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HEADER HYDROLASE 03-APR-19 6JR9
TITLE ZHD/W183F COMPLEX WITH ZEN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZEARALENONE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLONOSTACHYS ROSEA;
SOURCE 3 ORGANISM_TAXID: 29856;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LACTONASE, HYDROLASE, ALPHA-BETA FOLD, ZEARALENONE DEGRADE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.J.HU
REVDAT 1 08-APR-20 6JR9 0
JRNL AUTH X.J.HU,H.J.ZHOU,L.LI
JRNL TITL STRUCTURE OF ZHD COMPLEX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.72 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.72
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 78020
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) : 0.143
REMARK 3 R VALUE (WORKING SET) : 0.141
REMARK 3 FREE R VALUE : 0.164
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4228
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) : 1.72
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.76
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5694
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2280
REMARK 3 BIN FREE R VALUE SET COUNT : 294
REMARK 3 BIN FREE R VALUE : 0.2420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4110
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 480
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.82000
REMARK 3 B22 (A**2) : 0.63000
REMARK 3 B33 (A**2) : 0.20000
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): 0.072
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.072
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.044
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.372
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4563 ; 0.014 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4112 ; 0.003 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6249 ; 1.797 ; 1.654
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9591 ; 1.607 ; 1.583
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 587 ; 6.471 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 213 ;33.530 ;22.958
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 702 ;12.185 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;10.720 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 601 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5211 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 921 ; 0.003 ; 0.020
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): 2282 ; 1.404 ; 1.137
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2281 ; 1.399 ; 1.135
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2891 ; 2.026 ; 1.697
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2892 ; 2.027 ; 1.700
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2281 ; 2.931 ; 1.502
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2282 ; 2.932 ; 1.504
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3359 ; 4.236 ; 2.111
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 5299 ; 5.822 ;15.451
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 5240 ; 5.714 ;15.172
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 ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6JR9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-APR-19.
