Header list of 1ho0.pdb file
Complete list - 27 20 Bytes
HEADER HORMONE/GROWTH FACTOR 08-DEC-00 1HO0 TITLE NEW B-CHAIN MUTANT OF BOVINE INSULIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: INSULIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: B-CHAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. IT WAS SOURCE 4 OBTAINED BY SOLID PHASE SYNTHESIS USING A PEPTIDE SYNTHESIZER. KEYWDS BETA_TURN (20-23), ALPHA_HELIX (9-19), HORMONE-GROWTH FACTOR COMPLEX EXPDTA SOLUTION NMR NUMMDL 21 AUTHOR F.Y.DUPRADEAU,T.RICHARD,G.LE FLEM,H.OULYADI,Y.PRIGENT,J.P.MONTI REVDAT 4 27-OCT-21 1HO0 1 REMARK SEQADV REVDAT 3 24-FEB-09 1HO0 1 VERSN REVDAT 2 11-DEC-02 1HO0 1 JRNL AUTHOR REVDAT 1 20-DEC-00 1HO0 0 JRNL AUTH F.Y.DUPRADEAU,T.RICHARD,G.LE FLEM,H.OULYADI,Y.PRIGENT, JRNL AUTH 2 J.P.MONTI JRNL TITL A NEW B-CHAIN MUTANT OF INSULIN: COMPARISON WITH THE INSULIN JRNL TITL 2 CRYSTAL STRUCTURE AND ROLE OF SULFONATE GROUPS IN THE JRNL TITL 3 B-CHAIN STRUCTURE JRNL REF J.PEPT.RES. V. 60 56 2002 JRNL REFN ISSN 1397-002X JRNL PMID 12081626 JRNL DOI 10.1034/J.1399-3011.2002.02990.X REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.1, NMR-REFINE 98.0 REMARK 3 AUTHORS : BRUKER SA (XWINNMR), MOLECULAR SIMULATION INC. REMARK 3 (NMR-REFINE) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THESE STRUCTURES ARE BASED ON A TOTAL REMARK 3 OF 286 RESTRAINTS: 243 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 39 REMARK 3 DIHEDRAL ANGLE RESTRAINTS AND 4 DISTANCE RESTRAINTS FROM REMARK 3 HYDROGEN BONDS. REMARK 4 REMARK 4 1HO0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-DEC-00. REMARK 100 THE DEPOSITION ID IS D_1000012473. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 293 REMARK 210 PH : 3.6 REMARK 210 IONIC STRENGTH : 0 REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.5 MM PEPTIDE CONCENTRATION REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; TOCSY; NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : GIFA 4.2, INSIGHT II 98.0 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES REMARK 210 WITH THE LOWEST ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 21 REMARK 210 REMARK 210 REMARK: THIS FAMILY OF STRUCTURES WAS DETERMINED USING STANDARD 2D REMARK 210 HOMONUCLEAR TECHNIQUES. 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 GLU A 13 CD GLU A 13 OE2 0.118 REMARK 500 1 GLU A 21 CD GLU A 21 OE2 0.118 REMARK 500 2 GLU A 13 CD GLU A 13 OE2 0.118 REMARK 500 2 GLU A 21 CD GLU A 21 OE2 0.118 REMARK 500 3 GLU A 13 CD GLU A 13 OE2 0.119 REMARK 500 3 GLU A 21 CD GLU A 21 OE2 0.119 REMARK 500 4 GLU A 13 CD GLU A 13 OE2 0.118 REMARK 500 4 GLU A 21 CD GLU A 21 OE2 0.118 REMARK 500 5 GLU A 13 CD GLU A 13 OE2 0.118 REMARK 500 5 GLU A 21 CD GLU A 21 OE2 0.118 REMARK 500 6 GLU A 13 CD GLU A 13 OE2 0.118 REMARK 500 6 GLU A 21 CD GLU A 21 OE2 0.118 REMARK 500 7 GLU A 13 CD GLU A 13 OE2 0.117 REMARK 500 7 GLU A 21 CD GLU A 21 OE2 0.118 REMARK 500 8 GLU A 13 CD GLU A 13 OE2 0.117 REMARK 500 8 GLU A 21 CD GLU A 21 OE2 0.118 REMARK 500 9 GLU A 13 CD GLU A 13 OE2 0.118 REMARK 500 9 GLU A 21 CD GLU A 21 OE2 0.118 REMARK 500 10 GLU A 13 CD GLU A 13 OE2 0.118 REMARK 500 10 GLU A 21 CD GLU A 21 OE2 0.118 REMARK 500 11 GLU A 13 CD GLU A 13 OE2 0.118 REMARK 500 11 GLU A 21 CD GLU A 21 OE2 0.118 REMARK 500 12 GLU A 13 CD GLU A 13 OE2 0.118 REMARK 500 12 GLU A 21 CD GLU A 21 OE2 0.118 REMARK 500 13 GLU A 13 CD GLU A 13 OE2 0.118 REMARK 500 13 GLU A 21 CD GLU A 21 OE2 0.118 REMARK 500 14 GLU