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- PDB-3ain: R267G mutant of a HSL-like carboxylesterase from Sulfolobus tokodaii -

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Basic information

Entry
Database: PDB / ID: 3ain
TitleR267G mutant of a HSL-like carboxylesterase from Sulfolobus tokodaii
Components303aa long hypothetical esterase
KeywordsHYDROLASE / Carboxylesterase / thermophilic / dimer / archaea / R267G
Function / homology
Function and homology information


carboxylesterase / carboxylesterase activity / identical protein binding
Similarity search - Function
Alpha/beta hydrolase fold-3 / alpha/beta hydrolase fold / Alpha/Beta hydrolase fold, catalytic domain / Alpha/Beta hydrolase fold / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
PHOSPHATE ION / Carboxylesterase
Similarity search - Component
Biological speciesSulfolobus tokodaii (archaea)
MethodX-RAY DIFFRACTION / SYNCHROTRON / 3AIK / Resolution: 1.65 Å
AuthorsAngkawidjaja, C. / Kanaya, S.
CitationJournal: Febs J. / Year: 2012
Title: Structure and stability of a thermostable carboxylesterase from the thermoacidophilic archaeon Sulfolobustokodaii
Authors: Angkawidjaja, C. / Koga, Y. / Takano, K. / Kanaya, S.
History
DepositionMay 16, 2010Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jun 8, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Sep 5, 2012Group: Database references

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: 303aa long hypothetical esterase
B: 303aa long hypothetical esterase
C: 303aa long hypothetical esterase
D: 303aa long hypothetical esterase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)145,54421
Polymers143,6514
Non-polymers1,89317
Water13,601755
1
A: 303aa long hypothetical esterase
D: 303aa long hypothetical esterase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)72,82011
Polymers71,8262
Non-polymers9949
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: 303aa long hypothetical esterase
C: 303aa long hypothetical esterase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)72,72510
Polymers71,8262
Non-polymers8998
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
A: 303aa long hypothetical esterase
B: 303aa long hypothetical esterase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)72,93812
Polymers71,8262
Non-polymers1,11210
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1810 Å2
ΔGint-16 kcal/mol
Surface area21820 Å2
MethodPISA
4
C: 303aa long hypothetical esterase
D: 303aa long hypothetical esterase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)72,6069
Polymers71,8262
Non-polymers7817
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1810 Å2
ΔGint-17 kcal/mol
Surface area21810 Å2
MethodPISA
Unit cell
Length a, b, c (Å)76.370, 114.953, 102.064
Angle α, β, γ (deg.)90.00, 109.55, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein
303aa long hypothetical esterase / Carboxylesterase


Mass: 35912.805 Da / Num. of mol.: 4 / Mutation: R267G
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Sulfolobus tokodaii (archaea) / Strain: 7 / Gene: ST0071 / Plasmid: pET28a+ / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)CodonPlus / References: UniProt: Q976W8, carboxylesterase
#2: Chemical
ChemComp-MPD / (4S)-2-METHYL-2,4-PENTANEDIOL / 2-Methyl-2,4-pentanediol


Mass: 118.174 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C6H14O2 / Comment: precipitant*YM
#3: Chemical
ChemComp-PO4 / PHOSPHATE ION / Phosphate


Mass: 94.971 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: PO4
#4: Chemical
ChemComp-MRD / (4R)-2-METHYLPENTANE-2,4-DIOL / 2-Methyl-2,4-pentanediol


Mass: 118.174 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C6H14O2 / Comment: precipitant*YM
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 755 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.94 Å3/Da / Density % sol: 58.15 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: 0.1M Tris-HCl pH 8.5, 0.2M Ammonium phosphate monobasic, 50% MPD, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL38B1 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Apr 8, 2010 / Details: mirrors
RadiationMonochromator: mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.65→50 Å / Num. obs: 198205 / % possible obs: 99.7 % / Observed criterion σ(I): -3 / Redundancy: 3.8 % / Rmerge(I) obs: 0.052 / Net I/σ(I): 25.7
Reflection shellResolution: 1.65→1.71 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.381 / Mean I/σ(I) obs: 3.3 / % possible all: 98.9

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Processing

Software
NameVersionClassification
BL38B1BSSdata collection
MOLREPphasing
REFMAC5.5.0102refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: 3AIK / Resolution: 1.65→25.35 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.954 / SU B: 1.399 / SU ML: 0.048 / Cross valid method: THROUGHOUT / ESU R Free: 0.076
Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES
RfactorNum. reflection% reflectionSelection details
Rfree0.19727 9993 5 %RANDOM
Rwork0.17541 ---
obs0.1765 188002 99.6 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 20.104 Å2
Baniso -1Baniso -2Baniso -3
1-0 Å20 Å20 Å2
2--0 Å20 Å2
3---0 Å2
Refinement stepCycle: LAST / Resolution: 1.65→25.35 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8920 0 121 755 9796
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.0229247
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.2391.97312560
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.93851128
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.80324.112428
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.4151468
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.9711544
X-RAY DIFFRACTIONr_chiral_restr0.1160.21364
X-RAY DIFFRACTIONr_gen_planes_refined0.0210.0217056
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it2.1361.55612
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it3.30129044
X-RAY DIFFRACTIONr_scbond_it5.08433635
X-RAY DIFFRACTIONr_scangle_it7.734.53516
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.65→1.693 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.284 706 -
Rwork0.271 13678 -
obs--98.06 %

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