+Open data
-Basic information
Entry | Database: PDB / ID: 1ign | ||||||
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Title | DNA-BINDING DOMAIN OF RAP1 IN COMPLEX WITH TELOMERIC DNA SITE | ||||||
Components |
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Keywords | DNA BINDING PROTEIN/DNA / RAP1 / YEAST / TELOMERES / HOMOEODOMAIN / DNA BINDING PROTEIN-DNA COMPLEX | ||||||
Function / homology | Function and homology information positive regulation of ribosomal protein gene transcription by RNA polymerase II / G-quadruplex DNA formation / protection from non-homologous end joining at telomere / establishment of protein localization to chromatin / establishment of protein localization to telomere / telomere maintenance via telomere lengthening / shelterin complex / G-quadruplex DNA binding / double-stranded telomeric DNA binding / silent mating-type cassette heterochromatin formation ...positive regulation of ribosomal protein gene transcription by RNA polymerase II / G-quadruplex DNA formation / protection from non-homologous end joining at telomere / establishment of protein localization to chromatin / establishment of protein localization to telomere / telomere maintenance via telomere lengthening / shelterin complex / G-quadruplex DNA binding / double-stranded telomeric DNA binding / silent mating-type cassette heterochromatin formation / nucleosomal DNA binding / DNA binding, bending / regulation of glycolytic process / nuclear chromosome / telomeric DNA binding / subtelomeric heterochromatin formation / TFIID-class transcription factor complex binding / cis-regulatory region sequence-specific DNA binding / TBP-class protein binding / telomere maintenance / protein-DNA complex / histone binding / transcription regulator complex / RNA polymerase II-specific DNA-binding transcription factor binding / sequence-specific DNA binding / chromosome, telomeric region / DNA-binding transcription factor activity, RNA polymerase II-specific / DNA-binding transcription factor activity / regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.25 Å | ||||||
Authors | Koenig, P. / Giraldo, R. / Chapman, L. / Rhodes, D. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 1996 Title: The crystal structure of the DNA-binding domain of yeast RAP1 in complex with telomeric DNA. Authors: Konig, P. / Giraldo, R. / Chapman, L. / Rhodes, D. #1: Journal: Embo J. / Year: 1994 Title: The Yeast Telomere-Binding Protein RAP1 Binds to and Promotes the Formation of DNA Quadruplexes in Telomeric DNA Authors: Giraldo, R. / Rhodes, D. #2: Journal: Cell(Cambridge,Mass.) / Year: 1987 Title: Purification and Cloning of a DNA Binding Protein from Yeast that Binds to Both Silencer and Activator Elements Authors: Shore, D. / Nasmyth, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ign.cif.gz | 142.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ign.ent.gz | 103 KB | Display | PDB format |
PDBx/mmJSON format | 1ign.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ig/1ign ftp://data.pdbj.org/pub/pdb/validation_reports/ig/1ign | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.57, 0.8216, -0.0054), Vector: Details | MTRIX THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND. APPLIED TO TRANSFORMED TO MTRIX RESIDUES RESIDUES RMSD M1 A 360 .. A 594 B 360 .. B 594 0.62 | |
-Components
#1: DNA chain | Mass: 5673.695 Da / Num. of mol.: 2 / Source method: obtained synthetically #2: DNA chain | Mass: 5939.803 Da / Num. of mol.: 2 / Source method: obtained synthetically #3: Protein | Mass: 28704.143 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Description: T7 PROMOTER / Gene: RAP1 DNA BINDING DOMAIN / Plasmid: PET3C / Gene (production host): RAP1 DNA BINDING DOMAIN 353 TO 598 / Production host: Escherichia coli (E. coli) / References: UniProt: P11938 #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.33 Å3/Da / Density % sol: 49.1 % | |||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal | *PLUS Density % sol: 49.1 % | |||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 6 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Feb 22, 1995 |
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Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.25→16 Å / Num. obs: 33281 / % possible obs: 96 % / Observed criterion σ(I): 4 / Redundancy: 2.9 % / Rmerge(I) obs: 0.047 |
Reflection | *PLUS Highest resolution: 2.25 Å / Lowest resolution: 16 Å / % possible obs: 96 % / Observed criterion σ(I): 4 / Redundancy: 2.9 % / Rmerge(I) obs: 0.047 |
-Processing
Software |
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Refinement | Resolution: 2.25→16 Å / σ(F): 2 Details: ESTIMATED COORD. ERROR 0.426 ANGSTROMS FINAL RMS COORD. SHIFT 0.111 ANGSTROMS
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Displacement parameters | Biso mean: 30 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.35 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.25→16 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.25 Å / Lowest resolution: 16 Å / σ(F): 2 / % reflection Rfree: 5 % / Rfactor obs: 0.219 / Rfactor Rfree: 0.294 / Rfactor Rwork: 0.219 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 30 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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