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HEADER HYDROLASE 01-DEC-03 1USW
TITLE CRYSTAL STRUCTURE OF FERULIC ACID ESTERASE FROM ASPERGILLUS
TITLE 2 NIGER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERULOYL ESTERASE A;
COMPND 3 SYNONYM: FERULIC ACID ESTERASE, FAE-III;
COMPND 4 CHAIN: A;
COMPND 5 EC: 3.1.1.73;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;
SOURCE 3 STRAIN: CBS 120.49/N400;
SOURCE 4 EXPRESSION_SYSTEM: PICHIA PASTORIS
KEYWDS HYDROLASE, FERULOYL ESTERASE, DEGRADATION PLANT CELL WALLS
EXPDTA X-RAY DIFFRACTION
AUTHOR J.HERMOSO,J.SANZ-APARICIO,R.MOLINA,C.FAULDS
REVDAT 1 23-APR-04 1USW 0
JRNL AUTH J.HERMOSO,J.SANZ-APARICIO,R.MOLINA,N.JUGE,
JRNL AUTH 2 R.GONZALEZ,C.FAULDS
JRNL TITL THE CRYSTAL STRUCTURE OF FERULOYL ESTERASE A FROM
JRNL TITL 2 ASPERGILLUS NIGER SUGGESTS EVOLUTIVE FUNCTIONAL
JRNL TITL 3 CONVERGENCE IN FERULOYL ESTERASE FAMILY
JRNL REF J.MOL.BIOL. V. 338 495 2004
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.5 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,
REMARK 3 GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,
REMARK 3 PANNU,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) : 2.5
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 85.8
REMARK 3 NUMBER OF REFLECTIONS : 6830
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) : 0.212
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.7
REMARK 3 FREE R VALUE TEST SET COUNT : 527
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.013
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 63.6
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 772
REMARK 3 BIN R VALUE (WORKING SET) : 0.254
REMARK 3 BIN FREE R VALUE : 0.366
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.8
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 65
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.045
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1993
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 114
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.1
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.5
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.17
REMARK 3 B22 (A**2) : -1.22
REMARK 3 B33 (A**2) : -3.95
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 5.87
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM SIGMAA (A) : 0.29
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) : 0.46
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.44
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.4
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.3
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.89
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 : 0.43
REMARK 3 BSOL : 100.59
REMARK 3
REMARK 3 NCS MODEL : NONE
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 4 : CIS_PEPTIDE.PARAM
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1USW COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 1-DEC-2003.
REMARK 100 THE EBI ID CODE IS EBI-14089.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-2001
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : ENRAF-NONIUS
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6360
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.50
REMARK 200 RESOLUTION RANGE LOW (A) : 31.0
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.6
REMARK 200 DATA REDUNDANCY : 3.0
REMARK 200 R MERGE (I) : 0.112
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.6
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.3
REMARK 200 R MERGE FOR SHELL (I) : 0.213
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.7
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1TIB, 3TGL, 4TGL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.1
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 23.59000
REMARK 290 SMTRY3 2 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 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: MONOMERIC
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASN A 43 N - CA - C ANGL. DEV. = -10.8 DEGREES
REMARK 500 LEU A 134 CA - CB - CG ANGL. DEV. = 11.2 DEGREES
