+Open data
-Basic information
Entry | Database: PDB / ID: 1mhn | ||||||
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Title | High resolution crystal structure of the SMN Tudor domain | ||||||
Components | Survival motor neuron protein | ||||||
Keywords | RNA BINDING PROTEIN / SMN / SMA / spinal muscular atrophy | ||||||
Function / homology | Function and homology information Gemini of coiled bodies / SMN complex / SMN-Sm protein complex / Cajal body / spliceosomal complex assembly / spliceosomal snRNP assembly / DNA-templated transcription termination / Z disc / cytoplasmic ribonucleoprotein granule / nervous system development ...Gemini of coiled bodies / SMN complex / SMN-Sm protein complex / Cajal body / spliceosomal complex assembly / spliceosomal snRNP assembly / DNA-templated transcription termination / Z disc / cytoplasmic ribonucleoprotein granule / nervous system development / snRNP Assembly / SARS-CoV-2 modulates host translation machinery / perikaryon / nuclear body / neuron projection / axon / RNA binding / nucleoplasm / identical protein binding / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å | ||||||
Authors | Sprangers, R. / Groves, M.R. / Sinning, I. / Sattler, M. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2003 Title: High Resolution X-ray and NMR Structures of the SMN Tudor Domain: conformational variation in the binding site for symmetrically dimethylated arginine residues Authors: Sprangers, R. / Groves, M.R. / Sinning, I. / Sattler, M. #1: Journal: To be Published Title: Definition of domain boundaries and crystallization of the SMN Tudor domain Authors: Sprangers, R. / Selenko, P. / Sattler, M. / Sinning, I. / Groves, M.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mhn.cif.gz | 23.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1mhn.ent.gz | 14.4 KB | Display | PDB format |
PDBx/mmJSON format | 1mhn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1mhn_validation.pdf.gz | 413.9 KB | Display | wwPDB validaton report |
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Full document | 1mhn_full_validation.pdf.gz | 413.9 KB | Display | |
Data in XML | 1mhn_validation.xml.gz | 5 KB | Display | |
Data in CIF | 1mhn_validation.cif.gz | 6.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mh/1mhn ftp://data.pdbj.org/pub/pdb/validation_reports/mh/1mhn | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 6649.454 Da / Num. of mol.: 1 / Fragment: Tudor domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: smn1 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: Q16637 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.83 Å3/Da / Density % sol: 32.79 % |
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Crystal grow | Temperature: 285 K / Method: vapor diffusion, hanging drop / pH: 4.5 Details: Amonium Sulphate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 285K |
Crystal grow | *PLUS Details: Sprangers, R., (2003) Acta Crystallogr., D59, 366. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.934 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Dec 1, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→23.95 Å / Num. all: 4489 / Num. obs: 4499 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 1 / Redundancy: 11.4 % |
Reflection shell | Resolution: 1.8→1.9 Å / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.8→23.947 Å / Isotropic thermal model: Isotropic / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.8→23.947 Å
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LS refinement shell | Resolution: 1.8→1.9 Å | |||||||||||||||||||||||||
Refinement | *PLUS | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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