HEADER HYDROLASE 17-SEP-02 1MQP
TITLE THE CRYSTAL STRUCTURE OF ALPHA-D-GLUCURONIDASE FROM BACILLUS
TITLE 2 STEAROTHERMOPHILUS T-6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-D-GLUCURONIDASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.2.1.139;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 1422;
SOURCE 4 GENE: AGUA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET9D
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.GOLAN,D.SHALLOM,A.TEPLITSKY,G.ZAIDE,S.SHULAMI,T.BAASOV,V.STOJANOFF,
AUTHOR 2 A.THOMPSON,Y.SHOHAM,G.SHOHAM
REVDAT 5 13-JUL-11 1MQP 1 VERSN
REVDAT 4 24-FEB-09 1MQP 1 VERSN
REVDAT 3 17-FEB-04 1MQP 1 JRNL
REVDAT 2 28-OCT-03 1MQP 1 SOURCE AUTHOR JRNL
REVDAT 1 23-SEP-03 1MQP 0
JRNL AUTH G.GOLAN,D.SHALLOM,A.TEPLITSKY,G.ZAIDE,S.SHULAMI,T.BAASOV,
JRNL AUTH 2 V.STOJANOFF,A.THOMPSON,Y.SHOHAM,G.SHOHAM
JRNL TITL CRYSTAL STRUCTURES OF GEOBACILLUS STEAROTHERMOPHILUS
JRNL TITL 2 ALPHA-GLUCURONIDASE COMPLEXED WITH ITS SUBSTRATE AND
JRNL TITL 3 PRODUCTS: MECHANISTIC IMPLICATIONS.
JRNL REF J.BIOL.CHEM. V. 279 3014 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 14573597
JRNL DOI 10.1074/JBC.M310098200
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.3
REMARK 3 NUMBER OF REFLECTIONS : 66682
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) : 0.192
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 6760
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 9857
REMARK 3 BIN R VALUE (WORKING SET) : 0.2150
REMARK 3 BIN FREE R VALUE : 0.2630
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1116
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.008
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5442
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 415
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.47000
REMARK 3 B22 (A**2) : 2.47000
REMARK 3 B33 (A**2) : -4.93000
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) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.12
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) : 0.25
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.18
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.78
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 : 0.37
REMARK 3 BSOL : 46.91
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : GOL.PAR
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : GOL.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MQP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-SEP-02.
REMARK 100 THE RCSB ID CODE IS RCSB017110.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-SEP-00
REMARK 200 TEMPERATURE (KELVIN) : 203.4
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X13
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.913
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67273
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
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 (%) : 91.8
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.15100
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: AB INITIO PHASING
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB CODE 1K9D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% ISOPROPANOL, 14% PEG 4K, 0.1M NA-
REMARK 280 CITRATE, PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 164.76050
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 36.86100
