Header list of 2fws.pdb file
Complete list - r 9 2 Bytes
HEADER METAL TRANSPORT REGULATOR 03-FEB-06 2FWS
TITLE FIRST CA2+ BINDING DOMAIN OF THE NA,CA-EXCHANGER (NCX1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SODIUM/CALCIUM EXCHANGER 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CBD1, CA2+ BINDING DOMAIN 1;
COMPND 5 SYNONYM: NA(+)/CA(2+)-EXCHANGE PROTEIN 1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANIS LUPUS FAMILIARIS;
SOURCE 3 ORGANISM_COMMON: DOG;
SOURCE 4 ORGANISM_TAXID: 9615;
SOURCE 5 STRAIN: FAMILIARIS;
SOURCE 6 GENE: NCX1;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET23B
KEYWDS BETA-SANDWICH, GREEK KEY, CIS-PROLINE, BETA-BULGE, CA2+ BINDING,
KEYWDS 2 METAL TRANSPORT REGULATOR
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.HILGE,J.AELEN,G.W.VUISTER
REVDAT 3 09-MAR-22 2FWS 1 REMARK LINK
REVDAT 2 24-FEB-09 2FWS 1 VERSN
REVDAT 1 18-APR-06 2FWS 0
JRNL AUTH M.HILGE,J.AELEN,G.W.VUISTER
JRNL TITL CA(2+) REGULATION IN THE NA(+)/CA(2+) EXCHANGER INVOLVES TWO
JRNL TITL 2 MARKEDLY DIFFERENT CA(2+) SENSORS
JRNL REF MOL.CELL V. 22 15 2006
JRNL REFN ISSN 1097-2765
JRNL PMID 16600866
JRNL DOI 10.1016/J.MOLCEL.2006.03.008
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.1, X-PLOR NIH VERSION 2.9.7
REMARK 3 AUTHORS : DELAGLIO, F. (NMRPIPE), CLORE, G.M. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 2313 NOE
REMARK 3 -DERIVED DISTANCE CONSTRAINTS, 175 DIHEDRAL ANGLE RESTRAINTS
REMARK 3 (TALOS), 9 DISTANCE CONSTRAINTS TO THE 2 CA2+ IONS
REMARK 4
REMARK 4 2FWS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1000036405.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 306
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 20MM HEPES (SODIUM SALT)
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5-1.0MM 13C, 15N CBD1 SAMPLE
REMARK 210 (RESIDUES 371-509) IN 20MM HEPES
REMARK 210 BUFFER (PH 7.0), 20MM BETA-
REMARK 210 MERCAPTOETHANOL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C SEPARATED ALIPHATIC
REMARK 210 NOESY; 3D_13C SEPARATED AROMATIC
REMARK 210 NOESY; 3D_15N-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.13, CYANA 2.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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
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 5 GLU A 385 CD GLU A 385 OE1 -0.067
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 2 GLU A 454 OE1 - CD - OE2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 3 GLU A 454 OE1 - CD - OE2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 5 GLU A 454 OE1 - CD - OE2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 6 GLU A 454 OE1 - CD - OE2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 7 GLU A 454 OE1 - CD - OE2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 12 GLU A 454 OE1 - CD - OE2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 13 GLU A 454 OE1 - CD - OE2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 14 ASP A 447 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 16 GLU A 454 OE1 - CD - OE2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 17 GLU A 454 OE1 - CD - OE2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 18 GLU A 454 OE1 - CD - OE2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 19 GLU A 454 OE1 - CD - OE2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 20 GLU A 454 OE1 - CD - OE2 ANGL. DEV. = -7.5 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 LEU A 401 111.87 -160.35
