Header list of 1wm7.pdb file
Complete list - 2 20 Bytes
HEADER TOXIN 05-JUL-04 1WM7
TITLE SOLUTION STRUCTURE OF BMP01 FROM THE VENOM OF SCORPION BUTHUS
TITLE 2 MARTENSII KARSCH, 9 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROTOXIN BMP01;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: POTASSIUM ION CHANNEL BLOCKER P01
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 9
AUTHOR G.WU,Y.LI,D.WEI,F.HE,S.JIANG,G.HU,H.WU,X.CHEN
REVDAT 3 02-MAR-22 1WM7 1 REMARK
REVDAT 2 24-FEB-09 1WM7 1 VERSN
REVDAT 1 27-JUL-04 1WM7 0
JRNL AUTH G.WU,Y.LI,D.WEI,F.HE,S.JIANG,G.HU,H.WU
JRNL TITL SOLUTION STRUCTURE OF BMP01 FROM THE VENOM OF SCORPION
JRNL TITL 2 BUTHUS MARTENSII KARSCH
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 276 1148 2000
JRNL REFN ISSN 0006-291X
JRNL PMID 11027603
JRNL DOI 10.1006/BBRC.2000.3435
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, SYBYL 6.3
REMARK 3 AUTHORS : MIKE CARLISLE, DAN STEELE, MIKE MILLER (VNMR),
REMARK 3 TRIPOS, INC. (SYBYL)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE ARE BASED ON A TOTAL OF
REMARK 3 381 CONSTRAINTS, 337 ARE NOE-DERIVED DISTANCE CONSTRAINTS,21
REMARK 3 DIHEDRAL ANGLE CONSTRAINTS,23 DISTANCE CONSTRAINTS FROM SEVEN
REMARK 3 HYDROGEN BONDS AND THREE DISULFIDE BONDS.
REMARK 4
REMARK 4 1WM7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-JUL-04.
REMARK 100 THE DEPOSITION ID IS D_1000023733.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 313
REMARK 210 PH : 3.0; 3.0
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 3.25MM; 3.25MM
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY, 2D TOCSY, DQF-COSY
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, SYBYL(TRIADNMR MODEL)
REMARK 210 6.3, SYBYL(DIANA PROGRAM) 6.3
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 9
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 LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 GLU A 4 CD GLU A 4 OE1 0.137
REMARK 500 1 ASP A 5 CG ASP A 5 OD1 0.150
REMARK 500 1 GLU A 8 CD GLU A 8 OE1 0.139
REMARK 500 1 ARG A 16 NE ARG A 16 CZ 0.086
REMARK 500 1 ARG A 16 CZ ARG A 16 NH1 0.090
REMARK 500 1 ARG A 16 CZ ARG A 16 NH2 0.083
REMARK 500 1 ASP A 22 CG ASP A 22 OD1 0.152
REMARK 500 1 GLU A 27 CD GLU A 27 OE1 0.137
REMARK 500 2 GLU A 4 CD GLU A 4 OE1 0.141
REMARK 500 2 ASP A 5 CG ASP A 5 OD1 0.145
REMARK 500 2 GLU A 8 CD GLU A 8 OE2 0.137
REMARK 500 2 ARG A 16 NE ARG A 16 CZ 0.117
REMARK 500 2 ARG A 16 CZ ARG A 16 NH1 0.094
REMARK 500 2 ARG A 16 CZ ARG A 16 NH2 0.090
REMARK 500 2 ASP A 22 CG ASP A 22 OD1 0.142
REMARK 500 2 GLU A 27 CD GLU A 27 OE2 0.136
REMARK 500 3 GLU A 4 CD GLU A 4 OE2 0.139
REMARK 500 3 ASP A 5 CG ASP A 5 OD1 0.144
REMARK 500 3 ASP A 5 C CYS A 6 N 0.142
REMARK 500 3 CYS A 6 C PRO A 7 N 0.129
REMARK 500 3 GLU A 8 CD GLU A 8 OE2 0.125
REMARK 500 3 ARG A 16 NE ARG A 16 CZ 0.112
REMARK 500 3 ARG A 16 CZ ARG A 16 NH1 0.097
REMARK 500 3 ARG A 16 CZ ARG A 16 NH2 0.084
REMARK 500 3 ASP A 20 CG ASP A 20 OD2 0.154
REMARK 500 3 ASP A 22 CG ASP A 22 OD1 0.155
REMARK 500 3 VAL A 25 C CYS A 26 N 0.166
REMARK 500 3 GLU A 27 CD GLU A 27 OE1 0.138
REMARK 500 4 GLU A 4 CD GLU A 4 OE2 0.141
REMARK 500 4 ASP A 5 CG ASP A 5 OD1 0.148
REMARK 500 4 ASP A 5 C CYS A 6 N 0.147
REMARK 500 4 GLU A 8 CD GLU A 8 OE1 0.140
REMARK 500 4 ARG A 16 NE ARG A 16 CZ 0.089
REMARK 500 4 ARG A 16 CZ ARG A 16 NH1 0.094
REMARK 500 4 ARG A 16 CZ ARG A 16 NH2 0.089
REMARK 500 4 ASP A 20 CG ASP A 20 OD2 0.153
REMARK 500 4 ASP A 22 CG ASP A 22 OD1 0.138
REMARK 500 4 GLU A 27 CD GLU A 27 OE1 0.130
REMARK 500 5 GLU A 4 CD GLU A 4 OE2 0.145
REMARK 500 5 ASP A 5 CG ASP A 5 OD1 0.142
REMARK 500 5 GLU A 8 CD GLU A 8 OE2 0.134
REMARK 500 5 ARG A 16 NE ARG A 16 CZ 0.087
REMARK 500 5 ARG A 16 CZ ARG A 16 NH1 0.090
REMARK 500 5 ARG A 16 CZ ARG A 16 NH2 0.082
REMARK 500 5 ASP A 20 CG ASP A 20 OD2 0.164
REMARK 500 5 ASP A 22 CG ASP A 22 OD2 0.149
REMARK 500 5 GLU A 27 CD GLU A 27 OE1 0.139
REMARK 500 6 GLU A 4 CD GLU A 4 OE2 0.136
REMARK 500 6 ASP A 5 CG ASP A 5 OD1 0.150
REMARK 500 6 GLU A 8 CD GLU A 8 OE2 0.133
REMARK 500
REMARK 500 THIS ENTRY HAS 86 BOND DEVIATIONS.
