HEADER HYDROLASE 03-MAR-04 1UZ1
TITLE FAMILY 1 B-GLUCOSIDASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH
TITLE 2 ISOFAGOMINE LACTAM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-GLUCOSIDASE A;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BETA-D-GLUCOSIDE GLUCOHYDROLASE, GENTIOBIASE;
COMPND 5 EC: 3.2.1.21;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: CATALYTIC MODULE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PET-28A
KEYWDS HYDROLASE, GLUCOSIDE HYDROLYSIS, FAMILY GH1, ENZYME, ISOFAGOMINE
KEYWDS 2 LACTAM
EXPDTA X-RAY DIFFRACTION
AUTHOR T.M.GLOSTER,J.MACDONALD,R.V.STICK,G.J.DAVIES
REVDAT 5 13-DEC-23 1UZ1 1 REMARK
REVDAT 4 24-FEB-09 1UZ1 1 VERSN
REVDAT 3 06-MAR-07 1UZ1 1 REMARK
REVDAT 2 20-FEB-07 1UZ1 1 REMARK MASTER
REVDAT 1 23-NOV-04 1UZ1 0
JRNL AUTH F.VINCENT,T.M.GLOSTER,J.MACDONALD,C.MORLAND,R.V.STICK,
JRNL AUTH 2 F.M.V.DIAS,J.A.M.PRATES,C.M.G.A.FONTES,H.J.GILBERT,
JRNL AUTH 3 G.J.DAVIES
JRNL TITL COMMON INHIBITION OF BOTH -GLUCOSIDASES AND -MANNOSIDASES BY
JRNL TITL 2 ISOFAGOMINE LACTAM REFLECTS DIFFERENT CONFORMATIONAL
JRNL TITL 3 ITINERARIES FOR PYRANOSIDE HYDROLYSIS
JRNL REF CHEMBIOCHEM V. 5 1596 2004
JRNL REFN ISSN 1439-4227
JRNL PMID 15515081
JRNL DOI 10.1002/CBIC.200400169
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.M.GLOSTER,P.MELONCELLI,R.V.STICK,D.ZECHEL,A.VASELLA,
REMARK 1 AUTH 2 G.J.DAVIES
REMARK 1 TITL GLYCOSIDASE INHIBITION: AN ASSESSMENT OF THE BINDING OF 18
REMARK 1 TITL 2 PUTATIVE TRANSITION-STATE MIMICS.
REMARK 1 REF J.AM.CHEM.SOC. V. 129 2345 2007
REMARK 1 REFN ISSN 0002-7863
REMARK 1 PMID 17279749
REMARK 1 DOI 10.1021/JA066961G
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0000
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 72.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 62295
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 + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3228
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.06
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3843
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2460
REMARK 3 BIN FREE R VALUE SET COUNT : 200
REMARK 3 BIN FREE R VALUE : 0.3010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7147
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 521
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.20000
REMARK 3 B22 (A**2) : 0.43000
REMARK 3 B33 (A**2) : -0.23000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.200
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.178
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.129
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.608
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7452 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10134 ; 1.303 ; 1.915
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 876 ; 6.095 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 391 ;35.774 ;23.811
