HEADER OXIDOREDUCTASE 10-OCT-98 1BX0
TITLE FERREDOXIN:NADP+ OXIDOREDUCTASE (FERREDOXIN REDUCTASE) MUTANT E312L
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (FERREDOXIN:NADP+ OXIDOREDUCTASE);
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.18.1.2;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA;
SOURCE 3 ORGANISM_COMMON: SPINACH;
SOURCE 4 ORGANISM_TAXID: 3562;
SOURCE 5 ORGAN: LEAF;
SOURCE 6 ORGANELLE: CHLOROPLAST;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: RRIDM15
KEYWDS FLAVOPROTEIN, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ALIVERTI,Z.DENG,D.RAVASI,L.PIUBELLI,P.A.KARPLUS,G.ZANETTI
REVDAT 6 09-AUG-23 1BX0 1 REMARK SEQADV
REVDAT 5 14-MAR-18 1BX0 1 SEQADV
REVDAT 4 24-FEB-09 1BX0 1 VERSN
REVDAT 3 24-MAY-05 1BX0 1 COMPND SOURCE KEYWDS REVDAT
REVDAT 3 2 1 JRNL REMARK MASTER
REVDAT 2 22-DEC-99 1BX0 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 14-OCT-98 1BX0 0
JRNL AUTH A.ALIVERTI,Z.DENG,D.RAVASI,L.PIUBELLI,P.A.KARPLUS,G.ZANETTI
JRNL TITL PROBING THE FUNCTION OF THE INVARIANT GLUTAMYL RESIDUE 312
JRNL TITL 2 IN SPINACH FERREDOXIN-NADP+ REDUCTASE.
JRNL REF J.BIOL.CHEM. V. 273 34008 1998
JRNL REFN ISSN 0021-9258
JRNL PMID 9852055
JRNL DOI 10.1074/JBC.273.51.34008
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
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 : 27296
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.99
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3303
REMARK 3 BIN R VALUE (WORKING SET) : 0.2980
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2355
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 63
REMARK 3 SOLVENT ATOMS : 220
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.720
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.230
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
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 : PARAFAD.PRO
REMARK 3 PARAMETER FILE 3 : PARAM19.SOL
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPFAD.PRO
REMARK 3 TOPOLOGY FILE 3 : TOPH19.SOL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BX0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000008130.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 4.5
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27690
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.37500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1FNB
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): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 45.60000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 45.60000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 29.00000
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLN A 1
REMARK 465 ILE A 2
REMARK 465 ALA A 3
REMARK 465 SER A 4
REMARK 465 ASP A 5
REMARK 465 VAL A 6
REMARK 465 GLU A 7
REMARK 465 ALA A 8
REMARK 465 PRO A 9
REMARK 465 PRO A 10
REMARK 465 PRO A 11
REMARK 465 ALA A 12
REMARK 465 PRO A 13
REMARK 465 ALA A 14
REMARK 465 LYS A 15
REMARK 465 VAL A 16
REMARK 465 GLU A 17
REMARK 465 LYS A 18
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 ALA A 53 133.86 -33.99
REMARK 500 LYS A 275 -38.15 -37.04
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 PO4 A 316
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 317
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 315
DBREF 1BX0 A 1 314 UNP P00455 FENR_SPIOL 56 369
SEQADV 1BX0 LEU A 312 UNP P00455 GLU 367 ENGINEERED MUTATION
SEQRES 1 A 314 GLN ILE ALA SER ASP VAL GLU ALA PRO PRO PRO ALA PRO