REMARK 500 TYR A 150 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 CYS A 258 N - CA - C ANGL. DEV. = 8.5 DEGREES
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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500
REMARK 500 CYS A 29 -130.05 -39.18
REMARK 500 SER A 220 159.64 57.97
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525 PROTEIN CHAIN SOLVENT CHAIN
REMARK 525 A Z
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 ASN 79, GLYCOSYLATION SITE
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
DBREF 1USW A 1 260 SWS O42807 FAEA_ASPNG 22 281
SEQRES 1 A 260 ALA SER THR GLN GLY ILE SER GLU ASP LEU TYR ASN ARG
SEQRES 2 A 260 LEU VAL GLU MET ALA THR ILE SER GLN ALA ALA TYR ALA
SEQRES 3 A 260 ASP LEU CYS ASN ILE PRO SER THR ILE ILE LYS GLY GLU
SEQRES 4 A 260 LYS ILE TYR ASN ALA GLN THR ASP ILE ASN GLY TRP ILE
SEQRES 5 A 260 LEU ARG ASP ASP THR SER LYS GLU ILE ILE THR VAL PHE
SEQRES 6 A 260 ARG GLY THR GLY SER ASP THR ASN LEU GLN LEU ASP THR
SEQRES 7 A 260 ASN TYR THR LEU THR PRO PHE ASP THR LEU PRO GLN CYS
SEQRES 8 A 260 ASN ASP CYS GLU VAL HIS GLY GLY TYR TYR ILE GLY TRP
SEQRES 9 A 260 ILE SER VAL GLN ASP GLN VAL GLU SER LEU VAL LYS GLN
SEQRES 10 A 260 GLN ALA SER GLN TYR PRO ASP TYR ALA LEU THR VAL THR
SEQRES 11 A 260 GLY HIS SER LEU GLY ALA SER MET ALA ALA LEU THR ALA
SEQRES 12 A 260 ALA GLN LEU SER ALA THR TYR ASP ASN VAL ARG LEU TYR
SEQRES 13 A 260 THR PHE GLY GLU PRO ARG SER GLY ASN GLN ALA PHE ALA
SEQRES 14 A 260 SER TYR MET ASN ASP ALA PHE GLN VAL SER SER PRO GLU
SEQRES 15 A 260 THR THR GLN TYR PHE ARG VAL THR HIS SER ASN ASP GLY
SEQRES 16 A 260 ILE PRO ASN LEU PRO PRO ALA ASP GLU GLY TYR ALA HIS
SEQRES 17 A 260 GLY GLY VAL GLU TYR TRP SER VAL ASP PRO TYR SER ALA
SEQRES 18 A 260 GLN ASN THR PHE VAL CYS THR GLY ASP GLU VAL GLN CYS
SEQRES 19 A 260 CYS GLU ALA GLN GLY GLY GLN GLY VAL ASN ASP ALA HIS
SEQRES 20 A 260 THR THR TYR PHE GLY MET THR SER GLY ALA CYS THR TRP
HET SO4 A1261 5
HET SO4 A1262 5
HET SO4 A1263 5
HET NAG A1264 14
HET NAG A1265 14 ASN 79, GLYCOSILATION SITE
HETNAM SO4 SULFATE ION
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN NAG NAG
FORMUL 2 SO4 3(O4 S1 2-)
FORMUL 3 NAG 2(C8 H15 N1 O6)
FORMUL 4 HOH *114(H2 O1)
HELIX 1 1 SER A 7 ALA A 24 1 18
HELIX 2 2 SER A 70 ASN A 79 1 10
HELIX 3 3 GLY A 98 ILE A 105 1 8
HELIX 4 4 VAL A 107 SER A 120 1 14
HELIX 5 5 SER A 133 SER A 147 1 15
HELIX 6 6 ASN A 165 PHE A 176 1 12
HELIX 7 7 PRO A 201 GLY A 205 5 5
HELIX 8 8 GLN A 233 GLY A 239 1 7
HELIX 9 9 ASN A 244 THR A 248 1 5
SHEET 1 AA 9 SER A 2 GLN A 4 0
SHEET 2 AA 9 THR A 224 CYS A 227 -1 O VAL A 226 N THR A 3
SHEET 3 AA 9 VAL A 211 SER A 215 -1 O GLU A 212 N CYS A 227
SHEET 4 AA 9 TYR A 186 HIS A 191 1 O TYR A 186 N VAL A 211
SHEET 5 AA 9 VAL A 153 PHE A 158 1 O LEU A 155 N PHE A 187
SHEET 6 AA 9 ALA A 126 HIS A 132 1 O LEU A 127 N ARG A 154
SHEET 7 AA 9 GLU A 60 PHE A 65 1 O ILE A 61 N THR A 128
SHEET 8 AA 9 ILE A 48 ASP A 55 -1 O TRP A 51 N VAL A 64
SHEET 9 AA 9 ILE A 35 ASN A 43 -1 O ILE A 36 N ARG A 54
SHEET 1 AB 2 LEU A 82 PRO A 84 0
SHEET 2 AB 2 GLU A 95 HIS A 97 -1 O VAL A 96 N THR A 83
SHEET 1 AC 2 THR A 249 TYR A 250 0
SHEET 2 AC 2 MET A 253 THR A 254 -1 O MET A 253 N TYR A 250
SSBOND 1 CYS A 29 CYS A 258 1555 1555
SSBOND 2 CYS A 91 CYS A 94 1555 1555
SSBOND 3 CYS A 227 CYS A 234 1555 1555
LINK ND2 ASN A 79 C1 NAG A1264 1555 1555
LINK O4 NAG A1264 C1 NAG A1265 1555 1555
CISPEP 1 LEU A 199 PRO A 200 0 -0.77
CISPEP 2 ASP A 217 PRO A 218 0 -1.07
SITE 1 AC1 4 ARG A 162 ASN A 198 ALA A 202 GLU A 236
SITE 1 AC2 5 GLU A 39 ARG A 54 GLN A 118 GLN A 121
SITE 2 AC2 5 HOH Z 111
SITE 1 AC3 5 ARG A 162 ALA A 207 HIS A 208 GLU A 236
SITE 2 AC3 5 HOH Z 112
SITE 1 AC4 4 ASP A 9 ASN A 79 THR A 83 GLY A 98
SITE 1 AC5 5 THR A 81 LEU A 82 THR A 83 ILE A 102
SITE 2 AC5 5 HOH Z 113
CRYST1 39.200 47.180 62.400 90.00 96.14 90.00 P 1 21 1 2
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 0.025510 0.000000 0.002744 0.00000
SCALE2 0.000000 0.021195 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016118 0.00000
TER 1994 TRP A 260
MASTER 265 0 5 9 13 0 8 6 2150 1 50 20
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