Header list of 1xke.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN TRANSPORT 28-SEP-04 1XKE
TITLE SOLUTION STRUCTURE OF THE SECOND RAN-BINDING DOMAIN FROM HUMAN RANBP2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAN-BINDING PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RAN-BINDING DOMAIN 2 (RANBD2);
COMPND 5 SYNONYM: RANBP2, NUCLEAR PORE COMPLEX PROTEIN NUP358, NUCLEOPORIN
COMPND 6 NUP358, 358 KDA NUCLEOPORIN, P270;
COMPND 7 ENGINEERED: 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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS BETA BARREL, PLECKSTRIN-HOMOLOGY (PH) DOMAIN, PHOSPHOTYROSINE-BINDING
KEYWDS 2 (PTB) DOMAIN, PROTEIN TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.P.GEYER,R.DOEKER,W.KREMER,X.ZHAO,J.KUHLMANN,H.R.KALBITZER
REVDAT 3 02-MAR-22 1XKE 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1XKE 1 VERSN
REVDAT 1 19-APR-05 1XKE 0
JRNL AUTH J.P.GEYER,R.DOKER,W.KREMER,X.ZHAO,J.KUHLMANN,H.R.KALBITZER
JRNL TITL SOLUTION STRUCTURE OF THE RAN-BINDING DOMAIN 2 OF RANBP2 AND
JRNL TITL 2 ITS INTERACTION WITH THE C TERMINUS OF RAN.
JRNL REF J.MOL.BIOL. V. 348 711 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 15826666
JRNL DOI 10.1016/J.JMB.2005.02.033
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.DOEKER,X.ZHAO,W.KREMER,B.VILLA,J.KUHLMANN,H.R.KALBITZER
REMARK 1 TITL SEQUENCE-SPECIFIC RESONANCE ASSIGNMENT OF THE SECOND
REMARK 1 TITL 2 RAN-BINDING DOMAIN OF HUMAN RANBP2
REMARK 1 REF J.BIOMOL.NMR V. 22 185 2002
REMARK 1 REFN ISSN 0925-2738
REMARK 1 PMID 11883781
REMARK 1 DOI 10.1023/A:1014275704491
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.1
REMARK 3 AUTHORS : BRUKER (XWINNMR),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1492 RESTRAINTS (1281 NOE-
REMARK 3 DERIVED DISTANCE RESTRAINTS, 182 DIHEDRAL ANGLE RESTRAINTS AND 29
REMARK 3 HYDROGEN BOND RESTRAINTS).
REMARK 3 THE STRUCTURES WERE ALSO REFINED IN WATER USING XPLOR-NIH 2.9.6
REMARK 3 USING THE PROTOCOL OF LINGE ET AL. (LINGE, J. P., WILLIAMS, M. A.,
REMARK 3 SPRONK, C. A., BONVIN, A. M., & NILGES, M. ,2003. REFINEMENT OF
REMARK 3 PROTEIN STRUCTURES IN EXPLICIT SOLVENT. PROTEINS 50, 496-506).
REMARK 4
REMARK 4 1XKE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-SEP-04.
