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HEADER HYDROLASE 07-JUL-06 2IX9
TITLE RESPECTIVE ROLE OF PROTEIN FOLDING AND GLYCOSYLATION IN THE
TITLE 2 THERMAL STABILITY OF RECOMBINANT FERULOYL ESTERASE A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERULOYL ESTERASE A;
COMPND 3 SYNONYM: FERULOYL ESTERASE TYPE A, FAE-III,
COMPND 4 CINNAMOYL ESTERASE;
COMPND 5 CHAIN: A, B;
COMPND 6 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 22-281;
COMPND 7 EC: 3.1.1.73;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 3 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 4 EXPRESSION_SYSTEM_VECTOR: PDESTOI17;
SOURCE 5 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;
SOURCE 6 STRAIN: D15PYRG
KEYWDS XYLAN DEGRADATION, FERULOYL ESTERASE EC 3.1.1.73,
KEYWDS 2 HYDROLASE, GLYCOPROTEIN, SERINE ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.SULZENBACHER,I.BENOIT
REVDAT 2 25-OCT-06 2IX9 1 JRNL
REVDAT 1 18-OCT-06 2IX9 0
JRNL AUTH I.BENOIT,M.ASTHER,G.SULZENBACHER,E.RECORD,
JRNL AUTH 2 L.MARMUSE,G.PARSIEGLA,I.GIMBERT,M.ASTHER,C.BIGNON
JRNL TITL RESPECTIVE IMPORTANCE OF PROTEIN FOLDING AND
JRNL TITL 2 GLYCOSYLATION IN THE THERMAL STABILITY OF
JRNL TITL 3 RECOMBINANT FERULOYL ESTERASE A.
JRNL REF FEBS LETT. V. 580 5815 2006
JRNL REFN ASTM FEBLAL NE ISSN 0014-5793
REMARK 2
REMARK 2 RESOLUTION. 1.7 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 74.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.35
REMARK 3 NUMBER OF REFLECTIONS : 57868
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) : 0.15503
REMARK 3 R VALUE (WORKING SET) : 0.15317
REMARK 3 FREE R VALUE : 0.19022
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 3096
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) : 1.699
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.743
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3942
REMARK 3 BIN R VALUE (WORKING SET) : 0.204
REMARK 3 BIN FREE R VALUE SET COUNT : 208
REMARK 3 BIN FREE R VALUE : 0.266
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4067
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 70
REMARK 3 SOLVENT ATOMS : 525
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.42
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.831
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.49
REMARK 3 B22 (A**2) : -0.44
REMARK 3 B33 (A**2) : 0.96
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.04
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.091
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.094
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.062
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.707
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 4241 ; 0.013 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2698 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED (DEGREES): 5807 ; 1.383 ; 1.939
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6607 ; 0.918 ; 3.004
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 550 ; 6.035 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 210 ;35.763 ;25.714
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 619 ;12.271 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;10.586 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 638 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 4868 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 832 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED (A): 907 ; 0.215 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3015 ; 0.203 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED (A): 2178 ; 0.181 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2036 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED (A): 401 ; 0.140 ; 0.200
REMARK 3 SYMMETRY VDW REFINED (A): 5 ; 0.284 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 25 ; 0.266 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED (A): 26 ; 0.155 ; 0.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 3385 ; 1.681 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 4254 ; 2.038 ; 4.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 1892 ; 1.997 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 1537 ; 2.832 ; 4.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 260
REMARK 3 ORIGIN FOR THE GROUP (A): 9.1960 0.3350 21.9520
REMARK 3 T TENSOR
REMARK 3 T11: -0.0549 T22: -0.0403
REMARK 3 T33: -0.0448 T12: -0.0026
REMARK 3 T13: 0.0119 T23: 0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.6534 L22: 0.8816
REMARK 3 L33: 0.6423 L12: -0.0615
REMARK 3 L13: 0.0116 L23: 0.0907
REMARK 3 S TENSOR
REMARK 3 S11: -0.0019 S12: 0.0587 S13: 0.0331
REMARK 3 S21: -0.0335 S22: -0.0159 S23: -0.0550
REMARK 3 S31: -0.0117 S32: 0.0231 S33: 0.0178
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 260
REMARK 3 ORIGIN FOR THE GROUP (A): 2.4460 -20.3940 52.2990
REMARK 3 T TENSOR
REMARK 3 T11: -0.0362 T22: -0.0239
REMARK 3 T33: -0.0532 T12: 0.0075
REMARK 3 T13: 0.0061 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 1.0134 L22: 0.6926
REMARK 3 L33: 0.6844 L12: -0.1253
REMARK 3 L13: -0.0695 L23: -0.0868
REMARK 3 S TENSOR
REMARK 3 S11: -0.0066 S12: -0.1173 S13: -0.0531
REMARK 3 S21: 0.0618 S22: 0.0232 S23: 0.0067
REMARK 3 S31: 0.0219 S32: 0.0097 S33: -0.0166
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 :1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.B FACTORS CORRESPOND TO THE OVERALL
REMARK 3 B FACTORS EQUAL TO THE RESIDUAL PLUS THE TLS COMPONENT.
