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Yorodumi- PDB-2xtp: Crystal structure of nucleotide-free human GIMAP2, amino acid res... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 2xtp | ||||||
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| Title | Crystal structure of nucleotide-free human GIMAP2, amino acid residues 1-260 | ||||||
Components | GTPASE IMAP FAMILY MEMBER 2 | ||||||
Keywords | IMMUNE SYSTEM / G PROTEIN | ||||||
| Function / homology | Function and homology informationlipid droplet / GTP binding / endoplasmic reticulum / nucleoplasm / identical protein binding Similarity search - Function | ||||||
| Biological species | HOMO SAPIENS (human) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.5 Å | ||||||
Authors | Schwefel, D. / Froehlich, C. / Daumke, O. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2010Title: Structural Basis of Oligomerization in Septin-Like Gtpase of Immunity-Associated Protein 2 (Gimap2) Authors: Schwefel, D. / Froehlich, C. / Eichhorst, J. / Wiesner, B. / Behlke, J. / Aravind, L. / Daumke, O. #1: Journal: Acta Crystallogr.,Sect.F / Year: 2010 Title: Purification, Crystallization and Preliminary X- Ray Analysis of Human Gimap2. Authors: Schwefel, D. / Frohlich, C. / Daumke, O. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 2xtp.cif.gz | 101.6 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb2xtp.ent.gz | 79.2 KB | Display | PDB format |
| PDBx/mmJSON format | 2xtp.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 2xtp_validation.pdf.gz | 406.9 KB | Display | wwPDB validaton report |
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| Full document | 2xtp_full_validation.pdf.gz | 409 KB | Display | |
| Data in XML | 2xtp_validation.xml.gz | 13.2 KB | Display | |
| Data in CIF | 2xtp_validation.cif.gz | 18.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xt/2xtp ftp://data.pdbj.org/pub/pdb/validation_reports/xt/2xtp | HTTPS FTP |
-Related structure data
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| Unit cell |
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Components
| #1: Protein | Mass: 29354.859 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-260 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PGEX6P1 / Production host: ![]() |
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| #2: Water | ChemComp-HOH / |
| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.62 % / Description: NONE |
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| Crystal grow | pH: 7.5 / Details: 11-12% 2-PROPANOL, 15% GLYCEROL, pH 7.5 |
-Data collection
| Diffraction | Mean temperature: 100 K | |||||||||
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| Diffraction source | Source: SYNCHROTRON / Site: BESSY / Beamline: 14.2 / Wavelength: 0.9797, 0.9849 | |||||||||
| Detector | Type: MARRESEARCH / Detector: CCD / Date: Jan 23, 2008 | |||||||||
| Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||
| Radiation wavelength |
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| Reflection | Resolution: 1.75→50 Å / Num. obs: 183804 / % possible obs: 99.1 % / Observed criterion σ(I): 1 / Redundancy: 3.8 % / Biso Wilson estimate: 26.9 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 14.6 | |||||||||
| Reflection shell | Resolution: 1.75→1.8 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.5 / Mean I/σ(I) obs: 3.2 / % possible all: 95.9 |
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Processing
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| Refinement | Method to determine structure: SADStarting model: NONE Resolution: 1.5→19.14 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.951 / SU B: 2.353 / SU ML: 0.04 / Cross valid method: THROUGHOUT / ESU R: 0.069 / ESU R Free: 0.07 / 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: 12.251 Å2
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| Refinement step | Cycle: LAST / Resolution: 1.5→19.14 Å
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| Refine LS restraints |
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HOMO SAPIENS (human)
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