Header list of 1bwy.pdb file
Complete list - v 29 2 Bytes
HEADER LIPID BINDING PROTEIN 29-SEP-98 1BWY
TITLE NMR STUDY OF BOVINE HEART FATTY ACID BINDING PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (HEART FATTY ACID BINDING PROTEIN);
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: H-FABP, MAMMARY DERIVED GROWTH INHIBITOR, MDGI;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: PI 5.1 ISOFORM, HOLO PROTEIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 STRAIN: BL21 (DE3) PLYSS;
SOURCE 6 ORGAN: HEART;
SOURCE 7 TISSUE: HEART MUSCLE;
SOURCE 8 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS;
SOURCE 12 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PET-3D
KEYWDS INTRACELLULAR LIPID BINDING PROTEIN, FATTY ACID BINDING, HEART
KEYWDS 2 MUSCLE, FATTY ACID BINDING PROTEIN, LIPID BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR D.LASSEN,C.LUECKE,M.KVEDER,A.MESGARZADEH,J.M.SCHMIDT,B.SPECHT,
AUTHOR 2 A.LEZIUS,F.SPENER,H.RUETERJANS
REVDAT 5 29-NOV-17 1BWY 1 REMARK HELIX
REVDAT 4 24-FEB-09 1BWY 1 VERSN
REVDAT 3 01-APR-03 1BWY 1 JRNL
REVDAT 2 29-DEC-99 1BWY 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 07-OCT-98 1BWY 0
JRNL AUTH D.LASSEN,C.LUCKE,M.KVEDER,A.MESGARZADEH,J.M.SCHMIDT,
JRNL AUTH 2 B.SPECHT,A.LEZIUS,F.SPENER,H.RUTERJANS
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF BOVINE HEART
JRNL TITL 2 FATTY-ACID-BINDING PROTEIN WITH BOUND PALMITIC ACID,
JRNL TITL 3 DETERMINED BY MULTIDIMENSIONAL NMR SPECTROSCOPY.
JRNL REF EUR.J.BIOCHEM. V. 230 266 1995
JRNL REFN ISSN 0014-2956
JRNL PMID 7601110
JRNL DOI 10.1111/J.1432-1033.1995.TB20560.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.LUECKE,D.LASSEN,H.-J.KREIENKAMP,F.SPENER,H.RUETERJANS
REMARK 1 TITL SEQUENCE-SPECIFIC 1H-NMR ASSIGNMENT AND DETERMINATION OF THE
REMARK 1 TITL 2 SECONDARY STRUCTURE OF BOVINE HEART FATTY-ACID-BINDING
REMARK 1 TITL 3 PROTEIN
REMARK 1 REF EUR.J.BIOCHEM. V. 210 901 1992
REMARK 1 REFN ISSN 0014-2956
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.ZANOTTI,G.SCAPIN,P.SPADON,J.H.VEERKAMP,J.C.SACCHETTINI
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF RECOMBINANT HUMAN MUSCLE
REMARK 1 TITL 2 FATTY-ACID BINDING PROTEIN
REMARK 1 REF J.BIOL.CHEM. V. 267 18541 1992
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SYBYL 6.0
REMARK 3 AUTHORS : TRIPOS INC.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BWY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000008246.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HMQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA, SYBYL
