Header list of 1abt.pdb file
Complete list - 16 20 Bytes
HEADER TOXIN 17-NOV-93 1ABT
TITLE NMR SOLUTION STRUCTURE OF AN ALPHA-BUNGAROTOXIN(SLASH)NICOTINIC
TITLE 2 RECEPTOR PEPTIDE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-BUNGAROTOXIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: NICOTINIC RECEPTOR PEPTIDE;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 MOL_ID: 2
KEYWDS TOXIN
EXPDTA SOLUTION NMR
NUMMDL 4
AUTHOR V.J.BASUS,G.SONG,E.HAWROT
REVDAT 5 16-FEB-22 1ABT 1 REMARK
REVDAT 4 19-MAY-09 1ABT 1 REMARK
REVDAT 3 24-FEB-09 1ABT 1 VERSN
REVDAT 2 30-SEP-03 1ABT 1 JRNL DBREF
REVDAT 1 31-JAN-94 1ABT 0
JRNL AUTH V.J.BASUS,G.SONG,E.HAWROT
JRNL TITL NMR SOLUTION STRUCTURE OF AN ALPHA-BUNGAROTOXIN/NICOTINIC
JRNL TITL 2 RECEPTOR PEPTIDE COMPLEX.
JRNL REF BIOCHEMISTRY V. 32 12290 1993
JRNL REFN ISSN 0006-2960
JRNL PMID 8241115
JRNL DOI 10.1021/BI00097A004
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.F.A.PEARCE,P.PRESTON-HURLBURT,E.HAWROT
REMARK 1 TITL THE ROLE OF TYROSINE AT THE LIGAND-BINDING SITE OF THE
REMARK 1 TITL 2 NICOTINIC ACETYLCHOLINE RECEPTOR
REMARK 1 REF PROC.R.SOC.LONDON,SER.B V. 241 207 1990
REMARK 1 REFN ISSN 0080-4649
REMARK 1 REFERENCE 2
REMARK 1 AUTH V.J.BASUS,M.BILLETER,R.A.LOVE,R.M.STROUD,I.D.KUNTZ
REMARK 1 TITL STRUCTURAL STUDIES OF ALPHA-BUNGAROTOXIN. 1.
REMARK 1 TITL 2 SEQUENCE-SPECIFIC 1H NMR RESONANCE ASSIGNMENTS
REMARK 1 REF BIOCHEMISTRY V. 27 2763 1988
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VEMBED, GROMOS-87
REMARK 3 AUTHORS : KUNTZ (VEMBED), VAN GUNSTEREN (GROMOS-87)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NOE DATA CAME FROM SPECTRA COLLECTED AT
REMARK 3 35 DEGREES AND AT 25 DEGREES CELSIUS, PH 5.8. A LIST OF ALL NMR
REMARK 3 CONSTRAINTS WAS DEPOSITED IN THE PROTEIN DATA BANK TOGETHER WITH
REMARK 3 THE STRUCTURE LIST. THESE CONSTRAINTS CONSISTED OF 365
REMARK 3 INTRAMOLECULAR CONSTRAINTS (146 LONG-RANGE, 155 SEQUENTIAL AND
REMARK 3 64 DIHEDRAL ANGLES), AND 24 INTERMOLECULAR CONSTRAINTS BETWEEN
REMARK 3 THE 74 RESIDUES OF BGTX AND THE FIRST 6 RESIDUES OF THE 12
REMARK 3 RESIDUE PEPTIDE FRAGMENT OF NACHR USED IN THIS STUDY (LISTED
REMARK 3 HERE AS RESIDUES 75 B - 80 B). THE COORDINATES THAT FOLLOW ARE
REMARK 3 IN FOUR SEPARATE MODELS. THE 12 RESIDUE PEPTIDE FRAGMENT OF
REMARK 3 NACHR HAS BEEN MODELED FOR ONLY THE FIRST SIX RESIDUES AND HAS
REMARK 3 BEEN NUMBERED AS A CONTINUATION OF THE NUMBERS FOR THE BGTX
REMARK 3 PORTION OF THE COMPLEX AND GIVEN THE CHAIN IDENTIFIER 'B', AFTER
REMARK 3 THE TER ENTRY SEPARATING THE COORDINATES OF THE TWO COMPONENTS
REMARK 3 OF THE COMPLEX. THE AVERAGE RMS DEVIATION OF THE BACKBONE ATOMS,
REMARK 3 WHEN MATCHED IN A PAIRWISE MANNER, IS 2.6 ANGSTROMS, WITH THE
REMARK 3 POORLY DEFINED REGIONS OF RESIDUES 30 A - 38 A, AND 69 A - 74 A
REMARK 3 OF BGTX EXCLUDED. RESTRAINT VIOLATIONS: VIOLATIONS WERE
REMARK 3 CATEGORIZED ACCORDING TO SIZE. THE TOTAL NUMBER OF VIOLATIONS IN
REMARK 3 EACH CATEGORY WAS ADDED, AND THAT NUMBER DIVIDED BY 4 TO
REMARK 3 DETERMINE THE AVERAGE NUMBER OF VIOLATIONS PER STRUCTURE FOR
REMARK 3 EACH CATEGORY. VIOLATION RANGE AVERAGE NUMBER OF VIOLATIONS