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1160 ;15.490 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 43 ;19.097 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1042 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5873 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3700 ; 0.204 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 473 ; 0.153 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 64 ; 0.173 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 28 ; 0.156 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4488 ; 0.782 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7051 ; 1.262 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3510 ; 1.824 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3083 ; 2.730 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UZ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1290014451.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.065
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111) OR
REMARK 200 SI(311)
REMARK 200 OPTICS : TOROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65765
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 4.950
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.73
REMARK 200 R MERGE FOR SHELL (I) : 0.43700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.340
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1OD0
REMARK 200
REMARK 200 REMARK: STRUCTURE ISOMORPHOUS WITH STARTING MODEL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10MG/ML PROTEIN IN 15% PEG 4000, 0.2 M
REMARK 280 CAAC, 0.1 M IMIDAZOLE PH7, PH 7.00
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 47.20600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.53150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.16350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.53150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 47.20600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.16350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 -21
REMARK 465 GLY A -20
REMARK 465 SER A -19
REMARK 465 SER A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 GLY A -9
REMARK 465 LEU A -8
REMARK 465 VAL A -7
REMARK 465 PRO A -6
REMARK 465 ARG A -5
REMARK 465 GLY A -4
REMARK 465 SER A -3
REMARK 465 HIS A -2
REMARK 465 MET A -1
REMARK 465 ALA A 0
REMARK 465 SER A 1
REMARK 465 ASN A 2
REMARK 465 GLU A 233
REMARK 465 ASP A 305
REMARK 465 ALA A 306
REMARK 465 PRO A 307
REMARK 465 ASP A 446
REMARK 465 MET B -21
REMARK 465 GLY B -20
REMARK 465 SER B -19
REMARK 465 SER B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 SER B -11
REMARK 465 SER B -10
REMARK 465 GLY B -9
REMARK 465 LEU B -8
REMARK 465 VAL B -7
REMARK 465 PRO B -6
REMARK 465 ARG B -5
REMARK 465 GLY B -4
REMARK 465 SER B -3
REMARK 465 HIS B -2
REMARK 465 MET B -1
REMARK 465 ALA B 0
REMARK 465 SER B 1
REMARK 465 LYS B 213
REMARK 465 ALA B 306
REMARK 465 PRO B 307
REMARK 465 GLU B 445
REMARK 465 ASP B 446
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 309 CD CE NZ
REMARK 470 LYS A 425 CE NZ
REMARK 470 LYS A 440 CD CE NZ
REMARK 470 LYS B 5 CG CD CE NZ
REMARK 470 GLU B 8 CB CG CD OE1 OE2
REMARK 470 LYS B 46 CE NZ
REMARK 470 LYS B 62 CG CD CE NZ
REMARK 470 LYS B 70 CD CE NZ
