Header list of 1x9l.pdb file
Complete list - r 25 2 Bytes
HEADER METAL BINDING PROTEIN 23-AUG-04 1X9L
TITLE SOLUTION STRUCTURE OF CUI-DR1885 FROM DEINOCOCCUS RADIODURANS
CAVEAT 1X9L CHIRALITY ERRORS IN MODELS 1 AND 9.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUI-DR1885;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 3 ORGANISM_TAXID: 243230;
SOURCE 4 STRAIN: R1
KEYWDS COPPER BINDING PROTEIN, DEINOCOCCUS RADIODURANS, SOLUTION STRUCTURE,
KEYWDS 2 HOLO-FORM, STRUCTURAL PROTEOMICS IN EUROPE, SPINE, STRUCTURAL
KEYWDS 3 GENOMICS, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
MDLTYP MINIMIZED AVERAGE
AUTHOR L.BANCI,I.BERTINI,S.CIOFI-BAFFONI,E.KATSARI,N.KATSAROS,K.KUBICEK,
AUTHOR 2 STRUCTURAL PROTEOMICS IN EUROPE (SPINE)
REVDAT 4 13-JUL-11 1X9L 1 VERSN
REVDAT 3 24-FEB-09 1X9L 1 VERSN
REVDAT 2 19-APR-05 1X9L 1 JRNL
REVDAT 1 31-AUG-04 1X9L 0
JRNL AUTH L.BANCI,I.BERTINI,S.CIOFI-BAFFONI,E.KATSARI,N.KATSAROS,
JRNL AUTH 2 K.KUBICEK
JRNL TITL A COPPER(I) PROTEIN POSSIBLY INVOLVED IN THE ASSEMBLY OF CUA
JRNL TITL 2 CENTER OF BACTERIAL CYTOCHROME C OXIDASE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 3994 2005
JRNL REFN ISSN 0027-8424
JRNL PMID 15753304
JRNL DOI 10.1073/PNAS.0406150102
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5
REMARK 3 AUTHORS : GUENTERT, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X9L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-AUG-04.
REMARK 100 THE RCSB ID CODE IS RCSB030111.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 101.325 ATM
REMARK 210 SAMPLE CONTENTS : 1MM CUI-DR1885, 100MM PHOSPHATE
REMARK 210 BUFFER K, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY; 2D NOESY; 2D
REMARK 210 TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.5, NMRPIPE 2.2, SPARKY
REMARK 210 3.106
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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: 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 PRO A 11 C - N - CA ANGL. DEV. = 9.0 DEGREES
REMARK 500 9 ALA A 17 C - N - CA ANGL. DEV. = 16.9 DEGREES
REMARK 500 14 ARG A 149 NE - CZ - NH2 ANGL. DEV. = -3.1 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
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 THR A 4 85.12 -58.57
REMARK 500 1 MET A 5 -158.34 -62.05
REMARK 500 1 PRO A 6 -167.87 51.62
REMARK 500 1 ALA A 7 -94.41 61.87
REMARK 500 1 HIS A 8 -58.48 -136.79
REMARK 500 1 THR A 9 -76.21 -13.79
REMARK 500 1 PRO A 10 -109.14 61.61
REMARK 500 1 PRO A 11 66.30 -23.32
REMARK 500 1 ALA A 12 52.19 -103.64
REMARK 500 1 GLN A 13 -164.06 59.51
REMARK 500 1 PRO A 16 -91.56 -28.85
REMARK 500 1 GLN A 19 -64.51 93.03
REMARK 500 1 LYS A 20 -44.63 165.01
REMARK 500 1 ALA A 23 -54.93 80.82
REMARK 500 1 GLN A 24 -65.03 74.82
REMARK 500 1 ALA A 25 136.64 162.50
REMARK 500 1 THR A 29 57.42 -161.71
REMARK 500 1 VAL A 38 108.22 -17.50
REMARK 500 1 SER A 41 44.25 -165.40
REMARK 500 1 ILE A 42 169.07 74.20
REMARK 500 1 LYS A 54 57.02 -141.82
REMARK 500 1 SER A 55 -40.63 -156.16
REMARK 500 1 ASP A 56 62.22 65.99
REMARK 500 1 VAL A 62 54.28 -143.75
REMARK 500 1 ALA A 64 59.97 -156.21
REMARK 500 1 PRO A 67 49.65 -75.78
REMARK 500 1 LEU A 68 -70.59 -125.55
REMARK 500 1 SER A 80 -20.59 166.01
REMARK 500 1 MET A 83 -168.10 -166.05
REMARK 500 1 TRP A 91 -165.30 172.65
REMARK 500 1 ALA A 96 177.93 58.38
REMARK 500 1 ARG A 97 33.99 38.81
REMARK 500 1 THR A 99 57.16 -111.49
REMARK 500 1 ASP A 107 136.45 65.45
REMARK 500 1 HIS A 108 -179.20 179.82
REMARK 500 1 LYS A 115 -72.97 -76.45
REMARK 500 1 VAL A 120 107.37 -54.01
REMARK 500 1 THR A 135 73.15 -156.35
REMARK 500 1 ASN A 145 110.68 65.47
REMARK 500 2 MET A 5 88.83 -158.03
REMARK 500 2 ALA A 15 68.65 -168.61
REMARK 500 2 THR A 29 59.32 -156.60
REMARK 500 2 ALA A 36 38.49 -79.11
REMARK 500 2 ALA A 37 -145.23 47.02
REMARK 500 2 SER A 41 58.91 -166.99
REMARK 500 2 ILE A 42 164.09 76.30
REMARK 500 2 ALA A 64 61.96 -156.47
REMARK 500 2 LEU A 68 -48.45 -162.97
REMARK 500 2 THR A 77 59.86 -145.83
REMARK 500 2 SER A 80 -58.15 -163.32
REMARK 500
REMARK 500 THIS ENTRY HAS 543 RAMACHANDRAN OUTLIERS.
