Header list of 1jwd.pdb file
Complete list - b 23 2 Bytes
HEADER METAL BINDING PROTEIN 04-SEP-01 1JWD
TITLE CA2+-INDUCED STRUCTURAL CHANGES IN CALCYCLIN: HIGH-RESOLUTION SOLUTION
TITLE 2 STRUCTURE OF CA2+-BOUND CALCYCLIN.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALCYCLIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: LUNG 10 KDA PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: RABBIT;
SOURCE 4 ORGANISM_TAXID: 9986;
SOURCE 5 ORGAN: LUNG;
SOURCE 6 GENE: R-S100A6;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: DE3;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET1120
KEYWDS CA(2+)-BINDING PROTEIN, S100 PROTEIN, EF-HAND, S100A6, METAL BINDING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 22
AUTHOR L.MALER,M.SASTRY,W.J.CHAZIN
REVDAT 4 23-FEB-22 1JWD 1 REMARK
REVDAT 3 24-FEB-09 1JWD 1 VERSN
REVDAT 2 01-APR-03 1JWD 1 JRNL
REVDAT 1 27-MAR-02 1JWD 0
JRNL AUTH L.MALER,M.SASTRY,W.J.CHAZIN
JRNL TITL A STRUCTURAL BASIS FOR S100 PROTEIN SPECIFICITY DERIVED FROM
JRNL TITL 2 COMPARATIVE ANALYSIS OF APO AND CA(2+)-CALCYCLIN
JRNL REF J.MOL.BIOL. V. 317 279 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 11902843
JRNL DOI 10.1006/JMBI.2002.5421
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.MALER,B.C.M.POTTS,W.J.CHAZIN
REMARK 1 TITL HIGH RESOLUTION SOLUTION STRUCTURE OF APO CALCYCLIN AND
REMARK 1 TITL 2 STRUCTURAL VARIATIONS IN THE S100 FAMILY OF CALCIUM-BINDING
REMARK 1 TITL 3 PROTEINS.
REMARK 1 REF J.BIOMOL.NMR V. 13 233 1999
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1008315517955
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.SASTRY,R.R.KETCHEM,O.CRESCENZI,C.WEBER,M.J.LUBIENSKI,
REMARK 1 AUTH 2 H.HIDAKA,W.J.CHAZIN
REMARK 1 TITL THE THREE-DIMENISONAL STRUCTURE OF CA(2+)-BOUND CALCYCLIN:
REMARK 1 TITL 2 IMPLICATIONS FOR CA(2+)-SIGNAL TRANSDUCTION BY S100
REMARK 1 TITL 3 PROTEINS.
REMARK 1 REF STRUCTURE V. 6 223 1998
REMARK 1 REFN ISSN 0969-2126
REMARK 1 DOI 10.1016/S0969-2126(98)00023-9
REMARK 1 REFERENCE 3
REMARK 1 AUTH B.C.POTTS,J.SMITH,M.AKKE,T.J.MACKE,K.OKAZAKI,H.HIDAKA,
REMARK 1 AUTH 2 D.A.CHASE,W.J.CHAZIN
REMARK 1 TITL THE STRUCTURE OF CALCYCLIN REVEALS A NOVEL HOMODIMERIC FOLD
REMARK 1 TITL 2 FOR S100 CA(2+)-BINDING PROTEINS.
REMARK 1 REF NAT.STRUCT.BIOL. V. 2 790 1995
REMARK 1 REFN ISSN 1072-8368
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 97, AMBER 4.1
REMARK 3 AUTHORS : MSI (FELIX), PEARLMANN, CASE, CALDWELL, ROSS,
REMARK 3 CHEATHAM III, FERGUSON, SEIBEL, SINGH, WEINER &
REMARK 3 KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE CALCULATIONS WERE CARRIED OUT USING
REMARK 3 A TOTAL OF 3104 DISTANCE AND 294 TORSION ANGLE CONSTRAINTS.
REMARK 3 STARTING STRUCTURES WERE GENERATED AS MONOMERS (ONE CHAIN) WITH
REMARK 3 NO INTERSUBUNIT CONSTRAINTS USING DISTANCE GEOMETRY FOLLOWED BY
REMARK 3 RESTRAINED MOLECULAR DYNAMICS (RMD). THE DIMER STRUCTURES WERE
REMARK 3 GENERATED BY RMD DOCKING DRIVEN BY THE INTERSUBUNIT NOES USING
REMARK 3 TWO ARBITRARILY SELECTED STARTING SUBUNIT STRUCTURES. EACH DIMER
REMARK 3 WAS FURTHER REFINED BY RMD WITH ALL CONSTRAINTS.
