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HEADER HYDROLASE 14-JUN-12 4FLE
TITLE CRYSTAL STRUCTURE OF THE ESTERASE YQIA (YE3661) FROM YERSINIA
TITLE 2 ENTEROCOLITICA, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET YER85
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: YERSINIA ENTEROCOLITICA SUBSP. ENTEROCOLITICA;
SOURCE 3 ORGANISM_TAXID: 393305;
SOURCE 4 STRAIN: 8081;
SOURCE 5 GENE: YE3661;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, NORTHEAST STRUCTURAL GENOMICS
KEYWDS 2 CONSORTIUM, NESG, ALPHA-BETA PROTEIN, ROSSMANN FOLD, DISPLAYS
KEYWDS 3 ESTERASE ACTIVITY TOWARD PALMITOYL-COA AND PNP-BUTYRATE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.FOROUHAR,S.LEW,J.SEETHARAMAN,R.SHASTRY,E.KOHAN,M.MAGLAQUI,L.MAO,
AUTHOR 2 R.XIAO,T.B.ACTON,J.K.EVERETT,G.T.MONTELIONE,L.TONG,J.F.HUNT,
AUTHOR 3 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM,NORTHEAST STRUCTURAL
AUTHOR 4 GENOMICS CONSORTIUM (NESG)
REVDAT 1 08-AUG-12 4FLE 0
JRNL AUTH F.FOROUHAR,S.LEW,J.SEETHARAMAN,R.SHASTRY,E.KOHAN,M.MAGLAQUI,
JRNL AUTH 2 L.MAO,R.XIAO,T.B.ACTON,J.K.EVERETT,G.T.MONTELIONE,L.TONG,
JRNL AUTH 3 J.F.HUNT,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM
JRNL TITL CRYSTAL STRUCTURE OF THE ESTERASE YQIA (YE3661) FROM
JRNL TITL 2 YERSINIA ENTEROCOLITICA, NORTHEAST STRUCTURAL GENOMICS
JRNL TITL 3 CONSORTIUM TARGET YER85 (CASP TARGET)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.3
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.06
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 161453.650
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 22145
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.400
REMARK 3 FREE R VALUE TEST SET COUNT : 2078
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3109
REMARK 3 BIN R VALUE (WORKING SET) : 0.1860
REMARK 3 BIN FREE R VALUE : 0.2460
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 342
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1543
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 183
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 9.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.85000
REMARK 3 B22 (A**2) : -0.49000
REMARK 3 B33 (A**2) : 1.34000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.07
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.15
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.72
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 54.54
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 4FLE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUN-12.
REMARK 100 THE RCSB ID CODE IS RCSB073044.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97911
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22631
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 46.060
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : 0.05800
REMARK 200 FOR THE DATA SET : 31.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.20700
REMARK 200 R SYM FOR SHELL (I) : 0.21400
REMARK 200 FOR SHELL : 7.350
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 10 MM TRIS (PH 7.5),
REMARK 280 100 MM SODIUM CHLORIDE, AND 5 MM DTT. CRYSTILLIZATION SOLUTION:
REMARK 280 100 MM TRIS (PH 8), 24% PEG 20K, AND 100 MM MG(NO3)2:6H2O. ,
REMARK 280 MICROBATCH UNDEROIL, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 27.52800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.77150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.52800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.77150
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 300 REMARK: MONOMER ACCORDING TO STATIC LIGHT SCATTERING.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 MSE A 1
