+Open data
-Basic information
Entry | Database: PDB / ID: 4p7h | |||||||||
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Title | Structure of Human beta-Cardiac Myosin Motor Domain::GFP chimera | |||||||||
Components | Myosin-7,Green fluorescent protein | |||||||||
Keywords | Motor/Fluorescent Protein / Cardiac / Motor / Motor-Fluorescent Protein Complex | |||||||||
Function / homology | Function and homology information regulation of slow-twitch skeletal muscle fiber contraction / regulation of the force of skeletal muscle contraction / muscle myosin complex / muscle filament sliding / regulation of the force of heart contraction / transition between fast and slow fiber / myosin filament / myosin II complex / adult heart development / cardiac muscle hypertrophy in response to stress ...regulation of slow-twitch skeletal muscle fiber contraction / regulation of the force of skeletal muscle contraction / muscle myosin complex / muscle filament sliding / regulation of the force of heart contraction / transition between fast and slow fiber / myosin filament / myosin II complex / adult heart development / cardiac muscle hypertrophy in response to stress / myosin complex / sarcomere organization / microfilament motor activity / ventricular cardiac muscle tissue morphogenesis / myofibril / skeletal muscle contraction / striated muscle contraction / ATP metabolic process / stress fiber / cardiac muscle contraction / regulation of heart rate / sarcomere / bioluminescence / muscle contraction / generation of precursor metabolites and energy / Z disc / actin filament binding / calmodulin binding / ATP binding / cytoplasm Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) Aequorea victoria (jellyfish) | |||||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 3.2 Å | |||||||||
Authors | Winkelmann, D.A. / Miller, M.T. / Stock, A.M. | |||||||||
Funding support | United States, 1items
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Citation | Journal: Mol. Biol. Cell / Year: 2011 Title: Structure of Human beta-Cardiac Myosin Motor Domain at 3.2 A Authors: Winkelmann, D.A. / Miller, M.T. / Stock, A.M. / Liu, L. #1: Journal: J.Biol.Chem. / Year: 2002 Title: Folding of the striated muscle myosin motor domain. Authors: Chow, D. / Srikakulam, R. / Chen, Y. / Winkelmann, D.A. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4p7h.cif.gz | 392.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4p7h.ent.gz | 314.4 KB | Display | PDB format |
PDBx/mmJSON format | 4p7h.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/p7/4p7h ftp://data.pdbj.org/pub/pdb/validation_reports/p7/4p7h | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 116468.672 Da / Num. of mol.: 2 Fragment: UNP P12883 residues 1-787,UNP P42212 residues 5-238 Mutation: Q80R, K101N, V163A, I167T, S175G, D190N Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human), (gene. exp.) Aequorea victoria (jellyfish) Tissue: muscleSkeletal muscle / Gene: MYH7, MYHCB, GFP / Organ: heart / Cell (production host): myoblast / Cell line (production host): C2C12 / Organ (production host): skeletal muscle / Production host: Mus (mice) / Tissue (production host): muscle / References: UniProt: P12883, UniProt: P42212 #2: Chemical | #3: Water | ChemComp-HOH / | Sequence details | The mutations in GFP were engineered to enhance folding | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.67 Å3/Da / Density % sol: 53.95 % / Description: small orthorhombic crystals with green tint |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6 Details: 10% Tacsimate, pH 6.0, 10% glycerol, 14-15% PEG 3350, 0.2 mM MgCL2, and 5 mM TCEP PH range: 5.8-6.2 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.54056 Å |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: May 25, 2011 / Details: Varimax HR |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54056 Å / Relative weight: 1 |
Reflection | Resolution: 3.2→39.56 Å / Num. obs: 36487 / % possible obs: 90.4 % / Redundancy: 6.7 % / Net I/σ(I): 8.1 |
Reflection shell | Resolution: 3.2→3.37 Å / Redundancy: 6.6 % / Mean I/σ(I) obs: 1.8 / % possible all: 81.2 |
-Processing
Software | Name: PHENIX / Version: (phenix.refine: 1.8.4_1496) / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entries 2MYS, 2QLE Resolution: 3.2→37.939 Å / SU ML: 0.5 / Cross valid method: FREE R-VALUE / σ(F): 1.96 / Phase error: 30.65 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.8 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.2→37.939 Å
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Refine LS restraints |
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LS refinement shell |
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