Header list of 2fci.pdb file
Complete list - y 9 2 Bytes
HEADER HYDROLASE 12-DEC-05 2FCI
TITLE STRUCTURAL BASIS FOR THE REQUIREMENT OF TWO PHOSPHOTYROSINES IN
TITLE 2 SIGNALING MEDIATED BY SYK TYROSINE KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DOUBLY PHOSPHORYLATED PEPTIDE DERIVED FROM SYK KINASE
COMPND 3 COMPRISING RESIDUES 338-350;
COMPND 4 CHAIN: B;
COMPND 5 FRAGMENT: PHOSPHOPEPTIDE FROM SYK KINASE;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: C-TERMAINL SH2 DOMAIN FROM PHOSPHOLIPASE C-GAMMA-1
COMPND 9 COMPRISING RESIDUES 663-759;
COMPND 10 CHAIN: A;
COMPND 11 FRAGMENT: C-TERMINAL SH2 DOMAIN;
COMPND 12 SYNONYM: PLC-GAMMA-1, PHOSPHOLIPASE C-GAMMA-1;
COMPND 13 EC: 3.1.4.11;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: PEPTIDE SYNTHESIS;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 6 ORGANISM_COMMON: CATTLE;
SOURCE 7 ORGANISM_TAXID: 9913;
SOURCE 8 GENE: PLCG1;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 12 EXPRESSION_SYSTEM_VARIANT: BL21(DE3);
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PET11D
KEYWDS SH2 DOMAIN, PHOSPHOPEPTIDE, SYK KINASE, PLCGAMMA, PLCC, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 16
MDLTYP MINIMIZED AVERAGE
AUTHOR T.D.GROESCH,F.ZHOU,S.MATTILA,R.L.GEAHLEN,C.B.POST
REVDAT 4 02-MAY-12 2FCI 1 COMPND VERSN
REVDAT 3 24-FEB-09 2FCI 1 VERSN
REVDAT 2 21-FEB-06 2FCI 1 JRNL
REVDAT 1 31-JAN-06 2FCI 0
JRNL AUTH T.D.GROESCH,F.ZHOU,S.MATTILA,R.L.GEAHLEN,C.B.POST
JRNL TITL STRUCTURAL BASIS FOR THE REQUIREMENT OF TWO PHOSPHOTYROSINE
JRNL TITL 2 RESIDUES IN SIGNALING MEDIATED BY SYK TYROSINE KINASE
JRNL REF J.MOL.BIOL. V. 356 1222 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16410013
JRNL DOI 10.1016/J.JMB.2005.11.095
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR NIH
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2FCI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-DEC-05.
REMARK 100 THE RCSB ID CODE IS RCSB035715.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 278
REMARK 210 PH : 6.00
REMARK 210 IONIC STRENGTH : 100MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1 MM SH2 DOMAIN, 1 MM PEPTIDE,
REMARK 210 20 MM MES, 100 MM NACL, 3 MM
REMARK 210 TRIS(2-CARBOXYETHYL)-PHOSPHINE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : CBCA(CO)NH; HNCACB; HCCH-TOCSY;
REMARK 210 15N HSQC-TOCSY; 15N HSQC-NOESY;
REMARK 210 C(CO)NH; HC(CO)NH; SINGLE X-
REMARK 210 FILETED NOESY; DOUBLE X-FILTERED
