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HEADER HYDROLASE 04-MAY-24 8ZE9
TITLE ESTS1 PHTHALATE ESTER DEGRADING ESTERASE FROM SULFOBACILLUS
TITLE 2 ACIDOPHILUS S154A MUTANT IN COMPLEX WITH DIETHYLHEXYL PHTHALATE AT
TITLE 3 2.4A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIACYLGLYCEROL LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOBACILLUS ACIDOPHILUS DSM 10332;
SOURCE 3 ORGANISM_TAXID: 679936;
SOURCE 4 GENE: SULAC_0033;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693
KEYWDS ESTERASE, PHTHALATE ESTER DEGRADING, ESTS1, HYDROLASE DIETHYLHEXYL
KEYWDS 2 PHTHALATE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.VERMA,S.CHOUDHARY,P.KUMAR
REVDAT 1 25-DEC-24 8ZE9 0
JRNL AUTH S.VERMA,S.CHOUDHARY,K.AMITH KUMAR,J.K.MAHTO,A.K.VAMSI K,
JRNL AUTH 2 I.MISHRA,V.B.PRAKASH,D.SIRCAR,S.TOMAR,A.KUMAR SHARMA,
JRNL AUTH 3 J.SINGLA,P.KUMAR
JRNL TITL MECHANISTIC AND STRUCTURAL INSIGHTS INTO ESTS1 ESTERASE: A
JRNL TITL 2 POTENT BROAD-SPECTRUM PHTHALATE DIESTER DEGRADING ENZYME.
JRNL REF STRUCTURE 2024
JRNL REFN ISSN 0969-2126
JRNL PMID 39642872
JRNL DOI 10.1016/J.STR.2024.11.006
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0352
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.07
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 11791
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.995
REMARK 3 FREE R VALUE TEST SET COUNT : 589
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 825
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1990
REMARK 3 BIN FREE R VALUE SET COUNT : 43
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2294
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 73
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.71700
REMARK 3 B22 (A**2) : 0.71700
REMARK 3 B33 (A**2) : -2.32700
REMARK 3 B12 (A**2) : 0.35900
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): 0.549
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.281
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.191
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.123
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.889
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2428 ; 0.006 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3306 ; 1.456 ; 1.657
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 299 ; 6.362 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 21 ; 6.976 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 357 ;17.312 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 364 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1856 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1060 ; 0.228 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1579 ; 0.312 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 98 ; 0.175 ; 0.200
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): 1191 ; 1.538 ; 2.095
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1485 ; 2.484 ; 3.126
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1237 ; 2.530 ; 2.511
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1819 ; 3.908 ; 3.608
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 BULK SOLVENT
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 NOT BEEN USED
REMARK 4
REMARK 4 8ZE9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-MAY-24.
REMARK 100 THE DEPOSITION ID IS D_1300047584.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-MAR-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) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : RIGAKU HYPIX-6000HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSALISPRO