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 36.86100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 82.38025
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 36.86100
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 36.86100
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 247.14075
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 36.86100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 36.86100
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 82.38025
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 36.86100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 36.86100
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 247.14075
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 164.76050
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: DIMERIC
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 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 329.52100
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1171 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1166 LIES ON A SPECIAL POSITION.
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 THR A 2
REMARK 465 ASP A 283
REMARK 465 SER A 284
REMARK 465 GLU A 285
REMARK 465 PHE A 286
REMARK 465 PHE A 320
REMARK 465 VAL A 321
REMARK 465 TYR A 322
REMARK 465 ASN A 323
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 175 CG CD CE NZ
REMARK 470 ILE A 244 CG1 CG2 CD1
REMARK 470 ARG A 287 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 325 CG CD OE1 NE2
REMARK 470 ARG A 679 CG CD NE CZ NH1 NH2
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 CYS A 8 -125.68 57.52
REMARK 500 LEU A 10 54.71 -98.62
REMARK 500 SER A 135 82.57 -155.77
REMARK 500 MET A 363 -94.90 -108.05
REMARK 500 ASP A 364 77.23 -164.09
REMARK 500 GLN A 397 15.89 59.41
REMARK 500 TRP A 452 -41.75 67.06
REMARK 500 THR A 513 -140.57 -111.91
REMARK 500 TRP A 520 -130.32 59.69
REMARK 500 ASN A 531 81.79 -173.62
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 A1145 DISTANCE = 5.53 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 707
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1K9F RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A MUTATED FAMILY-67 ALPHA-D-
REMARK 900 GLUCURONIDASE (E285N) FROM BACILLUS STEAROTHERMOPHILUS T-6,
REMARK 900 COMPLEXED WITH ALDOTETRAOURONIC ACID
REMARK 900 RELATED ID: 1K9E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A MUTATED FAMILY-67 ALPHA-D-
REMARK 900 GLUCURONIDASE (E285N) FROM BACILLUS STEAROTHERMOPHILUS T-6,
REMARK 900 COMPLEXED WITH 4-O-METHYL-GLUCURONIC ACID
REMARK 900 RELATED ID: 1K9D RELATED DB: PDB
REMARK 900 THE 1.7 A CRYSTAL STRUCTURE OF ALPHA-D-GLUCURONIDASE, A
REMARK 900 FAMILY-67 GLYCOSIDE HYDROLASE FROM BACILLUS
REMARK 900 STEAROTHERMOPHILUS T-1
REMARK 900 RELATED ID: 1L8N RELATED DB: PDB
REMARK 900 THE 1.5A CRYSTAL STRUCTURE OF ALPHA-D-GLUCURONIDASE FROM
REMARK 900 BACILLUS STEAROTHERMOPHILUS T-1, COMPLEXED WITH 4-O-METHYL-
REMARK 900 GLUCURONIC ACID AND XYLOTRIOSE
REMARK 900 RELATED ID: 1MQQ RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF ALPHA-D-GLUCURONIDASE FROM
REMARK 900 BACILLUS STEAROTHERMOPHILUS T-1 COMPLEXED WITH GLUCURONIC
REMARK 900 ACID
REMARK 900 RELATED ID: 1MQR RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF ALPHA-D-GLUCURONIDASE (E386Q) FROM
REMARK 900 BACILLUS STEAROTHERMOPHILUS T-6
DBREF 1MQP A 1 679 UNP Q8VVD2 Q8VVD2_BACST 1 679
