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HEADER HYDROLASE 03-OCT-25 9X24
TITLE ZEARALENONE DEGRADING ENZYME MUTANT S102A/L134V/M157V WITH A-
TITLE 2 ZEARALENOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MONOSPORASCUS SP. GIB2;
SOURCE 3 ORGANISM_TAXID: 2211647;
SOURCE 4 GENE: DL765_008938;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.OUYANG,W.XU
REVDAT 1 07-OCT-26 9X24 0
JRNL AUTH B.OUYANG,W.XU
JRNL TITL CRYSTAL STRUCTURE OF A NOVEL THERMOSTABLE ZEARALENONE
JRNL TITL 2 DEGRADING ENZYME MUTANT S102A/L134V/M157V WITH A-ZEARALENOL
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.21_5207: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.96
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 16750
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.770
REMARK 3 FREE R VALUE TEST SET COUNT : 799
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 22.9600 - 3.5400 0.99 2722 124 0.1629 0.1913
REMARK 3 2 3.5400 - 2.8100 0.99 2689 115 0.2062 0.2866
REMARK 3 3 2.8100 - 2.4600 0.99 2648 137 0.2230 0.2759
REMARK 3 4 2.4600 - 2.2300 0.99 2645 149 0.2254 0.2696
REMARK 3 5 2.2300 - 2.0700 0.99 2608 139 0.2328 0.3114
REMARK 3 6 2.0700 - 1.9500 0.99 2639 135 0.2736 0.3237
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.900
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 2173
REMARK 3 ANGLE : 0.925 2963
REMARK 3 CHIRALITY : 0.051 324
REMARK 3 PLANARITY : 0.009 381
REMARK 3 DIHEDRAL : 17.482 792
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 9X24 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 07-OCT-25.
REMARK 100 THE DEPOSITION ID IS D_1300064022.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-OCT-24
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16750
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 22.960
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.29800
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MAGNESIUM CHLORIDE, 0.05 M TRIS
REMARK 280 -HCL PH 8.5, 30% PEG 550 MME, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 281K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 40.09000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.71450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 40.09000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.71450
REMARK 290 SMTRY3 4 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: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
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 HOH A 425 O HOH A 436 1.46
REMARK 500 O HOH A 416 O HOH A 502 1.68
REMARK 500 O HOH A 410 O HOH A 449 1.79
REMARK 500 O HOH A 507 O HOH A 510 1.95
REMARK 500 O LEU A 139 O HOH A 401 2.11
REMARK 500 O HOH A 446 O HOH A 448 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 471 O HOH A 505 4546 2.10
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 ALA A 59 131.10 -36.73
REMARK 500 SER A 62 -129.13 51.26
REMARK 500 ALA A 102 -122.24 56.20
REMARK 500 SER A 202 145.87 -170.12
REMARK 500 MET A 244 -111.45 -127.20
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 9X24 A 1 267 UNP A0A4Q4TP46_9PEZI
DBREF2 9X24 A A0A4Q4TP46 1 267
