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HEADER HYDROLASE 02-FEB-18 5Z97
TITLE CRYSTAL STRUCTURE OF A LACTONASE DOUBLE MUTANT IN COMPLEX WITH LIGAND
TITLE 2 N
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LACTONASE FOR PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 4-266;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHINOCLADIELLA MACKENZIEI CBS 650.93;
SOURCE 3 ORGANISM_TAXID: 1442369;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-46 EK/LIC
KEYWDS ALPHA/BETA-HYDROLASE, LACTONASE, ZEARALENONE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.Y.ZHENG,W.D.LIU,C.C.CHEN,R.T.GUO
REVDAT 1 02-MAY-18 5Z97 0
JRNL AUTH Y.Y.ZHENG,W.T.LIU,C.C.CHEN,X.Y.HU,W.D.LIU,T.P.KO,X.K.TANG,
JRNL AUTH 2 H.L.WEI,J.W.HUANG,R.T.GUO
JRNL TITL CRYSTAL STRUCTURE OF A MYCOESTROGEN-DETOXIFYING LACTONASE
JRNL TITL 2 FROM RHINOCLADIELLA MACKENZIEI: MOLECULAR INSIGHT INTO ZHD
JRNL TITL 3 SUBSTRATE SELECTIVITY
JRNL REF ACS CATALYSIS V. 8 4294 2018
JRNL REFN ESSN 2155-5435
JRNL DOI 10.1021/ACSCATAL.8B00464
REMARK 2
REMARK 2 RESOLUTION. 2.32 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
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) : 2.32
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 3 NUMBER OF REFLECTIONS : 47531
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) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2490
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) : 2.32
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.38
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3483
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.80
REMARK 3 BIN R VALUE (WORKING SET) : 0.2920
REMARK 3 BIN FREE R VALUE SET COUNT : 208
REMARK 3 BIN FREE R VALUE : 0.3360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8174
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 74
REMARK 3 SOLVENT ATOMS : 250
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.80000
REMARK 3 B22 (A**2) : 0.12000
REMARK 3 B33 (A**2) : 1.41000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.53000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.398
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.270
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.217
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.166
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.897
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8482 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 7660 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11586 ; 1.196 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): 17825 ; 0.725 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1046 ; 5.815 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 364 ;35.469 ;23.626
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1298 ;21.143 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 52 ;18.072 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1261 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9456 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1694 ; 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): 4196 ; 5.254 ; 4.822
