Header list of 1l8c.pdb file
Complete list - b 23 2 Bytes
HEADER GENE REGULATION 19-MAR-02 1L8C
TITLE STRUCTURAL BASIS FOR HIF-1ALPHA/CBP RECOGNITION IN THE CELLULAR
TITLE 2 HYPOXIC RESPONSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CREB-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TAZ1 (TRANSCRIPTION ACTIVATION ZINC FINGER) DOMAIN,
COMPND 5 RESIDUES 345-439;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HYPOXIA-INDUCIBLE FACTOR 1 ALPHA;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: CTAD (C-TERMINAL ACTIVATION) DOMAIN, RESIDUES 776-826;
COMPND 11 SYNONYM: HIF-1 ALPHA, ARNT INTERACTING PROTEIN, MEMBER OF PAS PROTEIN
COMPND 12 1, MOP1;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GENE REGULATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.A.DAMES,M.MARTINEZ-YAMOUT,R.N.DE GUZMAN,H.J.DYSON,P.E.WRIGHT
REVDAT 4 23-FEB-22 1L8C 1 REMARK LINK
REVDAT 3 24-FEB-09 1L8C 1 VERSN
REVDAT 2 24-APR-02 1L8C 1 JRNL
REVDAT 1 10-APR-02 1L8C 0
JRNL AUTH S.A.DAMES,M.MARTINEZ-YAMOUT,R.N.DE GUZMAN,H.J.DYSON,
JRNL AUTH 2 P.E.WRIGHT
JRNL TITL STRUCTURAL BASIS FOR HIF-1 ALPHA /CBP RECOGNITION IN THE
JRNL TITL 2 CELLULAR HYPOXIC RESPONSE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 99 5271 2002
JRNL REFN ISSN 0027-8424
JRNL PMID 11959977
JRNL DOI 10.1073/PNAS.082121399
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER VERSION 6
REMARK 3 AUTHORS : PEARLMAN, D.A. ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: PEARLMAN, D.A. ET AL. (1995) COMP.
REMARK 3 PHYS.COMMU.
REMARK 4
REMARK 4 1L8C COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015732.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.1
REMARK 210 IONIC STRENGTH : 2.0 MILLIMOLAR
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM 13C, 15N-TAZ1, 2MM HIF-1A;
REMARK 210 1MM 13C, 15N-HIF-1A, 2MM TAZ1;
REMARK 210 10MM D-TRIS, 10MM D-DTT, 0.02%
REMARK 210 NAN3, 0.5MM ZNSO4
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D HSQC; 3D HNCACB; 3D
REMARK 210 CBCA(CO)NH; 3D HNCO; 3D C(CO)NH-
REMARK 210 TOCSY; 3D H(CCO)NH-TOCSY; 3D CCH-
REMARK 210 TOCSY; 3D CCH-COSY; 3D HCCH-
REMARK 210 TOCSY; 3D 15N TOCSY-HSQC; 2D
REMARK 210 CBCGCD; 2D CBCGCE; 3D HNHA; 3D
REMARK 210 HNHB; 3D HACAHB-COSY; 3D 15N
REMARK 210 NOESY-HSQC; 3D 13C HSQC-NOESY;
REMARK 210 3D 13C,15N SIMULT. NOESY; 3D 13C
REMARK 210 HMQC-NOESY; 3D 12C-FILTERED/13C-
REMARK 210 EDITED NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX800; DRX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR, NMRPIPE, NMRVIEW
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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 : 1
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 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 ARG A 41 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 1 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 ARG A 79 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 2 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 ARG A 79 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 3 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 4 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 