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11809
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 23.073
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 15.20
REMARK 200 R MERGE (I) : 0.14500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.33700
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: ROD-SHAPED
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM SULPHATE, 0.1M TRIS, AMMONIUM
REMARK 280 SULPHATE, PH 8.5, VAPOR DIFFUSION, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
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 0.00000
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 0.00000
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 22.45950
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 22.45950
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 22.45950
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: 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 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 PRO A 15
REMARK 465 PRO A 16
REMARK 465 LEU A 17
REMARK 465 ASN A 18
REMARK 465 ARG A 19
REMARK 465 GLU A 20
REMARK 465 GLY A 21
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 O1 TKU A 401 O HOH A 501 1.88
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 154 -112.46 56.40
REMARK 500 TYR A 181 63.06 30.99
REMARK 500 LEU A 201 -56.16 75.94
REMARK 500 TYR A 247 59.70 -107.18
REMARK 500 ILE A 303 -70.72 -100.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 166 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 8ISL RELATED DB: PDB
REMARK 900 ESTS1 PHTHALATE ESTER DEGRADING ESTERASE FROM SULFOBACILLUS
REMARK 900 ACIDOPHILUS IN COMPLEX WITH PHTHALATE
REMARK 900 RELATED ID: 8ISD RELATED DB: PDB
REMARK 900 ESTS1 PHTHALATE ESTER DEGRADING ESTERASE FROM SULFOBACILLUS
REMARK 900 ACIDOPHILUS IN COMPLEX WITH PARANITROPHENYL BUTYRATE
REMARK 900 RELATED ID: 8IPH RELATED DB: PDB
REMARK 900 ESTS1 PHTHALATE ESTER DEGRADING ESTERASE FROM SULFOBACILLUS
REMARK 900 ACIDOPHILUS IN COMPLEX WITH MONOMETHYL PHTHALATE
REMARK 900 RELATED ID: 8IP7 RELATED DB: PDB
REMARK 900 ESTS1 PHTHALATE ESTER DEGRADING ESTERASE FROM SULFOBACILLUS
REMARK 900 ACIDOPHILUS IN COMPLEX WITH JEFFAMINE
REMARK 900 RELATED ID: 8IOQ RELATED DB: PDB
REMARK 900 ESTS1 PHTHALATE ESTER DEGRADING ESTERASE FROM SULFOBACILLUS
REMARK 900 ACIDOPHILUS
REMARK 900 RELATED ID: 8IX4 RELATED DB: PDB
REMARK 900 ESTS1 PHTHALATE ESTER DEGRADING ESTERASE FROM SULFOBACILLUS
REMARK 900 ACIDOPHILUS IN COMPLEX WITH P-NITROPHENOL
REMARK 900 RELATED ID: 8IZO RELATED DB: PDB
REMARK 900 ESTS1 PHTHALATE ESTER DEGRADING ESTERASE FROM SULFOBACILLUS
REMARK 900 ACIDOPHILUS AT 1.22A
REMARK 900 RELATED ID: 8IZX RELATED DB: PDB
REMARK 900 ESTS1 PHTHALATE ESTER DEGRADING ESTERASE FROM SULFOBACILLUS
REMARK 900 ACIDOPHILUS IN COMPLEX WITH DIMETHYL PHTHALATE
REMARK 900 RELATED ID: 8J3D RELATED DB: PDB
REMARK 900 ESTS1 PHTHALATE ESTER DEGRADING ESTERASE FROM SULFOBACILLUS
REMARK 900 ACIDOPHILUS IN COMPLEX WITH DIETHYLHEXYL PHTHALATE
REMARK 900 RELATED ID: 8J3E RELATED DB: PDB
REMARK 900 ESTS1 PHTHALATE ESTER DEGRADING ESTERASE FROM SULFOBACILLUS
REMARK 900 ACIDOPHILUS IN COMPLEX WITH DIMETHYL PHTHALATE ON SURFACE
REMARK 900 RELATED ID: 8W98 RELATED DB: PDB
REMARK 900 ESTS1 PHTHALATE ESTER DEGRADING ESTERASE FROM SULFOBACILLUS
REMARK 900 ACIDOPHILUS IN COMPLEX WITH MONOETHYL HEXYL PHTAHALATE AND 2-
REMARK 900 ETHYLHEXANOL
DBREF 8ZE9 A 1 304 UNP G8TV28 G8TV28_SULAD 1 304
SEQADV 8ZE9 ALA A 154 UNP G8TV28 SER 154 ENGINEERED MUTATION
