HEADER NUCLEOTIDYLTRANSFERASE 11-AUG-87 1DPI
TITLE STRUCTURE OF LARGE FRAGMENT OF ESCHERICHIA COLI DNA POLYMERASE I
TITLE 2 COMPLEXED WITH D/TMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA POLYMERASE I KLENOW FRAGMENT;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.7.7.7;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: T7;
SOURCE 5 EXPRESSION_SYSTEM_VECTOR_TYPE: T7;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: T7;
SOURCE 7 EXPRESSION_SYSTEM_GENE: T7
KEYWDS NUCLEOTIDYLTRANSFERASE
EXPDTA X-RAY DIFFRACTION
MDLTYP CA ATOMS ONLY, CHAIN A
AUTHOR L.BEESE,D.OLLIS,T.STEITZ
REVDAT 4 07-FEB-24 1DPI 1 REMARK
REVDAT 3 24-FEB-09 1DPI 1 VERSN
REVDAT 2 01-APR-03 1DPI 1 JRNL
REVDAT 1 16-OCT-87 1DPI 0
JRNL AUTH D.L.OLLIS,P.BRICK,R.HAMLIN,N.G.XUONG,T.A.STEITZ
JRNL TITL STRUCTURE OF LARGE FRAGMENT OF ESCHERICHIA COLI DNA
JRNL TITL 2 POLYMERASE I COMPLEXED WITH DTMP.
JRNL REF NATURE V. 313 762 1985
JRNL REFN ISSN 0028-0836
JRNL PMID 3883192
JRNL DOI 10.1038/313762A0
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.L.OLLIS,C.KLINE,T.A.STEITZ
REMARK 1 TITL DOMAIN OF E. COLI DNA POLYMERASE I SHOWING SEQUENCE HOMOLOGY
REMARK 1 TITL 2 TO T7 DNA POLYMERASE
REMARK 1 REF NATURE V. 313 818 1985
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.BRICK,D.OLLIS,T.A.STEITZ
REMARK 1 TITL CRYSTALLIZATION AND 7 ANGSTROMS RESOLUTION ELECTRON DENSITY
REMARK 1 TITL 2 MAP OF THE LARGE FRAGMENT OF ESCHERICHIA COLI DNA POLYMERASE
REMARK 1 TITL 3 I
REMARK 1 REF J.MOL.BIOL. V. 166 453 1983
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 3
REMARK 1 AUTH C.M.JOYCE,W.S.KELLEY,N.D.F.GRINDLEY
REMARK 1 TITL NUCLEOTIDE SEQUENCE OF THE ESCHERICHIA COLI POLA GENE AND
REMARK 1 TITL 2 PRIMARY STRUCTURE OF DNA POLYMERASE I
REMARK 1 REF J.BIOL.CHEM. V. 257 1958 1982
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 4
REMARK 1 AUTH W.E.BROWN,K.H.STUMP,W.S.KELLEY
REMARK 1 TITL ESCHERICHIA COLI DNA POLYMERASE I. SEQUENCE CHARACTERIZATION
REMARK 1 TITL 2 AND SECONDARY STRUCTURE PREDICTION
REMARK 1 REF J.BIOL.CHEM. V. 257 1965 1982
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
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 + TEST SET) : 0.200
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 546
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 0
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 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DPI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172888.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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: NULL
