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- PDB-5nyg: Anbu (Gly-1) mutant from Hyphomicrobium sp. strain MC1 - SG P2(1)... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5nyg | ||||||
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Title | Anbu (Gly-1) mutant from Hyphomicrobium sp. strain MC1 - SG P2(1)2(1)2(1) | ||||||
![]() | Anbu | ||||||
![]() | HYDROLASE / Ntn-hydrolase-fold / proteasome / evolution | ||||||
Function / homology | Uncharacterised conserved protein UCP009120, proteasome-type protease, Sll0069 / proteasome core complex / Proteasome subunit / Proteasome, subunit alpha/beta / Nucleophile aminohydrolases, N-terminal / proteolysis involved in protein catabolic process / Peptidase![]() | ||||||
Biological species | Hyphomicrobium sp. | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Vielberg, M.-T. / Groll, M. | ||||||
Funding support | ![]()
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![]() | ![]() Title: On the Trails of the Proteasome Fold: Structural and Functional Analysis of the Ancestral beta-Subunit Protein Anbu. Authors: Vielberg, M.T. / Bauer, V.C. / Groll, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 747.8 KB | Display | ![]() |
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PDB format | ![]() | 624.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 492.2 KB | Display | ![]() |
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Full document | ![]() | 496.4 KB | Display | |
Data in XML | ![]() | 67.8 KB | Display | |
Data in CIF | ![]() | 95.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5nyfSC ![]() 5nyjC ![]() 5nypC ![]() 5nyqC ![]() 5nyrC S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 27536.016 Da / Num. of mol.: 8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: HYPMC_4374 / Production host: ![]() ![]() #2: Chemical | ChemComp-TRS / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.86 Å3/Da / Density % sol: 56.92 % |
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Crystal grow | Temperature: 298.15 K / Method: vapor diffusion, sitting drop / pH: 7 / Details: 0.2 M Di-sodium tatrate, 20 % PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Dec 19, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→40 Å / Num. obs: 92239 / % possible obs: 98.5 % / Redundancy: 5.3 % / Rmerge(I) obs: 0.079 / Net I/σ(I): 14.1 |
Reflection shell | Resolution: 2.4→2.5 Å / Rmerge(I) obs: 0.572 / Mean I/σ(I) obs: 2.7 / % possible all: 99.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5NYF Resolution: 2.4→20 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.924 / SU B: 17.986 / SU ML: 0.184 / Cross valid method: THROUGHOUT / ESU R Free: 0.25 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 45.954 Å2
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Refinement step | Cycle: 1 / Resolution: 2.4→20 Å
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Refine LS restraints |
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