 156 0.1065 0.1166
REMARK 3 8 2.0400 - 1.9500 1.00 3944 140 0.1062 0.1041
REMARK 3 9 1.9500 - 1.8800 1.00 3892 174 0.0981 0.1288
REMARK 3 10 1.8800 - 1.8100 1.00 3885 135 0.1010 0.1346
REMARK 3 11 1.8100 - 1.7600 1.00 3887 149 0.1007 0.1355
REMARK 3 12 1.7600 - 1.7100 1.00 3939 150 0.0988 0.1359
REMARK 3 13 1.7100 - 1.6600 1.00 3902 145 0.0988 0.1317
REMARK 3 14 1.6600 - 1.6200 1.00 3941 169 0.0987 0.1287
REMARK 3 15 1.6200 - 1.5800 1.00 3905 131 0.0961 0.1218
REMARK 3 16 1.5800 - 1.5500 1.00 3912 144 0.0935 0.1240
REMARK 3 17 1.5500 - 1.5200 1.00 3904 163 0.0912 0.1326
REMARK 3 18 1.5200 - 1.4900 1.00 3926 133 0.0827 0.1113
REMARK 3 19 1.4900 - 1.4600 1.00 3893 172 0.0871 0.1255
REMARK 3 20 1.4600 - 1.4400 0.97 3801 128 0.0876 0.1229
REMARK 3 21 1.4400 - 1.4200 0.98 3779 162 0.0945 0.1442
REMARK 3 22 1.4200 - 1.3900 0.93 3686 127 0.1036 0.1288
REMARK 3 23 1.3900 - 1.3700 0.86 3418 108 0.1135 0.1940
REMARK 3 24 1.3700 - 1.3500 0.82 3132 144 0.1273 0.1771
REMARK 3 25 1.3500 - 1.3400 0.74 2879 123 0.1376 0.1610
REMARK 3 26 1.3400 - 1.3200 0.69 2687 85 0.1625 0.2327
REMARK 3 27 1.3200 - 1.3000 0.49 1907 75 0.1872 0.3248
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.100
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 12.061
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.32
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.81
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 2000
REMARK 3 ANGLE : 1.031 2723
REMARK 3 CHIRALITY : 0.091 298
REMARK 3 PLANARITY : 0.013 360
REMARK 3 DIHEDRAL : 11.576 710
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 9M8H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-MAR-25.
REMARK 100 THE DEPOSITION ID IS D_1300056480.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-NOV-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL45XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54275
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 47.460
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 200 DATA REDUNDANCY : 10.96
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.0700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 69.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.58
REMARK 200 R MERGE FOR SHELL (I) : 0.22900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BICINE-NAOH (PH 8.8), 30% (V/V)
REMARK 280 PEG 6000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 25.60150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 34.66200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.55800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 34.66200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.60150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.55800
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 GLY A 26
REMARK 465 PRO A 27
REMARK 465 GLN A 28
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 73 42.70 -143.20
REMARK 500 THR A 88 -7.89 74.92
REMARK 500 SER A 160 -124.05 67.17
REMARK 500 SER A 214 -85.14 -124.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 123 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 9M8H A 28 290 UNP PETH_PISS1
DBREF2 9M8H A A0A0K8P6T7 28 290
SEQADV 9M8H GLY A 26 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 9M8H PRO A 27 UNP A0A0K8P6T EXPRESSION TAG
SEQRES 1 A 265 GLY PRO GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO
SEQRES 2 A 265 THR ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR
SEQRES 3 A 265 VAL ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY
SEQRES 4 A 265 ALA GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR
SEQRES 5 A 265 VAL GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG
SEQRES 6 A 265 GLN SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER
SEQRES 7 A 265 HIS GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR
SEQRES 8 A 265 LEU ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA
SEQRES 9 A 265 ALA LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER
SEQRES 10 A 265 SER PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY
SEQRES 11 A 265 VAL MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE
SEQRES 12 A 265 SER ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO
SEQRES 13 A 265 GLN ALA PRO TRP ASP SER SER THR ASN PHE SER SER VAL
SEQRES 14 A 265 THR VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER
SEQRES 15 A 265 ILE ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP
SEQRES 16 A 265 SER MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN
SEQRES 17 A 265 GLY GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN
SEQRES 18 A 265 GLN ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS
SEQRES 19 A 265 ARG PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA
SEQRES 20 A 265 CYS GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG
SEQRES 21 A 265 THR ALA ASN CYS SER
HET GOL A 301 6
HET GOL A 302 6
HET GOL A 303 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL 3(C3 H8 O3)
FORMUL 5 HOH *327(H2 O)
HELIX 1 AA1 THR A 39 ALA A 45 1 7
HELIX 2 AA2 ARG A 90 LYS A 95 5 6
HELIX 3 AA3 TRP A 96 SER A 103 1 8
HELIX 4 AA4 GLN A 119 GLY A 139 1 21
HELIX 5 AA5 SER A 160 ASN A 173 1 14
HELIX 6 AA6 SER A 214 MET A 222 1 9
HELIX 7 AA7 ASN A 246 ASP A 263 1 18
HELIX 8 AA8 ASP A 265 ARG A 267 5 3
HELIX 9 AA9 TYR A 268 GLU A 274 1 7
SHEET 1 AA1 6 VAL A 52 THR A 56 0
SHEET 2 AA1 6 ALA A 65 PRO A 71 -1 O VAL A 68 N PHE A 55
SHEET 3 AA1 6 VAL A 107 ASP A 112 -1 O VAL A 108 N TYR A 69
SHEET 4 AA1 6 VAL A 78 VAL A 84 1 N ILE A 83 O ILE A 109
SHEET 5 AA1 6 VAL A 149 GLY A 158 1 O ASP A 150 N VAL A 78
SHEET 6 AA1 6 ALA A 178 ALA A 179 1 O ALA A 178 N VAL A 156
SHEET 1 AA2 3 THR A 198 CYS A 203 0
SHEET 2 AA2 3 LYS A 227 ILE A 232 1 O GLN A 228 N ILE A 200
SHEET 3 AA2 3 VAL A 281 ALA A 287 -1 O ARG A 285 N PHE A 229
SSBOND 1 CYS A 203 CYS A 239 1555 1555 2.06
SSBOND 2 CYS A 273 CYS A 289 1555 1555 2.08
CRYST1 51.203 65.116 69.324 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 0.019530 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015357 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014425 0.00000
TER 1939 SER A 290
MASTER 265 0 3 9 9 0 0 6 2271 1 22 21
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