HEADER LIGASE/ANTAGONIST 09-JAN-13 4IPF
TITLE THE 1.7A CRYSTAL STRUCTURE OF HUMANIZED XENOPUS MDM2 WITH RO5045337
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE MDM2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 21-105;
COMPND 5 SYNONYM: DOUBLE MINUTE 2 PROTEIN, XDM2, P53-BINDING PROTEIN MDM2;
COMPND 6 EC: 6.3.2.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 3 ORGANISM_COMMON: CLAWED FROG,COMMON PLATANNA,PLATANNA;
SOURCE 4 ORGANISM_TAXID: 8355;
SOURCE 5 GENE: MDM2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PUBS 520
KEYWDS MDM2, P53, PROTEIN-PROTEIN INTERACTION, IMIDAZOLINE, E3 UBIQUITIN
KEYWDS 2 LIGASE, NUCLEUS, LIGASE-ANTAGONIST COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.J.GRAVES,C.LUKACS,R.U.KAMMLOTT,R.CROWTHER
REVDAT 2 24-APR-13 4IPF 1 JRNL
REVDAT 1 20-FEB-13 4IPF 0
JRNL AUTH C.TOVAR,B.GRAVES,K.PACKMAN,Z.FILIPOVIC,B.H.XIA,C.TARDELL,
JRNL AUTH 2 R.GARRIDO,E.LEE,K.KOLINSKY,K.H.TO,M.LINN,F.PODLASKI,
JRNL AUTH 3 P.WOVKULICH,B.VU,L.T.VASSILEV
JRNL TITL MDM2 SMALL-MOLECULE ANTAGONIST RG7112 ACTIVATES P53
JRNL TITL 2 SIGNALING AND REGRESSES HUMAN TUMORS IN PRECLINICAL CANCER
JRNL TITL 3 MODELS.
JRNL REF CANCER RES. V. 73 2587 2013
JRNL REFN ISSN 0008-5472
JRNL PMID 23400593
JRNL DOI 10.1158/0008-5472.CAN-12-2807
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.T.VASSILEV,B.T.VU,B.GRAVES,D.CARVAJAL,F.PODLASKI,
REMARK 1 AUTH 2 Z.FILIPOVIC,N.KONG,U.KAMMLOTT,C.LUKACS,C.KLEIN,N.FOTOUHI,
REMARK 1 AUTH 3 E.A.LIU
REMARK 1 TITL IN VIVO ACTIVATION OF THE P53 PATHWAY BY SMALL-MOLECULE
REMARK 1 TITL 2 ANTAGONISTS OF MDM2
REMARK 1 REF SCIENCE V. 303 844 2004
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2005
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 850326.780
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 10703
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 548
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.2130
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.2120
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 548
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : 0.0100
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 10703
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) (%) : 82.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1417
REMARK 3 BIN R VALUE (WORKING SET) : 0.3380
REMARK 3 BIN FREE R VALUE : 0.3890
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 78
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.044
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 690
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 59
REMARK 3 SOLVENT ATOMS : 137
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.64000
REMARK 3 B22 (A**2) : 2.63000
REMARK 3 B33 (A**2) : -1.99000
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) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.07
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) : 0.24
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.09
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.004
REMARK 3 BOND ANGLES (DEGREES) : 1.40
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.94
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) : 1.100 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.670 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.970 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.830 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 48.57
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARA
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : RO5045337.PRX
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : RO5045337.TPX
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4IPF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JAN-13.
REMARK 100 THE RCSB ID CODE IS RCSB077042.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JAN-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11957
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 36.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 82.6
REMARK 200 DATA REDUNDANCY : 3.580
REMARK 200 R MERGE (I) : 0.03700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 20.5
REMARK 200 DATA REDUNDANCY IN SHELL : 1.99
REMARK 200 R MERGE FOR SHELL (I) : 0.16900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50% SATURATED AMMONIUM SULFATE, 100 MM
REMARK 280 BIS-TRIS, PH 6.5, 5% (V/V) PEG200, 5 MM DTT, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 278.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 33.36200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 33.36200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 21.54150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 33.74650
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 21.54150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 33.74650
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 33.36200
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 21.54150
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 33.74650
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 33.36200
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 21.54150
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 33.74650
REMARK 290 SMTRY3 8 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 300 REMARK: THE FULL-LENGTH PROTEIN WOULD FORM A DIMER THROUGH ITS C-
REMARK 300 TERMINAL DOMAIN BUT THIS N-TERMINAL DOMAIN FORMS ONLY MONOMERS.
