Header list of 1tba.pdb file
Complete list - r 2 2 Bytes
HEADER COMPLEX (TRANSCRIPTION FACTORS) 16-AUG-98 1TBA
TITLE SOLUTION STRUCTURE OF A TBP-TAFII230 COMPLEX: PROTEIN MIMICRY OF THE
TITLE 2 MINOR GROOVE SURFACE OF THE TATA BOX UNWOUND BY TBP, NMR, 25
TITLE 3 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTION INITIATION FACTOR IID 230K CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 11-77;
COMPND 5 SYNONYM: TAFII230;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: TRANSCRIPTION INITIATION FACTOR TFIID;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: CORE DOMAIN RESIDUES 60-249;
COMPND 11 SYNONYM: TBP;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 9 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 10 ORGANISM_TAXID: 4932;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 13 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS COMPLEX (TRANSCRIPTION FACTORS), TBP, TAF, TAFII230, TFIID, SOLUTION
KEYWDS 2 STRUCTURE
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR D.LIU,R.ISHIMA,K.I.TONG,S.BAGBY,T.KOKUBO,D.R.MUHANDIRAM,L.E.KAY,
AUTHOR 2 Y.NAKATANI,M.IKURA
REVDAT 3 02-MAR-22 1TBA 1 REMARK
REVDAT 2 24-FEB-09 1TBA 1 VERSN
REVDAT 1 16-AUG-99 1TBA 0
JRNL AUTH D.LIU,R.ISHIMA,K.I.TONG,S.BAGBY,T.KOKUBO,D.R.MUHANDIRAM,
JRNL AUTH 2 L.E.KAY,Y.NAKATANI,M.IKURA
JRNL TITL SOLUTION STRUCTURE OF A TBP-TAF(II)230 COMPLEX: PROTEIN
JRNL TITL 2 MIMICRY OF THE MINOR GROOVE SURFACE OF THE TATA BOX UNWOUND
JRNL TITL 3 BY TBP.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 94 573 1998
JRNL REFN ISSN 0092-8674
JRNL PMID 9741622
JRNL DOI 10.1016/S0092-8674(00)81599-8
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TBA 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_1000176592.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
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 : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING MULTIDIMENSIONAL
REMARK 210 HETERONUCLEAR NMR ON 13C, 15N AND 2H-LABELED TBP AND TAF
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 ASP A 29 H GLY A 32 1.49
REMARK 500 O LEU A 52 H ILE A 56 1.53
REMARK 500 O ASN A 27 H LEU A 35 1.55
REMARK 500 O ARG B 141 H LYS B 145 1.57
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 ASN A 27 112.39 33.04
REMARK 500 1 SER A 30 -28.69 -37.74
REMARK 500 1 ASP A 49 -147.58 -62.97
REMARK 500 1 ALA A 50 31.10 -99.53
REMARK 500 1 SER A 60 42.42 -85.72
REMARK 500 1 LYS A 61 13.05 -143.89
REMARK 500 1 LEU A 62 -31.90 -133.32
REMARK 500 1 GLU A 76 24.95 -141.92
REMARK 500 1 ILE B 63 -55.79 -126.83
