Header list of 1ag7.pdb file
Complete list - 16 20 Bytes
HEADER NEUROTOXIN 03-APR-97 1AG7
TITLE CONOTOXIN GS, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CONOTOXIN GS;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CONUS GEOGRAPHUS;
SOURCE 3 ORGANISM_COMMON: GEOGRAPHY CONE;
SOURCE 4 ORGANISM_TAXID: 6491
KEYWDS NEUROTOXIN, MU-CONOTOXIN, SODIUM CHANNEL BLOCKER, CYSTINE KNOT MOTIF
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.M.HILL,P.F.ALEWOOD,D.J.CRAIK
REVDAT 3 16-FEB-22 1AG7 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1AG7 1 VERSN
REVDAT 1 08-APR-98 1AG7 0
JRNL AUTH J.M.HILL,P.F.ALEWOOD,D.J.CRAIK
JRNL TITL SOLUTION STRUCTURE OF THE SODIUM CHANNEL ANTAGONIST
JRNL TITL 2 CONOTOXIN GS: A NEW MOLECULAR CALIPER FOR PROBING SODIUM
JRNL TITL 3 CHANNEL GEOMETRY.
JRNL REF STRUCTURE V. 5 571 1997
JRNL REFN ISSN 0969-2126
JRNL PMID 9115446
JRNL DOI 10.1016/S0969-2126(97)00212-8
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.YANAGAWA,T.ABE,M.SATAKE,S.ODANI,J.SUZUKI,K.ISHIKAWA
REMARK 1 TITL A NOVEL SODIUM CHANNEL INHIBITOR FROM CONUS GEOGRAPHUS:
REMARK 1 TITL 2 PURIFICATION, STRUCTURE, AND PHARMACOLOGICAL PROPERTIES
REMARK 1 REF BIOCHEMISTRY V. 27 6256 1988
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 50 INITIAL STRUCTURES WERE CALCULATED
REMARK 3 USING A SIMULATED ANNEALING PROTOCOL WITHIN THE PROGRAM X-PLOR.
REMARK 3 THESE STRUCTURES WERE THEN ENERGY MINIMIZED USING 1000 CYCLES OF
REMARK 3 CONJUGATE GRADIENT MINIMIZATION WITH A REFINED FORCEFIELD BASED
REMARK 3 ON THE PROGRAM CHARMM [BROOKS ET AL. (1983) J. COMPUT. CHEM., 4,
REMARK 3 187-217].
REMARK 4
REMARK 4 1AG7 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_1000170776.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 2.9
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; E-COSY; TOCSY; NOESY;
REMARK 210 1H-13C HMQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : ARX-500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGIES AND LEAST NUMBER
REMARK 210 OF RESTRAINT VIOLATIONS
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 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-20
REMARK 470 RES CSSEQI ATOMS
REMARK 470 CGU A 32 OE12 OE22
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 HG SER A 3 HG SER A 7 1.25
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 12 CYS A 27 CA - CB - SG ANGL. DEV. = 6.6 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 CYS A 2 177.76 -53.86
