+Open data
-Basic information
Entry | Database: PDB / ID: 2nlj | ||||||
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Title | Potassium Channel KcsA(M96V)-Fab complex in KCl | ||||||
Components |
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Keywords | MEMBRANE PROTEIN / Voltage-gated channel / Transmembrane / Ionic channel / Ion transport / K Channel / protein-antibody Fab complex | ||||||
Function / homology | Function and homology information delayed rectifier potassium channel activity / voltage-gated potassium channel complex / identical protein binding Similarity search - Function | ||||||
Biological species | Streptomyces lividans (bacteria) Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.52 Å | ||||||
Authors | Lockless, S.W. / Zhou, M. / MacKinnon, R. | ||||||
Citation | Journal: Plos Biol. / Year: 2007 Title: Structural and Thermodynamic Properties of Selective Ion Binding in a K(+) Channel. Authors: Lockless, S.W. / Zhou, M. / Mackinnon, R. | ||||||
History |
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Remark 999 | SEQUENCE Sequencing of the DNA construct shows that position 2 of chain C is an ALA. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2nlj.cif.gz | 117.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2nlj.ent.gz | 88.3 KB | Display | PDB format |
PDBx/mmJSON format | 2nlj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nl/2nlj ftp://data.pdbj.org/pub/pdb/validation_reports/nl/2nlj | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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Details | The biological assembly is generated from the following operators: x,y,z -x+2,-y+2,z y,-x+2,z -y+2,x,z |
-Components
-Protein , 1 types, 1 molecules C
#3: Protein | Mass: 13179.518 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-124 / Mutation: L90C, M96V Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptomyces lividans (bacteria) / Gene: kcsA, skc1 / Plasmid: pQE-60 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL-21(DE3) / References: UniProt: P0A334 |
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-Antibody , 2 types, 2 molecules AB
#1: Antibody | Mass: 23435.738 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse) |
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#2: Antibody | Mass: 23411.242 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse) |
-Non-polymers , 3 types, 125 molecules
#4: Chemical | ChemComp-DGA / | ||
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#5: Chemical | #6: 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: 3.8 Å3/Da / Density % sol: 67.66 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: PEG400, Magnesium Acetate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 200 K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: A1 / Wavelength: 0.9349 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: May 11, 2002 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.9349 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.5→30 Å / Num. obs: 29644 / % possible obs: 96.6 % / Rmerge(I) obs: 0.108 / Χ2: 1.105 / Net I/σ(I): 11 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.52→27.47 Å / Rfactor Rfree error: 0.007 / FOM work R set: 0.827 / Data cutoff high absF: 2183017.5 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 40.179 Å2 / ksol: 0.304 e/Å3 | |||||||||||||||||||||||||||
Displacement parameters | Biso mean: 50.5 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.52→27.47 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.5→2.66 Å / Rfactor Rfree error: 0.02 / Total num. of bins used: 6
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Xplor file |
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