5 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 6 ARG B 143 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 7 ARG A 41 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 7 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 7 ARG B 143 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 10 ARG A 33 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 11 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 11 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 12 ARG A 25 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 12 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 13 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 13 ARG A 79 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 15 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 15 ARG A 79 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 16 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 16 ARG A 79 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 16 ARG B 133 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 17 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 17 ARG A 41 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 19 ARG B 104 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 20 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 4.2 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 GLU A 31 -67.67 -144.16
REMARK 500 1 SER A 36 -52.15 -135.87
REMARK 500 1 VAL A 84 -52.51 -134.62
REMARK 500 1 CYS B 103 2.70 -67.08
REMARK 500 1 LEU B 105 58.63 37.42
REMARK 500 1 SER B 113 -58.60 67.67
REMARK 500 1 GLN B 117 62.59 -115.94
REMARK 500 2 PRO A 3 -106.52 -84.50
REMARK 500 2 ASN A 29 145.14 71.47
REMARK 500 2 SER A 36 -61.89 -135.62
REMARK 500 2 ALA A 55 -73.51 -80.88
REMARK 500 2 VAL A 84 -51.60 -133.05
REMARK 500 2 CYS B 103 35.87 -81.30
REMARK 500 2 ARG B 104 -75.22 -43.83
REMARK 500 2 GLN B 117 63.69 -117.78
REMARK 500 2 LEU B 135 86.29 0.59
REMARK 500 3 ALA A 34 -69.87 -135.72
REMARK 500 3 HIS A 80 3.25 -68.47
REMARK 500 3 ASP A 81 20.22 -146.25
REMARK 500 3 VAL A 84 -52.13 -123.62
REMARK 500 3 ALA A 91 -71.28 -131.64
REMARK 500 3 GLU B 112 -61.79 -91.21
REMARK 500 3 GLN B 117 63.77 -110.66
REMARK 500 3 LEU B 135 89.58 0.43
REMARK 500 4 GLU A 31 -86.04 -144.59
REMARK 500 4 ALA A 34 -63.40 -133.08
REMARK 500 4 SER A 36 -30.56 -133.38
REMARK 500 4 VAL A 84 -43.79 -135.65
REMARK 500 4 LEU B 101 -47.00 -147.31
REMARK 500 4 ARG B 104 -69.61 -26.04
REMARK 500 4 SER B 113 19.55 55.59
REMARK 500 4 GLN B 117 60.65 -119.19
REMARK 500 5 ASN A 29 -55.79 -153.13
REMARK 500 5 ARG A 33 74.94 -118.80
REMARK 500 5 PRO A 83 5.71 -63.29
REMARK 500 5 VAL A 84 -51.11 -140.84
REMARK 500 5 ALA A 91 -57.71 -131.61
REMARK 500 5 LEU B 101 99.00 -165.80
REMARK 500 5 ALA B 102 -74.42 -153.02
REMARK 500 5 ARG B 104 -67.07 179.67
REMARK 500 5 ASN B 134 -53.59 -139.59
REMARK 500 6 ASN A 29 107.80 -170.26
REMARK 500 6 VAL A 84 -51.62 -126.22
REMARK 500 6 CYS B 103 37.78 -80.02
REMARK 500 6 SER B 113 -50.72 -159.40
REMARK 500 7 GLU A 31 -101.50 -137.35
REMARK 500 7 ALA A 34 -65.61 -131.10
REMARK 500 7 PRO A 83 0.48 -62.86
REMARK 500 7 VAL A 84 -49.63 -138.40