REMARK 3 (ANGSTROMS) VIOLATION >0.7 5.0 0.7>=VIOLATION >0.6 6.0 0.6>=
REMARK 3 VIOLATION >0.5 5.75 0.5>=VIOLATION >0.4 9.5 0.4>=VIOLATION >0.3
REMARK 3 17.0 0.3>=VIOLATION >0.2 16.5 0.2>=VIOLATION >0.1 18.0. TO
REMARK 3 SIMPLIFY THE CALCULATIONS, ONLY THE FIRST SIX AMINO ACIDS (185 -
REMARK 3 190) OF THE DODECAPEPTIDE WERE INCORPORATED INTO THE STRUCTURE
REMARK 3 OF THE COMPLEX. THIS WAS APPROPRIATE AS NO INTERMOLECULAR NOE'S
REMARK 3 AND NO LONG-RANGE INTRAMOLECULAR NOE'S WERE ASSIGNED INVOLVING
REMARK 3 PEPTIDE RESIDUES 191 - 196. THE COORDINATES ARE PRESENTED IN
REMARK 3 FOUR SEPARATE MODELS, WITH TER STATEMENTS TO SEPARATE THE BGTX
REMARK 3 PART OF THE COMPLEX FROM THE NACHR PORTION OF THE COMPLEX. ALL
REMARK 3 STRUCTURES WERE MATCHED IN CARTESIAN SPACE SUCH THAT THE RMSD
REMARK 3 BETWEEN THEM WAS MINIMIZED, WITH THE EXCLUSION OF RESIDUES 30 A -
REMARK 3 38 A, AND 69 A - 74 A OF BGTX.
REMARK 4
REMARK 4 1ABT 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_1000170632.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 4
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-4
REMARK 465 RES C SSSEQI
REMARK 465 THR B 81
REMARK 465 CYS B 82
REMARK 465 CYS B 83
REMARK 465 PRO B 84
REMARK 465 ASP B 85
REMARK 465 THR B 86
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 1 TYR A 24 N - CA - C ANGL. DEV. = 16.6 DEGREES
REMARK 500 2 TYR A 24 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 2 ARG A 25 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 2 TYR B 79 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 3 ARG A 25 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 TYR A 54 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 3 TYR B 79 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 4 TYR A 24 CA - CB - CG ANGL. DEV. = 12.5 DEGREES
REMARK 500 4 TYR A 24 CB - CG - CD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 4 TYR A 24 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 4 ARG A 25 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 4 TYR B 79 CB - CG - CD2 ANGL. DEV. = -5.2 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 3 -138.70 -131.50
REMARK 500 1 ALA A 13 81.59 -68.85
REMARK 500 1 THR A 15 94.43 -69.73
REMARK 500 1 GLU A 20 -163.54 -119.26
REMARK 500 1 ASN A 21 13.90 -65.75
REMARK 500 1 TYR A 24 -84.80 -18.63
REMARK 500 1 ARG A 25 82.64 -2.20
REMARK 500 1 TRP A 28 -156.55 -146.34
REMARK 500 1 CYS A 29 116.38 -25.34
REMARK 500 1 ASP A 30 87.68 72.36
REMARK 500 1 PHE A 32 43.71 23.10
REMARK 500 1 CYS A 33 51.78 26.40
REMARK 500 1 SER A 34 -90.85 -166.74
REMARK 500 1 ARG A 36 100.85 70.41
REMARK 500 1 VAL A 39 95.62 -67.13
REMARK 500 1 PRO A 53 108.82 -59.40
REMARK 500 1 TYR A 54 88.74 -64.76
REMARK 500 1 SER A 61 -73.50 -79.23
REMARK 500 1 ASP A 63 76.38 71.97
REMARK 500 1 LYS A 64 -76.00 59.55
REMARK 500 1 CYS A 65 -64.20 56.64
REMARK 500 1 HIS A 68 -66.78 -18.45
REMARK 500 1 PRO A 69 -178.35 -66.47
REMARK 500 1 GLN A 71 75.33 -66.03
REMARK 500 2 CYS A 3 -124.05 -169.87
REMARK 500 2 THR A 6 -77.24 55.67
REMARK 500 2 ALA A 7 -80.63 -0.58
REMARK 500 2 THR A 8 37.19 -78.39
