Header list of 1l6e.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSFERASE 08-MAR-02 1L6E
TITLE SOLUTION STRUCTURE OF THE DOCKING AND DIMERIZATION DOMAIN OF PROTEIN
TITLE 2 KINASE A II-ALPHA (RIIALPHA D/D). ALTERNATIVELY CALLED THE N-TERMINAL
TITLE 3 DIMERIZATION DOMAIN OF THE REGULATORY SUBUNIT OF PROTEIN KINASE A.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE TYPE II-ALPHA REGULATORY
COMPND 3 CHAIN;
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: N-TERMINAL DOCKING AND DIMERIZATION DOMAIN;
COMPND 6 EC: 2.7.1.37;
COMPND 7 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 GENE: RIIA(1-44);
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-16B
KEYWDS FOUR-HELIX BUNDLE, HELIX-LOOP-HELIX, REGULATORY SUBUNIT,
KEYWDS 2 DIMERIZATION, DOCKING, ANCHORING, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 24
AUTHOR D.MORIKIS,M.ROY,M.G.NEWLON,J.D.SCOTT,P.A.JENNINGS
REVDAT 5 23-FEB-22 1L6E 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1L6E 1 VERSN
REVDAT 3 01-APR-03 1L6E 1 JRNL
REVDAT 2 28-AUG-02 1L6E 1 JRNL
REVDAT 1 03-APR-02 1L6E 0
JRNL AUTH D.MORIKIS,M.ROY,M.G.NEWLON,J.D.SCOTT,P.A.JENNINGS
JRNL TITL ELECTROSTATIC PROPERTIES OF THE STRUCTURE OF THE DOCKING AND
JRNL TITL 2 DIMERIZATION DOMAIN OF PROTEIN KINASE A IIALPHA
JRNL REF EUR.J.BIOCHEM. V. 269 2040 2002
JRNL REFN ISSN 0014-2956
JRNL PMID 11985580
JRNL DOI 10.1046/J.1432-1033.2002.02852.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.G.NEWLON,M.ROY,D.MORIKIS,Z.E.HAUSKEN,V.COGHLAN,J.D.SCOTT,
REMARK 1 AUTH 2 P.A.JENNINGS
REMARK 1 TITL THE MOLECULAR BASIS FOR PROTEIN KINASE A ANCHORING REVEALED
REMARK 1 TITL 2 BY SOLUTION NMR.
REMARK 1 REF NAT.STRUCT.BIOL. V. 6 222 1999
REMARK 1 REFN ISSN 1072-8368
REMARK 1 DOI 10.1038/6663
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.G.NEWLON,M.ROY,Z.E.HAUSKEN,J.D.SCOTT,P.A.JENNINGS
REMARK 1 TITL THE A-KINASE ANCHORING DOMAIN OF TYPE II-ALPHA
REMARK 1 TITL 2 CAMP-DEPENDENT PROTEIN KINASE IS HIGHLY HELICAL.
REMARK 1 REF J.BIOL.CHEM. V. 272 23637 1997
REMARK 1 REFN ISSN 0021-9258
REMARK 1 DOI 10.1074/JBC.272.38.23637
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851, X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER, A.T. (X-PLOR), BRUNGER, A.T. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 FILTERED NOESY SPECTRUM ON A 50% UNLABELED-50% 13C-15N-LABELED
REMARK 3 SAMPLE WAS
REMARK 3 USED TO OBTAIN INTER-MOLECULAR NOE CONTACTS OF THE HOMODIMER.
REMARK 3 OTHER NOES WERE
REMARK 3 CLASSIFIED AS INTRA-MOLECULAR AND AMBIGUOUS.
