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HEADER HYDROLASE 03-FEB-04 1UWC
TITLE FERULOYL ESTERASE FROM ASPERGILLUS NIGER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERULOYL ESTERASE A;
COMPND 3 SYNONYM: FERULIC ACID ESTERASE A, FAE-III,
COMPND 4 CINNAMOYL ESTERASE;
COMPND 5 CHAIN: A, B;
COMPND 6 EC: 3.1.1.73;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: N-ACETYLGLUCOSAMINE AT ASN 79
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;
SOURCE 3 EXPRESSION_SYSTEM: ASPERGILLUS ORYZAE
KEYWDS HYDROLASE, SERINE ESTERASE, XYLAN DEGRADATION
EXPDTA X-RAY DIFFRACTION
AUTHOR K.E.MCAULEY,A.SVENDSEN,S.A.PATKAR,K.S.WILSON
REVDAT 1 06-MAY-04 1UWC 0
JRNL AUTH K.E.MCAULEY,A.SVENDSEN,S.A.PATKAR,K.S.WILSON
JRNL TITL STRUCTURE OF A FERULOYL ESTERASE FROM ASPERGILLUS
JRNL TITL 2 NIGER
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 60 878 2004
JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449
REMARK 2
REMARK 2 RESOLUTION. 1.08 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 74.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 93
REMARK 3 NUMBER OF REFLECTIONS : 161840
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) : 0.116
REMARK 3 R VALUE (WORKING SET) : 0.11511
REMARK 3 FREE R VALUE : 0.13802
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 8620
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.081
REMARK 3 BIN RESOLUTION RANGE LOW : 1.109
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9961
REMARK 3 BIN R VALUE (WORKING SET) : 0.199
REMARK 3 BIN FREE R VALUE SET COUNT : 517
REMARK 3 BIN FREE R VALUE : 0.219
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4114
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 80
REMARK 3 SOLVENT ATOMS : 713
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 7.2
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 9.012
REMARK 3 B11 (A**2) : 0.13
REMARK 3 B22 (A**2) : 0.63
REMARK 3 B33 (A**2) : -0.58
REMARK 3 B12 (A**2) : -0.36
REMARK 3 B13 (A**2) : 0.26
REMARK 3 B23 (A**2) : -0.09
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.026
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.027
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.017
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.778
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.984
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.979
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 4295 ; 0.019 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 3575 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED (DEGREES): 5878 ; 1.755 ; 1.936
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8357 ; 0.961 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 526 ; 6.719 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 637 ;10.751 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 655 ; 0.114 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 4845 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 840 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED (A): 789 ; 0.235 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3049 ; 0.187 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1663 ; 0.111 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED (A): 335 ; 0.187 ; 0.200
REMARK 3 SYMMETRY VDW REFINED (A): 20 ; 0.302 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 75 ; 0.211 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED (A): 66 ; 0.134 ; 0.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 3378 ; 1.658 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 4270 ; 2.056 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 1994 ; 2.790 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 1608 ; 3.609 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS A**2): 9659 ; 1.358 ; 3.000
REMARK 3 SPHERICITY; FREE (A**2): 713 ; 7.541 ; 3.000
REMARK 3 SPHERICITY; BONDED (A**2): 7768 ; 3.041 ; 3.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NONE
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NONE
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 1UWC COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 3-FEB-2004.
REMARK 100 THE EBI ID CODE IS EBI-14472.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS BEAMLINE PX9.6
REMARK 200 BEAMLINE : PX9.6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD QUANTUM-4
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 170583
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.08
REMARK 200 RESOLUTION RANGE LOW (A) : 25
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 200 DATA REDUNDANCY : 2.9
REMARK 200 R MERGE (I) : 0.058
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.8
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.08
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 82
REMARK 200 DATA REDUNDANCY IN SHELL : 1.8
REMARK 200 R MERGE FOR SHELL (I) : 0.26
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.5
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIRECT METHODS
REMARK 200 SOFTWARE USED: ACORN
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.8
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M AMMONIUM SULPHATE,
REMARK 280 0.1M NA ACETATE PH 4.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,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
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 SSS
REMARK 295 M 1 A 1 .. 261 B 1 .. 261 0.500
REMARK 295
REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS
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 400
REMARK 400 COMPOUND
REMARK 400 INVOLVED IN DEGRADATION OF PLANT CELL WALLS. HYDROLYZES
REMARK 400 THE FERULOYL-ARABINOSE ESTER BOND IN ARABINOXYLANS, AND THE
REMARK 400 FERULOYL-GALACTOSE ESTER BOND IN PECTIN. BINDS TO CELLULOSE.
