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Open data
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Basic information
| Entry | Database: PDB / ID: 1msp | ||||||
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| Title | MAJOR SPERM PROTEIN, ALPHA ISOFORM (RECOMBINANT), PH 4.6 | ||||||
Components | MAJOR SPERM PROTEIN | ||||||
Keywords | CELL MOTILITY PROTEIN / CYTOSKELETAL PROTEIN / SPERM | ||||||
| Function / homology | Function and homology information | ||||||
| Biological species | Ascaris suum (pig roundworm) | ||||||
| Method | X-RAY DIFFRACTION / Resolution: 2.5 Å | ||||||
Authors | Bullock, T.L. / Roberts, T.M. / Stewart, M. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1996Title: 2.5 A resolution crystal structure of the motile major sperm protein (MSP) of Ascaris suum. Authors: Bullock, T.L. / Roberts, T.M. / Stewart, M. #1: Journal: Cell(Cambridge,Mass.) / Year: 1996Title: Worm Sperm and Advances in Cell Locomotion Authors: Theriot, J.A. #2: Journal: J.Struct.Biol. / Year: 1996Title: New Crystal Forms of the Motile Major Sperm Protein (Msp) of Ascaris Suum Authors: Bullock, T.L. / Parthasarathy, G. / King, K.L. / Kent, H.M. / Roberts, T.M. / Stewart, M. #3: Journal: Curr.Opin.Cell Biol. / Year: 1995Title: Nematode Sperm Locomotion Authors: Roberts, T.M. / Stewart, M. | ||||||
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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 | 1msp.cif.gz | 60.3 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1msp.ent.gz | 44.2 KB | Display | PDB format |
| PDBx/mmJSON format | 1msp.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1msp_validation.pdf.gz | 374.6 KB | Display | wwPDB validaton report |
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| Full document | 1msp_full_validation.pdf.gz | 392.4 KB | Display | |
| Data in XML | 1msp_validation.xml.gz | 8.8 KB | Display | |
| Data in CIF | 1msp_validation.cif.gz | 12.9 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ms/1msp ftp://data.pdbj.org/pub/pdb/validation_reports/ms/1msp | HTTPS FTP |
-Related structure data
| Similar 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: 14278.107 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: ALPHA ISOFORM, PH 4.6 / Source: (gene. exp.) Ascaris suum (pig roundworm) / Cell: SPERM CELL / Gene: ALPHA MSP / Plasmid: PET11D / Species (production host): Escherichia coli / Gene (production host): ALPHA MSP / Production host: ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION |
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Sample preparation
| Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 50 % | ||||||||||||||||||||
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| Crystal grow | pH: 4.6 / Details: pH 4.6 | ||||||||||||||||||||
| Crystal grow | *PLUS Method: vapor diffusion | ||||||||||||||||||||
| Components of the solutions | *PLUS
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-Data collection
| Diffraction source | Wavelength: 1.5418 |
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| Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
| Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
| Reflection | Num. obs: 8858 / % possible obs: 95 % / Observed criterion σ(I): 0 / Redundancy: 1.9 % / Rmerge(I) obs: 0.046 |
| Reflection | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 21 Å |
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Processing
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| Refinement | Resolution: 2.5→20 Å / Num. reflection obs: 8478 / σ(F): 0 / Stereochemistry target values: TNT | ||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 2.5→20 Å
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| Refine LS restraints |
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| Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||
| Refinement | *PLUS Lowest resolution: 21 Å / % reflection Rfree: 5 % / Rfactor obs: 0.195 / Rfactor Rfree: 0.292 | ||||||||||||||||||||||||||||||||||||||||
| Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||
| Refine LS restraints | *PLUS
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Ascaris suum (pig roundworm)
X-RAY DIFFRACTION
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