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HEADER HYDROLASE 02-APR-98 1RP1
TITLE DOG PANCREATIC LIPASE RELATED PROTEIN 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PANCREATIC LIPASE RELATED PROTEIN 1;
COMPND 3 CHAIN: NULL;
COMPND 4 EC: 3.1.1.3
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANIS FAMILIARIS;
SOURCE 3 ORGANISM_COMMON: DOG;
SOURCE 4 ORGAN: PANCREAS;
SOURCE 5 SECRETION: PANCREATIC JUICE
KEYWDS HYDROLASE, LIPID DEGRADATION, PANCREATIC LIPASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ROUSSEL,C.CAMBILLAU
REVDAT 1 17-JUN-98 1RP1 0
JRNL AUTH A.ROUSSEL,J.DE CARO,S.BEZZINE,L.GASTINEL,
JRNL AUTH 2 A.DE CARO,F.CARRIERE,S.LEYDIER,R.VERGER,
JRNL AUTH 3 C.CAMBILLAU
JRNL TITL REACTIVATION OF THE TOTALLY INACTIVE PANCREATIC
JRNL TITL 2 LIPASE RP1 BY STRUCTURE PREDICTED POINT MUTATIONS
JRNL REF TO BE PUBLISHED
JRNL REFN 0353
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.1 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.843
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.1
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 9.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1300
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 70.
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 30055
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NONE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.
REMARK 3 FREE R VALUE TEST SET COUNT : 1540
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.17
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.15
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1359
REMARK 3 BIN R VALUE (WORKING SET) : 0.1830
REMARK 3 BIN FREE R VALUE : 0.2697
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.01
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 67
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.032
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3425
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 359
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.178
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.017
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.6
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.4
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.6
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARAM19X.PRO
REMARK 3 PARAMETER FILE 2 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 3 : PARAM3_MOD.CHO
REMARK 3 TOPOLOGY FILE 1 : TOPH19X.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 3 : TOPH3.CHO
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RP1 COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : SEP-1997
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LURE
REMARK 200 BEAMLINE : W32
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : LURE MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30017
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.1
REMARK 200 RESOLUTION RANGE LOW (A) : 9.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.5
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 3.4
REMARK 200 R MERGE (I) : 0.067
REMARK 200 R SYM (I) : 0.067
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.1
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.2
REMARK 200 R MERGE FOR SHELL (I) : 0.368