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 3 ASP A 5 CA - C - N ANGL. DEV. = 16.0 DEGREES
REMARK 500 3 ASP A 5 O - C - N ANGL. DEV. = -10.4 DEGREES
REMARK 500 3 CYS A 6 N - CA - CB ANGL. DEV. = 9.1 DEGREES
REMARK 500 3 ARG A 16 CA - C - N ANGL. DEV. = 13.4 DEGREES
REMARK 500 3 CYS A 24 N - CA - CB ANGL. DEV. = -11.3 DEGREES
REMARK 500 3 VAL A 25 CA - C - N ANGL. DEV. = 14.4 DEGREES
REMARK 500 4 ASP A 5 CA - C - N ANGL. DEV. = 16.0 DEGREES
REMARK 500 4 ASP A 5 O - C - N ANGL. DEV. = -10.5 DEGREES
REMARK 500 4 CYS A 6 N - CA - CB ANGL. DEV. = 10.0 DEGREES
REMARK 500 4 CYS A 19 N - CA - C ANGL. DEV. = -17.8 DEGREES
REMARK 500 4 LYS A 23 CA - C - N ANGL. DEV. = 16.4 DEGREES
REMARK 500 4 LYS A 23 O - C - N ANGL. DEV. = -9.6 DEGREES
REMARK 500 5 CYS A 3 CB - CA - C ANGL. DEV. = 9.1 DEGREES
REMARK 500 6 CYS A 19 N - CA - C ANGL. DEV. = -19.0 DEGREES
REMARK 500 6 LYS A 23 CA - C - N ANGL. DEV. = 15.8 DEGREES
REMARK 500 7 LYS A 18 CA - C - N ANGL. DEV. = 13.4 DEGREES
REMARK 500 7 CYS A 19 N - CA - C ANGL. DEV. = -16.5 DEGREES
REMARK 500 8 ARG A 16 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 9 ASP A 5 CA - C - N ANGL. DEV. = 16.1 DEGREES
REMARK 500 9 ASP A 5 O - C - N ANGL. DEV. = -10.8 DEGREES
REMARK 500 9 CYS A 19 N - CA - CB ANGL. DEV. = -11.8 DEGREES
REMARK 500 9 LYS A 23 CA - C - N ANGL. DEV. = 13.9 DEGREES
REMARK 500 9 VAL A 25 CA - C - N ANGL. DEV. = 15.6 DEGREES
REMARK 500 9 CYS A 26 CB - CA - C ANGL. DEV. = -12.1 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 ALA A 15 -148.61 -139.57
REMARK 500 1 ARG A 16 -156.48 -136.25
REMARK 500 1 LYS A 18 146.00 -177.19
REMARK 500 1 CYS A 19 57.20 178.29
REMARK 500 1 ASP A 20 -148.17 -73.34
REMARK 500 1 ASP A 22 25.73 -173.56
REMARK 500 1 VAL A 25 -153.42 -150.28
REMARK 500 2 CYS A 3 38.14 -88.99
REMARK 500 2 ALA A 15 -135.25 -156.11
REMARK 500 2 ARG A 16 -135.45 -110.55
REMARK 500 2 ASP A 22 -1.23 -145.79
REMARK 500 2 LYS A 23 -152.99 -127.11
REMARK 500 2 VAL A 25 -91.73 -99.25
REMARK 500 3 CYS A 3 22.58 -78.72
REMARK 500 3 CYS A 6 -81.71 111.54
REMARK 500 3 GLN A 13 -49.59 -146.09
REMARK 500 3 ALA A 15 -140.67 -143.73
REMARK 500 3 ARG A 16 -150.16 -143.00
REMARK 500 3 LYS A 18 -126.64 -137.71
REMARK 500 3 ASN A 21 -46.87 -26.79
REMARK 500 3 ASP A 22 -39.45 -132.19
REMARK 500 3 VAL A 25 148.15 175.99
REMARK 500 4 THR A 2 -169.71 -126.95
REMARK 500 4 CYS A 3 35.00 -84.85
REMARK 500 4 CYS A 6 -58.75 115.04
REMARK 500 4 THR A 12 -36.73 -37.88
REMARK 500 4 GLN A 13 -59.81 -129.07
REMARK 500 4 ARG A 16 -156.90 -114.61
REMARK 500 4 CYS A 19 61.15 -173.58
REMARK 500 4 ASP A 20 -164.45 -77.78
