Header list of 1s8k.pdb file
Complete list - 2 20 Bytes
HEADER TOXIN 02-FEB-04 1S8K
TITLE SOLUTION STRUCTURE OF BMKK4, A NOVEL POTASSIUM CHANNEL BLOCKER FROM
TITLE 2 SCORPION BUTHUS MARTENSII KARSCH, 25 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TOXIN BMKK4;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: KK4, TOXIN TXKS4, ALPHA-KTX 17.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MESOBUTHUS MARTENSII;
SOURCE 3 ORGANISM_COMMON: CHINESE SCORPION;
SOURCE 4 ORGANISM_TAXID: 34649
KEYWDS ALPHA/BETA SCAFFOLD, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR N.ZHANG,X.CHEN,M.LI,C.CAO,Y.WANG,G.HU,H.WU
REVDAT 3 02-MAR-22 1S8K 1 REMARK SEQADV SEQRES LINK
REVDAT 2 24-FEB-09 1S8K 1 VERSN
REVDAT 1 08-FEB-05 1S8K 0
JRNL AUTH N.ZHANG,X.CHEN,M.LI,C.CAO,Y.WANG,G.WU,G.HU,H.WU
JRNL TITL SOLUTION STRUCTURE OF BMKK4, THE FIRST MEMBER OF SUBFAMILY
JRNL TITL 2 ALPHA-KTX 17 OF SCORPION TOXINS
JRNL REF BIOCHEMISTRY V. 43 12469 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15449936
JRNL DOI 10.1021/BI0490643
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, AMBER 5.0
REMARK 3 AUTHORS : MIKE CARLISLE,DAN STEELE,MIKE MILLER (VNMR),
REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH,
REMARK 3 WEINER,KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 315 CONSTRAINTS, 282 ARE NOE-DERIVED DISTANCE CONSTRAINTS,16
REMARK 3 DIHEDRAL ANGLE CONSTRAINTS, 17 DISTANCE CONSTRAINTS FROM FOUR
REMARK 3 HYDROGEN BONDS AND THREE DISULFIDE BONDS.
REMARK 4
REMARK 4 1S8K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-FEB-04.
REMARK 100 THE DEPOSITION ID IS D_1000021502.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 303
REMARK 210 PH : 3.02; 3.66
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 3.0MM; 3.0MM
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY, 2D TOCSY, DQF-COSY; 2D
REMARK 210 TOCSY, 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1B, XEASY 1994, DYANA 1.5
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE 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 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 2 CYS A 25 CB - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 2 CYS A 25 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 3 ARG A 19 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 3 CYS A 25 CB - CA - C ANGL. DEV. = 7.6 DEGREES
REMARK 500 4 CYS A 25 CB - CA - C ANGL. DEV. = 7.6 DEGREES
REMARK 500 5 CYS A 25 CB - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 6 ARG A 19 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 7 ARG A 19 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 7 CYS A 25 CB - CA - C ANGL. DEV. = 8.8 DEGREES
REMARK 500 7 CYS A 25 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 8 ARG A 19 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 9 ARG A 19 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 9 CYS A 25 CB - CA - C ANGL. DEV. = 8.4 DEGREES
REMARK 500 9 CYS A 25 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 10 ARG A 19 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 10 CYS A 25 CB - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 11 ARG A 19 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 11 CYS A 25 CB - CA - C ANGL. DEV. = 7.4 DEGREES
REMARK 500 12 CYS A 25 CB - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 13 CYS A 25 CB - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 14 CYS A 25 CB - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 14 CYS A 25 CA - CB - SG ANGL. DEV. = 7.1 DEGREES
