Header list of 1dwz.pdb file
Complete list - r 25 2 Bytes
HEADER PRION PROTEIN 15-DEC-99 1DWZ TITLE BOVINE PRION PROTEIN FRAGMENT 121-230 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PRION PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 121-230; COMPND 5 SYNONYM: PRP, MAJOR PRION PROTEIN; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: BOVINE; SOURCE 4 ORGANISM_TAXID: 9913; SOURCE 5 ORGAN: BRAIN; SOURCE 6 CELLULAR_LOCATION: EXTRACELLULAR; SOURCE 7 GENE: PRNP; SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 11 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM; SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PRSET A KEYWDS PRION PROTEIN, PRION, BRAIN, REPEAT EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR F.LOPEZ-GARCIA,R.ZAHN,R.RIEK,M.BILLETER,K.WUTHRICH REVDAT 5 24-FEB-09 1DWZ 1 VERSN REVDAT 4 04-APR-05 1DWZ 1 ATOM REVDAT 3 27-FEB-04 1DWZ 1 SSBOND ATOM CONECT REVDAT 2 26-FEB-02 1DWZ 1 JRNL REMARK MODEL REVDAT 1 20-JUL-00 1DWZ 0 REVDAT 1 13-FEB-07 1DWZ 0 JRNL AUTH F.LOPEZ-GARCIA,R.ZAHN,R.RIEK,K.WUTHRICH JRNL TITL NMR STRUCTURE OF THE BOVINE PRION PROTEIN JRNL REF PROC.NATL.ACAD.SCI.USA V. 97 8334 2000 JRNL REFN ISSN 0027-8424 JRNL PMID 10899999 JRNL DOI 10.1073/PNAS.97.15.8334 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : OPALP REMARK 3 AUTHORS : KORADI, BILLETER,GUNTERT REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1DWZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-DEC-99. REMARK 100 THE PDBE ID CODE IS EBI-4473. 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 : 0.01 REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 90% WATER/10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 750 REMARK 210 SPECTROMETER MODEL : DRX750 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 : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 9 REMARK 210 REMARK 210 REMARK: CLOSEST TO THE MEAN REMARK 210 (BACKBONE HEAVY ATOMS OF RESIDUES 125-227). THE STRUCTURE REMARK 210 WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON REMARK 210 13C, 15N-LABELED PROTEIN 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 THE PDB ENTRIES 1DWY, 1DWZ, 1DX0 AND 1DX1 FORM REMARK 400 A SET OF STRUCTURE DETERMINATIONS AS: REMARK 400 1DWY THE MINIMIZED CONFORMER CLOSEST TO THE MEAN REMARK 400 OF THE FRAGMENT BPRP(121-230) (ONLY SUBMITTED REMARK 400 RESIDUES 124-227) REMARK 400 1DWZ 20 MINIMIZED CONFORMERS OF THE FRAGMENT BPRP(121-230) REMARK 400 (ONLY SUBMITTED RESIDUES 124-227) REMARK 400 1DX0 THE MINIMIZED CONFORMER CLOSEST TO THE MEAN OF REMARK 400 THE FULL LENGTH BPRP(23-230) (ONLY SUBMITTED RESIDUES REMARK 400 124-227) REMARK 400 1DX1 20 MINIMIZED CONFORMERS OF THE FULL LENGTH BPRP(23-230) REMARK 400 (ONLY SUBMITTED RESIDUES 124-227) REMARK 400 REMARK 400 THE SEQUENCE