REMARK 210 NOESY; DOUBLE X-FILTERED TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR NIH
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : LACK OF NOE VIOLATIONS & CORRECT
REMARK 210 MAIN CHAIN GEOMETRY
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 OE1 GLU A 85 HZ3 LYS A 86 1.36
REMARK 500 O ASP B 12 HH TYR A 84 1.40
REMARK 500 O TYR A 45 H VAL A 60 1.42
REMARK 500 O VAL A 28 HH21 ARG A 50 1.44
REMARK 500 O LEU A 35 H SER A 48 1.50
REMARK 500 O GLN A 61 H MET A 68 1.51
REMARK 500 O GLU A 22 H MET A 26 1.52
REMARK 500 HE ARG A 39 OG SER A 44 1.52
REMARK 500 O GLU A 63 H GLN A 65 1.55
REMARK 500 O2P PTR B 10 HZ1 LYS A 56 1.55
REMARK 500 O VAL A 78 HG SER A 82 1.56
REMARK 500 H TYR A 45 O VAL A 60 1.56
REMARK 500 O GLU A 101 H SER A 105 1.56
REMARK 500 OE1 GLU A 7 HZ1 LYS A 86 1.58
REMARK 500 O VAL A 78 H SER A 82 1.59
REMARK 500 H ILE A 5 OG SER A 82 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 7 SER A 44 N - CA - CB ANGL. DEV. = -9.5 DEGREES
REMARK 500 10 SER A 44 N - CA - CB ANGL. DEV. = -9.2 DEGREES
REMARK 500 11 SER A 44 N - CA - CB ANGL. DEV. = -9.6 DEGREES
REMARK 500 13 SER A 44 N - CA - CB ANGL. DEV. = -9.6 DEGREES
REMARK 500 14 SER A 44 N - CA - CB ANGL. DEV. = -9.6 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 GLU B 4 59.46 -155.12
REMARK 500 1 VAL B 5 91.03 -170.46
REMARK 500 1 PTR B 6 -157.69 -125.45
REMARK 500 1 GLU B 7 -65.57 -151.91
REMARK 500 1 PRO B 9 -119.13 -84.85
REMARK 500 1 PRO A 3 -120.37 -78.00
REMARK 500 1 ILE A 5 -47.12 66.28
REMARK 500 1 SER A 8 -153.16 -77.93
REMARK 500 1 LYS A 9 -41.09 -151.33
REMARK 500 1 HIS A 13 59.02 -106.02
REMARK 500 1 ALA A 14 -74.82 -131.02
REMARK 500 1 LEU A 16 -157.36 -141.48
REMARK 500 1 ARG A 18 -131.96 -99.94
REMARK 500 1 ALA A 33 105.51 -30.51
REMARK 500 1 CYS A 58 -157.14 -153.80
REMARK 500 1 GLN A 65 -38.13 176.64
REMARK 500 1 ASN A 71 -38.92 175.17
REMARK 500 1 ASP A 75 86.19 -69.76
REMARK 500 1 SER A 76 134.94 71.58
REMARK 500 1 LEU A 89 -29.50 69.53
REMARK 500 1 TYR A 90 72.50 -58.87
REMARK 500 1 ARG A 91 -90.49 36.29
REMARK 500 1 LYS A 94 44.60 -159.83
REMARK 500 1 LEU A 95 26.91 40.81
REMARK 500 1 ARG A 96 52.28 -153.75
REMARK 500 1 PRO A 98 -167.59 -78.01
REMARK 500 1 ILE A 99 79.22 -116.93
REMARK 500 2 THR B 3 -165.14 63.11
REMARK 500 2 GLU B 7 -111.16 -122.59
REMARK 500 2 PRO B 9 -84.46 -89.14
REMARK 500 2 ALA B 11 -56.98 167.15
REMARK 500 2 ILE A 5 -33.87 65.90
REMARK 500 2 HIS A 6 -62.28 -98.96
REMARK 500 2 LYS A 9 -154.01 -145.56
REMARK 500 2 TYR A 12 56.77 -62.00
