HEADER ELECTRON TRANSPORT 03-SEP-99 1CZN
TITLE REFINED STRUCTURES OF OXIDIZED FLAVODOXIN FROM ANACYSTIS NIDULANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLAVODOXIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: WILDTYPE CRYSTAL FORM I, OXIDIZED
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS ELONGATUS;
SOURCE 3 ORGANISM_TAXID: 1140;
SOURCE 4 STRAIN: PCC 7942;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: W1485;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PKK233-2-ANFLD
KEYWDS FLAVODOXIN, FMN BINDING, REDOX POTENTIAL, ELECTRON TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR W.W.SMITH,K.A.PATTRIDGE,C.L.LUSCHINSKY,M.L.LUDWIG
REVDAT 6 07-FEB-24 1CZN 1 REMARK
REVDAT 5 04-APR-18 1CZN 1 REMARK
REVDAT 4 19-FEB-14 1CZN 1 JRNL
REVDAT 3 13-JUL-11 1CZN 1 VERSN
REVDAT 2 24-FEB-09 1CZN 1 VERSN
REVDAT 1 29-DEC-99 1CZN 0
JRNL AUTH C.L.DRENNAN,K.A.PATTRIDGE,C.H.WEBER,A.L.METZGER,D.M.HOOVER,
JRNL AUTH 2 M.L.LUDWIG
JRNL TITL REFINED STRUCTURES OF OXIDIZED FLAVODOXIN FROM ANACYSTIS
JRNL TITL 2 NIDULANS.
JRNL REF J.MOL.BIOL. V. 294 711 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 10610791
JRNL DOI 10.1006/JMBI.1999.3151
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.L.LUSCHINSKY,W.R.DUNHAM,C.OSBORNE,K.A.PATTRIDGE,M.L.LUDWIG
REMARK 1 TITL STRUCTURAL ANALYSIS OF FULLY REDUCED A. NIDULANS FLAVODOXIN
REMARK 1 REF FLAVINS AND FLAVOPROTEINS V. 10 409 1991
REMARK 1 REFN
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.E.LAUDENBACH,N.A.STRAUS,K.A.PATTRIDGE,M.L.LUDWIG
REMARK 1 TITL SEQUENCE AND STRUCTURE OF ANACYSTIS-NIDULANS FLAVODOXIN
REMARK 1 TITL 2 COMPARISONS WITH FLAVODOXINS FROM OTHER SPECIES
REMARK 1 REF FLAVINS AND FLAVOPROTEINS V. 9 249 1987
REMARK 1 REFN
REMARK 1 REFERENCE 3
REMARK 1 AUTH W.W.SMITH,K.A.PATTRIDGE,M.L.LUDWIG,G.A.PETSKO,D.TSERNOGLOU,
REMARK 1 AUTH 2 M.TANAKA,K.T.YASUNOBU
REMARK 1 TITL STRUCTURE OF OXIDIZED FLAVODOXIN FROM ANACYSTIS NIDULANS
REMARK 1 REF J.MOL.BIOL. V. 165 737 1983
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1016/S0022-2836(83)80277-0
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 19938
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : A POSTERIORI
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1980
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.81
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2816
REMARK 3 BIN R VALUE (WORKING SET) : 0.2560
REMARK 3 BIN FREE R VALUE : 0.2610
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 328
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.014
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1318
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 100
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.19
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.21
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.19
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.360 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.910 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.550 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.910 ; 2.500
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM.FMN
REMARK 3 PARAMETER FILE 3 : PARAM.WAT
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH.FMN
REMARK 3 TOPOLOGY FILE 3 : TOPH.WAT
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CZN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-SEP-99.