REMARK 500 2 PRO A 10 79.21 -69.23
REMARK 500 2 ILE A 11 114.83 65.30
REMARK 500 2 THR A 15 109.40 -57.42
REMARK 500 2 GLU A 20 53.12 20.15
REMARK 500 2 LYS A 26 -161.81 179.76
REMARK 500 2 ALA A 31 -53.70 72.56
REMARK 500 2 PHE A 32 -98.46 -49.63
REMARK 500 2 CYS A 33 -78.55 62.97
REMARK 500 2 ARG A 36 105.77 63.23
REMARK 500 2 LYS A 38 82.73 51.10
REMARK 500 2 GLU A 41 -167.68 -165.76
REMARK 500 2 LEU A 42 164.29 179.36
REMARK 500 2 ALA A 46 5.62 -62.44
REMARK 500 2 PRO A 49 88.51 -66.59
REMARK 500 2 LYS A 51 -5.24 84.40
REMARK 500 2 PRO A 53 106.95 -54.18
REMARK 500 2 TYR A 54 88.71 -65.88
REMARK 500 2 ASP A 63 -160.45 46.44
REMARK 500 2 LYS A 64 58.24 -67.74
REMARK 500 2 LYS A 70 -77.37 -28.56
REMARK 500 2 GLN A 71 -37.59 56.50
REMARK 500 2 TYR B 79 61.72 -100.30
REMARK 500
REMARK 500 THIS ENTRY HAS 96 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 TYR A 24 ARG A 25 1 -131.03
REMARK 500 GLU A 41 LEU A 42 2 134.97
REMARK 500 LYS A 38 VAL A 39 3 145.32
REMARK 500 VAL A 39 VAL A 40 4 -149.67
REMARK 500 VAL A 40 GLU A 41 4 128.73
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 HIS A 4 0.16 SIDE CHAIN
REMARK 500 1 TYR A 24 0.15 SIDE CHAIN
REMARK 500 1 PHE A 32 0.08 SIDE CHAIN
REMARK 500 1 TYR A 54 0.10 SIDE CHAIN
REMARK 500 1 HIS A 68 0.14 SIDE CHAIN
REMARK 500 1 TYR B 80 0.07 SIDE CHAIN
REMARK 500 2 TYR A 24 0.15 SIDE CHAIN
REMARK 500 2 TYR B 79 0.09 SIDE CHAIN
REMARK 500 3 TYR A 24 0.07 SIDE CHAIN
REMARK 500 3 TYR B 79 0.19 SIDE CHAIN
REMARK 500 3 TYR B 80 0.07 SIDE CHAIN
REMARK 500 4 ARG A 36 0.07 SIDE CHAIN
REMARK 500 4 HIS A 68 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 1 GLU A 56 11.41
REMARK 500 3 HIS A 4 10.34
REMARK 500 3 THR A 5 11.03
REMARK 500 3 ALA A 7 -10.34
REMARK 500 3 SER A 12 10.34
REMARK 500 3 TYR A 24 10.32
REMARK 500 3 ARG A 36 11.42
REMARK 500 3 LYS A 38 15.60
REMARK 500 3 PRO A 49 10.99
REMARK 500 3 LYS A 51 -10.60
REMARK 500 3 CYS A 65 -12.44
REMARK 500 4 VAL A 40 11.33
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ABT A 1 74 UNP P60615 NXL1A_BUNMU 1 74
DBREF 1ABT B 75 86 UNP P02710 ACHA_TORCA 209 220
SEQRES 1 A 74 ILE VAL CYS HIS THR THR ALA THR SER PRO ILE SER ALA
SEQRES 2 A 74 VAL THR CYS PRO PRO GLY GLU ASN LEU CYS TYR ARG LYS
SEQRES 3 A 74 MET TRP CYS ASP ALA PHE CYS SER SER ARG GLY LYS VAL
SEQRES 4 A 74 VAL GLU LEU GLY CYS ALA ALA THR CYS PRO SER LYS LYS
SEQRES 5 A 74 PRO TYR GLU GLU VAL THR CYS CYS SER THR ASP LYS CYS
SEQRES 6 A 74 ASN PRO HIS PRO LYS GLN ARG PRO GLY
SEQRES 1 B 12 LYS HIS TRP VAL TYR TYR THR CYS CYS PRO ASP THR
HELIX 1 1 ASP A 30 SER A 34 5 5
SHEET 1 S1 2 ILE A 1 THR A 5 0
SHEET 2 S1 2 SER A 12 CYS A 16 -1 O SER A 12 N THR A 5
SHEET 1 S2 3 VAL A 39 ALA A 45 0
SHEET 2 S2 3 LEU A 22 TRP A 28 -1 N LEU A 22 O ALA A 45
SHEET 3 S2 3 GLU A 56 CYS A 60 -1 O GLU A 56 N MET A 27
SSBOND 1 CYS A 3 CYS A 23 1555 1555 2.03
SSBOND 2 CYS A 16 CYS A 44 1555 1555 2.04
SSBOND 3 CYS A 29 CYS A 33 1555 1555 2.04
SSBOND 4 CYS A 48 CYS A 59 1555 1555 2.04
SSBOND 5 CYS A 60 CYS A 65 1555 1555 2.04
CISPEP 1 CYS A 29 ASP A 30 1 17.57
CISPEP 2 TYR A 24 ARG A 25 4 9.57
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