REMARK 4
REMARK 4 1L6E COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015682.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298; 298
REMARK 210 PH : 4; 4; 4; 4
REMARK 210 IONIC STRENGTH : 0.012; 0.012; 0.012; 0.012
REMARK 210 PRESSURE : 1 ATM; 1 ATM; 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 2MM DIMER PROTEIN IN 20 MM
REMARK 210 SODIUM PHOSPHATE BUFFER, 90%H2O-
REMARK 210 10% D2O, AT PH 4 AND TEMPERATURE
REMARK 210 298K; 1MM DIMER PROTEIN 15N IN
REMARK 210 20 MM SODIUM PHOSPHATE BUFFER,
REMARK 210 90%H2O-10% D2O, AT PH 4 AND
REMARK 210 TEMPERATURE 298K; 1MM DIMER
REMARK 210 PROTEIN 13C-15N IN 20 MM SODIUM
REMARK 210 PHOSPHATE BUFFER, 90%H2O-10% D2O,
REMARK 210 AT PH 4 AND TEMPERATURE 298K;
REMARK 210 MIXTURE OF 2MM UNLABELED AND 2
REMARK 210 MM 13C-15N LABELED SAMPLE
REMARK 210 UNFOLDED IN 5 M GUANADINE
REMARK 210 HYDROCHLORIDE AND REFOLDED IN 20
REMARK 210 MM SODIUM PHOSPHATE BUFFER, 90%
REMARK 210 H2O-10% D2O, AT PH 4 AND
REMARK 210 TEMPERATURE 298K
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : HYBRID DISTANCE GEOMETRY
REMARK 210 -DYNAMICAL SIMULATED ANNEALING
REMARK 210 AND REFINEMENT PROTOCOL FOR
REMARK 210 MONOMER STRUCTURE DETERMINATION,
REMARK 210 WITH 457 NOE-DERIVED DISTANCE
REMARK 210 RESTRAINTS (185 INTRA-RESIDUE, I-
REMARK 210 J=0; 136 SEQUENTIAL, |I-J|=1; 95
REMARK 210 MEDIUM RANGE, 1<|I-J|<5; 41 LONG
REMARK 210 RANGE, |I-J|>4), 19 DISTANCE
REMARK 210 RESTRAINTS REPRESENTING HYDROGEN
REMARK 210 BONDS (ENTERED AS 2 DISTANCES
REMARK 210 EACH), 25 PHI- AND 5 CHI1-
REMARK 210 TORSION ANGLE RESTRAINTS.
REMARK 210 MOLECULAR DYNAMICAL SIMULATED
REMARK 210 ANNEALING PROTOCOL FOR DIMER
REMARK 210 STRUCTURE DETERMINATION, USING
REMARK 210 505 NOE-DERIVED DISTANCE
REMARK 210 RESTRAINTS (185 INTRA-RESIDUE, I-
REMARK 210 J=0; 136 SEQUENTIAL, |I-J|=1; 95
REMARK 210 MEDIUM RANGE, 1<|I-J|<5; 25 LONG
REMARK 210 RANGE, |I-J|>4; 38 INTER-
REMARK 210 MOLECULAR; 26 AMBIGUOUS), 19
REMARK 210 DISTANCE RESTRAINTS REPRESENTING
REMARK 210 HYDROGEN BONDS (ENTERED AS 2
REMARK 210 DISTANCES EACH), 25 PHI- AND 5
REMARK 210 CHI1-TORSION ANGLE RESTRAINTS.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 49
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24
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:
REMARK 210 THIS STRUCTURE WAS DETERMINED USING STANDARD HOMONUCLEAR,
REMARK 210 HETERONUCLEAR, AND TRIPLE RESONANCE SPECTROSCOPY,
REMARK 210 AND 3D 13C-EDITED(W2)-12C-FILTERED(W1)/13C-FILTERED(W3) NOESY.
