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HEADER HYDROLASE 02-FEB-05 2BJH
TITLE CRYSTAL STRUCTURE OF S133A ANFAEA-FERULIC ACID COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERULOYL ESTERASE A;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: FERULIC ACID ESTERASE A, FAE-III, CINNAMOYL
COMPND 5 ESTERASE;
COMPND 6 EC: 3.1.1.73;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;
SOURCE 3 ORGANISM_TAXID: 5061;
SOURCE 4 STRAIN: CBS 120.49/N400;
SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS DEGRADATION PLANT CELL WALLS, FERULOYL ESTERASE,
KEYWDS 2 GLYCOPROTEIN, HYDROLASE, SERINE ESTERASE, SIGNAL, XYLAN
KEYWDS 3 DEGRADATION
EXPDTA X-RAY DIFFRACTION
AUTHOR C.B.FAULDS,R.MOLINA,R.GONZALEZ,F.HUSBAND,N.JUGE,
AUTHOR 2 J.SANZ-APARICIO,J.A.HERMOSO
REVDAT 2 24-FEB-09 2BJH 1 VERSN
REVDAT 1 07-SEP-05 2BJH 0
JRNL AUTH C.B.FAULDS,R.MOLINA,R.GONZALEZ,F.HUSBAND,N.JUGE,
JRNL AUTH 2 J.SANZ-APARICIO,J.A.HERMOSO
JRNL TITL PROBING THE DETERMINANTS OF SUBSTRATE SPECIFICITY
JRNL TITL 2 OF A FERULOYL ESTERASE, ANFAEA, FROM ASPERGILLUS
JRNL TITL 3 NIGER
JRNL REF FEBS J. V. 272 4362 2005
JRNL REFN ISSN 1742-464X
JRNL PMID 16128806
JRNL DOI 10.1111/J.1742-4658.2005.04849.X
REMARK 2
REMARK 2 RESOLUTION. 2.54 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) : 2.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.49
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1573406.34
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 29512
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) : 0.216
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.6
REMARK 3 FREE R VALUE TEST SET COUNT : 1958
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) : 2.54
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.70
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.1
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4680
REMARK 3 BIN R VALUE (WORKING SET) : 0.270
REMARK 3 BIN FREE R VALUE : 0.319
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 248
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5973
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 132
REMARK 3 SOLVENT ATOMS : 373
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.5
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.1
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -10.66
REMARK 3 B22 (A**2) : 12.32
REMARK 3 B33 (A**2) : -1.67
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : -2.06
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.34
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) : 0.40
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.47
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.3
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.6
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.83
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 : 0.376446
REMARK 3 BSOL : 44.0691
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 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : FERULATE.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : FERULATE.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2BJH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-FEB-05.
REMARK 100 THE PDBE ID CODE IS EBI-22801.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-OCT-03
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
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) : 0.918381
REMARK 200 MONOCHROMATOR : DIAMOND
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47613
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 49.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.20000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.41
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.50000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1USW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.7 M AMMONIUM SULPHATE, 0.1 M
REMARK 280 HEPES, PH = 7.5, [FAXX]= 10 MM.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 65.37500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 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 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 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 350 BIOMOLECULE: 3
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: C
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 400
REMARK 400 ENGINEERED RESIDUE SER 154 ALA, CHAINS A, B AND C. RESIDUE
REMARK 400 133 IN THE COORDINATE RECORDS BELOW.