REMARK 500 1 SER A 420 -51.83 -126.13
REMARK 500 1 THR A 425 56.37 32.93
REMARK 500 1 ASN A 462 86.91 49.60
REMARK 500 1 ILE A 474 89.31 -68.70
REMARK 500 1 ALA A 477 22.72 -73.07
REMARK 500 1 VAL A 480 -70.41 -79.85
REMARK 500 1 ALA A 482 -55.77 70.41
REMARK 500 1 LEU A 483 -58.23 -156.13
REMARK 500 1 CYS A 485 -173.94 -175.53
REMARK 500 1 ASP A 499 -7.10 68.91
REMARK 500 2 THR A 425 58.12 37.08
REMARK 500 2 ASN A 462 89.75 47.75
REMARK 500 2 GLU A 468 -60.64 -124.05
REMARK 500 2 GLU A 471 -62.28 -105.06
REMARK 500 2 HIS A 479 -36.06 -140.32
REMARK 500 2 LEU A 483 -76.32 -116.67
REMARK 500 2 ALA A 484 114.51 -165.65
REMARK 500 2 SER A 488 75.27 -110.81
REMARK 500 2 ASP A 499 -8.98 67.05
REMARK 500 2 ILE A 504 85.63 54.06
REMARK 500 3 SER A 420 -57.83 -123.73
REMARK 500 3 ASN A 462 81.77 50.86
REMARK 500 3 GLU A 468 -49.36 67.87
REMARK 500 3 ASP A 472 174.95 66.44
REMARK 500 3 GLU A 476 44.29 -82.87
REMARK 500 3 ALA A 482 85.28 -69.59
REMARK 500 3 LEU A 483 -39.94 171.36
REMARK 500 3 ASP A 499 -38.19 78.01
REMARK 500 4 ALA A 416 -159.53 -135.57
REMARK 500 4 THR A 425 67.12 37.59
REMARK 500 4 ASN A 462 82.46 39.45
REMARK 500 4 ALA A 469 -79.16 -102.13
REMARK 500 4 SER A 470 10.19 54.30
REMARK 500 4 LEU A 483 -79.68 -120.78
REMARK 500 4 ASP A 500 -63.38 -95.80
REMARK 500 5 ALA A 416 -159.22 -117.72
REMARK 500 5 SER A 420 -54.79 -128.88
REMARK 500 5 ASN A 462 88.39 45.70
REMARK 500 5 VAL A 480 -169.45 -113.45
REMARK 500 5 SER A 481 -151.49 -162.84
REMARK 500 5 LEU A 486 -164.41 -68.98
REMARK 500 5 SER A 488 65.34 -113.28
REMARK 500 5 PRO A 489 -80.55 -98.15
REMARK 500 5 ASP A 499 -5.74 69.29
REMARK 500 5 ALA A 502 -73.95 -72.38
REMARK 500 6 ALA A 416 -157.58 -147.03
REMARK 500 6 THR A 425 67.16 36.69
REMARK 500 6 GLU A 435 -70.16 -73.24
REMARK 500 6 THR A 436 -35.33 71.26
REMARK 500
REMARK 500 THIS ENTRY HAS 166 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 8 ARG A 396 0.12 SIDE CHAIN
REMARK 500 14 ARG A 396 0.08 SIDE CHAIN
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 CA A 600 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 385 OE1
REMARK 620 2 ASP A 448 OD1 116.6
REMARK 620 3 GLU A 451 OE1 102.5 112.7
REMARK 620 4 ASP A 498 OD1 112.8 113.0 97.0
REMARK 620 5 ASP A 500 OD2 81.5 74.5 168.0 71.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 650 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 421 OD2
REMARK 620 2 ASP A 421 OD1 8.5
REMARK 620 3 ASP A 447 OD1 97.6 95.0
REMARK 620 4 ASP A 447 OD2 94.9 86.4 66.3
REMARK 620 5 GLU A 451 OE2 161.4 160.3 100.6 88.9
REMARK 620 6 GLU A 454 OE1 74.5 76.6 171.2 110.2 87.2