REMARK 4
REMARK 4 1JWD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000014261.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 30 MM CACL2
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM CALCYCLIN, 50 MM TRIS
REMARK 210 BUFFER, 30 MM CACL2; 2 MM 15N,
REMARK 210 13C-ENRICHED CALCYCLIN, 50 MM
REMARK 210 TRIS-BUFFER, 0.05% NAN3, 30 MM
REMARK 210 CACL2; 1:1 15N,13C-ENRICHED:
REMARK 210 UNLABLED CALCYCLIN, 50 MM TRIS-
REMARK 210 BUFFER, 0.05% NAN3, 30 MM CACL2;
REMARK 210 15N-ENRICHED CALCYCLIN, 50 MM
REMARK 210 TRIS-BUFFER, 0.05% NAN3, 30 MM
REMARK 210 CACL2; 10% 13C-ENRICHED
REMARK 210 CALCYCLIN, 50 MM TRIS-BUFFER,
REMARK 210 0.05% NAN3, 30 MM CACL2
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; 3D_HACAHB; 3D_
REMARK 210 13C-FILTER,13C-EDITED_NOESY; 2D_
REMARK 210 13C_HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; DRX; AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA 2.8, FINDFAM 1.0
REMARK 210 METHOD USED : DISTANCE GEOMETRY, RESTRAINED
REMARK 210 MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 22
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE PROGRAM FINDFAM WAS USED TO
REMARK 210 ESTABLISH THAT THE NUMBER OF
REMARK 210 STRUCTURES REQUIRED TO
REMARK 210 ACCURATELY REPRESENT THE
REMARK 210 ENSEMBLE WAS LESS THAN 22 (THE
REMARK 210 NUMBER SELECTED TO REPRESENT
REMARK 210 PREVIOUS S100A6 ENSEMBLES).
REMARK 210 STRUCTURES WERE ORDERED BY
REMARK 210 LOWEST RESTRAINT VIOLATIONS,
REMARK 210 THEN ACCEPTED IF TOTAL MOLECULAR
REMARK 210 ENERGY AND EACH CONTRIBUTING
REMARK 210 TERM WAS WITHIN TWO STANDARD
REMARK 210 DEVIATIONS OF THE MEAN. THE 22
REMARK 210 STRUCTURES WITH LEAST RESTRAINT
REMARK 210 VIOLATIONS (ENERGY PENALTY AND
REMARK 210 MAGNITUDE OF LARGEST VIOLATION)
REMARK 210 ALL MET THESE CRITERIA.
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: DIMER CONSTRAINTS WERE OBTAINED FROM
REMARK 210 THE 3D_13C-FILTER,13C-EDITED EXPERIMENT
REMARK 210 IN COMBINATION WITH 3D_13C-SEPARATED_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: 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 HIS A 27 38.18 -90.76
REMARK 500 1 THR A 43 74.46 -64.49
REMARK 500 1 GLN A 49 4.15 -68.02
REMARK 500 1 LYS A 64 22.11 -148.44
REMARK 500 1 ASP A 65 -43.17 63.36
REMARK 500 1 TYR A 84 38.53 -70.82
REMARK 500 1 ALA B 2 31.12 -159.21
REMARK 500 1 LYS B 22 -39.54 -39.21
REMARK 500 1 GLU B 23 39.75 -141.31
REMARK 500 1 ASP B 25 47.57 -80.34
REMARK 500 1 LYS B 26 -107.98 39.35
REMARK 500 1 THR B 43 79.01 -64.58
REMARK 500 1 SER B 46 69.97 -69.93
REMARK 500 1 ASP B 65 -58.20 58.08
REMARK 500 2 ALA A 2 -61.95 67.63
REMARK 500 2 HIS A 27 37.08 -77.92
