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- PDB-1ass: APICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM -

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Basic information

Entry
Database: PDB / ID: 1ass
TitleAPICAL DOMAIN OF THE CHAPERONIN FROM THERMOPLASMA ACIDOPHILUM
ComponentsTHERMOSOME
KeywordsCHAPERONIN / HSP60 / THERMOSOME / TCP1 / GROEL / THERMOPLASMA ACIDOPHILUM / ATP-BINDING
Function / homology
Function and homology information


unfolded protein binding / protein folding / ATP binding
Chaperonin TCP-1, conserved site / Chaperonin Cpn60/TCP-1 family / Thermosome, archaeal / Chaperone tailless complex polypeptide 1 (TCP-1) / GroEL-like apical domain superfamily / TCP-1-like chaperonin intermediate domain superfamily / GroEL-like equatorial domain superfamily / GroEL / GroEL / 3-Layer(bba) Sandwich / Alpha Beta
Thermosome subunit alpha
Biological speciesThermoplasma acidophilum (acidophilic)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MIR / Resolution: 2.3 Å
AuthorsKlumpp, M. / Baumeister, W. / Essen, L.-O.
CitationJournal: Cell(Cambridge,Mass.) / Year: 1997
Title: Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin.
Authors: Klumpp, M. / Baumeister, W. / Essen, L.O.
Validation Report
SummaryFull reportAbout validation report
History
DepositionAug 11, 1997Processing site: BNL
Revision 1.0Dec 3, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Derived calculations / Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: THERMOSOME
hetero molecules


Theoretical massNumber of molelcules
Total (without water)18,1315
Polymers17,8231
Non-polymers3084
Water63135
1
A: THERMOSOME
hetero molecules

A: THERMOSOME
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,26110
Polymers35,6452
Non-polymers6168
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_556y,x,-z+11
Buried area3910 Å2
ΔGint-75 kcal/mol
Surface area14710 Å2
MethodPISA, PQS
Unit cell
γ
α
β
Length a, b, c (Å)82.350, 82.350, 77.830
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number152
Space group name H-MP3121

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Components

#1: Protein/peptide THERMOSOME /


Mass: 17822.625 Da / Num. of mol.: 1
Fragment: ALPHA-SUBUNIT, APICAL DOMAIN, SUBSTRATE-BINDING DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Thermoplasma acidophilum (acidophilic) / Cell line: BL21 / Cellular location: CYTOPLASM / Gene: THSA / Plasmid: PRSET6A / Species (production host): Escherichia coli / Gene (production host): THSA / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P48424
#2: Chemical ChemComp-NA / SODIUM ION / Sodium


Mass: 22.990 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Na
#3: Chemical ChemComp-PO4 / PHOSPHATE ION / Phosphate


Mass: 94.971 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: PO4
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 35 / 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: 4.27 Å3/Da / Density % sol: 70 %
Crystal growpH: 3.5 / Details: pH 3.5
Crystal grow
*PLUS
Temperature: 30 ℃ / pH: 3.8 / Method: vapor diffusion
Components of the solutions
*PLUS

Crystal-ID: 1 / Sol-ID: drop

IDConc.Common name
127 mg/mlprotein
23.0 Mammonium sulfate
30.1 Msodium citrate

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: MPG/DESY, HAMBURG / Beamline: BW6 / Wavelength: 1.05
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 14, 1997 / Details: MIRRORS
RadiationMonochromator: SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.05 Å / Relative weight: 1
ReflectionResolution: 2.3→18 Å / Num. obs: 10935 / % possible obs: 96.3 % / Observed criterion σ(I): -3 / Redundancy: 4 % / Biso Wilson estimate: 57.4 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 24.3
Reflection shellHighest resolution: 2.3 Å / Rmerge(I) obs: 0.256 / Mean I/σ(I) obs: 7 / % possible all: 95.5
Reflection
*PLUS
Num. measured all: 44064
Reflection shell
*PLUS
% possible obs: 95.5 %

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Processing

Software
NameVersionClassification
MLPHAREphasing
SOLOMONphasing
X-PLOR3.851refinement
DENZOdata reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MIR / Resolution: 2.3→10 Å / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: RESTRAINED / Cross valid method: RFREE / σ(F): 0
RfactorNum. reflection% reflectionSelection details
Rfree0.251 516 4 %CONCENTRIC SHELLS
Rwork0.222 ---
Obs0.222 12774 96.3 %-
Displacement parametersBiso mean: 60 Å2
Baniso -1Baniso -2Baniso -3
1-22.95 Å28.95 Å20 Å2
2--22.95 Å20 Å2
3---16.28 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.48 Å0.39 Å
Luzzati d res low-5 Å
Luzzati sigma a0.43 Å0.46 Å
Refinement stepCycle: LAST / Resolution: 2.3→10 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1175 0 16 35 1226
Refine LS restraints

Refinement-ID: X-RAY DIFFRACTION

TypeDev idealDev ideal target
x_bond_d0.017
x_bond_d_na
x_bond_d_prot
x_angle_d
x_angle_d_na
x_angle_d_prot
x_angle_deg2.031
x_angle_deg_na
x_angle_deg_prot
x_dihedral_angle_d25.7
x_dihedral_angle_d_na
x_dihedral_angle_d_prot
x_improper_angle_d1.686
x_improper_angle_d_na
x_improper_angle_d_prot
x_mcbond_it3.251.5
x_mcangle_it4.622
x_scbond_it5.062
x_scangle_it7.352.5
LS refinement shellResolution: 2.33→2.4 Å / % reflection obs: 95.5 %
Xplor file

Refinement-ID: X-RAY DIFFRACTION

Serial noParam fileTopol file
1PARHCSDX.PROTOPHCSDX.PRO
2
Software
*PLUS
Name: X-PLOR / Version: 3.851 / Classification: refinement
Refine LS restraints
*PLUS
Refinement-IDTypeDev ideal
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_deg25.704
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_deg1.686

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