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HEADER HYDROLASE 16-JUL-12 4G4I
TITLE CRYSTAL STRUCTURE OF GLUCURONOYL ESTERASE S213A MUTANT FROM
TITLE 2 SPOROTRICHUM THERMOPHILE DETERMINED AT 1.9 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 4-O-METHYL-GLUCURONOYL METHYLESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCELIOPHTHORA THERMOPHILA;
SOURCE 3 ORGANISM_TAXID: 573729;
SOURCE 4 STRAIN: ATCC 42464;
SOURCE 5 GENE: MYCTH_55568;
SOURCE 6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: X-33;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPICZALPHAC
KEYWDS ALPHA/BETA HYDROLASE, 3-LAYER ALPHA/BETA/ALPHA SANDWICH, ROSSMANN
KEYWDS 2 FOLD, GLUCURONOYL ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.D.CHARVAGI,M.DIMAROGONA,E.TOPAKAS,P.CHRISTAKOPOULOS,E.D.CHRYSINA
REVDAT 1 02-JAN-13 4G4I 0
JRNL AUTH M.-D.CHARAVGI,M.DIMAROGONA,E.TOPAKAS,P.CHRISTAKOPOULOS,
JRNL AUTH 2 E.D.CHRYSINA
JRNL TITL THE STRUCTURE OF A NOVEL GLUCURONOYL ESTERASE FROM
JRNL TITL 2 MYCELIOPHTHORA THERMOPHILA GIVES NEW INSIGHTS INTO ITS ROLE
JRNL TITL 3 AS A POTENTIAL BIOCATALYST.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 69 63 2013
JRNL REFN ISSN 0907-4449
JRNL DOI 10.1107/S0907444912042400
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 13.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 28557
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) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1524
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1811
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.82
REMARK 3 BIN R VALUE (WORKING SET) : 0.2120
REMARK 3 BIN FREE R VALUE SET COUNT : 90
REMARK 3 BIN FREE R VALUE : 0.2540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2736
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 437
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 8.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 9.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.150
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.136
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.084
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.827
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2874 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3906 ; 0.997 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 382 ; 5.117 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 121 ;28.646 ;24.628
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 419 ;12.314 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;16.110 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 428 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2219 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : 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: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4G4I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUL-12.
REMARK 100 THE RCSB ID CODE IS RCSB073727.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : OXFORD DIFFRACTION SUPERNOVA
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : OTHER
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5419
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MUTLTI-LAYER XRAY OPTIC
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ATLAS 135MM CCD DETECTOR
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSALISPRO