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 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 29 -108.38 -23.37
REMARK 500 ASN A 30 70.39 -108.82
REMARK 500 PRO A 32 146.98 -34.00
REMARK 500 ASP A 93 14.85 59.01
REMARK 500 ALA A 133 -130.21 60.11
REMARK 500 SER A 192 -124.76 38.14
REMARK 500 SER A 220 168.38 178.61
REMARK 500 ASN A 223 43.74 -101.07
REMARK 500 CYS A 234 -134.58 35.96
REMARK 500 ALA A 257 172.74 -48.71
REMARK 500 ALA B 26 -112.41 -93.01
REMARK 500 ASP B 27 40.72 -145.68
REMARK 500 LEU B 28 61.54 69.54
REMARK 500 ASN B 30 65.26 15.73
REMARK 500 ALA B 133 -115.54 58.38
REMARK 500 SER B 179 -38.49 -39.51
REMARK 500 SER B 192 -125.98 47.03
REMARK 500 VAL B 232 108.75 -53.69
REMARK 500 CYS B 234 -123.89 38.16
REMARK 500 VAL B 243 61.77 60.31
REMARK 500 ALA B 257 174.51 -44.59
REMARK 500 ASP C 27 45.88 76.62
REMARK 500 CYS C 29 -174.20 -48.75
REMARK 500 ASN C 30 82.72 -41.48
REMARK 500 SER C 33 -16.22 -46.82
REMARK 500 ASN C 43 119.57 -169.11
REMARK 500 GLN C 90 -18.34 -47.72
REMARK 500 ALA C 133 -128.67 66.59
REMARK 500 GLU C 182 27.60 -71.25
REMARK 500 THR C 183 -11.90 -151.10
REMARK 500 SER C 192 -117.33 51.43
REMARK 500 ASN C 223 36.59 -95.18
REMARK 500 GLN C 233 168.76 174.50
REMARK 500 CYS C 234 -127.87 52.20
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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG C 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FER A 908
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FER B 908
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FER C 908
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
DBREF 2BJH A 1 260 UNP O42807 FAEA_ASPNG 22 281
DBREF 2BJH B 1 260 UNP O42807 FAEA_ASPNG 22 281
DBREF 2BJH C 1 260 UNP O42807 FAEA_ASPNG 22 281
SEQADV 2BJH ALA A 133 UNP O42807 SER 154 ENGINEERED MUTATION
SEQADV 2BJH ALA B 133 UNP O42807 SER 154 ENGINEERED MUTATION
SEQADV 2BJH ALA C 133 UNP O42807 SER 154 ENGINEERED MUTATION
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 ALA 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 ASP GLU 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 ALA 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 ASP GLU 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
SEQRES 1 C 260 ALA SER THR GLN GLY ILE SER GLU ASP LEU TYR ASN ARG
SEQRES 2 C 260 LEU VAL GLU MET ALA THR ILE SER GLN ALA ALA TYR ALA
SEQRES 3 C 260 ASP LEU CYS ASN ILE PRO SER THR ILE ILE LYS GLY GLU
SEQRES 4 C 260 LYS ILE TYR ASN ALA GLN THR ASP ILE ASN GLY TRP ILE
SEQRES 5 C 260 LEU ARG ASP ASP THR SER LYS GLU ILE ILE THR VAL PHE
SEQRES 6 C 260 ARG GLY THR GLY SER ASP THR ASN LEU GLN LEU ASP THR
SEQRES 7 C 260 ASN TYR THR LEU THR PRO PHE ASP THR LEU PRO GLN CYS
