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- PDB-3x3t: Recombinant thaumatin in the presence of 1.5M PST at 293K -

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Basic information

Entry
Database: PDB / ID: 3x3t
TitleRecombinant thaumatin in the presence of 1.5M PST at 293K
Componentsthaumatin I
KeywordsPLANT PROTEIN / thaumatin / sweet-tasting protein / sweet receptor / mainly beta / taste protein / sweet taste receptor / aril
Function / homology
Function and homology information


defense response / cytoplasmic vesicle / extracellular region
Similarity search - Function
Thaumatin / Thaumatin / Thaumatin, conserved site / Thaumatin family signature. / Thaumatin family / Thaumatin family / Thaumatin family profile. / Thaumatin family / Osmotin/thaumatin-like superfamily / Sandwich / Mainly Beta
Similarity search - Domain/homology
L(+)-TARTARIC ACID / Thaumatin I / Thaumatin I
Similarity search - Component
Biological speciesThaumatococcus daniellii (katemfe)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.501 Å
AuthorsMasuda, T. / Okubo, K. / Mikami, B.
CitationJournal: To be Published
Title: Structure of the recombinant thaumatin in the presence of PST at room temperature
Authors: Masuda, T. / Okubo, K. / Mikami, B.
History
DepositionJan 26, 2015Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Feb 3, 2016Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: thaumatin I
hetero molecules


Theoretical massNumber of molelcules
Total (without water)22,3782
Polymers22,2281
Non-polymers1501
Water2,954164
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)58.505, 58.505, 151.666
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212

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Components

#1: Protein thaumatin I


Mass: 22228.043 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Thaumatococcus daniellii (katemfe) / Plasmid: pPIC6-pre-TH / Production host: Komagataella pastoris (fungus) / Strain (production host): X-33 / References: UniProt: A1IIJ1, UniProt: P02883*PLUS
#2: Chemical ChemComp-TLA / L(+)-TARTARIC ACID


Mass: 150.087 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H6O6
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 164 / 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: 2.92 Å3/Da / Density % sol: 57.87 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 0.05M ADA, 1.5 M K-Na TARTRATE, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 293 K
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL26B1 / Wavelength: 1 Å
DetectorType: RIGAKU SATURN A200 / Detector: CCD / Date: Oct 13, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.5→50 Å / Num. obs: 43097 / % possible obs: 99.8 % / Redundancy: 13.3 % / Rmerge(I) obs: 0.046 / Net I/σ(I): 69.33
Reflection shellResolution: 1.5→1.53 Å / Redundancy: 12.5 % / Rmerge(I) obs: 0.435 / Mean I/σ(I) obs: 7.3 / % possible all: 99.2

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHENIX(phenix.refine: 1.9_1692)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.501→27.292 Å / SU ML: 0.1 / σ(F): 1.34 / Phase error: 10.29 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1299 2150 5 %
Rwork0.1126 --
obs0.1135 43012 99.8 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 69.7 Å2 / Biso mean: 20.5269 Å2 / Biso min: 8.92 Å2
Refinement stepCycle: LAST / Resolution: 1.501→27.292 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1551 0 10 164 1725
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0061826
X-RAY DIFFRACTIONf_angle_d1.0782493
X-RAY DIFFRACTIONf_chiral_restr0.043257
X-RAY DIFFRACTIONf_plane_restr0.005346
X-RAY DIFFRACTIONf_dihedral_angle_d11.866684
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 15

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.5006-1.53550.17751390.12222641278099
1.5355-1.57390.13161400.101926612801100
1.5739-1.61640.12841400.09326662806100
1.6164-1.6640.10941410.08212673281499
1.664-1.71770.11141390.080826742813100
1.7177-1.77910.10091420.081126872829100
1.7791-1.85030.1181420.082526972839100
1.8503-1.93450.12781420.087926972839100
1.9345-2.03640.12261430.090127052848100
2.0364-2.1640.12421430.100227272870100
2.164-2.3310.1151430.108727332876100
2.331-2.56540.1451450.129527402885100
2.5654-2.93620.16061460.141827842930100
2.9362-3.69790.13761480.129728012949100
3.6979-27.29680.121570.117429763133100

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