REMARK 500 2 LYS A 64 62.22 -161.41
REMARK 500 2 ASP A 65 -72.90 26.26
REMARK 500 2 ASN A 85 -54.58 68.94
REMARK 500 2 ALA B 2 6.22 59.78
REMARK 500 2 HIS B 27 34.14 -75.81
REMARK 500 2 THR B 43 179.51 68.56
REMARK 500 2 ILE B 44 -58.80 -141.98
REMARK 500 2 LYS B 64 -65.34 -105.11
REMARK 500 2 ASP B 65 -84.75 -178.05
REMARK 500 3 HIS A 27 48.91 -80.72
REMARK 500 3 SER A 46 72.37 -67.44
REMARK 500 3 LYS A 64 91.93 -165.43
REMARK 500 3 ALA B 2 -28.11 73.16
REMARK 500 3 THR B 43 74.60 -67.22
REMARK 500 3 SER B 46 70.35 -68.67
REMARK 500 3 ASN B 63 -67.92 -27.01
REMARK 500 3 LYS B 64 48.56 -155.20
REMARK 500 3 ASP B 65 -75.79 48.33
REMARK 500 4 ALA A 2 -56.29 70.30
REMARK 500 4 HIS A 27 33.29 -79.60
REMARK 500 4 LYS A 64 59.13 -147.16
REMARK 500 4 ASP A 65 82.93 13.61
REMARK 500 4 GLN A 66 -15.43 104.51
REMARK 500 4 ASP B 25 -113.80 -166.51
REMARK 500 4 LYS B 26 156.41 69.76
REMARK 500 4 HIS B 27 33.45 -96.40
REMARK 500 4 SER B 46 19.53 58.00
REMARK 500 4 ASP B 65 -65.27 56.48
REMARK 500 4 ASN B 85 -61.54 70.49
REMARK 500 5 ALA A 2 37.04 -78.23
REMARK 500 5 HIS A 27 48.78 -78.18
REMARK 500 5 SER A 46 62.71 -67.77
REMARK 500 5 ARG A 62 -39.48 -34.16
REMARK 500 5 LYS A 64 32.97 -152.71
REMARK 500
REMARK 500 THIS ENTRY HAS 280 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 TYR A 19 0.07 SIDE CHAIN
REMARK 500 1 ARG A 62 0.08 SIDE CHAIN
REMARK 500 1 TYR A 73 0.06 SIDE CHAIN
REMARK 500 1 HIS B 17 0.08 SIDE CHAIN
REMARK 500 1 TYR B 19 0.17 SIDE CHAIN
REMARK 500 1 ARG B 62 0.10 SIDE CHAIN
REMARK 500 1 TYR B 73 0.07 SIDE CHAIN
REMARK 500 2 TYR A 73 0.09 SIDE CHAIN
REMARK 500 2 TYR A 84 0.09 SIDE CHAIN
REMARK 500 2 TYR B 19 0.13 SIDE CHAIN
REMARK 500 2 PHE B 70 0.08 SIDE CHAIN
REMARK 500 3 TYR A 19 0.11 SIDE CHAIN
REMARK 500 3 TYR B 19 0.13 SIDE CHAIN
REMARK 500 3 TYR B 73 0.08 SIDE CHAIN
REMARK 500 4 TYR A 19 0.12 SIDE CHAIN
REMARK 500 4 TYR A 73 0.08 SIDE CHAIN
REMARK 500 5 TYR A 19 0.08 SIDE CHAIN
REMARK 500 5 ARG A 62 0.13 SIDE CHAIN
REMARK 500 5 PHE A 70 0.07 SIDE CHAIN
REMARK 500 5 TYR A 73 0.07 SIDE CHAIN
REMARK 500 5 TYR B 19 0.13 SIDE CHAIN
REMARK 500 5 ARG B 62 0.12 SIDE CHAIN
REMARK 500 6 TYR A 19 0.16 SIDE CHAIN
REMARK 500 6 TYR A 73 0.09 SIDE CHAIN
REMARK 500 6 TYR B 19 0.07 SIDE CHAIN
REMARK 500 6 TYR B 73 0.07 SIDE CHAIN
REMARK 500 6 TYR B 84 0.06 SIDE CHAIN
REMARK 500 7 TYR A 19 0.07 SIDE CHAIN
REMARK 500 7 TYR B 19 0.12 SIDE CHAIN
REMARK 500 8 TYR A 19 0.09 SIDE CHAIN
REMARK 500 8 TYR A 73 0.07 SIDE CHAIN
REMARK 500 8 TYR B 19 0.14 SIDE CHAIN
REMARK 500 8 TYR B 73 0.08 SIDE CHAIN
REMARK 500 9 TYR A 19 0.10 SIDE CHAIN
REMARK 500 9 TYR A 73 0.08 SIDE CHAIN