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4195 ; 5.251 ; 4.821
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5238 ; 7.250 ; 7.214
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5239 ; 7.250 ; 7.216
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4286 ; 5.220 ; 4.990
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4287 ; 5.219 ; 4.991
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6349 ; 7.086 ; 7.395
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 39546 ;10.616 ;90.425
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 39545 ;10.615 ;90.421
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 5Z97 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1300006385.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-AUG-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL15A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50048
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.320
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.32
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.48600
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: 5IE4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE, 0.085M SODIUM
REMARK 280 CACODYLATE PH 6.5, 25-28%(W/V) POLYETHYLENE GLYCOL 8000, 15%(V/V)
REMARK 280 GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 55.26000
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
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: 1470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 1290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 D 265
REMARK 465 LYS D 266
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 O ALA D 160 N HIS D 243 2.13
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO D 172 C - N - CA ANGL. DEV. = 12.7 DEGREES
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 34 -178.41 -64.74
REMARK 500 SER A 65 -133.62 47.38
REMARK 500 ALA A 105 -129.79 63.34
REMARK 500 GLU A 129 75.25 60.73
REMARK 500 ASN A 163 92.16 -178.96
REMARK 500 ASN A 242 -106.10 -129.55
REMARK 500 SER B 65 -120.48 51.99
REMARK 500 ALA B 105 -120.28 62.02
REMARK 500 GLU B 129 70.68 56.76
REMARK 500 ASN B 163 92.60 -176.34
REMARK 500 ASN B 242 -119.40 -127.83
REMARK 500 ASP C 34 -175.54 -64.32
REMARK 500 SER C 65 -118.27 47.35
REMARK 500 ALA C 105 -123.24 63.96
REMARK 500 GLU C 129 71.93 41.80
REMARK 500 ASN C 163 90.77 -176.84
REMARK 500 ASN C 242 -106.07 -126.32
REMARK 500 GLU D 23 134.68 -178.23
REMARK 500 PRO D 33 -176.36 -64.30
REMARK 500 ASP D 34 -157.76 -94.53
REMARK 500 SER D 51 30.13 -81.55
REMARK 500 SER D 65 -120.05 52.11
REMARK 500 ASP D 95 78.65 58.88
REMARK 500 ALA D 105 -125.48 48.51
REMARK 500 GLU D 129 74.38 52.90
REMARK 500 SER D 150 -71.31 -45.02
REMARK 500 ASN D 163 -146.91 -168.39
REMARK 500 VAL D 164 -26.64 -157.81
REMARK 500 TYR D 189 -66.69 -109.15
REMARK 500 ASP D 203 1.69 -69.83
REMARK 500 ASN D 242 -111.29 -109.95