REMARK 465 MSE A 2
REMARK 465 HIS A 198
REMARK 465 HIS A 199
REMARK 465 HIS A 200
REMARK 465 HIS A 201
REMARK 465 HIS A 202
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 SER A 13 -165.60 -104.31
REMARK 500 SER A 70 -125.94 56.74
REMARK 500 PHE A 175 102.98 75.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NESG-YER85 RELATED DB: TARGETTRACK
DBREF 4FLE A 1 194 UNP A1JQU0 A1JQU0_YERE8 1 194
SEQADV 4FLE LEU A 195 UNP A1JQU0 EXPRESSION TAG
SEQADV 4FLE GLU A 196 UNP A1JQU0 EXPRESSION TAG
SEQADV 4FLE HIS A 197 UNP A1JQU0 EXPRESSION TAG
SEQADV 4FLE HIS A 198 UNP A1JQU0 EXPRESSION TAG
SEQADV 4FLE HIS A 199 UNP A1JQU0 EXPRESSION TAG
SEQADV 4FLE HIS A 200 UNP A1JQU0 EXPRESSION TAG
SEQADV 4FLE HIS A 201 UNP A1JQU0 EXPRESSION TAG
SEQADV 4FLE HIS A 202 UNP A1JQU0 EXPRESSION TAG
SEQRES 1 A 202 MSE MSE SER THR LEU LEU TYR ILE HIS GLY PHE ASN SER
SEQRES 2 A 202 SER PRO SER SER ALA LYS ALA THR THR PHE LYS SER TRP
SEQRES 3 A 202 LEU GLN GLN HIS HIS PRO HIS ILE GLU MSE GLN ILE PRO
SEQRES 4 A 202 GLN LEU PRO PRO TYR PRO ALA GLU ALA ALA GLU MSE LEU
SEQRES 5 A 202 GLU SER ILE VAL MSE ASP LYS ALA GLY GLN SER ILE GLY
SEQRES 6 A 202 ILE VAL GLY SER SER LEU GLY GLY TYR PHE ALA THR TRP
SEQRES 7 A 202 LEU SER GLN ARG PHE SER ILE PRO ALA VAL VAL VAL ASN
SEQRES 8 A 202 PRO ALA VAL ARG PRO PHE GLU LEU LEU SER ASP TYR LEU
SEQRES 9 A 202 GLY GLU ASN GLN ASN PRO TYR THR GLY GLN LYS TYR VAL
SEQRES 10 A 202 LEU GLU SER ARG HIS ILE TYR ASP LEU LYS ALA MSE GLN
SEQRES 11 A 202 ILE GLU LYS LEU GLU SER PRO ASP LEU LEU TRP LEU LEU
SEQRES 12 A 202 GLN GLN THR GLY ASP GLU VAL LEU ASP TYR ARG GLN ALA
SEQRES 13 A 202 VAL ALA TYR TYR THR PRO CYS ARG GLN THR VAL GLU SER
SEQRES 14 A 202 GLY GLY ASN HIS ALA PHE VAL GLY PHE ASP HIS TYR PHE
SEQRES 15 A 202 SER PRO ILE VAL THR PHE LEU GLY LEU ALA THR ALA LEU
SEQRES 16 A 202 GLU HIS HIS HIS HIS HIS HIS
MODRES 4FLE MSE A 36 MET SELENOMETHIONINE
MODRES 4FLE MSE A 51 MET SELENOMETHIONINE
MODRES 4FLE MSE A 57 MET SELENOMETHIONINE
MODRES 4FLE MSE A 129 MET SELENOMETHIONINE
HET MSE A 36 8
HET MSE A 51 8
HET MSE A 57 8
HET MSE A 129 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 4(C5 H11 N O2 SE)
FORMUL 2 HOH *183(H2 O)
HELIX 1 1 SER A 17 HIS A 31 1 15
HELIX 2 2 TYR A 44 ALA A 60 1 17
HELIX 3 3 LEU A 71 PHE A 83 1 13
HELIX 4 4 ARG A 95 LEU A 100 1 6
HELIX 5 5 SER A 101 LEU A 104 5 4
HELIX 6 6 GLU A 119 ALA A 128 1 10
HELIX 7 7 SER A 136 ASP A 138 5 3
HELIX 8 8 ASP A 152 TYR A 160 1 9
HELIX 9 9 GLY A 177 HIS A 180 5 4
HELIX 10 10 TYR A 181 GLY A 190 1 10
SHEET 1 A 6 GLU A 35 GLN A 37 0
SHEET 2 A 6 THR A 4 ILE A 8 1 N LEU A 5 O GLU A 35
SHEET 3 A 6 ILE A 64 SER A 69 1 O GLY A 65 N LEU A 6
SHEET 4 A 6 ALA A 87 VAL A 90 1 O VAL A 88 N ILE A 66
SHEET 5 A 6 LEU A 140 GLN A 145 1 O LEU A 143 N VAL A 89
SHEET 6 A 6 ARG A 164 GLU A 168 1 O GLU A 168 N GLN A 144
SHEET 1 B 2 GLY A 105 GLN A 108 0
SHEET 2 B 2 LYS A 115 LEU A 118 -1 O TYR A 116 N ASN A 107
LINK C GLU A 35 N MSE A 36 1555 1555 1.33
LINK C MSE A 36 N GLN A 37 1555 1555 1.33
LINK C GLU A 50 N MSE A 51 1555 1555 1.33
LINK C MSE A 51 N LEU A 52 1555 1555 1.33
LINK C VAL A 56 N MSE A 57 1555 1555 1.33
LINK C MSE A 57 N ASP A 58 1555 1555 1.33
LINK C ALA A 128 N MSE A 129 1555 1555 1.33
LINK C MSE A 129 N GLN A 130 1555 1555 1.33
CRYST1 55.056 79.543 46.060 90.00 90.00 90.00 P 21 21 2 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 0.018163 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012572 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021711 0.00000
TER 1544 HIS A 197
MASTER 250 0 4 10 8 0 0 6 1726 1 40 16
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