REMARK 500 16 ARG A 19 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 16 CYS A 25 CB - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 18 CYS A 25 CB - CA - C ANGL. DEV. = 7.8 DEGREES
REMARK 500 19 CYS A 25 CB - CA - C ANGL. DEV. = 8.4 DEGREES
REMARK 500 20 ARG A 19 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 20 CYS A 25 CB - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 23 CYS A 25 CB - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 24 ARG A 19 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 24 CYS A 25 CB - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 25 ARG A 19 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 25 CYS A 25 CB - CA - C ANGL. DEV. = 7.5 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 ARG A 8 -54.03 -29.14
REMARK 500 1 ASP A 18 -61.77 -92.41
REMARK 500 1 THR A 29 88.21 -153.26
REMARK 500 2 THR A 2 -117.43 -145.07
REMARK 500 2 ASP A 18 -61.36 -96.58
REMARK 500 2 THR A 29 54.08 -152.23
REMARK 500 3 ASP A 18 -61.96 -104.84
REMARK 500 4 THR A 2 139.60 81.77
REMARK 500 4 ASP A 18 -62.28 -93.84
REMARK 500 4 THR A 29 30.75 -154.61
REMARK 500 5 THR A 2 -116.32 -113.16
REMARK 500 5 LYS A 28 40.12 -81.71
REMARK 500 6 THR A 29 58.62 -153.27
REMARK 500 7 THR A 2 -118.70 -113.28
REMARK 500 7 ARG A 8 -51.31 -27.18
REMARK 500 8 THR A 29 45.83 -83.36
REMARK 500 9 THR A 2 -113.63 -103.21
REMARK 500 9 LYS A 28 48.19 -80.42
REMARK 500 10 THR A 2 -133.05 -110.49
REMARK 500 10 THR A 29 56.10 -150.04
REMARK 500 11 THR A 2 143.30 81.62
REMARK 500 12 THR A 2 -117.93 -148.44
REMARK 500 13 THR A 2 -114.28 -101.12
REMARK 500 14 THR A 2 -109.54 -143.92
REMARK 500 14 LYS A 28 36.59 -79.67
REMARK 500 14 THR A 29 47.67 -83.80
REMARK 500 15 ASP A 18 -62.90 -96.67
REMARK 500 15 THR A 29 -138.96 -148.18
REMARK 500 16 THR A 2 -116.63 -138.14
REMARK 500 16 THR A 29 74.29 -151.14
REMARK 500 17 THR A 2 -109.52 -89.46
REMARK 500 18 THR A 2 -113.78 -94.45
REMARK 500 18 THR A 29 -137.71 -144.55
REMARK 500 19 THR A 2 -115.71 -141.29
REMARK 500 19 ASP A 18 -60.85 -96.12
REMARK 500 20 THR A 2 -110.95 -99.11
REMARK 500 20 THR A 29 -135.51 -126.82
REMARK 500 21 THR A 16 81.25 -150.16
REMARK 500 22 THR A 2 -120.42 -97.99
REMARK 500 22 THR A 29 48.70 -75.86
REMARK 500 23 THR A 2 -111.70 -144.31
REMARK 500 23 THR A 29 -86.04 -124.45
REMARK 500 24 THR A 2 -113.25 -99.28
REMARK 500 24 THR A 29 -154.09 -160.17
REMARK 500 25 THR A 2 -117.05 -144.08
REMARK 500 25 ASP A 18 -60.69 -92.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ARG A 19 CYS A 20 1 149.77
REMARK 500 ARG A 19 CYS A 20 3 146.01
REMARK 500 ARG A 19 CYS A 20 5 146.36
REMARK 500 ARG A 19 CYS A 20 6 143.45
REMARK 500 ARG A 19 CYS A 20 7 147.12
REMARK 500 ARG A 19 CYS A 20 8 141.59
REMARK 500 ARG A 19 CYS A 20 9 147.33
REMARK 500 ARG A 19 CYS A 20 10 143.77
REMARK 500 ARG A 19 CYS A 20 11 146.36
REMARK 500 ARG A 19 CYS A 20 12 147.80
REMARK 500 ARG A 19 CYS A 20 15 145.31
REMARK 500 ARG A 19 CYS A 20 16 147.45
REMARK 500 ARG A 19 CYS A 20 17 147.52
REMARK 500 ARG A 19 CYS A 20 18 146.59
REMARK 500 ARG A 19 CYS A 20 20 145.77
REMARK 500 ARG A 19 CYS A 20 22 146.71
REMARK 500 ARG A 19 CYS A 20 23 148.73
REMARK 500 ARG A 19 CYS A 20 24 145.16
REMARK 500 ARG A 19 CYS A 20 25 146.63
