Header list of 1aj1.pdb file
Complete list - 11 20 Bytes
HEADER ANTIBIOTIC 14-MAY-97 1AJ1
TITLE NMR STRUCTURE OF THE LANTIBIOTIC ACTAGARDINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LANTIBIOTIC ACTAGARDINE;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACTINOPLANES LIGURIENSIS;
SOURCE 3 ORGANISM_TAXID: 69484;
SOURCE 4 ATCC: 31048, 31049
KEYWDS ANTIBIOTIC, LANTIBIOTIC, ANTIMICROBIAL, BACTERIOCIN, THIOESTER,
KEYWDS 2 TRANSMEMBRANE PORE
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR N.ZIMMERMANN,G.JUNG
REVDAT 5 11-DEC-19 1AJ1 1 COMPND SOURCE JRNL DBREF
REVDAT 5 2 1 LINK
REVDAT 4 27-JUL-11 1AJ1 1 ATOM DBREF HETATM REMARK
REVDAT 4 2 1 REVDAT SEQRES
REVDAT 3 13-JUL-11 1AJ1 1 VERSN
REVDAT 2 24-FEB-09 1AJ1 1 VERSN
REVDAT 1 15-OCT-97 1AJ1 0
JRNL AUTH N.ZIMMERMANN,G.JUNG
JRNL TITL THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE LANTIBIOTIC
JRNL TITL 2 MUREIN-BIOSYNTHESIS-INHIBITOR ACTAGARDINE DETERMINED BY NMR.
JRNL REF EUR.J.BIOCHEM. V. 246 809 1997
JRNL REFN ISSN 0014-2956
JRNL PMID 9219543
JRNL DOI 10.1111/J.1432-1033.1997.00809.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.ZIMMERMANN,J.W.METZGER,G.JUNG
REMARK 1 TITL THE TETRACYCLIC LANTIBIOTIC ACTAGARDINE. 1H-NMR AND 13C-NMR
REMARK 1 TITL 2 ASSIGNMENTS AND REVISED PRIMARY STRUCTURE
REMARK 1 REF EUR.J.BIOCHEM. V. 228 786 1995
REMARK 1 REFN ISSN 0014-2956
REMARK 1 PMID 7737178
REMARK 1 DOI 10.1111/J.1432-1033.1995.TB20324.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : IRMA
REMARK 3 AUTHORS : BOELENS,BONVIN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1AJ1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170876.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 3.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX2-600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : BRUKER UXNMR UXNMR, BIOSYM FELIX
REMARK 210 2.3, BIOSYM NMRCHITECT NMRCHITECT
REMARK 210 METHOD USED : DISTANCE GEOMETRY, ITERATIVE
REMARK 210 RELAXATION MATRIX REFINEMENT,
REMARK 210 RESTRAINED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATIONS, BEST
REMARK 210 RELAXATION MATRIX R- FACTORS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE ACTAGARDINE IS OLIGOPEPTIDE, A MEMBER OF LANTIBIOTIC CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: ACTAGARDINE
REMARK 400 CHAIN: A
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: ACTAGARDINE IS A TRICYCLIC PEPTIDE. POST
REMARK 400 TRANSLATIONAL MATURATION OF LANTIBIOTICS INVOLVES
REMARK 400 THE ENZYMIC CONVERSION OF THR AND SER INTO
REMARK 400 DEHYDRATED AMINO ACIDS AND THE FORMATION OF
REMARK 400 THIOETHER BONDS WITH CYSTEINE. THE THIOETHER BONDS
REMARK 400 WITH CYSTEINE RESULT IN THREE RING STRUCTURES. THIS
REMARK 400 IS FOLLOWED BY MEMBRANE TRANSLOCATION AND CLEAVAGE
REMARK 400 OF THE MODIFIED PRECURSOR.