REMARK 500 7 LEU B 101 -91.68 -146.53
REMARK 500
REMARK 500 THIS ENTRY HAS 145 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 5 HIS A 73 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 96 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 18 NE2
REMARK 620 2 CYS A 22 SG 114.8
REMARK 620 3 CYS A 35 SG 110.5 110.4
REMARK 620 4 CYS A 40 SG 110.2 107.3 103.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 97 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 49 NE2
REMARK 620 2 CYS A 53 SG 106.9
REMARK 620 3 CYS A 59 SG 115.7 108.3
REMARK 620 4 CYS A 64 SG 108.7 107.3 109.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 98 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 73 NE2
REMARK 620 2 CYS A 77 SG 111.5
REMARK 620 3 CYS A 82 SG 111.9 108.0
REMARK 620 4 CYS A 85 SG 111.0 107.9 106.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 96
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 97
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 98
REMARK 999
REMARK 999 SEQEUNCE
REMARK 999 AUTHOR STATES RESIDUE GLY56 IS A SEQUENCE VARIANT
DBREF 1L8C A 1 95 UNP P45481 CBP_MOUSE 345 439
DBREF 1L8C B 99 149 UNP Q16665 HIF1A_HUMAN 776 826
SEQADV 1L8C GLY A 56 UNP P45481 PRO 400 SEE REMARK 999
SEQRES 1 A 95 ALA ASP PRO GLU LYS ARG LYS LEU ILE GLN GLN GLN LEU
SEQRES 2 A 95 VAL LEU LEU LEU HIS ALA HIS LYS CYS GLN ARG ARG GLU
SEQRES 3 A 95 GLN ALA ASN GLY GLU VAL ARG ALA CYS SER LEU PRO HIS
SEQRES 4 A 95 CYS ARG THR MET LYS ASN VAL LEU ASN HIS MET THR HIS
SEQRES 5 A 95 CYS GLN ALA GLY LYS ALA CYS GLN VAL ALA HIS CYS ALA
SEQRES 6 A 95 SER SER ARG GLN ILE ILE SER HIS TRP LYS ASN CYS THR
SEQRES 7 A 95 ARG HIS ASP CYS PRO VAL CYS LEU PRO LEU LYS ASN ALA
SEQRES 8 A 95 SER ASP LYS ARG
SEQRES 1 B 51 SER ASP LEU ALA CYS ARG LEU LEU GLY GLN SER MET ASP
SEQRES 2 B 51 GLU SER GLY LEU PRO GLN LEU THR SER TYR ASP CYS GLU
SEQRES 3 B 51 VAL ASN ALA PRO ILE GLN GLY SER ARG ASN LEU LEU GLN
SEQRES 4 B 51 GLY GLU GLU LEU LEU ARG ALA LEU ASP GLN VAL ASN
HET ZN A 96 1
HET ZN A 97 1
HET ZN A 98 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 3(ZN 2+)
HELIX 1 1 ASP A 2 ASN A 29 1 28
HELIX 2 2 HIS A 39 CYS A 53 1 15
HELIX 3 3 ALA A 55 CYS A 59 5 5
HELIX 4 4 VAL A 61 CYS A 77 1 17
HELIX 5 5 VAL A 84 ASN A 90 1 7
HELIX 6 6 LEU B 106 ASP B 111 1 6
HELIX 7 7 THR B 119 ALA B 127 1 9
HELIX 8 8 GLY B 138 GLN B 147 1 10
LINK NE2 HIS A 18 ZN ZN A 96 1555 1555 2.09
LINK SG CYS A 22 ZN ZN A 96 1555 1555 2.29
LINK SG CYS A 35 ZN ZN A 96 1555 1555 2.27
LINK SG CYS A 40 ZN ZN A 96 1555 1555 2.26
LINK NE2 HIS A 49 ZN ZN A 97 1555 1555 2.07
LINK SG CYS A 53 ZN ZN A 97 1555 1555 2.26
LINK SG CYS A 59 ZN ZN A 97 1555 1555 2.27
LINK SG CYS A 64 ZN ZN A 97 1555 1555 2.26
LINK NE2 HIS A 73 ZN ZN A 98 1555 1555 2.08
LINK SG CYS A 77 ZN ZN A 98 1555 1555 2.27
LINK SG CYS A 82 ZN ZN A 98 1555 1555 2.27
LINK SG CYS A 85 ZN ZN A 98 1555 1555 2.26
SITE 1 AC1 5 HIS A 18 CYS A 22 CYS A 35 CYS A 40
SITE 2 AC1 5 LYS A 44
SITE 1 AC2 4 HIS A 49 CYS A 53 CYS A 59 CYS A 64
SITE 1 AC3 5 HIS A 73 CYS A 77 ARG A 79 CYS A 82
SITE 2 AC3 5 CYS A 85
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 - b 23 2 Bytes