REMARK 100 THE DEPOSITION ID IS D_1000030454.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 150 MM NA2SO4
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.4MM RANBD2 U-13C; U-15N; 150MM
REMARK 210 NA2SO4; 10MM DTE; 0.5 MM EDTA;
REMARK 210 1MM NAN3; 0.1MM DSS; 10MM
REMARK 210 POTASSIUM PHOSPHATE BUFFER AT PH
REMARK 210 6.5;; 0.7MM RANBD2 U-13C; U-15N;
REMARK 210 150MM NA2SO4; 10MM DTE; 0.5MM
REMARK 210 EDTA; 1MM NAN3; 0.1MM DSS; 10MM
REMARK 210 POTASSIUM PHOSPHATE BUFFER AT PH
REMARK 210 6.5;; 1.0MM RANBD2 U-15N; 150MM
REMARK 210 NA2SO4; 10MM DTE; 0.5MM EDTA;
REMARK 210 1MM NAN3; 0.1 MM DSS; 10MM
REMARK 210 POTASSIUM PHOSPHATE BUFFER AT PH
REMARK 210 6.5;; 1.0MM RANBD2 U-15N; 150MM
REMARK 210 NA2SO4; 10MM DTE; 0.5MM EDTA;
REMARK 210 1MM NAN3; 0.1MM DSS; 10MM
REMARK 210 POTASSIUM PHOSPHATE BUFFER AT PH
REMARK 210 6.5;
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, AUREMOL 2.0.3, CNS
REMARK 210 1.1, XPLOR-NIH 2.9.6
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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 HZ1 LYS A 111 OE2 GLU A 115 1.57
REMARK 500 O GLN A 13 H LEU A 35 1.57
REMARK 500 O LEU A 17 H ARG A 30 1.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 MET A 50 N MET A 50 CA -0.132
REMARK 500 1 MET A 50 C ARG A 51 N -0.150
REMARK 500 1 GLN A 96 N GLN A 96 CA -0.125
REMARK 500 2 MET A 50 N MET A 50 CA -0.137
REMARK 500 2 MET A 50 C ARG A 51 N -0.157
REMARK 500 2 GLN A 96 N GLN A 96 CA -0.139
REMARK 500 3 ARG A 19 C PHE A 20 N -0.139
REMARK 500 3 MET A 50 N MET A 50 CA -0.144
REMARK 500 3 MET A 50 C ARG A 51 N -0.154
REMARK 500 3 GLN A 96 N GLN A 96 CA -0.135
REMARK 500 4 MET A 50 N MET A 50 CA -0.142
REMARK 500 4 MET A 50 C ARG A 51 N -0.150
REMARK 500 4 MET A 81 C TRP A 82 N -0.141
REMARK 500 4 GLN A 96 N GLN A 96 CA -0.135
REMARK 500 5 MET A 50 N MET A 50 CA -0.144
REMARK 500 5 MET A 50 C ARG A 51 N -0.160
REMARK 500 5 ASP A 86 N ASP A 86 CA -0.125
REMARK 500 5 GLN A 96 N GLN A 96 CA -0.125
REMARK 500 5 PRO A 104 C PRO A 104 O -0.121
REMARK 500 6 MET A 50 N MET A 50 CA -0.131
REMARK 500 6 MET A 50 C ARG A 51 N -0.143
REMARK 500 6 GLN A 96 N GLN A 96 CA -0.126
REMARK 500 7 MET A 50 N MET A 50 CA -0.143
REMARK 500 7 MET A 50 C ARG A 51 N -0.161
REMARK 500 7 GLN A 96 N GLN A 96 CA -0.123
REMARK 500 8 MET A 50 C ARG A 51 N -0.153
REMARK 500 9 MET A 50 N MET A 50 CA -0.129
REMARK 500 9 MET A 50 C ARG A 51 N -0.150
REMARK 500 9 GLY A 90 N GLY A 90 CA -0.090
REMARK 500 9 GLN A 96 N GLN A 96 CA -0.124