REMARK 470 LYS B 74 CG CD CE NZ
REMARK 470 ARG B 92 CD NE CZ NH1 NH2
REMARK 470 LYS B 206 CD CE NZ
REMARK 470 ASP B 214 CB CG OD1 OD2
REMARK 470 LYS B 216 CG CD CE NZ
REMARK 470 GLU B 231 CB CG CD OE1 OE2
REMARK 470 LYS B 232 CG CD CE NZ
REMARK 470 ASP B 305 CB CG OD1 OD2
REMARK 470 LYS B 309 CE NZ
REMARK 470 GLU B 362 CB CG CD OE1 OE2
REMARK 470 LYS B 376 CG CD CE NZ
REMARK 470 LYS B 440 CG CD CE NZ
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 64 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 106 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 357 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 28 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 106 CB - CG - OD2 ANGL. DEV. = 6.3 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
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 ALA A 54 -131.37 53.77
REMARK 500 TRP A 122 -14.34 96.53
REMARK 500 GLU A 231 7.88 -66.46
REMARK 500 TYR A 295 -41.56 -134.18
REMARK 500 ASP A 303 104.51 -163.58
REMARK 500 GLU A 405 59.73 -91.07
REMARK 500 TRP A 406 -127.75 52.81
REMARK 500 PRO B 7 152.71 -45.92
REMARK 500 ALA B 54 -119.61 55.23
REMARK 500 TRP B 122 -6.77 94.98
REMARK 500 TYR B 295 -43.89 -132.99
REMARK 500 ASP B 303 105.93 171.96
REMARK 500 PRO B 391 49.65 -72.25
REMARK 500 TRP B 406 -123.43 52.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2040 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH A2054 DISTANCE = 7.47 ANGSTROMS
REMARK 525 HOH A2074 DISTANCE = 7.56 ANGSTROMS
REMARK 525 HOH A2080 DISTANCE = 7.14 ANGSTROMS
REMARK 525 HOH A2138 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A2168 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH B2002 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH B2003 DISTANCE = 6.91 ANGSTROMS
REMARK 525 HOH B2028 DISTANCE = 6.19 ANGSTROMS
REMARK 700
REMARK 700 SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB"
REMARK 700 AND "BB" IN EACH CHAIN ON SHEET RECORDS BELOW ARE ACTUALLY 8-
REMARK 700 STRANDED BARRELS THAT ARE REPRESENTED BY 9-STRANDED SHEETS IN
REMARK 700 WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IFL A1446
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IFL B1445
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OD0 RELATED DB: PDB
REMARK 900 FAMILY 1 B-GLUCOSIDASE FROM THERMOTOGA MARITIMA
REMARK 900 RELATED ID: 1OIF RELATED DB: PDB
REMARK 900 FAMILY 1 B-GLUCOSIDASE FROM THERMOTOGA MARITIMA
REMARK 900 RELATED ID: 1OIM RELATED DB: PDB
REMARK 900 FAMILY 1 B-GLUCOSIDASE FROM THERMOTOGA MARITIMA
REMARK 900 RELATED ID: 1OIN RELATED DB: PDB
REMARK 900 FAMILY 1 B-GLUCOSIDASE FROM THERMOTOGA MARITIMA
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FULL LENGTH PROTEIN ALSO CONTAINS A HIS-TAG FROM THE
REMARK 999 PET28A CLONING VECTOR. NUMBERING OF THE PROTEIN AGREES
REMARK 999 WITH THE UNIPROT ENTRY AND THUS IGNORES THE HIS-TAG. ANY
REMARK 999 MISSING RESIDUES/ATOMS ARE DUE TO POOR OR A LACK OF
REMARK 999 ELECTRON DENSITY
DBREF 1UZ1 A -21 1 PDB 1UZ1 1UZ1 -21 1
DBREF 1UZ1 A 2 446 UNP Q08638 BGLA_THEMA 2 446
DBREF 1UZ1 B -21 1 PDB 1UZ1 1UZ1 -21 1