REMARK 620 7 GLU A 454 OE2 79.9 87.5 133.0 160.3 90.5 50.2
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 650
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2FWU RELATED DB: PDB
REMARK 900 SECOND CA2+ BINDING DOMAIN
DBREF 2FWS A 371 509 UNP P23685 NAC1_CANFA 403 541
SEQRES 1 A 139 VAL SER LYS ILE PHE PHE GLU GLN GLY THR TYR GLN CYS
SEQRES 2 A 139 LEU GLU ASN CYS GLY THR VAL ALA LEU THR ILE ILE ARG
SEQRES 3 A 139 ARG GLY GLY ASP LEU THR ASN THR VAL PHE VAL ASP PHE
SEQRES 4 A 139 ARG THR GLU ASP GLY THR ALA ASN ALA GLY SER ASP TYR
SEQRES 5 A 139 GLU PHE THR GLU GLY THR VAL VAL PHE LYS PRO GLY GLU
SEQRES 6 A 139 THR GLN LYS GLU ILE ARG VAL GLY ILE ILE ASP ASP ASP
SEQRES 7 A 139 ILE PHE GLU GLU ASP GLU ASN PHE LEU VAL HIS LEU SER
SEQRES 8 A 139 ASN VAL LYS VAL SER SER GLU ALA SER GLU ASP GLY ILE
SEQRES 9 A 139 LEU GLU ALA ASN HIS VAL SER ALA LEU ALA CYS LEU GLY
SEQRES 10 A 139 SER PRO SER THR ALA THR VAL THR ILE PHE ASP ASP ASP
SEQRES 11 A 139 HIS ALA GLY ILE PHE THR PHE GLU GLU
HET CA A 600 1
HET CA A 650 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 2(CA 2+)
SHEET 1 A 3 LYS A 373 PHE A 376 0
SHEET 2 A 3 THR A 389 ARG A 397 -1 O ILE A 395 N PHE A 375
SHEET 3 A 3 GLN A 437 GLY A 443 -1 O LYS A 438 N ILE A 394
SHEET 1 B 5 THR A 380 LEU A 384 0
SHEET 2 B 5 ALA A 492 PHE A 497 1 O PHE A 497 N CYS A 383
SHEET 3 B 5 ASN A 455 SER A 466 -1 N PHE A 456 O VAL A 494
SHEET 4 B 5 THR A 404 GLU A 412 -1 N GLU A 412 O LEU A 457
SHEET 5 B 5 GLY A 427 PHE A 431 -1 O VAL A 429 N VAL A 407
LINK OE1 GLU A 385 CA CA A 600 1555 1555 1.74
LINK OD2 ASP A 421 CA CA A 650 1555 1555 4.05
LINK OD1 ASP A 421 CA CA A 650 1555 1555 1.88
LINK OD1 ASP A 447 CA CA A 650 1555 1555 1.84
LINK OD2 ASP A 447 CA CA A 650 1555 1555 1.98
LINK OD1 ASP A 448 CA CA A 600 1555 1555 1.75
LINK OE1 GLU A 451 CA CA A 600 1555 1555 1.77
LINK OE2 GLU A 451 CA CA A 650 1555 1555 1.79
LINK OE1 GLU A 454 CA CA A 650 1555 1555 2.83
LINK OE2 GLU A 454 CA CA A 650 1555 1555 1.80
LINK OD1 ASP A 498 CA CA A 600 1555 1555 1.72
LINK OD2 ASP A 500 CA CA A 600 1555 1555 3.03
CISPEP 1 PRO A 489 SER A 490 1 1.20
CISPEP 2 PRO A 489 SER A 490 2 -7.94
CISPEP 3 PRO A 489 SER A 490 3 3.70
CISPEP 4 PRO A 489 SER A 490 4 3.40
CISPEP 5 PRO A 489 SER A 490 5 -5.93
CISPEP 6 PRO A 489 SER A 490 6 2.40
CISPEP 7 PRO A 489 SER A 490 7 1.41
CISPEP 8 PRO A 489 SER A 490 8 1.06
CISPEP 9 PRO A 489 SER A 490 9 0.50
CISPEP 10 PRO A 489 SER A 490 10 -2.01
CISPEP 11 PRO A 489 SER A 490 11 2.85
CISPEP 12 PRO A 489 SER A 490 12 -0.59
CISPEP 13 PRO A 489 SER A 490 13 -3.13
CISPEP 14 PRO A 489 SER A 490 14 0.64
CISPEP 15 PRO A 489 SER A 490 15 -3.42
CISPEP 16 PRO A 489 SER A 490 16 2.49
CISPEP 17 PRO A 489 SER A 490 17 1.93
CISPEP 18 PRO A 489 SER A 490 18 1.05
CISPEP 19 PRO A 489 SER A 490 19 -6.83
CISPEP 20 PRO A 489 SER A 490 20 0.51
SITE 1 AC1 6 GLU A 385 ASP A 447 ASP A 448 GLU A 451
SITE 2 AC1 6 ASP A 498 ASP A 500
SITE 1 AC2 4 ASP A 421 ASP A 447 GLU A 451 GLU A 454
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 9 2 Bytes