REMARK 100 THE DEPOSITION ID IS D_1300011617.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-APR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97916
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 82387
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.720
REMARK 200 RESOLUTION RANGE LOW (A) : 113.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.70
REMARK 200 R MERGE (I) : 0.21000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.72
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.63200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
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: 5C8Z
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM PHOSPHATE, IMIDAZOLE,
REMARK 280 POTASSIUM CHLORIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 37.33000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.76000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.08500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.76000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.33000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.08500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 VAL A 270
REMARK 465 ASP A 271
REMARK 465 LYS A 272
REMARK 465 LEU A 273
REMARK 465 ALA A 274
REMARK 465 ALA A 275
REMARK 465 ALA A 276
REMARK 465 LEU A 277
REMARK 465 GLU A 278
REMARK 465 HIS A 279
REMARK 465 HIS A 280
REMARK 465 HIS A 281
REMARK 465 HIS A 282
REMARK 465 HIS A 283
REMARK 465 HIS A 284
REMARK 465 VAL B 270
REMARK 465 ASP B 271
REMARK 465 LYS B 272
REMARK 465 LEU B 273
REMARK 465 ALA B 274
REMARK 465 ALA B 275
REMARK 465 ALA B 276
REMARK 465 LEU B 277
REMARK 465 GLU B 278
REMARK 465 HIS B 279
REMARK 465 HIS B 280
REMARK 465 HIS B 281
REMARK 465 HIS B 282
REMARK 465 HIS B 283
REMARK 465 HIS B 284
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),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 70 CD GLU A 70 OE1 0.072
REMARK 500
REMARK 500 REMARK: NULL
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 ASP A 31 -177.41 -66.49
REMARK 500 SER A 62 -120.33 47.57
REMARK 500 SER A 102 -125.81 68.70
REMARK 500 GLU A 126 70.32 48.54
REMARK 500 PRO A 196 43.64 -83.72
REMARK 500 MET A 241 -114.64 -131.09
REMARK 500 ASP B 31 -176.71 -69.24
REMARK 500 SER B 62 -125.41 45.61
REMARK 500 SER B 102 -124.74 66.53
REMARK 500 GLU B 126 71.73 50.47
REMARK 500 PRO B 196 36.10 -86.99
REMARK 500 MET B 241 -109.79 -128.56
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 ZER A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZER B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K B 304
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5C8Z RELATED DB: PDB
REMARK 900 SAME ENZYME
REMARK 900 RELATED ID: 6JQZ RELATED DB: PDB
REMARK 900 SAME ENZYME
REMARK 900 RELATED ID: 6JR2 RELATED DB: PDB
REMARK 900 SAME ENZYME
REMARK 900 RELATED ID: 6JR5 RELATED DB: PDB
REMARK 900 SAME ENZYME
DBREF 6JR9 A 1 284 PDB 6JR9 6JR9 1 284
DBREF 6JR9 B 1 284 PDB 6JR9 6JR9 1 284
SEQRES 1 A 284 MET ARG THR ARG SER THR ILE SER THR PRO ASN GLY ILE
SEQRES 2 A 284 THR TRP TYR TYR GLU GLN GLU GLY THR GLY PRO ASP ILE
SEQRES 3 A 284 VAL LEU VAL PRO ASP GLY LEU GLY GLU CYS GLN MET PHE
SEQRES 4 A 284 ASP SER SER VAL SER GLN ILE ALA ALA GLN GLY PHE ARG
SEQRES 5 A 284 VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER ALA
SEQRES 6 A 284 LYS ALA PRO ALA GLU THR TYR THR GLU VAL THR ALA GLN
SEQRES 7 A 284 LYS LEU ALA SER TYR VAL ILE SER ILE LEU ASP ALA LEU