REMARK 400 FERULOYL-POLYSACCHARIDE + H(2)O = FERULATE + POLYSACCHARIDE.
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 ASP B 9 CG OD1 OD2
REMARK 470 GLN B 177 CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500
REMARK 500 O HOH Z 19 O HOH Z 21 2.20
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500
REMARK 500 SER A 133 -118.66 60.50
REMARK 500 SER B 133 -119.50 60.73
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER B 2 THR B 3 143.85
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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: FER BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: NAG BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: FER BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: FER BINDING SITE FOR CHAIN A
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 999
REMARK 999 SEQUENCE
REMARK 999 THE CONFLICT DESCRIBED IN THE SEQADV RECORDS BELOW
REMARK 999 HAVE BEEN DESCRIBED IN UNIPROT ENTRY O42807 BY
REMARK 999 JUGE ET AL 2001
DBREF 1UWC A 1 260 UNP O42807 FAEA_ASPNG 22 281
DBREF 1UWC A 261 261 PDB 1UWC 1UWC 261 261
DBREF 1UWC B 1 260 UNP O42807 FAEA_ASPNG 22 281
DBREF 1UWC B 261 261 PDB 1UWC 1UWC 261 261
SEQADV 1UWC GLU A 203 UNP O42807 ASP 224 CONFLICT SEE REMARK 999
SEQADV 1UWC GLN A 204 UNP O42807 GLU 225 CONFLICT SEE REMARK 999
SEQADV 1UWC GLU B 203 UNP O42807 ASP 224 CONFLICT SEE REMARK 999
SEQADV 1UWC GLN B 204 UNP O42807 GLU 225 CONFLICT SEE REMARK 999
SEQRES 1 A 261 ALA SER THR GLN GLY ILE SER GLU ASP LEU TYR ASN ARG
SEQRES 2 A 261 LEU VAL GLU MET ALA THR ILE SER GLN ALA ALA TYR ALA
SEQRES 3 A 261 ASP LEU CYS ASN ILE PRO SER THR ILE ILE LYS GLY GLU
SEQRES 4 A 261 LYS ILE TYR ASN ALA GLN THR ASP ILE ASN GLY TRP ILE
SEQRES 5 A 261 LEU ARG ASP ASP THR SER LYS GLU ILE ILE THR VAL PHE
SEQRES 6 A 261 ARG GLY THR GLY SER ASP THR ASN LEU GLN LEU ASP THR
SEQRES 7 A 261 ASN TYR THR LEU THR PRO PHE ASP THR LEU PRO GLN CYS
SEQRES 8 A 261 ASN ASP CYS GLU VAL HIS GLY GLY TYR TYR ILE GLY TRP
SEQRES 9 A 261 ILE SER VAL GLN ASP GLN VAL GLU SER LEU VAL LYS GLN
SEQRES 10 A 261 GLN ALA SER GLN TYR PRO ASP TYR ALA LEU THR VAL THR
SEQRES 11 A 261 GLY HIS SER LEU GLY ALA SER MET ALA ALA LEU THR ALA
SEQRES 12 A 261 ALA GLN LEU SER ALA THR TYR ASP ASN VAL ARG LEU TYR
SEQRES 13 A 261 THR PHE GLY GLU PRO ARG SER GLY ASN GLN ALA PHE ALA
SEQRES 14 A 261 SER TYR MET ASN ASP ALA PHE GLN VAL SER SER PRO GLU
SEQRES 15 A 261 THR THR GLN TYR PHE ARG VAL THR HIS SER ASN ASP GLY
SEQRES 16 A 261 ILE PRO ASN LEU PRO PRO ALA GLU GLN GLY TYR ALA HIS
SEQRES 17 A 261 GLY GLY VAL GLU TYR TRP SER VAL ASP PRO TYR SER ALA
SEQRES 18 A 261 GLN ASN THR PHE VAL CYS THR GLY ASP GLU VAL GLN CYS