REMARK 500 9 LYS A 100 C PHE A 101 N -0.139
REMARK 500 10 LEU A 35 N LEU A 35 CA -0.128
REMARK 500 10 MET A 50 N MET A 50 CA -0.146
REMARK 500 10 MET A 50 C ARG A 51 N -0.151
REMARK 500 10 GLY A 90 N GLY A 90 CA -0.092
REMARK 500 10 GLN A 96 N GLN A 96 CA -0.128
REMARK 500 11 MET A 50 N MET A 50 CA -0.128
REMARK 500 11 MET A 50 C ARG A 51 N -0.141
REMARK 500 12 MET A 50 N MET A 50 CA -0.141
REMARK 500 12 MET A 50 C ARG A 51 N -0.162
REMARK 500 12 ASP A 91 C ALA A 92 N -0.144
REMARK 500 12 GLN A 96 N GLN A 96 CA -0.120
REMARK 500 13 MET A 50 N MET A 50 CA -0.158
REMARK 500 13 MET A 50 C ARG A 51 N -0.162
REMARK 500 13 MET A 81 C TRP A 82 N -0.142
REMARK 500 13 GLY A 90 N GLY A 90 CA -0.097
REMARK 500 13 GLN A 96 N GLN A 96 CA -0.135
REMARK 500 14 MET A 50 N MET A 50 CA -0.142
REMARK 500 14 MET A 50 C ARG A 51 N -0.163
REMARK 500 14 GLN A 96 N GLN A 96 CA -0.121
REMARK 500
REMARK 500 THIS ENTRY HAS 68 BOND 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 GLU A 5 -157.92 -140.83
REMARK 500 1 LEU A 56 10.82 52.48
REMARK 500 1 VAL A 58 124.87 -37.64
REMARK 500 1 PHE A 87 61.66 -158.45
REMARK 500 1 ASP A 89 33.87 177.93
REMARK 500 1 ASP A 91 125.97 80.51
REMARK 500 1 PRO A 104 -8.07 -55.95
REMARK 500 2 SER A 2 -79.89 64.58
REMARK 500 2 GLU A 4 43.36 -102.33
REMARK 500 2 ASP A 6 -0.41 88.26
REMARK 500 2 LEU A 10 -65.53 -92.12
REMARK 500 2 GLU A 53 -76.46 -45.45
REMARK 500 2 LEU A 56 10.40 51.31
REMARK 500 2 VAL A 58 122.11 -28.91
REMARK 500 2 ARG A 78 39.12 -152.64
REMARK 500 2 PHE A 87 109.51 158.54
REMARK 500 2 ASP A 91 132.50 86.29
REMARK 500 3 ASP A 6 3.39 81.62
REMARK 500 3 LEU A 56 10.91 52.59
REMARK 500 3 VAL A 58 116.39 -28.95
REMARK 500 3 ARG A 78 37.03 -149.95
REMARK 500 3 PHE A 87 21.03 -141.17
REMARK 500 3 ASP A 89 10.63 -152.75
REMARK 500 3 ASP A 91 159.80 70.92
REMARK 500 4 GLU A 5 -143.18 -129.19
REMARK 500 4 ASP A 6 -1.64 104.19
REMARK 500 4 LEU A 10 -68.41 -94.77
REMARK 500 4 LEU A 56 10.90 50.31
REMARK 500 4 VAL A 58 123.85 -29.97
REMARK 500 4 ARG A 78 48.79 -167.79
REMARK 500 4 PHE A 87 79.78 -152.25
REMARK 500 4 ASP A 89 36.25 162.53
REMARK 500 4 ASP A 91 144.69 178.75
REMARK 500 5 ASP A 6 -12.88 146.68
REMARK 500 5 GLU A 53 -73.31 -48.09
REMARK 500 5 LEU A 56 9.56 52.16
REMARK 500 5 VAL A 58 125.85 -30.39
REMARK 500 5 ARG A 78 43.98 177.45
REMARK 500 5 PHE A 87 108.74 -168.83
REMARK 500 5 ASP A 89 45.05 159.95
REMARK 500 6 SER A 2 86.92 -153.15
REMARK 500 6 GLU A 4 70.26 49.57