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 SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZER B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZER C 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5Z5J RELATED DB: PDB
REMARK 900 APO FORM
REMARK 900 RELATED ID: 5Z7J RELATED DB: PDB
REMARK 900 WITH LIGAND ZOL
DBREF1 5Z97 A 4 266 UNP A0A0D2ILK1_9EURO
DBREF2 5Z97 A A0A0D2ILK1 4 266
DBREF1 5Z97 B 4 266 UNP A0A0D2ILK1_9EURO
DBREF2 5Z97 B A0A0D2ILK1 4 266
DBREF1 5Z97 C 4 266 UNP A0A0D2ILK1_9EURO
DBREF2 5Z97 C A0A0D2ILK1 4 266
DBREF1 5Z97 D 4 266 UNP A0A0D2ILK1_9EURO
DBREF2 5Z97 D A0A0D2ILK1 4 266
SEQADV 5Z97 ALA A 105 UNP A0A0D2ILK SER 105 ENGINEERED MUTATION
SEQADV 5Z97 ALA A 160 UNP A0A0D2ILK TYR 160 ENGINEERED MUTATION
SEQADV 5Z97 ALA B 105 UNP A0A0D2ILK SER 105 ENGINEERED MUTATION
SEQADV 5Z97 ALA B 160 UNP A0A0D2ILK TYR 160 ENGINEERED MUTATION
SEQADV 5Z97 ALA C 105 UNP A0A0D2ILK SER 105 ENGINEERED MUTATION
SEQADV 5Z97 ALA C 160 UNP A0A0D2ILK TYR 160 ENGINEERED MUTATION
SEQADV 5Z97 ALA D 105 UNP A0A0D2ILK SER 105 ENGINEERED MUTATION
SEQADV 5Z97 ALA D 160 UNP A0A0D2ILK TYR 160 ENGINEERED MUTATION
SEQRES 1 A 263 THR ARG THR ARG GLY TYR VAL THR THR LYS ASP GLY ILE
SEQRES 2 A 263 LYS TRP TYR TYR GLU GLN GLU GLY SER GLY PRO ASP VAL
SEQRES 3 A 263 VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS GLN MET PHE
SEQRES 4 A 263 ASP LYS PRO MET SER LEU ILE ALA SER ASN GLY PHE ARG
SEQRES 5 A 263 VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER SER
SEQRES 6 A 263 ASP ALA PRO PRO GLU THR TYR GLN ASP ILE THR GLY ARG
SEQRES 7 A 263 LYS LEU ALA GLY TYR ILE ILE THR LEU LEU ASP THR LEU
SEQRES 8 A 263 ASP ILE LYS ILE ALA SER VAL TRP GLY CYS ALA SER GLY
SEQRES 9 A 263 ALA SER THR VAL LEU ALA LEU CYS SER ASP TYR PRO GLU
SEQRES 10 A 263 ARG VAL ARG ASN GLY MET PRO HIS GLU VAL PRO THR GLU
SEQRES 11 A 263 ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU VAL ASP PRO
SEQRES 12 A 263 ALA THR ILE SER GLN GLU MET ALA ALA ASN SER ARG ALA
SEQRES 13 A 263 ALA SER GLY ASN VAL GLU ALA TRP ASP ALA LEU GLY PRO
SEQRES 14 A 263 GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR PRO ARG TRP
SEQRES 15 A 263 ALA TYR GLY TYR PRO ARG THR ILE PRO PRO SER ALA PRO
SEQRES 16 A 263 VAL LYS THR GLU ASP LEU HIS LYS VAL PRO ILE ASP TRP
SEQRES 17 A 263 THR VAL GLY ALA SER THR PRO THR LYS LEU PHE PHE GLU
SEQRES 18 A 263 ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE ASN ILE GLY
SEQRES 19 A 263 THR LEU PRO GLY ASN HIS PHE PRO TYR VAL SER HIS PRO
SEQRES 20 A 263 GLU GLU PHE ALA LYS TYR VAL VAL GLU THR SER ARG LYS
SEQRES 21 A 263 TYR LEU LYS
SEQRES 1 B 263 THR ARG THR ARG GLY TYR VAL THR THR LYS ASP GLY ILE
SEQRES 2 B 263 LYS TRP TYR TYR GLU GLN GLU GLY SER GLY PRO ASP VAL
SEQRES 3 B 263 VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS GLN MET PHE
SEQRES 4 B 263 ASP LYS PRO MET SER LEU ILE ALA SER ASN GLY PHE ARG
SEQRES 5 B 263 VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER SER
SEQRES 6 B 263 ASP ALA PRO PRO GLU THR TYR GLN ASP ILE THR GLY ARG
