Header list of 1e1u.pdb file
Complete list - r 25 2 Bytes
HEADER PRION PROTEIN 11-MAY-00 1E1U
TITLE HUMAN PRION PROTEIN VARIANT R220K
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PRION PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GLOBULAR DOMAIN 125-228;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PRION PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR L.CALZOLAI,D.A.LYSEK,P.GUNTERT,C.VON SCHROETTER,R.ZAHN,
AUTHOR 2 R.RIEK,K.WUTHRICH
REVDAT 2 24-FEB-09 1E1U 1 VERSN
REVDAT 1 20-JUL-00 1E1U 0
JRNL AUTH L.CALZOLAI,D.A.LYSEK,P.GUNTERT,C.VON SCHROETTER,
JRNL AUTH 2 R.ZAHN,R.RIEK,K.WUTHRICH
JRNL TITL NMR STRUCTURES OF THREE SINGLE-RESIDUE VARIANTS OF
JRNL TITL 2 THE HUMAN PRION PROTEIN
JRNL REF PROC.NATL.ACAD.SCI.USA V. 97 8340 2000
JRNL REFN ISSN 0027-8424
JRNL PMID 10900000
JRNL DOI 10.1073/PNAS.97.15.8340
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : OPALP
REMARK 3 AUTHORS : R.KORADI,M.BILLETER,P.GUNTERT
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1E1U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-MAY-00.
REMARK 100 THE PDBE ID CODE IS EBI-4936.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 4.5
REMARK 210 IONIC STRENGTH : 50 MM SODIUM ACETATE
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 750
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 7
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 400
REMARK 400 COMPOUND
REMARK 400 CHAIN A ENGINEERED MUTATION ARG220LYS
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 ARG A 151 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 7 TYR A 157 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 8 TYR A 163 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 9 CYS A 179 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 15 CYS A 179 CA - CB - SG 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 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 SER A 135 -143.61 46.65
REMARK 500 1 ASN A 153 32.45 -96.16
REMARK 500 1 MET A 166 108.69 -57.76
REMARK 500 1 GLU A 168 -166.86 55.87
REMARK 500 1 TYR A 169 41.67 33.78
REMARK 500 1 ASN A 171 -93.90 -152.11
REMARK 500 1 GLN A 172 -102.05 -89.82
REMARK 500 1 GLU A 219 24.74 -67.08
REMARK 500 1 LYS A 220 -92.34 -122.25
REMARK 500 1 TYR A 226 56.73 -99.10
REMARK 500 1 GLN A 227 -57.41 -124.44
REMARK 500 2 ILE A 138 76.27 48.93
REMARK 500 2 MET A 166 84.84 -69.77
REMARK 500 2 ASP A 167 -53.31 -148.87
REMARK 500 2 PHE A 198 109.92 48.97
REMARK 500 2 LYS A 220 -34.67 -132.64
REMARK 500 2 GLN A 227 -43.49 -132.05
REMARK 500 3 ARG A 136 106.30 -36.23
REMARK 500 3 ILE A 138 73.28 51.75
REMARK 500 3 HIS A 140 98.03 -67.60
REMARK 500 3 ASP A 167 69.35 -150.18
REMARK 500 3 GLU A 168 -50.43 -158.74
REMARK 500 3 TYR A 169 -36.62 -156.57
REMARK 500 3 SER A 170 159.37 56.46