REMARK 500 6 GLU A 5 -167.38 -120.27
REMARK 500 6 ASN A 43 -14.23 153.58
REMARK 500 6 GLU A 53 -73.74 -48.50
REMARK 500 6 LEU A 56 9.42 50.58
REMARK 500 6 VAL A 58 126.11 -33.52
REMARK 500 6 ARG A 78 40.74 -167.64
REMARK 500 6 PHE A 87 79.81 176.94
REMARK 500 6 ASP A 89 31.93 171.79
REMARK 500
REMARK 500 THIS ENTRY HAS 150 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 51 0.09 SIDE CHAIN
REMARK 500 3 ARG A 30 0.07 SIDE CHAIN
REMARK 500 3 ARG A 51 0.08 SIDE CHAIN
REMARK 500 5 ARG A 30 0.10 SIDE CHAIN
REMARK 500 5 ARG A 51 0.08 SIDE CHAIN
REMARK 500 5 ARG A 78 0.08 SIDE CHAIN
REMARK 500 8 ARG A 19 0.07 SIDE CHAIN
REMARK 500 11 ARG A 30 0.09 SIDE CHAIN
REMARK 500 12 ARG A 30 0.09 SIDE CHAIN
REMARK 500 12 ARG A 78 0.09 SIDE CHAIN
REMARK 500 15 ARG A 51 0.10 SIDE CHAIN
REMARK 500 16 ARG A 51 0.08 SIDE CHAIN
REMARK 500 19 ARG A 119 0.11 SIDE CHAIN
REMARK 500 20 ARG A 51 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5159 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFT ASSIGNMENT
DBREF 1XKE A 3 129 UNP P49792 RBP2_HUMAN 2028 2154
SEQADV 1XKE GLY A 1 UNP P49792 CLONING ARTIFACT
SEQADV 1XKE SER A 2 UNP P49792 CLONING ARTIFACT
SEQADV 1XKE LYS A 130 UNP P49792 CLONING ARTIFACT
SEQRES 1 A 130 GLY SER GLY GLU GLU ASP GLU LYS VAL LEU TYR SER GLN
SEQRES 2 A 130 ARG VAL LYS LEU PHE ARG PHE ASP ALA GLU VAL SER GLN
SEQRES 3 A 130 TRP LYS GLU ARG GLY LEU GLY ASN LEU LYS ILE LEU LYS
SEQRES 4 A 130 ASN GLU VAL ASN GLY LYS LEU ARG MET LEU MET ARG ARG
SEQRES 5 A 130 GLU GLN VAL LEU LYS VAL CYS ALA ASN HIS TRP ILE THR
SEQRES 6 A 130 THR THR MET ASN LEU LYS PRO LEU SER GLY SER ASP ARG
SEQRES 7 A 130 ALA TRP MET TRP LEU ALA SER ASP PHE SER ASP GLY ASP
SEQRES 8 A 130 ALA LYS LEU GLU GLN LEU ALA ALA LYS PHE LYS THR PRO
SEQRES 9 A 130 GLU LEU ALA GLU GLU PHE LYS GLN LYS PHE GLU GLU CYS
SEQRES 10 A 130 GLN ARG LEU LEU LEU ASP ILE PRO LEU GLN THR PRO LYS
HELIX 1 1 THR A 103 LEU A 121 1 19
SHEET 1 A 4 GLU A 7 VAL A 9 0
SHEET 2 A 4 GLN A 26 ASN A 40 -1 O LYS A 39 N LYS A 8
SHEET 3 A 4 LEU A 46 ARG A 52 -1 O LEU A 49 N LYS A 36
SHEET 4 A 4 LYS A 57 TRP A 63 -1 O HIS A 62 N MET A 48
SHEET 1 B 6 GLU A 7 VAL A 9 0
SHEET 2 B 6 GLN A 26 ASN A 40 -1 O LYS A 39 N LYS A 8
SHEET 3 B 6 GLN A 13 ASP A 21 -1 N ARG A 19 O LYS A 28
SHEET 4 B 6 LYS A 93 LYS A 100 -1 O ALA A 98 N PHE A 18
SHEET 5 B 6 TRP A 80 ASP A 86 -1 N ALA A 84 O GLU A 95
SHEET 6 B 6 LEU A 70 PRO A 72 -1 N LYS A 71 O MET A 81
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