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Yorodumi- PDB-1vkk: Crystal structure of Glia maturation factor-gamma (GMFG) from Mus... -
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Basic information
| Entry | Database: PDB / ID: 1vkk | ||||||
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| Title | Crystal structure of Glia maturation factor-gamma (GMFG) from Mus musculus at 1.50 A resolution | ||||||
Components | Glia maturation factor gamma | ||||||
Keywords | HORMONE/GROWTH FACTOR / 15079298 / GMFG / GLIA MATURATION FACTOR-GAMMA / STRUCTURAL GENOMICS / JCSG / PROTEIN STRUCTURE INITIATIVE / PSI / Joint Center for Structural Genomics / HORMONE-GROWTH FACTOR COMPLEX | ||||||
| Function / homology | Function and homology informationactin filament debranching / Arp2/3 complex binding / negative regulation of Arp2/3 complex-mediated actin nucleation / Neutrophil degranulation / growth factor activity / actin binding Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.35 Å | ||||||
Authors | Joint Center for Structural Genomics (JCSG) | ||||||
Citation | Journal: To be publishedTitle: Crystal structure of Glia maturation factor-gamma (GMFG) from Mus musculus at 1.50 A resolution Authors: Joint Center for Structural Genomics (JCSG) | ||||||
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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 | 1vkk.cif.gz | 47.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1vkk.ent.gz | 32 KB | Display | PDB format |
| PDBx/mmJSON format | 1vkk.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1vkk_validation.pdf.gz | 430.2 KB | Display | wwPDB validaton report |
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| Full document | 1vkk_full_validation.pdf.gz | 430.4 KB | Display | |
| Data in XML | 1vkk_validation.xml.gz | 9.3 KB | Display | |
| Data in CIF | 1vkk_validation.cif.gz | 13.2 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vk/1vkk ftp://data.pdbj.org/pub/pdb/validation_reports/vk/1vkk | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 1f7sS S: Starting model for refinement |
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| Similar structure data | |
| Other databases |
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Links
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Assembly
| Deposited unit | ![]()
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| Unit cell |
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Components
| #1: Protein | Mass: 18232.957 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #2: Chemical | ChemComp-PO4 / |
| #3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 1.81 Å3/Da / Density % sol: 31.56 % |
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| Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop, nanodrop / pH: 8.5 Details: 30% PEG-4000, 0.1M Tris hydrochloride pH 8.5,0.2M lithium sulfate monohydrate, VAPOR DIFFUSION,SITTING DROP,NANODROP, temperature 277K |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 5.0.3 / Wavelength: 1 |
| Detector | Type: ADSC / Detector: CCD / Date: Oct 8, 2003 |
| Radiation | Monochromator: Single crystal, cylindrically bent, Si(220) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
| Reflection | Resolution: 1.35→35.92 Å / Num. obs: 22189 / % possible obs: 76.6 % / Redundancy: 2.6 % / Biso Wilson estimate: 22.11 Å2 / Rsym value: 0.044 / Net I/σ(I): 16.4 |
| Reflection shell | Resolution: 1.35→1.39 Å / Redundancy: 1.9 % / Mean I/σ(I) obs: 2.2 / Num. unique all: 518 / Rsym value: 0.38 / % possible all: 23.8 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 1f7s Resolution: 1.35→35.92 Å / Cor.coef. Fo:Fc: 0.972 / Cor.coef. Fo:Fc free: 0.959 / SU B: 1.954 / SU ML: 0.04 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.069 / ESU R Free: 0.074 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS 2. ARG 142 SIDE CHAIN CONFORMATION IS SUSPICIOUS. ITS DENSITY IS POOR. 3. THE NOMINAL RESOLUTION IS 1.50 A WITH 2779 OBSERVED REFLECTIONS ...Details: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS 2. ARG 142 SIDE CHAIN CONFORMATION IS SUSPICIOUS. ITS DENSITY IS POOR. 3. THE NOMINAL RESOLUTION IS 1.50 A WITH 2779 OBSERVED REFLECTIONS BETWEEN 1.50-1.35A (35% COMPLETE FOR THIS SHELL) INCLUDED IN THE REFINEMENT. 4. TEMPERATURE FACTORS WERE REFINED AS ISOTROPIC
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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: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 14.682 Å2
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| Refinement step | Cycle: LAST / Resolution: 1.35→35.92 Å
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| Refine LS restraints |
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| LS refinement shell | Resolution: 1.35→1.385 Å / Total num. of bins used: 20
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| Refinement TLS params. | Method: refined / Origin x: -0.052 Å / Origin y: 1.213 Å / Origin z: -1.971 Å
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| Refinement TLS group | Selection: ALL |
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