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HEADER HYDROLASE 03-MAR-25 9QBN
TITLE CRYSTAL STRUCTURE OF THE POLYESTER HYDROLASE LEIPZIG 7 (PHL7) MUT3
TITLE 2 VARIANT WITH GLYCOSYLATION BY EXPRESSION IN PICHIA PASTORIS
TITLE 3 (P_PHL7MUT3)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYESTER HYDROLASE LEIPZIG 7 (PHL-7), CATALYSIS-DEFICIENT
COMPND 3 S131A MUTANT;
COMPND 4 CHAIN: A;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: COMPOST METAGENOME;
SOURCE 3 ORGANISM_TAXID: 702656;
SOURCE 4 EXPRESSION_SYSTEM: PICHIA;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 4919
KEYWDS E. COLI, LCC, K. PHAFFII, PETASE, P. PASTORIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.USEINI,N.STRATER,G.STRIEDNER,C.SONNENDECKER
REVDAT 1 10-SEP-25 9QBN 0
JRNL AUTH L.FOHLER,F.FASCHINGEDER,L.LEIBETSEDER,Z.ZHAO,A.USEINI,
JRNL AUTH 2 N.STRATER,C.SONNENDECKER,T.A.EWING,A.P.H.A.MOERS,
JRNL AUTH 3 M.W.T.WERTEN,D.M.VAN VLIET,M.K.JULSING,W.ZIMMERMANN,
JRNL AUTH 4 G.STRIEDNER
JRNL TITL TRADE-OFFS BETWEEN STABILITY AND ACTIVITY OF GLYCOSYLATED
JRNL TITL 2 AND NON-GLYCOSYLATED POLYESTER HYDROLASES PHL7 AND PHL7MUT3
JRNL REF ACS ES T ENG 2025
JRNL DOI 10.1021/ACSESTENGG.5C00272
REMARK 2
REMARK 2 RESOLUTION. 1.37 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.21.2_5419
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) : 1.37
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.43
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 84.3
REMARK 3 NUMBER OF REFLECTIONS : 47787
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.135
REMARK 3 R VALUE (WORKING SET) : 0.134
REMARK 3 FREE R VALUE : 0.168
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.040
REMARK 3 FREE R VALUE TEST SET COUNT : 2135
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 41.4300 - 3.3800 0.96 4089 194 0.1263 0.1452
REMARK 3 2 3.3800 - 2.6800 0.98 3996 163 0.1085 0.1445
REMARK 3 3 2.6800 - 2.3400 0.97 3952 147 0.1030 0.1315
REMARK 3 4 2.3400 - 2.1300 0.98 3937 168 0.1034 0.1385
REMARK 3 5 2.1300 - 1.9800 0.99 3942 180 0.1104 0.1470
REMARK 3 6 1.9800 - 1.8600 0.94 3743 168 0.1260 0.1820
REMARK 3 7 1.8600 - 1.7700 0.97 3868 166 0.1457 0.2139
REMARK 3 8 1.7700 - 1.6900 0.97 3852 167 0.1625 0.2073
REMARK 3 9 1.6900 - 1.6200 0.97 3852 159 0.1688 0.1767
REMARK 3 10 1.6200 - 1.5700 0.96 3816 153 0.1797 0.2346
REMARK 3 11 1.5700 - 1.5200 0.90 3586 135 0.1977 0.2429
REMARK 3 12 1.5200 - 1.4800 0.69 2755 92 0.2209 0.2757
REMARK 3 13 1.4800 - 1.4400 0.54 2144 104 0.2539 0.3212
REMARK 3 14 1.4400 - 1.4000 0.44 1716 83 0.2718 0.3121
REMARK 3 15 1.4000 - 1.3700 0.37 1459 56 0.2933 0.3207
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) : 0.134
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.622
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.76
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.73
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 : 0.003 2176
REMARK 3 ANGLE : 0.725 2982
REMARK 3 CHIRALITY : 0.067 332
REMARK 3 PLANARITY : 0.008 395
REMARK 3 DIHEDRAL : 12.138 818
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 9QBN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-MAR-25.