REMARK 500 3 ASN A 171 147.00 154.96
REMARK 500 3 PHE A 198 179.83 56.10
REMARK 500 3 GLU A 221 -178.90 -69.97
REMARK 500 3 SER A 222 -37.30 72.68
REMARK 500 3 GLN A 227 3.27 50.16
REMARK 500 4 TYR A 128 -175.14 56.06
REMARK 500 4 ARG A 136 95.36 65.71
REMARK 500 4 ILE A 138 102.21 60.15
REMARK 500 4 MET A 166 81.79 -64.01
REMARK 500 4 ASP A 167 -36.52 -164.15
REMARK 500 4 ASN A 171 100.59 82.19
REMARK 500 4 PHE A 198 -176.43 61.07
REMARK 500 5 ILE A 138 104.97 67.48
REMARK 500 5 ASN A 159 -11.59 -147.38
REMARK 500 5 GLU A 168 -137.60 -129.34
REMARK 500 5 GLU A 221 -3.46 50.43
REMARK 500 6 ALA A 133 22.04 -75.07
REMARK 500 6 MET A 134 -167.81 37.11
REMARK 500 6 ILE A 138 -86.01 55.53
REMARK 500 6 ILE A 139 114.53 81.20
REMARK 500 6 MET A 166 45.74 -80.87
REMARK 500 6 GLN A 172 -101.04 -96.58
REMARK 500 6 GLU A 219 -66.08 -105.03
REMARK 500 6 TYR A 226 23.28 -79.54
REMARK 500 7 TYR A 128 -164.09 49.98
REMARK 500 7 ARG A 136 76.00 60.81
REMARK 500 7 HIS A 140 78.64 -103.58
REMARK 500 7 GLU A 168 -63.65 154.49
REMARK 500 7 GLU A 219 -66.65 -105.32
REMARK 500 7 TYR A 226 54.66 -103.53
REMARK 500 8 SER A 135 -171.47 64.45
REMARK 500 8 ILE A 138 131.02 64.62
REMARK 500 8 TYR A 163 -169.00 -169.58
REMARK 500 8 MET A 166 91.33 -63.48
REMARK 500 8 ASP A 167 32.27 -168.06
REMARK 500 8 GLU A 168 -69.55 -141.41
REMARK 500 8 ASN A 171 103.04 86.30
REMARK 500 8 LYS A 220 -58.52 -136.03
REMARK 500 9 ARG A 136 95.18 65.36
REMARK 500 9 ILE A 138 -56.47 70.07
REMARK 500 9 ILE A 139 151.99 63.83
REMARK 500 9 MET A 166 105.74 -56.81
REMARK 500 9 ASP A 167 111.07 -165.74
REMARK 500 9 GLU A 168 166.61 65.68
REMARK 500 9 TYR A 169 12.42 42.15
REMARK 500 9 SER A 170 98.65 -47.30
REMARK 500 10 TYR A 128 -168.62 54.47
REMARK 500 10 SER A 132 -156.25 -141.49
REMARK 500 10 ILE A 138 124.62 66.70
REMARK 500 10 ASP A 167 -36.12 -157.12
REMARK 500 10 GLU A 168 -55.35 -121.46
REMARK 500 10 GLN A 172 -98.58 -81.84
REMARK 500 10 LYS A 220 -105.96 -119.34
REMARK 500 11 ARG A 136 107.55 -56.54
REMARK 500 11 MET A 166 74.52 24.57
REMARK 500 11 ASP A 167 -80.83 -57.86
REMARK 500 11 GLU A 168 -60.11 -160.15
REMARK 500 11 SER A 170 0.90 51.08
REMARK 500 11 GLU A 219 17.59 -65.94
REMARK 500 11 GLU A 221 -58.61 -127.09
REMARK 500 11 GLN A 227 43.18 -102.75
REMARK 500 12 TYR A 128 -176.23 53.56
REMARK 500 12 ARG A 136 106.86 -32.97
REMARK 500 12 ASP A 167 -3.13 -145.28
REMARK 500 12 GLU A 168 -4.83 -140.62
REMARK 500 12 TYR A 169 -70.53 -133.68
REMARK 500 12 SER A 170 76.52 37.63
REMARK 500 12 GLN A 172 -101.87 -102.00
REMARK 500 12 GLU A 219 26.07 -74.69
REMARK 500 13 ILE A 139 -7.67 59.31
REMARK 500 13 HIS A 140 173.57 50.03
REMARK 500 13 MET A 154 -7.29 -57.53
REMARK 500 13 PRO A 165 92.29 -68.18
REMARK 500 13 MET A 166 56.07 39.23
REMARK 500 13 GLU A 168 -52.79 -156.81
REMARK 500 13 GLN A 172 -92.72 -90.56
