+Open data
-Basic information
Entry | Database: PDB / ID: 2bvu | ||||||
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Title | D83R mutant of Asaris suum major sperm protein (MSP) | ||||||
Components | MAJOR SPERM PROTEIN, ISOFORM ALPHA | ||||||
Keywords | STRUCTURAL PROTEIN / CYTOSKETAL PROTEIN / MAJOR SPERM PROTEIN | ||||||
Function / homology | Function and homology information | ||||||
Biological species | ASCARIS SUUM (pig roundworm) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å | ||||||
Authors | Stewart, M. / Grant, R.P. / Roberts, T.M. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2008 Title: The Role of Filament-Packing Dynamics in Powering Amoeboid Cell Motility. Authors: Miao, L. / Vanderlinde, O. / Liu, J. / Grant, R.P. / Wouterse, A. / Shimabukuro, K. / Philipse, A. / Stewart, M. / Roberts, T.M. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2bvu.cif.gz | 110.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2bvu.ent.gz | 86.3 KB | Display | PDB format |
PDBx/mmJSON format | 2bvu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bv/2bvu ftp://data.pdbj.org/pub/pdb/validation_reports/bv/2bvu | HTTPS FTP |
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-Related structure data
Related structure data | 1grwS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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3 |
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4 |
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Unit cell |
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-Components
#1: Protein | Mass: 14320.215 Da / Num. of mol.: 4 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ASCARIS SUUM (pig roundworm) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): PET / References: UniProt: P27439 #2: Water | ChemComp-HOH / | Compound details | ENGINEERED RESIDUE IN CHAIN A, ASP 83 TO ARG ENGINEERED RESIDUE IN CHAIN B, ASP 83 TO ARG ...ENGINEERED | |
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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: 2.97 Å3/Da / Density % sol: 58.59 % |
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Crystal grow | Details: PROTEIN 5 MG/ML; 15% PEG4000; 0.1M AMMONIUM ACETATE (PH 5.9); 2% AMMONIUM SULPHATE; 10 MM DTT |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SRS / Beamline: PX14.1 / Wavelength: 1.488 |
Detector | Type: ADSC / Date: Sep 18, 2003 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.488 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→20 Å / Num. obs: 17093 / % possible obs: 93.3 % / Redundancy: 7.7 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 19.9 |
Reflection shell | Resolution: 2.5→2.56 Å / Redundancy: 6.2 % / Rmerge(I) obs: 0.34 / Mean I/σ(I) obs: 4.7 / % possible all: 78.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1GRW Resolution: 2.5→20 Å / Cor.coef. Fo:Fc: 0.937 / Cor.coef. Fo:Fc free: 0.889 / SU B: 11.914 / SU ML: 0.252 / Cross valid method: THROUGHOUT / ESU R: 0.466 / ESU R Free: 0.32 / 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: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 56.07 Å2
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Refinement step | Cycle: LAST / Resolution: 2.5→20 Å
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Refine LS restraints |
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