SEQRES 1 A 304 MET PRO LEU ASP PRO ARG VAL GLU GLN PHE LEU ALA GLN
SEQRES 2 A 304 MET PRO PRO LEU ASN ARG GLU GLY LEU SER LEU ALA GLU
SEQRES 3 A 304 ALA ARG GLN GLN PHE LYS GLN GLY ALA LEU LEU LEU ASP
SEQRES 4 A 304 GLN MET VAL PRO PRO PRO PRO VAL ASP THR GLU ASP GLY
SEQRES 5 A 304 THR VAL VAL THR THR HIS GLY PRO VAL ARG ILE ARG ARG
SEQRES 6 A 304 TYR ILE PRO ASP ARG LEU ARG PHE SER HIS PRO LEU VAL
SEQRES 7 A 304 PHE TYR HIS GLY GLY GLY PHE VAL PHE GLY ASP ILE ASP
SEQRES 8 A 304 THR HIS HIS GLY LEU VAL ALA ARG LEU CYS GLN THR VAL
SEQRES 9 A 304 GLY ALA THR VAL ILE SER VAL ASP TYR SER LEU ALA PRO
SEQRES 10 A 304 GLU ALA LYS PHE PRO VAL PRO VAL ALA GLU CYS ILE ASP
SEQRES 11 A 304 VAL ALA ARG TRP ALA ALA HIS GLU ALA PRO GLY TRP GLY
SEQRES 12 A 304 LEU LYS PRO SER ILE VAL VAL ALA GLY ASP ALA ALA GLY
SEQRES 13 A 304 GLY ASN LEU ALA ALA VAL VAL SER GLN ARG ALA LYS ASP
SEQRES 14 A 304 GLU SER LEU PRO ILE ALA ALA GLN LEU LEU PHE TYR PRO
SEQRES 15 A 304 ALA LEU ASP MET VAL HIS GLU THR PRO SER LYS ARG ASP
SEQRES 16 A 304 PHE ALA ARG GLY TYR LEU LEU GLU ALA ASP ALA MET GLN
SEQRES 17 A 304 TRP PHE GLY GLU GLN TYR LEU ARG THR PRO ASP ASP VAL
SEQRES 18 A 304 SER HIS PRO TRP ALA SER PRO ALA LEU SER PRO ASP LEU
SEQRES 19 A 304 THR GLY LEU PRO PRO ALA LEU VAL ILE THR ALA GLU TYR
SEQRES 20 A 304 ASP PRO LEU ARG ASP GLU GLY GLU ALA TYR ALA GLU ALA
SEQRES 21 A 304 LEU ARG ALA ALA GLY VAL PRO THR GLU GLN ILE ARG PHE
SEQRES 22 A 304 ASP GLY MET ILE HIS GLY PHE MET THR MET PRO ILE PHE
SEQRES 23 A 304 PRO GLN MET GLU ALA ALA ILE GLU ALA VAL ALA ARG PHE
SEQRES 24 A 304 LEU GLU ARG ILE ASP
HET TKU A 401 28
HET TRS A 402 8
HET GOL A 403 6
HET GOL A 404 6
HET GOL A 405 6
HET GOL A 406 6
HETNAM TKU ~{O}1-[(2~{R})-2-ETHYLHEXYL] ~{O}2-[(2~{S})-2-
HETNAM 2 TKU ETHYLHEXYL] BENZENE-1,2-DICARBOXYLATE
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM GOL GLYCEROL
HETSYN TKU BIS(2-ETHYLHEXYL) PHTHALATE; DIETHYLHEXYL PHTHALATE; 1-
HETSYN 2 TKU O-[(2S)-2-ETHYLHEXYL] 2-O-[(2R)-2-ETHYLHEXYL] BENZENE-
HETSYN 3 TKU 1,2-DICARBOXYLATE
HETSYN TRS TRIS BUFFER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 TKU C24 H38 O4
FORMUL 3 TRS C4 H12 N O3 1+
FORMUL 4 GOL 4(C3 H8 O3)
FORMUL 8 HOH *73(H2 O)
HELIX 1 AA1 ASP A 4 GLN A 13 1 10
HELIX 2 AA2 SER A 23 VAL A 42 1 20
HELIX 3 AA3 HIS A 93 GLY A 105 1 13
HELIX 4 AA4 PRO A 122 ALA A 139 1 18
HELIX 5 AA5 PRO A 140 GLY A 143 5 4
HELIX 6 AA6 ALA A 154 ALA A 167 1 14
HELIX 7 AA7 THR A 190 PHE A 196 1 7
HELIX 8 AA8 GLU A 203 LEU A 215 1 13
HELIX 9 AA9 THR A 217 HIS A 223 5 7
HELIX 10 AB1 SER A 227 SER A 231 5 5
HELIX 11 AB2 LEU A 250 ALA A 264 1 15
HELIX 12 AB3 GLY A 279 MET A 283 5 5
HELIX 13 AB4 PRO A 287 ARG A 302 1 16
SHEET 1 AA1 8 ASP A 48 THR A 56 0
SHEET 2 AA1 8 GLY A 59 ILE A 67 -1 O ILE A 67 N ASP A 48
SHEET 3 AA1 8 VAL A 108 ASP A 112 -1 O ASP A 112 N ARG A 62
SHEET 4 AA1 8 LEU A 77 TYR A 80 1 N LEU A 77 O ILE A 109
SHEET 5 AA1 8 ILE A 148 ASP A 153 1 O VAL A 149 N VAL A 78
SHEET 6 AA1 8 ILE A 174 PHE A 180 1 O ALA A 175 N ILE A 148
SHEET 7 AA1 8 ALA A 240 TYR A 247 1 O LEU A 241 N LEU A 179
SHEET 8 AA1 8 THR A 268 ILE A 277 1 O PHE A 273 N THR A 244
CISPEP 1 ALA A 116 PRO A 117 0 1.87
CISPEP 2 PHE A 121 PRO A 122 0 3.10
CRYST1 107.499 107.499 44.919 90.00 90.00 120.00 P 63 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 0.009302 0.005371 0.000000 0.00000
SCALE2 0.000000 0.010742 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022262 0.00000
TER 2308 ASP A 304
MASTER 339 0 6 13 8 0 0 6 2427 1 60 24
END |