REMARK 500 2 HIS A 13 78.07 -109.22
REMARK 500 2 ALA A 14 -66.67 -166.48
REMARK 500 2 LEU A 16 -153.25 -166.12
REMARK 500 2 ARG A 18 -143.75 -88.94
REMARK 500 2 ALA A 19 -16.71 -46.41
REMARK 500 2 VAL A 28 160.14 -46.21
REMARK 500 2 TYR A 45 -161.56 -106.11
REMARK 500 2 SER A 48 81.47 -153.23
REMARK 500 2 LYS A 54 111.36 -171.97
REMARK 500 2 LYS A 56 64.83 -166.78
REMARK 500 2 CYS A 58 -164.32 -118.62
REMARK 500 2 GLN A 65 -40.78 152.74
REMARK 500 2 THR A 66 109.34 -161.61
REMARK 500 2 ASN A 71 39.62 83.87
REMARK 500 2 SER A 72 118.92 -165.01
REMARK 500
REMARK 500 THIS ENTRY HAS 461 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 18 0.28 SIDE CHAIN
REMARK 500 1 ARG A 27 0.31 SIDE CHAIN
REMARK 500 1 ARG A 30 0.32 SIDE CHAIN
REMARK 500 1 ARG A 37 0.32 SIDE CHAIN
REMARK 500 1 ARG A 39 0.30 SIDE CHAIN
REMARK 500 1 ARG A 50 0.31 SIDE CHAIN
REMARK 500 1 ARG A 59 0.31 SIDE CHAIN
REMARK 500 1 ARG A 91 0.20 SIDE CHAIN
REMARK 500 1 ARG A 96 0.30 SIDE CHAIN
REMARK 500 2 ARG A 18 0.28 SIDE CHAIN
REMARK 500 2 ARG A 27 0.29 SIDE CHAIN
REMARK 500 2 ARG A 30 0.26 SIDE CHAIN
REMARK 500 2 ARG A 37 0.30 SIDE CHAIN
REMARK 500 2 ARG A 39 0.31 SIDE CHAIN
REMARK 500 2 ARG A 50 0.30 SIDE CHAIN
REMARK 500 2 ARG A 59 0.29 SIDE CHAIN
REMARK 500 2 ARG A 91 0.28 SIDE CHAIN
REMARK 500 2 ARG A 96 0.31 SIDE CHAIN
REMARK 500 3 ARG A 18 0.28 SIDE CHAIN
REMARK 500 3 ARG A 27 0.31 SIDE CHAIN
REMARK 500 3 ARG A 30 0.29 SIDE CHAIN
REMARK 500 3 ARG A 39 0.27 SIDE CHAIN
REMARK 500 3 ARG A 50 0.31 SIDE CHAIN
REMARK 500 3 ARG A 59 0.31 SIDE CHAIN
REMARK 500 3 ARG A 91 0.18 SIDE CHAIN
REMARK 500 3 ARG A 96 0.19 SIDE CHAIN
REMARK 500 4 ARG A 18 0.24 SIDE CHAIN
REMARK 500 4 ARG A 27 0.29 SIDE CHAIN
REMARK 500 4 ARG A 30 0.30 SIDE CHAIN
REMARK 500 4 ARG A 37 0.31 SIDE CHAIN
REMARK 500 4 ARG A 39 0.26 SIDE CHAIN
REMARK 500 4 ARG A 50 0.32 SIDE CHAIN
REMARK 500 4 ARG A 59 0.32 SIDE CHAIN
REMARK 500 4 ARG A 91 0.29 SIDE CHAIN
REMARK 500 4 ARG A 96 0.28 SIDE CHAIN
REMARK 500 5 ARG A 18 0.27 SIDE CHAIN
REMARK 500 5 ARG A 27 0.26 SIDE CHAIN
REMARK 500 5 ARG A 30 0.31 SIDE CHAIN
REMARK 500 5 ARG A 37 0.16 SIDE CHAIN
REMARK 500 5 ARG A 39 0.30 SIDE CHAIN
REMARK 500 5 ARG A 50 0.31 SIDE CHAIN
REMARK 500 5 ARG A 59 0.32 SIDE CHAIN
REMARK 500 5 ARG A 91 0.32 SIDE CHAIN
REMARK 500 5 ARG A 96 0.30 SIDE CHAIN
REMARK 500 6 ARG A 18 0.31 SIDE CHAIN
REMARK 500 6 ARG A 27 0.29 SIDE CHAIN
REMARK 500 6 ARG A 30 0.31 SIDE CHAIN
REMARK 500 6 ARG A 37 0.21 SIDE CHAIN