NUMBERING GIVEN IN THESE ENTRIES IS THAT REMARK 400 FOR HUMAN PRION PROTEIN (RATHER THAN SEQUENTIAL) BASED REMARK 400 ON SEQUENCE ALIGNMENT. REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 119 REMARK 465 SER A 120 REMARK 465 VAL A 121 REMARK 465 VAL A 122 REMARK 465 GLY A 123 REMARK 465 ARG A 228 REMARK 465 GLY A 229 REMARK 465 ALA A 230 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT 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 GLU A 186 - HG1 THR A 190 1.60 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 1 ARG A 164 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 6 ARG A 151 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 8 TYR A 150 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES REMARK 500 11 ARG A 136 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES REMARK 500 12 ARG A 136 CD - NE - CZ ANGL. DEV. = 10.1 DEGREES REMARK 500 19 TYR A 157 CB - CG - CD2 ANGL. DEV. = -4.1 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 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 GLN A 172 -92.68 -80.21 REMARK 500 1 TYR A 226 -71.02 -69.99 REMARK 500 2 MET A 154 -65.95 -24.96 REMARK 500 2 GLN A 168 -40.36 79.24 REMARK 500 2 ASN A 171 -166.23 52.73 REMARK 500 2 GLN A 172 -80.78 -122.57 REMARK 500 3 GLN A 168 -150.07 -78.91 REMARK 500 3 ASN A 171 -170.78 50.50 REMARK 500 3 GLN A 172 -77.14 -121.39 REMARK 500 4 TYR A 150 -72.52 -73.63 REMARK 500 4 ASP A 167 94.57 -62.87 REMARK 500 4 GLN A 168 171.92 62.50 REMARK 500 4 TYR A 169 -26.11 62.69 REMARK 500 4 ASN A 171 -163.23 54.16 REMARK 500 4 HIS A 187 -71.42 -55.03 REMARK 500 4 THR A 199 -153.29 -128.73 REMARK 500 5 TYR A 150 -75.12 -67.72 REMARK 500 5 GLN A 168 -21.62 74.16 REMARK 500 6 SER A 132 -169.40 -161.58 REMARK 500 6 VAL A 166 -75.94 -69.64 REMARK 500 6 ASP A 167 80.30 33.97 REMARK 500 6 GLN A 168 -133.99 81.00 REMARK 500 6 SER A 170 -65.92 -146.86 REMARK 500 6 ASN A 171 -168.01 58.02 REMARK 500 7 TYR A 128 -172.74 38.04 REMARK 500 7 MET A 154 -59.69 -25.43 REMARK 500 7 GLN A 168 -35.73 68.87 REMARK 500 7 SER A 170 170.66 60.47 REMARK 500 7 ASN A 171 166.88 88.43 REMARK 500 8 ASP A 167 32.71 -76.97 REMARK 500 8 GLN A 168 -44.79 -147.74 REMARK 500 8 TYR A 169 67.71 -150.42 REMARK 500 8 ARG A 220 -75.30 -56.78 REMARK 500 9 GLN A 168 -20.26 71.41 REMARK 500 10 MET A 154 -67.21 -24.67 REMARK 500 10 ASP A 167 -148.95 -87.76 REMARK 500 10 TYR A 169 82.76 48.75 REMARK 500 10 SER A 170 -90.17 -118.15 REMARK 500 10 ASN A 171 123.89 60.83 REMARK 500 11 SER A 132 -163.88 48.90 REMARK 500 11 GLN A 168 -57.92 71.35 REMARK 500 11 SER A 170 37.00 -71.80 REMARK 500 12 GLN A 168 -34.52 83.28 REMARK 500 12 GLN A 172 -81.39 -121.41 REMARK 500 13 TYR A 150 -74.43 -63.63 REMARK 500 13 ASP A 167 -92.43 51.08 REMARK 500 13 ASN A 171 135.98 82.10 