SEQRES 8 C 260 ASN ASP CYS GLU VAL HIS GLY GLY TYR TYR ILE GLY TRP
SEQRES 9 C 260 ILE SER VAL GLN ASP GLN VAL GLU SER LEU VAL LYS GLN
SEQRES 10 C 260 GLN ALA SER GLN TYR PRO ASP TYR ALA LEU THR VAL THR
SEQRES 11 C 260 GLY HIS ALA LEU GLY ALA SER MET ALA ALA LEU THR ALA
SEQRES 12 C 260 ALA GLN LEU SER ALA THR TYR ASP ASN VAL ARG LEU TYR
SEQRES 13 C 260 THR PHE GLY GLU PRO ARG SER GLY ASN GLN ALA PHE ALA
SEQRES 14 C 260 SER TYR MET ASN ASP ALA PHE GLN VAL SER SER PRO GLU
SEQRES 15 C 260 THR THR GLN TYR PHE ARG VAL THR HIS SER ASN ASP GLY
SEQRES 16 C 260 ILE PRO ASN LEU PRO PRO ALA ASP GLU GLY TYR ALA HIS
SEQRES 17 C 260 GLY GLY VAL GLU TYR TRP SER VAL ASP PRO TYR SER ALA
SEQRES 18 C 260 GLN ASN THR PHE VAL CYS THR GLY ASP GLU VAL GLN CYS
SEQRES 19 C 260 CYS GLU ALA GLN GLY GLY GLN GLY VAL ASN ASP ALA HIS
SEQRES 20 C 260 THR THR TYR PHE GLY MET THR SER GLY ALA CYS THR TRP
HET NAG A 900 15
HET NDG A 901 15
HET NAG B 900 15
HET NDG B 901 15
HET NAG C 900 15
HET NDG C 901 15
HET FER A 908 14
HET FER B 908 14
HET FER C 908 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM FER 3-(4-HYDROXY-3-METHOXYPHENYL)-2-PROPENOIC
HETNAM 2 FER ACID
HETSYN FER FERULIC ACID
HETSYN NAG NAG
FORMUL 4 NAG 3(C8 H15 N O6)
FORMUL 5 NDG 3(C8 H15 N O6)
FORMUL 10 FER 3(C10 H10 O4)
FORMUL 13 HOH *373(H2 O1)
HELIX 1 1 SER A 7 ALA A 24 1 18
HELIX 2 2 SER A 70 ASN A 79 1 10
HELIX 3 3 GLY A 98 SER A 120 1 23
HELIX 4 4 ALA A 133 ALA A 148 1 16
HELIX 5 5 GLN A 166 PHE A 176 1 11
HELIX 6 6 ILE A 196 LEU A 199 5 4
HELIX 7 7 PRO A 201 GLU A 204 5 4
HELIX 8 8 CYS A 234 GLN A 238 5 5
HELIX 9 9 ASN A 244 THR A 248 1 5
HELIX 10 10 SER B 7 ALA B 24 1 18
HELIX 11 11 SER B 70 THR B 78 1 9
HELIX 12 12 GLY B 98 SER B 120 1 23
HELIX 13 13 ALA B 133 ALA B 148 1 16
HELIX 14 14 ASN B 165 PHE B 176 1 12
HELIX 15 15 GLY B 195 LEU B 199 5 5
HELIX 16 16 PRO B 201 GLY B 205 5 5
HELIX 17 17 SER B 220 GLN B 222 5 3
HELIX 18 18 GLN B 233 GLN B 238 5 6
HELIX 19 19 ASN B 244 THR B 248 1 5
HELIX 20 20 SER C 7 ALA C 24 1 18
HELIX 21 21 TYR C 25 ASP C 27 5 3
HELIX 22 22 SER C 70 THR C 78 1 9
HELIX 23 23 GLY C 98 SER C 106 1 9
HELIX 24 24 VAL C 107 TYR C 122 1 16
HELIX 25 25 ALA C 133 TYR C 150 1 18
HELIX 26 26 ASN C 165 PHE C 176 1 12
HELIX 27 27 SER C 180 THR C 184 5 5
HELIX 28 28 GLY C 195 LEU C 199 5 5
HELIX 29 29 PRO C 201 GLY C 205 5 5
HELIX 30 30 GLN C 233 GLN C 238 1 6
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 GLY A 164 ASN A 165 0
SHEET 2 AC 2 TYR A 206 ALA A 207 -1 O ALA A 207 N GLY A 164
SHEET 1 AD 2 THR A 249 TYR A 250 0
SHEET 2 AD 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 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
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
SHEET 1 CA 9 SER C 2 GLN C 4 0