REMARK 500 1 ARG A 8 -169.87 -79.95
REMARK 500 1 CYS A 14 172.70 -56.09
REMARK 500 2 CYS A 2 178.55 -56.30
REMARK 500 2 ARG A 5 92.03 -67.10
REMARK 500 2 CYS A 14 172.25 -55.16
REMARK 500 2 ARG A 21 -163.50 71.43
REMARK 500 2 GLN A 25 158.82 -49.65
REMARK 500 2 HIS A 31 32.19 -88.77
REMARK 500 2 ASP A 33 48.02 -106.92
REMARK 500 3 CYS A 2 178.56 -54.85
REMARK 500 3 ARG A 5 96.06 -67.49
REMARK 500 3 ARG A 8 -169.57 -75.12
REMARK 500 3 GLN A 25 105.02 -59.01
REMARK 500 3 ILE A 28 -167.57 -127.00
REMARK 500 3 HIS A 31 59.09 -92.02
REMARK 500 3 CGU A 32 -131.48 -130.20
REMARK 500 3 ASP A 33 52.11 -158.28
REMARK 500 4 ARG A 8 -168.46 -71.04
REMARK 500 4 GLN A 12 129.66 -39.90
REMARK 500 4 CYS A 14 170.36 -56.77
REMARK 500 4 HIS A 31 67.27 -116.49
REMARK 500 4 CGU A 32 -130.34 -113.76
REMARK 500 4 ASP A 33 34.66 -162.47
REMARK 500 5 CYS A 2 -175.75 -67.57
REMARK 500 5 CYS A 14 174.18 -56.70
REMARK 500 5 ASN A 23 102.78 -160.49
REMARK 500 5 GLN A 25 175.69 -57.70
REMARK 500 5 HIS A 31 33.39 -98.45
REMARK 500 5 ASP A 33 50.74 -113.90
REMARK 500 6 ARG A 5 91.88 -69.06
REMARK 500 6 ARG A 8 -169.03 -77.51
REMARK 500 6 GLN A 12 124.64 -39.99
REMARK 500 6 CYS A 14 170.19 -57.85
REMARK 500 6 ARG A 21 21.96 -73.56
REMARK 500 6 HIS A 31 59.37 -92.84
REMARK 500 7 CYS A 2 -178.65 -57.71
REMARK 500 7 ARG A 5 92.81 -69.05
REMARK 500 7 ARG A 8 -162.33 -76.46
REMARK 500 7 ASN A 23 110.83 -160.10
REMARK 500 7 ILE A 28 -168.58 -129.24
REMARK 500 7 HIS A 31 31.37 -92.90
REMARK 500 7 CGU A 32 91.61 -167.56
REMARK 500 7 ASP A 33 50.93 -100.15
REMARK 500 8 CYS A 2 179.89 -58.37
REMARK 500 8 ARG A 5 94.80 -67.09
REMARK 500 8 ARG A 8 -167.78 -76.74
REMARK 500 8 ASN A 23 97.84 -160.36
REMARK 500 8 ILE A 28 -167.60 -126.17
REMARK 500 8 CGU A 32 89.74 -155.23
REMARK 500
REMARK 500 THIS ENTRY HAS 113 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 1 ARG A 5 0.31 SIDE CHAIN
REMARK 500 1 ARG A 8 0.20 SIDE CHAIN
REMARK 500 1 ARG A 18 0.25 SIDE CHAIN
REMARK 500 1 ARG A 21 0.27 SIDE CHAIN
REMARK 500 2 ARG A 5 0.31 SIDE CHAIN
REMARK 500 2 ARG A 8 0.32 SIDE CHAIN
REMARK 500 2 ARG A 18 0.21 SIDE CHAIN
REMARK 500 2 ARG A 21 0.27 SIDE CHAIN
REMARK 500 3 ARG A 5 0.30 SIDE CHAIN
REMARK 500 3 ARG A 8 0.27 SIDE CHAIN
REMARK 500 3 ARG A 18 0.26 SIDE CHAIN
REMARK 500 3 ARG A 21 0.27 SIDE CHAIN
REMARK 500 4 ARG A 5 0.31 SIDE CHAIN
REMARK 500 4 ARG A 8 0.20 SIDE CHAIN