REMARK 500 14 VAL A 189 -64.62 -95.42 REMARK 500 15 TYR A 128 -170.84 36.14 REMARK 500 15 GLN A 168 -40.98 -140.66 REMARK 500 16 SER A 132 -164.89 64.41 REMARK 500 16 TYR A 169 29.50 41.27 REMARK 500 16 SER A 170 98.88 -33.57 REMARK 500 16 THR A 188 -70.36 -64.13 REMARK 500 16 THR A 193 -6.32 -59.56 REMARK 500 17 ALA A 133 141.58 -38.09 REMARK 500 17 TYR A 150 -73.67 -66.40 REMARK 500 17 GLN A 168 -71.80 -71.02 REMARK 500 17 ASN A 171 117.70 95.37 REMARK 500 18 TYR A 128 -156.03 39.88 REMARK 500 18 GLN A 168 -54.76 76.35 REMARK 500 18 SER A 170 -169.81 -74.26 REMARK 500 18 ASN A 171 177.38 71.30 REMARK 500 19 SER A 132 -165.52 60.13 REMARK 500 19 ARG A 151 -68.67 -94.98 REMARK 500 20 GLN A 168 -44.09 61.65 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 171 GLN A 172 2 141.67 REMARK 500 ASN A 153 MET A 154 17 -147.53 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 151 0.12 SIDE CHAIN REMARK 500 1 ARG A 156 0.12 SIDE CHAIN REMARK 500 2 TYR A 128 0.07 SIDE CHAIN REMARK 500 2 TYR A 157 0.08 SIDE CHAIN REMARK 500 2 ARG A 164 0.17 SIDE CHAIN REMARK 500 2 PHE A 175 0.09 SIDE CHAIN REMARK 500 2 ARG A 208 0.09 SIDE CHAIN REMARK 500 3 ARG A 136 0.08 SIDE CHAIN REMARK 500 3 ARG A 148 0.12 SIDE CHAIN REMARK 500 3 TYR A 157 0.10 SIDE CHAIN REMARK 500 3 PHE A 175 0.10 SIDE CHAIN REMARK 500 3 ARG A 208 0.09 SIDE CHAIN REMARK 500 4 ARG A 148 0.12 SIDE CHAIN REMARK 500 4 TYR A 157 0.09 SIDE CHAIN REMARK 500 4 ARG A 164 0.09 SIDE CHAIN REMARK 500 5 TYR A 128 0.07 SIDE CHAIN REMARK 500 5 ARG A 156 0.08 SIDE CHAIN REMARK 500 5 TYR A 157 0.07 SIDE CHAIN REMARK 500 5 ARG A 208 0.10 SIDE CHAIN REMARK 500 5 TYR A 226 0.07 SIDE CHAIN REMARK 500 6 TYR A 157 0.11 SIDE CHAIN REMARK 500 7 ARG A 164 0.08 SIDE CHAIN REMARK 500 8 TYR A 157 0.09 SIDE CHAIN REMARK 500 9 ARG A 151 0.10 SIDE CHAIN REMARK 500 9 TYR A 163 0.10 SIDE CHAIN REMARK 500 10 TYR A 128 0.07 SIDE CHAIN REMARK 500 10 PHE A 175 0.10 SIDE CHAIN REMARK 500 11 TYR A 157 0.10 SIDE CHAIN REMARK 500 11 ARG A 220 0.08 SIDE CHAIN REMARK 500 12 TYR A 128 0.07 SIDE CHAIN REMARK 500 12 ARG A 156 0.09 SIDE CHAIN REMARK 500 12 TYR A 157 0.12 SIDE CHAIN REMARK 500 12 PHE A 175 0.08 SIDE CHAIN REMARK 500 12 ARG A 208 0.11 SIDE CHAIN REMARK 500 12 ARG A 220 0.10 SIDE CHAIN REMARK 500 12 TYR A 225 0.07 SIDE CHAIN REMARK 500 13 ARG A 148 0.07 SIDE CHAIN REMARK 500 13 ARG A 156 0.11 SIDE CHAIN REMARK 500 13 TYR A 157 0.08 SIDE CHAIN REMARK 500 14 TYR A 128 0.10 SIDE CHAIN REMARK 500 14 ARG A 156 0.16 SIDE CHAIN REMARK 500 14 TYR A 157 0.10 SIDE CHAIN REMARK 500 15 TYR A 128 0.09 SIDE CHAIN REMARK 500 15 TYR A 149 0.10 SIDE CHAIN REMARK 500 15 TYR A 157 0.07 SIDE CHAIN REMARK 500 16 TYR A 157 0.08 SIDE CHAIN REMARK 500 16 ARG A 164 0.10 SIDE CHAIN REMARK 500 17 TYR A 150 0.07 SIDE CHAIN REMARK 500 