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Yorodumi- PDB-2l3l: The solution structure of the N-terminal domain of human Tubulin ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2l3l | ||||||
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Title | The solution structure of the N-terminal domain of human Tubulin Binding Cofactor C reveals a platform for the interaction with ab-tubulin | ||||||
Components | Tubulin-specific chaperone C | ||||||
Keywords | CHAPERONE / tubulin binding cofactor | ||||||
Function / homology | Function and homology information post-chaperonin tubulin folding pathway / Post-chaperonin tubulin folding pathway / photoreceptor connecting cilium / tubulin complex assembly / tubulin binding / protein folding / protein-folding chaperone binding / microtubule / cytoskeleton / GTPase activity ...post-chaperonin tubulin folding pathway / Post-chaperonin tubulin folding pathway / photoreceptor connecting cilium / tubulin complex assembly / tubulin binding / protein folding / protein-folding chaperone binding / microtubule / cytoskeleton / GTPase activity / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
Model details | target function, model 1 | ||||||
Authors | Garcia-Mayoral, M.F. / Castano, R. / Lopez-Fanarraga, M.L. / Zabala, J.C. / Rico, M. / Bruix, M. | ||||||
Citation | Journal: To be Published Title: The solution structure of the N-terminal domain of human tubulin binding cofactor C reveals a platform for tubulin interaction Authors: Garcia-Mayoral, M.F. / Castano, R. / Lopez-Fanarraga, M.L. / Zabala, J.C. / Rico, M. / Bruix, M. #1: Journal: Biomol.Nmr Assign. / Year: 2010 Title: 1H, 13C, and 15N resonance assignments of the N-terminal domain of human Tubulin Binding Cofactor C. Authors: Garcia-Mayoral, M.F. / Castano, R. / Zabala, J.C. / Santoro, J. / Rico, M. / Bruix, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2l3l.cif.gz | 721.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2l3l.ent.gz | 607.2 KB | Display | PDB format |
PDBx/mmJSON format | 2l3l.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2l3l_validation.pdf.gz | 351.3 KB | Display | wwPDB validaton report |
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Full document | 2l3l_full_validation.pdf.gz | 461.9 KB | Display | |
Data in XML | 2l3l_validation.xml.gz | 29 KB | Display | |
Data in CIF | 2l3l_validation.cif.gz | 52.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l3/2l3l ftp://data.pdbj.org/pub/pdb/validation_reports/l3/2l3l | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 13169.887 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 26-135 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TBCC / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: Q15814 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.5-1.0 mM [U-13C; U-15N] TBCC_Nterm-1, 20 mM potassium phosphate-2, 20 mM potassium chloride-3, 1.0 mM TCEP-4, 1.0 mM EDTA-5, 0.05 mM DSS-6, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||||||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0.02 / pH: 6.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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-Processing
NMR software |
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Refinement | Method: molecular dynamics / Software ordinal: 1 Details: Generalized Born continuum solvent model with AMBER9 | ||||||||||||||||||||||||
NMR representative | Selection criteria: target function | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 / Representative conformer: 1 |