Header list of 1m9w.pdb file
Complete list - b 23 2 Bytes
HEADER ELECTRON TRANSPORT 30-JUL-02 1M9W
TITLE STUDY OF ELECTROSTATIC POTENTIAL SURFACE DISTRIBUTION USING HIGH
TITLE 2 RESOLUTION SIDE-CHAIN CONFORMATION DETERMINED BY NMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLASTOCYANIN;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP.;
SOURCE 3 ORGANISM_TAXID: 1143
KEYWDS SIDECHAIN ORIENTATION, CONGEN, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR D.MONLEON,B.CELDA
REVDAT 4 23-FEB-22 1M9W 1 REMARK
REVDAT 3 24-FEB-09 1M9W 1 VERSN
REVDAT 2 25-SEP-02 1M9W 1 AUTHOR
REVDAT 1 14-AUG-02 1M9W 0
JRNL AUTH D.MONLEON,B.CELDA
JRNL TITL STUDY OF ELECTROSTATIC POTENTIAL SURFACE DISTRIBUTION OF
JRNL TITL 2 WILD-TYPE PLASTOCYANIN SYNECHOCYSTIS SOLUTION STRUCTURE
JRNL TITL 3 DETERMINED BY HOMONUCLEAR NMR.
JRNL REF BIOPOLYMERS V. 70 212 2003
JRNL REFN ISSN 0006-3525
JRNL PMID 14517909
JRNL DOI 10.1002/BIP.10472
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CONGEN 2.1.2178
REMARK 3 AUTHORS : BRUCCOLERI
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1M9W COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-AUG-02.
REMARK 100 THE DEPOSITION ID IS D_1000016778.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 303
REMARK 210 PH : 5.4; 5.4
REMARK 210 IONIC STRENGTH : 1; 1
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : PLASTOCYANIN 4MM, 0.5MM TRICINE
REMARK 210 -KOH, 5% D2O, SODIUM DITHIONITE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY; DRX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : GIFA 3.9
REMARK 210 METHOD USED : CONGEN SIMULATED ANNEALING
REMARK 210 RESTRAINED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: 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: 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 OD2 ASP A 49 HH TYR A 79 1.48
REMARK 500 HG SER A 9 OE1 GLU A 17 1.53
REMARK 500 OD2 ASP A 46 HG1 THR A 80 1.58
REMARK 500 HH TYR A 82 OE2 GLU A 84 1.59
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 PHE A 69 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 1 TYR A 79 CB - CG - CD1 ANGL. DEV. = -5.1 DEGREES
REMARK 500 1 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 HIS A 58 C - N - CA ANGL. DEV. = 19.2 DEGREES
REMARK 500 2 PHE A 69 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 2 PHE A 73 CB - CG - CD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 2 PHE A 73 CB - CG - CD1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 2 TYR A 79 CB - CG - CD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 2 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 3 VAL A 5 CA - CB - CG1 ANGL. DEV. = 9.1 DEGREES
REMARK 500 3 PRO A 18 N - CA - C ANGL. DEV. = 16.3 DEGREES
REMARK 500 3 GLU A 28 CA - CB - CG ANGL. DEV. = 15.0 DEGREES
REMARK 500 3 HIS A 39 CB - CG - ND1 ANGL. DEV. = -8.4 DEGREES
REMARK 500 3 PHE A 73 CB - CG - CD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 3 PHE A 73 CB - CG - CD1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 3 TYR A 79 CA - CB - CG ANGL. DEV. = 16.6 DEGREES
REMARK 500 3 TYR A 79 CB - CG - CD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 4 ALA A 62 CB - CA - C ANGL. DEV. = 11.3 DEGREES
REMARK 500 4 PHE A 69 CB - CG - CD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 4 PHE A 69 CB - CG - CD1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 4 PHE A 73 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 4 TYR A 79 CB - CG - CD1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 5 HIS A 39 CA - CB - CG ANGL. DEV. = 11.7 DEGREES
REMARK 500 5 HIS A 58 C - N - CA ANGL. DEV. = 16.7 DEGREES
REMARK 500 5 PHE A 69 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 5 PHE A 73 CB - CG - CD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 5 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 5 GLU A 98 C - N - CA ANGL. DEV. = 15.8 DEGREES
REMARK 500 6 PHE A 73 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 6 TYR A 79 CB - CG - CD1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 6 ARG A 87 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 6 VAL A 97 CA - CB - CG2 ANGL. DEV. = 9.5 DEGREES
REMARK 500 7 HIS A 39 CB - CG - CD2 ANGL. DEV. = -10.1 DEGREES
REMARK 500 7 PHE A 69 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 7 TYR A 79 CB - CG - CD1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 7 TYR A 81 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 8 TRP A 31 CA - CB - CG ANGL. DEV. = 13.7 DEGREES
REMARK 500 8 HIS A 39 CB - CG - CD2 ANGL. DEV. = -10.6 DEGREES
REMARK 500 8 PHE A 73 CB - CG - CD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 8 PHE A 73 CB - CG - CD1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 8 TYR A 79 CB - CG - CD2 ANGL. DEV. = 4.4 DEGREES
REMARK 500 8 TYR A 79 CB - CG - CD1 ANGL. DEV. = -7.0 DEGREES
REMARK 500 9 HIS A 39 CB - CG - CD2 ANGL. DEV. = -10.4 DEGREES
REMARK 500 9 ASN A 40 N - CA - CB ANGL. DEV. = -11.2 DEGREES
REMARK 500 9 PHE A 69 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 9 PHE A 73 CB - CG - CD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 9 PHE A 73 CB - CG - CD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 9 TYR A 79 CA - CB - CG ANGL. DEV. = 16.4 DEGREES
REMARK 500 9 TYR A 79 CB - CG - CD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 10 HIS A 58 C - N - CA ANGL. DEV. = 15.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 55 ANGLE DEVIATIONS.
