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- PDB-5wlq: Crystal Structure of Amino Acids 1677-1755 of Human Beta Cardiac ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5wlq | ||||||
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Title | Crystal Structure of Amino Acids 1677-1755 of Human Beta Cardiac Myosin Fused to Gp7 and Eb1 | ||||||
![]() | Capsid assembly scaffolding protein,Myosin-7,Microtubule-associated protein RP/EB family member 1 | ||||||
![]() | MOTOR PROTEIN / Myosin / Gp7 / Coiled-Coil / Eb1 | ||||||
Function / homology | ![]() viral scaffold / protein localization to astral microtubule / regulation of slow-twitch skeletal muscle fiber contraction / cortical microtubule cytoskeleton / regulation of the force of skeletal muscle contraction / mitotic spindle astral microtubule end / protein localization to microtubule / muscle myosin complex / muscle filament sliding / microtubule plus-end ...viral scaffold / protein localization to astral microtubule / regulation of slow-twitch skeletal muscle fiber contraction / cortical microtubule cytoskeleton / regulation of the force of skeletal muscle contraction / mitotic spindle astral microtubule end / protein localization to microtubule / muscle myosin complex / muscle filament sliding / microtubule plus-end / cell projection membrane / transition between fast and slow fiber / regulation of the force of heart contraction / myosin filament / attachment of mitotic spindle microtubules to kinetochore / non-motile cilium assembly / adult heart development / microtubule bundle formation / microtubule plus-end binding / cardiac muscle hypertrophy in response to stress / myosin complex / protein localization to centrosome / ventricular cardiac muscle tissue morphogenesis / microtubule organizing center / negative regulation of microtubule polymerization / myosin II complex / microfilament motor activity / myofibril / sarcomere organization / virion assembly / mitotic spindle pole / microtubule polymerization / cytoplasmic microtubule / establishment of mitotic spindle orientation / skeletal muscle contraction / regulation of microtubule polymerization or depolymerization / spindle assembly / spindle midzone / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / striated muscle contraction / cardiac muscle contraction / stress fiber / ATP metabolic process / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of mitotic centrosome proteins and complexes / positive regulation of microtubule polymerization / Recruitment of NuMA to mitotic centrosomes / Resolution of Sister Chromatid Cohesion / Anchoring of the basal body to the plasma membrane / regulation of heart rate / sarcomere / AURKA Activation by TPX2 / ciliary basal body / muscle contraction / RHO GTPases Activate Formins / protein localization / Z disc / Separation of Sister Chromatids / The role of GTSE1 in G2/M progression after G2 checkpoint / Regulation of PLK1 Activity at G2/M Transition / actin filament binding / cell migration / microtubule / calmodulin binding / cadherin binding / cell division / focal adhesion / centrosome / protein kinase binding / Golgi apparatus / DNA binding / RNA binding / ATP binding / identical protein binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Andreas, M.P. / Ajay, G. / Gellings, J. / Rayment, I. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Design considerations in coiled-coil fusion constructs for the structural determination of a problematic region of the human cardiac myosin rod. Authors: Andreas, M.P. / Ajay, G. / Gellings, J.A. / Rayment, I. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 60.1 KB | Display | ![]() |
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PDB format | ![]() | 42.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 449.3 KB | Display | ![]() |
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Full document | ![]() | 449.8 KB | Display | |
Data in XML | ![]() | 6.3 KB | Display | |
Data in CIF | ![]() | 7.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5wj7C ![]() 5wjbC ![]() 5wlzC ![]() 5wmeC ![]() 1ik9S 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
#1: Protein | Mass: 20781.934 Da / Num. of mol.: 1 Fragment: UNP P13848 residues 2-48 UNP Q15691 residues 208-256, UNP P12883 residues 1677-1755 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Gene: MYH7, MYHCB, MAPRE1 / Production host: ![]() ![]() References: UniProt: P13848, UniProt: P12883, UniProt: Q15691 | ||
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#2: Chemical | ChemComp-SO4 / | ||
#3: Chemical | ChemComp-TMO / #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 6.3 Å3/Da / Density % sol: 80.4 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 9 Details: 1.6 M Ammonium Aulfate, 500 mM Trimethyl Ammonium N-Oxide, 100 mM Bis-tris Propane pH 9.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Dec 7, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97934 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→50 Å / Num. obs: 9815 / % possible obs: 100 % / Redundancy: 19.6 % / Rmerge(I) obs: 0.117 / Net I/σ(I): 24.2 |
Reflection shell | Resolution: 3.1→3.15 Å / Redundancy: 19.5 % / Rmerge(I) obs: 0.667 / Mean I/σ(I) obs: 4.46 / Num. unique obs: 478 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1IK9 Resolution: 3.104→41.161 Å / SU ML: 0.29 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 25.75
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.104→41.161 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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