HEADER TRANSFERASE 10-JUN-15 5AUU
TITLE CRYSTAL STRUCTURE OF DAPK1 IN COMPLEX WITH LUTEOLIN.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEATH-ASSOCIATED PROTEIN KINASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-285;
COMPND 5 SYNONYM: DAP KINASE 1;
COMPND 6 EC: 2.7.11.1;
COMPND 7 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: DAPK1, DAPK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-20B(+)
KEYWDS DEATH-ASSOCIATED PROTEIN KINASE 1, SERINE/THREONINE PROTEIN KINASE,
KEYWDS 2 NATURAL FLAVONOID, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.YOKOYAMA,M.MIZUGUCHI
REVDAT 3 20-MAR-24 5AUU 1 REMARK
REVDAT 2 19-FEB-20 5AUU 1 SOURCE KEYWDS JRNL REMARK
REVDAT 1 07-OCT-15 5AUU 0
JRNL AUTH T.YOKOYAMA,Y.KOSAKA,M.MIZUGUCHI
JRNL TITL STRUCTURAL INSIGHT INTO THE INTERACTIONS BETWEEN
JRNL TITL 2 DEATH-ASSOCIATED PROTEIN KINASE 1 AND NATURAL FLAVONOIDS.
JRNL REF J.MED.CHEM. V. 58 7400 2015
JRNL REFN ISSN 0022-2623
JRNL PMID 26322379
JRNL DOI 10.1021/ACS.JMEDCHEM.5B00893
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.07
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 28134
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 1414
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 36.0759 - 3.6617 0.98 2914 151 0.1799 0.2018
REMARK 3 2 3.6617 - 2.9068 0.99 2784 147 0.1741 0.2218
REMARK 3 3 2.9068 - 2.5395 0.98 2729 171 0.1828 0.2189
REMARK 3 4 2.5395 - 2.3073 0.98 2675 151 0.1800 0.2267
REMARK 3 5 2.3073 - 2.1420 0.97 2702 134 0.1629 0.2061
REMARK 3 6 2.1420 - 2.0157 0.96 2635 147 0.1624 0.2091
REMARK 3 7 2.0157 - 1.9148 0.95 2640 124 0.1761 0.2107
REMARK 3 8 1.9148 - 1.8314 0.94 2581 111 0.1916 0.2353
REMARK 3 9 1.8314 - 1.7609 0.93 2548 137 0.2060 0.2332
REMARK 3 10 1.7609 - 1.7002 0.92 2512 141 0.2208 0.2579
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.010
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 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 : 0.006 2288
REMARK 3 ANGLE : 1.086 3093
REMARK 3 CHIRALITY : 0.075 341
REMARK 3 PLANARITY : 0.005 397
REMARK 3 DIHEDRAL : 14.583 869
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 5AUU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JUN-15.
REMARK 100 THE DEPOSITION ID IS D_1300000027.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28155
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 44.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.3000
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: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M AMMONIUM SULFATE, 0.1 M MES, PH
REMARK 280 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 23.50300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.23950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.14350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.23950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.50300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.14350
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 MET A 1
REMARK 465 LYS A 108
REMARK 465 GLU A 109
REMARK 465 LYS A 278
REMARK 465 ASP A 279
REMARK 465 THR A 280
REMARK 465 GLN A 281
REMARK 465 GLN A 282
REMARK 465 ALA A 283
REMARK 465 LEU A 284
REMARK 465 SER A 285
REMARK 465 LEU A 286
REMARK 465 GLU A 287
REMARK 465 HIS A 288
REMARK 465 HIS A 289
REMARK 465 HIS A 290
REMARK 465 HIS A 291
REMARK 465 HIS A 292
REMARK 465 HIS A 293
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 PHE A 138 -0.12 71.74
REMARK 500 ASP A 139 36.98 -140.57
REMARK 500 ASN A 151 43.24 -102.66
REMARK 500 ASP A 161 72.58 61.00
REMARK 500 ILE A 168 76.59 -114.40
REMARK 500 PHE A 178 114.64 -162.92
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 LU2 A 400
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5AUT RELATED DB: PDB
REMARK 900 RELATED ID: 5AUV RELATED DB: PDB
REMARK 900 RELATED ID: 5AUW RELATED DB: PDB
