+Open data
-Basic information
Entry | Database: PDB / ID: 4age | ||||||
---|---|---|---|---|---|---|---|
Title | MTSSL spin labeled D67C mutant of MscS in the open form | ||||||
Components | SMALL-CONDUCTANCE MECHANOSENSITIVE CHANNEL | ||||||
Keywords | TRANSPORT PROTEIN | ||||||
Function / homology | Function and homology information intracellular water homeostasis / mechanosensitive monoatomic ion channel activity / monoatomic ion transmembrane transport / protein homooligomerization / membrane / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | ESCHERICHIA COLI (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4.84 Å | ||||||
Authors | Pliotas, C. / Brannigan, E. / Naismith, J.H. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2012 Title: Conformational State of the Mscs Mechanosensitive Channel in Solution Revealed by Pulsed Electron-Electron Double Resonance (Peldor) Spectroscopy. Authors: Pliotas, C. / Ward, R. / Branigan, E. / Rasmussen, A. / Hagelueken, G. / Huang, H. / Black, S.S. / Booth, I.R. / Schiemann, O. / Naismith, J.H. | ||||||
History |
| ||||||
Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 35-STRANDED BARREL THIS IS REPRESENTED BY A 36-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "AC" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 7-STRANDED BARREL THIS IS REPRESENTED BY A 8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 4age.cif.gz | 324.7 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb4age.ent.gz | 266.9 KB | Display | PDB format |
PDBx/mmJSON format | 4age.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ag/4age ftp://data.pdbj.org/pub/pdb/validation_reports/ag/4age | HTTPS FTP |
---|
-Related structure data
Related structure data | 4agfC 2vv5S S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 30910.957 Da / Num. of mol.: 7 / Mutation: YES Source method: isolated from a genetically manipulated source Details: THE PROTEIN IS SPIN LABELED ON D67C. / Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P0C0S2, UniProt: P0C0S1*PLUS Compound details | ENGINEERED RESIDUE IN CHAIN A, ASP 67 TO CYS ENGINEERED RESIDUE IN CHAIN B, ASP 67 TO CYS ...ENGINEERED | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 4.33 Å3/Da / Density % sol: 71.34 % / Description: NONE |
---|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.9173 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Jul 1, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9173 Å / Relative weight: 1 |
Reflection | Resolution: 4.84→22 Å / Num. obs: 16401 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 13 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 16 |
Reflection shell | Resolution: 4.84→4.97 Å / Redundancy: 13 % / Rmerge(I) obs: 0.68 / Mean I/σ(I) obs: 4.4 / % possible all: 100 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2VV5 Resolution: 4.84→102.7 Å / Cor.coef. Fo:Fc: 0.801 / Cor.coef. Fo:Fc free: 0.771 / SU B: 114.27 / SU ML: 1.319 / Cross valid method: THROUGHOUT / ESU R Free: 1.638 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY. D67C, REFINED USED JELLY BODY, NCS LOCAL RESTRAINTS.
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.1 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 92.577 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 4.84→102.7 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|