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HEADER TRANSFERASE 16-MAY-00 1F0P
TITLE MYCOBACTERIUM TUBERCULOSIS ANTIGEN 85B WITH TREHALOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIGEN 85-B;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 EXPRESSION_SYSTEM: MYCOBACTERIUM SMEGMATIS;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PSMT3
KEYWDS MYCOLYL TRANSFERASE; ANTIGEN 85B; TREHALOSE BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR D.H.ANDERSON,G.HARTH,M.A.HORWITZ,D.EISENBERG
REVDAT 2 28-MAR-01 1F0P 1 JRNL
REVDAT 1 24-JAN-01 1F0P 0
JRNL AUTH D.H.ANDERSON,G.HARTH,M.A.HORWITZ,D.EISENBERG
JRNL TITL AN INTERFACIAL MECHANISM AND A CLASS OF INHIBITORS
JRNL TITL 2 INFERRED FROM TWO CRYSTAL STRUCTURES OF THE
JRNL TITL 3 MYCOBACTERIUM TUBERCULOSIS 30KDA MAJOR SECRETORY
JRNL TITL 4 PROTEIN (ANTIGEN 85B), A MYCOLYL TRANFERASE
JRNL REF J.MOL.BIOL. V. 307 671 2001
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.R.RONNING,T.KLABUNDE,G.S.BESRA,V.D.VISSA,
REMARK 1 AUTH 2 J.T.BELISLE,J.C.SACCHETTINI
REMARK 1 TITL CRYSTAL STRUCTURE OF THE SECRETED FORM OF ANTIGEN
REMARK 1 TITL 2 85C REVEALS POTENTIAL TARGETS FOR MYCOBACTERIAL
REMARK 1 TITL 3 DRUGS AND VACCINES
REMARK 1 REF NAT.STRUCT.BIOL. V. 7 141 2000
REMARK 1 REFN ASTM NSBIEW US ISSN 1072-8368
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM (CCP4
REMARK 3 UNIQUEIFY)
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.195
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.192
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1177
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 23077
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.189
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.186
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 1099
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 21692
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2154
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 247
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2447.50
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 0
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 9849
REMARK 3 NUMBER OF RESTRAINTS : 9291
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 ANGLE DISTANCES (A) : 0.020
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.024
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.031
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.038
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.007
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.000
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.077
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-
REMARK 3 228
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER SPECIAL
REMARK 3 CASES: 2-METHYL-2,4-
REMARK 3 PENTANEDIOL (MPD) IS
REMARK 3 RESTRAINED TO MATCH PDB
REMARK 3 CODE 3AL1; 2-(4-
REMARK 3 MORPHOLINO)-
REMARK 3 ETHANESULFONIC ACID (MES)
REMARK 3 IS RESTRAINED TO MATCH
REMARK 3 PDB CODE 3CHB; TREHALOSE
REMARK 3 IS RESTRAINED TO MATCH
REMARK 3 CAMBRIDGE STRUCTURAL DATA
REMARK 3 BASE CODE DEKYEX.
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ANISOTROPIC SCALING APPLIED BY
REMARK 3 THE METHOD OF PARKIN, MOEZZI & HOPE,
REMARK 3 J.APPL.CRYST.28(1995)53-56
REMARK 4
REMARK 4 1F0P COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAY-2000.
REMARK 100 THE RCSB ID CODE IS RCSB011101.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-APR-2000
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97950
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : PARABOLIC COLLIMATING MIR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM 4R)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23441
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : 0.06800
REMARK 200 FOR THE DATA SET : 22.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.90
REMARK 200 R MERGE FOR SHELL (I) : 0.36700
REMARK 200 R SYM FOR SHELL (I) : 0.36700
REMARK 200 FOR SHELL : 7.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: SHELXL-97
REMARK 200 STARTING MODEL: APO ANTIGEN 85B (PDB CODE 1F0N)
REMARK 200
REMARK 200 REMARK: APO AND TREHALOSE CRYSTALS ARE ISOMORPHOUS.
REMARK 200 TREHALOSE BINDING SITES WERE LOCATED BY FO-FO DIFFERENCE
REMARK 200 FOURIER.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.9
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, MPD, MES,
REMARK 280 TREHALOSE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,1/3+Z
REMARK 290 3555 -X+Y,-X,2/3+Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,2/3-Z
REMARK 290 6555 -X,-X+Y,1/3-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 -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 30.84800
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 61.69600
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 61.69600
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 30.84800
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 551 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 PHE A 1
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
REMARK 500 O HOH 503 O HOH 557 2.07
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 3 C - N - CA ANGL. DEV. =-13.7 DEGREES
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1F0N RELATED DB: PDB
REMARK 900 THE SAME ANTIGEN 85B, ISOMORPHOUS, WITHOUT TREHALOSE.
REMARK 900 RELATED ID: 1DQZ RELATED DB: PDB
REMARK 900 ANTIGEN 85C
REMARK 900 RELATED ID: 1DQY RELATED DB: PDB
REMARK 900 ANTIGEN 85C WITH DIETHYL PHOSPHATE INHIBITOR.