REMARK 4
REMARK 4 2IX9 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 7-JUL-2006.
REMARK 100 THE EBI ID CODE IS EBI-29180.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-APR-2006
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF BEAMLINE ID14-EH1
REMARK 200 BEAMLINE : ID14-EH1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60965
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.70
REMARK 200 RESOLUTION RANGE LOW (A) : 62.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 4.6
REMARK 200 R MERGE (I) : 0.09
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.80
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.9
REMARK 200 R MERGE FOR SHELL (I) : 0.45
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.30
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2HL6
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M AMMONIUM SULPHATE 0.2 M
REMARK 280 LITHIUM SULPHATE 0.1 M CAPS PH 9.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 1/2+X,1/2+Y,Z
REMARK 290 4555 1/2-X,1/2+Y,-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 79.41250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.77800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 79.41250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.77800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 M 1 A 1 .. 260 A 1 .. 260 0.359
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 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 350 BIOMOLECULE: 2
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 HOH Z 34 LIES ON A SPECIAL POSITION.
REMARK 375 HOH Z 82 LIES ON A SPECIAL POSITION.
REMARK 375 HOH Z 85 LIES ON A SPECIAL POSITION.
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 SER A 192 -116.58 42.89
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 525 B Y
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: DEPOSITOR PROVIDED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DEPOSITOR PROVIDED
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: CXS BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: CXS BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: EDO BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: EDO BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: EDO BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: EDO BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: EDO BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: EDO BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: EDO BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: EDO BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN B
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1USW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FERULIC ACID ESTERASE
REMARK 900 FROM ASPERGILLUS NIGER
REMARK 900 RELATED ID: 1UWC RELATED DB: PDB
REMARK 900 FERULOYL ESTERASE FROM ASPERGILLUS NIGER