17 ARG A 151 0.11 SIDE CHAIN REMARK 500 17 PHE A 175 0.08 SIDE CHAIN REMARK 500 18 ARG A 151 0.10 SIDE CHAIN REMARK 500 18 TYR A 157 0.11 SIDE CHAIN REMARK 500 19 TYR A 128 0.09 SIDE CHAIN REMARK 500 19 TYR A 157 0.07 SIDE CHAIN REMARK 500 19 TYR A 225 0.08 SIDE CHAIN REMARK 500 20 ARG A 151 0.09 SIDE CHAIN REMARK 500 20 TYR A 157 0.09 SIDE CHAIN REMARK 500 20 TYR A 218 0.07 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1DWY RELATED DB: PDB REMARK 900 BOVINE PRION PROTEIN FRAGMENT 121-230 NMR,REPRESENTATIVE REMARK 900 MINIMIZED STRUCTURE REMARK 900 RELATED ID: 1DX0 RELATED DB: PDB REMARK 900 BOVINE PRION PROTEIN NMR, REPRESENTATIVE MINIMIZED STRUCTURE REMARK 900 RELATED ID: 1DX1 RELATED DB: PDB REMARK 900 BOVINE PRION PROTEIN NMR, 20 STRUCTURES REMARK 900 RELATED ID: 1AG2 RELATED DB: PDB REMARK 900 PRION PROTEIN DOMAIN PRP(121-231) FROM MOUSE, NMR, REMARK 900 MINIMIZED AVERAGE STRUCTURE REMARK 900 RELATED ID: 1B10 RELATED DB: PDB REMARK 900 SOLUTION NMR STRUCTURE OF RECOMBINANT SYRIAN HAMSTER PRION REMARK 900 PROTEIN RPRP(90-231), 25 STRUCTURES REMARK 900 RELATED ID: 1QLX RELATED DB: PDB REMARK 900 HUMAN PRION PROTEIN RESIDUES 23-230 NMR, REMARK 900 REPRESENTATIVE STRUCTURE REMARK 900 RELATED ID: 1QM0 RELATED DB: PDB REMARK 900 HUMAN PRION PROTEIN FRAGMENT 90-230 NMR, REMARK 900 REPRESENTATIVE STRUCTURE REMARK 900 RELATED ID: 1QM1 RELATED DB: PDB REMARK 900 HUMAN PRION PROTEIN FRAGMENT 90-230 NMR, 20 STRUCTURES REMARK 900 RELATED ID: 1QM2 RELATED DB: PDB REMARK 900 HUMAN PRION PROTEIN FRAGMENT 121-230 NMR, REMARK 900 REPRESENTATIVE STRUCTURE REMARK 900 RELATED ID: 1QM3 RELATED DB: PDB REMARK 900 HUMAN PRION PROTEIN FRAGMENT 121-230 NMR, 20 STRUCTURES REMARK 999 REMARK 999 SEQUENCE REMARK 999 RESIDUES (GLY SER) INSERTED AT THE N-TERMINUS REMARK 999 GLY A 119 CLONING ARTIFACT REMARK 999 SER A 120 CLONING ARTIFACT DBREF 1DWZ A 119 120 PDB 1DWZ 1DWZ 119 120 DBREF 1DWZ A 121 230 UNP P10279 PRIO_BOVIN 132 241 SEQRES 1 A 112 GLY SER VAL VAL GLY GLY LEU GLY GLY TYR MET LEU GLY SEQRES 2 A 112 SER ALA MET SER ARG PRO LEU ILE HIS PHE GLY SER ASP SEQRES 3 A 112 TYR GLU ASP ARG TYR TYR ARG GLU ASN MET HIS ARG TYR SEQRES 4 A 112 PRO ASN GLN VAL TYR TYR ARG PRO VAL ASP GLN TYR SER SEQRES 5 A 112 ASN GLN ASN ASN PHE VAL HIS ASP CYS VAL ASN ILE THR SEQRES 6 A 112 VAL LYS GLU HIS THR VAL THR THR THR THR LYS GLY GLU SEQRES 7 A 112 ASN PHE THR GLU THR ASP ILE LYS MET MET GLU ARG VAL SEQRES 8 A 112 VAL GLU GLN MET CYS ILE THR GLN TYR GLN ARG GLU SER SEQRES 9 A 112 GLN ALA TYR TYR GLN ARG GLY ALA HELIX 1 H1 ASP A 144 GLU A 152 1 9 HELIX 2 H2 ASN A 173 THR A 192 1 20 HELIX 3 H3 GLU A 200 TYR A 225 1 26 SHEET 1 A 2 TYR A 128 GLY A 131 0 SHEET 2 A 2 VAL A 161 ARG A 164 -1 O TYR A 163 N MET A 129 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