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 2 96.47 13.51
REMARK 500 1 LEU A 14 65.28 -68.23
REMARK 500 1 ALA A 25 99.67 -11.59
REMARK 500 1 LYS A 30 52.51 -104.77
REMARK 500 1 LEU A 36 51.33 38.22
REMARK 500 1 SER A 37 151.39 -48.86
REMARK 500 1 ALA A 45 39.75 72.67
REMARK 500 1 THR A 52 1.49 -63.40
REMARK 500 1 SER A 57 154.40 150.74
REMARK 500 1 HIS A 58 15.05 -69.77
REMARK 500 1 LYS A 59 -18.04 -145.03
REMARK 500 2 ASN A 2 77.85 50.40
REMARK 500 2 LEU A 14 64.17 -67.42
REMARK 500 2 ALA A 25 84.20 -61.66
REMARK 500 2 LEU A 36 -66.32 74.22
REMARK 500 2 SER A 37 147.88 66.22
REMARK 500 2 ALA A 45 70.82 63.67
REMARK 500 2 SER A 57 99.12 66.32
REMARK 500 2 HIS A 58 5.32 24.82
REMARK 500 2 LYS A 59 -12.40 -154.72
REMARK 500 2 THR A 72 89.11 -151.38
REMARK 500 3 ASN A 2 91.85 4.16
REMARK 500 3 LEU A 14 70.28 -66.19
REMARK 500 3 ALA A 45 70.11 79.93
REMARK 500 3 SER A 68 172.08 70.27
REMARK 500 4 ASN A 2 78.24 34.47
REMARK 500 4 ALA A 25 87.50 -7.83
REMARK 500 4 GLU A 27 -172.33 -64.19
REMARK 500 4 ASN A 34 -30.95 -147.19
REMARK 500 4 LEU A 36 52.79 37.79
REMARK 500 4 SER A 57 49.44 -1.11
REMARK 500 4 HIS A 58 1.84 50.33
REMARK 500 4 LYS A 59 -11.11 -152.78
REMARK 500 4 THR A 74 52.16 -151.16
REMARK 500 5 ASN A 2 86.92 26.66
REMARK 500 5 LEU A 14 69.70 -69.54
REMARK 500 5 THR A 20 -75.99 -135.04
REMARK 500 5 VAL A 21 160.29 73.29
REMARK 500 5 ALA A 25 100.18 -54.91
REMARK 500 5 LEU A 36 53.33 85.48
REMARK 500 5 ALA A 44 -2.87 -59.15
REMARK 500 5 SER A 57 42.76 -58.11
REMARK 500 5 HIS A 58 -37.01 41.57
REMARK 500 5 THR A 74 44.38 -152.31
REMARK 500 5 PRO A 76 105.35 -51.32
REMARK 500 5 LYS A 94 -62.98 -121.02
REMARK 500 5 VAL A 95 127.94 75.56
REMARK 500 6 ASN A 2 99.03 20.65
REMARK 500 6 LEU A 14 62.90 -67.26
REMARK 500 6 ALA A 25 103.20 -31.16
REMARK 500
REMARK 500 THIS ENTRY HAS 86 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 HIS A 39 0.16 SIDE CHAIN
REMARK 500 1 TYR A 79 0.19 SIDE CHAIN
REMARK 500 1 TYR A 81 0.07 SIDE CHAIN
REMARK 500 1 ARG A 87 0.17 SIDE CHAIN
REMARK 500 2 HIS A 39 0.18 SIDE CHAIN
REMARK 500 2 TYR A 79 0.12 SIDE CHAIN
REMARK 500 3 HIS A 39 0.08 SIDE CHAIN
REMARK 500 3 TYR A 79 0.17 SIDE CHAIN
REMARK 500 3 TYR A 81 0.10 SIDE CHAIN
REMARK 500 4 HIS A 39 0.11 SIDE CHAIN
REMARK 500 4 HIS A 58 0.10 SIDE CHAIN
REMARK 500 4 PHE A 69 0.07 SIDE CHAIN
REMARK 500 4 TYR A 79 0.18 SIDE CHAIN
REMARK 500 4 ARG A 87 0.12 SIDE CHAIN
REMARK 500 5 HIS A 39 0.08 SIDE CHAIN