SEQRES 7 B 263 LYS LEU ALA GLY TYR ILE ILE THR LEU LEU ASP THR LEU
SEQRES 8 B 263 ASP ILE LYS ILE ALA SER VAL TRP GLY CYS ALA SER GLY
SEQRES 9 B 263 ALA SER THR VAL LEU ALA LEU CYS SER ASP TYR PRO GLU
SEQRES 10 B 263 ARG VAL ARG ASN GLY MET PRO HIS GLU VAL PRO THR GLU
SEQRES 11 B 263 ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU VAL ASP PRO
SEQRES 12 B 263 ALA THR ILE SER GLN GLU MET ALA ALA ASN SER ARG ALA
SEQRES 13 B 263 ALA SER GLY ASN VAL GLU ALA TRP ASP ALA LEU GLY PRO
SEQRES 14 B 263 GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR PRO ARG TRP
SEQRES 15 B 263 ALA TYR GLY TYR PRO ARG THR ILE PRO PRO SER ALA PRO
SEQRES 16 B 263 VAL LYS THR GLU ASP LEU HIS LYS VAL PRO ILE ASP TRP
SEQRES 17 B 263 THR VAL GLY ALA SER THR PRO THR LYS LEU PHE PHE GLU
SEQRES 18 B 263 ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE ASN ILE GLY
SEQRES 19 B 263 THR LEU PRO GLY ASN HIS PHE PRO TYR VAL SER HIS PRO
SEQRES 20 B 263 GLU GLU PHE ALA LYS TYR VAL VAL GLU THR SER ARG LYS
SEQRES 21 B 263 TYR LEU LYS
SEQRES 1 C 263 THR ARG THR ARG GLY TYR VAL THR THR LYS ASP GLY ILE
SEQRES 2 C 263 LYS TRP TYR TYR GLU GLN GLU GLY SER GLY PRO ASP VAL
SEQRES 3 C 263 VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS GLN MET PHE
SEQRES 4 C 263 ASP LYS PRO MET SER LEU ILE ALA SER ASN GLY PHE ARG
SEQRES 5 C 263 VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER SER
SEQRES 6 C 263 ASP ALA PRO PRO GLU THR TYR GLN ASP ILE THR GLY ARG
SEQRES 7 C 263 LYS LEU ALA GLY TYR ILE ILE THR LEU LEU ASP THR LEU
SEQRES 8 C 263 ASP ILE LYS ILE ALA SER VAL TRP GLY CYS ALA SER GLY
SEQRES 9 C 263 ALA SER THR VAL LEU ALA LEU CYS SER ASP TYR PRO GLU
SEQRES 10 C 263 ARG VAL ARG ASN GLY MET PRO HIS GLU VAL PRO THR GLU
SEQRES 11 C 263 ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU VAL ASP PRO
SEQRES 12 C 263 ALA THR ILE SER GLN GLU MET ALA ALA ASN SER ARG ALA
SEQRES 13 C 263 ALA SER GLY ASN VAL GLU ALA TRP ASP ALA LEU GLY PRO
SEQRES 14 C 263 GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR PRO ARG TRP
SEQRES 15 C 263 ALA TYR GLY TYR PRO ARG THR ILE PRO PRO SER ALA PRO
SEQRES 16 C 263 VAL LYS THR GLU ASP LEU HIS LYS VAL PRO ILE ASP TRP
SEQRES 17 C 263 THR VAL GLY ALA SER THR PRO THR LYS LEU PHE PHE GLU
SEQRES 18 C 263 ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE ASN ILE GLY
SEQRES 19 C 263 THR LEU PRO GLY ASN HIS PHE PRO TYR VAL SER HIS PRO
SEQRES 20 C 263 GLU GLU PHE ALA LYS TYR VAL VAL GLU THR SER ARG LYS
SEQRES 21 C 263 TYR LEU LYS
SEQRES 1 D 263 THR ARG THR ARG GLY TYR VAL THR THR LYS ASP GLY ILE
SEQRES 2 D 263 LYS TRP TYR TYR GLU GLN GLU GLY SER GLY PRO ASP VAL
SEQRES 3 D 263 VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS GLN MET PHE
SEQRES 4 D 263 ASP LYS PRO MET SER LEU ILE ALA SER ASN GLY PHE ARG
SEQRES 5 D 263 VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER SER
SEQRES 6 D 263 ASP ALA PRO PRO GLU THR TYR GLN ASP ILE THR GLY ARG
SEQRES 7 D 263 LYS LEU ALA GLY TYR ILE ILE THR LEU LEU ASP THR LEU
