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HEADER HYDROLASE 20-AUG-01 1JT2
TITLE STRUCTURAL BASIS FOR THE SUBSTRATE SPECIFICITY OF THE FERUL
TITLE 2 DOMAIN OF THE CELLULOSOMAL XYLANASE Z FROM C. THERMOCELLUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-1,4-BETA-XYLANASE Z;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 20-287;
COMPND 5 SYNONYM: FERULOYL ESTERASE, XYLANASE Z, 1,4-BETA-D-XYLAN
COMPND 6 XYLANOHYDROLASE Z;
COMPND 7 EC: 3.2.1.8;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM THERMOCELLUM;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: XYNZ;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21B
KEYWDS FERULOYL ESTERASE, FERULIC ACID ESTERASE, FAE_XYNZ, XYNZ,
KEYWDS 2 FERULOYL ESTERASE SUBSTRATE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR F.D.SCHUBOT,I.A.KATAEVA,D.L.BLUM,A.K.SHAH,L.G.LJUNGDAHL,
AUTHOR 2 J.P.ROSE,B.-C.WANG
REVDAT 1 27-MAR-02 1JT2 0
JRNL AUTH F.D.SCHUBOT,I.A.KATAEVA,D.L.BLUM,A.K.SHAH,
JRNL AUTH 2 L.G.LJUNGDAHL,J.P.ROSE,B.-C.WANG
JRNL TITL STRUCTURAL BASIS FOR THE SUBSTRATE SPECIFICITY OF
JRNL TITL 2 THE FERULOYL ESTERASE DOMAIN OF THE CELLULOSOMAL
JRNL TITL 3 XYLANASE Z OF CLOSTRIDIUM THERMOCELLUM
JRNL REF BIOCHEMISTRY V. 40 12524 2001
JRNL REFN ASTM BICHAW US ISSN 0006-2960
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.3
REMARK 3 NUMBER OF REFLECTIONS : 24752
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) : 0.187
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1193
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.86
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 39.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1743
REMARK 3 BIN R VALUE (WORKING SET) : 0.2620
REMARK 3 BIN FREE R VALUE : 0.2770
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 83
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.029
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1967
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 309
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.83000
REMARK 3 B22 (A**2) : 0.83000
REMARK 3 B33 (A**2) : -1.67000
REMARK 3 B12 (A**2) : 0.67000
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) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.15
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) : 0.23
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.16
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.96
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) : 1.140 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.680 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.970 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.830 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 49.87
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JT2 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-AUG-2001.
REMARK 100 THE RCSB ID CODE IS RCSB014150.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAY-2001
REMARK 200 TEMPERATURE (KELVIN) : 93.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : RIGAKU/MSC BLUE CONFOCAL
REMARK 200 OPTICS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24752
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.29700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1JJF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEGMME2000, AMMONIUM SULFATE,
REMARK 280 SODIUM ACETATE, GLYCEROL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,1/3+Z
REMARK 290 3555 -X+Y,-X,2/3+Z
REMARK 290 4555 -X,-Y,1/2+Z
REMARK 290 5555 Y,-X+Y,5/6+Z
REMARK 290 6555 X-Y,X,1/6+Z
REMARK 290 7555 Y,X,1/3-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,2/3-Z
REMARK 290 10555 -Y,-X,5/6-Z
REMARK 290 11555 -X+Y,Y,1/2-Z
REMARK 290 12555 X,X-Y,1/6-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.27267
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 148.54533
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 111.40900
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 185.68167
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 37.13633
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 74.27267
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 148.54533