DBREF 1UZ1 B 2 446 UNP Q08638 BGLA_THEMA 2 446
SEQRES 1 A 468 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 468 LEU VAL PRO ARG GLY SER HIS MET ALA SER ASN VAL LYS
SEQRES 3 A 468 LYS PHE PRO GLU GLY PHE LEU TRP GLY VAL ALA THR ALA
SEQRES 4 A 468 SER TYR GLN ILE GLU GLY SER PRO LEU ALA ASP GLY ALA
SEQRES 5 A 468 GLY MET SER ILE TRP HIS THR PHE SER HIS THR PRO GLY
SEQRES 6 A 468 ASN VAL LYS ASN GLY ASP THR GLY ASP VAL ALA CYS ASP
SEQRES 7 A 468 HIS TYR ASN ARG TRP LYS GLU ASP ILE GLU ILE ILE GLU
SEQRES 8 A 468 LYS LEU GLY VAL LYS ALA TYR ARG PHE SER ILE SER TRP
SEQRES 9 A 468 PRO ARG ILE LEU PRO GLU GLY THR GLY ARG VAL ASN GLN
SEQRES 10 A 468 LYS GLY LEU ASP PHE TYR ASN ARG ILE ILE ASP THR LEU
SEQRES 11 A 468 LEU GLU LYS GLY ILE THR PRO PHE VAL THR ILE TYR HIS
SEQRES 12 A 468 TRP ASP LEU PRO PHE ALA LEU GLN LEU LYS GLY GLY TRP
SEQRES 13 A 468 ALA ASN ARG GLU ILE ALA ASP TRP PHE ALA GLU TYR SER
SEQRES 14 A 468 ARG VAL LEU PHE GLU ASN PHE GLY ASP ARG VAL LYS ASN
SEQRES 15 A 468 TRP ILE THR LEU ASN GLU PRO TRP VAL VAL ALA ILE VAL
SEQRES 16 A 468 GLY HIS LEU TYR GLY VAL HIS ALA PRO GLY MET ARG ASP
SEQRES 17 A 468 ILE TYR VAL ALA PHE ARG ALA VAL HIS ASN LEU LEU ARG
SEQRES 18 A 468 ALA HIS ALA ARG ALA VAL LYS VAL PHE ARG GLU THR VAL
SEQRES 19 A 468 LYS ASP GLY LYS ILE GLY ILE VAL PHE ASN ASN GLY TYR
SEQRES 20 A 468 PHE GLU PRO ALA SER GLU LYS GLU GLU ASP ILE ARG ALA
SEQRES 21 A 468 VAL ARG PHE MET HIS GLN PHE ASN ASN TYR PRO LEU PHE
SEQRES 22 A 468 LEU ASN PRO ILE TYR ARG GLY ASP TYR PRO GLU LEU VAL
SEQRES 23 A 468 LEU GLU PHE ALA ARG GLU TYR LEU PRO GLU ASN TYR LYS
SEQRES 24 A 468 ASP ASP MET SER GLU ILE GLN GLU LYS ILE ASP PHE VAL
SEQRES 25 A 468 GLY LEU ASN TYR TYR SER GLY HIS LEU VAL LYS PHE ASP
SEQRES 26 A 468 PRO ASP ALA PRO ALA LYS VAL SER PHE VAL GLU ARG ASP
SEQRES 27 A 468 LEU PRO LYS THR ALA MET GLY TRP GLU ILE VAL PRO GLU
SEQRES 28 A 468 GLY ILE TYR TRP ILE LEU LYS LYS VAL LYS GLU GLU TYR
SEQRES 29 A 468 ASN PRO PRO GLU VAL TYR ILE THR GLU ASN GLY ALA ALA
SEQRES 30 A 468 PHE ASP ASP VAL VAL SER GLU ASP GLY ARG VAL HIS ASP
SEQRES 31 A 468 GLN ASN ARG ILE ASP TYR LEU LYS ALA HIS ILE GLY GLN
SEQRES 32 A 468 ALA TRP LYS ALA ILE GLN GLU GLY VAL PRO LEU LYS GLY
SEQRES 33 A 468 TYR PHE VAL TRP SER LEU LEU ASP ASN PHE GLU TRP ALA
SEQRES 34 A 468 GLU GLY TYR SER LYS ARG PHE GLY ILE VAL TYR VAL ASP
SEQRES 35 A 468 TYR SER THR GLN LYS ARG ILE VAL LYS ASP SER GLY TYR
SEQRES 36 A 468 TRP TYR SER ASN VAL VAL LYS ASN ASN GLY LEU GLU ASP
SEQRES 1 B 468 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 468 LEU VAL PRO ARG GLY SER HIS MET ALA SER ASN VAL LYS
SEQRES 3 B 468 LYS PHE PRO GLU GLY PHE LEU TRP GLY VAL ALA THR ALA
SEQRES 4 B 468 SER TYR GLN ILE GLU GLY SER PRO LEU ALA ASP GLY ALA
SEQRES 5 B 468 GLY MET SER ILE TRP HIS THR PHE SER HIS THR PRO GLY
SEQRES 6 B 468 ASN VAL LYS ASN GLY ASP THR GLY ASP VAL ALA CYS ASP
SEQRES 7 B 468 HIS TYR ASN ARG TRP LYS GLU ASP ILE GLU ILE ILE GLU
SEQRES 8 B 468 LYS LEU GLY VAL LYS ALA TYR ARG PHE SER ILE SER TRP
SEQRES 9 B 468 PRO ARG ILE LEU PRO GLU GLY THR GLY ARG VAL ASN GLN