SEQRES 8 D 263 ASP ILE LYS ILE ALA SER VAL TRP GLY CYS ALA SER GLY
SEQRES 9 D 263 ALA SER THR VAL LEU ALA LEU CYS SER ASP TYR PRO GLU
SEQRES 10 D 263 ARG VAL ARG ASN GLY MET PRO HIS GLU VAL PRO THR GLU
SEQRES 11 D 263 ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU VAL ASP PRO
SEQRES 12 D 263 ALA THR ILE SER GLN GLU MET ALA ALA ASN SER ARG ALA
SEQRES 13 D 263 ALA SER GLY ASN VAL GLU ALA TRP ASP ALA LEU GLY PRO
SEQRES 14 D 263 GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR PRO ARG TRP
SEQRES 15 D 263 ALA TYR GLY TYR PRO ARG THR ILE PRO PRO SER ALA PRO
SEQRES 16 D 263 VAL LYS THR GLU ASP LEU HIS LYS VAL PRO ILE ASP TRP
SEQRES 17 D 263 THR VAL GLY ALA SER THR PRO THR LYS LEU PHE PHE GLU
SEQRES 18 D 263 ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE ASN ILE GLY
SEQRES 19 D 263 THR LEU PRO GLY ASN HIS PHE PRO TYR VAL SER HIS PRO
SEQRES 20 D 263 GLU GLU PHE ALA LYS TYR VAL VAL GLU THR SER ARG LYS
SEQRES 21 D 263 TYR LEU LYS
HET ZER A 301 23
HET SO4 A 302 5
HET ZER B 301 23
HET ZER C 301 23
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 SO4 SULFATE ION
HETSYN ZER ZEARALENONE
FORMUL 5 ZER 3(C18 H22 O5)
FORMUL 6 SO4 O4 S 2-
FORMUL 9 HOH *250(H2 O)
HELIX 1 AA1 GLU A 38 MET A 41 5 4
HELIX 2 AA2 PHE A 42 SER A 51 1 10
HELIX 3 AA3 MET A 64 SER A 68 5 5
HELIX 4 AA4 PRO A 71 TYR A 75 5 5
HELIX 5 AA5 THR A 79 LEU A 94 1 16
HELIX 6 AA6 ALA A 105 TYR A 118 1 14
HELIX 7 AA7 PRO A 135 LEU A 139 5 5
HELIX 8 AA8 HIS A 140 VAL A 144 5 5
HELIX 9 AA9 ASP A 145 ALA A 160 1 16
HELIX 10 AB1 ASN A 163 ALA A 169 1 7
HELIX 11 AB2 GLY A 171 TYR A 189 1 19
HELIX 12 AB3 ILE A 193 ALA A 197 5 5
HELIX 13 AB4 LYS A 200 LEU A 204 5 5
HELIX 14 AB5 PRO A 218 LEU A 221 5 4
HELIX 15 AB6 PHE A 222 GLY A 233 1 12
HELIX 16 AB7 PHE A 244 HIS A 249 1 6
HELIX 17 AB8 HIS A 249 LYS A 263 1 15
HELIX 18 AB9 GLU B 38 MET B 41 5 4
HELIX 19 AC1 PHE B 42 SER B 51 1 10
HELIX 20 AC2 MET B 64 SER B 68 5 5
HELIX 21 AC3 PRO B 71 GLN B 76 5 6
HELIX 22 AC4 THR B 79 LEU B 94 1 16
HELIX 23 AC5 ALA B 105 TYR B 118 1 14
HELIX 24 AC6 PRO B 135 LEU B 139 5 5
HELIX 25 AC7 HIS B 140 VAL B 144 5 5
HELIX 26 AC8 ASP B 145 ALA B 160 1 16
HELIX 27 AC9 ASN B 163 ALA B 169 1 7
HELIX 28 AD1 GLY B 171 TYR B 189 1 19
HELIX 29 AD2 LYS B 200 LEU B 204 5 5
HELIX 30 AD3 PRO B 218 LEU B 221 5 4
HELIX 31 AD4 PHE B 222 GLY B 233 1 12
HELIX 32 AD5 PHE B 244 HIS B 249 1 6
HELIX 33 AD6 HIS B 249 LYS B 263 1 15
HELIX 34 AD7 GLU C 38 MET C 41 5 4
HELIX 35 AD8 PHE C 42 SER C 51 1 10
HELIX 36 AD9 MET C 64 SER C 68 5 5
HELIX 37 AE1 PRO C 71 GLN C 76 5 6
HELIX 38 AE2 THR C 79 LEU C 94 1 16
HELIX 39 AE3 ALA C 105 TYR C 118 1 14
HELIX 40 AE4 PRO C 135 LEU C 139 5 5
HELIX 41 AE5 ASP C 145 ALA C 160 1 16
HELIX 42 AE6 ASN C 163 LEU C 170 1 8
HELIX 43 AE7 GLY C 171 TYR C 189 1 19
HELIX 44 AE8 ILE C 193 ALA C 197 5 5
HELIX 45 AE9 PHE C 222 ALA C 230 1 9
HELIX 46 AF1 ARG C 231 GLY C 233 5 3
HELIX 47 AF2 PHE C 244 HIS C 249 1 6
HELIX 48 AF3 HIS C 249 LYS C 263 1 15
HELIX 49 AF4 GLU D 38 MET D 41 5 4
HELIX 50 AF5 PHE D 42 SER D 51 1 10