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 THR A 4 MET A 5 1 149.46
REMARK 500 ALA A 7 HIS A 8 1 117.38
REMARK 500 PRO A 11 ALA A 12 1 132.87
REMARK 500 ALA A 12 GLN A 13 1 -145.98
REMARK 500 THR A 14 ALA A 15 1 141.40
REMARK 500 ALA A 15 PRO A 16 1 -105.72
REMARK 500 ALA A 21 GLY A 22 1 -144.87
REMARK 500 PRO A 27 VAL A 28 1 -148.04
REMARK 500 MET A 83 ALA A 84 2 145.04
REMARK 500 ALA A 37 VAL A 38 3 -144.02
REMARK 500 GLY A 148 ARG A 149 3 -135.85
REMARK 500 MET A 1 GLY A 2 8 -137.46
REMARK 500 ALA A 7 HIS A 8 9 -148.98
REMARK 500 PRO A 11 ALA A 12 9 56.71
REMARK 500 SER A 55 ASP A 56 15 140.77
REMARK 500 ALA A 37 VAL A 38 16 140.22
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 TYR A 48 0.07 SIDE CHAIN
REMARK 500 1 ARG A 149 0.08 SIDE CHAIN
REMARK 500 2 TYR A 48 0.08 SIDE CHAIN
REMARK 500 2 ARG A 149 0.13 SIDE CHAIN
REMARK 500 5 TYR A 48 0.11 SIDE CHAIN
REMARK 500 5 ARG A 104 0.12 SIDE CHAIN
REMARK 500 6 HIS A 108 0.08 SIDE CHAIN
REMARK 500 7 TYR A 48 0.07 SIDE CHAIN
REMARK 500 8 TYR A 48 0.12 SIDE CHAIN
REMARK 500 9 ARG A 97 0.07 SIDE CHAIN
REMARK 500 9 ARG A 134 0.09 SIDE CHAIN
REMARK 500 9 ARG A 149 0.08 SIDE CHAIN
REMARK 500 11 TYR A 48 0.11 SIDE CHAIN
REMARK 500 12 ARG A 134 0.10 SIDE CHAIN
REMARK 500 13 TYR A 48 0.07 SIDE CHAIN
REMARK 500 14 TYR A 48 0.13 SIDE CHAIN
REMARK 500 14 ARG A 97 0.17 SIDE CHAIN
REMARK 500 14 ARG A 104 0.16 SIDE CHAIN
REMARK 500 14 ARG A 149 0.09 SIDE CHAIN
REMARK 500 15 TYR A 48 0.09 SIDE CHAIN
REMARK 500 15 ARG A 97 0.12 SIDE CHAIN
REMARK 500 16 TYR A 48 0.13 SIDE CHAIN
REMARK 500 19 ARG A 104 0.11 SIDE CHAIN
REMARK 500 20 TYR A 48 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 1 HIS A 3 -24.8 L D WRONG HAND
REMARK 500 1 THR A 4 -30.6 L D WRONG HAND
REMARK 500 1 MET A 5 -30.4 L D WRONG HAND
REMARK 500 1 PRO A 6 -34.0 L D WRONG HAND
REMARK 500 1 HIS A 8 -28.3 L D WRONG HAND
REMARK 500 1 THR A 9 -29.7 L D WRONG HAND
REMARK 500 1 PRO A 10 -36.4 L D WRONG HAND
REMARK 500 1 GLN A 13 -34.3 L D WRONG HAND
REMARK 500 9 MET A 1 -35.2 L D WRONG HAND
REMARK 500 9 HIS A 8 -35.6 L D WRONG HAND
REMARK 500 9 THR A 9 -36.5 L D WRONG HAND
REMARK 500 9 PRO A 10 -37.2 L D WRONG HAND
REMARK 500 9 PRO A 11 -31.6 L D WRONG HAND
REMARK 500 9 ALA A 12 -32.9 L D WRONG HAND
REMARK 500 9 GLN A 13 -32.9 L D WRONG HAND
REMARK 500 9 ALA A 17 19.2 L L OUTSIDE RANGE
REMARK 500 9 LYS A 20 -36.1 L D WRONG HAND
REMARK 500 9 ALA A 21 -34.1 L D WRONG HAND
REMARK 500 1 THR A 14 -35.9 R S CBETA WRONG HAND
REMARK 500 9 THR A 14 -31.1 R S CBETA WRONG HAND
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 1 CU1 A 150 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 108 NE2