REMARK 900 RELATED ID: 1UZA RELATED DB: PDB
REMARK 900 CRYSTALLOGRAPHIC STRUCTURE OF A FERULOYL
REMARK 900 ESTERASE FROM ASPERGILLUS NIGER
REMARK 900 RELATED ID: 2BJH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF S133A ANFAEA-FERULIC
REMARK 900 ACID COMPLEX
DBREF 2IX9 A 1 260 UNP O42807 FAEA_ASPNG 22 281
DBREF 2IX9 B 1 260 UNP O42807 FAEA_ASPNG 22 281
SEQADV 2IX9 GLU A 203 UNP O42807 ASP 224 CONFLICT
SEQADV 2IX9 GLN A 204 UNP O42807 GLU 225 CONFLICT
SEQADV 2IX9 GLU B 203 UNP O42807 ASP 224 CONFLICT
SEQADV 2IX9 GLN B 204 UNP O42807 GLU 225 CONFLICT
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 GLU GLN 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
SEQRES 1 B 260 ALA SER THR GLN GLY ILE SER GLU ASP LEU TYR ASN ARG
SEQRES 2 B 260 LEU VAL GLU MET ALA THR ILE SER GLN ALA ALA TYR ALA
SEQRES 3 B 260 ASP LEU CYS ASN ILE PRO SER THR ILE ILE LYS GLY GLU
SEQRES 4 B 260 LYS ILE TYR ASN ALA GLN THR ASP ILE ASN GLY TRP ILE
SEQRES 5 B 260 LEU ARG ASP ASP THR SER LYS GLU ILE ILE THR VAL PHE
SEQRES 6 B 260 ARG GLY THR GLY SER ASP THR ASN LEU GLN LEU ASP THR
SEQRES 7 B 260 ASN TYR THR LEU THR PRO PHE ASP THR LEU PRO GLN CYS
SEQRES 8 B 260 ASN ASP CYS GLU VAL HIS GLY GLY TYR TYR ILE GLY TRP
SEQRES 9 B 260 ILE SER VAL GLN ASP GLN VAL GLU SER LEU VAL LYS GLN
SEQRES 10 B 260 GLN ALA SER GLN TYR PRO ASP TYR ALA LEU THR VAL THR
SEQRES 11 B 260 GLY HIS SER LEU GLY ALA SER MET ALA ALA LEU THR ALA
SEQRES 12 B 260 ALA GLN LEU SER ALA THR TYR ASP ASN VAL ARG LEU TYR
SEQRES 13 B 260 THR PHE GLY GLU PRO ARG SER GLY ASN GLN ALA PHE ALA
SEQRES 14 B 260 SER TYR MET ASN ASP ALA PHE GLN VAL SER SER PRO GLU
SEQRES 15 B 260 THR THR GLN TYR PHE ARG VAL THR HIS SER ASN ASP GLY
SEQRES 16 B 260 ILE PRO ASN LEU PRO PRO ALA GLU GLN GLY TYR ALA HIS
SEQRES 17 B 260 GLY GLY VAL GLU TYR TRP SER VAL ASP PRO TYR SER ALA
SEQRES 18 B 260 GLN ASN THR PHE VAL CYS THR GLY ASP GLU VAL GLN CYS
SEQRES 19 B 260 CYS GLU ALA GLN GLY GLY GLN GLY VAL ASN ASP ALA HIS
SEQRES 20 B 260 THR THR TYR PHE GLY MET THR SER GLY ALA CYS THR TRP
HET CXS A1261 14
HET CXS B1261 14
HET EDO B1262 4
HET EDO A1262 4
HET EDO B1263 4
HET EDO A1263 4
HET EDO B1264 4
HET EDO A1264 4
HET EDO A1265 4
HET EDO A1266 4
HET SO4 A1267 5
HET SO4 B1265 5
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
HETNAM CXS 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID
HETNAM SO4 SULFATE ION
FORMUL 3 EDO 8(C2 H6 O2)
FORMUL 4 CXS 2(C9 H19 N1 O3 S1)
FORMUL 5 SO4 2(O4 S1 2-)
FORMUL 6 HOH *525(H2 O1)
HELIX 1 1 GLU A 8 TYR A 25 1 18
HELIX 2 2 SER A 70 THR A 78 1 9
HELIX 3 3 GLY A 98 TRP A 104 1 7
HELIX 4 4 GLN A 108 TYR A 122 1 15
HELIX 5 5 LEU A 134 THR A 149 1 16
HELIX 6 6 GLN A 166 PHE A 176 1 11
HELIX 7 7 ILE A 196 ASN A 198 5 3
HELIX 8 8 ALA A 202 GLN A 204 5 3
HELIX 9 9 CYS A 235 GLN A 238 5 4
HELIX 10 10 ASP A 245 THR A 248 1 4
HELIX 11 11 GLU B 8 TYR B 25 1 18