REMARK 200 R SYM FOR SHELL (I) : 0.368
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.
REMARK 200
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1THG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM
REMARK 280 20% PEG 8000 WITH 25MM POTASSIUM PHOSPHATE BUFFER AT PH
REMARK 280 4.2.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,1/2+Z
REMARK 290 3555 -X,Y,1/2-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 1/2+X,1/2+Y,Z
REMARK 290 6555 1/2-X,1/2-Y,1/2+Z
REMARK 290 7555 1/2-X,1/2+Y,1/2-Z
REMARK 290 8555 1/2+X,1/2-Y,-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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.00660
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.00660
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 27.01243
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 75.36931
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 27.01243
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 75.36931
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 66.00660
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 27.01243
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 75.36931
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 66.00660
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 27.01243
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 75.36931
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 4*RMSD AND BY MORE THAN 0.150 ANGSTROMS (M=MODEL
REMARK 500 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 500 NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,1X,2(A4,A1,3X),12X,F5.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 0 MET 134 SD MET 134 CE 0.171
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 0 HOH 343 DISTANCE = 5.71 ANGSTROMS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1RP1 SWS P06857 1 - 17 NOT IN ATOMS LIST
DBREF 1RP1 1 315 SWS P06857 LIP1_CANFA 18 333
DBREF 1RP1 323 406 SWS P06857 LIP1_CANFA 341 423
DBREF 1RP1 409 449 SWS P06857 LIP1_CANFA 426 467
SEQADV 1RP1 GLY 60 SWS P06857 GLU 79 CONFLICT
SEQADV 1RP1 SWS P06857 VAL 334 GAP IN PDB ENTRY
SEQADV 1RP1 SWS P06857 LYS 335 GAP IN PDB ENTRY
SEQADV 1RP1 SWS P06857 THR 336 GAP IN PDB ENTRY
SEQADV 1RP1 SWS P06857 SER 337 GAP IN PDB ENTRY
SEQADV 1RP1 SWS P06857 ASP 338 GAP IN PDB ENTRY
SEQADV 1RP1 SWS P06857 GLU 339 GAP IN PDB ENTRY
SEQADV 1RP1 SWS P06857 THR 340 GAP IN PDB ENTRY
SEQADV 1RP1 SWS P06857 VAL 424 GAP IN PDB ENTRY
SEQADV 1RP1 SWS P06857 VAL 425 GAP IN PDB ENTRY
SEQRES 1 441 LYS GLU VAL CYS TYR GLU GLN ILE GLY CYS PHE SER ASP
SEQRES 2 441 ALA GLU PRO TRP ALA GLY THR ALA ILE ARG PRO LEU LYS
SEQRES 3 441 VAL LEU PRO TRP SER PRO GLU ARG ILE GLY THR ARG PHE
SEQRES 4 441 LEU LEU TYR THR ASN LYS ASN PRO ASN ASN PHE GLN THR
SEQRES 5 441 LEU LEU PRO SER ASP PRO SER THR ILE GLY ALA SER ASN
SEQRES 6 441 PHE GLN THR ASP LYS LYS THR ARG PHE ILE ILE HIS GLY
SEQRES 7 441 PHE ILE ASP LYS GLY GLU GLU ASN TRP LEU LEU ASP MET
SEQRES 8 441 CYS LYS ASN MET PHE LYS VAL GLU GLU VAL ASN CYS ILE
SEQRES 9 441 CYS VAL ASP TRP LYS LYS GLY SER GLN THR SER TYR THR
SEQRES 10 441 GLN ALA ALA ASN ASN VAL ARG VAL VAL GLY ALA GLN VAL
SEQRES 11 441 ALA GLN MET LEU SER MET LEU SER ALA ASN TYR SER TYR
SEQRES 12 441 SER PRO SER GLN VAL GLN LEU ILE GLY HIS SER LEU GLY