REMARK 500 1 VAL B 64 129.28 62.11
REMARK 500 1 PHE B 99 -165.19 -170.47
REMARK 500 1 ALA B 100 54.00 -115.29
REMARK 500 1 GLU B 108 88.94 -161.05
REMARK 500 1 LYS B 151 -157.97 -113.47
REMARK 500 1 LYS B 167 -4.51 73.59
REMARK 500 1 PHE B 182 -34.96 -169.82
REMARK 500 1 LEU B 189 -44.02 -148.66
REMARK 500 2 SER A 13 174.29 -58.24
REMARK 500 2 ASP A 19 82.50 -66.91
REMARK 500 2 ASN A 27 132.01 -20.27
REMARK 500 2 SER A 30 -28.07 -37.96
REMARK 500 2 GLN A 36 13.91 -152.65
REMARK 500 2 ASP A 37 -53.17 71.74
REMARK 500 2 ARG A 43 56.77 -167.96
REMARK 500 2 THR A 46 -80.03 -112.70
REMARK 500 2 ASP A 49 178.43 -48.65
REMARK 500 2 SER A 60 52.56 -107.38
REMARK 500 2 LYS A 61 24.88 -169.82
REMARK 500 2 LEU A 74 66.94 -103.96
REMARK 500 2 ILE B 63 -56.40 64.57
REMARK 500 2 VAL B 64 139.40 63.76
REMARK 500 2 ARG B 98 -71.64 -100.07
REMARK 500 2 ALA B 100 47.96 -82.51
REMARK 500 2 GLU B 108 85.22 170.70
REMARK 500 2 ALA B 126 158.58 -42.48
REMARK 500 2 ALA B 149 34.72 -99.65
REMARK 500 2 PHE B 152 108.34 -58.97
REMARK 500 2 LYS B 167 -2.25 73.53
REMARK 500 2 LEU B 189 -37.30 -150.93
REMARK 500 2 GLN B 219 -152.04 -136.17
REMARK 500 3 ILE A 14 90.14 47.58
REMARK 500 3 ASN A 16 -68.73 -146.19
REMARK 500 3 ASN A 27 135.73 -24.49
REMARK 500 3 SER A 30 -26.69 -39.53
REMARK 500 3 SER A 60 43.50 -91.18
REMARK 500 3 LYS A 61 27.25 -172.88
REMARK 500 3 ILE A 72 68.21 -150.51
REMARK 500 3 ILE B 63 -39.00 -140.63
REMARK 500 3 VAL B 64 142.22 59.34
REMARK 500 3 PHE B 99 -159.23 -163.07
REMARK 500
REMARK 500 THIS ENTRY HAS 571 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 33 0.28 SIDE CHAIN
REMARK 500 1 ARG A 43 0.29 SIDE CHAIN
REMARK 500 1 ARG A 53 0.31 SIDE CHAIN
REMARK 500 1 ARG B 79 0.28 SIDE CHAIN
REMARK 500 1 ARG B 90 0.16 SIDE CHAIN
REMARK 500 1 ARG B 98 0.32 SIDE CHAIN
REMARK 500 1 ARG B 105 0.18 SIDE CHAIN
REMARK 500 1 ARG B 107 0.19 SIDE CHAIN
REMARK 500 1 ARG B 137 0.27 SIDE CHAIN
REMARK 500 1 ARG B 141 0.30 SIDE CHAIN
REMARK 500 1 ARG B 171 0.31 SIDE CHAIN
REMARK 500 1 ARG B 196 0.21 SIDE CHAIN
REMARK 500 1 ARG B 220 0.32 SIDE CHAIN
REMARK 500 1 ARG B 238 0.27 SIDE CHAIN
REMARK 500 2 ARG A 33 0.15 SIDE CHAIN
REMARK 500 2 ARG A 43 0.28 SIDE CHAIN
REMARK 500 2 ARG A 53 0.27 SIDE CHAIN
REMARK 500 2 ARG B 79 0.24 SIDE CHAIN
REMARK 500 2 ARG B 90 0.13 SIDE CHAIN
REMARK 500 2 ARG B 98 0.21 SIDE CHAIN
REMARK 500 2 ARG B 105 0.28 SIDE CHAIN
REMARK 500 2 ARG B 107 0.26 SIDE CHAIN
REMARK 500 2 ARG B 137 0.28 SIDE CHAIN
REMARK 500 2 ARG B 141 0.14 SIDE CHAIN
REMARK 500 2 ARG B 171 0.12 SIDE CHAIN
