+Open data
-Basic information
Entry | Database: PDB / ID: 2lmu | ||||||
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Title | Androcam at high calcium | ||||||
Components | Calmodulin-related protein 97A | ||||||
Keywords | METAL BINDING PROTEIN / spermatogenesis | ||||||
Function / homology | Function and homology information investment cone / myosin VI complex / myosin VI head/neck binding / actin filament-based movement / Neutrophil degranulation / enzyme regulator activity / calcium ion binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Drosophila melanogaster (fruit fly) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Joshi, M.K. / Moran, S.T. / Beckingham, K.M. / Mackenzie, K.R. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2012 Title: Structure of androcam supports specialized interactions with myosin VI. Authors: Joshi, M.K. / Moran, S. / Beckingham, K.M. / Mackenzie, K.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2lmu.cif.gz | 998.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2lmu.ent.gz | 875 KB | Display | PDB format |
PDBx/mmJSON format | 2lmu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lm/2lmu ftp://data.pdbj.org/pub/pdb/validation_reports/lm/2lmu | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 17028.871 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Gene: And, Camr97A, CG17769 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P49258 |
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#2: Chemical |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR / Details: structure of androcam in high (10mM) calcium | ||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1.8 mM [U-100% 13C; U-100% 15N] androcam, 10 mM calcium chloride, 10 % D2O, 10 mM potassium chloride, 10 mM TRIS, 10 mM DTT, 0.1 mM TSP, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 10 / pH: 7.4 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||
NMR constraints | Protein chi angle constraints total count: 55 / Protein phi angle constraints total count: 103 / Protein psi angle constraints total count: 103 | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Average torsion angle constraint violation: 0.3 ° Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 20 / Maximum torsion angle constraint violation: 1 ° |