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: 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 O LEU B 30 H ALA B 34 1.55
REMARK 500 O LEU A 30 H ALA A 34 1.56
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 GLN A 6 48.65 -143.69
REMARK 500 1 THR A 12 -70.70 -59.06
REMARK 500 1 GLU A 21 -64.32 -90.86
REMARK 500 1 GLN A 25 20.58 -159.20
REMARK 500 1 GLN A 26 89.42 0.59
REMARK 500 1 ARG A 45 -36.84 -32.93
REMARK 500 1 GLN B 6 49.73 -143.28
REMARK 500 1 THR B 12 -70.63 -59.04
REMARK 500 1 GLU B 21 -64.80 -90.84
REMARK 500 1 GLN B 25 19.68 -158.74
REMARK 500 1 GLN B 26 89.30 1.72
REMARK 500 1 ARG B 45 -36.60 -32.81
REMARK 500 2 LEU A 11 -73.97 -58.66
REMARK 500 2 VAL A 31 -54.05 -27.98
REMARK 500 2 ALA A 44 -73.40 -124.00
REMARK 500 2 ARG A 45 84.23 -15.80
REMARK 500 2 LEU B 11 -73.63 -58.69
REMARK 500 2 VAL B 31 -54.24 -27.91
REMARK 500 2 ALA B 44 -73.44 -123.92
REMARK 500 2 ARG B 45 84.33 -15.81
REMARK 500 3 MET A 2 54.16 -110.84
REMARK 500 3 GLU A 13 -78.44 -53.62
REMARK 500 3 GLN A 26 70.24 37.82
REMARK 500 3 VAL A 31 -66.61 -22.73
REMARK 500 3 ALA A 44 -70.87 -51.41
REMARK 500 3 ARG A 45 133.89 -22.14
REMARK 500 3 MET B 2 54.39 -110.40
REMARK 500 3 GLU B 13 -78.38 -52.48
REMARK 500 3 GLN B 26 70.08 37.73
REMARK 500 3 VAL B 31 -66.78 -22.99
REMARK 500 3 ALA B 44 -70.87 -51.40
REMARK 500 3 ARG B 45 134.17 -22.24
REMARK 500 4 GLN A 26 72.67 36.47
REMARK 500 4 ASP A 29 119.65 -160.62
REMARK 500 4 ALA A 44 -70.48 -56.14
REMARK 500 4 ARG A 45 -92.09 -28.02
REMARK 500 4 GLN B 26 72.89 36.60
REMARK 500 4 ASP B 29 119.54 -160.84
REMARK 500 4 ARG B 45 -91.74 -30.54
REMARK 500 5 MET A 2 -56.11 68.97
REMARK 500 5 HIS A 4 -89.97 -143.62
REMARK 500 5 THR A 12 -73.47 -55.19
REMARK 500 5 GLU A 21 -61.25 -94.03
REMARK 500 5 GLN A 25 20.68 -165.10
REMARK 500 5 GLN A 26 91.08 -3.35
REMARK 500 5 LEU A 30 -70.41 -90.62
REMARK 500 5 ARG A 45 -89.24 -20.83
REMARK 500 5 MET B 2 -56.23 68.82
REMARK 500 5 HIS B 4 -89.78 -143.36
REMARK 500 5 THR B 12 -73.53 -53.71
REMARK 500
REMARK 500 THIS ENTRY HAS 327 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 40 0.13 SIDE CHAIN
REMARK 500 1 ARG A 42 0.31 SIDE CHAIN
REMARK 500 1 ARG A 45 0.11 SIDE CHAIN
REMARK 500 1 ARG A 46 0.23 SIDE CHAIN
REMARK 500 1 ARG B 40 0.13 SIDE CHAIN
REMARK 500 1 ARG B 42 0.31 SIDE CHAIN
REMARK 500 1 ARG B 45 0.12 SIDE CHAIN
REMARK 500 1 ARG B 46 0.23 SIDE CHAIN
REMARK 500 2 ARG A 24 0.30 SIDE CHAIN
REMARK 500 2 ARG A 40 0.19 SIDE CHAIN
REMARK 500 2 ARG A 42 0.11 SIDE CHAIN
REMARK 500 2 ARG A 45 0.18 SIDE CHAIN
REMARK 500 2 ARG B 24 0.30 SIDE CHAIN
REMARK 500 2 ARG B 40 0.19 SIDE CHAIN
REMARK 500 2 ARG B 42 0.10 SIDE CHAIN
REMARK 500 2 ARG B 45 0.18 SIDE CHAIN
REMARK 500 3 ARG A 24 0.32 SIDE CHAIN
REMARK 500 3 ARG A 40 0.16 SIDE CHAIN