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 GLU A 11 CD GLU A 11 OE2 0.119
REMARK 500 1 CYS A 19 C CYS A 19 OXT 0.200
REMARK 500 2 GLU A 11 CD GLU A 11 OE2 0.119
REMARK 500 2 CYS A 19 C CYS A 19 OXT 0.200
REMARK 500 3 GLU A 11 CD GLU A 11 OE2 0.119
REMARK 500 3 CYS A 19 C CYS A 19 OXT 0.200
REMARK 500 4 GLU A 11 CD GLU A 11 OE2 0.119
REMARK 500 4 CYS A 19 C CYS A 19 OXT 0.200
REMARK 500 5 GLU A 11 CD GLU A 11 OE2 0.119
REMARK 500 5 CYS A 19 C CYS A 19 OXT 0.199
REMARK 500 6 GLU A 11 CD GLU A 11 OE2 0.120
REMARK 500 6 CYS A 19 C CYS A 19 OXT 0.200
REMARK 500 7 GLU A 11 CD GLU A 11 OE2 0.119
REMARK 500 7 CYS A 19 C CYS A 19 OXT 0.199
REMARK 500 8 GLU A 11 CD GLU A 11 OE2 0.119
REMARK 500 8 CYS A 19 C CYS A 19 OXT 0.200
REMARK 500 9 GLU A 11 CD GLU A 11 OE2 0.120
REMARK 500 9 CYS A 19 C CYS A 19 OXT 0.200
REMARK 500 10 GLU A 11 CD GLU A 11 OE2 0.119
REMARK 500 10 CYS A 19 C CYS A 19 OXT 0.200
REMARK 500 11 GLU A 11 CD GLU A 11 OE2 0.119
REMARK 500 11 CYS A 19 C CYS A 19 OXT 0.200
REMARK 500 12 GLU A 11 CD GLU A 11 OE2 0.119
REMARK 500 12 CYS A 19 C CYS A 19 OXT 0.200
REMARK 500 13 GLU A 11 CD GLU A 11 OE2 0.120
REMARK 500 13 CYS A 19 C CYS A 19 OXT 0.199
REMARK 500 14 GLU A 11 CD GLU A 11 OE2 0.119
REMARK 500 14 CYS A 19 C CYS A 19 OXT 0.199
REMARK 500 15 GLU A 11 CD GLU A 11 OE2 0.120
REMARK 500 15 CYS A 19 C CYS A 19 OXT 0.200
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 15 CYS A 17 CB - CA - C ANGL. DEV. = 7.2 DEGREES
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 VAL A 5 -75.92 -77.67
REMARK 500 1 CYS A 6 119.22 52.47
REMARK 500 1 LEU A 8 64.22 -110.30
REMARK 500 1 VAL A 15 -36.07 -139.02
REMARK 500 2 VAL A 5 -74.07 -78.40
REMARK 500 2 CYS A 6 123.08 48.17
REMARK 500 2 DBB A 7 -34.64 96.61
REMARK 500 2 LEU A 8 42.49 -96.71
REMARK 500 2 VAL A 15 -49.00 -135.97
REMARK 500 3 VAL A 5 -70.59 -79.20
REMARK 500 3 CYS A 6 124.95 30.45
REMARK 500 3 LEU A 8 61.26 -115.97
REMARK 500 3 VAL A 15 -33.95 -141.59
REMARK 500 4 VAL A 5 -76.19 -77.99
REMARK 500 4 CYS A 6 120.05 49.71
REMARK 500 4 DBB A 7 -33.70 97.17
REMARK 500 4 LEU A 8 55.33 -98.27
REMARK 500 4 VAL A 15 -51.07 -136.57
REMARK 500 5 VAL A 5 -74.64 -78.84
REMARK 500 5 CYS A 6 121.09 38.11
REMARK 500 5 LEU A 8 61.21 -111.26
REMARK 500 5 VAL A 15 -49.41 -136.57
REMARK 500 6 VAL A 5 -73.86 -78.54
REMARK 500 6 CYS A 6 122.70 44.11
REMARK 500 6 DBB A 7 -33.19 97.05
REMARK 500 6 LEU A 8 43.09 -98.20
