+Open data
-Basic information
Entry | Database: PDB / ID: 2l3n | ||||||
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Title | Solution structure of Rap1-Taz1 fusion protein | ||||||
Components | DNA-binding protein rap1,Telomere length regulator taz1 | ||||||
Keywords | DNA BINDING PROTEIN / RAP1 / TAZ1 | ||||||
Function / homology | Function and homology information nucleus leading edge / meiotic attachment of telomeric heterochromatin to spindle pole body / meiotic spindle pole body / mitotic telomere tethering at nuclear periphery / Removal of the Flap Intermediate from the C-strand / meiotic attachment of telomere to nuclear envelope / chromosome, telomeric repeat region / protection from non-homologous end joining at telomere / telomere maintenance via telomere lengthening / shelterin complex ...nucleus leading edge / meiotic attachment of telomeric heterochromatin to spindle pole body / meiotic spindle pole body / mitotic telomere tethering at nuclear periphery / Removal of the Flap Intermediate from the C-strand / meiotic attachment of telomere to nuclear envelope / chromosome, telomeric repeat region / protection from non-homologous end joining at telomere / telomere maintenance via telomere lengthening / shelterin complex / double-stranded telomeric DNA binding / nuclear telomere cap complex / telomere capping / telomeric DNA binding / telomere maintenance / nuclear periphery / molecular adaptor activity / chromatin / protein homodimerization activity / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Schizosaccharomyces pombe (fission yeast) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Zhou, Z.R. / Wang, F. / Chen, Y. / Lei, M. / Hu, H. | ||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2011 Title: A conserved motif within RAP1 has diversified roles in telomere protection and regulation in different organisms. Authors: Chen, Y. / Rai, R. / Zhou, Z.R. / Kanoh, J. / Ribeyre, C. / Yang, Y. / Zheng, H. / Damay, P. / Wang, F. / Tsujii, H. / Hiraoka, Y. / Shore, D. / Hu, H.Y. / Chang, S. / Lei, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2l3n.cif.gz | 608.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2l3n.ent.gz | 515 KB | Display | PDB format |
PDBx/mmJSON format | 2l3n.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2l3n_validation.pdf.gz | 347.9 KB | Display | wwPDB validaton report |
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Full document | 2l3n_full_validation.pdf.gz | 417.2 KB | Display | |
Data in XML | 2l3n_validation.xml.gz | 28.2 KB | Display | |
Data in CIF | 2l3n_validation.cif.gz | 50.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l3/2l3n ftp://data.pdbj.org/pub/pdb/validation_reports/l3/2l3n | HTTPS FTP |
-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: 11117.336 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 639-693, 362-395 Source method: isolated from a genetically manipulated source Details: The fusion protein of DNA-binding protein rap1 (639-693), Linker (GGSGGSKLGGSGGS) and Telomere length regulator taz1 (362-395) Source: (gene. exp.) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (yeast) Strain: 972 / ATCC 24843 / Gene: rap1, SPBC1778.02, taz1, myb, myb1, SPAC16A10.07c / Production host: Escherichia coli (E. coli) / References: UniProt: Q96TL7, UniProt: P79005 |
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Sequence details | THE FUSION PROTEIN OF DNA-BINDING PROTEIN RAP1 (639-693), LINKER (GGSGGSKLGGSGGS) AND TELOMERE ...THE FUSION PROTEIN OF DNA-BINDING PROTEIN RAP1 (639-693), LINKER (GGSGGSKLGG |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions |
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-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
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-Processing
NMR software | Name: Amber / Version: 9 Developer: Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, and Kollm Classification: refinement |
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Refinement | Method: simulated annealing / Software ordinal: 1 |
NMR representative | Selection criteria: lowest energy |
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 / Representative conformer: 1 |