SEQADV 9X24 ALA A 102 UNP A0A4Q4TP4 SER 102 ENGINEERED MUTATION
SEQADV 9X24 VAL A 134 UNP A0A4Q4TP4 LEU 134 ENGINEERED MUTATION
SEQADV 9X24 VAL A 157 UNP A0A4Q4TP4 MET 157 ENGINEERED MUTATION
SEQRES 1 A 267 MET ARG THR ARG SER THR LEU THR ASP ARG ASN GLY ILE
SEQRES 2 A 267 THR TRP TYR TYR GLU GLN GLU GLY SER GLY PRO HIS VAL
SEQRES 3 A 267 VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS HIS MET MET
SEQRES 4 A 267 ASP LYS PRO MET SER LEU ILE ALA ALA LYS GLY PHE THR
SEQRES 5 A 267 CYS THR THR PHE ASP MET ALA GLY MET SER ARG SER TRP
SEQRES 6 A 267 ASP ALA PRO PRO GLU THR TYR GLN ASP VAL THR ALA GLN
SEQRES 7 A 267 LYS LEU ALA SER TYR VAL ILE SER ILE LEU ASP GLU LEU
SEQRES 8 A 267 HIS ILE ASP TYR ALA THR PHE TRP GLY CYS ALA SER GLY
SEQRES 9 A 267 GLY ALA THR VAL LEU ALA LEU ALA ALA ASP TYR PRO GLU
SEQRES 10 A 267 ARG MET ARG ASN GLY LEU PRO HIS GLU VAL PRO THR ALA
SEQRES 11 A 267 ALA SER PRO VAL PHE GLY GLN LEU LEU LYS LEU ALA GLU
SEQRES 12 A 267 MET GLU ASP GLU ALA ILE VAL LYS MET LEU SER GLU GLU
SEQRES 13 A 267 VAL PRO GLN THR ASN PHE GLY HIS ASP LEU THR ALA TRP
SEQRES 14 A 267 HIS GLU LEU GLY GLU GLU VAL HIS ALA ARG LEU ARG LYS
SEQRES 15 A 267 ASN TYR PRO ARG TRP ALA ARG GLY TYR PRO HIS THR LEU
SEQRES 16 A 267 PRO LEU SER SER PRO THR SER LYS GLU ASP LEU THR LYS
SEQRES 17 A 267 ARG PRO LEU ASP TRP THR VAL GLY GLY ASP THR PRO THR
SEQRES 18 A 267 ARG VAL PHE PHE ASP ASN ILE VAL THR ALA SER LYS ALA
SEQRES 19 A 267 GLY ILE PRO ILE GLY THR LEU PRO GLY MET HIS PHE PRO
SEQRES 20 A 267 TYR LEU SER HIS PRO GLU VAL LEU ALA GLU HIS ILE VAL
SEQRES 21 A 267 ASP THR THR ARG LYS TYR LEU
HET 36J A 301 23
HETNAM 36J (3S,7R,11E)-7,14,16-TRIHYDROXY-3-METHYL-3,4,5,6,7,8,9,
HETNAM 2 36J 10-OCTAHYDRO-1H-2-BENZOXACYCLOTETRADECIN-1-ONE
FORMUL 2 36J C18 H24 O5
FORMUL 3 HOH *110(H2 O)
HELIX 1 AA1 GLU A 35 MET A 38 5 4
HELIX 2 AA2 MET A 39 ALA A 48 1 10
HELIX 3 AA3 MET A 61 TRP A 65 5 5
HELIX 4 AA4 PRO A 68 TYR A 72 5 5
HELIX 5 AA5 THR A 76 HIS A 92 1 17
HELIX 6 AA6 ALA A 102 TYR A 115 1 14
HELIX 7 AA7 PRO A 133 LEU A 138 1 6
HELIX 8 AA8 LEU A 139 MET A 144 5 6
HELIX 9 AA9 GLU A 145 GLY A 163 1 19
HELIX 10 AB1 LEU A 166 GLU A 171 1 6
HELIX 11 AB2 GLY A 173 TYR A 191 1 19
HELIX 12 AB3 LEU A 195 SER A 199 5 5
HELIX 13 AB4 SER A 202 LYS A 208 1 7
HELIX 14 AB5 PHE A 224 GLY A 235 1 12
HELIX 15 AB6 PHE A 246 HIS A 251 1 6
HELIX 16 AB7 HIS A 251 LYS A 265 1 15
SHEET 1 AA1 6 ARG A 2 THR A 8 0
SHEET 2 AA1 6 THR A 14 GLU A 20 -1 O GLN A 19 N THR A 3
SHEET 3 AA1 6 THR A 52 PHE A 56 -1 O CYS A 53 N GLU A 20
SHEET 4 AA1 6 HIS A 25 ILE A 29 1 N VAL A 26 O THR A 52
SHEET 5 AA1 6 ALA A 96 CYS A 101 1 O TRP A 99 N ILE A 29
SHEET 6 AA1 6 MET A 119 HIS A 125 1 O LEU A 123 N PHE A 98
SHEET 1 AA2 2 TRP A 213 GLY A 216 0
SHEET 2 AA2 2 ILE A 238 LEU A 241 1 O GLY A 239 N TRP A 213
CRYST1 80.180 45.429 64.011 90.00 95.35 90.00 C 1 2 1 4
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 0.012472 0.000000 0.001167 0.00000
SCALE2 0.000000 0.022012 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015691 0.00000
TER 2090 LEU A 267
MASTER 263 0 1 16 8 0 0 6 2222 1 23 21
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