REMARK 500 13 GLU A 219 6.58 -65.16
REMARK 500 13 LYS A 220 -46.91 -131.32
REMARK 500 14 SER A 132 -106.98 -79.08
REMARK 500 14 ARG A 136 89.62 57.39
REMARK 500 14 ILE A 138 122.10 65.97
REMARK 500 14 MET A 166 -35.79 58.06
REMARK 500 14 ASP A 167 -75.60 50.94
REMARK 500 14 GLU A 168 -65.09 -161.59
REMARK 500 14 GLU A 219 6.44 -66.90
REMARK 500 14 LYS A 220 -84.59 -106.91
REMARK 500 15 SER A 132 -106.72 36.53
REMARK 500 15 ILE A 139 177.46 54.40
REMARK 500 15 ARG A 156 -30.97 -171.70
REMARK 500 15 MET A 166 -164.74 -68.41
REMARK 500 15 ASP A 167 -66.73 90.24
REMARK 500 15 GLN A 172 -89.23 -108.47
REMARK 500 15 PHE A 198 109.07 -38.09
REMARK 500 15 GLU A 219 43.77 -76.35
REMARK 500 16 ARG A 136 104.31 -25.40
REMARK 500 16 ILE A 139 107.63 55.96
REMARK 500 16 MET A 154 -35.28 -39.17
REMARK 500 16 GLU A 168 -76.81 62.06
REMARK 500 16 SER A 170 8.64 50.72
REMARK 500 16 GLU A 219 33.35 -72.04
REMARK 500 16 GLU A 221 -28.88 -143.96
REMARK 500 16 GLN A 227 32.62 -83.18
REMARK 500 17 MET A 134 55.85 -160.62
REMARK 500 17 SER A 135 -134.21 44.71
REMARK 500 17 ILE A 138 89.14 54.35
REMARK 500 17 MET A 166 73.50 38.96
REMARK 500 17 GLU A 168 128.89 73.19
REMARK 500 17 TYR A 169 136.06 47.23
REMARK 500 17 GLN A 172 -81.62 -87.49
REMARK 500 17 GLU A 221 27.92 -142.00
REMARK 500 17 SER A 222 -57.91 -123.49
REMARK 500 18 SER A 132 -165.64 -172.28
REMARK 500 18 ALA A 133 -169.85 -102.94
REMARK 500 18 ILE A 138 -73.63 64.46
REMARK 500 18 ILE A 139 165.89 62.60
REMARK 500 18 GLU A 168 -115.29 -152.31
REMARK 500 18 SER A 170 163.15 54.86
REMARK 500 18 GLN A 172 -93.75 -77.51
REMARK 500 18 LYS A 220 -73.77 -78.23
REMARK 500 19 MET A 166 97.63 -67.97
REMARK 500 19 ASP A 167 -52.17 -157.17
REMARK 500 19 GLN A 172 -101.44 -81.65
REMARK 500 19 GLU A 221 -73.45 35.25
REMARK 500 20 MET A 134 44.26 -143.08
REMARK 500 20 SER A 135 -172.47 54.83
REMARK 500 20 ILE A 138 77.75 58.12
REMARK 500 20 MET A 166 -93.09 -67.54
REMARK 500 20 ASP A 167 14.23 50.89
REMARK 500 20 GLU A 168 -85.06 -146.40
REMARK 500 20 SER A 170 146.50 55.00
REMARK 500 20 ASN A 171 -173.31 -170.05
REMARK 500 20 GLN A 172 -86.55 -86.00
REMARK 500 20 PHE A 198 -173.56 53.60
REMARK 500 20 GLU A 221 -77.18 52.62
REMARK 500 20 GLN A 227 43.89 36.72
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 MET A 134 SER A 135 6 145.96
REMARK 500 TYR A 226 GLN A 227 10 -148.55
REMARK 500 GLY A 131 SER A 132 15 -149.46
REMARK 500 ASN A 153 MET A 154 17 -145.82
REMARK 500 ASP A 167 GLU A 168 18 138.88
REMARK 500 SER A 170 ASN A 171 20 139.87
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 208 0.10 SIDE CHAIN
REMARK 500 2 ARG A 148 0.11 SIDE CHAIN
REMARK 500 2 TYR A 149 0.07 SIDE CHAIN
REMARK 500 2 TYR A 150 0.07 SIDE CHAIN
REMARK 500 2 ARG A 156 0.11 SIDE CHAIN
REMARK 500 2 TYR A 226 0.10 SIDE CHAIN
