+Open data
-Basic information
Entry | Database: PDB / ID: 1grw | ||||||
---|---|---|---|---|---|---|---|
Title | C. elegans major sperm protein | ||||||
Components | MAJOR SPERM PROTEIN 31/40/142 | ||||||
Keywords | CYTOSKETAL PROTEIN / CYTOSKELETON / SPERM / CELL MOTILITY | ||||||
Function / homology | Function and homology information | ||||||
Biological species | CAENORHABDITIS ELEGANS (invertebrata) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å | ||||||
Authors | Baker, A.M.E. / Roberts, T.M. / Stewart, M. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2002 Title: 2.6 A Resolution Crystal Structure of Helices of the Motile Major Sperm Protein (Msp) of Caenorhabditis Elegans Authors: Baker, A.M.E. / Roberts, T.M. / Stewart, M. | ||||||
History |
| ||||||
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 |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1grw.cif.gz | 111.7 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1grw.ent.gz | 86.4 KB | Display | PDB format |
PDBx/mmJSON format | 1grw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1grw_validation.pdf.gz | 454.4 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1grw_full_validation.pdf.gz | 472.1 KB | Display | |
Data in XML | 1grw_validation.xml.gz | 22.5 KB | Display | |
Data in CIF | 1grw_validation.cif.gz | 30.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gr/1grw ftp://data.pdbj.org/pub/pdb/validation_reports/gr/1grw | HTTPS FTP |
-Related structure data
Related structure data | 2mspS S: Starting model for refinement |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||||||||||
2 |
| ||||||||||||||||
3 |
| ||||||||||||||||
4 |
| ||||||||||||||||
Unit cell |
| ||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
|
-Components
#1: Protein | Mass: 14095.839 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) CAENORHABDITIS ELEGANS (invertebrata) / Cell: SPERM / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): PLYSS / References: UniProt: P53017 #2: Water | ChemComp-HOH / | Compound details | PROTEIN IS AN IMPORTANT COMPONENT IN THE MOLECULAR INTERACTIO | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.9 Å3/Da / Density % sol: 51.6 % | ||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 293 K / Method: vapor diffusion / pH: 5 Details: VAPOUR DIFFUSION AT 20DEGC IN 16% PEG 8000, 100 MM NA ACETATE BUFFER PH5.0, pH 5.00 | ||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion | ||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-3 / Type: ESRF / Wavelength: 0.9311 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Feb 5, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9311 Å / Relative weight: 1 |
Reflection | Resolution: 2.43→37.8 Å / Num. obs: 24601 / % possible obs: 98 % / Redundancy: 3.66 % / Rmerge(I) obs: 0.088 / Net I/σ(I): 6.3039 |
Reflection shell | Resolution: 2.43→2.56 Å / Redundancy: 2.4 % / Rmerge(I) obs: 0.54 / Mean I/σ(I) obs: 1 / % possible all: 87.6 |
Reflection | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 38 Å / Num. obs: 21887 / % possible obs: 97.7 % / Redundancy: 3.9 % / Rmerge(I) obs: 0.072 |
Reflection shell | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 2.74 Å / % possible obs: 97.7 % / Redundancy: 3.8 % / Rmerge(I) obs: 0.359 / Mean I/σ(I) obs: 1.9 |
-Processing
Software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2MSP Resolution: 2.6→20 Å / SU B: 10.38 / SU ML: 0.219 / Cross valid method: THROUGHOUT / ESU R: 0.507 / ESU R Free: 0.291 / Details: NONE
| ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.6→20 Å
| ||||||||||||||||||||
Software | *PLUS Name: REFMAC / Version: '4.0.0 01/12/1999' / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.228 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
|