HEADER TRANSFERASE/TRANSFERASE INHIBITOR 15-NOV-11 3UNK
TITLE CDK2 IN COMPLEX WITH INHIBITOR YL5-083
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLIN-DEPENDENT KINASE 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CELL DIVISION PROTEIN KINASE 2, P33 PROTEIN KINASE;
COMPND 5 EC: 2.7.11.22;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CDK2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TUNER(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX6P-1
KEYWDS PROTEIN KINASE, ALLOSTERIC LIGAND, ANS, TRANSFERASE-TRANSFERASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.-Y.ZHU,M.P.MARTIN,R.ALAM,E.SCHONBRUNN
REVDAT 3 13-SEP-23 3UNK 1 REMARK
REVDAT 2 02-MAY-12 3UNK 1 JRNL
REVDAT 1 25-JAN-12 3UNK 0
JRNL AUTH M.P.MARTIN,J.Y.ZHU,H.R.LAWRENCE,R.PIREDDU,Y.LUO,R.ALAM,
JRNL AUTH 2 S.OZCAN,S.M.SEBTI,N.J.LAWRENCE,E.SCHONBRUNN
JRNL TITL A NOVEL MECHANISM BY WHICH SMALL MOLECULE INHIBITORS INDUCE
JRNL TITL 2 THE DFG FLIP IN AURORA A.
JRNL REF ACS CHEM.BIOL. V. 7 698 2012
JRNL REFN ISSN 1554-8929
JRNL PMID 22248356
JRNL DOI 10.1021/CB200508B
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.74
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 16682
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 835
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 18.7448 - 3.8071 1.00 2775 147 0.1732 0.2070
REMARK 3 2 3.8071 - 3.0259 1.00 2654 139 0.1802 0.2334
REMARK 3 3 3.0259 - 2.6446 1.00 2627 138 0.1856 0.2533
REMARK 3 4 2.6446 - 2.4034 1.00 2608 138 0.1783 0.2642
REMARK 3 5 2.4034 - 2.2314 1.00 2604 137 0.1779 0.2497
REMARK 3 6 2.2314 - 2.1000 1.00 2579 136 0.1766 0.2582
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 38.84
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.020
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.82210
REMARK 3 B22 (A**2) : -4.67290
REMARK 3 B33 (A**2) : 7.49500
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.010 2462
REMARK 3 ANGLE : 1.305 3341
REMARK 3 CHIRALITY : 0.098 372
REMARK 3 PLANARITY : 0.008 421
REMARK 3 DIHEDRAL : 17.522 917
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3UNK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-NOV-11.
REMARK 100 THE DEPOSITION ID IS D_1000068977.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 7.5
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 MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16682
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : 0.07100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 0.23800
REMARK 200 R SYM FOR SHELL (I) : 0.29700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 3PXR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5 MG/ML CDK2 PROTEIN, 1.5 MM YL5-83, 5
REMARK 280 % (V/V) PEG 3350, 50 MM HEPES/NAOH (PH 7.5), 50 MM PHOSPHATE (NA/
REMARK 280 K, PH 7.5), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 26.47500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.18500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.01000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 36.18500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.47500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.01000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 LEU A 37
REMARK 465 ASP A 38
REMARK 465 THR A 39
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 40 CG CD OE1 OE2
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 LYS A 6 67.88 37.37
REMARK 500 GLU A 73 -136.86 52.43
REMARK 500 ARG A 126 -7.05 72.22
REMARK 500 ASP A 145 37.13 72.02
REMARK 500 THR A 158 -71.15 -71.31
REMARK 500 TYR A 159 -62.75 -133.02
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 0BY A 299
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 300
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3UNJ RELATED DB: PDB
REMARK 900 RELATED ID: 3UNZ RELATED DB: PDB