SEQRES 8 A 284 ASP ILE LYS HIS ALA THR VAL TRP GLY CYS SER SER GLY
SEQRES 9 A 284 ALA SER THR VAL VAL ALA LEU LEU LEU GLY TYR PRO ASP
SEQRES 10 A 284 ARG ILE ARG ASN ALA MET CYS HIS GLU LEU PRO THR LYS
SEQRES 11 A 284 LEU LEU ASP HIS LEU SER ASN THR ALA VAL LEU GLU ASP
SEQRES 12 A 284 GLU GLU ILE SER ASN ILE LEU ALA ASN VAL MET LEU ASN
SEQRES 13 A 284 ASP VAL SER GLY GLY SER GLU ALA TRP GLN ALA LEU GLY
SEQRES 14 A 284 VAL GLU VAL HIS ALA ARG LEU HIS LYS ASN TYR PRO VAL
SEQRES 15 A 284 PHE ALA ARG GLY TYR PRO ARG THR ILE PRO PRO SER ALA
SEQRES 16 A 284 PRO VAL GLN ASP VAL GLU ALA LEU ARG GLY LYS PRO LEU
SEQRES 17 A 284 ASP TRP THR VAL GLY ALA ALA THR PRO THR GLU SER PHE
SEQRES 18 A 284 PHE ASP ASN ILE VAL THR ALA THR LYS ALA GLY VAL ASN
SEQRES 19 A 284 ILE GLY LEU LEU PRO GLY MET HIS PHE PRO TYR VAL SER
SEQRES 20 A 284 HIS PRO ASP VAL PHE ALA LYS TYR VAL VAL GLU THR THR
SEQRES 21 A 284 GLN LYS HIS LEU TRP ASN SER SER SER VAL ASP LYS LEU
SEQRES 22 A 284 ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 284 MET ARG THR ARG SER THR ILE SER THR PRO ASN GLY ILE
SEQRES 2 B 284 THR TRP TYR TYR GLU GLN GLU GLY THR GLY PRO ASP ILE
SEQRES 3 B 284 VAL LEU VAL PRO ASP GLY LEU GLY GLU CYS GLN MET PHE
SEQRES 4 B 284 ASP SER SER VAL SER GLN ILE ALA ALA GLN GLY PHE ARG
SEQRES 5 B 284 VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER ALA
SEQRES 6 B 284 LYS ALA PRO ALA GLU THR TYR THR GLU VAL THR ALA GLN
SEQRES 7 B 284 LYS LEU ALA SER TYR VAL ILE SER ILE LEU ASP ALA LEU
SEQRES 8 B 284 ASP ILE LYS HIS ALA THR VAL TRP GLY CYS SER SER GLY
SEQRES 9 B 284 ALA SER THR VAL VAL ALA LEU LEU LEU GLY TYR PRO ASP
SEQRES 10 B 284 ARG ILE ARG ASN ALA MET CYS HIS GLU LEU PRO THR LYS
SEQRES 11 B 284 LEU LEU ASP HIS LEU SER ASN THR ALA VAL LEU GLU ASP
SEQRES 12 B 284 GLU GLU ILE SER ASN ILE LEU ALA ASN VAL MET LEU ASN
SEQRES 13 B 284 ASP VAL SER GLY GLY SER GLU ALA TRP GLN ALA LEU GLY
SEQRES 14 B 284 VAL GLU VAL HIS ALA ARG LEU HIS LYS ASN TYR PRO VAL
SEQRES 15 B 284 PHE ALA ARG GLY TYR PRO ARG THR ILE PRO PRO SER ALA
SEQRES 16 B 284 PRO VAL GLN ASP VAL GLU ALA LEU ARG GLY LYS PRO LEU
SEQRES 17 B 284 ASP TRP THR VAL GLY ALA ALA THR PRO THR GLU SER PHE
SEQRES 18 B 284 PHE ASP ASN ILE VAL THR ALA THR LYS ALA GLY VAL ASN
SEQRES 19 B 284 ILE GLY LEU LEU PRO GLY MET HIS PHE PRO TYR VAL SER
SEQRES 20 B 284 HIS PRO ASP VAL PHE ALA LYS TYR VAL VAL GLU THR THR
SEQRES 21 B 284 GLN LYS HIS LEU TRP ASN SER SER SER VAL ASP LYS LEU
SEQRES 22 B 284 ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
HET ZER A 301 23
HET GOL A 302 6
HET GOL A 303 6
HET GOL A 304 6
HET GOL A 305 6
HET GOL A 306 6
HET GOL A 307 6
HET K A 308 1
HET ZER B 301 23
HET GOL B 302 6
HET GOL B 303 6
HET K B 304 1
HETNAM ZER (3S,11E)-14,16-DIHYDROXY-3-METHYL-3,4,5,6,9,10-
HETNAM 2 ZER HEXAHYDRO-1H-2-BENZOXACYCLOTETRADECINE-1,7(8H)-DIONE
HETNAM GOL GLYCEROL
HETNAM K POTASSIUM ION
HETSYN ZER ZEARALENONE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 ZER 2(C18 H22 O5)
FORMUL 4 GOL 8(C3 H8 O3)
FORMUL 10 K 2(K 1+)
FORMUL 15 HOH *480(H2 O)
HELIX 1 AA1 GLU A 35 MET A 38 5 4
HELIX 2 AA2 PHE A 39 ALA A 48 1 10
HELIX 3 AA3 MET A 61 ALA A 65 5 5
HELIX 4 AA4 PRO A 68 THR A 73 5 6
HELIX 5 AA5 THR A 76 LEU A 91 1 16
HELIX 6 AA6 SER A 102 TYR A 115 1 14
HELIX 7 AA7 LEU A 132 ASN A 137 1 6
HELIX 8 AA8 THR A 138 LEU A 141 5 4