SHEET 2 CA 9 THR C 224 CYS C 227 -1 O VAL C 226 N THR C 3
SHEET 3 CA 9 VAL C 211 SER C 215 -1 O GLU C 212 N CYS C 227
SHEET 4 CA 9 TYR C 186 HIS C 191 1 O TYR C 186 N VAL C 211
SHEET 5 CA 9 VAL C 153 PHE C 158 1 O LEU C 155 N PHE C 187
SHEET 6 CA 9 ALA C 126 HIS C 132 1 O LEU C 127 N ARG C 154
SHEET 7 CA 9 GLU C 60 PHE C 65 1 O ILE C 61 N THR C 128
SHEET 8 CA 9 GLY C 50 ASP C 55 -1 O TRP C 51 N VAL C 64
SHEET 9 CA 9 ILE C 36 ILE C 41 -1 O ILE C 36 N ARG C 54
SHEET 1 CB 2 LEU C 82 PRO C 84 0
SHEET 2 CB 2 GLU C 95 HIS C 97 -1 O VAL C 96 N THR C 83
SHEET 1 CC 2 THR C 249 TYR C 250 0
SHEET 2 CC 2 MET C 253 THR C 254 -1 O MET C 253 N TYR C 250
SSBOND 1 CYS A 29 CYS A 258 1555 1555 2.02
SSBOND 2 CYS A 91 CYS A 94 1555 1555 2.03
SSBOND 3 CYS A 227 CYS A 234 1555 1555 2.03
SSBOND 4 CYS B 29 CYS B 258 1555 1555 2.02
SSBOND 5 CYS B 91 CYS B 94 1555 1555 2.03
SSBOND 6 CYS B 227 CYS B 234 1555 1555 2.03
SSBOND 7 CYS C 29 CYS C 258 1555 1555 2.03
SSBOND 8 CYS C 91 CYS C 94 1555 1555 2.03
SSBOND 9 CYS C 227 CYS C 234 1555 1555 2.03
CISPEP 1 LEU A 199 PRO A 200 0 -0.88
CISPEP 2 ASP A 217 PRO A 218 0 0.07
CISPEP 3 LEU B 199 PRO B 200 0 -0.60
CISPEP 4 ASP B 217 PRO B 218 0 -0.37
CISPEP 5 LEU C 199 PRO C 200 0 -0.48
CISPEP 6 ASP C 217 PRO C 218 0 0.01
SITE 1 AC1 8 ASP A 9 ASN A 79 THR A 83 GLY A 98
SITE 2 AC1 8 GLY A 99 NDG A 901 HOH A2152 HOH A2153
SITE 1 AC2 4 THR A 83 TYR A 101 NAG A 900 HOH A2155
SITE 1 AC3 6 GLU B 8 ASP B 9 ASN B 79 THR B 83
SITE 2 AC3 6 GLY B 98 NDG B 901
SITE 1 AC4 4 THR B 83 ILE B 105 NAG B 900 HOH B2135
SITE 1 AC5 6 ASN C 79 THR C 83 GLY C 98 TYR C 101
SITE 2 AC5 6 ILE C 102 NDG C 901
SITE 1 AC6 5 THR C 83 ILE C 105 NAG C 900 HOH C2076
SITE 2 AC6 5 HOH C2077
SITE 1 AC7 8 ASP A 77 TYR A 80 TYR A 100 ALA A 133
SITE 2 AC7 8 PRO A 161 VAL A 243 HIS A 247 HOH A2064
SITE 1 AC8 9 THR B 68 ASP B 77 TYR B 80 TYR B 100
SITE 2 AC8 9 ALA B 133 VAL B 243 HIS B 247 HOH B2138
SITE 3 AC8 9 HOH B2139
SITE 1 AC9 9 THR C 68 ASP C 77 TYR C 80 TYR C 100
SITE 2 AC9 9 ALA C 133 PRO C 161 ILE C 196 LEU C 199
SITE 3 AC9 9 HIS C 247
CRYST1 46.750 130.750 76.500 90.00 98.14 90.00 P 1 21 1 6
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 0.021390 0.000000 0.003060 0.00000
SCALE2 0.000000 0.007648 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013205 0.00000
MTRIX1 1 -0.999990 -0.001660 -0.003930 23.46257 1
MTRIX2 1 0.001720 -0.999890 -0.015020 94.88925 1
MTRIX3 1 -0.003900 -0.015030 0.999880 -0.39180 1
MTRIX1 2 0.431550 0.131120 0.892510 -23.78529 1
MTRIX2 2 -0.559360 0.815100 0.150720 62.56401 1
MTRIX3 2 -0.707730 -0.564280 0.425100 39.55011 1
TER 1992 TRP A 260
TER 3984 TRP B 260
TER 5976 TRP C 260
MASTER 345 0 9 30 41 0 18 12 6478 3 150 60
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