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 26 0.18 SIDE CHAIN
REMARK 500 2 TYR A 26 0.15 SIDE CHAIN
REMARK 500 3 ARG A 19 0.08 SIDE CHAIN
REMARK 500 4 TYR A 26 0.14 SIDE CHAIN
REMARK 500 5 ARG A 19 0.14 SIDE CHAIN
REMARK 500 5 TYR A 26 0.07 SIDE CHAIN
REMARK 500 6 ARG A 19 0.15 SIDE CHAIN
REMARK 500 6 TYR A 26 0.25 SIDE CHAIN
REMARK 500 7 ARG A 19 0.16 SIDE CHAIN
REMARK 500 7 TYR A 26 0.25 SIDE CHAIN
REMARK 500 8 ARG A 19 0.11 SIDE CHAIN
REMARK 500 9 TYR A 13 0.11 SIDE CHAIN
REMARK 500 9 ARG A 19 0.16 SIDE CHAIN
REMARK 500 9 TYR A 26 0.24 SIDE CHAIN
REMARK 500 10 ARG A 19 0.11 SIDE CHAIN
REMARK 500 11 ARG A 19 0.12 SIDE CHAIN
REMARK 500 12 TYR A 13 0.12 SIDE CHAIN
REMARK 500 12 ARG A 19 0.14 SIDE CHAIN
REMARK 500 12 TYR A 26 0.07 SIDE CHAIN
REMARK 500 13 TYR A 26 0.20 SIDE CHAIN
REMARK 500 14 ARG A 19 0.17 SIDE CHAIN
REMARK 500 15 TYR A 13 0.12 SIDE CHAIN
REMARK 500 15 TYR A 26 0.21 SIDE CHAIN
REMARK 500 16 ARG A 19 0.17 SIDE CHAIN
REMARK 500 16 TYR A 26 0.27 SIDE CHAIN
REMARK 500 17 ARG A 19 0.17 SIDE CHAIN
REMARK 500 18 TYR A 13 0.12 SIDE CHAIN
REMARK 500 18 ARG A 19 0.14 SIDE CHAIN
REMARK 500 19 TYR A 13 0.12 SIDE CHAIN
REMARK 500 19 ARG A 19 0.10 SIDE CHAIN
REMARK 500 19 TYR A 26 0.24 SIDE CHAIN
REMARK 500 20 TYR A 13 0.13 SIDE CHAIN
REMARK 500 20 ARG A 19 0.18 SIDE CHAIN
REMARK 500 20 TYR A 26 0.26 SIDE CHAIN
REMARK 500 21 ARG A 19 0.09 SIDE CHAIN
REMARK 500 21 TYR A 26 0.26 SIDE CHAIN
REMARK 500 22 ARG A 19 0.12 SIDE CHAIN
REMARK 500 23 TYR A 13 0.12 SIDE CHAIN
REMARK 500 23 ARG A 19 0.13 SIDE CHAIN
REMARK 500 24 ARG A 19 0.15 SIDE CHAIN
REMARK 500 24 TYR A 26 0.23 SIDE CHAIN
REMARK 500 25 ARG A 19 0.16 SIDE CHAIN
REMARK 500 25 TYR A 26 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 31
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DU9 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURES OF BMP02, A NATURAL SCORPION TOXIN WHICH BLOCKS
REMARK 900 APAMIN-SENSITIVE CALCIUM-ACTIVATED POTASSIUM CHANNEL
REMARK 900 RELATED ID: 1PNH RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURES OF P05-NH2, A SCORPION TOXIN ANALOG WITH HIGH
REMARK 900 AFFINITY FOR THE APAMIN-SENSITIVE POTASSIUM CHANNEL
REMARK 900 RELATED ID: 1ACW RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURES OF P01, A NATURAL SCORPION PEPTIDE STRUCTURALLY
REMARK 900 ANALOGUS TO SCORPION TOXINS SPECIFIC FOR APAMIN-SENSITIVE POTASSIUM
REMARK 900 CHANNEL
REMARK 900 RELATED ID: 1SCY RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURES OF SCYLLATOXIN, A SCORPION TOXIN WITH HIGH
REMARK 900 AFFINITY FOR APAMIN-SENSITIVE CALCIUM-ACTIVATED POTASSIUM CHANNELS
DBREF 1S8K A 1 30 UNP Q95NJ8 SKK4_MESMA 24 53
SEQRES 1 A 31 PCA THR GLN CYS GLN SER VAL ARG ASP CYS GLN GLN TYR
SEQRES 2 A 31 CYS LEU THR PRO ASP ARG CYS SER TYR GLY THR CYS TYR
SEQRES 3 A 31 CYS LYS THR THR NH2
MODRES 1S8K PCA A 1 GLN PYROGLUTAMIC ACID
HET PCA A 1 13
HET NH2 A 31 3
HETNAM PCA PYROGLUTAMIC ACID
HETNAM NH2 AMINO GROUP
FORMUL 1 PCA C5 H7 N O3
FORMUL 1 NH2 H2 N
HELIX 1 1 SER A 6 CYS A 14 1 9
SHEET 1 A 2 PRO A 17 SER A 21 0
SHEET 2 A 2 THR A 24 CYS A 27 -1 O TYR A 26 N ASP A 18
SSBOND 1 CYS A 4 CYS A 20 1555 1555 2.08
SSBOND 2 CYS A 10 CYS A 25 1555 1555 2.07
SSBOND 3 CYS A 14 CYS A 27 1555 1555 2.08
LINK C PCA A 1 N THR A 2 1555 1555 1.33
LINK C THR A 30 N NH2 A 31 1555 1555 1.33
SITE 1 AC1 1 THR A 30
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 - 2 20 Bytes