REMARK 500 4 ARG A 18 0.15 SIDE CHAIN
REMARK 500 4 ARG A 21 0.31 SIDE CHAIN
REMARK 500 5 ARG A 5 0.31 SIDE CHAIN
REMARK 500 5 ARG A 8 0.31 SIDE CHAIN
REMARK 500 5 ARG A 18 0.29 SIDE CHAIN
REMARK 500 5 ARG A 21 0.32 SIDE CHAIN
REMARK 500 6 ARG A 5 0.27 SIDE CHAIN
REMARK 500 6 ARG A 8 0.27 SIDE CHAIN
REMARK 500 6 ARG A 18 0.31 SIDE CHAIN
REMARK 500 6 ARG A 21 0.31 SIDE CHAIN
REMARK 500 7 ARG A 5 0.32 SIDE CHAIN
REMARK 500 7 ARG A 8 0.29 SIDE CHAIN
REMARK 500 7 ARG A 18 0.26 SIDE CHAIN
REMARK 500 7 ARG A 21 0.31 SIDE CHAIN
REMARK 500 8 ARG A 5 0.32 SIDE CHAIN
REMARK 500 8 ARG A 8 0.30 SIDE CHAIN
REMARK 500 8 ARG A 18 0.27 SIDE CHAIN
REMARK 500 8 ARG A 21 0.31 SIDE CHAIN
REMARK 500 9 ARG A 5 0.27 SIDE CHAIN
REMARK 500 9 ARG A 8 0.31 SIDE CHAIN
REMARK 500 9 ARG A 18 0.29 SIDE CHAIN
REMARK 500 9 ARG A 21 0.32 SIDE CHAIN
REMARK 500 10 ARG A 5 0.32 SIDE CHAIN
REMARK 500 10 ARG A 8 0.32 SIDE CHAIN
REMARK 500 10 ARG A 18 0.30 SIDE CHAIN
REMARK 500 10 ARG A 21 0.31 SIDE CHAIN
REMARK 500 11 ARG A 5 0.24 SIDE CHAIN
REMARK 500 11 ARG A 8 0.32 SIDE CHAIN
REMARK 500 11 ARG A 18 0.20 SIDE CHAIN
REMARK 500 11 ARG A 21 0.32 SIDE CHAIN
REMARK 500 12 ARG A 5 0.26 SIDE CHAIN
REMARK 500 12 ARG A 8 0.30 SIDE CHAIN
REMARK 500 12 ARG A 18 0.31 SIDE CHAIN
REMARK 500 12 ARG A 21 0.27 SIDE CHAIN
REMARK 500 13 ARG A 5 0.29 SIDE CHAIN
REMARK 500 13 ARG A 8 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 80 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1AG7 A 1 34 UNP P15472 CXGS_CONGE 1 34
SEQADV 1AG7 HYP A 10 UNP P15472 PRO 10 MODIFIED RESIDUE
SEQADV 1AG7 HYP A 11 UNP P15472 PRO 11 MODIFIED RESIDUE
SEQADV 1AG7 CGU A 32 UNP P15472 GLU 32 MODIFIED RESIDUE
SEQRES 1 A 34 ALA CYS SER GLY ARG GLY SER ARG CYS HYP HYP GLN CYS
SEQRES 2 A 34 CYS MET GLY LEU ARG CYS GLY ARG GLY ASN PRO GLN LYS
SEQRES 3 A 34 CYS ILE GLY ALA HIS CGU ASP VAL
MODRES 1AG7 HYP A 10 PRO 4-HYDROXYPROLINE
MODRES 1AG7 HYP A 11 PRO 4-HYDROXYPROLINE
MODRES 1AG7 CGU A 32 GLU GAMMA-CARBOXY-GLUTAMIC ACID
HET HYP A 10 15
HET HYP A 11 15
HET CGU A 32 15
HETNAM HYP 4-HYDROXYPROLINE
HETNAM CGU GAMMA-CARBOXY-GLUTAMIC ACID
HETSYN HYP HYDROXYPROLINE
FORMUL 1 HYP 2(C5 H9 N O3)
FORMUL 1 CGU C6 H9 N O6
SHEET 1 A 2 LEU A 17 GLY A 20 0
SHEET 2 A 2 LYS A 26 GLY A 29 -1 N ILE A 28 O ARG A 18
SSBOND 1 CYS A 2 CYS A 14 1555 1555 2.02
SSBOND 2 CYS A 9 CYS A 19 1555 1555 2.02
SSBOND 3 CYS A 13 CYS A 27 1555 1555 2.02
LINK C CYS A 9 N HYP A 10 1555 1555 1.32