REMARK 900 RELATED ID: 3UO4 RELATED DB: PDB
REMARK 900 RELATED ID: 3UO5 RELATED DB: PDB
REMARK 900 RELATED ID: 3UO6 RELATED DB: PDB
REMARK 900 RELATED ID: 3UOD RELATED DB: PDB
REMARK 900 RELATED ID: 3UOH RELATED DB: PDB
REMARK 900 RELATED ID: 3UOJ RELATED DB: PDB
REMARK 900 RELATED ID: 3UOK RELATED DB: PDB
REMARK 900 RELATED ID: 3UOL RELATED DB: PDB
REMARK 900 RELATED ID: 3UP2 RELATED DB: PDB
REMARK 900 RELATED ID: 3UP7 RELATED DB: PDB
DBREF 3UNK A 1 298 UNP P24941 CDK2_HUMAN 1 298
SEQRES 1 A 298 MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY
SEQRES 2 A 298 THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR
SEQRES 3 A 298 GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR
SEQRES 4 A 298 GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE
SEQRES 5 A 298 SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS
SEQRES 6 A 298 LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU
SEQRES 7 A 298 VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET
SEQRES 8 A 298 ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE
SEQRES 9 A 298 LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE
SEQRES 10 A 298 CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO
SEQRES 11 A 298 GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU
SEQRES 12 A 298 ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL
SEQRES 13 A 298 ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR ARG
SEQRES 14 A 298 ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR
SEQRES 15 A 298 ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU
SEQRES 16 A 298 MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU
SEQRES 17 A 298 ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR
SEQRES 18 A 298 PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO
SEQRES 19 A 298 ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP
SEQRES 20 A 298 PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG
SEQRES 21 A 298 SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS
SEQRES 22 A 298 ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE
SEQRES 23 A 298 GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU
HET 0BY A 299 24
HET PO4 A 300 5
HETNAM 0BY 4-({4-[(2-CHLOROPHENYL)AMINO]PYRIMIDIN-2-YL}AMINO)
HETNAM 2 0BY BENZOIC ACID
HETNAM PO4 PHOSPHATE ION
FORMUL 2 0BY C17 H13 CL N4 O2
FORMUL 3 PO4 O4 P 3-
FORMUL 4 HOH *153(H2 O)
HELIX 1 1 PRO A 45 LYS A 56 1 12
HELIX 2 2 LEU A 87 SER A 94 1 8
HELIX 3 3 PRO A 100 HIS A 121 1 22
HELIX 4 4 LYS A 129 GLN A 131 5 3
HELIX 5 5 GLY A 147 GLY A 153 1 7
HELIX 6 6 ALA A 170 LEU A 175 1 6
HELIX 7 7 THR A 182 ARG A 199 1 18
HELIX 8 8 SER A 207 GLY A 220 1 14
HELIX 9 9 GLY A 229 MET A 233 5 5
HELIX 10 10 ASP A 247 VAL A 251 5 5
HELIX 11 11 ASP A 256 LEU A 267 1 12
HELIX 12 12 SER A 276 LEU A 281 1 6
HELIX 13 13 ALA A 282 GLN A 287 5 6
SHEET 1 A 5 GLU A 8 GLY A 13 0
SHEET 2 A 5 GLY A 16 ARG A 22 -1 O VAL A 18 N GLY A 11
SHEET 3 A 5 VAL A 29 ILE A 35 -1 O LEU A 32 N TYR A 19
SHEET 4 A 5 LYS A 75 GLU A 81 -1 O LEU A 76 N ILE A 35
SHEET 5 A 5 LEU A 66 THR A 72 -1 N LEU A 67 O VAL A 79
SHEET 1 B 3 GLN A 85 ASP A 86 0
SHEET 2 B 3 LEU A 133 ILE A 135 -1 O ILE A 135 N GLN A 85
SHEET 3 B 3 ILE A 141 LEU A 143 -1 O LYS A 142 N LEU A 134
SITE 1 AC1 16 ILE A 10 VAL A 18 ALA A 31 LYS A 33
SITE 2 AC1 16 PHE A 80 GLU A 81 PHE A 82 LEU A 83
SITE 3 AC1 16 HIS A 84 LYS A 89 GLN A 131 ASN A 132
SITE 4 AC1 16 LEU A 134 ASP A 145 HOH A 365 HOH A 376
SITE 1 AC2 10 GLY A 13 THR A 14 TYR A 15 LYS A 33
SITE 2 AC2 10 ASP A 127 LYS A 129 ASN A 132 ASP A 145
SITE 3 AC2 10 HOH A 369 HOH A 394
CRYST1 52.950 72.020 72.370 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 0.018886 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013885 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013818 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