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 (%): 63.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
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 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
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 42.90000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 64.35000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 21.45000
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 VAL A 324
REMARK 465 ILE A 325
REMARK 465 ALA A 574
REMARK 465 GLY A 575
REMARK 465 GLU A 576
REMARK 465 GLU A 577
REMARK 465 PHE A 578
REMARK 465 ASN A 579
REMARK 465 LEU A 580
REMARK 465 SER A 581
REMARK 465 SER A 582
REMARK 465 THR A 583
REMARK 465 LYS A 584
REMARK 465 GLN A 585
REMARK 465 LEU A 586
REMARK 465 GLN A 587
REMARK 465 THR A 588
REMARK 465 ILE A 589
REMARK 465 LEU A 590
REMARK 465 PHE A 591
REMARK 465 GLU A 592
REMARK 465 LYS A 593
REMARK 465 GLN A 594
REMARK 465 GLY A 595
REMARK 465 ILE A 596
REMARK 465 LYS A 597
REMARK 465 PRO A 598
REMARK 465 LEU A 599
REMARK 465 LYS A 600
REMARK 465 LYS A 601
REMARK 465 THR A 602
REMARK 465 PRO A 603
REMARK 465 GLY A 604
REMARK 465 GLY A 605
REMARK 465 ALA A 606
REMARK 465 PRO A 607
REMARK 465 SER A 608
REMARK 465 THR A 609
REMARK 465 SER A 610
REMARK 465 GLU A 611
REMARK 465 GLU A 612
REMARK 465 VAL A 613
REMARK 465 LEU A 614
REMARK 465 GLU A 615
REMARK 465 GLU A 616
REMARK 465 LEU A 617
REMARK 465 ALA A 618
REMARK 465 LEU A 619
REMARK 465 ASP A 620
REMARK 465 TYR A 621
REMARK 465 PRO A 622
REMARK 465 PRO A 780
REMARK 465 ARG A 781
REMARK 465 LYS A 782
REMARK 465 GLU A 783
REMARK 465 ALA A 784
REMARK 465 GLN A 785
REMARK 465 LYS A 786
REMARK 465 TYR A 787
DBREF 1DPI A 324 928 UNP P00582 DPO1_ECOLI 324 928
SEQRES 1 A 605 VAL ILE SER TYR ASP ASN TYR VAL THR ILE LEU ASP GLU
SEQRES 2 A 605 GLU THR LEU LYS ALA TRP ILE ALA LYS LEU GLU LYS ALA
SEQRES 3 A 605 PRO VAL PHE ALA PHE ASP THR GLU THR ASP SER LEU ASP
SEQRES 4 A 605 ASN ILE SER ALA ASN LEU VAL GLY LEU SER PHE ALA ILE
SEQRES 5 A 605 GLU PRO GLY VAL ALA ALA TYR ILE PRO VAL ALA HIS ASP
SEQRES 6 A 605 TYR LEU ASP ALA PRO ASP GLN ILE SER ARG GLU ARG ALA
SEQRES 7 A 605 LEU GLU LEU LEU LYS PRO LEU LEU GLU ASP GLU LYS ALA
SEQRES 8 A 605 LEU LYS VAL GLY GLN ASN LEU LYS TYR ASP ARG GLY ILE
SEQRES 9 A 605 LEU ALA ASN TYR GLY ILE GLU LEU ARG GLY ILE ALA PHE
SEQRES 10 A 605 ASP THR MET LEU GLU SER TYR ILE LEU ASN SER VAL ALA
SEQRES 11 A 605 GLY ARG HIS ASP MET ASP SER LEU ALA GLU ARG TRP LEU
SEQRES 12 A 605 LYS HIS LYS THR ILE THR PHE GLU GLU ILE ALA GLY LYS
SEQRES 13 A 605 GLY LYS ASN GLN LEU THR PHE ASN GLN ILE ALA LEU GLU
