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HEADER HYDROLASE 08-JAN-07 2OGT
TITLE CRYSTAL STRUCTURE OF THE GEOBACILLUS STEAROTHERMOPHILUS
TITLE 2 CARBOXYLESTERASE EST55 AT PH 6.8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOSTABLE CARBOXYLESTERASE EST50;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS STEAROTHERMOPHILUS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: TOP 10
KEYWDS CARBOXYLESTERASE, ALPHA/BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.LIU,H.E.EWIS,P.C.TAI,C.D.LU,I.T.WEBER
REVDAT 1 13-FEB-07 2OGT 0
JRNL AUTH P.LIU,H.E.EWIS,P.C.TAI,C.D.LU,I.T.WEBER
JRNL TITL CRYSTAL STRUCTURE OF THE GEOBACILLUS
JRNL TITL 2 STEAROTHERMOPHILUS CARBOXYLESTERASE EST55 AND ITS
JRNL TITL 3 ACTIVATION OF PRODRUG CPT-11.
JRNL REF J.MOL.BIOL. 2006
JRNL REFN ASTM JMOBAK UK ESSN 1089-8638
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.58 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.58
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.176
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.173
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 3427
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 68569
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.163
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.160
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 2884
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 57163
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3715
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 159
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 3771.34
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 22
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 34904
REMARK 3 NUMBER OF RESTRAINTS : 45343
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 ANGLE DISTANCES (A) : 0.026
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.024
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.041
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.049
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.045
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.005
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.064
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.082
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2OGT COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-2007.
REMARK 100 THE RCSB ID CODE IS RCSB041117.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-2003
REMARK 200 TEMPERATURE (KELVIN) : 95.0
REMARK 200 PH : 6.80
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MARCCD
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68569
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.580
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.37800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4, CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1QE3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350,POTASSIUM IODINE, PH 6.8,
REMARK 280 VAPOR DIFFUSION, HANGING DROP