HELIX 9 AA9 GLU A 142 ASP A 157 1 16
HELIX 10 AB1 GLY A 161 ALA A 167 1 7
HELIX 11 AB2 GLY A 169 TYR A 187 1 19
HELIX 12 AB3 ILE A 191 ALA A 195 5 5
HELIX 13 AB4 ASP A 199 ARG A 204 1 6
HELIX 14 AB5 PHE A 221 GLY A 232 1 12
HELIX 15 AB6 PHE A 243 HIS A 248 1 6
HELIX 16 AB7 HIS A 248 SER A 269 1 22
HELIX 17 AB8 GLU B 35 MET B 38 5 4
HELIX 18 AB9 PHE B 39 ALA B 48 1 10
HELIX 19 AC1 MET B 61 ALA B 65 5 5
HELIX 20 AC2 PRO B 68 TYR B 72 5 5
HELIX 21 AC3 THR B 76 LEU B 91 1 16
HELIX 22 AC4 SER B 102 TYR B 115 1 14
HELIX 23 AC5 LEU B 132 ASN B 137 1 6
HELIX 24 AC6 THR B 138 LEU B 141 5 4
HELIX 25 AC7 GLU B 142 VAL B 158 1 17
HELIX 26 AC8 GLY B 161 ALA B 167 1 7
HELIX 27 AC9 GLY B 169 TYR B 187 1 19
HELIX 28 AD1 ILE B 191 ALA B 195 5 5
HELIX 29 AD2 ASP B 199 ARG B 204 1 6
HELIX 30 AD3 PRO B 217 GLY B 232 1 16
HELIX 31 AD4 PHE B 243 HIS B 248 1 6
HELIX 32 AD5 HIS B 248 SER B 269 1 22
SHEET 1 AA1 8 THR A 3 SER A 8 0
SHEET 2 AA1 8 THR A 14 GLU A 20 -1 O TRP A 15 N ILE A 7
SHEET 3 AA1 8 ARG A 52 PHE A 56 -1 O VAL A 53 N GLU A 20
SHEET 4 AA1 8 ASP A 25 VAL A 29 1 N ILE A 26 O ARG A 52
SHEET 5 AA1 8 ALA A 96 CYS A 101 1 O THR A 97 N VAL A 27
SHEET 6 AA1 8 ILE A 119 HIS A 125 1 O MET A 123 N VAL A 98
SHEET 7 AA1 8 LEU A 208 GLY A 213 1 O ASP A 209 N ALA A 122
SHEET 8 AA1 8 ASN A 234 LEU A 238 1 O ASN A 234 N TRP A 210
SHEET 1 AA2 8 ARG B 2 SER B 8 0
SHEET 2 AA2 8 THR B 14 GLU B 20 -1 O TRP B 15 N ILE B 7
SHEET 3 AA2 8 ARG B 52 PHE B 56 -1 O VAL B 53 N GLU B 20
SHEET 4 AA2 8 ASP B 25 VAL B 29 1 N LEU B 28 O THR B 54
SHEET 5 AA2 8 ALA B 96 CYS B 101 1 O TRP B 99 N VAL B 29
SHEET 6 AA2 8 ILE B 119 HIS B 125 1 O MET B 123 N VAL B 98
SHEET 7 AA2 8 LEU B 208 GLY B 213 1 O THR B 211 N CYS B 124
SHEET 8 AA2 8 ASN B 234 LEU B 238 1 O ASN B 234 N TRP B 210
SITE 1 AC1 11 GLY A 32 LEU A 33 SER A 102 SER A 103
SITE 2 AC1 11 MET A 154 PHE A 183 TYR A 187 PRO A 188
SITE 3 AC1 11 PRO A 192 HIS A 242 HOH A 403
SITE 1 AC2 6 GLN A 19 ARG A 52 LEU A 91 HOH A 416
SITE 2 AC2 6 SER B 162 GLU B 163
SITE 1 AC3 7 LEU A 155 ASN A 156 ASP A 157 VAL A 158
SITE 2 AC3 7 SER A 159 GLY A 160 MET A 241
SITE 1 AC4 10 GLN A 78 PRO A 193 SER A 194 ALA A 195
SITE 2 AC4 10 GLN A 198 HOH A 408 HOH A 420 HOH A 456
SITE 3 AC4 10 HOH A 530 ARG B 189
SITE 1 AC5 7 THR A 6 ARG A 63 LYS A 66 HOH A 468
SITE 2 AC5 7 HOH A 501 HOH A 545 HOH A 598
SITE 1 AC6 6 LEU A 127 PRO A 128 THR A 129 LYS A 130
SITE 2 AC6 6 SER A 220 ASP A 223
SITE 1 AC7 6 GLY A 236 LEU A 237 HOH A 417 HOH A 423
SITE 2 AC7 6 LYS B 130 PHE B 222
SITE 1 AC8 4 HIS A 248 PRO A 249 ASP A 250 VAL A 251
SITE 1 AC9 10 ASP B 31 GLY B 32 SER B 102 SER B 103
SITE 2 AC9 10 MET B 154 PHE B 183 TYR B 187 PRO B 192
SITE 3 AC9 10 HIS B 242 HOH B 401
SITE 1 AD1 6 LYS A 79 HOH A 458 GLU B 70 GLU B 74
SITE 2 AD1 6 LYS B 79 HOH B 442
SITE 1 AD2 9 LEU B 155 ASN B 156 ASP B 157 VAL B 158
SITE 2 AD2 9 SER B 159 GLY B 160 MET B 241 HOH B 459
SITE 3 AD2 9 HOH B 554
SITE 1 AD3 4 HIS B 248 PRO B 249 ASP B 250 VAL B 251
CRYST1 74.660 90.170 113.520 90.00 90.00 90.00 P 21 21 21 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 0.013394 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011090 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008809 0.00000
TER 2164 SER A 269
TER 4313 SER B 269
MASTER 384 0 12 32 16 0 26 6 4686 2 94 44
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