REMARK 500 9 TYR B 19 0.10 SIDE CHAIN
REMARK 500 9 ARG B 62 0.10 SIDE CHAIN
REMARK 500 9 TYR B 73 0.07 SIDE CHAIN
REMARK 500 10 TYR A 19 0.14 SIDE CHAIN
REMARK 500 10 TYR A 73 0.09 SIDE CHAIN
REMARK 500 10 TYR B 19 0.15 SIDE CHAIN
REMARK 500 10 TYR B 73 0.07 SIDE CHAIN
REMARK 500 11 TYR A 19 0.11 SIDE CHAIN
REMARK 500 11 TYR A 73 0.07 SIDE CHAIN
REMARK 500 11 TYR B 19 0.11 SIDE CHAIN
REMARK 500 12 TYR A 19 0.16 SIDE CHAIN
REMARK 500 13 TYR A 19 0.10 SIDE CHAIN
REMARK 500 13 TYR A 73 0.07 SIDE CHAIN
REMARK 500 13 TYR B 19 0.14 SIDE CHAIN
REMARK 500 13 TYR B 73 0.08 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 78 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A03 RELATED DB: PDB
REMARK 900 LOW-RESOLUTION STRUCTURE OF CA2+-BOUND CALCYCLIN
REMARK 900 RELATED ID: 2CNP RELATED DB: PDB
REMARK 900 HIGH-RESOLUTION STRUCTURE OF APO CALCYCLIN
REMARK 900 RELATED ID: 1CNP RELATED DB: PDB
REMARK 900 LOW-RESOLUTION SOLUTION STRUCTURE OF APO CALCYCLIN
DBREF 1JWD A 1 90 UNP P30801 S10A6_RABIT 1 90
DBREF 1JWD B 1 90 UNP P30801 S10A6_RABIT 1 90
SEQRES 1 A 90 MET ALA SER PRO LEU ASP GLN ALA ILE GLY LEU LEU ILE
SEQRES 2 A 90 GLY ILE PHE HIS LYS TYR SER GLY LYS GLU GLY ASP LYS
SEQRES 3 A 90 HIS THR LEU SER LYS LYS GLU LEU LYS GLU LEU ILE GLN
SEQRES 4 A 90 LYS GLU LEU THR ILE GLY SER LYS LEU GLN ASP ALA GLU
SEQRES 5 A 90 ILE VAL LYS LEU MET ASP ASP LEU ASP ARG ASN LYS ASP
SEQRES 6 A 90 GLN GLU VAL ASN PHE GLN GLU TYR ILE THR PHE LEU GLY
SEQRES 7 A 90 ALA LEU ALA MET ILE TYR ASN GLU ALA LEU LYS GLY
SEQRES 1 B 90 MET ALA SER PRO LEU ASP GLN ALA ILE GLY LEU LEU ILE
SEQRES 2 B 90 GLY ILE PHE HIS LYS TYR SER GLY LYS GLU GLY ASP LYS
SEQRES 3 B 90 HIS THR LEU SER LYS LYS GLU LEU LYS GLU LEU ILE GLN
SEQRES 4 B 90 LYS GLU LEU THR ILE GLY SER LYS LEU GLN ASP ALA GLU
SEQRES 5 B 90 ILE VAL LYS LEU MET ASP ASP LEU ASP ARG ASN LYS ASP
SEQRES 6 B 90 GLN GLU VAL ASN PHE GLN GLU TYR ILE THR PHE LEU GLY
SEQRES 7 B 90 ALA LEU ALA MET ILE TYR ASN GLU ALA LEU LYS GLY
HELIX 1 1 ALA A 2 GLY A 24 1 23
HELIX 2 2 LYS A 31 LEU A 42 1 12
HELIX 3 3 SER A 46 LEU A 48 5 3
HELIX 4 4 GLN A 49 ARG A 62 1 14
HELIX 5 5 PHE A 70 TYR A 84 1 15
HELIX 6 6 TYR A 84 GLY A 90 1 7
HELIX 7 7 ALA B 2 LYS B 22 1 21
HELIX 8 8 LYS B 31 LEU B 42 1 12
HELIX 9 9 SER B 46 LEU B 48 5 3
HELIX 10 10 GLN B 49 ASN B 63 1 15
HELIX 11 11 PHE B 70 TYR B 84 1 15
HELIX 12 12 TYR B 84 GLY B 90 1 7
SHEET 1 A 2 THR A 28 SER A 30 0
SHEET 2 A 2 GLU A 67 ASN A 69 -1 O VAL A 68 N LEU A 29
SHEET 1 B 2 THR B 28 SER B 30 0
SHEET 2 B 2 GLU B 67 ASN B 69 -1 O VAL B 68 N LEU B 29
CRYST1 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