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Open data
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Basic information
| Entry | Database: PDB / ID: 7odk | ||||||
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| Title | Plant peptide hormone receptor H1 | ||||||
Components | Receptor-like protein kinase HSL1 | ||||||
Keywords | PEPTIDE BINDING PROTEIN / Plant receptor LRR pepide hormone | ||||||
| Function / homology | Function and homology informationnon-specific serine/threonine protein kinase / protein serine kinase activity / protein serine/threonine kinase activity / ATP binding / plasma membrane Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.83 Å | ||||||
Authors | Roman, A.O. / Jimenez-Sandoval, P. / Santiago, J. | ||||||
| Funding support | Switzerland, 1items
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Citation | Journal: Nat Commun / Year: 2022Title: HSL1 and BAM1/2 impact epidermal cell development by sensing distinct signaling peptides. Authors: Roman, A.O. / Jimenez-Sandoval, P. / Augustin, S. / Broyart, C. / Hothorn, L.A. / Santiago, J. | ||||||
| History |
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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 | 7odk.cif.gz | 277 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb7odk.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 7odk.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7odk_validation.pdf.gz | 4.4 MB | Display | wwPDB validaton report |
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| Full document | 7odk_full_validation.pdf.gz | 4.4 MB | Display | |
| Data in XML | 7odk_validation.xml.gz | 48.1 KB | Display | |
| Data in CIF | 7odk_validation.cif.gz | 70.9 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/od/7odk ftp://data.pdbj.org/pub/pdb/validation_reports/od/7odk | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 7odvC ![]() 7ogoC ![]() 7ogqC ![]() 7oguC ![]() 7ogzC ![]() 5ixoS 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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| 1 | ![]()
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| 2 | ![]()
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| Unit cell |
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| Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: GLN / Beg label comp-ID: GLN / End auth comp-ID: GLY / End label comp-ID: GLY / Auth seq-ID: 18 - 600 / Label seq-ID: 7 - 589
NCS ensembles : (Details: Local NCS retraints between domains: 1 2) |
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Components
-Protein , 1 types, 2 molecules AAABBB
| #1: Protein | Mass: 66569.797 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Trichoplusia ni (cabbage looper)References: UniProt: Q9SGP2, non-specific serine/threonine protein kinase |
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-Sugars , 5 types, 20 molecules 
| #2: Polysaccharide | Source method: isolated from a genetically manipulated source #3: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source #4: Polysaccharide | Source method: isolated from a genetically manipulated source #5: Polysaccharide | alpha-L-fucopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)]2-acetamido-2-deoxy-beta- ...alpha-L-fucopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)]2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #7: Sugar | ChemComp-NAG / |
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-Non-polymers , 4 types, 696 molecules 






| #6: Chemical | ChemComp-EDO / #8: Chemical | #9: Chemical | ChemComp-NA / | #10: Water | ChemComp-HOH / | |
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-Details
| Has ligand of interest | N |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 3.57 Å3/Da / Density % sol: 65.57 % |
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| Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 5 Details: 0.2 M ammonium sulfate 0.1 M citric acid pH 4.0 30% w/v PEG 1000 |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | |||||||||||||||||||||
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| Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1.000033 Å | |||||||||||||||||||||
| Detector | Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Apr 27, 2019 | |||||||||||||||||||||
| Radiation | Monochromator: double-channel cut fixed-exit / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||
| Radiation wavelength | Wavelength: 1.000033 Å / Relative weight: 1 | |||||||||||||||||||||
| Reflection | Resolution: 1.83→47.084 Å / Num. obs: 158310 / % possible obs: 97.4 % / Redundancy: 3.5 % / CC1/2: 0.999 / Rmerge(I) obs: 0.042 / Rpim(I) all: 0.042 / Rrim(I) all: 0.06 / Net I/σ(I): 10.3 | |||||||||||||||||||||
| Reflection shell | Diffraction-ID: 1
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 5IXO Resolution: 1.83→47.08 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.951 / SU B: 3.248 / SU ML: 0.093 / Cross valid method: FREE R-VALUE / ESU R: 0.117 / ESU R Free: 0.106 Details: Hydrogens have been added in their 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 / Solvent model: MASK BULK SOLVENT | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 29.287 Å2
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| Refinement step | Cycle: LAST / Resolution: 1.83→47.08 Å
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| Refine LS restraints |
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| Refine LS restraints NCS |
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| LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 20
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X-RAY DIFFRACTION
Switzerland, 1items
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PDBj






Trichoplusia ni (cabbage looper)