SEQRES 14 A 605 GLU ALA GLY ARG TYR ALA ALA GLU ASP ALA ASP VAL THR
SEQRES 15 A 605 LEU GLN LEU HIS LEU LYS MET TRP PRO ASP LEU GLN LYS
SEQRES 16 A 605 HIS LYS GLY PRO LEU ASN VAL PHE GLU ASN ILE GLU MET
SEQRES 17 A 605 PRO LEU VAL PRO VAL LEU SER ARG ILE GLU ARG ASN GLY
SEQRES 18 A 605 VAL LYS ILE ASP PRO LYS VAL LEU HIS ASN HIS SER GLU
SEQRES 19 A 605 GLU LEU THR LEU ARG LEU ALA GLU LEU GLU LYS LYS ALA
SEQRES 20 A 605 HIS GLU ILE ALA GLY GLU GLU PHE ASN LEU SER SER THR
SEQRES 21 A 605 LYS GLN LEU GLN THR ILE LEU PHE GLU LYS GLN GLY ILE
SEQRES 22 A 605 LYS PRO LEU LYS LYS THR PRO GLY GLY ALA PRO SER THR
SEQRES 23 A 605 SER GLU GLU VAL LEU GLU GLU LEU ALA LEU ASP TYR PRO
SEQRES 24 A 605 LEU PRO LYS VAL ILE LEU GLU TYR ARG GLY LEU ALA LYS
SEQRES 25 A 605 LEU LYS SER THR TYR THR ASP LYS LEU PRO LEU MET ILE
SEQRES 26 A 605 ASN PRO LYS THR GLY ARG VAL HIS THR SER TYR HIS GLN
SEQRES 27 A 605 ALA VAL THR ALA THR GLY ARG LEU SER SER THR ASP PRO
SEQRES 28 A 605 ASN LEU GLN ASN ILE PRO VAL ARG ASN GLU GLU GLY ARG
SEQRES 29 A 605 ARG ILE ARG GLN ALA PHE ILE ALA PRO GLU ASP TYR VAL
SEQRES 30 A 605 ILE VAL SER ALA ASP TYR SER GLN ILE GLU LEU ARG ILE
SEQRES 31 A 605 MET ALA HIS LEU SER ARG ASP LYS GLY LEU LEU THR ALA
SEQRES 32 A 605 PHE ALA GLU GLY LYS ASP ILE HIS ARG ALA THR ALA ALA
SEQRES 33 A 605 GLU VAL PHE GLY LEU PRO LEU GLU THR VAL THR SER GLU
SEQRES 34 A 605 GLN ARG ARG SER ALA LYS ALA ILE ASN PHE GLY LEU ILE
SEQRES 35 A 605 TYR GLY MET SER ALA PHE GLY LEU ALA ARG GLN LEU ASN
SEQRES 36 A 605 ILE PRO ARG LYS GLU ALA GLN LYS TYR MET ASP LEU TYR
SEQRES 37 A 605 PHE GLU ARG TYR PRO GLY VAL LEU GLU TYR MET GLU ARG
SEQRES 38 A 605 THR ARG ALA GLN ALA LYS GLU GLN GLY TYR VAL GLU THR
SEQRES 39 A 605 LEU ASP GLY ARG ARG LEU TYR LEU PRO ASP ILE LYS SER
SEQRES 40 A 605 SER ASN GLY ALA ARG ARG ALA ALA ALA GLU ARG ALA ALA
SEQRES 41 A 605 ILE ASN ALA PRO MET GLN GLY THR ALA ALA ASP ILE ILE
SEQRES 42 A 605 LYS ARG ALA MET ILE ALA VAL ASP ALA TRP LEU GLN ALA
SEQRES 43 A 605 GLU GLN PRO ARG VAL ARG MET ILE MET GLN VAL HIS ASP
SEQRES 44 A 605 GLU LEU VAL PHE GLU VAL HIS LYS ASP ASP VAL ASP ALA
SEQRES 45 A 605 VAL ALA LYS GLN ILE HIS GLN LEU MET GLU ASN CYS THR
SEQRES 46 A 605 ARG LEU ASP VAL PRO LEU LEU VAL GLU VAL GLY SER GLY
SEQRES 47 A 605 GLU ASN TRP ASP GLN ALA HIS
HET ZN A 1 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
CRYST1 102.900 102.900 85.800 90.00 90.00 90.00 P 43 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 0.009718 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009718 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011655 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