REMARK 500 5 TYR A 79 0.19 SIDE CHAIN
REMARK 500 5 TYR A 81 0.10 SIDE CHAIN
REMARK 500 6 HIS A 39 0.16 SIDE CHAIN
REMARK 500 6 TYR A 79 0.22 SIDE CHAIN
REMARK 500 6 TYR A 81 0.07 SIDE CHAIN
REMARK 500 7 HIS A 39 0.17 SIDE CHAIN
REMARK 500 7 TYR A 81 0.10 SIDE CHAIN
REMARK 500 8 HIS A 39 0.15 SIDE CHAIN
REMARK 500 8 TYR A 79 0.09 SIDE CHAIN
REMARK 500 9 HIS A 39 0.20 SIDE CHAIN
REMARK 500 9 TYR A 79 0.14 SIDE CHAIN
REMARK 500 9 TYR A 81 0.12 SIDE CHAIN
REMARK 500 10 HIS A 39 0.16 SIDE CHAIN
REMARK 500 10 TYR A 79 0.27 SIDE CHAIN
REMARK 500 10 TYR A 81 0.08 SIDE CHAIN
REMARK 500 10 ARG A 87 0.12 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1M9W A 1 98 UNP P21697 PLAS_SYNY3 29 126
SEQRES 1 A 98 ALA ASN ALA THR VAL LYS MET GLY SER ASP SER GLY ALA
SEQRES 2 A 98 LEU VAL PHE GLU PRO SER THR VAL THR ILE LYS ALA GLY
SEQRES 3 A 98 GLU GLU VAL LYS TRP VAL ASN ASN LYS LEU SER PRO HIS
SEQRES 4 A 98 ASN ILE VAL PHE ALA ALA ASP GLY VAL ASP ALA ASP THR
SEQRES 5 A 98 ALA ALA LYS LEU SER HIS LYS GLY LEU ALA PHE ALA ALA
SEQRES 6 A 98 GLY GLU SER PHE THR SER THR PHE THR GLU PRO GLY THR
SEQRES 7 A 98 TYR THR TYR TYR CYS GLU PRO HIS ARG GLY ALA GLY MET
SEQRES 8 A 98 VAL GLY LYS VAL VAL VAL GLU
HELIX 1 1 ALA A 50 ALA A 54 5 5
HELIX 2 2 GLU A 84 GLY A 90 5 7
SHEET 1 A 3 PHE A 16 GLU A 17 0
SHEET 2 A 3 LYS A 6 MET A 7 -1 N LYS A 6 O GLU A 17
SHEET 3 A 3 VAL A 32 ASN A 33 1 O VAL A 32 N MET A 7
SHEET 1 B 4 THR A 20 ILE A 23 0
SHEET 2 B 4 VAL A 92 VAL A 97 1 O VAL A 96 N ILE A 23
SHEET 3 B 4 THR A 78 TYR A 82 -1 N TYR A 79 O VAL A 95
SHEET 4 B 4 VAL A 42 PHE A 43 -1 N VAL A 42 O TYR A 82
SHEET 1 C 2 GLU A 28 VAL A 29 0
SHEET 2 C 2 SER A 71 THR A 72 -1 O SER A 71 N VAL A 29
CISPEP 1 GLU A 17 PRO A 18 1 -2.14
CISPEP 2 SER A 37 PRO A 38 1 -2.02
CISPEP 3 GLU A 17 PRO A 18 2 -2.09
CISPEP 4 SER A 37 PRO A 38 2 -2.22
CISPEP 5 GLU A 17 PRO A 18 3 -2.10
CISPEP 6 SER A 37 PRO A 38 3 -1.97
CISPEP 7 GLU A 17 PRO A 18 4 -2.10
CISPEP 8 SER A 37 PRO A 38 4 -2.04
CISPEP 9 GLU A 17 PRO A 18 5 -2.29
CISPEP 10 SER A 37 PRO A 38 5 0.69
CISPEP 11 GLU A 17 PRO A 18 6 -2.04
CISPEP 12 SER A 37 PRO A 38 6 0.44
CISPEP 13 GLU A 17 PRO A 18 7 -2.08
CISPEP 14 SER A 37 PRO A 38 7 -2.21
CISPEP 15 GLU A 17 PRO A 18 8 -2.07
CISPEP 16 SER A 37 PRO A 38 8 2.04
CISPEP 17 GLU A 17 PRO A 18 9 -2.18
CISPEP 18 SER A 37 PRO A 38 9 -1.92
CISPEP 19 GLU A 17 PRO A 18 10 2.76
CISPEP 20 SER A 37 PRO A 38 10 -2.14
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 - b 23 2 Bytes