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Yorodumi- PDB-1tud: ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, CIRCULAR PERMUTANT, CUT AT ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1tud | ||||||
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Title | ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, CIRCULAR PERMUTANT, CUT AT N47-D48 | ||||||
Components | ALPHA-SPECTRIN | ||||||
Keywords | CYTOSKELETON / CAPPING PROTEIN / CALCIUM-BINDING / DUPLICATION / SH3 DOMAIN | ||||||
Function / homology | Function and homology information actin filament capping / costamere / cortical actin cytoskeleton / cell projection / actin filament binding / cell junction / actin cytoskeleton organization / calmodulin binding / calcium ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | Gallus gallus (chicken) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.77 Å | ||||||
Authors | Viguera, A.R. / Serrano, L. / Wilmanns, M. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1995 Title: The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics. Authors: Viguera, A.R. / Blanco, F.J. / Serrano, L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1tud.cif.gz | 26.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1tud.ent.gz | 15 KB | Display | PDB format |
PDBx/mmJSON format | 1tud.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1tud_validation.pdf.gz | 351.9 KB | Display | wwPDB validaton report |
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Full document | 1tud_full_validation.pdf.gz | 352 KB | Display | |
Data in XML | 1tud_validation.xml.gz | 2.4 KB | Display | |
Data in CIF | 1tud_validation.cif.gz | 3.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tu/1tud ftp://data.pdbj.org/pub/pdb/validation_reports/tu/1tud | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 7129.172 Da / Num. of mol.: 1 / Fragment: SRC HOMOLOGY 3 DOMAIN Mutation: CIRCULAR PERMUTANT, CUT AT N47-D48, INS(M-D48), INS(SG-T4) Source method: isolated from a genetically manipulated source Details: THIS IS A CIRCULAR PERMUTANT OF THE WT ALPHA-SPECTRIN SH3 SEQUENCE (PDB CODE WT-3D STRUCTURE: 1SGB). THE RESIDUE NUMBERS ARE AS IN THE WT SPECTRIN-SH3 DOMAIN (1SGB). THR 4 (N-TERMINUS) AND ...Details: THIS IS A CIRCULAR PERMUTANT OF THE WT ALPHA-SPECTRIN SH3 SEQUENCE (PDB CODE WT-3D STRUCTURE: 1SGB). THE RESIDUE NUMBERS ARE AS IN THE WT SPECTRIN-SH3 DOMAIN (1SGB). THR 4 (N-TERMINUS) AND ASP 62 (C-TERMINUS) OF THE WT-SH3 SEQUENCE ARE LINKED BY TWO ADDITIONAL RESIDUES (SER 2, GLY 3). THE CHAIN IS CLEAVED BETWEEN ASN 47 AND ASP 48. MET 0 IS ADDED AT THE NEW N-TERMINUS. Source: (gene. exp.) Gallus gallus (chicken) / Organ: BRAIN / Plasmid: PET3D / Production host: Escherichia coli (E. coli) / References: UniProt: P07751 |
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#2: Water | ChemComp-HOH / |
Sequence details | THIS IS A CIRCULAR PERMUTANT OF THE WT ALPHA-SPECTRIN SH3 SEQUENCE (PDB CODE WT-3D STRUCTURE: 1SGB). ...THIS IS A CIRCULAR PERMUTANT OF THE WT ALPHA-SPECTRIN SH3 SEQUENCE (PDB CODE WT-3D STRUCTURE: 1SGB). THE RESIDUE NUMBERS ARE AS IN THE WT SPECTRIN-SH3 DOMAIN (1SGB). THR 4 (N-TERMINUS) AND ASP 62 (C-TERMINUS) OF THE WT-SH3 SEQUENCE ARE LINKED BY TWO ADDITIONAL |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 52.74 % |
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Crystal grow | *PLUS Method: other / Details: NMR |
-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jun 26, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.77→100 Å / Num. obs: 6591 / % possible obs: 90.3 % / Observed criterion σ(I): 0 / Redundancy: 2.64 % / Rmerge(I) obs: 0.043 |
-Processing
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Refinement | Resolution: 1.77→6 Å / σ(F): 1 Details: THE FIRST TWO RESIDUES OF THE NEW N-TERMINUS (MET 0, ASP 48) ARE NOT VISIBLE IN THE ELECTRON DENSITY MAP.
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Displacement parameters | Biso mean: 13.49 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.77→6 Å
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Refine LS restraints |
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