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- PDB-3now: UNC-45 from Drosophila melanogaster -

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Basic information

Entry
Database: PDB / ID: 3now
TitleUNC-45 from Drosophila melanogaster
ComponentsUNC-45 protein, SD10334p
KeywordsPROTEIN BINDING / Armadillo Repeat / Hsp90 / Myosin / Tetra-tricopeptide Repeat / TPR / binding protein required for myosin function
Function / homology
Function and homology information


somatic muscle development / myosin filament assembly / muscle organ development / chaperone-mediated protein folding / negative regulation of innate immune response / cellular response to heat / defense response to Gram-negative bacterium / cell differentiation / perinuclear region of cytoplasm
Similarity search - Function
UNC-45/Cro1/She4, central domain / Myosin-binding striated muscle assembly central / Tetratricopeptide repeat / Leucine-rich Repeat Variant / Leucine-rich Repeat Variant / Tetratricopeptide repeat / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Armadillo-like helical ...UNC-45/Cro1/She4, central domain / Myosin-binding striated muscle assembly central / Tetratricopeptide repeat / Leucine-rich Repeat Variant / Leucine-rich Repeat Variant / Tetratricopeptide repeat / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Armadillo-like helical / Alpha Horseshoe / Tetratricopeptide-like helical domain superfamily / Armadillo-type fold / Mainly Alpha
Similarity search - Domain/homology
Biological speciesDrosophila melanogaster (fruit fly)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.992 Å
AuthorsLee, C.F. / Hauenstein, A.V. / Fleming, J.K. / Gasper, W.C. / Engelke, V. / Banumathi, S. / Bernstein, S.I. / Huxford, T.
CitationJournal: Structure / Year: 2011
Title: X-ray Crystal Structure of the UCS Domain-Containing UNC-45 Myosin Chaperone from Drosophila melanogaster.
Authors: Lee, C.F. / Hauenstein, A.V. / Fleming, J.K. / Gasper, W.C. / Engelke, V. / Sankaran, B. / Bernstein, S.I. / Huxford, T.
History
DepositionJun 25, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 16, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Dec 27, 2023Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: UNC-45 protein, SD10334p


Theoretical massNumber of molelcules
Total (without water)89,8141
Polymers89,8141
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
A: UNC-45 protein, SD10334p

A: UNC-45 protein, SD10334p

A: UNC-45 protein, SD10334p


Theoretical massNumber of molelcules
Total (without water)269,4413
Polymers269,4413
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation8_555-z,x,-y1
crystal symmetry operation11_555y,-z,-x1
Buried area7000 Å2
ΔGint-38 kcal/mol
Surface area100150 Å2
MethodPISA
Unit cell
Length a, b, c (Å)184.079, 184.079, 184.079
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number195
Space group name H-MP23

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Components

#1: Protein UNC-45 protein, SD10334p


Mass: 89813.523 Da / Num. of mol.: 1 / Fragment: UNP residues 138-947
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Gene: CG2708, Tom34 / Plasmid: pET16b / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta (DE3) pLysS / References: UniProt: Q960B1

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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: 5.79 Å3/Da / Density % sol: 78.7 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 5.6
Details: 0.1 M sodium citrate, 0.2 M ammonium acetate, 25% (w/v) PEG 4000, 1% (v/v) ethylene glycol, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 291.0K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.2.2 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Aug 10, 2007
RadiationScattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.992→50 Å / Num. obs: 42099 / % possible obs: 99.8 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 9.5 % / Rsym value: 0.0115 / Net I/σ(I): 19.2
Reflection shellResolution: 2.992→3.11 Å / Redundancy: 6.5 % / Num. unique all: 4113 / % possible all: 97.8

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHENIX(phenix.refine: 1.5_2)model building
PHENIX(phenix.refine: 1.5_2)refinement
HKL-2000data reduction
HKL-2000data scaling
PHENIX1.5_2phasing
RefinementMethod to determine structure: SAD / Resolution: 2.992→49.197 Å / SU ML: 0.45 / σ(F): 0.15 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2355 1865 4.74 %random
Rwork0.2007 ---
obs0.2024 39354 93.27 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 20.07 Å2 / ksol: 0.292 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-0 Å20 Å20 Å2
2---0 Å2-0 Å2
3---0 Å2
Refinement stepCycle: LAST / Resolution: 2.992→49.197 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6077 0 0 0 6077
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0136145
X-RAY DIFFRACTIONf_angle_d1.2938296
X-RAY DIFFRACTIONf_dihedral_angle_d17.6142309
X-RAY DIFFRACTIONf_chiral_restr0.082992
X-RAY DIFFRACTIONf_plane_restr0.0041064
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.9917-3.09860.3511530.29983183X-RAY DIFFRACTION79
3.0986-3.22260.31521720.28183432X-RAY DIFFRACTION87
3.2226-3.36930.3031740.26063628X-RAY DIFFRACTION91
3.3693-3.54680.28371830.23263697X-RAY DIFFRACTION93
3.5468-3.7690.28161870.20863782X-RAY DIFFRACTION95
3.769-4.05990.23521930.18193815X-RAY DIFFRACTION96
4.0599-4.46820.19971980.16223891X-RAY DIFFRACTION97
4.4682-5.11420.17091990.15473929X-RAY DIFFRACTION97
5.1142-6.4410.22751960.18113994X-RAY DIFFRACTION98
6.441-49.20380.18152100.16584138X-RAY DIFFRACTION99

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