HEADER HORMONE RECEPTOR 13-APR-07 2PIO
TITLE ANDROGEN RECEPTOR LBD WITH SMALL MOLECULE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANDROGEN RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LIGAND-BINDING DOMAIN (RESIDUES 669-919);
COMPND 5 SYNONYM: DIHYDROTESTOSTERONE RECEPTOR;
COMPND 6 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: AR, DHTR, NR3C4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ANDROGEN RECEPTOR LIGAND BINDING DOMAIN, INHIBITORS COACTIVATOR
KEYWDS 2 BINDING AF-2 POCKET, HORMONE RECEPTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR E.ESTEBANEZ-PERPINA,A.A.ARNOLD,J.D.BAXTER,P.WEBB,R.K.GUY,
AUTHOR 2 K.R.FLETTERICK
REVDAT 6 21-FEB-24 2PIO 1 REMARK
REVDAT 5 18-OCT-17 2PIO 1 REMARK
REVDAT 4 07-APR-09 2PIO 1 REMARK
REVDAT 3 24-FEB-09 2PIO 1 VERSN
REVDAT 2 27-MAY-08 2PIO 1 JRNL
REVDAT 1 25-SEP-07 2PIO 0
JRNL AUTH E.ESTEBANEZ-PERPINA,L.A.ARNOLD,A.A.ARNOLD,P.NGUYEN,
JRNL AUTH 2 E.D.RODRIGUES,E.MAR,R.BATEMAN,P.PALLAI,K.M.SHOKAT,
JRNL AUTH 3 J.D.BAXTER,R.K.GUY,P.WEBB,R.J.FLETTERICK
JRNL TITL A SURFACE ON THE ANDROGEN RECEPTOR THAT ALLOSTERICALLY
JRNL TITL 2 REGULATES COACTIVATOR BINDING.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 104 16074 2007
JRNL REFN ISSN 0027-8424
JRNL PMID 17911242
JRNL DOI 10.1073/PNAS.0708036104
REMARK 2
REMARK 2 RESOLUTION. 2.03 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.03
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
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 : 18075
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) : 0.246
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
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 : 2028
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 138
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 2PIO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-07.
REMARK 100 THE DEPOSITION ID IS D_1000042415.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : ELVES
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17047
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.030
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
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) : 0.06300
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) : 2.03
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) : 0.06300
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: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
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 27.30800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.27350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.00750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 35.27350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.30800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.00750
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 CYS A 669
REMARK 465 GLN A 670
REMARK 465 GLN A 919
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 OE1 GLN A 802 O HOH A 1014 2.16
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 LYS A 845 16.34 54.22
REMARK 500 LYS A 847 -52.74 -143.01
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 SO4 A 932
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DHT A 931
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2MI A 933