SEQRES 1 A 679 MET THR ALA GLY TYR GLU PRO CYS TRP LEU ARG TYR GLU
SEQRES 2 A 679 ARG LYS ASP GLN TYR SER ARG LEU ARG PHE GLU GLU ILE
SEQRES 3 A 679 VAL ALA LYS ARG THR SER PRO ILE PHE GLN ALA VAL VAL
SEQRES 4 A 679 GLU GLU LEU GLN LYS GLY LEU ARG SER MET MET GLU ILE
SEQRES 5 A 679 GLU PRO GLN VAL VAL GLN GLU VAL ASN GLU THR ALA ASN
SEQRES 6 A 679 SER ILE TRP LEU GLY THR LEU GLU ASP GLU GLU PHE GLU
SEQRES 7 A 679 ARG PRO LEU GLU GLY THR LEU VAL HIS PRO GLU GLY TYR
SEQRES 8 A 679 VAL ILE ARG SER ASP VAL ASP ASP GLY PRO PHE ARG ILE
SEQRES 9 A 679 TYR ILE ILE GLY LYS THR ASP ALA GLY VAL LEU TYR GLY
SEQRES 10 A 679 VAL PHE HIS PHE LEU ARG LEU LEU GLN MET GLY GLU ASN
SEQRES 11 A 679 ILE ALA GLN LEU SER ILE ILE GLU GLN PRO LYS ASN ARG
SEQRES 12 A 679 LEU ARG MET ILE ASN HIS TRP ASP ASN MET ASP GLY SER
SEQRES 13 A 679 ILE GLU ARG GLY TYR ALA GLY ARG SER ILE PHE PHE VAL
SEQRES 14 A 679 ASP ASP GLN PHE VAL LYS GLN ASN GLN ARG ILE LYS ASP
SEQRES 15 A 679 TYR ALA ARG LEU LEU ALA SER VAL GLY ILE ASN ALA ILE
SEQRES 16 A 679 SER ILE ASN ASN VAL ASN VAL HIS LYS THR GLU THR LYS
SEQRES 17 A 679 LEU ILE THR ASP HIS PHE LEU PRO ASP VAL ALA GLU VAL
SEQRES 18 A 679 ALA ASP ILE PHE ARG THR TYR GLY ILE LYS THR PHE LEU
SEQRES 19 A 679 SER ILE ASN TYR ALA SER PRO ILE GLU ILE GLY GLY LEU
SEQRES 20 A 679 PRO THR ALA ASP PRO LEU ASP PRO GLU VAL ARG ARG TRP
SEQRES 21 A 679 TRP LYS GLU THR ALA LYS ARG ILE TYR GLN TYR ILE PRO
SEQRES 22 A 679 ASP PHE GLY GLY PHE VAL VAL LYS ALA ASP SER GLU PHE
SEQRES 23 A 679 ARG PRO GLY PRO PHE THR TYR GLY ARG ASP HIS ALA GLU
SEQRES 24 A 679 GLY ALA ASN MET LEU ALA GLU ALA LEU ALA PRO PHE GLY
SEQRES 25 A 679 GLY LEU VAL ILE TRP ARG CYS PHE VAL TYR ASN CYS GLN
SEQRES 26 A 679 GLN ASP TRP ARG ASP ARG THR THR ASP ARG ALA LYS ALA
SEQRES 27 A 679 ALA TYR ASP HIS PHE LYS PRO LEU ASP GLY GLN PHE ARG
SEQRES 28 A 679 GLU ASN VAL ILE LEU GLN ILE LYS ASN GLY PRO MET ASP
SEQRES 29 A 679 PHE GLN VAL ARG GLU PRO VAL SER PRO LEU PHE GLY ALA
SEQRES 30 A 679 MET PRO LYS THR ASN GLN MET MET GLU VAL GLN ILE THR
SEQRES 31 A 679 GLN GLU TYR THR GLY GLN GLN LYS HIS LEU CYS PHE LEU
SEQRES 32 A 679 ILE PRO GLN TRP LYS GLU VAL LEU ASP PHE ASP THR TYR
SEQRES 33 A 679 ALA LYS GLY LYS GLY SER GLU VAL LYS LYS VAL ILE ASP
SEQRES 34 A 679 GLY SER LEU PHE ASP TYR ARG TYR SER GLY ILE ALA GLY
SEQRES 35 A 679 VAL SER ASN ILE GLY SER ASP PRO ASN TRP THR GLY HIS
SEQRES 36 A 679 THR LEU ALA GLN ALA ASN LEU TYR GLY PHE GLY ARG LEU
SEQRES 37 A 679 ALA TRP ASN PRO ASP LEU SER ALA GLU GLU ILE ALA ASN
SEQRES 38 A 679 GLU TRP VAL VAL GLN THR PHE GLY ASP ASP SER GLN VAL
SEQRES 39 A 679 VAL GLU THR ILE SER TRP MET LEU LEU SER SER TRP ARG
SEQRES 40 A 679 ILE TYR GLU ASN TYR THR SER PRO LEU GLY VAL GLY TRP
SEQRES 41 A 679 MET VAL ASN PRO GLY HIS HIS TYR GLY PRO ASN VAL ASP
SEQRES 42 A 679 GLY TYR GLU TYR SER HIS TRP GLY THR TYR HIS TYR ALA
SEQRES 43 A 679 ASP ARG ASP GLY ILE GLY VAL ASP ARG THR VAL ALA THR
SEQRES 44 A 679 GLY THR GLY TYR THR ALA GLN TYR PHE PRO GLU ASN ALA
SEQRES 45 A 679 ALA MET TYR GLU SER LEU ASP THR CYS PRO ASP GLU LEU
SEQRES 46 A 679 LEU LEU PHE PHE HIS HIS VAL PRO TYR THR HIS ARG LEU
SEQRES 47 A 679 HIS SER GLY GLU THR VAL ILE GLN HIS ILE TYR ASN THR
SEQRES 48 A 679 HIS PHE GLU GLY VAL GLU GLN ALA LYS GLN LEU ARG LYS
SEQRES 49 A 679 ARG TRP GLU GLN LEU LYS GLY LYS ILE ASP GLU LYS ARG
SEQRES 50 A 679 TYR HIS ASP VAL LEU GLU ARG LEU THR ILE GLN VAL GLU