REMARK 500 3 ARG A 42 0.08 SIDE CHAIN
REMARK 500 3 ARG A 45 0.23 SIDE CHAIN
REMARK 500 3 ARG A 46 0.08 SIDE CHAIN
REMARK 500 3 ARG B 24 0.32 SIDE CHAIN
REMARK 500 3 ARG B 40 0.16 SIDE CHAIN
REMARK 500 3 ARG B 42 0.09 SIDE CHAIN
REMARK 500 3 ARG B 45 0.24 SIDE CHAIN
REMARK 500 3 ARG B 46 0.08 SIDE CHAIN
REMARK 500 4 ARG A 24 0.30 SIDE CHAIN
REMARK 500 4 ARG A 40 0.20 SIDE CHAIN
REMARK 500 4 ARG A 42 0.30 SIDE CHAIN
REMARK 500 4 ARG A 45 0.16 SIDE CHAIN
REMARK 500 4 ARG A 46 0.32 SIDE CHAIN
REMARK 500 4 ARG B 24 0.30 SIDE CHAIN
REMARK 500 4 ARG B 40 0.20 SIDE CHAIN
REMARK 500 4 ARG B 42 0.29 SIDE CHAIN
REMARK 500 4 ARG B 45 0.16 SIDE CHAIN
REMARK 500 4 ARG B 46 0.32 SIDE CHAIN
REMARK 500 5 ARG A 24 0.32 SIDE CHAIN
REMARK 500 5 ARG A 40 0.29 SIDE CHAIN
REMARK 500 5 ARG A 42 0.27 SIDE CHAIN
REMARK 500 5 ARG A 45 0.29 SIDE CHAIN
REMARK 500 5 ARG A 46 0.22 SIDE CHAIN
REMARK 500 5 ARG B 24 0.32 SIDE CHAIN
REMARK 500 5 ARG B 40 0.30 SIDE CHAIN
REMARK 500 5 ARG B 42 0.27 SIDE CHAIN
REMARK 500 5 ARG B 45 0.29 SIDE CHAIN
REMARK 500 5 ARG B 46 0.22 SIDE CHAIN
REMARK 500 6 ARG A 24 0.14 SIDE CHAIN
REMARK 500 6 ARG A 40 0.16 SIDE CHAIN
REMARK 500 6 ARG A 42 0.32 SIDE CHAIN
REMARK 500 6 ARG A 45 0.24 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 222 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1R2A RELATED DB: PDB
REMARK 900 1R2A CONTAINS THE SAME PROTEIN.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FIRST 3 RESIDUES ARE DIFFERENT DUE TO
REMARK 999 RECOMBINANT EXPRESSION AND PROTEOLYTIC
REMARK 999 CLEAVAGE.
DBREF 1L6E A 4 46 UNP P12367 KAP2_MOUSE 2 43
DBREF 1L6E B 4 46 UNP P12367 KAP2_MOUSE 2 43
SEQADV 1L6E HIS A 1 UNP P12367 SEE REMARK 999
SEQADV 1L6E MET A 2 UNP P12367 SEE REMARK 999
SEQADV 1L6E GLY A 3 UNP P12367 SEE REMARK 999
SEQADV 1L6E LEU A 23A UNP P12367 INSERTION
SEQADV 1L6E ARG A 24 UNP P12367 GLY 21 VARIANT
SEQADV 1L6E HIS B 1 UNP P12367 SEE REMARK 999
SEQADV 1L6E MET B 2 UNP P12367 SEE REMARK 999
SEQADV 1L6E GLY B 3 UNP P12367 SEE REMARK 999
SEQADV 1L6E LEU B 23B UNP P12367 INSERTION
SEQADV 1L6E ARG B 24 UNP P12367 GLY 21 VARIANT
SEQRES 1 A 46 HIS MET GLY HIS ILE GLN ILE PRO PRO GLY LEU THR GLU
SEQRES 2 A 46 LEU LEU GLN GLY TYR THR VAL GLU VAL LEU ARG GLN GLN
SEQRES 3 A 46 PRO PRO ASP LEU VAL ASP PHE ALA VAL GLU TYR PHE THR
SEQRES 4 A 46 ARG LEU ARG GLU ALA ARG ARG
SEQRES 1 B 46 HIS MET GLY HIS ILE GLN ILE PRO PRO GLY LEU THR GLU
SEQRES 2 B 46 LEU LEU GLN GLY TYR THR VAL GLU VAL LEU ARG GLN GLN
SEQRES 3 B 46 PRO PRO ASP LEU VAL ASP PHE ALA VAL GLU TYR PHE THR
SEQRES 4 B 46 ARG LEU ARG GLU ALA ARG ARG
HELIX 1 1 GLY A 10 GLN A 25 1 16
HELIX 2 2 ASP A 29 ARG A 42 1 14
HELIX 3 3 GLY B 10 GLN B 25 1 16
HELIX 4 4 ASP B 29 ARG B 42 1 14
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