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30113
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 13.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.4000
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) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.21000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4G4G
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 550 MME, 0.1M SODIUM ACETATE
REMARK 280 , PH 4.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21
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,-Z+1/2
REMARK 290 4555 -X+1/2,-Y,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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 26.00500
REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.91100
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 26.00500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 51.91100
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: 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 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 A 928 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 SER A -13
REMARK 465 MET A -12
REMARK 465 ALA A -11
REMARK 465 PRO A -10
REMARK 465 MET A -9
REMARK 465 ASN A -8
REMARK 465 HIS A -7
REMARK 465 ILE A -6
REMARK 465 PHE A -5
REMARK 465 GLU A -4
REMARK 465 ARG A -3
REMARK 465 GLN A -2
REMARK 465 ASP A -1
REMARK 465 THR A 0
REMARK 465 MET A 1
REMARK 465 VAL A 2
REMARK 465 HIS A 3
REMARK 465 LEU A 4
REMARK 465 THR A 5
REMARK 465 SER A 6
REMARK 465 ALA A 7
REMARK 465 LEU A 8
REMARK 465 LEU A 9
REMARK 465 VAL A 10
REMARK 465 ALA A 11
REMARK 465 GLY A 12
REMARK 465 ALA A 13
REMARK 465 ALA A 14
REMARK 465 PHE A 15
REMARK 465 ALA A 16
REMARK 465 ALA A 17
REMARK 465 ALA A 18
REMARK 465 ALA A 19
REMARK 465 PRO A 20
REMARK 465 MET A 21
REMARK 465 ASN A 22
REMARK 465 HIS A 23
REMARK 465 ILE A 24
REMARK 465 PHE A 25
REMARK 465 GLU A 26
REMARK 465 ARG A 27
REMARK 465 GLN A 28
REMARK 465 LEU A 398
REMARK 465 GLU A 399
REMARK 465 GLN A 400
REMARK 465 LYS A 401
REMARK 465 LEU A 402
REMARK 465 ILE A 403
REMARK 465 SER A 404
REMARK 465 GLU A 405
REMARK 465 GLU A 406
REMARK 465 ASP A 407
REMARK 465 LEU A 408
REMARK 465 ASN A 409
REMARK 465 SER A 410
REMARK 465 ALA A 411
REMARK 465 VAL A 412
REMARK 465 ASP A 413
REMARK 465 HIS A 414
REMARK 465 HIS A 415
REMARK 465 HIS A 416
REMARK 465 HIS A 417
REMARK 465 HIS A 418
REMARK 465 HIS A 419
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 VAL A 40 -167.35 -120.45
REMARK 500 GLU A 78 -49.24 -149.07
REMARK 500 ALA A 213 -121.34 63.05
REMARK 500 PRO A 269 44.19 -82.65
REMARK 500 SER A 281 54.99 -143.75
REMARK 500 PRO A 286 33.87 -77.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 511
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4G4G RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RECOMBINANT GLUCURONOYL ESTERASE FROM
REMARK 900 SPOROTRICHUM THERMOPHILE DETERMINED AT 1.55 A RESOLUTION
REMARK 900 RELATED ID: 4G4J RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS SEGMENT CORRESPONDS TO A C-MYC EPITOPE
DBREF 4G4I A 1 397 UNP G2QJR6 G2QJR6_THIHA 1 397
SEQADV 4G4I SER A -13 UNP G2QJR6 INSERTION
SEQADV 4G4I MET A -12 UNP G2QJR6 INSERTION
SEQADV 4G4I ALA A -11 UNP G2QJR6 INSERTION
SEQADV 4G4I PRO A -10 UNP G2QJR6 INSERTION
SEQADV 4G4I MET A -9 UNP G2QJR6 INSERTION
SEQADV 4G4I ASN A -8 UNP G2QJR6 INSERTION