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 185.68167
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 111.40900
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 37.13633
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
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 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 LEU A 20
REMARK 465 VAL A 21
REMARK 465 THR A 22
REMARK 465 ILE A 23
REMARK 465 SER A 24
REMARK 465 SER A 25
REMARK 465 THR A 26
REMARK 465 SER A 27
REMARK 465 ALA A 28
REMARK 465 ALA A 29
REMARK 465 GLY A 285
REMARK 465 ASN A 286
REMARK 465 THR A 287
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO A 66 CD PRO A 66 CG 0.032
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 71 N - CA - C ANGL. DEV. = -7.3 DEGREES
REMARK 500 ASN A 126 N - CA - C ANGL. DEV. =-10.5 DEGREES
REMARK 500 THR A 127 N - CA - C ANGL. DEV. = 7.8 DEGREES
REMARK 500 ASN A 147 N - CA - C ANGL. DEV. = 7.2 DEGREES
REMARK 500 TYR A 160 N - CA - C ANGL. DEV. = -7.6 DEGREES
REMARK 500 LYS A 218 N - CA - C ANGL. DEV. = 7.8 DEGREES
REMARK 500 LEU A 222 N - CA - C ANGL. DEV. =-11.1 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 ALA A 172 -115.54 50.39
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JJF RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR THE SUBSTRATE SPECIFICITY OF THE FERUL
REMARK 900 DOMAIN OF THE CELLULOSOMAL XYLANASE Z OF C. THERMOCELLUM
DBREF 1JT2 A 20 287 SWS P10478 XYNZ_CLOTM 20 287
SEQADV 1JT2 ALA A 172 SWS P10478 SER 172 ENGINEERED
SEQRES 1 A 268 LEU VAL THR ILE SER SER THR SER ALA ALA SER LEU PRO
SEQRES 2 A 268 THR MET PRO PRO SER GLY TYR ASP GLN VAL ARG ASN GLY
SEQRES 3 A 268 VAL PRO ARG GLY GLN VAL VAL ASN ILE SER TYR PHE SER
SEQRES 4 A 268 THR ALA THR ASN SER THR ARG PRO ALA ARG VAL TYR LEU
SEQRES 5 A 268 PRO PRO GLY TYR SER LYS ASP LYS LYS TYR SER VAL LEU
SEQRES 6 A 268 TYR LEU LEU HIS GLY ILE GLY GLY SER GLU ASN ASP TRP
SEQRES 7 A 268 PHE GLU GLY GLY GLY ARG ALA ASN VAL ILE ALA ASP ASN
SEQRES 8 A 268 LEU ILE ALA GLU GLY LYS ILE LYS PRO LEU ILE ILE VAL
SEQRES 9 A 268 THR PRO ASN THR ASN ALA ALA GLY PRO GLY ILE ALA ASP
SEQRES 10 A 268 GLY TYR GLU ASN PHE THR LYS ASP LEU LEU ASN SER LEU
SEQRES 11 A 268 ILE PRO TYR ILE GLU SER ASN TYR SER VAL TYR THR ASP
SEQRES 12 A 268 ARG GLU HIS ARG ALA ILE ALA GLY LEU ALA MET GLY GLY
SEQRES 13 A 268 GLY GLN SER PHE ASN ILE GLY LEU THR ASN LEU ASP LYS
SEQRES 14 A 268 PHE ALA TYR ILE GLY PRO ILE SER ALA ALA PRO ASN THR
SEQRES 15 A 268 TYR PRO ASN GLU ARG LEU PHE PRO ASP GLY GLY LYS ALA
SEQRES 16 A 268 ALA ARG GLU LYS LEU LYS LEU LEU PHE ILE ALA CYS GLY
SEQRES 17 A 268 THR ASN ASP SER LEU ILE GLY PHE GLY GLN ARG VAL HIS
SEQRES 18 A 268 GLU TYR CYS VAL ALA ASN ASN ILE ASN HIS VAL TYR TRP
SEQRES 19 A 268 LEU ILE GLN GLY GLY GLY HIS ASP PHE ASN VAL TRP LYS
SEQRES 20 A 268 PRO GLY LEU TRP ASN PHE LEU GLN MET ALA ASP GLU ALA
SEQRES 21 A 268 GLY LEU THR ARG ASP GLY ASN THR
HET FER 388 14
HETNAM FER 3-(4-HYDROXY-3-METHOXYPHENYL)-2-PROPENOIC ACID
HETSYN FER FERULIC ACID
FORMUL 2 FER C10 H10 O4
FORMUL 3 HOH *309(H2 O1)
HELIX 1 1 ARG A 103 GLU A 114 1 12
HELIX 2 2 ASP A 136 SER A 148 1 13
HELIX 3 3 SER A 148 TYR A 157 1 10
HELIX 4 4 ASP A 162 GLU A 164 5 3
HELIX 5 5 ALA A 172 THR A 184 1 13
HELIX 6 6 PRO A 203 PHE A 208 1 6
HELIX 7 7 GLY A 212 LEU A 219 1 8
HELIX 8 8 LEU A 232 ASN A 246 1 15
HELIX 9 9 ASP A 261 ALA A 279 1 19
SHEET 1 A 8 GLN A 50 SER A 58 0
SHEET 2 A 8 SER A 63 LEU A 71 -1 O LEU A 71 N GLN A 50
SHEET 3 A 8 ILE A 121 PRO A 125 -1 O ILE A 122 N TYR A 70
SHEET 4 A 8 VAL A 83 LEU A 87 1 N LEU A 84 O VAL A 123
SHEET 5 A 8 ARG A 166 LEU A 171 1 O ALA A 169 N LEU A 87
SHEET 6 A 8 TYR A 191 ILE A 195 1 O ILE A 195 N GLY A 170
SHEET 7 A 8 LEU A 221 GLY A 227 1 O PHE A 223 N ILE A 192
SHEET 8 A 8 VAL A 251 ILE A 255 1 O VAL A 251 N ILE A 224
CISPEP 1 LEU A 31 PRO A 32 0 -0.19
CRYST1 64.539 64.539 222.818 90.00 90.00 120.00 P 61 2 2 12
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 0.015495 0.008946 0.000000 0.00000
SCALE2 0.000000 0.017892 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004488 0.00000
TER 1968 ASP A 284
MASTER 315 0 1 9 8 0 0 6 2290 1 14 21
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