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Yorodumi- PDB-9qlu: Amyloid structure of 17kDa alpha-amylase/trypsin inhibitor 2 (Uni... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9qlu | |||||||||||||||||||||||||||
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| Title | Amyloid structure of 17kDa alpha-amylase/trypsin inhibitor 2 (Uniprot ID: AI172_ORYSJ) | |||||||||||||||||||||||||||
Components | 17kDa alpha-amylase/trypsin inhibitor 2 | |||||||||||||||||||||||||||
Keywords | PROTEIN FIBRIL / Amyloid / Plant protein / Storage protein / Trypsin inhibitor | |||||||||||||||||||||||||||
| Function / homology | Cereal seed allergen/grain softness/trypsin and alpha-amylase inhibitor / Protease inhibitor/seed storage/LTP family / Bifunctional inhibitor/plant lipid transfer protein/seed storage helical domain / Bifunctional inhibitor/plant lipid transfer protein/seed storage helical domain superfamily / nutrient reservoir activity / IgE binding / serine-type endopeptidase inhibitor activity / extracellular region / 17kDa alpha-amylase/trypsin inhibitor 2 Function and homology information | |||||||||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 2.54 Å | |||||||||||||||||||||||||||
Authors | Rhyner, D. / Riek, R. / Greenwald, J. / Frey, L. / Kwiatkowski, W. | |||||||||||||||||||||||||||
| Funding support | Switzerland, 1items
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Citation | Journal: To Be PublishedTitle: Amyloid structure of 17kDa alpha-amylase/trypsin inhibitor 2 (Uniprot ID: AI172_ORYSJ) Authors: Rhyner, D. / Riek, R. / Greenwald, J. / Frey, L. / Kwiatkowski, W. | |||||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9qlu.cif.gz | 73.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9qlu.ent.gz | 52 KB | Display | PDB format |
| PDBx/mmJSON format | 9qlu.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9qlu_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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| Full document | 9qlu_full_validation.pdf.gz | 1.2 MB | Display | |
| Data in XML | 9qlu_validation.xml.gz | 33.7 KB | Display | |
| Data in CIF | 9qlu_validation.cif.gz | 46.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ql/9qlu ftp://data.pdbj.org/pub/pdb/validation_reports/ql/9qlu | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 53234MC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 16493.027 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: Os07g0216700, LOC_Os07g11650, OJ1080_F08.106, OJ1779_B07.133, OsJ_23556 Production host: ![]() References: UniProt: Q7X8H9 Has protein modification | N | |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: FILAMENT / 3D reconstruction method: helical reconstruction |
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Sample preparation
| Component | Name: Amyloid fibril of 17kDa alpha-amylase/trypsin inhibitor 2 Type: ORGANELLE OR CELLULAR COMPONENT / Entity ID: all / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7 / Details: DTT 100 mM |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: COPPER / Grid type: Quantifoil R2/1 |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE-PROPANE / Humidity: 95 % / Chamber temperature: 288.15 K |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 3000 nm / Nominal defocus min: 800 nm / Cs: 2.7 mm / C2 aperture diameter: 70 µm / Alignment procedure: COMA FREE |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Average exposure time: 1 sec. / Electron dose: 62.79 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
| EM imaging optics | Energyfilter name: GIF Bioquantum / Energyfilter slit width: 20 eV |
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Processing
| EM software | Name: RELION / Version: 4.0.0 / Category: 3D reconstruction |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
| Helical symmerty | Angular rotation/subunit: -2.277 ° / Axial rise/subunit: 4.734 Å / Axial symmetry: C1 |
| 3D reconstruction | Resolution: 2.54 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 121923 / Symmetry type: HELICAL |
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