HEADER TRANSCRIPTION/DNA 13-FEB-96 1TGH
TITLE TATA BINDING PROTEIN (TBP)/DNA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-D(*CP*GP*TP*AP*TP*AP*TP*AP*TP*AP*CP*G)-3');
COMPND 3 CHAIN: B, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: PROTEIN (TATA BINDING PROTEIN (TBP));
COMPND 7 CHAIN: A;
COMPND 8 SYNONYM: HTBP;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 5 ORGANISM_COMMON: HUMAN;
SOURCE 6 ORGANISM_TAXID: 9606;
SOURCE 7 GENE: TBP;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI K12;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: K12;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET21D
KEYWDS TRANSCRIPTION FACTOR, DNA BINDING PROTEIN, DNA, TRANSCRIPTION-DNA
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.S.JUO,R.E.DICKERSON
REVDAT 4 14-FEB-24 1TGH 1 SEQADV
REVDAT 3 24-FEB-09 1TGH 1 VERSN
REVDAT 2 01-APR-03 1TGH 1 JRNL
REVDAT 1 01-AUG-96 1TGH 0
JRNL AUTH Z.S.JUO,T.K.CHIU,P.M.LEIBERMAN,I.BAIKALOV,A.J.BERK,
JRNL AUTH 2 R.E.DICKERSON
JRNL TITL HOW PROTEINS RECOGNIZE THE TATA BOX.
JRNL REF J.MOL.BIOL. V. 261 239 1996
JRNL REFN ISSN 0022-2836
JRNL PMID 8757291
JRNL DOI 10.1006/JMBI.1996.0456
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.L.KIM,S.K.BURLEY
REMARK 1 TITL 1.9 A RESOLUTION REFINED STRUCTURE OF TBP RECOGNIZING THE
REMARK 1 TITL 2 MINOR GROOVE OF TATAAAAG
REMARK 1 REF NAT.STRUCT.BIOL. V. 1 638 1994
REMARK 1 REFN ISSN 1072-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.L.KIM,D.B.NIKOLOV,S.K.BURLEY
REMARK 1 TITL CO-CRYSTAL STRUCTURE OF TBP RECOGNIZING THE MINOR GROOVE OF
REMARK 1 TITL 2 A TATA ELEMENT
REMARK 1 REF NATURE V. 365 520 1993
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. 2.90 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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
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 : 9013
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) : 0.214
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
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 : 1429
REMARK 3 NUCLEIC ACID ATOMS : 486
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 18
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) : 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) : 2.000
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.50
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.490
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TGH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY NDB.
REMARK 100 THE DEPOSITION ID IS D_1000176666.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-APR-95
REMARK 200 TEMPERATURE (KELVIN) : 92.00
REMARK 200 PH : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05500
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.00
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 33.48250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.11300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.69850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.11300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.48250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.69850
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, 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 151
REMARK 465 SER A 152
REMARK 465 ARG A 153
REMARK 465 GLY A 154
REMARK 465 THR A 335
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O2 DC B 111 H22 DG C 114 1.54
