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HEADER HYDROLASE 06-MAR-25 9QDE
TITLE CRYSTAL STRUCTURE OF THE NON-GLYCOSYLATED POLYESTER HYDROLASE LEIPZIG
TITLE 2 7 (PHL7) MUT3 VARIANT EXPRESSED IN PICHIA PASTORIS (P_PHL7MUT3_NG)
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 9QDE 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. 1.02 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) : 1.02
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.92
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 76.4
REMARK 3 NUMBER OF REFLECTIONS : 90258
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.124
REMARK 3 R VALUE (WORKING SET) : 0.124
REMARK 3 FREE R VALUE : 0.150
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.970
REMARK 3 FREE R VALUE TEST SET COUNT : 1776
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 27.9200 - 2.4100 0.99 9291 188 0.1257 0.1575
REMARK 3 2 2.4100 - 1.9100 1.00 9031 185 0.1124 0.1137
REMARK 3 3 1.9100 - 1.6700 1.00 8975 165 0.1009 0.1225
REMARK 3 4 1.6700 - 1.5200 1.00 8921 170 0.0967 0.1250
REMARK 3 5 1.5200 - 1.4100 1.00 8867 176 0.1067 0.1389
REMARK 3 6 1.4100 - 1.3300 0.99 8823 184 0.1228 0.1927
REMARK 3 7 1.3300 - 1.2600 0.98 8697 178 0.1400 0.1876
REMARK 3 8 1.2600 - 1.2000 0.94 8295 166 0.1649 0.1791
REMARK 3 9 1.2000 - 1.1600 0.85 7560 158 0.1837 0.2356
REMARK 3 10 1.1600 - 1.1200 0.62 5448 111 0.2074 0.2086
REMARK 3 11 1.1200 - 1.0800 0.33 2916 65 0.2360 0.2338
REMARK 3 12 1.0800 - 1.0500 0.16 1367 26 0.2682 0.2374
REMARK 3 13 1.0500 - 1.0200 0.03 291 4 0.2873 0.4236
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) : 0.077
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.052
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.75
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.99
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 : 0.011 2168
REMARK 3 ANGLE : 1.125 2976
REMARK 3 CHIRALITY : 0.086 325
REMARK 3 PLANARITY : 0.015 402
REMARK 3 DIHEDRAL : 13.570 800
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 9QDE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-MAR-25.
REMARK 100 THE DEPOSITION ID IS D_1292145496.
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 EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : STARANISO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 90273
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.020
REMARK 200 RESOLUTION RANGE LOW (A) : 48.690
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 200 DATA REDUNDANCY : 7.900
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.02
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.12
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.14700
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 (%): 39.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BICINE (PH 9.0), 5% W/V PEG
REMARK 280 6000, VAPOR DIFFUSION, HANGING DROP, 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 23.02600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.07550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.50700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.07550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.02600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.50700
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 HIS A 263
REMARK 465 HIS A 264
REMARK 465 HIS A 265
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 THR A 64 -2.07 76.27
