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HEADER HYDROLASE 20-APR-23 8OTA
TITLE HIGH RESOLUTION CRYSTAL STRUCTURE OF A LEAF-BRANCH COMPOST CUTINASE
TITLE 2 QUADRUPLE VARIANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LEAF-BRANCH COMPOST CUTINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LC-CUTINASE,LCC,PET-DIGESTING ENZYME,POLY(ETHYLENE
COMPND 5 TEREPHTHALATE) HYDROLASE,PET HYDROLASE,PETASE;
COMPND 6 EC: 3.1.1.74,3.1.1.101;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS HYDROLASE, SERINE ESTERASE, CUTINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.GAVALDA,G.CIOCI,A.MARTY,S.DUQUESNE
REVDAT 1 04-SEP-24 8OTA 0
JRNL AUTH C.CHARLIER,S.GAVALDA,J.GRGA,L.PERROT,V.GABRIELLI,F.LOHR,
JRNL AUTH 2 J.SCHORGHUBER,R.LICHTENECKER,G.ARNAL,A.MARTY,V.TOURNIER,
JRNL AUTH 3 G.LIPPENS
JRNL TITL EXPLORING THE PH DEPENDENCE OF AN IMPROVED PETASE.
JRNL REF BIOPHYS.J. V. 123 1542 2024
JRNL REFN ESSN 1542-0086
JRNL PMID 38664965
JRNL DOI 10.1016/J.BPJ.2024.04.026
REMARK 2
REMARK 2 RESOLUTION. 1.72 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
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) : 1.72
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.07
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 26667
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.280
REMARK 3 FREE R VALUE TEST SET COUNT : 1407
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 10.0000 - 3.7000 1.00 2602 180 0.1642 0.1828
REMARK 3 2 3.7000 - 2.9400 1.00 2557 124 0.1731 0.2078
REMARK 3 3 2.9400 - 2.5700 1.00 2526 138 0.1628 0.2001
REMARK 3 4 2.5700 - 2.3300 1.00 2512 153 0.1715 0.2073
REMARK 3 5 2.3300 - 2.1700 1.00 2519 139 0.1436 0.1832
REMARK 3 6 2.1700 - 2.0400 1.00 2523 124 0.1818 0.2097
REMARK 3 7 2.0400 - 1.9400 1.00 2498 132 0.1523 0.1656
REMARK 3 8 1.9400 - 1.8500 1.00 2503 132 0.1727 0.2234
REMARK 3 9 1.8500 - 1.7800 1.00 2490 136 0.2242 0.2547
REMARK 3 10 1.7800 - 1.7200 1.00 2530 149 0.3480 0.4270
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) : 0.245
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.444
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.53
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.22
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 : 0.007 2048
REMARK 3 ANGLE : 0.851 2815
REMARK 3 CHIRALITY : 0.060 319
REMARK 3 PLANARITY : 0.009 371
REMARK 3 DIHEDRAL : 5.897 306
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 8OTA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-APR-23.
REMARK 100 THE DEPOSITION ID IS D_1292129987.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-OCT-20
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 : ESRF
REMARK 200 BEAMLINE : MASSIF-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9677
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26667
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.719
REMARK 200 RESOLUTION RANGE LOW (A) : 36.070
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.72
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.63000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.300
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 (%): 45.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BICINE PH9, 10% PEG20000, 2%
REMARK 280 DIOXANE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 285K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 17.79100
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 17.79100
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 17.79100
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 766 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 768 LIES ON A SPECIAL POSITION.