REMARK 210 METHOD USED : DISTANCE GEOMETRY, ENERGY
REMARK 210 MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST VIOLATION OF EXPERIMENTAL
REMARK 210 DISTANCE CONSTRAINTS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: SET OF 25 ENERGY-MINIMIZED NMR STRUCTURES
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 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 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 ALA A 132 C ALA A 132 OXT 0.151
REMARK 500 2 ALA A 132 C ALA A 132 OXT 0.151
REMARK 500 3 ALA A 132 C ALA A 132 OXT 0.151
REMARK 500 4 ALA A 132 C ALA A 132 OXT 0.151
REMARK 500 5 ALA A 132 C ALA A 132 OXT 0.151
REMARK 500 6 ALA A 132 C ALA A 132 OXT 0.151
REMARK 500 7 ALA A 132 C ALA A 132 OXT 0.151
REMARK 500 8 ALA A 132 C ALA A 132 OXT 0.151
REMARK 500 9 ALA A 132 C ALA A 132 OXT 0.151
REMARK 500 10 ALA A 132 C ALA A 132 OXT 0.151
REMARK 500 11 ALA A 132 C ALA A 132 OXT 0.151
REMARK 500 12 ALA A 132 C ALA A 132 OXT 0.150
REMARK 500 13 ALA A 132 C ALA A 132 OXT 0.151
REMARK 500 14 ALA A 132 C ALA A 132 OXT 0.151
REMARK 500 15 ALA A 132 C ALA A 132 OXT 0.151
REMARK 500 16 ALA A 132 C ALA A 132 OXT 0.151
REMARK 500 17 ALA A 132 C ALA A 132 OXT 0.151
REMARK 500 18 ALA A 132 C ALA A 132 OXT 0.151
REMARK 500 19 ALA A 132 C ALA A 132 OXT 0.151
REMARK 500 20 ALA A 132 C ALA A 132 OXT 0.150
REMARK 500 21 ALA A 132 C ALA A 132 OXT 0.150
REMARK 500 22 ALA A 132 C ALA A 132 OXT 0.151
REMARK 500 23 ALA A 132 C ALA A 132 OXT 0.151
REMARK 500 24 ALA A 132 C ALA A 132 OXT 0.151
REMARK 500 25 ALA A 132 C ALA A 132 OXT 0.151
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 1 ALA A 3 -56.52 -157.38
REMARK 500 1 VAL A 5 102.60 -35.52
REMARK 500 1 VAL A 11 -71.23 -119.15
REMARK 500 1 ASP A 17 -71.75 -52.25
REMARK 500 1 LYS A 21 46.76 -72.01
REMARK 500 1 SER A 22 -58.74 179.04
REMARK 500 1 ALA A 28 -66.82 171.32
REMARK 500 1 LYS A 37 58.57 -149.26
REMARK 500 1 THR A 56 -80.69 -82.86
REMARK 500 1 LYS A 58 133.04 81.29
REMARK 500 1 LEU A 66 105.01 -49.82
REMARK 500 1 ASP A 76 42.19 -102.45
REMARK 500 1 ASP A 77 -37.39 -143.58
REMARK 500 1 ARG A 78 -172.24 86.55
REMARK 500 1 TRP A 97 -67.25 -107.74
REMARK 500 1 ASN A 98 -81.32 -172.11
REMARK 500 1 ASP A 110 -124.44 51.85
REMARK 500 1 THR A 121 140.22 85.52
REMARK 500 1 ALA A 122 145.62 77.55
REMARK 500 2 ASP A 2 63.90 -65.80
REMARK 500 2 ALA A 3 -44.89 -169.94
REMARK 500 2 VAL A 5 105.26 -37.04