SEQADV 4G4I HIS A -7 UNP G2QJR6 INSERTION
SEQADV 4G4I ILE A -6 UNP G2QJR6 INSERTION
SEQADV 4G4I PHE A -5 UNP G2QJR6 INSERTION
SEQADV 4G4I GLU A -4 UNP G2QJR6 INSERTION
SEQADV 4G4I ARG A -3 UNP G2QJR6 INSERTION
SEQADV 4G4I GLN A -2 UNP G2QJR6 INSERTION
SEQADV 4G4I ASP A -1 UNP G2QJR6 INSERTION
SEQADV 4G4I THR A 0 UNP G2QJR6 INSERTION
SEQADV 4G4I ALA A 213 UNP G2QJR6 SER 213 ENGINEERED MUTATION
SEQADV 4G4I LEU A 398 UNP G2QJR6 SEE REMARK 999
SEQADV 4G4I GLU A 399 UNP G2QJR6 SEE REMARK 999
SEQADV 4G4I GLN A 400 UNP G2QJR6 SEE REMARK 999
SEQADV 4G4I LYS A 401 UNP G2QJR6 SEE REMARK 999
SEQADV 4G4I LEU A 402 UNP G2QJR6 SEE REMARK 999
SEQADV 4G4I ILE A 403 UNP G2QJR6 SEE REMARK 999
SEQADV 4G4I SER A 404 UNP G2QJR6 SEE REMARK 999
SEQADV 4G4I GLU A 405 UNP G2QJR6 SEE REMARK 999
SEQADV 4G4I GLU A 406 UNP G2QJR6 SEE REMARK 999
SEQADV 4G4I ASP A 407 UNP G2QJR6 SEE REMARK 999
SEQADV 4G4I LEU A 408 UNP G2QJR6 SEE REMARK 999
SEQADV 4G4I ASN A 409 UNP G2QJR6 SEE REMARK 999
SEQADV 4G4I SER A 410 UNP G2QJR6 SEE REMARK 999
SEQADV 4G4I ALA A 411 UNP G2QJR6 SEE REMARK 999
SEQADV 4G4I VAL A 412 UNP G2QJR6 SEE REMARK 999
SEQADV 4G4I ASP A 413 UNP G2QJR6 SEE REMARK 999
SEQADV 4G4I HIS A 414 UNP G2QJR6 EXPRESSION TAG
SEQADV 4G4I HIS A 415 UNP G2QJR6 EXPRESSION TAG
SEQADV 4G4I HIS A 416 UNP G2QJR6 EXPRESSION TAG
SEQADV 4G4I HIS A 417 UNP G2QJR6 EXPRESSION TAG
SEQADV 4G4I HIS A 418 UNP G2QJR6 EXPRESSION TAG
SEQADV 4G4I HIS A 419 UNP G2QJR6 EXPRESSION TAG
SEQRES 1 A 433 SER MET ALA PRO MET ASN HIS ILE PHE GLU ARG GLN ASP
SEQRES 2 A 433 THR MET VAL HIS LEU THR SER ALA LEU LEU VAL ALA GLY
SEQRES 3 A 433 ALA ALA PHE ALA ALA ALA ALA PRO MET ASN HIS ILE PHE
SEQRES 4 A 433 GLU ARG GLN ASP THR CYS SER VAL SER ASP ASN TYR PRO
SEQRES 5 A 433 THR VAL ASN SER ALA LYS LEU PRO ASP PRO PHE THR THR
SEQRES 6 A 433 ALA SER GLY GLU LYS VAL THR THR LYS ASP GLN PHE GLU
SEQRES 7 A 433 CYS ARG ARG ALA GLU ILE ASN LYS ILE LEU GLN GLN TYR
SEQRES 8 A 433 GLU LEU GLY GLU TYR PRO GLY PRO PRO ASP SER VAL GLU
SEQRES 9 A 433 ALA SER LEU SER GLY ASN SER ILE THR VAL ARG VAL THR
SEQRES 10 A 433 VAL GLY SER LYS SER ILE SER PHE SER ALA SER ILE ARG
SEQRES 11 A 433 LYS PRO SER GLY ALA GLY PRO PHE PRO ALA ILE ILE GLY
SEQRES 12 A 433 ILE GLY GLY ALA SER ILE PRO ILE PRO SER ASN VAL ALA
SEQRES 13 A 433 THR ILE THR PHE ASN ASN ASP GLU PHE GLY ALA GLN MET
SEQRES 14 A 433 GLY SER GLY SER ARG GLY GLN GLY LYS PHE TYR ASP LEU
SEQRES 15 A 433 PHE GLY ARG ASP HIS SER ALA GLY SER LEU THR ALA TRP
SEQRES 16 A 433 ALA TRP GLY VAL ASP ARG LEU ILE ASP GLY LEU GLU GLN
SEQRES 17 A 433 VAL GLY ALA GLN ALA SER GLY ILE ASP THR LYS ARG LEU
SEQRES 18 A 433 GLY VAL THR GLY CYS ALA ARG ASN GLY LYS GLY ALA PHE
SEQRES 19 A 433 ILE THR GLY ALA LEU VAL ASP ARG ILE ALA LEU THR ILE
SEQRES 20 A 433 PRO GLN GLU SER GLY ALA GLY GLY ALA ALA CYS TRP ARG
SEQRES 21 A 433 ILE SER ASP GLN GLN LYS ALA ALA GLY ALA ASN ILE GLN
SEQRES 22 A 433 THR ALA ALA GLN ILE ILE THR GLU ASN PRO TRP PHE SER
SEQRES 23 A 433 ARG ASN PHE ASP PRO HIS VAL ASN SER ILE THR SER VAL
SEQRES 24 A 433 PRO GLN ASP HIS HIS LEU LEU ALA ALA LEU ILE VAL PRO
SEQRES 25 A 433 ARG GLY LEU ALA VAL PHE GLU ASN ASN ILE ASP TRP LEU
SEQRES 26 A 433 GLY PRO VAL SER THR THR GLY CYS MET ALA ALA GLY ARG
SEQRES 27 A 433 LEU ILE TYR LYS ALA TYR GLY VAL PRO ASN ASN MET GLY
SEQRES 28 A 433 PHE SER LEU VAL GLY GLY HIS ASN HIS CYS GLN PHE PRO