REMARK 500 6 VAL A 15 -47.96 -135.98
REMARK 500 7 VAL A 5 -76.09 -77.84
REMARK 500 7 CYS A 6 119.34 52.31
REMARK 500 7 DBB A 7 -33.97 97.66
REMARK 500 7 LEU A 8 55.30 -98.07
REMARK 500 7 VAL A 15 -50.94 -136.57
REMARK 500 8 VAL A 5 -76.08 -77.81
REMARK 500 8 CYS A 6 119.21 52.04
REMARK 500 8 DBB A 7 -33.35 98.04
REMARK 500 8 LEU A 8 55.14 -98.24
REMARK 500 8 VAL A 15 -34.35 -140.63
REMARK 500 8 CYS A 17 -162.91 -79.52
REMARK 500 9 VAL A 5 -76.02 -77.69
REMARK 500 9 CYS A 6 120.48 51.74
REMARK 500 9 LEU A 8 63.11 -107.63
REMARK 500 9 VAL A 15 -50.02 -134.27
REMARK 500 10 VAL A 5 -75.65 -77.91
REMARK 500 10 CYS A 6 117.75 48.35
REMARK 500 10 LEU A 8 51.62 -95.77
REMARK 500 10 VAL A 15 -46.80 -137.37
REMARK 500 11 VAL A 5 -76.12 -77.78
REMARK 500 11 CYS A 6 119.34 52.34
REMARK 500 11 DBB A 7 -33.98 97.68
REMARK 500 11 LEU A 8 55.01 -97.74
REMARK 500
REMARK 500 THIS ENTRY HAS 69 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 VAL A 5 CYS A 6 1 139.32
REMARK 500 CYS A 6 DBB A 7 1 146.55
REMARK 500 ALA A 18 CYS A 19 1 102.52
REMARK 500 VAL A 5 CYS A 6 2 138.81
REMARK 500 ALA A 18 CYS A 19 2 103.53
REMARK 500 TRP A 4 VAL A 5 3 148.48
REMARK 500 VAL A 5 CYS A 6 3 137.43
REMARK 500 ALA A 18 CYS A 19 3 103.40
REMARK 500 VAL A 5 CYS A 6 4 140.91
REMARK 500 CYS A 6 DBB A 7 4 149.26
REMARK 500 ALA A 18 CYS A 19 4 99.60
REMARK 500 TRP A 4 VAL A 5 5 146.69
REMARK 500 VAL A 5 CYS A 6 5 139.48
REMARK 500 ALA A 18 CYS A 19 5 101.68
REMARK 500 VAL A 5 CYS A 6 6 140.88
REMARK 500 ALA A 18 CYS A 19 6 103.44
REMARK 500 VAL A 5 CYS A 6 7 141.34
REMARK 500 CYS A 6 DBB A 7 7 148.89
REMARK 500 ALA A 18 CYS A 19 7 99.40
REMARK 500 VAL A 5 CYS A 6 8 141.29
REMARK 500 CYS A 6 DBB A 7 8 148.49
REMARK 500 ALA A 18 CYS A 19 8 103.07
REMARK 500 VAL A 5 CYS A 6 9 139.12
REMARK 500 CYS A 6 DBB A 7 9 146.62
REMARK 500 ALA A 18 CYS A 19 9 103.31
REMARK 500 VAL A 5 CYS A 6 10 141.24
REMARK 500 CYS A 6 DBB A 7 10 149.20
REMARK 500 ALA A 18 CYS A 19 10 100.95
REMARK 500 VAL A 5 CYS A 6 11 141.35
REMARK 500 CYS A 6 DBB A 7 11 148.70
REMARK 500 ALA A 18 CYS A 19 11 102.14
REMARK 500 VAL A 5 CYS A 6 12 141.76
REMARK 500 CYS A 6 DBB A 7 12 146.73
REMARK 500 ALA A 18 CYS A 19 12 103.81
REMARK 500 VAL A 5 CYS A 6 13 140.21
REMARK 500 ALA A 18 CYS A 19 13 102.20
REMARK 500 VAL A 5 CYS A 6 14 141.32
REMARK 500 CYS A 6 DBB A 7 14 148.02
REMARK 500 ALA A 18 CYS A 19 14 101.95