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2MI A 934
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PIN RELATED DB: PDB
REMARK 900 RELATED ID: 2PIP RELATED DB: PDB
REMARK 900 RELATED ID: 2PIQ RELATED DB: PDB
REMARK 900 RELATED ID: 2PIR RELATED DB: PDB
REMARK 900 RELATED ID: 2PIT RELATED DB: PDB
REMARK 900 RELATED ID: 2PIU RELATED DB: PDB
REMARK 900 RELATED ID: 2PIV RELATED DB: PDB
REMARK 900 RELATED ID: 2PIW RELATED DB: PDB
REMARK 900 RELATED ID: 2PIX RELATED DB: PDB
REMARK 900 RELATED ID: 2PKL RELATED DB: PDB
DBREF 2PIO A 669 919 UNP P10275 ANDR_HUMAN 669 919
SEQRES 1 A 251 CYS GLN PRO ILE PHE LEU ASN VAL LEU GLU ALA ILE GLU
SEQRES 2 A 251 PRO GLY VAL VAL CYS ALA GLY HIS ASP ASN ASN GLN PRO
SEQRES 3 A 251 ASP SER PHE ALA ALA LEU LEU SER SER LEU ASN GLU LEU
SEQRES 4 A 251 GLY GLU ARG GLN LEU VAL HIS VAL VAL LYS TRP ALA LYS
SEQRES 5 A 251 ALA LEU PRO GLY PHE ARG ASN LEU HIS VAL ASP ASP GLN
SEQRES 6 A 251 MET ALA VAL ILE GLN TYR SER TRP MET GLY LEU MET VAL
SEQRES 7 A 251 PHE ALA MET GLY TRP ARG SER PHE THR ASN VAL ASN SER
SEQRES 8 A 251 ARG MET LEU TYR PHE ALA PRO ASP LEU VAL PHE ASN GLU
SEQRES 9 A 251 TYR ARG MET HIS LYS SER ARG MET TYR SER GLN CYS VAL
SEQRES 10 A 251 ARG MET ARG HIS LEU SER GLN GLU PHE GLY TRP LEU GLN
SEQRES 11 A 251 ILE THR PRO GLN GLU PHE LEU CYS MET LYS ALA LEU LEU
SEQRES 12 A 251 LEU PHE SER ILE ILE PRO VAL ASP GLY LEU LYS ASN GLN
SEQRES 13 A 251 LYS PHE PHE ASP GLU LEU ARG MET ASN TYR ILE LYS GLU
SEQRES 14 A 251 LEU ASP ARG ILE ILE ALA CYS LYS ARG LYS ASN PRO THR
SEQRES 15 A 251 SER CYS SER ARG ARG PHE TYR GLN LEU THR LYS LEU LEU
SEQRES 16 A 251 ASP SER VAL GLN PRO ILE ALA ARG GLU LEU HIS GLN PHE
SEQRES 17 A 251 THR PHE ASP LEU LEU ILE LYS SER HIS MET VAL SER VAL
SEQRES 18 A 251 ASP PHE PRO GLU MET MET ALA GLU ILE ILE SER VAL GLN
SEQRES 19 A 251 VAL PRO LYS ILE LEU SER GLY LYS VAL LYS PRO ILE TYR
SEQRES 20 A 251 PHE HIS THR GLN
HET SO4 A 932 5
HET DHT A 931 21
HET 2MI A 933 10
HET 2MI A 934 10
HETNAM SO4 SULFATE ION
HETNAM DHT 5-ALPHA-DIHYDROTESTOSTERONE
HETNAM 2MI 2-METHYL-1H-INDOLE
FORMUL 2 SO4 O4 S 2-
FORMUL 3 DHT C19 H30 O2
FORMUL 4 2MI 2(C9 H9 N)
FORMUL 6 HOH *138(H2 O)
HELIX 1 1 PRO A 671 GLU A 681 1 11
HELIX 2 2 SER A 696 ALA A 721 1 26
HELIX 3 3 GLY A 724 LEU A 728 5 5
HELIX 4 4 HIS A 729 ASN A 758 1 30
HELIX 5 5 ASN A 771 SER A 778 1 8
HELIX 6 6 MET A 780 LEU A 797 1 18
HELIX 7 7 THR A 800 PHE A 813 1 14
HELIX 8 8 ASN A 823 CYS A 844 1 22
HELIX 9 9 ASN A 848 SER A 888 1 41
HELIX 10 10 PRO A 892 GLN A 902 1 11
HELIX 11 11 GLN A 902 SER A 908 1 7
SHEET 1 A 2 LEU A 762 ALA A 765 0
SHEET 2 A 2 LEU A 768 PHE A 770 -1 O PHE A 770 N LEU A 762
SHEET 1 B 2 ILE A 815 PRO A 817 0
SHEET 2 B 2 VAL A 911 PRO A 913 -1 O LYS A 912 N ILE A 816
SITE 1 AC1 6 SER A 696 PHE A 697 LYS A 777 ARG A 779
SITE 2 AC1 6 SER A 853 HOH A1005
SITE 1 AC2 7 LEU A 704 ASN A 705 MET A 749 ARG A 752
SITE 2 AC2 7 PHE A 764 THR A 877 PHE A 891
SITE 1 AC3 3 MET A 734 GLN A 738 ILE A 898
SITE 1 AC4 5 PHE A 673 ASN A 833 GLU A 837 HIS A 885
SITE 2 AC4 5 HOH A1072
CRYST1 54.616 66.015 70.547 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 0.018310 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015148 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014175 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