SEQRES 13 441 ALA HIS VAL ALA GLY GLU ALA GLY SER ARG THR PRO GLY
SEQRES 14 441 LEU GLY ARG ILE THR GLY LEU ASP PRO VAL GLU ALA SER
SEQRES 15 441 PHE GLN GLY THR PRO GLU GLU VAL ARG LEU ASP PRO THR
SEQRES 16 441 ASP ALA ASP PHE VAL ASP VAL ILE HIS THR ASP ALA ALA
SEQRES 17 441 PRO LEU ILE PRO PHE LEU GLY PHE GLY THR SER GLN GLN
SEQRES 18 441 MET GLY HIS LEU ASP PHE PHE PRO ASN GLY GLY GLU GLU
SEQRES 19 441 MET PRO GLY CYS LYS LYS ASN ALA LEU SER GLN ILE VAL
SEQRES 20 441 ASP LEU ASP GLY ILE TRP GLU GLY THR ARG ASP PHE VAL
SEQRES 21 441 ALA CYS ASN HIS LEU ARG SER TYR LYS TYR TYR SER GLU
SEQRES 22 441 SER ILE LEU ASN PRO ASP GLY PHE ALA SER TYR PRO CYS
SEQRES 23 441 ALA SER TYR ARG ALA PHE GLU SER ASN LYS CYS PHE PRO
SEQRES 24 441 CYS PRO ASP GLN GLY CYS PRO GLN MET GLY HIS TYR ALA
SEQRES 25 441 ASP LYS PHE ALA GLN LYS TYR PHE LEU ASN THR GLY ASP
SEQRES 26 441 SER SER ASN PHE ALA ARG TRP ARG TYR GLY VAL SER ILE
SEQRES 27 441 THR LEU SER GLY LYS ARG ALA THR GLY GLN ALA LYS VAL
SEQRES 28 441 ALA LEU PHE GLY SER LYS GLY ASN THR HIS GLN PHE ASN
SEQRES 29 441 ILE PHE LYS GLY ILE LEU LYS PRO GLY SER THR HIS SER
SEQRES 30 441 ASN GLU PHE ASP ALA LYS LEU ASP VAL GLY THR ILE GLU
SEQRES 31 441 LYS VAL LYS PHE LEU TRP ASN ASN ASN ASN PRO THR PHE
SEQRES 32 441 PRO LYS VAL GLY ALA ALA LYS ILE THR VAL GLN LYS GLY
SEQRES 33 441 GLU GLU LYS THR VAL HIS SER PHE CYS SER GLU SER THR
SEQRES 34 441 VAL ARG GLU ASP VAL LEU LEU THR LEU THR PRO CYS
HET NAG 500 14
HET CA 501 1
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM CA CALCIUM ION
FORMUL 2 NAG C8 H15 N1 O6
FORMUL 3 CA CA1 2+
FORMUL 4 HOH *358(H2 O1)
HELIX 1 1 PRO 56 GLY 60 5 5
HELIX 2 2 TRP 85 LYS 95 1 11
HELIX 3 3 TYR 114 TYR 139 1 26
HELIX 4 4 SER 152 SER 163 5 12
HELIX 5 5 LEU 248 TRP 252 1 5
HELIX 6 6 CYS 261 LEU 275 1 15
HELIX 7 7 TYR 288 GLU 292 1 5
SHEET 1 A 2 GLU 2 TYR 5 0
SHEET 2 A 2 GLY 9 SER 12 -1 N PHE 11 O VAL 3
SHEET 1 B 9 GLN 50 LEU 52 0
SHEET 2 B 9 ARG 37 THR 42 -1 N LEU 40 O GLN 50
SHEET 3 B 9 VAL 99 ASP 105 -1 N ASP 105 O ARG 37
SHEET 4 B 9 LYS 69 ILE 74 1 N LYS 69 O ASN 100
SHEET 5 B 9 VAL 146 HIS 151 1 N GLN 147 O THR 70
SHEET 6 B 9 ARG 171 LEU 175 1 N ARG 171 O LEU 148
SHEET 7 B 9 PHE 198 ILE 202 1 N PHE 198 O ILE 172
SHEET 8 B 9 LEU 224 PRO 228 1 N LEU 224 O VAL 201
SHEET 9 B 9 LYS 324 LEU 327 1 N TYR 325 O ASP 225
SHEET 1 C 4 THR 381 ALA 388 0
SHEET 2 C 4 TRP 338 GLY 348 -1 N ILE 344 O HIS 382
SHEET 3 C 4 VAL 415 LYS 424 -1 N GLN 423 O GLY 341
SHEET 4 C 4 HIS 701 CYS 433 -1 N PHE 432 O ILE 420
SHEET 1 D 4 LEU 444 THR 447 0
SHEET 2 D 4 ILE 395 ASN 404 -1 N PHE 400 O LEU 444
SHEET 3 D 4 ALA 351 GLY 361 -1 N PHE 360 O GLU 396
SHEET 4 D 4 PHE 369 LEU 376 -1 N LEU 376 O ALA 351
SSBOND 1 CYS 4 CYS 10
SSBOND 2 CYS 90 CYS 101
SSBOND 3 CYS 237 CYS 261
SSBOND 4 CYS 285 CYS 296
SSBOND 5 CYS 299 CYS 304
SSBOND 6 CYS 433 CYS 449
LINK C1 NAG 500 ND2 ASN 138
LINK CA CA 501 O GLU 187
LINK CA CA 501 O ARG 190
LINK CA CA 501 OD1 ASP 192
CISPEP 1 GLU 15 PRO 16 0 0.59
CISPEP 2 ILE 210 PRO 211 0 0.46
CISPEP 3 PHE 297 PRO 298 0 0.79
CRYST1 54.026 150.748 132.006 90.00 90.00 90.00 C 2 2 21 8
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 0.018510 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006634 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007575 0.00000 |