A 13 CD GLU A 13 OE2 0.118 REMARK 500 14 GLU A 21 CD GLU A 21 OE2 0.118 REMARK 500 15 GLU A 13 CD GLU A 13 OE2 0.119 REMARK 500 15 GLU A 21 CD GLU A 21 OE2 0.118 REMARK 500 16 GLU A 13 CD GLU A 13 OE2 0.118 REMARK 500 16 GLU A 21 CD GLU A 21 OE2 0.118 REMARK 500 17 GLU A 13 CD GLU A 13 OE2 0.119 REMARK 500 17 GLU A 21 CD GLU A 21 OE2 0.118 REMARK 500 18 GLU A 13 CD GLU A 13 OE2 0.119 REMARK 500 18 GLU A 21 CD GLU A 21 OE2 0.119 REMARK 500 19 GLU A 13 CD GLU A 13 OE2 0.118 REMARK 500 19 GLU A 21 CD GLU A 21 OE2 0.118 REMARK 500 20 GLU A 13 CD GLU A 13 OE2 0.118 REMARK 500 20 GLU A 21 CD GLU A 21 OE2 0.118 REMARK 500 21 GLU A 13 CD GLU A 13 OE2 0.117 REMARK 500 21 GLU A 21 CD GLU A 21 OE2 0.118 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 1 HIS A 5 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES REMARK 500 1 HIS A 10 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES REMARK 500 1 TYR A 16 N - CA - CB ANGL. DEV. = -14.5 DEGREES REMARK 500 1 TYR A 16 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 1 TYR A 16 CB - CG - CD1 ANGL. DEV. = 3.8 DEGREES REMARK 500 1 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES REMARK 500 1 ARG A 22 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 2 VAL A 2 CB - CA - C ANGL. DEV. = 12.2 DEGREES REMARK 500 2 HIS A 5 ND1 - CE1 - NE2 ANGL. DEV. = 8.1 DEGREES REMARK 500 2 HIS A 10 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES REMARK 500 2 TYR A 16 N - CA - CB ANGL. DEV. = -15.2 DEGREES REMARK 500 2 TYR A 16 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES REMARK 500 2 TYR A 16 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES REMARK 500 2 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES REMARK 500 2 ARG A 22 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 3 HIS A 5 ND1 - CE1 - NE2 ANGL. DEV. = 8.1 DEGREES REMARK 500 3 HIS A 10 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES REMARK 500 3 TYR A 16 N - CA - CB ANGL. DEV. = -15.3 DEGREES REMARK 500 3 TYR A 16 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 3 TYR A 16 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES REMARK 500 3 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES REMARK 500 3 ARG A 22 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 4 HIS A 5 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES REMARK 500 4 HIS A 10 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES REMARK 500 4 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES REMARK 500 4 ARG A 22 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 5 HIS A 5 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES REMARK 500 5 HIS A 10 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES REMARK 500 5 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES REMARK 500 5 ARG A 22 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 6 HIS A 5 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES REMARK 500 6 HIS A 10 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES REMARK 500 6 ALA A 14 N - CA - CB ANGL. DEV. = -12.6 DEGREES REMARK 500 6 TYR A 16 N - CA - CB ANGL. DEV. = -15.7 DEGREES REMARK 500 6 TYR A 16 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES REMARK 500 6 TYR A 16 CB - CG - CD1 ANGL. DEV. = 4.0 DEGREES REMARK 500 6 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES REMARK 500 6 ARG A 22 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 7 HIS A 5 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES REMARK 500 7 HIS A 10 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES REMARK 500 7 TYR A 16 N - CA - CB ANGL. DEV. = -14.7 DEGREES REMARK 500 7 TYR A 16 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES REMARK 500 7 TYR A 16 CB - CG - CD1 ANGL. DEV. = 3.9 DEGREES REMARK 500 7 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 5.9 DEGREES REMARK 500 7 ARG A 22 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 8 HIS A 5 ND1 - CE1 - NE2 ANGL. DEV. = 8.1 DEGREES REMARK 500 8 HIS A 10 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES REMARK 500 8 TYR A 16 N - CA - CB ANGL. DEV. = -14.5 DEGREES REMARK 500 8 TYR A 16 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES REMARK 500 8 TYR A 16 CB - CG - CD1 ANGL. DEV. = 3.8 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 142 ANGLE DEVIATIONS. 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 LEU A 6 -55.17 -139.81 REMARK 500 1 LEU A 11 -70.80 -63.37 REMARK 500 1 ALA A 14 -36.51 -36.53 REMARK 500 1 TYR A 16 -29.71 -39.31 REMARK 500 1 ARG A 22 -41.64 -164.99 REMARK 500 1 PHE A 25 -58.28 -126.63 REMARK 500 1 THR A 27 124.19 64.41 REMARK 500 2 VAL A 2 -96.07 -98.63 REMARK 500 2 LEU A 6 -53.33 -138.45 REMARK 500 2 LEU A 11 -72.35 -61.60 REMARK 500 2 TYR A 16 -29.85 -39.34 REMARK 500 2 PHE A 25 -68.22 69.96 REMARK 500 3 ASN A 3 115.74 56.96 REMARK 500 3 GLN A 4 -65.90 -126.83 REMARK 500 3 LEU A 11 -72.38 -62.28 REMARK 500 3 TYR A 16 -29.67 -39.30 REMARK 500 3 PHE A 24 96.75 63.89 REMARK 500 4 ASN A 3 117.93 59.46 REMARK 500 5 GLU A 21 -36.43 -37.64 REMARK 500 5 LYS A 29 127.66 65.06 REMARK 500 6 ALA A 14 -34.30 -33.60 REMARK 500 6 TYR A 16 -33.62 -39.53 REMARK 500 6 LYS A 29 -66.70 -120.85 REMARK 500 7 LEU A 11 -71.02 -63.77 REMARK 500 7 ALA A 14 -34.94 -36.45 REMARK 500 7 TYR A 16 -34.73 -38.72 REMARK 500 7 THR A 27 125.43 65.07 REMARK 500 8 LEU A 11 -70.69 -63.10 REMARK 500 8 ALA A 14 -36.85 -36.54 REMARK 500 8 TYR A 16 -30.52 -39.18 REMARK 500 9 VAL A 2 96.30 85.23 REMARK 500 9 GLN A 4 -61.99 -138.46 REMARK 500 9 SER A 7 -50.43 -120.24 REMARK 500 9 LEU A 11 -70.91 -64.54 REMARK 500 9 ALA A 14 -35.09 -36.38 REMARK 500 9 TYR A 16 -35.01 -38.56 REMARK 500 9 GLU A 21 -38.36 -39.86 REMARK 500 10 LEU A 6 136.64 64.44 REMARK 500 10 LEU A 11 -71.38 -59.23 REMARK 500 10 TYR A 16 -28.98 -38.86 REMARK 500 10 LYS A 29 129.22 64.51 REMARK 500 11 HIS A 5 132.82 63.21 REMARK 500 11 LEU A 6 82.32 60.11 REMARK 500 11 LEU A 11 -71.53 -58.88 REMARK 500 11 TYR A 16 -29.55 -39.22 REMARK 500 11 TYR A 26 -60.91 -124.81 REMARK 500 12 LEU A 11 -70.78 -63.53 REMARK 500 12 ALA A 14 -36.60 -36.58 REMARK 500 12 TYR A 16 -29.67 -39.32 REMARK 500 12 GLU A 21 -38.09 -38.94 REMARK 500 REMARK 500 THIS ENTRY HAS 95 RAMACHANDRAN OUTLIERS. 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 4 TYR A 16 0.12 SIDE CHAIN REMARK 500 5 TYR A 16 0.11 SIDE CHAIN REMARK 500 6 TYR A 16 0.07 SIDE CHAIN REMARK 500 7 TYR A 16 0.06 SIDE CHAIN REMARK 500 9 TYR A 16 0.06 SIDE CHAIN REMARK 500 15 TYR A 16 0.11 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1HO0 A 1 30 UNP P01317 INS_BOVIN 25 54 SEQADV 1HO0 SER A 7 UNP P01317 CYS 31 ENGINEERED MUTATION SEQADV 1HO0 SER A 19 UNP P01317 CYS 43 ENGINEERED MUTATION SEQRES 1 A 30 PHE VAL ASN GLN HIS LEU SER GLY SER HIS LEU VAL GLU SEQRES 2 A 30 ALA LEU TYR LEU VAL SER GLY GLU ARG GLY PHE PHE TYR SEQRES 3 A 30 THR PRO LYS ALA HELIX 1 1 GLY A 8 LEU A 15 1 8 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 - 27 20 Bytes