REMARK 100 THE DEPOSITION ID IS D_1292145288.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-SEP-24
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 : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P13 (MX1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
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 : STARANISO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47787
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.370
REMARK 200 RESOLUTION RANGE LOW (A) : 101.030
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.8
REMARK 200 DATA REDUNDANCY : 8.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.37
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.49
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: 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 (%): 51.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LITHIUM SULFATE, 0.1 M TRIS-HCL
REMARK 280 (PH 8.5), 30% W/V PEG 4000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 292.15K
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 22.71100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.51250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.99850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.51250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.71100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.99850
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, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 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 131 -126.52 59.38
REMARK 500 HIS A 185 -95.06 -117.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 844 DISTANCE = 6.87 ANGSTROMS
DBREF1 9QBN A 1 259 UNP A0AA82WPD4_9ZZZZ
DBREF2 9QBN A A0AA82WPD4 1 259
SEQADV 9QBN SER A 131 UNP A0AA82WPD ALA 131 ENGINEERED MUTATION
SEQADV 9QBN GLU A 175 UNP A0AA82WPD GLN 175 ENGINEERED MUTATION
SEQADV 9QBN THR A 210 UNP A0AA82WPD LEU 210 ENGINEERED MUTATION
SEQADV 9QBN LYS A 233 UNP A0AA82WPD ASP 233 ENGINEERED MUTATION
SEQADV 9QBN HIS A 260 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QBN HIS A 261 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QBN HIS A 262 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QBN HIS A 263 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QBN HIS A 264 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QBN HIS A 265 UNP A0AA82WPD EXPRESSION TAG
SEQRES 1 A 265 MET ALA ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU
SEQRES 2 A 265 SER SER ILE GLU ALA VAL ARG GLY PRO PHE ALA VAL ALA
SEQRES 3 A 265 GLN THR THR VAL SER ARG LEU GLN ALA ASP GLY PHE GLY
SEQRES 4 A 265 GLY GLY THR ILE TYR TYR PRO THR ASP THR SER GLN GLY
SEQRES 5 A 265 THR PHE GLY ALA VAL ALA ILE SER PRO GLY PHE THR ALA
SEQRES 6 A 265 GLY GLN GLU SER ILE ALA TRP LEU GLY PRO ARG ILE ALA
SEQRES 7 A 265 SER GLN GLY PHE VAL VAL ILE THR ILE ASP THR ILE THR
SEQRES 8 A 265 ARG LEU ASP GLN PRO ASP SER ARG GLY ARG GLN LEU GLN
SEQRES 9 A 265 ALA ALA LEU ASP HIS LEU ARG THR ASN SER VAL VAL ARG
SEQRES 10 A 265 ASN ARG ILE ASP PRO ASN ARG MET ALA VAL MET GLY HIS
SEQRES 11 A 265 SER MET GLY GLY GLY GLY ALA LEU SER ALA ALA ALA ASN
SEQRES 12 A 265 ASN THR SER LEU GLU ALA ALA ILE PRO LEU GLN GLY TRP
SEQRES 13 A 265 HIS THR ARG LYS ASN TRP SER SER VAL ARG THR PRO THR
SEQRES 14 A 265 LEU VAL VAL GLY ALA GLU LEU ASP THR ILE ALA PRO VAL
SEQRES 15 A 265 SER SER HIS SER GLU ALA PHE TYR ASN SER LEU PRO SER
SEQRES 16 A 265 ASP LEU ASP LYS ALA TYR MET GLU LEU ARG GLY ALA SER
SEQRES 17 A 265 HIS THR VAL SER ASN THR PRO ASP THR THR THR ALA LYS
SEQRES 18 A 265 TYR SER ILE ALA TRP LEU LYS ARG PHE VAL ASP LYS ASP
SEQRES 19 A 265 LEU ARG TYR GLU GLN PHE LEU CYS PRO ALA PRO ASP ASP
SEQRES 20 A 265 PHE ALA ILE SER GLU TYR ARG SER THR CYS PRO PHE HIS
SEQRES 21 A 265 HIS HIS HIS HIS HIS
HET NAG B 1 26
HET NAG B 2 27
HET SO4 A 301 5
HET SO4 A 302 5
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 2 NAG 2(C8 H15 N O6)
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *445(H2 O)
HELIX 1 AA1 THR A 12 ALA A 18 1 7
HELIX 2 AA2 GLY A 66 ALA A 71 5 6
HELIX 3 AA3 TRP A 72 SER A 79 1 8
HELIX 4 AA4 GLN A 95 ARG A 111 1 17
HELIX 5 AA5 SER A 131 ASN A 143 1 13
HELIX 6 AA6 HIS A 185 LEU A 193 1 9
HELIX 7 AA7 SER A 208 THR A 214 5 7
HELIX 8 AA8 ASP A 216 ASP A 232 1 17
HELIX 9 AA9 ASP A 234 ARG A 236 5 3
HELIX 10 AB1 TYR A 237 CYS A 242 1 6
SHEET 1 AA1 6 VAL A 25 VAL A 30 0
SHEET 2 AA1 6 GLY A 41 PRO A 46 -1 O GLY A 41 N VAL A 30
SHEET 3 AA1 6 VAL A 83 ILE A 87 -1 O VAL A 84 N TYR A 44
SHEET 4 AA1 6 PHE A 54 SER A 60 1 N VAL A 57 O ILE A 85
SHEET 5 AA1 6 ILE A 120 HIS A 130 1 O MET A 128 N ALA A 58
SHEET 6 AA1 6 ALA A 149 LEU A 153 1 O LEU A 153 N GLY A 129
SHEET 1 AA2 3 THR A 169 ALA A 174 0
SHEET 2 AA2 3 LYS A 199 LEU A 204 1 O ALA A 200 N VAL A 171
SHEET 3 AA2 3 ILE A 250 SER A 255 -1 O ARG A 254 N TYR A 201
SSBOND 1 CYS A 242 CYS A 257 1555 1555 2.03
LINK ND2AASN A 143 C1 ANAG B 1 1555 1555 1.44
LINK O4 ANAG B 1 C1 ANAG B 2 1555 1555 1.43
CISPEP 1 CYS A 242 PRO A 243 0 -1.81
CISPEP 2 CYS A 257 PRO A 258 0 -5.58
CRYST1 45.422 63.997 101.025 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 0.022016 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015626 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009899 0.00000
TER 4073 HIS A 265
MASTER 242 0 4 10 9 0 0 6 2504 1 66 21
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