+Open data
-Basic information
Entry | Database: PDB / ID: 7v9b | ||||||
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Title | Crystal Structure of 14-3-3 epsilon with FOXO3a peptide | ||||||
Components |
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Keywords | PROTEIN BINDING / FOXO3a / 14-3-3 / 14-3-3 epsilon | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.85 Å | ||||||
Authors | Mathivanan, S. / Kamariah, N. | ||||||
Funding support | India, 1items
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Citation | Journal: Acs Omega / Year: 2022 Title: Structure of a 14-3-3 epsilon :FOXO3a pS253 Phosphopeptide Complex Reveals 14-3-3 Isoform-Specific Binding of Forkhead Box Class O Transcription Factor (FOXO) Phosphoproteins. Authors: Mathivanan, S. / Chunchagatta Lakshman, P.K. / Singh, M. / Giridharan, S. / Sathish, K. / Hurakadli, M.A. / Bharatham, K. / Kamariah, N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7v9b.cif.gz | 70.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7v9b.ent.gz | 49.1 KB | Display | PDB format |
PDBx/mmJSON format | 7v9b.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7v9b_validation.pdf.gz | 808.6 KB | Display | wwPDB validaton report |
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Full document | 7v9b_full_validation.pdf.gz | 809.2 KB | Display | |
Data in XML | 7v9b_validation.xml.gz | 12.9 KB | Display | |
Data in CIF | 7v9b_validation.cif.gz | 18.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v9/7v9b ftp://data.pdbj.org/pub/pdb/validation_reports/v9/7v9b | HTTPS FTP |
-Related structure data
Related structure data | 2br9S S: Starting model for refinement |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
-Protein / Protein/peptide , 2 types, 2 molecules AB
#1: Protein | Mass: 28281.205 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: YWHAE/FAM22B fusion / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: G9K389 |
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#2: Protein/peptide | Mass: 1388.429 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: TAMRA Labeled peptide / Source: (synth.) Homo sapiens (human) |
-Non-polymers , 5 types, 166 molecules
#3: Chemical | #4: Chemical | ChemComp-MPD / ( | #5: Chemical | ChemComp-IMD / | #6: Chemical | ChemComp-323 / | #7: Water | ChemComp-HOH / | |
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-Details
Has ligand of interest | Y |
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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: 2.35 Å3/Da / Density % sol: 47.66 % |
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Crystal grow | Temperature: 289.15 K / Method: vapor diffusion, hanging drop / pH: 8 / Details: 0.1 M Imidazole pH 8.0, 10 % PEG 4000, 30 % MPD |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: RRCAT INDUS-2 / Beamline: PX-BL21 / Wavelength: 0.97947 Å |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Mar 12, 2020 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97947 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→36.46 Å / Num. obs: 22570 / % possible obs: 99.4 % / Redundancy: 6.2 % / Biso Wilson estimate: 19.4 Å2 / CC1/2: 0.994 / Rmerge(I) obs: 0.12 / Rpim(I) all: 0.052 / Rrim(I) all: 0.131 / Rsym value: 0.12 / Net I/σ(I): 9.8 |
Reflection shell | Resolution: 1.85→1.95 Å / Redundancy: 5.8 % / Rmerge(I) obs: 0.743 / Mean I/σ(I) obs: 2.6 / Num. unique obs: 3185 / CC1/2: 0.773 / Rpim(I) all: 0.33 / Rrim(I) all: 0.815 / Rsym value: 0.743 / % possible all: 98.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2BR9 Resolution: 1.85→36.46 Å / Cor.coef. Fo:Fc: 0.961 / Cor.coef. Fo:Fc free: 0.951 / SU B: 2.787 / SU ML: 0.08 / Cross valid method: THROUGHOUT / ESU R: 0.129 / ESU R Free: 0.113 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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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: 24.092 Å2
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Refinement step | Cycle: 1 / Resolution: 1.85→36.46 Å
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