REMARK 500 2 ARG B 196 0.32 SIDE CHAIN
REMARK 500 2 ARG B 220 0.22 SIDE CHAIN
REMARK 500 2 ARG B 238 0.31 SIDE CHAIN
REMARK 500 3 ARG A 33 0.31 SIDE CHAIN
REMARK 500 3 ARG A 43 0.28 SIDE CHAIN
REMARK 500 3 ARG A 53 0.32 SIDE CHAIN
REMARK 500 3 ARG B 79 0.19 SIDE CHAIN
REMARK 500 3 ARG B 90 0.27 SIDE CHAIN
REMARK 500 3 ARG B 98 0.17 SIDE CHAIN
REMARK 500 3 ARG B 105 0.19 SIDE CHAIN
REMARK 500 3 ARG B 107 0.29 SIDE CHAIN
REMARK 500 3 ARG B 137 0.32 SIDE CHAIN
REMARK 500 3 ARG B 141 0.32 SIDE CHAIN
REMARK 500 3 ARG B 171 0.29 SIDE CHAIN
REMARK 500 3 ARG B 196 0.32 SIDE CHAIN
REMARK 500 3 ARG B 220 0.23 SIDE CHAIN
REMARK 500 3 ARG B 238 0.20 SIDE CHAIN
REMARK 500 4 ARG A 33 0.29 SIDE CHAIN
REMARK 500 4 ARG A 43 0.21 SIDE CHAIN
REMARK 500 4 ARG A 53 0.20 SIDE CHAIN
REMARK 500 4 ARG B 79 0.31 SIDE CHAIN
REMARK 500 4 ARG B 90 0.32 SIDE CHAIN
REMARK 500 4 ARG B 98 0.27 SIDE CHAIN
REMARK 500 4 ARG B 105 0.21 SIDE CHAIN
REMARK 500 4 ARG B 137 0.25 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 331 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1TBA A 11 77 UNP P51123 TAF1_DROME 11 77
DBREF 1TBA B 61 240 UNP P13393 TBP_YEAST 60 239
SEQRES 1 A 67 GLU GLY SER ILE GLY ASN GLY LEU ASP LEU THR GLY ILE
SEQRES 2 A 67 LEU PHE GLY ASN ILE ASP SER GLU GLY ARG LEU LEU GLN
SEQRES 3 A 67 ASP ASP ASP GLY GLU GLY ARG GLY GLY THR GLY PHE ASP
SEQRES 4 A 67 ALA GLU LEU ARG GLU ASN ILE GLY SER LEU SER LYS LEU
SEQRES 5 A 67 GLY LEU ASP SER MET LEU LEU GLU VAL ILE ASP LEU LYS
SEQRES 6 A 67 GLU ALA
SEQRES 1 B 180 SER GLY ILE VAL PRO THR LEU GLN ASN ILE VAL ALA THR
SEQRES 2 B 180 VAL THR LEU GLY CYS ARG LEU ASP LEU LYS THR VAL ALA
SEQRES 3 B 180 LEU HIS ALA ARG ASN ALA GLU TYR ASN PRO LYS ARG PHE
SEQRES 4 B 180 ALA ALA VAL ILE MET ARG ILE ARG GLU PRO LYS THR THR
SEQRES 5 B 180 ALA LEU ILE PHE ALA SER GLY LYS MET VAL VAL THR GLY
SEQRES 6 B 180 ALA LYS SER GLU ASP ASP SER LYS LEU ALA SER ARG LYS
SEQRES 7 B 180 TYR ALA ARG ILE ILE GLN LYS ILE GLY PHE ALA ALA LYS
SEQRES 8 B 180 PHE THR ASP PHE LYS ILE GLN ASN ILE VAL GLY SER CYS
SEQRES 9 B 180 ASP VAL LYS PHE PRO ILE ARG LEU GLU GLY LEU ALA PHE
SEQRES 10 B 180 SER HIS GLY THR PHE SER SER TYR GLU PRO GLU LEU PHE
SEQRES 11 B 180 PRO GLY LEU ILE TYR ARG MET VAL LYS PRO LYS ILE VAL
SEQRES 12 B 180 LEU LEU ILE PHE VAL SER GLY LYS ILE VAL LEU THR GLY
SEQRES 13 B 180 ALA LYS GLN ARG GLU GLU ILE TYR GLN ALA PHE GLU ALA
SEQRES 14 B 180 ILE TYR PRO VAL LEU SER GLU PHE ARG LYS MET
HELIX 1 1 ILE A 23 GLY A 26 1 4
HELIX 2 2 ARG A 53 SER A 58 1 6
HELIX 3 3 LEU A 64 LEU A 69 1 6
HELIX 4 4 LEU B 82 HIS B 88 1 7