SEQRES 19 A 261 CYS GLU ALA GLN GLY GLY GLN GLY VAL ASN ASP ALA HIS
SEQRES 20 A 261 THR THR TYR PHE GLY MET THR SER GLY ALA CYS THR TRP
SEQRES 21 A 261 VAL
SEQRES 1 B 261 ALA SER THR GLN GLY ILE SER GLU ASP LEU TYR ASN ARG
SEQRES 2 B 261 LEU VAL GLU MET ALA THR ILE SER GLN ALA ALA TYR ALA
SEQRES 3 B 261 ASP LEU CYS ASN ILE PRO SER THR ILE ILE LYS GLY GLU
SEQRES 4 B 261 LYS ILE TYR ASN ALA GLN THR ASP ILE ASN GLY TRP ILE
SEQRES 5 B 261 LEU ARG ASP ASP THR SER LYS GLU ILE ILE THR VAL PHE
SEQRES 6 B 261 ARG GLY THR GLY SER ASP THR ASN LEU GLN LEU ASP THR
SEQRES 7 B 261 ASN TYR THR LEU THR PRO PHE ASP THR LEU PRO GLN CYS
SEQRES 8 B 261 ASN ASP CYS GLU VAL HIS GLY GLY TYR TYR ILE GLY TRP
SEQRES 9 B 261 ILE SER VAL GLN ASP GLN VAL GLU SER LEU VAL LYS GLN
SEQRES 10 B 261 GLN ALA SER GLN TYR PRO ASP TYR ALA LEU THR VAL THR
SEQRES 11 B 261 GLY HIS SER LEU GLY ALA SER MET ALA ALA LEU THR ALA
SEQRES 12 B 261 ALA GLN LEU SER ALA THR TYR ASP ASN VAL ARG LEU TYR
SEQRES 13 B 261 THR PHE GLY GLU PRO ARG SER GLY ASN GLN ALA PHE ALA
SEQRES 14 B 261 SER TYR MET ASN ASP ALA PHE GLN VAL SER SER PRO GLU
SEQRES 15 B 261 THR THR GLN TYR PHE ARG VAL THR HIS SER ASN ASP GLY
SEQRES 16 B 261 ILE PRO ASN LEU PRO PRO ALA GLU GLN GLY TYR ALA HIS
SEQRES 17 B 261 GLY GLY VAL GLU TYR TRP SER VAL ASP PRO TYR SER ALA
SEQRES 18 B 261 GLN ASN THR PHE VAL CYS THR GLY ASP GLU VAL GLN CYS
SEQRES 19 B 261 CYS GLU ALA GLN GLY GLY GLN GLY VAL ASN ASP ALA HIS
SEQRES 20 B 261 THR THR TYR PHE GLY MET THR SER GLY ALA CYS THR TRP
SEQRES 21 B 261 VAL
HET NAG A 262 14
HET FER A1262 14
HET NAG B 262 14
HET FER B1262 14
HET SO4 A1263 5
HET SO4 A1264 5
HET FER A1265 14
HETNAM SO4 SULFATE ION
HETNAM FER 3-(4-HYDROXY-3-METHOXYPHENYL)-2-PROPENOIC
HETNAM 2 FER ACID
HETSYN FER FERULIC ACID
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETSYN NAG NAG
FORMUL 3 NAG 2(C8 H15 N1 O6)
FORMUL 4 FER 3(C10 H10 O4)
FORMUL 5 SO4 2(O4 S1 2-)
FORMUL 6 HOH *713(H2 O1)
HELIX 1 1 SER A 7 ALA A 24 1 18
HELIX 2 2 SER A 70 THR A 78 1 9
HELIX 3 3 GLY A 98 TYR A 122 1 25
HELIX 4 4 SER A 133 ALA A 148 1 16
HELIX 5 5 ASN A 165 PHE A 176 1 12
HELIX 6 6 GLY A 195 LEU A 199 5 5
HELIX 7 7 PRO A 201 GLY A 205 5 5
HELIX 8 8 SER A 220 GLN A 222 5 3
HELIX 9 9 GLN A 233 GLY A 239 1 7
HELIX 10 10 ASN A 244 THR A 248 1 5
HELIX 11 11 SER B 7 ALA B 24 1 18
HELIX 12 12 TYR B 25 ASP B 27 5 3
HELIX 13 13 SER B 70 THR B 78 1 9
HELIX 14 14 GLY B 98 TYR B 122 1 25
HELIX 15 15 SER B 133 ALA B 148 1 16
HELIX 16 16 ASN B 165 PHE B 176 1 12
HELIX 17 17 GLY B 195 LEU B 199 5 5
HELIX 18 18 PRO B 201 GLY B 205 5 5
HELIX 19 19 GLN B 233 GLY B 239 5 7
HELIX 20 20 ASN B 244 THR B 248 1 5