HELIX 51 AF6 MET D 64 SER D 68 5 5
HELIX 52 AF7 PRO D 71 GLN D 76 5 6
HELIX 53 AF8 THR D 79 ASP D 95 1 17
HELIX 54 AF9 ALA D 105 TYR D 118 1 14
HELIX 55 AG1 PRO D 135 LEU D 139 5 5
HELIX 56 AG2 ASP D 145 ALA D 160 1 16
HELIX 57 AG3 VAL D 164 ALA D 169 1 6
HELIX 58 AG4 LEU D 170 TYR D 189 1 20
HELIX 59 AG5 PHE D 222 GLY D 233 1 12
HELIX 60 AG6 PHE D 244 HIS D 249 1 6
HELIX 61 AG7 HIS D 249 LYS D 263 1 15
SHEET 1 AA1 6 THR A 6 THR A 11 0
SHEET 2 AA1 6 LYS A 17 GLY A 24 -1 O GLN A 22 N THR A 6
SHEET 3 AA1 6 ARG A 55 PHE A 59 -1 O VAL A 56 N GLU A 23
SHEET 4 AA1 6 ASP A 28 ILE A 32 1 N VAL A 29 O THR A 57
SHEET 5 AA1 6 ALA A 99 CYS A 104 1 O SER A 100 N ASP A 28
SHEET 6 AA1 6 VAL A 122 HIS A 128 1 O MET A 126 N VAL A 101
SHEET 1 AA2 2 ASP A 210 GLY A 214 0
SHEET 2 AA2 2 ASN A 235 LEU A 239 1 O ASN A 235 N TRP A 211
SHEET 1 AA3 6 ARG B 5 THR B 11 0
SHEET 2 AA3 6 LYS B 17 GLU B 23 -1 O GLN B 22 N THR B 6
SHEET 3 AA3 6 ARG B 55 PHE B 59 -1 O VAL B 56 N GLU B 23
SHEET 4 AA3 6 ASP B 28 ILE B 32 1 N VAL B 29 O THR B 57
SHEET 5 AA3 6 ALA B 99 CYS B 104 1 O SER B 100 N VAL B 30
SHEET 6 AA3 6 VAL B 122 HIS B 128 1 O MET B 126 N VAL B 101
SHEET 1 AA4 2 ASP B 210 GLY B 214 0
SHEET 2 AA4 2 ASN B 235 LEU B 239 1 O ASN B 235 N TRP B 211
SHEET 1 AA5 6 THR C 6 THR C 11 0
SHEET 2 AA5 6 LYS C 17 GLU C 23 -1 O GLN C 22 N THR C 6
SHEET 3 AA5 6 ARG C 55 PHE C 59 -1 O VAL C 56 N GLU C 23
SHEET 4 AA5 6 ASP C 28 ILE C 32 1 N LEU C 31 O THR C 57
SHEET 5 AA5 6 ALA C 99 CYS C 104 1 O SER C 100 N VAL C 30
SHEET 6 AA5 6 VAL C 122 HIS C 128 1 O MET C 126 N VAL C 101
SHEET 1 AA6 2 ASP C 210 GLY C 214 0
SHEET 2 AA6 2 ASN C 235 LEU C 239 1 O ASN C 235 N TRP C 211
SHEET 1 AA7 6 THR D 6 THR D 11 0
SHEET 2 AA7 6 LYS D 17 GLU D 23 -1 O TRP D 18 N VAL D 10
SHEET 3 AA7 6 ARG D 55 ASP D 60 -1 O THR D 58 N GLU D 21
SHEET 4 AA7 6 ASP D 28 ILE D 32 1 N VAL D 29 O ARG D 55
SHEET 5 AA7 6 ALA D 99 CYS D 104 1 O TRP D 102 N ILE D 32
SHEET 6 AA7 6 VAL D 122 HIS D 128 1 O ARG D 123 N ALA D 99
SHEET 1 AA8 2 THR D 212 GLY D 214 0
SHEET 2 AA8 2 GLY D 237 LEU D 239 1 O GLY D 237 N VAL D 213
SITE 1 AC1 11 GLY A 35 LEU A 36 ALA A 105 SER A 106
SITE 2 AC1 11 ASN A 134 ASN A 156 TRP A 185 TYR A 189
SITE 3 AC1 11 PRO A 190 PRO A 194 HIS A 243
SITE 1 AC2 4 ASP A 168 HIS A 175 HIS A 205 HOH A 419
SITE 1 AC3 13 GLY B 35 LEU B 36 ALA B 105 SER B 106
SITE 2 AC3 13 ASN B 134 LEU B 138 MET B 153 SER B 157
SITE 3 AC3 13 TRP B 185 TYR B 189 PRO B 190 PRO B 194
SITE 4 AC3 13 HIS B 243
SITE 1 AC4 10 GLY C 35 LEU C 36 ALA C 105 SER C 106
SITE 2 AC4 10 ASN C 134 MET C 153 TRP C 185 PRO C 190
SITE 3 AC4 10 PRO C 194 HIS C 243
CRYST1 44.319 110.520 127.779 90.00 99.93 90.00 P 1 21 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 0.022564 0.000000 0.003948 0.00000
SCALE2 0.000000 0.009048 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007945 0.00000
TER 2049 LYS A 266
TER 4098 LYS B 266
TER 6147 LYS C 266
TER 8178 TYR D 264
MASTER 353 0 4 61 32 0 11 6 8498 4 74 84
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