HEADER BINDING PROTEIN 15-MAR-96 1VIN
TITLE BOVINE CYCLIN A3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLIN A;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 OTHER_DETAILS: HIS 6 TAGGED AT C-TERMINUS
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 GENE: BOVINE CYCLIN A3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET21D;
SOURCE 9 EXPRESSION_SYSTEM_GENE: BOVINE CYCLIN A3
KEYWDS CYCLIN, CELL CYCLE, KINASE-REGULATORY-SUBUNIT, BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.E.M.NOBLE,J.A.E.ENDICOTT,N.R.BROWN
REVDAT 3 14-FEB-24 1VIN 1 REMARK
REVDAT 2 24-FEB-09 1VIN 1 VERSN
REVDAT 1 17-AUG-96 1VIN 0
JRNL AUTH N.R.BROWN,M.E.NOBLE,J.A.ENDICOTT,E.F.GARMAN,S.WAKATSUKI,
JRNL AUTH 2 E.MITCHELL,B.RASMUSSEN,T.HUNT,L.N.JOHNSON
JRNL TITL THE CRYSTAL STRUCTURE OF CYCLIN A.
JRNL REF STRUCTURE V. 3 1235 1995
JRNL REFN ISSN 0969-2126
JRNL PMID 8591034
JRNL DOI 10.1016/S0969-2126(01)00259-3
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.J.OWEN,M.E.M.NOBLE,E.F.GARMAN,A.C.PAPAGEORGIOU,L.N.JOHNSON
REMARK 1 TITL TWO STRUCTURES OF THE CATALYTIC DOMAIN OF PHOSPHORYLASE
REMARK 1 TITL 2 KINASE: AN ACTIVE PROTEIN KINASE COMPLEXED WITH SUBSTRATE
REMARK 1 TITL 3 ANALOGUE AND PRODUCT
REMARK 1 REF STRUCTURE V. 3 467 1995
REMARK 1 REFN ISSN 0969-2126
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.J.OWEN,A.C.PAPAGEORGIOU,E.F.GARMAN,M.E.NOBLE,L.N.JOHNSON
REMARK 1 TITL EXPRESSION, PURIFICATION AND CRYSTALLISATION OF
REMARK 1 TITL 2 PHOSPHORYLASE KINASE CATALYTIC DOMAIN
REMARK 1 REF J.MOL.BIOL. V. 246 374 1995
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
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) : 0.216
REMARK 3 FREE R VALUE : 0.299
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
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 : 2030
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 174
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.80
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) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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) : 3.840 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 5.580 ; 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 : NULL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1VIN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000177049.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : MAY-95
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX7.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.488
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17065
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.4
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
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 (%): 30.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 26.35000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.75000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.45000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.75000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.35000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.45000
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 GLY A 171
REMARK 465 VAL A 172
REMARK 465 ASN A 173
REMARK 465 GLU A 174
REMARK 465 VAL A 175
REMARK 465 PRO A 176
REMARK 465 ASP A 177
REMARK 465 TYR A 178
REMARK 465 HIS A 179
REMARK 465 GLU A 180
REMARK 465 HIS A 433
REMARK 465 HIS A 434
REMARK 465 HIS A 435
REMARK 465 HIS A 436
REMARK 465 HIS A 437
REMARK 465 HIS A 438
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU A 428 O HOH A 607 1455 1.13
REMARK 500 O HOH A 475 O HOH A 504 3755 1.71
REMARK 500 CD GLU A 428 O HOH A 607 1455 1.86
REMARK 500 OE1 GLU A 274 O HOH A 575 3745 2.12
REMARK 500 OE1 GLU A 428 O HOH A 607 1455 2.18
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 GLN A 323 -89.99 -28.43
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 TYR A 347 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1VIN A 172 431 UNP P30274 CCNA2_BOVIN 146 405
SEQRES 1 A 268 GLY VAL ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS
SEQRES 2 A 268 THR TYR LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS
SEQRES 3 A 268 VAL GLY TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER
SEQRES 4 A 268 MET ARG ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY
SEQRES 5 A 268 GLU GLU TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA
SEQRES 6 A 268 VAL ASN TYR ILE ASP ARG PHE LEU SER SER MET SER VAL
SEQRES 7 A 268 LEU ARG GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET
SEQRES 8 A 268 LEU LEU ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU
SEQRES 9 A 268 VAL ALA GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR
SEQRES 10 A 268 LYS LYS GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS
SEQRES 11 A 268 VAL LEU ALA PHE ASP LEU ALA ALA PRO THR ILE ASN GLN
SEQRES 12 A 268 PHE LEU THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN
SEQRES 13 A 268 CYS LYS VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU
SEQRES 14 A 268 SER LEU ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO
SEQRES 15 A 268 SER VAL ILE ALA ALA ALA ALA PHE HIS LEU ALA LEU TYR
SEQRES 16 A 268 THR VAL THR GLY GLN SER TRP PRO GLU SER LEU VAL GLN
SEQRES 17 A 268 LYS THR GLY TYR THR LEU GLU THR LEU LYS PRO CYS LEU
SEQRES 18 A 268 LEU ASP LEU HIS GLN THR TYR LEU ARG ALA PRO GLN HIS
SEQRES 19 A 268 ALA GLN GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS
SEQRES 20 A 268 TYR HIS GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU
SEQRES 21 A 268 ASN LEU HIS HIS HIS HIS HIS HIS
FORMUL 2 HOH *174(H2 O)
HELIX 1 1 ILE A 182 CYS A 193 1 12
HELIX 2 2 TYR A 199 LYS A 202 5 4
HELIX 3 3 ASN A 208 GLU A 224 1 17
HELIX 4 4 ASN A 229 LEU A 243 1 15
HELIX 5 5 ARG A 250 GLU A 268 1 19
HELIX 6 6 VAL A 275 THR A 282 1 8
HELIX 7 7 LYS A 288 VAL A 301 1 14
HELIX 8 8 ILE A 311 HIS A 321 1 11
HELIX 9 9 CYS A 327 ILE A 342 1 16
HELIX 10 10 ALA A 344 LYS A 349 1 6
HELIX 11 11 PRO A 352 THR A 368 1 17
HELIX 12 12 GLU A 374 THR A 380 1 7
HELIX 13 13 LYS A 388 GLN A 403 1 16
HELIX 14 14 SER A 408 LYS A 414 1 7
HELIX 15 15 SER A 416 TYR A 418 5 3
HELIX 16 16 VAL A 421 LEU A 423 5 3
CISPEP 1 ASP A 345 PRO A 346 0 0.97
CRYST1 52.700 60.900 83.500 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 0.018975 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016420 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011976 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