SEQRES 2 A 314 ALA LYS VAL GLU LYS HIS SER LYS LYS MET GLU GLU GLY
SEQRES 3 A 314 ILE THR VAL ASN LYS PHE LYS PRO LYS THR PRO TYR VAL
SEQRES 4 A 314 GLY ARG CYS LEU LEU ASN THR LYS ILE THR GLY ASP ASP
SEQRES 5 A 314 ALA PRO GLY GLU THR TRP HIS MET VAL PHE SER HIS GLU
SEQRES 6 A 314 GLY GLU ILE PRO TYR ARG GLU GLY GLN SER VAL GLY VAL
SEQRES 7 A 314 ILE PRO ASP GLY GLU ASP LYS ASN GLY LYS PRO HIS LYS
SEQRES 8 A 314 LEU ARG LEU TYR SER ILE ALA SER SER ALA LEU GLY ASP
SEQRES 9 A 314 PHE GLY ASP ALA LYS SER VAL SER LEU CYS VAL LYS ARG
SEQRES 10 A 314 LEU ILE TYR THR ASN ASP ALA GLY GLU THR ILE LYS GLY
SEQRES 11 A 314 VAL CYS SER ASN PHE LEU CYS ASP LEU LYS PRO GLY ALA
SEQRES 12 A 314 GLU VAL LYS LEU THR GLY PRO VAL GLY LYS GLU MET LEU
SEQRES 13 A 314 MET PRO LYS ASP PRO ASN ALA THR ILE ILE MET LEU GLY
SEQRES 14 A 314 THR GLY THR GLY ILE ALA PRO PHE ARG SER PHE LEU TRP
SEQRES 15 A 314 LYS MET PHE PHE GLU LYS HIS ASP ASP TYR LYS PHE ASN
SEQRES 16 A 314 GLY LEU ALA TRP LEU PHE LEU GLY VAL PRO THR SER SER
SEQRES 17 A 314 SER LEU LEU TYR LYS GLU GLU PHE GLU LYS MET LYS GLU
SEQRES 18 A 314 LYS ALA PRO ASP ASN PHE ARG LEU ASP PHE ALA VAL SER
SEQRES 19 A 314 ARG GLU GLN THR ASN GLU LYS GLY GLU LYS MET TYR ILE
SEQRES 20 A 314 GLN THR ARG MET ALA GLN TYR ALA VAL GLU LEU TRP GLU
SEQRES 21 A 314 MET LEU LYS LYS ASP ASN THR TYR PHE TYR MET CYS GLY
SEQRES 22 A 314 LEU LYS GLY MET GLU LYS GLY ILE ASP ASP ILE MET VAL
SEQRES 23 A 314 SER LEU ALA ALA ALA GLU GLY ILE ASP TRP ILE GLU TYR
SEQRES 24 A 314 LYS ARG GLN LEU LYS LYS ALA GLU GLN TRP ASN VAL LEU
SEQRES 25 A 314 VAL TYR
HET PO4 A 316 5
HET SO4 A 317 5
HET FAD A 315 53
HETNAM PO4 PHOSPHATE ION
HETNAM SO4 SULFATE ION
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
FORMUL 2 PO4 O4 P 3-
FORMUL 3 SO4 O4 S 2-
FORMUL 4 FAD C27 H33 N9 O15 P2
FORMUL 5 HOH *220(H2 O)
HELIX 1 1 PRO A 34 THR A 36 5 3
HELIX 2 2 VAL A 131 ASP A 138 1 8
HELIX 3 3 GLY A 171 PHE A 185 5 15
HELIX 4 4 SER A 207 SER A 209 5 3
HELIX 5 5 LYS A 213 LYS A 222 1 10
HELIX 6 6 ILE A 247 LYS A 263 1 17
HELIX 7 7 LYS A 275 GLU A 292 5 18
HELIX 8 8 TRP A 296 LYS A 305 1 10
SHEET 1 A 6 LEU A 92 SER A 96 0
SHEET 2 A 6 SER A 75 ILE A 79 -1 N VAL A 78 O ARG A 93
SHEET 3 A 6 GLU A 144 THR A 148 -1 N THR A 148 O GLY A 77
SHEET 4 A 6 TYR A 38 LYS A 47 -1 N GLY A 40 O VAL A 145
SHEET 5 A 6 THR A 57 SER A 63 -1 N SER A 63 O ARG A 41
SHEET 6 A 6 SER A 110 LYS A 116 -1 N VAL A 115 O TRP A 58
SHEET 1 B 2 ILE A 119 THR A 121 0
SHEET 2 B 2 THR A 127 LYS A 129 -1 N ILE A 128 O TYR A 120
SHEET 1 C 5 TRP A 309 TYR A 314 0
SHEET 2 C 5 THR A 267 LEU A 274 1 N PHE A 269 O ASN A 310
SHEET 3 C 5 THR A 164 THR A 170 1 N THR A 164 O TYR A 268
SHEET 4 C 5 LEU A 197 VAL A 204 1 N LEU A 197 O ILE A 165
SHEET 5 C 5 PHE A 227 VAL A 233 1 N ARG A 228 O ALA A 198
CISPEP 1 GLY A 149 PRO A 150 0 1.31
SITE 1 AC1 4 SER A 234 ARG A 235 LYS A 244 TYR A 246
SITE 1 AC2 4 ASP A 84 HIS A 90 LYS A 91 ARG A 93
SITE 1 AC3 21 ARG A 93 LEU A 94 TYR A 95 SER A 96
SITE 2 AC3 21 CYS A 114 VAL A 115 LYS A 116 TYR A 120
SITE 3 AC3 21 GLY A 130 VAL A 131 CYS A 132 SER A 133
SITE 4 AC3 21 THR A 172 TYR A 314 HOH A 404 HOH A 406
SITE 5 AC3 21 HOH A 407 HOH A 418 HOH A 423 HOH A 526
SITE 6 AC3 21 HOH A 549
CRYST1 91.200 58.000 68.200 90.00 99.90 90.00 C 1 2 1 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 0.010965 0.000000 0.001914 0.00000
SCALE2 0.000000 0.017241 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014884 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