SEQRES 51 A 679 HIS ALA LYS GLU TRP ARG ASP VAL ILE ASN THR TYR PHE
SEQRES 52 A 679 TYR ARG LYS SER GLY ILE ASP ASP GLN TYR GLY ARG LYS
SEQRES 53 A 679 ILE TYR ARG
HET GOL A 701 6
HET GOL A 702 6
HET GOL A 703 6
HET GOL A 704 6
HET GOL A 705 6
HET GOL A 706 6
HET GOL A 707 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL 7(C3 H8 O3)
FORMUL 9 HOH *415(H2 O)
HELIX 1 1 SER A 32 GLU A 51 1 20
HELIX 2 2 GLU A 73 GLU A 75 5 3
HELIX 3 3 ARG A 79 THR A 84 1 6
HELIX 4 4 THR A 110 MET A 127 1 18
HELIX 5 5 ASN A 177 VAL A 190 1 14
HELIX 6 6 HIS A 203 LYS A 208 1 6
HELIX 7 7 LEU A 209 THR A 211 5 3
HELIX 8 8 PHE A 214 TYR A 228 1 15
HELIX 9 9 ALA A 239 ILE A 244 1 6
HELIX 10 10 ASP A 254 ILE A 272 1 19
HELIX 11 11 GLY A 289 GLY A 294 5 6
HELIX 12 12 ASP A 296 ALA A 309 1 14
HELIX 13 13 PRO A 310 GLY A 312 5 3
HELIX 14 14 ASP A 334 ALA A 336 5 3
HELIX 15 15 LYS A 337 LYS A 344 1 8
HELIX 16 16 PRO A 345 ASP A 347 5 3
HELIX 17 17 LEU A 403 ASP A 412 1 10
HELIX 18 18 GLU A 423 ASP A 429 1 7
HELIX 19 19 HIS A 455 LEU A 457 5 3
HELIX 20 20 ALA A 458 ASN A 471 1 14
HELIX 21 21 SER A 475 GLY A 489 1 15
HELIX 22 22 ASP A 491 TYR A 512 1 22
HELIX 23 23 GLY A 562 TYR A 567 5 6
HELIX 24 24 PHE A 568 SER A 577 1 10
HELIX 25 25 PRO A 582 GLU A 584 5 3
HELIX 26 26 LEU A 585 HIS A 590 1 6
HELIX 27 27 THR A 603 GLN A 628 1 26
HELIX 28 28 ASP A 634 GLY A 668 1 35
SHEET 1 A 6 GLN A 55 VAL A 57 0
SHEET 2 A 6 GLU A 25 ALA A 28 1 N ILE A 26 O VAL A 57
SHEET 3 A 6 SER A 66 THR A 71 1 O LEU A 69 N VAL A 27
SHEET 4 A 6 ARG A 103 GLY A 108 1 O ILE A 104 N TRP A 68
SHEET 5 A 6 TYR A 91 SER A 95 -1 N ARG A 94 O TYR A 105
SHEET 6 A 6 SER A 135 GLU A 138 -1 O ILE A 136 N ILE A 93
SHEET 1 B 9 LEU A 144 ASN A 148 0
SHEET 2 B 9 ALA A 194 SER A 196 1 O SER A 196 N ILE A 147
SHEET 3 B 9 LYS A 231 ILE A 236 1 O PHE A 233 N ILE A 195
SHEET 4 B 9 GLY A 277 VAL A 280 1 O VAL A 279 N LEU A 234
SHEET 5 B 9 LEU A 314 ARG A 318 1 O ILE A 316 N VAL A 280
SHEET 6 B 9 VAL A 354 LYS A 359 1 O ILE A 355 N VAL A 315
SHEET 7 B 9 GLN A 383 GLN A 388 1 O GLU A 386 N ILE A 358
SHEET 8 B 9 GLY A 439 VAL A 443 1 O ALA A 441 N MET A 385
SHEET 9 B 9 LEU A 144 ASN A 148 1 N ASN A 148 O GLY A 442
SHEET 1 C 2 PHE A 168 VAL A 169 0
SHEET 2 C 2 GLN A 172 PHE A 173 -1 O GLN A 172 N VAL A 169
SHEET 1 D 2 GLY A 550 ILE A 551 0
SHEET 2 D 2 VAL A 592 PRO A 593 -1 O VAL A 592 N ILE A 551
LINK OG1BTHR A 580 O1 GOL A 707 1555 1555 1.98
SITE 1 AC1 11 TYR A 91 TYR A 116 HIS A 120 ARG A 123
SITE 2 AC1 11 SER A 189 VAL A 190 GLY A 191 ARG A 467
SITE 3 AC1 11 TRP A 470 HOH A 884 HOH A 930
SITE 1 AC2 10 ARG A 368 GLU A 369 VAL A 371 GLU A 409
SITE 2 AC2 10 PHE A 413 LEU A 585 HOH A 809 HOH A 848
SITE 3 AC2 10 HOH A 983 HOH A1038
SITE 1 AC3 5 LYS A 620 LYS A 653 ARG A 656 HOH A1011
SITE 2 AC3 5 HOH A1193
SITE 1 AC4 6 SER A 19 GLU A 129 HIS A 599 HOH A 890
SITE 2 AC4 6 HOH A 918 HOH A1215
SITE 1 AC5 7 TYR A 340 ALA A 377 ALA A 565 GLN A 566
SITE 2 AC5 7 TYR A 567 PHE A 568 PRO A 569
SITE 1 AC6 5 ARG A 335 HIS A 527 TYR A 535 TRP A 540
SITE 2 AC6 5 HOH A 971
SITE 1 AC7 4 GLU A 570 MET A 574 THR A 580 HOH A1218
CRYST1 73.722 73.722 329.521 90.00 90.00 90.00 P 41 21 2 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 0.013564 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013564 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003035 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