SHEET 1 AA 9 SER A 2 GLN A 4 0
SHEET 2 AA 9 THR A 224 CYS A 227 -1 O VAL A 226 N THR A 3
SHEET 3 AA 9 VAL A 211 SER A 215 -1 O GLU A 212 N CYS A 227
SHEET 4 AA 9 TYR A 186 HIS A 191 1 O TYR A 186 N VAL A 211
SHEET 5 AA 9 VAL A 153 PHE A 158 1 O LEU A 155 N PHE A 187
SHEET 6 AA 9 ALA A 126 HIS A 132 1 O LEU A 127 N ARG A 154
SHEET 7 AA 9 GLU A 60 PHE A 65 1 O ILE A 61 N THR A 128
SHEET 8 AA 9 ILE A 48 ASP A 55 -1 O TRP A 51 N VAL A 64
SHEET 9 AA 9 ILE A 35 ASN A 43 -1 O ILE A 36 N ARG A 54
SHEET 1 AB 2 LEU A 82 PRO A 84 0
SHEET 2 AB 2 GLU A 95 HIS A 97 -1 O VAL A 96 N THR A 83
SHEET 1 AC 2 THR A 249 TYR A 250 0
SHEET 2 AC 2 MET A 253 THR A 254 -1 O MET A 253 N TYR A 250
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 36 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
SHEET 1 BC 2 THR B 249 TYR B 250 0
SHEET 2 BC 2 MET B 253 THR B 254 -1 O MET B 253 N TYR B 250
SSBOND 1 CYS A 29 CYS A 258 1555 1555
SSBOND 2 CYS A 91 CYS A 94 1555 1555
SSBOND 3 CYS A 227 CYS A 234 1555 1555
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
LINK ND2 ASN A 79 C1 NAG A 262 1555 1555
LINK ND2 ASN B 79 C1 NAG B 262 1555 1555
CISPEP 1 LEU A 199 PRO A 200 0 -15.84
CISPEP 2 ASP A 217 PRO A 218 0 -8.12
CISPEP 3 LEU B 199 PRO B 200 0 -15.65
CISPEP 4 ASP B 217 PRO B 218 0 -4.18
SITE 1 AC1 13 ASN A 79 THR A 83 GLY A 98 TYR A 101
SITE 2 AC1 13 ILE A 102 ASN B 43 ILE B 105 SER B 106
SITE 3 AC1 13 GLN B 108 ASP B 109 GLN B 110 HOH Z 146
SITE 4 AC1 13 HOH Z 336
SITE 1 AC2 10 THR A 68 ASP A 77 TYR A 80 TYR A 100
SITE 2 AC2 10 SER A 133 LEU A 134 HIS A 247 HOH Z 337
SITE 3 AC2 10 HOH Z 338 HOH Z 339
SITE 1 AC3 12 ASN A 43 ILE A 105 SER A 106 GLN A 108
SITE 2 AC3 12 ASP A 109 GLN A 110 ASN B 79 THR B 83
SITE 3 AC3 12 GLY B 98 ILE B 102 HOH Y 178 HOH Y 362
SITE 1 AC4 10 THR B 68 ASP B 77 TYR B 80 TYR B 100
SITE 2 AC4 10 SER B 133 LEU B 134 HIS B 247 HOH Y 363
SITE 3 AC4 10 HOH Y 364 HOH Y 365
SITE 1 AC5 8 ARG A 162 ALA A 207 HIS A 208 HOH Z 273
SITE 2 AC5 8 HOH Z 340 HOH Z 341 HOH Z 342 HOH Z 343
SITE 1 AC6 5 ASN A 193 ASN A 244 HOH Z 344 HOH Z 345
SITE 2 AC6 5 HOH Z 346
SITE 1 AC7 8 PRO A 218 ASN A 223 SER B 192 ASN B 193
SITE 2 AC7 8 TRP B 214 GLN B 238 HOH Y 330 HOH Z 348
CRYST1 38.759 40.182 77.953 74.96 78.63 71.10 P 1 2
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.025800 -0.008833 -0.003401 0.00000
SCALE2 0.000000 0.026305 -0.005676 0.00000
SCALE3 0.000000 0.000000 0.013386 0.00000
MTRIX1 1 0.376000 0.902000 0.213000 21.11000 1
MTRIX2 1 0.902000 -0.409000 0.138000 15.88000 1
MTRIX3 1 0.212000 0.141000 -0.967000 38.18000 1
MASTER 313 0 7 20 26 0 19 9 4907 2 94 42
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