REMARK 500 6 ARG A 39 0.29 SIDE CHAIN
REMARK 500 6 ARG A 50 0.29 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 143 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2FCI A 6 102 UNP P08487 PLCG1_BOVIN 663 759
DBREF 2FCI B 1 14 PDB 2FCI 2FCI 1 14
SEQADV 2FCI GLY A 1 UNP P08487 CLONING ARTIFACT
SEQADV 2FCI SER A 2 UNP P08487 CLONING ARTIFACT
SEQADV 2FCI PRO A 3 UNP P08487 CLONING ARTIFACT
SEQADV 2FCI GLY A 4 UNP P08487 CLONING ARTIFACT
SEQADV 2FCI ILE A 5 UNP P08487 CLONING ARTIFACT
SEQADV 2FCI ASN A 103 UNP P08487 CLONING ARTIFACT
SEQADV 2FCI SER A 104 UNP P08487 CLONING ARTIFACT
SEQADV 2FCI SER A 105 UNP P08487 CLONING ARTIFACT
SEQRES 1 B 14 ACE ASP THR GLU VAL PTR GLU SER PRO PTR ALA ASP PRO
SEQRES 2 B 14 GMA
SEQRES 1 A 105 GLY SER PRO GLY ILE HIS GLU SER LYS GLU TRP TYR HIS
SEQRES 2 A 105 ALA SER LEU THR ARG ALA GLN ALA GLU HIS MET LEU MET
SEQRES 3 A 105 ARG VAL PRO ARG ASP GLY ALA PHE LEU VAL ARG LYS ARG
SEQRES 4 A 105 ASN GLU PRO ASN SER TYR ALA ILE SER PHE ARG ALA GLU
SEQRES 5 A 105 GLY LYS ILE LYS HIS CYS ARG VAL GLN GLN GLU GLY GLN
SEQRES 6 A 105 THR VAL MET LEU GLY ASN SER GLU PHE ASP SER LEU VAL
SEQRES 7 A 105 ASP LEU ILE SER TYR TYR GLU LYS HIS PRO LEU TYR ARG
SEQRES 8 A 105 LYS MET LYS LEU ARG TYR PRO ILE ASN GLU GLU ASN SER
SEQRES 9 A 105 SER
MODRES 2FCI PTR B 6 TYR O-PHOSPHOTYROSINE
MODRES 2FCI PTR B 10 TYR O-PHOSPHOTYROSINE
MODRES 2FCI GMA B 14 GLU 4-AMIDO-4-CARBAMOYL-BUTYRIC ACID
HET ACE B 1 6
HET PTR B 6 25
HET PTR B 10 25
HET GMA B 14 18
HETNAM ACE ACETYL GROUP
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM GMA 4-AMIDO-4-CARBAMOYL-BUTYRIC ACID
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 1 ACE C2 H4 O
FORMUL 1 PTR 2(C9 H12 N O6 P)
FORMUL 1 GMA C5 H10 N2 O3
HELIX 1 1 ARG A 18 VAL A 28 1 11
HELIX 2 2 LEU A 77 HIS A 87 1 11
SHEET 1 A 3 PHE A 34 LYS A 38 0
SHEET 2 A 3 TYR A 45 ALA A 51 -1 O SER A 48 N LEU A 35
SHEET 3 A 3 LYS A 54 ILE A 55 -1 O LYS A 54 N ALA A 51
SHEET 1 B 3 PHE A 34 LYS A 38 0
SHEET 2 B 3 TYR A 45 ALA A 51 -1 O SER A 48 N LEU A 35
SHEET 3 B 3 ARG A 59 VAL A 60 -1 O VAL A 60 N TYR A 45
SHEET 1 C 2 VAL A 67 MET A 68 0
SHEET 2 C 2 GLU A 73 PHE A 74 -1 O PHE A 74 N VAL A 67
LINK C ACE B 1 N ASP B 2 1555 1555 1.32
LINK C VAL B 5 N PTR B 6 1555 1555 1.33
LINK C PTR B 6 N GLU B 7 1555 1555 1.33
LINK C PRO B 9 N PTR B 10 1555 1555 1.32
LINK C PTR B 10 N ALA B 11 1555 1555 1.31
LINK C PRO B 13 N GMA B 14 1555 1555 1.31
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 - y 9 2 Bytes