REMARK 500 VAL A 5 CYS A 6 15 138.06
REMARK 500 CYS A 6 DBB A 7 15 148.25
REMARK 500 ALA A 18 CYS A 19 15 105.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MQX RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF TYPE B LANTIBIOTICS MERSACIDIN IN MEOH/H2O
REMARK 900 MIXTURE
REMARK 900 RELATED ID: 1MQY RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF TYPE B LANTIBIOTICS MERSACIDIN IN DPC MICELLES
REMARK 900 RELATED ID: 1MQZ RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF TYPE B LANTIBIOTICS MERSACIDIN BOUND TO LIPID
REMARK 900 II IN DPC MICELLES
REMARK 900 RELATED ID: 1QOW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE TUPE B LANTIBIOTIC MERSACIDIN
REMARK 900 RELATED ID: 1W9N RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE LANTIBIOTIC EPILANCIN 15X
REMARK 900 RELATED ID: 1WCO RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF NISIN AND LIPID II COMPLEX
REMARK 900 RELATED ID: 2DDE RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE LANTIBIOTIC CINNAMYCIN COMPLEXED WITH
REMARK 900 LYSOPHOSPHATIDYLETHANOLAMINE
REMARK 900 RELATED ID: 2KTN RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF LCH-ALPHA PEPTIDE FROM TWO-COMPONENT
REMARK 900 LANTIBIOTIC SYSTEM LICHENICIDIN VK21 A1
REMARK 900 RELATED ID: 2KTO RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF LCH-BETA PEPTIDE FROM TWO-COMPONENT
REMARK 900 LANTIBIOTIC LICHENICIDIN VK21 A2
DBREF 1AJ1 A 1 19 PDB 1AJ1 1AJ1 1 19
SEQRES 1 A 19 DAL SER GLY TRP VAL CYS DBB LEU DBB ILE GLU CYS GLY
SEQRES 2 A 19 DBB VAL ILE CYS ALA CYS
MODRES 1AJ1 DBB A 7 THR POST-TRANSLATIONAL MODIFICATION
MODRES 1AJ1 DBB A 9 THR POST-TRANSLATIONAL MODIFICATION
MODRES 1AJ1 DBB A 14 THR POST-TRANSLATIONAL MODIFICATION
HET DAL A 1 10
HET DBB A 7 12
HET DBB A 9 12
HET DBB A 14 12
HETNAM DAL D-ALANINE
HETNAM DBB D-ALPHA-AMINOBUTYRIC ACID
FORMUL 1 DAL C3 H7 N O2
FORMUL 1 DBB 3(C4 H9 N O2)
LINK C DAL A 1 N SER A 2 1555 1555 1.35
LINK CB DAL A 1 SG CYS A 6 1555 1555 1.81
LINK C CYS A 6 N DBB A 7 1555 1555 1.32
LINK C DBB A 7 N LEU A 8 1555 1555 1.35
LINK CB DBB A 7 SG CYS A 12 1555 1555 1.84
LINK C LEU A 8 N DBB A 9 1555 1555 1.35
LINK CB DBB A 9 SG CYS A 17 1555 1555 1.82
LINK C DBB A 9 N ILE A 10 1555 1555 1.35
LINK C GLY A 13 N DBB A 14 1555 1555 1.35
LINK CB DBB A 14 SG CYS A 19 1555 1555 1.82
LINK C DBB A 14 N VAL A 15 1555 1555 1.36
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 - 11 20 Bytes