REMARK 500 H3 DT B 103 N1 DA C 122 1.58
REMARK 500 H3 DT B 109 N1 DA C 116 1.60
REMARK 500 H22 DG B 102 O2 DC C 123 1.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 DC B 101 O5' - C5' - C4' ANGL. DEV. = -5.0 DEGREES
REMARK 500 PRO A 243 C - N - CA ANGL. DEV. = 10.7 DEGREES
REMARK 500 PRO A 281 C - N - CA ANGL. DEV. = 10.7 DEGREES
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 CYS A 172 116.05 175.17
REMARK 500 ARG A 184 -45.13 56.50
REMARK 500 ASN A 189 88.66 -159.64
REMARK 500 PRO A 190 -1.11 -54.77
REMARK 500 GLU A 202 116.81 -163.90
REMARK 500 ARG A 204 106.70 -49.13
REMARK 500 ALA A 220 179.94 -38.95
REMARK 500 LYS A 221 14.49 -144.99
REMARK 500 PRO A 243 70.17 -63.66
REMARK 500 LYS A 261 56.01 72.36
REMARK 500 PHE A 262 148.57 165.47
REMARK 500 HIS A 273 22.04 -140.07
REMARK 500 ARG A 295 82.56 -68.54
REMARK 500 ARG A 314 -39.09 -39.10
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1TGH A 151 335 UNP P20226 TBP_HUMAN 113 297
DBREF 1TGH B 101 112 PDB 1TGH 1TGH 101 112
DBREF 1TGH C 113 124 PDB 1TGH 1TGH 113 124
SEQADV 1TGH GLY A 151 UNP P20226 ALA 113 CONFLICT
SEQADV 1TGH ARG A 153 UNP P20226 GLU 115 CONFLICT
SEQADV 1TGH GLY A 154 UNP P20226 SER 116 CONFLICT
SEQRES 1 B 12 DC DG DT DA DT DA DT DA DT DA DC DG
SEQRES 1 C 12 DC DG DT DA DT DA DT DA DT DA DC DG
SEQRES 1 A 185 GLY SER ARG GLY SER GLY ILE VAL PRO GLN LEU GLN ASN
SEQRES 2 A 185 ILE VAL SER THR VAL ASN LEU GLY CYS LYS LEU ASP LEU
SEQRES 3 A 185 LYS THR ILE ALA LEU ARG ALA ARG ASN ALA GLU TYR ASN
SEQRES 4 A 185 PRO LYS ARG PHE ALA ALA VAL ILE MET ARG ILE ARG GLU
SEQRES 5 A 185 PRO ARG THR THR ALA LEU ILE PHE SER SER GLY LYS MET
SEQRES 6 A 185 VAL CYS THR GLY ALA LYS SER GLU GLU GLN SER ARG LEU
SEQRES 7 A 185 ALA ALA ARG LYS TYR ALA ARG VAL VAL GLN LYS LEU GLY
SEQRES 8 A 185 PHE PRO ALA LYS PHE LEU ASP PHE LYS ILE GLN ASN MET
SEQRES 9 A 185 VAL GLY SER CYS ASP VAL LYS PHE PRO ILE ARG LEU GLU
SEQRES 10 A 185 GLY LEU VAL LEU THR HIS GLN GLN PHE SER SER TYR GLU
SEQRES 11 A 185 PRO GLU LEU PHE PRO GLY LEU ILE TYR ARG MET ILE LYS
SEQRES 12 A 185 PRO ARG ILE VAL LEU LEU ILE PHE VAL SER GLY LYS VAL
SEQRES 13 A 185 VAL LEU THR GLY ALA LYS VAL ARG ALA GLU ILE TYR GLU
SEQRES 14 A 185 ALA PHE GLU ASN ILE TYR PRO ILE LEU LYS GLY PHE ARG
SEQRES 15 A 185 LYS THR THR
FORMUL 4 HOH *18(H2 O)
HELIX 1 1 LEU A 176 ARG A 182 1 7
HELIX 2 2 GLU A 223 GLY A 241 1 19
HELIX 3 3 LEU A 266 THR A 272 1 7
HELIX 4 4 ARG A 314 PHE A 331 1 18
SHEET 1 A 5 SER A 166 ASN A 169 0
SHEET 2 A 5 LYS A 214 THR A 218 -1 N CYS A 217 O SER A 166
SHEET 3 A 5 THR A 206 PHE A 210 -1 N LEU A 208 O VAL A 216
SHEET 4 A 5 ALA A 195 MET A 198 -1 N MET A 198 O ALA A 207
SHEET 5 A 5 ALA A 186 TYR A 188 -1 N GLU A 187 O ILE A 197
SHEET 1 B 5 GLY A 286 ARG A 290 0
SHEET 2 B 5 VAL A 297 PHE A 301 -1 N ILE A 300 O LEU A 287
SHEET 3 B 5 LYS A 305 THR A 309 -1 N THR A 309 O VAL A 297
SHEET 4 B 5 ASN A 253 ASP A 259 -1 N CYS A 258 O VAL A 306
SHEET 5 B 5 GLN A 160 VAL A 165 -1 N VAL A 165 O ASN A 253
CISPEP 1 GLU A 202 PRO A 203 0 0.04
CISPEP 2 LYS A 293 PRO A 294 0 0.13
CRYST1 66.965 67.397 86.226 90.00 90.00 90.00 P 21 21 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 0.014933 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014837 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011597 0.00000
(ATOM LINES ARE NOT SHOWN.)
END