REMARK 620 2 MET A 86 SD 121.0
REMARK 620 3 MET A 110 SD 108.3 127.9
REMARK 620 4 MET A 75 SD 116.9 83.1 89.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A 150
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CIRMMP12 RELATED DB: TARGETDB
DBREF 1X9L A 2 145 UNP Q9RT80 Q9RT80_DEIRA 35 178
SEQADV 1X9L MET A 1 UNP Q9RT80 INITIATING METHIONINE
SEQADV 1X9L ILE A 146 UNP Q9RT80 CLONING ARTIFACT
SEQADV 1X9L GLU A 147 UNP Q9RT80 CLONING ARTIFACT
SEQADV 1X9L GLY A 148 UNP Q9RT80 CLONING ARTIFACT
SEQADV 1X9L ARG A 149 UNP Q9RT80 CLONING ARTIFACT
SEQRES 1 A 149 MET GLY HIS THR MET PRO ALA HIS THR PRO PRO ALA GLN
SEQRES 2 A 149 THR ALA PRO ALA ALA GLN LYS ALA GLY ALA GLN ALA LEU
SEQRES 3 A 149 PRO VAL THR VAL GLN GLY ALA THR VAL ALA ALA VAL PRO
SEQRES 4 A 149 PRO SER ILE ARG ASP THR ALA ALA TYR MET THR LEU THR
SEQRES 5 A 149 ASN LYS SER ASP GLN PRO ILE LYS LEU VAL GLY ALA ALA
SEQRES 6 A 149 THR PRO LEU ALA THR SER PRO MET LEU MET THR THR THR
SEQRES 7 A 149 HIS SER GLY GLY MET ALA GLY MET LYS MET VAL PRO TRP
SEQRES 8 A 149 LEU THR ILE PRO ALA ARG GLY THR LEU THR LEU GLN ARG
SEQRES 9 A 149 ASP GLY ASP HIS VAL MET LEU MET GLY LEU LYS ARG PRO
SEQRES 10 A 149 LEU LYS VAL GLY GLU THR VAL ASN ILE THR LEU LYS ALA
SEQRES 11 A 149 THR ASP GLY ARG THR LEU ASN VAL ALA ALA THR VAL LYS
SEQRES 12 A 149 LYS ASN ILE GLU GLY ARG
HET CU1 A 150 1
HETNAM CU1 COPPER (I) ION
FORMUL 2 CU1 CU 1+
SHEET 1 A 5 THR A 101 LEU A 102 0
SHEET 2 A 5 ALA A 47 THR A 50 -1 N MET A 49 O LEU A 102
SHEET 3 A 5 THR A 34 VAL A 35 -1 N THR A 34 O TYR A 48
SHEET 4 A 5 LEU A 136 VAL A 142 1 O THR A 141 N VAL A 35
SHEET 5 A 5 GLU A 122 LEU A 128 -1 N VAL A 124 O ALA A 140
SHEET 1 B 2 PRO A 58 LEU A 61 0
SHEET 2 B 2 LEU A 92 PRO A 95 -1 O ILE A 94 N ILE A 59
SHEET 1 C 3 ALA A 84 GLY A 85 0
SHEET 2 C 3 ALA A 69 THR A 77 -1 N THR A 76 O GLY A 85
SHEET 3 C 3 HIS A 108 LEU A 114 -1 O MET A 112 N SER A 71
LINK CU CU1 A 150 NE2 HIS A 108 1555 1555 2.15
LINK CU CU1 A 150 SD MET A 86 1555 1555 2.50
LINK CU CU1 A 150 SD MET A 110 1555 1555 2.41
LINK CU CU1 A 150 SD MET A 75 1555 1555 2.44
CISPEP 1 GLY A 2 HIS A 3 1 -1.49
CISPEP 2 MET A 5 PRO A 6 1 6.46
CISPEP 3 HIS A 8 THR A 9 1 -12.25
CISPEP 4 PRO A 16 ALA A 17 1 -7.32
CISPEP 5 ALA A 18 GLN A 19 1 -14.49
CISPEP 6 GLY A 2 HIS A 3 9 1.25
CISPEP 7 HIS A 3 THR A 4 9 9.97
CISPEP 8 THR A 14 ALA A 15 9 13.55
CISPEP 9 PRO A 16 ALA A 17 9 -4.50
CISPEP 10 GLN A 19 LYS A 20 9 9.88
CISPEP 11 GLY A 22 ALA A 23 9 -2.24
SITE 1 AC1 4 MET A 75 MET A 86 HIS A 108 MET A 110
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