HELIX 5 5 GLU B 129 ILE B 146 1 18
HELIX 6 6 LEU B 172 SER B 178 1 7
HELIX 7 7 ARG B 220 PHE B 237 1 18
SHEET 1 A 8 ALA B 101 ILE B 106 0
SHEET 2 A 8 THR B 111 PHE B 116 -1 N ILE B 115 O VAL B 102
SHEET 3 A 8 LYS B 120 ALA B 126 -1 N THR B 124 O THR B 112
SHEET 4 A 8 THR B 66 THR B 75 -1 N VAL B 74 O MET B 121
SHEET 5 A 8 ASN B 159 ASP B 165 -1 N SER B 163 O THR B 66
SHEET 6 A 8 LYS B 211 THR B 215 -1 N LEU B 214 O GLY B 162
SHEET 7 A 8 ILE B 202 ILE B 206 -1 N LEU B 205 O VAL B 213
SHEET 8 A 8 LEU B 193 MET B 197 -1 N MET B 197 O ILE B 202
CISPEP 1 GLU B 108 PRO B 109 1 -0.40
CISPEP 2 LYS B 199 PRO B 200 1 -0.08
CISPEP 3 GLU B 108 PRO B 109 2 -0.33
CISPEP 4 LYS B 199 PRO B 200 2 -0.24
CISPEP 5 GLU B 108 PRO B 109 3 -0.40
CISPEP 6 LYS B 199 PRO B 200 3 0.10
CISPEP 7 GLU B 108 PRO B 109 4 -0.48
CISPEP 8 LYS B 199 PRO B 200 4 -0.13
CISPEP 9 GLU B 108 PRO B 109 5 -0.32
CISPEP 10 LYS B 199 PRO B 200 5 -0.01
CISPEP 11 GLU B 108 PRO B 109 6 -0.25
CISPEP 12 LYS B 199 PRO B 200 6 -0.05
CISPEP 13 GLU B 108 PRO B 109 7 -0.36
CISPEP 14 LYS B 199 PRO B 200 7 0.22
CISPEP 15 GLU B 108 PRO B 109 8 -0.34
CISPEP 16 LYS B 199 PRO B 200 8 -0.14
CISPEP 17 GLU B 108 PRO B 109 9 -0.65
CISPEP 18 LYS B 199 PRO B 200 9 -0.12
CISPEP 19 GLU B 108 PRO B 109 10 -0.46
CISPEP 20 LYS B 199 PRO B 200 10 -0.15
CISPEP 21 GLU B 108 PRO B 109 11 -0.17
CISPEP 22 LYS B 199 PRO B 200 11 -0.13
CISPEP 23 GLU B 108 PRO B 109 12 -0.38
CISPEP 24 LYS B 199 PRO B 200 12 -0.24
CISPEP 25 GLU B 108 PRO B 109 13 -0.38
CISPEP 26 LYS B 199 PRO B 200 13 0.09
CISPEP 27 GLU B 108 PRO B 109 14 -0.55
CISPEP 28 LYS B 199 PRO B 200 14 -0.23
CISPEP 29 GLU B 108 PRO B 109 15 -0.12
CISPEP 30 LYS B 199 PRO B 200 15 -0.19
CISPEP 31 GLU B 108 PRO B 109 16 -0.29
CISPEP 32 LYS B 199 PRO B 200 16 -0.01
CISPEP 33 GLU B 108 PRO B 109 17 -0.25
CISPEP 34 LYS B 199 PRO B 200 17 -0.42
CISPEP 35 GLU B 108 PRO B 109 18 -0.50
CISPEP 36 LYS B 199 PRO B 200 18 -0.21
CISPEP 37 GLU B 108 PRO B 109 19 -0.55
CISPEP 38 LYS B 199 PRO B 200 19 -0.05
CISPEP 39 GLU B 108 PRO B 109 20 -0.29
CISPEP 40 LYS B 199 PRO B 200 20 0.15
CISPEP 41 GLU B 108 PRO B 109 21 0.15
CISPEP 42 LYS B 199 PRO B 200 21 -0.33
CISPEP 43 GLU B 108 PRO B 109 22 -0.51
CISPEP 44 LYS B 199 PRO B 200 22 0.16
CISPEP 45 GLU B 108 PRO B 109 23 -0.46
CISPEP 46 LYS B 199 PRO B 200 23 0.05
CISPEP 47 GLU B 108 PRO B 109 24 -0.24
CISPEP 48 LYS B 199 PRO B 200 24 -0.22
CISPEP 49 GLU B 108 PRO B 109 25 -0.10
CISPEP 50 LYS B 199 PRO B 200 25 0.11
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 - r 2 2 Bytes