LINK C HYP A 10 N HYP A 11 1555 1555 1.32
LINK C HYP A 11 N GLN A 12 1555 1555 1.31
LINK C HIS A 31 N CGU A 32 1555 1555 1.31
LINK C CGU A 32 N ASP A 33 1555 1555 1.30
CISPEP 1 CYS A 9 HYP A 10 1 -10.29
CISPEP 2 HYP A 10 HYP A 11 1 1.41
CISPEP 3 ASN A 23 PRO A 24 1 -5.61
CISPEP 4 CYS A 9 HYP A 10 2 -9.79
CISPEP 5 HYP A 10 HYP A 11 2 -8.69
CISPEP 6 ASN A 23 PRO A 24 2 -16.34
CISPEP 7 CYS A 9 HYP A 10 3 -12.32
CISPEP 8 HYP A 10 HYP A 11 3 -2.34
CISPEP 9 ASN A 23 PRO A 24 3 -1.23
CISPEP 10 CYS A 9 HYP A 10 4 -7.91
CISPEP 11 HYP A 10 HYP A 11 4 2.12
CISPEP 12 ASN A 23 PRO A 24 4 -1.15
CISPEP 13 CYS A 9 HYP A 10 5 -11.71
CISPEP 14 HYP A 10 HYP A 11 5 -0.05
CISPEP 15 ASN A 23 PRO A 24 5 -6.35
CISPEP 16 CYS A 9 HYP A 10 6 -9.98
CISPEP 17 HYP A 10 HYP A 11 6 -6.67
CISPEP 18 ASN A 23 PRO A 24 6 -3.07
CISPEP 19 CYS A 9 HYP A 10 7 -1.04
CISPEP 20 HYP A 10 HYP A 11 7 5.22
CISPEP 21 ASN A 23 PRO A 24 7 -8.47
CISPEP 22 CYS A 9 HYP A 10 8 -12.06
CISPEP 23 HYP A 10 HYP A 11 8 0.98
CISPEP 24 ASN A 23 PRO A 24 8 -4.83
CISPEP 25 CYS A 9 HYP A 10 9 -9.69
CISPEP 26 HYP A 10 HYP A 11 9 -1.46
CISPEP 27 ASN A 23 PRO A 24 9 -7.65
CISPEP 28 CYS A 9 HYP A 10 10 -10.40
CISPEP 29 HYP A 10 HYP A 11 10 -2.93
CISPEP 30 ASN A 23 PRO A 24 10 -0.28
CISPEP 31 CYS A 9 HYP A 10 11 -12.20
CISPEP 32 HYP A 10 HYP A 11 11 -8.35
CISPEP 33 ASN A 23 PRO A 24 11 -6.01
CISPEP 34 CYS A 9 HYP A 10 12 -9.82
CISPEP 35 HYP A 10 HYP A 11 12 -2.82
CISPEP 36 ASN A 23 PRO A 24 12 -7.51
CISPEP 37 CYS A 9 HYP A 10 13 -1.85
CISPEP 38 HYP A 10 HYP A 11 13 13.56
CISPEP 39 ASN A 23 PRO A 24 13 -2.25
CISPEP 40 CYS A 9 HYP A 10 14 -8.97
CISPEP 41 HYP A 10 HYP A 11 14 -5.80
CISPEP 42 ASN A 23 PRO A 24 14 -18.73
CISPEP 43 CYS A 9 HYP A 10 15 -11.64
CISPEP 44 HYP A 10 HYP A 11 15 -3.30
CISPEP 45 ASN A 23 PRO A 24 15 -5.59
CISPEP 46 CYS A 9 HYP A 10 16 -1.98
CISPEP 47 HYP A 10 HYP A 11 16 7.36
CISPEP 48 ASN A 23 PRO A 24 16 -3.88
CISPEP 49 CYS A 9 HYP A 10 17 -10.96
CISPEP 50 HYP A 10 HYP A 11 17 -4.51
CISPEP 51 ASN A 23 PRO A 24 17 -5.21
CISPEP 52 CYS A 9 HYP A 10 18 -6.57
CISPEP 53 HYP A 10 HYP A 11 18 -0.90
CISPEP 54 ASN A 23 PRO A 24 18 -7.17
CISPEP 55 CYS A 9 HYP A 10 19 -3.79
CISPEP 56 HYP A 10 HYP A 11 19 8.87
CISPEP 57 ASN A 23 PRO A 24 19 -3.43
CISPEP 58 CYS A 9 HYP A 10 20 -13.80
CISPEP 59 HYP A 10 HYP A 11 20 -5.19
CISPEP 60 ASN A 23 PRO A 24 20 -5.29
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 - 16 20 Bytes