+Open data
-Basic information
Entry | Database: PDB / ID: 1ala | ||||||
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Title | STRUCTURE OF CHICKEN ANNEXIN V AT 2.25-ANGSTROMS RESOLUTION | ||||||
Components | ANNEXIN V | ||||||
Keywords | CALCIUM/PHOSPHOLIPID-BINDING PROTEIN / CALCIUM-PHOSPHOLIPID-BINDING PROTEIN complex | ||||||
Function / homology | Function and homology information Platelet degranulation / negative regulation of coagulation / calcium-dependent phospholipid binding / vesicle membrane / phosphatidylserine binding / calcium ion homeostasis / calcium channel complex / calcium channel activity / sarcolemma / vesicle ...Platelet degranulation / negative regulation of coagulation / calcium-dependent phospholipid binding / vesicle membrane / phosphatidylserine binding / calcium ion homeostasis / calcium channel complex / calcium channel activity / sarcolemma / vesicle / calcium ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | Gallus gallus (chicken) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.25 Å | ||||||
Authors | Waller, D.A. / Bewley, M.C. / Huber, R. | ||||||
Citation | Journal: Biochemistry / Year: 1993 Title: Structure of chicken annexin V at 2.25-A resolution. Authors: Bewley, M.C. / Boustead, C.M. / Walker, J.H. / Waller, D.A. / Huber, R. #1: Journal: Biochem.Soc.Trans. / Year: 1992 Title: Annexin V, a Calcium-Dependent Phospholipid-Binding Protein Authors: Walker, J.H. / Boustead, C.M. / Koster, J.J. / Bewley, M. / Waller, D.A. #2: Journal: FEBS Lett. / Year: 1991 Title: Crystallization and Preliminary X-Ray Studies of Annexin Iv (Endonexin), a Calcium-Dependent Phospholipid-Binding Protein Authors: Boustead, C.M. / Walker, J.H. / Kennedy, D. / Waller, D.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ala.cif.gz | 77.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ala.ent.gz | 57.2 KB | Display | PDB format |
PDBx/mmJSON format | 1ala.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ala_validation.pdf.gz | 372.1 KB | Display | wwPDB validaton report |
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Full document | 1ala_full_validation.pdf.gz | 401.1 KB | Display | |
Data in XML | 1ala_validation.xml.gz | 11.5 KB | Display | |
Data in CIF | 1ala_validation.cif.gz | 16.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/al/1ala ftp://data.pdbj.org/pub/pdb/validation_reports/al/1ala | 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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Atom site foot note | 1: RESIDUE 14 IS A CIS PROLINE. |
-Components
#1: Protein | Mass: 36262.355 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Gallus gallus (chicken) / References: UniProt: P17153 | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.52 Å3/Da / Density % sol: 51.23 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.25 Å / Num. obs: 16189 / % possible obs: 90 % / Num. measured all: 37651 / Rmerge(I) obs: 0.045 |
-Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.25→10 Å /
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Refinement step | Cycle: LAST / Resolution: 2.25→10 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.25 Å / Lowest resolution: 10 Å / Num. reflection all: 16189 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 19.4 Å2 |