REMARK 500 4 ASP A 22 8.51 -166.38
REMARK 500 4 LYS A 23 37.91 -162.91
REMARK 500 4 VAL A 25 -122.20 -101.56
REMARK 500 5 PRO A 7 -2.49 -29.33
REMARK 500 5 GLN A 13 -15.87 -164.88
REMARK 500 5 ALA A 15 -150.20 -165.51
REMARK 500 5 ARG A 16 -130.95 -120.68
REMARK 500 5 LYS A 18 154.53 179.54
REMARK 500 5 CYS A 19 55.59 -169.21
REMARK 500 5 ASP A 20 -159.39 -69.41
REMARK 500 5 ASP A 22 -6.56 -156.01
REMARK 500 5 VAL A 25 -88.05 -115.28
REMARK 500 6 CYS A 3 35.80 -78.69
REMARK 500 6 GLN A 13 -50.25 -131.87
REMARK 500 6 ARG A 16 -153.23 -101.36
REMARK 500 6 CYS A 19 82.79 -160.92
REMARK 500 6 ASP A 20 -150.79 -84.97
REMARK 500 6 ASP A 22 -8.81 -164.02
REMARK 500 6 LYS A 23 46.23 -172.14
REMARK 500 6 VAL A 25 -127.09 -122.97
REMARK 500
REMARK 500 THIS ENTRY HAS 78 RAMACHANDRAN OUTLIERS.
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 ASN A 14 ALA A 15 1 -141.63
REMARK 500 LYS A 23 CYS A 24 1 -143.50
REMARK 500 VAL A 25 CYS A 26 1 -140.47
REMARK 500 LYS A 18 CYS A 19 2 -78.98
REMARK 500 ASN A 14 ALA A 15 3 -148.70
REMARK 500 ASN A 14 ALA A 15 4 -137.60
REMARK 500 CYS A 19 ASP A 20 4 -143.37
REMARK 500 ASN A 14 ALA A 15 6 -140.36
REMARK 500 CYS A 19 ASP A 20 6 -139.37
REMARK 500 ASP A 22 LYS A 23 6 -149.32
REMARK 500 VAL A 25 CYS A 26 7 -136.29
REMARK 500 ASN A 14 ALA A 15 8 -147.09
REMARK 500 LYS A 18 CYS A 19 9 -149.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
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: 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 STRUCTURE OF P05-NH2,A SCORPION TOXIN ANALOG WITH HIGH
REMARK 900 AFFINITY FOR THE APAMIN-SENSITIVE POTASSIUM 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 CHANNEL
DBREF 1WM7 A 1 29 UNP Q9U8D2 SCP1_MESMA 29 57
SEQRES 1 A 29 ALA THR CYS GLU ASP CYS PRO GLU HIS CYS ALA THR GLN
SEQRES 2 A 29 ASN ALA ARG ALA LYS CYS ASP ASN ASP LYS CYS VAL CYS
SEQRES 3 A 29 GLU PRO LYS
HELIX 1 1 THR A 2 CYS A 6 5 5
SHEET 1 A 2 ARG A 16 LYS A 18 0
SHEET 2 A 2 VAL A 25 GLU A 27 -1 O VAL A 25 N LYS A 18
SSBOND 1 CYS A 3 CYS A 19 1555 1555 2.12
SSBOND 2 CYS A 6 CYS A 24 1555 1555 2.07
SSBOND 3 CYS A 10 CYS A 26 1555 1555 2.10
CISPEP 1 LYS A 18 CYS A 19 1 -7.88
CISPEP 2 ASP A 5 CYS A 6 3 13.19
CISPEP 3 VAL A 25 CYS A 26 3 -18.10
CISPEP 4 ASP A 5 CYS A 6 4 6.12
CISPEP 5 LYS A 18 CYS A 19 4 -13.60
CISPEP 6 LYS A 23 CYS A 24 4 -12.91
CISPEP 7 LYS A 18 CYS A 19 5 -11.86
CISPEP 8 LYS A 18 CYS A 19 6 -29.59
CISPEP 9 LYS A 23 CYS A 24 6 -9.83
CISPEP 10 LYS A 18 CYS A 19 7 -7.15
CISPEP 11 ASP A 5 CYS A 6 9 -3.09
CISPEP 12 LYS A 23 CYS A 24 9 -11.83
CISPEP 13 VAL A 25 CYS A 26 9 -10.08
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