REMARK 500 2 SER A 13 102.68 177.07
REMARK 500 2 SER A 22 -58.99 168.60
REMARK 500 2 VAL A 25 -52.43 -133.31
REMARK 500 2 PHE A 27 101.46 -45.45
REMARK 500 2 ALA A 28 -39.77 135.16
REMARK 500 2 MET A 35 -2.57 -152.62
REMARK 500 2 LYS A 37 73.02 -117.08
REMARK 500 2 THR A 53 62.95 -111.61
REMARK 500 2 THR A 56 -75.70 63.92
REMARK 500 2 PHE A 57 27.85 -158.33
REMARK 500 2 ASP A 77 -42.38 -148.25
REMARK 500 2 ARG A 78 -160.53 114.69
REMARK 500 2 ASN A 98 -85.10 -163.66
REMARK 500 2 ASP A 110 -129.66 53.75
REMARK 500 2 ALA A 122 142.72 92.14
REMARK 500 3 VAL A 5 108.13 -46.23
REMARK 500 3 SER A 13 126.47 -171.49
REMARK 500 3 SER A 22 -56.96 162.77
REMARK 500 3 ASN A 34 -42.38 -160.41
REMARK 500 3 THR A 36 66.53 -67.06
REMARK 500 3 LYS A 37 72.57 44.24
REMARK 500 3 THR A 56 -109.51 -150.70
REMARK 500 3 LEU A 66 32.24 37.04
REMARK 500 3 THR A 73 100.81 -52.46
REMARK 500 3 ALA A 75 49.64 -79.48
REMARK 500 3 ASP A 76 -58.79 -172.04
REMARK 500 3 ARG A 78 -169.44 83.40
REMARK 500 3 TRP A 97 -59.19 -125.74
REMARK 500
REMARK 500 THIS ENTRY HAS 467 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE A 16 ASP A 17 7 147.68
REMARK 500 PHE A 16 ASP A 17 8 148.12
REMARK 500 GLU A 101 THR A 102 8 148.67
REMARK 500 PHE A 16 ASP A 17 9 144.13
REMARK 500 THR A 121 ALA A 122 10 144.53
REMARK 500 ASP A 77 ARG A 78 13 149.29
REMARK 500 ILE A 62 SER A 63 17 -149.96
REMARK 500 ASP A 77 ARG A 78 18 148.25
REMARK 500 THR A 125 ARG A 126 21 144.15
REMARK 500 ASP A 77 ARG A 78 25 149.03
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 1 PHE A 16 0.10 SIDE CHAIN
REMARK 500 1 TYR A 19 0.07 SIDE CHAIN
REMARK 500 1 ARG A 30 0.09 SIDE CHAIN
REMARK 500 1 TYR A 128 0.08 SIDE CHAIN
REMARK 500 2 PHE A 16 0.10 SIDE CHAIN
REMARK 500 2 ARG A 30 0.09 SIDE CHAIN
REMARK 500 2 TYR A 128 0.11 SIDE CHAIN
REMARK 500 3 TYR A 19 0.16 SIDE CHAIN
REMARK 500 4 ARG A 126 0.08 SIDE CHAIN
REMARK 500 4 TYR A 128 0.11 SIDE CHAIN
REMARK 500 5 PHE A 4 0.12 SIDE CHAIN
REMARK 500 5 TYR A 128 0.12 SIDE CHAIN
REMARK 500 6 TYR A 128 0.08 SIDE CHAIN
REMARK 500 7 PHE A 4 0.08 SIDE CHAIN
REMARK 500 7 TYR A 19 0.09 SIDE CHAIN
REMARK 500 7 PHE A 70 0.08 SIDE CHAIN
REMARK 500 7 TYR A 128 0.10 SIDE CHAIN
REMARK 500 8 TYR A 19 0.07 SIDE CHAIN
REMARK 500 8 TYR A 128 0.12 SIDE CHAIN
REMARK 500 9 PHE A 4 0.08 SIDE CHAIN
REMARK 500 9 TYR A 19 0.14 SIDE CHAIN
REMARK 500 9 TYR A 128 0.07 SIDE CHAIN
REMARK 500 10 PHE A 4 0.09 SIDE CHAIN
REMARK 500 10 TYR A 19 0.08 SIDE CHAIN
