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Open data
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Basic information
Entry | Database: PDB / ID: 1fhg | ||||||
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Title | HIGH RESOLUTION REFINEMENT OF TELOKIN | ||||||
![]() | TELOKIN | ||||||
![]() | CONTRACTILE PROTEIN / immunoglobulin fold / beta barrel | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Tomchick, D.R. / Minor, W. / Kiyatkin, A. / Lewinski, K. / Somlyo, A.V. / Somlyo, A.P. | ||||||
![]() | ![]() Title: X-ray structure determination of telokin, the C-terminal domain of myosin light chain kinase, at 2.8 A resolution. Authors: Holden, H.M. / Ito, M. / Hartshorne, D.J. / Rayment, I. #1: ![]() Title: X-Ray Structure Determination of Telokin, the C-terminal Domain of Myosin Light Chain Kinase, at 2.8 Angstroms Resolution Authors: Holden, H.M. / Ito, M. / Hartshorne, D.J. / Rayment, I. #2: ![]() Title: Regulation of the Cross-bridge Cycle: the Effects of MgADP, LC17 Isoforms and Telokin. Authors: Somlyo, A.V. / Matthew, J.D. / Wu, X. / Khromov, A.S. / Somlyo, A.P. #3: ![]() Title: Acceleration of Myosin Light Chain Dephosphorylation and Relaxation of Smooth Muscle by Telokin. Synergism with Cyclic Nucleotide-activated Kinase. Authors: Wu, X. / Haystead, T.A. / Nakamoto, R.K. / Somlyo, A.V. / Somlyo, A.P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 35.2 KB | Display | ![]() |
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PDB format | ![]() | 22.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 421.7 KB | Display | ![]() |
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Full document | ![]() | 423.3 KB | Display | |
Data in XML | ![]() | 7.2 KB | Display | |
Data in CIF | ![]() | 9.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1tlkSC S: Starting model for refinement C: citing same article ( |
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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 on special symmetry positions |
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Components
#1: Protein | Mass: 16974.352 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.03 Å3/Da / Density % sol: 30 % |
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Crystal grow | Temperature: 273 K / Method: vapor diffusion, sitting drop / pH: 4 Details: PEG6000, sodium acetate, pH 4.0, VAPOR DIFFUSION, SITTING DROP, temperature 273.0K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Detector: CCD / Date: Sep 1, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.98→20 Å / Num. all: 9904 / Num. obs: 9904 / % possible obs: 99.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 10.5 % / Biso Wilson estimate: 47.3 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 35.7 |
Reflection shell | Resolution: 1.98→2.05 Å / Redundancy: 4.7 % / Rmerge(I) obs: 0.574 / Mean I/σ(I) obs: 2.34 / Num. unique all: 967 / % possible all: 99.6 |
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Processing
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Refinement | Method to determine structure: IR Starting model: 1tlk Resolution: 2→20 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Bsol: 52.72 Å2 / ksol: 0.369 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 42.95 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.07 Å / Total num. of bins used: 10
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Xplor file | Serial no: 1 / Param file: protein_rep.param / Topol file: protein.top |