+Open data
-Basic information
Entry | Database: PDB / ID: 4abn | ||||||
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Title | Crystal structure of full length mouse Strap (TTC5) | ||||||
Components | TETRATRICOPEPTIDE REPEAT PROTEIN 5 | ||||||
Keywords | GENE REGULATION / P53 COFACTOR / STRESS-RESPONSE / DNA REPAIR | ||||||
Function / homology | Function and homology information Regulation of TP53 Activity through Methylation / DNA repair / chromatin binding / positive regulation of transcription by RNA polymerase II / DNA binding / nucleoplasm / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | MUS MUSCULUS (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.05 Å | ||||||
Authors | Pike, A.C.W. / Bullock, A.N. / Kleinekofort, W. / Zimmermann, T. / Burgess-Brown, N. / Sharpe, T.D. / Thangaratnarajah, C. / Keates, T. / Ugochukwu, E. / Bunkoczi, G. ...Pike, A.C.W. / Bullock, A.N. / Kleinekofort, W. / Zimmermann, T. / Burgess-Brown, N. / Sharpe, T.D. / Thangaratnarajah, C. / Keates, T. / Ugochukwu, E. / Bunkoczi, G. / Uppenberg, J. / von Delft, F. / Arrowsmith, C.H. / Weigelt, J. / Edwards, A. / Bountra, C. / La Thangue, N.B. / Knapp, S. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2012 Title: The P53 Cofactor Strap Exhibits an Unexpected Tpr Motif and Oligonucleotide-Binding (Ob)-Fold Structure. Authors: Adams, C.J. / Pike, A.C. / Maniam, S. / Sharpe, T.D. / Coutts, A.S. / Knapp, S. / La Thangue, N.B. / Bullock, A.N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4abn.cif.gz | 346.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4abn.ent.gz | 284.1 KB | Display | PDB format |
PDBx/mmJSON format | 4abn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ab/4abn ftp://data.pdbj.org/pub/pdb/validation_reports/ab/4abn | HTTPS FTP |
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-Related structure data
-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: (1, -0.008, -0.014), Vector: |
-Components
#1: Protein | Mass: 52408.031 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) MUS MUSCULUS (house mouse) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): R3 / References: UniProt: Q99LG4 #2: Chemical | #3: Water | ChemComp-HOH / | Sequence details | A120T, V256A SEQUENCE CONFLICTS AS DOCUMENTED | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 49 % / Description: NONE |
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Crystal grow | pH: 8.5 / Details: 0.1 M TRIS PH 8.5, 25% TERT-BUTANOL |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.97892 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Sep 22, 2007 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97892 Å / Relative weight: 1 |
Reflection | Resolution: 2.05→55.22 Å / Num. obs: 62502 / % possible obs: 99.9 % / Observed criterion σ(I): 0 / Redundancy: 3.7 % / Biso Wilson estimate: 31.5 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 10.7 |
Reflection shell | Resolution: 2.05→2.16 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.6 / Mean I/σ(I) obs: 2.1 / % possible all: 99.4 |
-Processing
Software |
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Refinement | Method to determine structure: SAD Starting model: NONE Resolution: 2.05→55 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.936 / SU B: 9.086 / SU ML: 0.123 / Cross valid method: THROUGHOUT / ESU R: 0.188 / ESU R Free: 0.168 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES WITH TLS ADDED. LOCAL NCS RESTRAINTS USED.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 37.22 Å2
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Refinement step | Cycle: LAST / Resolution: 2.05→55 Å
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Refine LS restraints |
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