SEQRES 10 B 468 LYS GLY LEU ASP PHE TYR ASN ARG ILE ILE ASP THR LEU
SEQRES 11 B 468 LEU GLU LYS GLY ILE THR PRO PHE VAL THR ILE TYR HIS
SEQRES 12 B 468 TRP ASP LEU PRO PHE ALA LEU GLN LEU LYS GLY GLY TRP
SEQRES 13 B 468 ALA ASN ARG GLU ILE ALA ASP TRP PHE ALA GLU TYR SER
SEQRES 14 B 468 ARG VAL LEU PHE GLU ASN PHE GLY ASP ARG VAL LYS ASN
SEQRES 15 B 468 TRP ILE THR LEU ASN GLU PRO TRP VAL VAL ALA ILE VAL
SEQRES 16 B 468 GLY HIS LEU TYR GLY VAL HIS ALA PRO GLY MET ARG ASP
SEQRES 17 B 468 ILE TYR VAL ALA PHE ARG ALA VAL HIS ASN LEU LEU ARG
SEQRES 18 B 468 ALA HIS ALA ARG ALA VAL LYS VAL PHE ARG GLU THR VAL
SEQRES 19 B 468 LYS ASP GLY LYS ILE GLY ILE VAL PHE ASN ASN GLY TYR
SEQRES 20 B 468 PHE GLU PRO ALA SER GLU LYS GLU GLU ASP ILE ARG ALA
SEQRES 21 B 468 VAL ARG PHE MET HIS GLN PHE ASN ASN TYR PRO LEU PHE
SEQRES 22 B 468 LEU ASN PRO ILE TYR ARG GLY ASP TYR PRO GLU LEU VAL
SEQRES 23 B 468 LEU GLU PHE ALA ARG GLU TYR LEU PRO GLU ASN TYR LYS
SEQRES 24 B 468 ASP ASP MET SER GLU ILE GLN GLU LYS ILE ASP PHE VAL
SEQRES 25 B 468 GLY LEU ASN TYR TYR SER GLY HIS LEU VAL LYS PHE ASP
SEQRES 26 B 468 PRO ASP ALA PRO ALA LYS VAL SER PHE VAL GLU ARG ASP
SEQRES 27 B 468 LEU PRO LYS THR ALA MET GLY TRP GLU ILE VAL PRO GLU
SEQRES 28 B 468 GLY ILE TYR TRP ILE LEU LYS LYS VAL LYS GLU GLU TYR
SEQRES 29 B 468 ASN PRO PRO GLU VAL TYR ILE THR GLU ASN GLY ALA ALA
SEQRES 30 B 468 PHE ASP ASP VAL VAL SER GLU ASP GLY ARG VAL HIS ASP
SEQRES 31 B 468 GLN ASN ARG ILE ASP TYR LEU LYS ALA HIS ILE GLY GLN
SEQRES 32 B 468 ALA TRP LYS ALA ILE GLN GLU GLY VAL PRO LEU LYS GLY
SEQRES 33 B 468 TYR PHE VAL TRP SER LEU LEU ASP ASN PHE GLU TRP ALA
SEQRES 34 B 468 GLU GLY TYR SER LYS ARG PHE GLY ILE VAL TYR VAL ASP
SEQRES 35 B 468 TYR SER THR GLN LYS ARG ILE VAL LYS ASP SER GLY TYR
SEQRES 36 B 468 TRP TYR SER ASN VAL VAL LYS ASN ASN GLY LEU GLU ASP
HET IFL A1446 11
HET IFL B1445 11
HETNAM IFL (3S,4R,5R)-3,4-DIHYDROXY-5-(HYDROXYMETHYL)PIPERIDIN-2-
HETNAM 2 IFL ONE
HETSYN IFL ISOFAGOMINE LACTAM
FORMUL 3 IFL 2(C6 H11 N O4)
FORMUL 5 HOH *521(H2 O)
HELIX 1 1 ALA A 17 GLU A 22 1 6
HELIX 2 2 LEU A 26 ALA A 30 5 5
HELIX 3 3 SER A 33 HIS A 40 1 8
HELIX 4 4 VAL A 45 ASP A 49 5 5
HELIX 5 5 ASP A 56 LEU A 71 1 16
HELIX 6 6 SER A 81 LEU A 86 1 6
HELIX 7 7 ASN A 94 LYS A 111 1 18
HELIX 8 8 PRO A 125 LEU A 130 1 6
HELIX 9 9 LYS A 131 ARG A 137 5 7
HELIX 10 10 GLU A 138 GLY A 155 1 18
HELIX 11 11 GLU A 166 LEU A 176 1 11
HELIX 12 12 ASP A 186 VAL A 212 1 27
HELIX 13 13 GLU A 234 ASN A 247 1 14
HELIX 14 14 TYR A 248 GLY A 258 1 11
HELIX 15 15 PRO A 261 ARG A 269 1 9
HELIX 16 16 GLU A 270 LEU A 272 5 3
HELIX 17 17 ASN A 275 ASP A 278 5 4
HELIX 18 18 ASP A 279 GLN A 284 1 6
HELIX 19 19 PRO A 328 ASN A 343 1 16
HELIX 20 20 ASP A 368 GLU A 388 1 21
HELIX 21 21 GLU A 405 LYS A 412 5 8
HELIX 22 22 LYS A 429 ASN A 441 1 13
HELIX 23 23 ALA B 17 GLU B 22 1 6
HELIX 24 24 LEU B 26 ALA B 30 5 5
HELIX 25 25 SER B 33 HIS B 40 1 8
HELIX 26 26 VAL B 45 ASP B 49 5 5
HELIX 27 27 ASP B 56 GLY B 72 1 17
HELIX 28 28 SER B 81 LEU B 86 1 6
HELIX 29 29 ASN B 94 LYS B 111 1 18
HELIX 30 30 PRO B 125 LEU B 130 1 6