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 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-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 34.68050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.30300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.21500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.30300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.68050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.21500
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 GLU A 2
REMARK 465 ASP A 66
REMARK 465 PRO A 67
REMARK 465 ILE A 68
REMARK 465 PHE A 69
REMARK 465 SER A 70
REMARK 465 GLY A 71
REMARK 465 LEU A 72
REMARK 465 LEU A 73
REMARK 465 GLY A 74
REMARK 465 ARG A 75
REMARK 465 MET A 76
REMARK 465 SER A 77
REMARK 465 GLU A 78
REMARK 465 ALA A 79
REMARK 465 LYS A 349
REMARK 465 GLU A 350
REMARK 465 THR A 351
REMARK 465 ALA A 352
REMARK 465 GLU A 353
REMARK 465 PRO A 354
REMARK 465 SER A 355
REMARK 465 ALA A 356
REMARK 465 PRO A 357
REMARK 465 THR A 358
REMARK 465 PHE A 401
REMARK 465 GLY A 402
REMARK 465 GLY A 403
REMARK 465 GLN A 404
REMARK 465 LEU A 405
REMARK 465 LYS A 406
REMARK 465 ALA A 407
REMARK 465 GLY A 497
REMARK 465 ARG A 498
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 LYS A 327 CG CD CE NZ
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 1138 DISTANCE = 5.39 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2OGS RELATED DB: PDB
DBREF 2OGT A 1 498 UNP Q8GCC7 Q8GCC7_BACST 1 498
SEQRES 1 A 498 MET GLU ARG THR VAL VAL GLU THR ARG TYR GLY ARG LEU
SEQRES 2 A 498 ARG GLY GLU MET ASN GLU GLY VAL PHE VAL TRP LYS GLY
SEQRES 3 A 498 ILE PRO TYR ALA LYS ALA PRO VAL GLY GLU ARG ARG PHE
SEQRES 4 A 498 LEU PRO PRO GLU PRO PRO ASP ALA TRP ASP GLY VAL ARG
SEQRES 5 A 498 GLU ALA THR SER PHE GLY PRO VAL VAL MET GLN PRO SER
SEQRES 6 A 498 ASP PRO ILE PHE SER GLY LEU LEU GLY ARG MET SER GLU
SEQRES 7 A 498 ALA PRO SER GLU ASP GLY LEU TYR LEU ASN ILE TRP SER
SEQRES 8 A 498 PRO ALA ALA ASP GLY LYS LYS ARG PRO VAL LEU PHE TRP
SEQRES 9 A 498 ILE HIS GLY GLY ALA PHE LEU PHE GLY SER GLY SER SER
SEQRES 10 A 498 PRO TRP TYR ASP GLY THR ALA PHE ALA LYS HIS GLY ASP
SEQRES 11 A 498 VAL VAL VAL VAL THR ILE ASN TYR ARG MET ASN VAL PHE
SEQRES 12 A 498 GLY PHE LEU HIS LEU GLY ASP SER PHE GLY GLU ALA TYR
SEQRES 13 A 498 ALA GLN ALA GLY ASN LEU GLY ILE LEU ASP GLN VAL ALA
SEQRES 14 A 498 ALA LEU ARG TRP VAL LYS GLU ASN ILE ALA ALA PHE GLY
SEQRES 15 A 498 GLY ASP PRO ASP ASN ILE THR ILE PHE GLY GLU SER ALA
SEQRES 16 A 498 GLY ALA ALA SER VAL GLY VAL LEU LEU SER LEU PRO GLU
SEQRES 17 A 498 ALA SER GLY LEU PHE ARG ARG ALA MET LEU GLN SER GLY
SEQRES 18 A 498 SER GLY SER LEU LEU LEU ARG SER PRO GLU THR ALA MET
SEQRES 19 A 498 ALA MET THR GLU ARG ILE LEU ASP LYS ALA GLY ILE ARG
SEQRES 20 A 498 PRO GLY ASP ARG GLU ARG LEU LEU SER ILE PRO ALA GLU
SEQRES 21 A 498 GLU LEU LEU ARG ALA ALA LEU SER LEU GLY PRO GLY VAL
SEQRES 22 A 498 MET TYR GLY PRO VAL VAL ASP GLY ARG VAL LEU ARG ARG
SEQRES 23 A 498 HIS PRO ILE GLU ALA LEU ARG TYR GLY ALA ALA SER GLY
SEQRES 24 A 498 ILE PRO ILE LEU ILE GLY VAL THR LYS ASP GLU TYR ASN