HELIX 12 12 SER B 70 THR B 78 1 9
HELIX 13 13 GLY B 98 TRP B 104 1 7
HELIX 14 14 GLN B 108 TYR B 122 1 15
HELIX 15 15 LEU B 134 THR B 149 1 16
HELIX 16 16 GLN B 166 PHE B 176 1 11
HELIX 17 17 ILE B 196 ASN B 198 5 3
HELIX 18 18 ALA B 202 GLN B 204 5 3
HELIX 19 19 CYS B 235 GLN B 238 5 4
HELIX 20 20 ASP B 245 THR B 248 1 4
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 36 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 BA 9 SER B 2 GLN B 4 0
SHEET 2 BA 9 THR B 224 CYS B 227 -1 O VAL B 226 N THR B 3
SHEET 3 BA 9 VAL B 211 SER B 215 -1 O GLU B 212 N CYS B 227
SHEET 4 BA 9 TYR B 186 HIS B 191 1 O TYR B 186 N VAL B 211
SHEET 5 BA 9 VAL B 153 PHE B 158 1 O LEU B 155 N PHE B 187
SHEET 6 BA 9 ALA B 126 HIS B 132 1 O LEU B 127 N ARG B 154
SHEET 7 BA 9 GLU B 60 PHE B 65 1 O ILE B 61 N THR B 128
SHEET 8 BA 9 ILE B 48 ASP B 55 -1 O TRP B 51 N VAL B 64
SHEET 9 BA 9 ILE B 35 ASN B 43 -1 O ILE B 36 N ARG B 54
SHEET 1 BB 2 LEU B 82 PRO B 84 0
SHEET 2 BB 2 GLU B 95 HIS B 97 -1 O VAL B 96 N THR B 83
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
SSBOND 4 CYS B 29 CYS B 258 1555 1555
SSBOND 5 CYS B 91 CYS B 94 1555 1555
SSBOND 6 CYS B 227 CYS B 234 1555 1555
CISPEP 1 LEU A 199 PRO A 200 0 -13.99
CISPEP 2 ASP A 217 PRO A 218 0 -3.99
CISPEP 3 LEU B 199 PRO B 200 0 -14.25
CISPEP 4 ASP B 217 PRO B 218 0 -5.25
SITE 1 AC1 11 TYR A 25 THR A 68 SER A 133 HIS A 247
SITE 2 AC1 11 SER A 255 GLY A 256 ASP B 71 HOH Z 273
SITE 3 AC1 11 HOH Z 274 HOH Z 275 HOH Z 276
SITE 1 AC2 9 ASP A 71 LEU A 74 TYR B 25 THR B 68
SITE 2 AC2 9 HIS B 247 SER B 255 GLY B 256 HOH Y 237
SITE 3 AC2 9 HOH Z 102
SITE 1 AC3 4 ASP B 77 TYR B 80 HIS B 97 TYR B 100
SITE 1 AC4 5 ASP A 77 TYR A 80 HIS A 97 TYR A 100
SITE 2 AC4 5 LEU A 199
SITE 1 AC5 8 GLU B 160 SER B 163 GLY B 164 PHE B 168
SITE 2 AC5 8 TYR B 186 ALA B 207 GLY B 209 HOH Y 239
SITE 1 AC6 10 GLU A 160 SER A 163 GLY A 164 PHE A 168
SITE 2 AC6 10 ALA A 169 MET A 172 TYR A 186 ALA A 207
SITE 3 AC6 10 GLY A 209 HOH Z 278
SITE 1 AC7 3 LEU B 74 ASP B 77 HOH Y 240
SITE 1 AC8 4 ASP A 77 TYR A 100 SER A 133 HOH Z 279
SITE 1 AC9 7 THR A 248 THR A 254 SER A 255 GLN B 45
SITE 2 AC9 7 ASP B 71 HOH Z 268 HOH Z 280
SITE 1 BC1 4 SER A 7 GLU A 8 ASP A 9 HOH Z 281
SITE 1 BC2 5 ARG A 162 ALA A 207 HIS A 208 HOH Z 283
SITE 2 BC2 5 HOH Z 284
SITE 1 BC3 4 ARG B 162 ALA B 207 HIS B 208 HOH Y 241
CRYST1 158.825 51.556 72.553 90.00 109.27 90.00 C 1 2 1 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 0.006296 0.000000 0.002201 0.00000
SCALE2 0.000000 0.019396 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014601 0.00000
MTRIX1 1 -0.250290 0.707530 0.660870 -9.98216 1
MTRIX2 1 0.713840 -0.326270 0.619660 -40.47337 1
MTRIX3 1 0.654060 0.626850 -0.423400 55.38137 1
TER 2019 TRP A 260
TER 4069 TRP B 260
MASTER 353 0 12 20 22 0 22 9 4662 2 82 40
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