HELIX 31 31 LYS B 131 ARG B 137 5 7
HELIX 32 32 GLU B 138 GLY B 155 1 18
HELIX 33 33 GLU B 166 LEU B 176 1 11
HELIX 34 34 ASP B 186 VAL B 212 1 27
HELIX 35 35 LYS B 232 ASN B 247 1 16
HELIX 36 36 TYR B 248 GLY B 258 1 11
HELIX 37 37 PRO B 261 ARG B 269 1 9
HELIX 38 38 GLU B 270 LEU B 272 5 3
HELIX 39 39 ASN B 275 ASP B 278 5 4
HELIX 40 40 ASP B 279 GLN B 284 1 6
HELIX 41 41 GLU B 329 ASN B 343 1 15
HELIX 42 42 ASP B 368 GLU B 388 1 21
HELIX 43 43 GLU B 405 LYS B 412 5 8
HELIX 44 44 LYS B 429 ASN B 441 1 13
SHEET 1 AA 2 LYS A 4 LYS A 5 0
SHEET 2 AA 2 GLY A 443 LEU A 444 -1 O LEU A 444 N LYS A 4
SHEET 1 AB 9 LEU A 11 ALA A 15 0
SHEET 2 AB 9 LEU A 392 TRP A 398 1 O LYS A 393 N LEU A 11
SHEET 3 AB 9 VAL A 347 ASN A 352 1 O VAL A 347 N LYS A 393
SHEET 4 AB 9 PHE A 289 ASN A 293 1 O VAL A 290 N TYR A 348
SHEET 5 AB 9 LYS A 216 PHE A 221 1 O ILE A 219 N GLY A 291
SHEET 6 AB 9 ASN A 160 ASN A 165 1 O TRP A 161 N GLY A 218
SHEET 7 AB 9 THR A 114 TYR A 120 1 O PRO A 115 N ASN A 160
SHEET 8 AB 9 ALA A 75 SER A 79 1 O TYR A 76 N PHE A 116
SHEET 9 AB 9 LEU A 11 ALA A 15 1 O TRP A 12 N ALA A 75
SHEET 1 AC 3 TYR A 225 PRO A 228 0
SHEET 2 AC 3 GLY A 297 PHE A 302 1 O HIS A 298 N GLU A 227
SHEET 3 AC 3 VAL A 310 VAL A 313 -1 O SER A 311 N LYS A 301
SHEET 1 AD 2 VAL A 417 VAL A 419 0
SHEET 2 AD 2 ARG A 426 VAL A 428 -1 O ILE A 427 N TYR A 418
SHEET 1 BA 2 LYS B 4 LYS B 5 0
SHEET 2 BA 2 GLY B 443 LEU B 444 -1 O LEU B 444 N LYS B 4
SHEET 1 BB 9 LEU B 11 ALA B 15 0
SHEET 2 BB 9 LEU B 392 TRP B 398 1 O LYS B 393 N LEU B 11
SHEET 3 BB 9 VAL B 347 ASN B 352 1 O VAL B 347 N LYS B 393
SHEET 4 BB 9 PHE B 289 ASN B 293 1 O VAL B 290 N TYR B 348
SHEET 5 BB 9 LYS B 216 PHE B 221 1 O ILE B 219 N GLY B 291
SHEET 6 BB 9 ASN B 160 ASN B 165 1 O TRP B 161 N GLY B 218
SHEET 7 BB 9 THR B 114 TYR B 120 1 O PRO B 115 N ASN B 160
SHEET 8 BB 9 ALA B 75 SER B 79 1 O TYR B 76 N PHE B 116
SHEET 9 BB 9 LEU B 11 ALA B 15 1 O TRP B 12 N ALA B 75
SHEET 1 BC 3 TYR B 225 PRO B 228 0
SHEET 2 BC 3 GLY B 297 PHE B 302 1 O HIS B 298 N GLU B 227
SHEET 3 BC 3 VAL B 310 VAL B 313 -1 O SER B 311 N LYS B 301
SHEET 1 BD 2 VAL B 417 VAL B 419 0
SHEET 2 BD 2 ARG B 426 VAL B 428 -1 O ILE B 427 N TYR B 418
CISPEP 1 ALA A 181 PRO A 182 0 3.75
CISPEP 2 TRP A 398 SER A 399 0 2.02
CISPEP 3 ALA B 181 PRO B 182 0 3.69
CISPEP 4 TRP B 398 SER B 399 0 1.87
SITE 1 AC1 11 GLN A 20 HIS A 121 ASN A 165 GLU A 166
SITE 2 AC1 11 TYR A 295 TRP A 324 GLU A 351 TRP A 398
SITE 3 AC1 11 GLU A 405 TRP A 406 PHE A 414
SITE 1 AC2 11 GLN B 20 HIS B 121 ASN B 165 GLU B 166
SITE 2 AC2 11 TYR B 295 TRP B 324 GLU B 351 TRP B 398
SITE 3 AC2 11 GLU B 405 TRP B 406 PHE B 414
CRYST1 94.412 94.327 113.063 90.00 90.00 90.00 P 21 21 21 8
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 0.010592 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010601 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008845 0.00000
MTRIX1 1 -0.020780 -0.992120 -0.123580 -31.33893 1
MTRIX2 1 0.991000 -0.004090 -0.133800 28.67401 1
MTRIX3 1 0.132240 -0.125250 0.983270 13.81138 1
(ATOM LINES ARE NOT SHOWN.)
END
