HEADER LIGASE 31-MAY-01 1JAT
TITLE MMS2/UBC13 UBIQUITIN CONJUGATING ENZYME COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2-17.5 KDA;
COMPND 3 CHAIN: A;
COMPND 4 EC: 6.3.2.19;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: UBIQUITIN-CONJUGATING ENZYME VARIANT MMS2;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: UBC13;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21PJY2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 13 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 14 ORGANISM_TAXID: 4932;
SOURCE 15 GENE: MMS2;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21PJY2;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET16B
KEYWDS UBIQUITIN, UBIQUITIN-CONJUGATING ENZYME, E2, UEV, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.P.VANDEMARK,R.M.HOFMANN,C.TSUI,C.M.PICKART,C.WOLBERGER
REVDAT 4 07-FEB-24 1JAT 1 SEQADV
REVDAT 3 24-FEB-09 1JAT 1 VERSN
REVDAT 2 01-APR-03 1JAT 1 JRNL
REVDAT 1 20-JUN-01 1JAT 0
JRNL AUTH A.P.VANDEMARK,R.M.HOFMANN,C.TSUI,C.M.PICKART,C.WOLBERGER
JRNL TITL MOLECULAR INSIGHTS INTO POLYUBIQUITIN CHAIN ASSEMBLY:
JRNL TITL 2 CRYSTAL STRUCTURE OF THE MMS2/UBC13 HETERODIMER.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 105 711 2001
JRNL REFN ISSN 0092-8674
JRNL PMID 11440714
JRNL DOI 10.1016/S0092-8674(01)00387-7
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1023636.200
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 36093
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 SET) : 0.203
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1810
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.67
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4144
REMARK 3 BIN R VALUE (WORKING SET) : 0.2900
REMARK 3 BIN FREE R VALUE : 0.3170
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 211
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2238
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 276
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.96000
REMARK 3 B22 (A**2) : -1.57000
REMARK 3 B33 (A**2) : -0.40000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -5.13000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.20
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) : 0.23
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.280
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) : 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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.42
REMARK 3 BSOL : 66.72
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 1JAT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-01.
REMARK 100 THE DEPOSITION ID IS D_1000013565.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-AUG-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9115
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36093
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.35900
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 1000, TRIS, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 31.89850
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 -1
REMARK 465 SER A 0
REMARK 465 GLU A 153
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 GLY B 20
REMARK 465 PHE B 21
REMARK 465 GLY B 22
REMARK 465 PRO B 23
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 13 CG CD OE1 OE2
REMARK 470 ASP A 29 CG OD1 OD2
REMARK 470 LYS A 149 CG CD CE NZ
REMARK 470 LYS A 150 CG CD CE NZ