REMARK 100 THE DEPOSITION ID IS D_1000009650.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JUL-88
REMARK 200 TEMPERATURE (KELVIN) : 277
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SDMS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SDMS
REMARK 200 DATA SCALING SOFTWARE : SDMS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19844
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 2.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, POTASSIUM PHOSPHATE,
REMARK 280 PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 28.54000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 22.77500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.62000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 22.77500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.54000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.62000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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: 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 ASN A 97 35.27 -144.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN A 170
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OFV RELATED DB: PDB
REMARK 900 FURTHER REFINEMENT OF THE DATA USING X-PLOR
REMARK 900 RELATED ID: 1CZN RELATED DB: PDB
REMARK 900 WILDTYPE FORM I OXIDIZED FLAVODOXIN
REMARK 900 RELATED ID: 1CZU RELATED DB: PDB
REMARK 900 WILDTYPE FORM II OXIDIZED FLAVODOXIN
REMARK 900 RELATED ID: 1CZL RELATED DB: PDB
REMARK 900 WILDTYPE SEMIQUINONE FLAVODOXIN
REMARK 900 RELATED ID: 1D04 RELATED DB: PDB
REMARK 900 WILDTYPE HYDROQUINONE FLAVODOXIN
REMARK 900 RELATED ID: 1D03 RELATED DB: PDB
REMARK 900 MUTANT N58G OXIDIZED FLAVODOXIN
REMARK 900 RELATED ID: 1CZH RELATED DB: PDB
REMARK 900 MUTANT N58G SEMIQUINONE FLAVODOXIN
REMARK 900 RELATED ID: 1CZO RELATED DB: PDB
REMARK 900 MUTANT N58G HYDROQUINONE FLAVODOXIN
REMARK 900 RELATED ID: 1CZR RELATED DB: PDB
REMARK 900 MUTANT D90N OXIDIZED FLAVODOXIN
REMARK 900 RELATED ID: 1CZK RELATED DB: PDB
REMARK 900 MUTANT D100N OXIDIZED FLAVODOXIN
DBREF 1CZN A 1 169 UNP P10340 FLAV_SYNP7 1 169
SEQRES 1 A 169 ALA LYS ILE GLY LEU PHE TYR GLY THR GLN THR GLY VAL
SEQRES 2 A 169 THR GLN THR ILE ALA GLU SER ILE GLN GLN GLU PHE GLY
SEQRES 3 A 169 GLY GLU SER ILE VAL ASP LEU ASN ASP ILE ALA ASN ALA
SEQRES 4 A 169 ASP ALA SER ASP LEU ASN ALA TYR ASP TYR LEU ILE ILE
SEQRES 5 A 169 GLY CYS PRO THR TRP ASN VAL GLY GLU LEU GLN SER ASP
SEQRES 6 A 169 TRP GLU GLY ILE TYR ASP ASP LEU ASP SER VAL ASN PHE
SEQRES 7 A 169 GLN GLY LYS LYS VAL ALA TYR PHE GLY ALA GLY ASP GLN
SEQRES 8 A 169 VAL GLY TYR SER ASP ASN PHE GLN ASP ALA MET GLY ILE
SEQRES 9 A 169 LEU GLU GLU LYS ILE SER SER LEU GLY SER GLN THR VAL
SEQRES 10 A 169 GLY TYR TRP PRO ILE GLU GLY TYR ASP PHE ASN GLU SER
SEQRES 11 A 169 LYS ALA VAL ARG ASN ASN GLN PHE VAL GLY LEU ALA ILE
SEQRES 12 A 169 ASP GLU ASP ASN GLN PRO ASP LEU THR LYS ASN ARG ILE
SEQRES 13 A 169 LYS THR TRP VAL SER GLN LEU LYS SER GLU PHE GLY LEU
HET FMN A 170 31
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
FORMUL 2 FMN C17 H21 N4 O9 P
FORMUL 3 HOH *100(H2 O)
HELIX 1 1 GLY A 12 GLY A 26 1 15
HELIX 2 2 ALA A 37 ALA A 39 5 3
HELIX 3 3 ASP A 40 TYR A 47 5 8
HELIX 4 4 GLN A 63 TYR A 70 1 8
HELIX 5 5 ASP A 71 VAL A 76 5 6
HELIX 6 6 GLN A 99 LEU A 112 1 14
HELIX 7 7 GLN A 148 ASP A 150 5 3
HELIX 8 8 LEU A 151 PHE A 167 1 17
SHEET 1 A 5 VAL A 31 ASP A 35 0
SHEET 2 A 5 ILE A 3 TYR A 7 1 O ILE A 3 N ASP A 32
SHEET 3 A 5 TYR A 49 GLY A 53 1 O TYR A 49 N GLY A 4
SHEET 4 A 5 LYS A 82 ALA A 88 1 O LYS A 82 N LEU A 50
SHEET 5 A 5 GLN A 115 THR A 116 1 O GLN A 115 N VAL A 83
SHEET 1 A1 5 VAL A 31 ASP A 35 0
SHEET 2 A1 5 ILE A 3 TYR A 7 1 O ILE A 3 N ASP A 32
SHEET 3 A1 5 TYR A 49 GLY A 53 1 O TYR A 49 N GLY A 4
SHEET 4 A1 5 LYS A 82 ALA A 88 1 O LYS A 82 N LEU A 50
SHEET 5 A1 5 LEU A 141 ILE A 143 1 N LEU A 141 O TYR A 85
SHEET 1 B 2 THR A 56 TRP A 57 0
SHEET 2 B 2 GLU A 61 LEU A 62 -1 N GLU A 61 O TRP A 57
SHEET 1 C 3 TRP A 120 PRO A 121 0
SHEET 2 C 3 GLN A 137 PHE A 138 -1 N PHE A 138 O TRP A 120
SHEET 3 C 3 VAL A 133 ARG A 134 -1 N ARG A 134 O GLN A 137
SITE 1 AC1 25 THR A 9 GLN A 10 THR A 11 GLY A 12
SITE 2 AC1 25 VAL A 13 THR A 14 PRO A 55 THR A 56
SITE 3 AC1 25 TRP A 57 ASN A 58 VAL A 59 GLY A 60
SITE 4 AC1 25 ALA A 88 GLY A 89 ASP A 90 TYR A 94
SITE 5 AC1 25 ASN A 97 PHE A 98 GLN A 99 TYR A 119
SITE 6 AC1 25 ARG A 134 ASP A 146 HOH A 173 HOH A 174
SITE 7 AC1 25 HOH A 181
CRYST1 57.080 69.240 45.550 90.00 90.00 90.00 P 21 21 21 4
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 0.017519 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014443 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021954 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