REMARK 900 RELATED ID: 5AUX RELATED DB: PDB
REMARK 900 RELATED ID: 5AUY RELATED DB: PDB
REMARK 900 RELATED ID: 5AUZ RELATED DB: PDB
REMARK 900 RELATED ID: 5AV0 RELATED DB: PDB
REMARK 900 RELATED ID: 5AV1 RELATED DB: PDB
REMARK 900 RELATED ID: 5AV2 RELATED DB: PDB
REMARK 900 RELATED ID: 5AV3 RELATED DB: PDB
REMARK 900 RELATED ID: 5AV4 RELATED DB: PDB
DBREF 5AUU A 1 285 UNP P53355 DAPK1_HUMAN 1 285
SEQADV 5AUU LEU A 286 UNP P53355 EXPRESSION TAG
SEQADV 5AUU GLU A 287 UNP P53355 EXPRESSION TAG
SEQADV 5AUU HIS A 288 UNP P53355 EXPRESSION TAG
SEQADV 5AUU HIS A 289 UNP P53355 EXPRESSION TAG
SEQADV 5AUU HIS A 290 UNP P53355 EXPRESSION TAG
SEQADV 5AUU HIS A 291 UNP P53355 EXPRESSION TAG
SEQADV 5AUU HIS A 292 UNP P53355 EXPRESSION TAG
SEQADV 5AUU HIS A 293 UNP P53355 EXPRESSION TAG
SEQRES 1 A 293 MET THR VAL PHE ARG GLN GLU ASN VAL ASP ASP TYR TYR
SEQRES 2 A 293 ASP THR GLY GLU GLU LEU GLY SER GLY GLN PHE ALA VAL
SEQRES 3 A 293 VAL LYS LYS CYS ARG GLU LYS SER THR GLY LEU GLN TYR
SEQRES 4 A 293 ALA ALA LYS PHE ILE LYS LYS ARG ARG THR LYS SER SER
SEQRES 5 A 293 ARG ARG GLY VAL SER ARG GLU ASP ILE GLU ARG GLU VAL
SEQRES 6 A 293 SER ILE LEU LYS GLU ILE GLN HIS PRO ASN VAL ILE THR
SEQRES 7 A 293 LEU HIS GLU VAL TYR GLU ASN LYS THR ASP VAL ILE LEU
SEQRES 8 A 293 ILE LEU GLU LEU VAL ALA GLY GLY GLU LEU PHE ASP PHE
SEQRES 9 A 293 LEU ALA GLU LYS GLU SER LEU THR GLU GLU GLU ALA THR
SEQRES 10 A 293 GLU PHE LEU LYS GLN ILE LEU ASN GLY VAL TYR TYR LEU
SEQRES 11 A 293 HIS SER LEU GLN ILE ALA HIS PHE ASP LEU LYS PRO GLU
SEQRES 12 A 293 ASN ILE MET LEU LEU ASP ARG ASN VAL PRO LYS PRO ARG
SEQRES 13 A 293 ILE LYS ILE ILE ASP PHE GLY LEU ALA HIS LYS ILE ASP
SEQRES 14 A 293 PHE GLY ASN GLU PHE LYS ASN ILE PHE GLY THR PRO GLU
SEQRES 15 A 293 PHE VAL ALA PRO GLU ILE VAL ASN TYR GLU PRO LEU GLY
SEQRES 16 A 293 LEU GLU ALA ASP MET TRP SER ILE GLY VAL ILE THR TYR
SEQRES 17 A 293 ILE LEU LEU SER GLY ALA SER PRO PHE LEU GLY ASP THR
SEQRES 18 A 293 LYS GLN GLU THR LEU ALA ASN VAL SER ALA VAL ASN TYR
SEQRES 19 A 293 GLU PHE GLU ASP GLU TYR PHE SER ASN THR SER ALA LEU
SEQRES 20 A 293 ALA LYS ASP PHE ILE ARG ARG LEU LEU VAL LYS ASP PRO
SEQRES 21 A 293 LYS LYS ARG MET THR ILE GLN ASP SER LEU GLN HIS PRO
SEQRES 22 A 293 TRP ILE LYS PRO LYS ASP THR GLN GLN ALA LEU SER LEU
SEQRES 23 A 293 GLU HIS HIS HIS HIS HIS HIS
HET LU2 A 400 21
HETNAM LU2 2-(3,4-DIHYDROXYPHENYL)-5,7-DIHYDROXY-4H-CHROMEN-4-ONE
HETSYN LU2 LUTEOLIN
FORMUL 2 LU2 C15 H10 O6
FORMUL 3 HOH *180(H2 O)
HELIX 1 AA1 ASN A 8 ASP A 11 5 4
HELIX 2 AA2 SER A 57 ILE A 71 1 15
HELIX 3 AA3 GLU A 100 GLU A 107 1 8
HELIX 4 AA4 THR A 112 LEU A 133 1 22
HELIX 5 AA5 LYS A 141 GLU A 143 5 3
HELIX 6 AA6 ALA A 185 ASN A 190 1 6
HELIX 7 AA7 LEU A 196 GLY A 213 1 18
HELIX 8 AA8 THR A 221 ALA A 231 1 11
HELIX 9 AA9 GLU A 237 SER A 242 1 6
HELIX 10 AB1 SER A 245 ARG A 254 1 10
HELIX 11 AB2 ASP A 259 ARG A 263 5 5
HELIX 12 AB3 THR A 265 HIS A 272 1 8
SHEET 1 AA1 5 TYR A 13 GLY A 22 0
SHEET 2 AA1 5 ALA A 25 GLU A 32 -1 O LYS A 29 N GLU A 17
SHEET 3 AA1 5 GLN A 38 LYS A 45 -1 O ALA A 41 N LYS A 28
SHEET 4 AA1 5 ASP A 88 GLU A 94 -1 O LEU A 93 N ALA A 40
SHEET 5 AA1 5 LEU A 79 GLU A 84 -1 N TYR A 83 O ILE A 90
SHEET 1 AA2 2 ILE A 135 ALA A 136 0
SHEET 2 AA2 2 HIS A 166 LYS A 167 -1 O HIS A 166 N ALA A 136
SHEET 1 AA3 2 ILE A 145 LEU A 147 0
SHEET 2 AA3 2 ILE A 157 ILE A 159 -1 O LYS A 158 N MET A 146
SITE 1 AC1 13 LEU A 19 ALA A 40 LYS A 42 GLU A 64
SITE 2 AC1 13 LEU A 68 ILE A 77 LEU A 93 GLU A 94
SITE 3 AC1 13 LEU A 95 VAL A 96 ILE A 160 ASP A 161
SITE 4 AC1 13 PHE A 162
CRYST1 47.006 62.287 88.479 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 0.021274 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016055 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011302 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