SEQRES 25 A 498 LEU PHE THR LEU THR ASP PRO SER TRP THR LYS LEU GLY
SEQRES 26 A 498 GLU LYS GLU LEU LEU ASP ARG ILE ASN ARG GLU VAL GLY
SEQRES 27 A 498 PRO VAL PRO GLU GLU ALA ILE ARG TYR TYR LYS GLU THR
SEQRES 28 A 498 ALA GLU PRO SER ALA PRO THR TRP GLN THR TRP LEU ARG
SEQRES 29 A 498 ILE MET THR TYR ARG VAL PHE VAL GLU GLY MET LEU ARG
SEQRES 30 A 498 THR ALA ASP ALA GLN ALA ALA GLN GLY ALA ASP VAL TYR
SEQRES 31 A 498 MET TYR ARG PHE ASP TYR GLU THR PRO VAL PHE GLY GLY
SEQRES 32 A 498 GLN LEU LYS ALA CYS HIS ALA LEU GLU LEU PRO PHE VAL
SEQRES 33 A 498 PHE HIS ASN LEU HIS GLN PRO GLY VAL ALA ASN PHE VAL
SEQRES 34 A 498 GLY ASN ARG PRO GLU ARG GLU ALA ILE ALA ASN GLU MET
SEQRES 35 A 498 HIS TYR ALA TRP LEU SER PHE ALA ARG THR GLY ASP PRO
SEQRES 36 A 498 ASN GLY ALA HIS LEU PRO GLU ALA TRP PRO ALA TYR THR
SEQRES 37 A 498 ASN GLU ARG LYS ALA ALA PHE VAL PHE SER ALA ALA SER
SEQRES 38 A 498 HIS VAL GLU ASP ASP PRO PHE GLY ARG GLU ARG ALA ALA
SEQRES 39 A 498 TRP GLN GLY ARG
HET IOD 601 1
HET GOL 501 6
HET GOL 502 6
HETNAM IOD IODIDE ION
HETNAM GOL GLYCEROL
FORMUL 2 IOD I1 1-
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 5 HOH *147(H2 O1)
HELIX 1 1 VAL A 34 ARG A 38 5 5
HELIX 2 2 SER A 117 ASP A 121 5 5
HELIX 3 3 GLY A 122 ASP A 130 1 9
HELIX 4 4 MET A 140 PHE A 145 1 6
HELIX 5 5 GLY A 153 ALA A 157 5 5
HELIX 6 6 GLN A 158 GLY A 160 5 3
HELIX 7 7 ASN A 161 ILE A 178 1 18
HELIX 8 8 ALA A 179 PHE A 181 5 3
HELIX 9 9 SER A 194 LEU A 206 1 13
HELIX 10 10 PRO A 207 SER A 210 5 4
HELIX 11 11 SER A 229 GLY A 245 1 17
HELIX 12 12 ASP A 250 ILE A 257 1 8
HELIX 13 13 PRO A 258 SER A 268 1 11
HELIX 14 14 HIS A 287 TYR A 294 1 8
HELIX 15 15 ASP A 309 PHE A 314 1 6
HELIX 16 16 PRO A 319 LEU A 324 1 6
HELIX 17 17 GLY A 325 GLY A 338 1 14
HELIX 18 18 PRO A 341 TYR A 348 1 8
HELIX 19 19 TRP A 362 PHE A 371 1 10
HELIX 20 20 PHE A 371 GLN A 385 1 15
HELIX 21 21 GLU A 412 HIS A 418 1 7
HELIX 22 22 ASN A 431 GLY A 453 1 23
HELIX 23 23 PHE A 488 GLN A 496 1 9
SHEET 1 A 3 VAL A 5 THR A 8 0
SHEET 2 A 3 GLY A 11 ARG A 14 -1 O LEU A 13 N VAL A 6
SHEET 3 A 3 VAL A 51 GLU A 53 1 O ARG A 52 N ARG A 12
SHEET 1 B11 GLU A 16 ASN A 18 0
SHEET 2 B11 VAL A 21 PRO A 28 -1 O VAL A 21 N ASN A 18
SHEET 3 B11 TYR A 86 SER A 91 -1 O LEU A 87 N ILE A 27
SHEET 4 B11 VAL A 132 ILE A 136 -1 O VAL A 133 N TRP A 90
SHEET 5 B11 ARG A 99 ILE A 105 1 N TRP A 104 O VAL A 134
SHEET 6 B11 GLY A 183 GLU A 193 1 O THR A 189 N VAL A 101
SHEET 7 B11 ARG A 215 GLN A 219 1 O GLN A 219 N GLY A 192
SHEET 8 B11 ILE A 302 THR A 307 1 O LEU A 303 N LEU A 218
SHEET 9 B11 VAL A 389 PHE A 394 1 O PHE A 394 N VAL A 306
SHEET 10 B11 ALA A 473 PHE A 477 1 O PHE A 475 N MET A 391
SHEET 11 B11 HIS A 482 ASP A 485 -1 O HIS A 482 N VAL A 476
CISPEP 1 GLY A 338 PRO A 339 0 -1.54
CRYST1 69.361 74.430 98.606 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 0.014417 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013435 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010141 0.00000
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