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 383 LIES ON A SPECIAL POSITION.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1F0 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RV1 RELATED DB: PDB
REMARK 900 EARLIER STRUCTURE WITH A RELATED CIS-IMIDAZOLINE COMPOUND
DBREF 4IPF A 21 105 UNP P56273 MDM2_XENLA 21 105
SEQADV 4IPF LEU A 50 UNP P56273 ILE 50 ENGINEERED MUTATION
SEQADV 4IPF HIS A 92 UNP P56273 PRO 92 ENGINEERED MUTATION
SEQADV 4IPF ILE A 95 UNP P56273 LEU 95 ENGINEERED MUTATION
SEQRES 1 A 85 GLU LYS LEU VAL GLN PRO THR PRO LEU LEU LEU SER LEU
SEQRES 2 A 85 LEU LYS SER ALA GLY ALA GLN LYS GLU THR PHE THR MET
SEQRES 3 A 85 LYS GLU VAL LEU TYR HIS LEU GLY GLN TYR ILE MET ALA
SEQRES 4 A 85 LYS GLN LEU TYR ASP GLU LYS GLN GLN HIS ILE VAL HIS
SEQRES 5 A 85 CYS SER ASN ASP PRO LEU GLY GLU LEU PHE GLY VAL GLN
SEQRES 6 A 85 GLU PHE SER VAL LYS GLU HIS ARG ARG ILE TYR ALA MET
SEQRES 7 A 85 ILE SER ARG ASN LEU VAL SER
HET 1F0 A 201 49
HET SO4 A 202 5
HET SO4 A 203 5
HETNAM 1F0 [(4S,5R)-2-(4-TERT-BUTYL-2-ETHOXYPHENYL)-4,5-BIS(4-
HETNAM 2 1F0 CHLOROPHENYL)-4,5-DIMETHYL-4,5-DIHYDRO-1H-IMIDAZOL-1-
HETNAM 3 1F0 YL]{4-[3-(METHYLSULFONYL)PROPYL]PIPERAZIN-1-
HETNAM 4 1F0 YL}METHANONE
HETNAM SO4 SULFATE ION
HETSYN 1F0 RO5045337, RG7112
FORMUL 2 1F0 C38 H48 CL2 N4 O4 S
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *137(H2 O)
HELIX 1 1 THR A 27 ALA A 37 1 11
HELIX 2 2 THR A 45 LYS A 60 1 16
HELIX 3 3 ASP A 76 PHE A 82 5 7
HELIX 4 4 GLU A 91 ARG A 101 1 11
SHEET 1 A 2 ILE A 70 HIS A 72 0
SHEET 2 A 2 GLU A 86 SER A 88 -1 O PHE A 87 N VAL A 71
SITE 1 AC1 17 LYS A 35 SER A 36 GLY A 38 LEU A 50
SITE 2 AC1 17 LEU A 53 GLY A 54 ILE A 57 MET A 58
SITE 3 AC1 17 GLN A 68 HIS A 69 GLN A 85 VAL A 89
SITE 4 AC1 17 HIS A 92 TYR A 96 HOH A 316 HOH A 341
SITE 5 AC1 17 HOH A 366
SITE 1 AC2 8 ASN A 75 GLU A 91 HIS A 92 ARG A 93
SITE 2 AC2 8 ARG A 94 HOH A 356 HOH A 379 HOH A 387
SITE 1 AC3 8 PHE A 82 GLY A 83 VAL A 84 ARG A 94
SITE 2 AC3 8 ARG A 101 HOH A 378 HOH A 416 HOH A 417
CRYST1 43.083 67.493 66.724 90.00 90.00 90.00 C 2 2 21 8
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 0.023211 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014816 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014987 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