REMARK 500 SER A 131 -131.09 63.67
REMARK 500 HIS A 185 -95.56 -117.14
REMARK 500 PRO A 243 -176.47 -68.95
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 99 0.10 SIDE CHAIN
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 843 DISTANCE = 5.87 ANGSTROMS
DBREF1 9QDE A 2 259 UNP A0AA82WPD4_9ZZZZ
DBREF2 9QDE A A0AA82WPD4 2 259
SEQADV 9QDE SER A 131 UNP A0AA82WPD ALA 131 ENGINEERED MUTATION
SEQADV 9QDE GLN A 143 UNP A0AA82WPD ASN 143 ENGINEERED MUTATION
SEQADV 9QDE GLN A 144 UNP A0AA82WPD ASN 144 ENGINEERED MUTATION
SEQADV 9QDE GLN A 161 UNP A0AA82WPD ASN 161 ENGINEERED MUTATION
SEQADV 9QDE GLU A 175 UNP A0AA82WPD GLN 175 ENGINEERED MUTATION
SEQADV 9QDE THR A 210 UNP A0AA82WPD LEU 210 ENGINEERED MUTATION
SEQADV 9QDE LYS A 233 UNP A0AA82WPD ASP 233 ENGINEERED MUTATION
SEQADV 9QDE HIS A 260 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QDE HIS A 261 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QDE HIS A 262 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QDE HIS A 263 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QDE HIS A 264 UNP A0AA82WPD EXPRESSION TAG
SEQADV 9QDE HIS A 265 UNP A0AA82WPD EXPRESSION TAG
SEQRES 1 A 264 ALA ASN PRO TYR GLU ARG GLY PRO ASP PRO THR GLU SER
SEQRES 2 A 264 SER ILE GLU ALA VAL ARG GLY PRO PHE ALA VAL ALA GLN
SEQRES 3 A 264 THR THR VAL SER ARG LEU GLN ALA ASP GLY PHE GLY GLY
SEQRES 4 A 264 GLY THR ILE TYR TYR PRO THR ASP THR SER GLN GLY THR
SEQRES 5 A 264 PHE GLY ALA VAL ALA ILE SER PRO GLY PHE THR ALA GLY
SEQRES 6 A 264 GLN GLU SER ILE ALA TRP LEU GLY PRO ARG ILE ALA SER
SEQRES 7 A 264 GLN GLY PHE VAL VAL ILE THR ILE ASP THR ILE THR ARG
SEQRES 8 A 264 LEU ASP GLN PRO ASP SER ARG GLY ARG GLN LEU GLN ALA
SEQRES 9 A 264 ALA LEU ASP HIS LEU ARG THR ASN SER VAL VAL ARG ASN
SEQRES 10 A 264 ARG ILE ASP PRO ASN ARG MET ALA VAL MET GLY HIS SER
SEQRES 11 A 264 MET GLY GLY GLY GLY ALA LEU SER ALA ALA ALA GLN GLN
SEQRES 12 A 264 THR SER LEU GLU ALA ALA ILE PRO LEU GLN GLY TRP HIS
SEQRES 13 A 264 THR ARG LYS GLN TRP SER SER VAL ARG THR PRO THR LEU
SEQRES 14 A 264 VAL VAL GLY ALA GLU LEU ASP THR ILE ALA PRO VAL SER
SEQRES 15 A 264 SER HIS SER GLU ALA PHE TYR ASN SER LEU PRO SER ASP
SEQRES 16 A 264 LEU ASP LYS ALA TYR MET GLU LEU ARG GLY ALA SER HIS
SEQRES 17 A 264 THR VAL SER ASN THR PRO ASP THR THR THR ALA LYS TYR
SEQRES 18 A 264 SER ILE ALA TRP LEU LYS ARG PHE VAL ASP LYS ASP LEU
SEQRES 19 A 264 ARG TYR GLU GLN PHE LEU CYS PRO ALA PRO ASP ASP PHE
SEQRES 20 A 264 ALA ILE SER GLU TYR ARG SER THR CYS PRO PHE HIS HIS
SEQRES 21 A 264 HIS HIS HIS HIS
HET CL A 301 1
HETNAM CL CHLORIDE ION
FORMUL 2 CL CL 1-
FORMUL 3 HOH *443(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 GLN A 144 1 14
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 LEU A 241 5 8
SHEET 1 AA1 6 VAL A 25 VAL A 30 0
SHEET 2 AA1 6 GLY A 41 PRO A 46 -1 O ILE A 43 N THR A 28
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 ASP A 121 N PHE A 54
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 GLU A 252 N GLU A 203
SSBOND 1 CYS A 242 CYS A 257 1555 1555 2.03
CISPEP 1 CYS A 242 PRO A 243 0 -5.91
CISPEP 2 CYS A 257 PRO A 258 0 -2.41
CRYST1 46.052 59.014 86.151 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 0.021715 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016945 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011608 0.00000
TER 4140 HIS A 262
MASTER 259 0 1 9 9 0 0 6 2438 1 2 21
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