REMARK 500 10 ARG A 30 0.10 SIDE CHAIN
REMARK 500 11 PHE A 70 0.09 SIDE CHAIN
REMARK 500 11 ARG A 78 0.11 SIDE CHAIN
REMARK 500 11 TYR A 128 0.07 SIDE CHAIN
REMARK 500 12 PHE A 4 0.08 SIDE CHAIN
REMARK 500 12 PHE A 16 0.13 SIDE CHAIN
REMARK 500 12 TYR A 19 0.07 SIDE CHAIN
REMARK 500 12 ARG A 78 0.12 SIDE CHAIN
REMARK 500 13 TYR A 19 0.11 SIDE CHAIN
REMARK 500 13 TYR A 128 0.10 SIDE CHAIN
REMARK 500 14 PHE A 4 0.11 SIDE CHAIN
REMARK 500 14 TYR A 19 0.09 SIDE CHAIN
REMARK 500 14 ARG A 30 0.13 SIDE CHAIN
REMARK 500 15 TYR A 19 0.15 SIDE CHAIN
REMARK 500 16 TYR A 19 0.15 SIDE CHAIN
REMARK 500 16 ARG A 30 0.12 SIDE CHAIN
REMARK 500 17 PHE A 4 0.11 SIDE CHAIN
REMARK 500 17 PHE A 27 0.11 SIDE CHAIN
REMARK 500 17 ARG A 30 0.09 SIDE CHAIN
REMARK 500 17 TYR A 128 0.06 SIDE CHAIN
REMARK 500 18 TYR A 19 0.09 SIDE CHAIN
REMARK 500 18 ARG A 126 0.09 SIDE CHAIN
REMARK 500 19 PHE A 4 0.08 SIDE CHAIN
REMARK 500 19 ARG A 78 0.09 SIDE CHAIN
REMARK 500 20 TYR A 19 0.10 SIDE CHAIN
REMARK 500 20 TYR A 128 0.09 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 62 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BWY A 1 132 UNP P10790 FABPH_BOVIN 1 132
SEQRES 1 A 132 VAL ASP ALA PHE VAL GLY THR TRP LYS LEU VAL ASP SER
SEQRES 2 A 132 LYS ASN PHE ASP ASP TYR MET LYS SER LEU GLY VAL GLY
SEQRES 3 A 132 PHE ALA THR ARG GLN VAL GLY ASN MET THR LYS PRO THR
SEQRES 4 A 132 THR ILE ILE GLU VAL ASN GLY ASP THR VAL ILE ILE LYS
SEQRES 5 A 132 THR GLN SER THR PHE LYS ASN THR GLU ILE SER PHE LYS
SEQRES 6 A 132 LEU GLY VAL GLU PHE ASP GLU THR THR ALA ASP ASP ARG
SEQRES 7 A 132 LYS VAL LYS SER ILE VAL THR LEU ASP GLY GLY LYS LEU
SEQRES 8 A 132 VAL HIS VAL GLN LYS TRP ASN GLY GLN GLU THR SER LEU
SEQRES 9 A 132 VAL ARG GLU MET VAL ASP GLY LYS LEU ILE LEU THR LEU
SEQRES 10 A 132 THR HIS GLY THR ALA VAL CYS THR ARG THR TYR GLU LYS
SEQRES 11 A 132 GLN ALA
HELIX 1 1 PHE A 16 LEU A 23 1 8
HELIX 2 2 PHE A 27 ASN A 34 1 8
SHEET 1 A 4 VAL A 5 LYS A 14 0
SHEET 2 A 4 PRO A 38 VAL A 44 -1 N THR A 40 O TRP A 8
SHEET 3 A 4 VAL A 49 GLN A 54 -1 N LYS A 52 O ILE A 41
SHEET 4 A 4 ASN A 59 PHE A 64 -1 N ILE A 62 O ILE A 51
SHEET 1 B 6 GLU A 69 THR A 74 0
SHEET 2 B 6 ARG A 78 LEU A 86 -1 N VAL A 80 O GLU A 72
SHEET 3 B 6 LEU A 91 LYS A 96 -1 N VAL A 92 O THR A 85
SHEET 4 B 6 GLU A 101 MET A 108 -1 N LEU A 104 O HIS A 93
SHEET 5 B 6 LEU A 113 THR A 118 -1 N THR A 116 O VAL A 105
SHEET 6 B 6 VAL A 123 GLN A 131 -1 N ARG A 126 O LEU A 115
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - v 29 2 Bytes