REMARK 470 GLU B 24 CG CD OE1 OE2
REMARK 470 GLU B 54 CG CD OE1 OE2
REMARK 470 LYS B 104 CG CD CE NZ
REMARK 470 LYS B 127 CG CD CE NZ
REMARK 470 LYS B 132 CG CD CE NZ
REMARK 470 GLU B 133 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 92 -134.51 -113.11
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1JAT A 2 153 UNP P52490 UBC13_YEAST 2 153
DBREF 1JAT B 1 137 UNP P53152 MMS2_YEAST 1 137
SEQADV 1JAT GLY A -1 UNP P52490 CLONING ARTIFACT
SEQADV 1JAT SER A 0 UNP P52490 CLONING ARTIFACT
SEQADV 1JAT ALA A 1 UNP P52490 CLONING ARTIFACT
SEQADV 1JAT HIS B 0 UNP P53152 EXPRESSION TAG
SEQRES 1 A 155 GLY SER ALA ALA SER LEU PRO LYS ARG ILE ILE LYS GLU
SEQRES 2 A 155 THR GLU LYS LEU VAL SER ASP PRO VAL PRO GLY ILE THR
SEQRES 3 A 155 ALA GLU PRO HIS ASP ASP ASN LEU ARG TYR PHE GLN VAL
SEQRES 4 A 155 THR ILE GLU GLY PRO GLU GLN SER PRO TYR GLU ASP GLY
SEQRES 5 A 155 ILE PHE GLU LEU GLU LEU TYR LEU PRO ASP ASP TYR PRO
SEQRES 6 A 155 MET GLU ALA PRO LYS VAL ARG PHE LEU THR LYS ILE TYR
SEQRES 7 A 155 HIS PRO ASN ILE ASP ARG LEU GLY ARG ILE CYS LEU ASP
SEQRES 8 A 155 VAL LEU LYS THR ASN TRP SER PRO ALA LEU GLN ILE ARG
SEQRES 9 A 155 THR VAL LEU LEU SER ILE GLN ALA LEU LEU ALA SER PRO
SEQRES 10 A 155 ASN PRO ASN ASP PRO LEU ALA ASN ASP VAL ALA GLU ASP
SEQRES 11 A 155 TRP ILE LYS ASN GLU GLN GLY ALA LYS ALA LYS ALA ARG
SEQRES 12 A 155 GLU TRP THR LYS LEU TYR ALA LYS LYS LYS PRO GLU
SEQRES 1 B 138 HIS MET SER LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU
SEQRES 2 B 138 GLU LEU GLU LYS GLY GLU LYS GLY PHE GLY PRO GLU SER
SEQRES 3 B 138 CYS SER TYR GLY LEU ALA ASP SER ASP ASP ILE THR MET
SEQRES 4 B 138 THR LYS TRP ASN GLY THR ILE LEU GLY PRO PRO HIS SER
SEQRES 5 B 138 ASN HIS GLU ASN ARG ILE TYR SER LEU SER ILE ASP CYS
SEQRES 6 B 138 GLY PRO ASN TYR PRO ASP SER PRO PRO LYS VAL THR PHE
SEQRES 7 B 138 ILE SER LYS ILE ASN LEU PRO CYS VAL ASN PRO THR THR
SEQRES 8 B 138 GLY GLU VAL GLN THR ASP PHE HIS THR LEU ARG ASP TRP
SEQRES 9 B 138 LYS ARG ALA TYR THR MET GLU THR LEU LEU LEU ASP LEU
SEQRES 10 B 138 ARG LYS GLU MET ALA THR PRO ALA ASN LYS LYS LEU ARG
SEQRES 11 B 138 GLN PRO LYS GLU GLY GLU THR PHE
FORMUL 3 HOH *276(H2 O)
HELIX 1 1 PRO A 5 ASP A 18 1 14
HELIX 2 2 LEU A 88 LYS A 92 5 5
HELIX 3 3 GLN A 100 SER A 114 1 15
HELIX 4 4 VAL A 125 ASN A 132 1 8
HELIX 5 5 ASN A 132 ALA A 148 1 17
HELIX 6 6 PRO B 5 LYS B 19 1 15
HELIX 7 7 PHE B 97 ASP B 102 1 6
HELIX 8 8 THR B 108 ALA B 121 1 14
HELIX 9 9 THR B 122 LYS B 127 1 6
SHEET 1 A 4 ILE A 23 HIS A 28 0
SHEET 2 A 4 ASN A 31 GLU A 40 -1 N ASN A 31 O HIS A 28
SHEET 3 A 4 GLY A 50 TYR A 57 -1 N PHE A 52 O ILE A 39
SHEET 4 A 4 LYS A 68 PHE A 71 -1 N LYS A 68 O TYR A 57
SHEET 1 B 4 ILE A 23 HIS A 28 0
SHEET 2 B 4 ASN A 31 GLU A 40 -1 N ASN A 31 O HIS A 28
SHEET 3 B 4 GLY A 50 TYR A 57 -1 N PHE A 52 O ILE A 39
SHEET 4 B 4 LYS A 149 LYS A 150 -1 N LYS A 149 O ILE A 51
SHEET 1 C 4 CYS B 26 LEU B 30 0
SHEET 2 C 4 LYS B 40 LEU B 46 -1 N ASN B 42 O GLY B 29
SHEET 3 C 4 ILE B 57 ASP B 63 -1 N TYR B 58 O ILE B 45
SHEET 4 C 4 LYS B 74 PHE B 77 -1 O LYS B 74 N ASP B 63
CISPEP 1 TYR A 62 PRO A 63 0 1.06
CISPEP 2 TYR B 68 PRO B 69 0 0.48
CRYST1 43.158 63.797 53.152 90.00 105.83 90.00 P 1 21 1 2
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 0.023171 0.000000 0.006570 0.00000
SCALE2 0.000000 0.015675 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019556 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