REMARK 500 3 ARG A 136 0.08 SIDE CHAIN
REMARK 500 3 ARG A 148 0.11 SIDE CHAIN
REMARK 500 3 TYR A 149 0.07 SIDE CHAIN
REMARK 500 3 TYR A 226 0.07 SIDE CHAIN
REMARK 500 5 TYR A 128 0.12 SIDE CHAIN
REMARK 500 6 ARG A 136 0.09 SIDE CHAIN
REMARK 500 6 ARG A 148 0.08 SIDE CHAIN
REMARK 500 6 ARG A 208 0.09 SIDE CHAIN
REMARK 500 8 ARG A 164 0.13 SIDE CHAIN
REMARK 500 9 TYR A 128 0.10 SIDE CHAIN
REMARK 500 9 ARG A 136 0.12 SIDE CHAIN
REMARK 500 9 TYR A 145 0.06 SIDE CHAIN
REMARK 500 9 TYR A 226 0.11 SIDE CHAIN
REMARK 500 9 ARG A 228 0.08 SIDE CHAIN
REMARK 500 10 ARG A 228 0.13 SIDE CHAIN
REMARK 500 11 TYR A 145 0.08 SIDE CHAIN
REMARK 500 11 ARG A 148 0.08 SIDE CHAIN
REMARK 500 12 ARG A 136 0.08 SIDE CHAIN
REMARK 500 12 ARG A 156 0.08 SIDE CHAIN
REMARK 500 12 TYR A 162 0.07 SIDE CHAIN
REMARK 500 12 ARG A 228 0.08 SIDE CHAIN
REMARK 500 13 ARG A 228 0.08 SIDE CHAIN
REMARK 500 14 ARG A 208 0.10 SIDE CHAIN
REMARK 500 15 ARG A 151 0.09 SIDE CHAIN
REMARK 500 16 TYR A 145 0.07 SIDE CHAIN
REMARK 500 16 TYR A 149 0.08 SIDE CHAIN
REMARK 500 16 TYR A 150 0.07 SIDE CHAIN
REMARK 500 17 ARG A 148 0.08 SIDE CHAIN
REMARK 500 18 TYR A 128 0.07 SIDE CHAIN
REMARK 500 18 TYR A 145 0.07 SIDE CHAIN
REMARK 500 18 TYR A 163 0.08 SIDE CHAIN
REMARK 500 19 TYR A 150 0.10 SIDE CHAIN
REMARK 500 20 TYR A 149 0.08 SIDE CHAIN
REMARK 500 20 ARG A 156 0.15 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E1G RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN VARIANT M166V
REMARK 900 RELATED ID: 1E1P RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN VARIANT S170N
REMARK 900 RELATED ID: 1E1S RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN VARIANT S170N
REMARK 900 RELATED ID: 1E1J RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN VARIANT M166V
REMARK 900 RELATED ID: 1E1W RELATED DB: PDB
REMARK 900 HUMAN PRION PROTEIN VARIANT R220K
DBREF 1E1U A 125 228 UNP P78446 P78446 118 221
SEQADV 1E1U LYS A 220 UNP P78446 ARG 213 ENGINEERED MUTATION
SEQRES 1 A 104 LEU GLY GLY TYR MET LEU GLY SER ALA MET SER ARG PRO
SEQRES 2 A 104 ILE ILE HIS PHE GLY SER ASP TYR GLU ASP ARG TYR TYR
SEQRES 3 A 104 ARG GLU ASN MET HIS ARG TYR PRO ASN GLN VAL TYR TYR
SEQRES 4 A 104 ARG PRO MET ASP GLU TYR SER ASN GLN ASN ASN PHE VAL
SEQRES 5 A 104 HIS ASP CYS VAL ASN ILE THR ILE LYS GLN HIS THR VAL
SEQRES 6 A 104 THR THR THR THR LYS GLY GLU ASN PHE THR GLU THR ASP
SEQRES 7 A 104 VAL LYS MET MET GLU ARG VAL VAL GLU GLN MET CYS ILE
SEQRES 8 A 104 THR GLN TYR GLU LYS GLU SER GLN ALA TYR TYR GLN ARG
HELIX 1 H1 ASP A 144 MET A 154 1 11
HELIX 2 H2 ASN A 173 LYS A 194 1 22
HELIX 3 H3 GLU A 200 GLU A 219 1 20
SHEET 1 S1 2 TYR A 128 GLY A 131 0
SHEET 2 S1 2 VAL A 161 ARG A 164 -1 O VAL A 161 N GLY A 131
SSBOND 1 CYS A 179 CYS A 214 1555 1555 2.03
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 25 2 Bytes