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD1 ASP A 98 OG SER A 100 2.14
REMARK 500
REMARK 500 REMARK: NULL
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 145 23.31 -142.96
REMARK 500 SER A 165 -126.70 64.35
REMARK 500 THR A 188 58.94 34.23
REMARK 500 HIS A 218 -82.94 -125.94
REMARK 500 ASN A 239 47.04 38.35
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 768 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH A 769 DISTANCE = 6.41 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6THT RELATED DB: PDB
REMARK 900 INACTIVE MUTANT
DBREF 8OTA A 36 293 UNP G9BY57 PETH_UNKP 36 293
SEQADV 8OTA MET A 35 UNP G9BY57 INITIATING METHIONINE
SEQADV 8OTA GLY A 127 UNP G9BY57 TYR 127 ENGINEERED MUTATION
SEQADV 8OTA CYS A 238 UNP G9BY57 ASP 238 ENGINEERED MUTATION
SEQADV 8OTA ILE A 243 UNP G9BY57 PHE 243 ENGINEERED MUTATION
SEQADV 8OTA CYS A 283 UNP G9BY57 SER 283 ENGINEERED MUTATION
SEQRES 1 A 259 MET SER ASN PRO TYR GLN ARG GLY PRO ASN PRO THR ARG
SEQRES 2 A 259 SER ALA LEU THR ALA ASP GLY PRO PHE SER VAL ALA THR
SEQRES 3 A 259 TYR THR VAL SER ARG LEU SER VAL SER GLY PHE GLY GLY
SEQRES 4 A 259 GLY VAL ILE TYR TYR PRO THR GLY THR SER LEU THR PHE
SEQRES 5 A 259 GLY GLY ILE ALA MET SER PRO GLY TYR THR ALA ASP ALA
SEQRES 6 A 259 SER SER LEU ALA TRP LEU GLY ARG ARG LEU ALA SER HIS
SEQRES 7 A 259 GLY PHE VAL VAL LEU VAL ILE ASN THR ASN SER ARG PHE
SEQRES 8 A 259 ASP GLY PRO ASP SER ARG ALA SER GLN LEU SER ALA ALA
SEQRES 9 A 259 LEU ASN TYR LEU ARG THR SER SER PRO SER ALA VAL ARG
SEQRES 10 A 259 ALA ARG LEU ASP ALA ASN ARG LEU ALA VAL ALA GLY HIS
SEQRES 11 A 259 SER MET GLY GLY GLY GLY THR LEU ARG ILE ALA GLU GLN
SEQRES 12 A 259 ASN PRO SER LEU LYS ALA ALA VAL PRO LEU THR PRO TRP
SEQRES 13 A 259 HIS THR ASP LYS THR PHE ASN THR SER VAL PRO VAL LEU
SEQRES 14 A 259 ILE VAL GLY ALA GLU ALA ASP THR VAL ALA PRO VAL SER
SEQRES 15 A 259 GLN HIS ALA ILE PRO PHE TYR GLN ASN LEU PRO SER THR
SEQRES 16 A 259 THR PRO LYS VAL TYR VAL GLU LEU CYS ASN ALA SER HIS
SEQRES 17 A 259 ILE ALA PRO ASN SER ASN ASN ALA ALA ILE SER VAL TYR
SEQRES 18 A 259 THR ILE SER TRP MET LYS LEU TRP VAL ASP ASN ASP THR
SEQRES 19 A 259 ARG TYR ARG GLN PHE LEU CYS ASN VAL ASN ASP PRO ALA
SEQRES 20 A 259 LEU CYS ASP PHE ARG THR ASN ASN ARG HIS CYS GLN
HET DIO A 301 6
HETNAM DIO 1,4-DIETHYLENE DIOXIDE
FORMUL 2 DIO C4 H8 O2
FORMUL 3 HOH *369(H2 O)
HELIX 1 AA1 THR A 46 ALA A 52 5 7
HELIX 2 AA2 SER A 64 VAL A 68 5 5
HELIX 3 AA3 ASP A 98 SER A 101 5 4
HELIX 4 AA4 LEU A 102 HIS A 112 1 11
HELIX 5 AA5 GLY A 127 SER A 145 1 19
HELIX 6 AA6 PRO A 147 ALA A 152 1 6
HELIX 7 AA7 SER A 165 ASN A 178 1 14
HELIX 8 AA8 HIS A 218 LEU A 226 1 9
HELIX 9 AA9 ILE A 243 SER A 247 5 5
HELIX 10 AB1 ASN A 249 ASP A 265 1 17
HELIX 11 AB2 ASP A 267 LEU A 274 5 8
HELIX 12 AB3 ASN A 289 GLN A 293 5 5
SHEET 1 AA1 6 SER A 57 VAL A 63 0
SHEET 2 AA1 6 GLY A 74 THR A 80 -1 O GLY A 74 N VAL A 63
SHEET 3 AA1 6 VAL A 115 ILE A 119 -1 O VAL A 116 N TYR A 77
SHEET 4 AA1 6 PHE A 86 SER A 92 1 N ILE A 89 O VAL A 115
SHEET 5 AA1 6 LEU A 154 HIS A 164 1 O ASP A 155 N PHE A 86
SHEET 6 AA1 6 ALA A 184 LEU A 187 1 O LEU A 187 N GLY A 163
SHEET 1 AA2 3 VAL A 202 ALA A 207 0
SHEET 2 AA2 3 LYS A 232 LEU A 237 1 O VAL A 235 N GLY A 206
SHEET 3 AA2 3 LEU A 282 THR A 287 -1 O ARG A 286 N TYR A 234
SSBOND 1 CYS A 238 CYS A 283 1555 1555 2.04
SSBOND 2 CYS A 275 CYS A 292 1555 1555 2.05
CRYST1 110.184 110.184 35.582 90.00 90.00 120.00 P 63 6
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 0.009076 0.005240 0.000000 0.00000
SCALE2 0.000000 0.010480 0.000000 0.00000
SCALE3 0.000000 0.000000 0.028104 0.00000
TER 1984 GLN A 293
MASTER 271 0 1 12 9 0 0 6 2324 1 10 20
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