SEQRES 29 A 433 SER SER GLN ASN GLN ASP LEU ASN SER TYR ILE ASN TYR
SEQRES 30 A 433 PHE LEU LEU GLY GLN GLY SER PRO SER GLY VAL GLU HIS
SEQRES 31 A 433 SER ASP VAL ASN VAL ASN VAL ALA GLU TRP ALA PRO TRP
SEQRES 32 A 433 GLY ALA GLY ALA PRO THR LEU ALA LEU GLU GLN LYS LEU
SEQRES 33 A 433 ILE SER GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS
SEQRES 34 A 433 HIS HIS HIS HIS
HET EDO A 501 4
HET EDO A 502 4
HET EDO A 503 4
HET EDO A 504 4
HET EDO A 505 4
HET EDO A 506 4
HET EDO A 507 4
HET EDO A 508 4
HET GOL A 509 6
HET GOL A 510 6
HET GOL A 511 6
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 EDO 8(C2 H6 O2)
FORMUL 10 GOL 3(C3 H8 O3)
FORMUL 13 HOH *437(H2 O)
HELIX 1 1 THR A 59 GLU A 78 1 20
HELIX 2 2 GLY A 156 ARG A 160 5 5
HELIX 3 3 GLY A 163 GLY A 170 1 8
HELIX 4 4 GLY A 176 GLY A 196 1 21
HELIX 5 5 GLY A 196 GLY A 201 1 6
HELIX 6 6 ALA A 213 VAL A 226 1 14
HELIX 7 7 CYS A 244 ALA A 254 1 11
HELIX 8 8 THR A 260 ILE A 265 1 6
HELIX 9 9 SER A 272 VAL A 279 5 8
HELIX 10 10 SER A 281 VAL A 285 5 5
HELIX 11 11 ASP A 288 HIS A 290 5 3
HELIX 12 12 LEU A 291 VAL A 297 1 7
HELIX 13 13 ILE A 308 LEU A 311 5 4
HELIX 14 14 GLY A 312 GLY A 331 1 20
HELIX 15 15 VAL A 332 ASN A 334 5 3
HELIX 16 16 PRO A 350 SER A 352 5 3
HELIX 17 17 GLN A 353 LEU A 365 1 13
HELIX 18 18 ASN A 382 ALA A 387 1 6
SHEET 1 A10 SER A 88 SER A 94 0
SHEET 2 A10 SER A 97 VAL A 104 -1 O ARG A 101 N GLU A 90
SHEET 3 A10 LYS A 107 ARG A 116 -1 O PHE A 111 N VAL A 100
SHEET 4 A10 ALA A 142 PHE A 146 -1 O THR A 143 N ARG A 116
SHEET 5 A10 PHE A 124 ILE A 130 1 N GLY A 129 O ILE A 144
SHEET 6 A10 ILE A 202 CYS A 212 1 O GLY A 208 N ILE A 128
SHEET 7 A10 LEU A 231 GLN A 235 1 O ILE A 233 N VAL A 209
SHEET 8 A10 GLY A 300 GLU A 305 1 O ALA A 302 N THR A 232
SHEET 9 A10 MET A 336 LEU A 340 1 O SER A 339 N GLU A 305
SHEET 10 A10 GLU A 375 HIS A 376 1 O HIS A 376 N LEU A 340
SSBOND 1 CYS A 31 CYS A 65 1555 1555 2.03
SSBOND 2 CYS A 212 CYS A 347 1555 1555 2.03
SSBOND 3 CYS A 244 CYS A 319 1555 1555 2.03
CISPEP 1 GLY A 122 PRO A 123 0 -1.81
CISPEP 2 VAL A 297 PRO A 298 0 -0.15
SITE 1 AC1 5 LYS A 56 ASP A 87 GOL A 510 HOH A 881
SITE 2 AC1 5 HOH A 969
SITE 1 AC2 7 GLU A 90 ALA A 91 SER A 92 THR A 99
SITE 2 AC2 7 ARG A 101 SER A 110 HOH A 882
SITE 1 AC3 4 LYS A 107 ASP A 167 LEU A 168 GLY A 170
SITE 1 AC4 6 LYS A 328 ALA A 329 ALA A 393 PRO A 394
SITE 2 AC4 6 THR A 395 HOH A 799
SITE 1 AC5 7 CYS A 31 VAL A 33 ALA A 68 PRO A 277
SITE 2 AC5 7 HOH A 708 HOH A 734 HOH A 971
SITE 1 AC6 1 ARG A 214
SITE 1 AC7 5 LYS A 44 GLU A 385 TRP A 386 HOH A 972
SITE 2 AC7 5 HOH A1032
SITE 1 AC8 4 LYS A 217 GLN A 259 GLU A 267 TRP A 310
SITE 1 AC9 7 SER A 32 THR A 51 SER A 53 GLU A 55
SITE 2 AC9 7 GLU A 193 HOH A 625 HOH A 704
SITE 1 BC1 11 ASP A 47 PHE A 49 THR A 50 LYS A 56
SITE 2 BC1 11 TRP A 389 GLY A 392 EDO A 501 HOH A 626
SITE 3 BC1 11 HOH A 649 HOH A 883 HOH A 969
SITE 1 BC2 6 ARG A 116 ILE A 137 PRO A 138 VAL A 141
SITE 2 BC2 6 ALA A 142 THR A 143
CRYST1 52.010 69.616 103.822 90.00 90.00 90.00 P 21 2 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 0.019227 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014365 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009632 0.00000
TER 2761 ALA A 397
MASTER 386 0 11 18 10 0 20 6 3223 1 56 34
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