DBREF 1F0P A 1 285 SWS P31952 A85B_MYCTU 41 325
SEQRES 1 A 285 PHE SER ARG PRO GLY LEU PRO VAL GLU TYR LEU GLN VAL
SEQRES 2 A 285 PRO SER PRO SER MET GLY ARG ASP ILE LYS VAL GLN PHE
SEQRES 3 A 285 GLN SER GLY GLY ASN ASN SER PRO ALA VAL TYR LEU LEU
SEQRES 4 A 285 ASP GLY LEU ARG ALA GLN ASP ASP TYR ASN GLY TRP ASP
SEQRES 5 A 285 ILE ASN THR PRO ALA PHE GLU TRP TYR TYR GLN SER GLY
SEQRES 6 A 285 LEU SER ILE VAL MET PRO VAL GLY GLY GLN SER SER PHE
SEQRES 7 A 285 TYR SER ASP TRP TYR SER PRO ALA CYS GLY LYS ALA GLY
SEQRES 8 A 285 CYS GLN THR TYR LYS TRP GLU THR PHE LEU THR SER GLU
SEQRES 9 A 285 LEU PRO GLN TRP LEU SER ALA ASN ARG ALA VAL LYS PRO
SEQRES 10 A 285 THR GLY SER ALA ALA ILE GLY LEU SER MET ALA GLY SER
SEQRES 11 A 285 SER ALA MET ILE LEU ALA ALA TYR HIS PRO GLN GLN PHE
SEQRES 12 A 285 ILE TYR ALA GLY SER LEU SER ALA LEU LEU ASP PRO SER
SEQRES 13 A 285 GLN GLY MET GLY PRO SER LEU ILE GLY LEU ALA MET GLY
SEQRES 14 A 285 ASP ALA GLY GLY TYR LYS ALA ALA ASP MET TRP GLY PRO
SEQRES 15 A 285 SER SER ASP PRO ALA TRP GLU ARG ASN ASP PRO THR GLN
SEQRES 16 A 285 GLN ILE PRO LYS LEU VAL ALA ASN ASN THR ARG LEU TRP
SEQRES 17 A 285 VAL TYR CYS GLY ASN GLY THR PRO ASN GLU LEU GLY GLY
SEQRES 18 A 285 ALA ASN ILE PRO ALA GLU PHE LEU GLU ASN PHE VAL ARG
SEQRES 19 A 285 SER SER ASN LEU LYS PHE GLN ASP ALA TYR ASN ALA ALA
SEQRES 20 A 285 GLY GLY HIS ASN ALA VAL PHE ASN PHE PRO PRO ASN GLY
SEQRES 21 A 285 THR HIS SER TRP GLU TYR TRP GLY ALA GLN LEU ASN ALA
SEQRES 22 A 285 MET LYS GLY ASP LEU GLN SER SER LEU GLY ALA GLY
HET MES 1101 12
HET TRE 1151 23
HET TRE 1152 23
HET MPD 1001 8
HET MPD 1002 8
HET MPD 1003 8
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM TRE TREHALOSE
HETNAM MPD 2-METHYL-2,4-PENTANEDIOL
HETSYN TRE ALPHA-D-GLUCOPYRANOSYL-ALPHA-D-GLUCOPYRANOSIDE
FORMUL 2 MES C6 H13 N1 O4 S1
FORMUL 3 TRE 2(C12 H22 O11)
FORMUL 5 HOH *223(H2 O1)
FORMUL 6 MPD 3(C6 H14 O2)
HELIX 1 1 ASN A 49 THR A 55 1 7
HELIX 2 2 PRO A 56 TYR A 62 1 7
HELIX 3 3 LYS A 96 SER A 103 1 8
HELIX 4 4 SER A 103 ALA A 114 1 12
HELIX 5 5 SER A 126 HIS A 139 1 14
HELIX 6 6 MET A 159 ALA A 171 1 13
HELIX 7 7 LYS A 175 GLY A 181 1 7
HELIX 8 8 PRO A 186 ASN A 191 1 6
HELIX 9 9 GLN A 196 ASN A 203 1 8
HELIX 10 10 ASN A 223 ALA A 247 1 25
HELIX 11 11 SER A 263 MET A 274 1 12
HELIX 12 12 MET A 274 GLY A 283 1 10
SHEET 1 A 8 GLU A 9 SER A 15 0
SHEET 2 A 8 ARG A 20 GLN A 27 -1 O ARG A 20 N SER A 15
SHEET 3 A 8 SER A 67 PRO A 71 -1 N ILE A 68 O GLN A 27
SHEET 4 A 8 ALA A 35 LEU A 39 1 O VAL A 36 N VAL A 69
SHEET 5 A 8 SER A 120 LEU A 125 1 O ALA A 121 N TYR A 37
SHEET 6 A 8 PHE A 143 LEU A 149 1 N ILE A 144 O SER A 120
SHEET 7 A 8 ARG A 206 TYR A 210 1 O ARG A 206 N ALA A 146
SHEET 8 A 8 ALA A 252 ASN A 255 1 N VAL A 253 O LEU A 207
SHEET 1 B 2 ALA A 86 GLY A 88 0
SHEET 2 B 2 GLY A 91 GLN A 93 -1 O GLY A 91 N GLY A 88
SSBOND 1 CYS A 87 CYS A 92
CRYST1 73.210 73.210 92.544 90.00 90.00 120.00 P 31 2 1 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 0.013659 0.007886 0.000000 0.00000
SCALE2 0.000000 0.015772 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010806 0.00000
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