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Yorodumi- SASDFW4: Conformation of R8-15 human dystrophin fragment (Human dystrophin... -
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-Basic information
Entry | Database: SASBDB / ID: SASDFW4 |
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Sample | Conformation of R8-15 human dystrophin fragment
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Function / homology | Function and homology information regulation of muscle system process / regulation of cellular response to growth factor stimulus / regulation of skeletal muscle contraction / syntrophin complex / synaptic signaling / regulation of voltage-gated calcium channel activity / negative regulation of peptidyl-cysteine S-nitrosylation / cardiac muscle cell action potential / positive regulation of sodium ion transmembrane transporter activity / dystrophin-associated glycoprotein complex ...regulation of muscle system process / regulation of cellular response to growth factor stimulus / regulation of skeletal muscle contraction / syntrophin complex / synaptic signaling / regulation of voltage-gated calcium channel activity / negative regulation of peptidyl-cysteine S-nitrosylation / cardiac muscle cell action potential / positive regulation of sodium ion transmembrane transporter activity / dystrophin-associated glycoprotein complex / cell-substrate junction / peptide biosynthetic process / motile cilium assembly / dystroglycan binding / regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion / vinculin binding / muscle cell development / costamere / neuron projection terminus / Striated Muscle Contraction / filopodium membrane / muscle organ development / structural constituent of muscle / muscle cell cellular homeostasis / myosin binding / maintenance of blood-brain barrier / nitric-oxide synthase binding / negative regulation of peptidyl-serine phosphorylation / Non-integrin membrane-ECM interactions / regulation of ryanodine-sensitive calcium-release channel activity / neuron development / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / cardiac muscle contraction / skeletal muscle tissue development / response to muscle stretch / positive regulation of neuron differentiation / regulation of heart rate / filopodium / structural constituent of cytoskeleton / sarcolemma / Z disc / positive regulation of neuron projection development / protein localization / actin binding / protein-containing complex assembly / postsynaptic membrane / cytoskeleton / membrane raft / synapse / cell surface / protein-containing complex / zinc ion binding / nucleus / plasma membrane / cytosol Similarity search - Function |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Data source
SASBDB page | SASDFW4 |
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-Related structure data
Similar structure data |
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-External links
Related items in Molecule of the Month |
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-Models
Model #2888 | Type: atomic / Chi-square value: 1.819 Search similar-shape structures of this assembly by Omokage search (details) |
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-Sample
Sample | Name: Conformation of R8-15 human dystrophin fragment |
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Buffer | Name: NaP 10 mM, NaCl 500 mM, EDTA 1 mM, Glycerol 2% / pH: 7.5 |
Entity #1554 | Type: protein / Description: Human dystrophin central domain R8-15 fragment / Formula weight: 100.208 / Num. of mol.: 1 / References: UniProt: P11532 Sequence: MSYYHHHHHH DYDIPTTENL YFQGAMDPEF DCGSRKEALK GGLEKTVSLQ KDLSEMHEWM TQAEEEYLER DFEYKTPDEL QKAVEEMKRA KEEAQQKEAK VKLLTESVNS VIAQAPPVAQ EALKKELETL TTNYQWLCTR LNGKCKTLEE VWACWHELLS YLEKANKWLN ...Sequence: MSYYHHHHHH DYDIPTTENL YFQGAMDPEF DCGSRKEALK GGLEKTVSLQ KDLSEMHEWM TQAEEEYLER DFEYKTPDEL QKAVEEMKRA KEEAQQKEAK VKLLTESVNS VIAQAPPVAQ EALKKELETL TTNYQWLCTR LNGKCKTLEE VWACWHELLS YLEKANKWLN EVEFKLKTTE NIPGGAEEIS EVLDSLENLM RHSEDNPNQI RILAQTLTDG GVMDELINEE LETFNSRWRE LHEEAVRRQK LLEQSIQSAQ ETEKSLHLIQ ESLTFIDKQL AAYIADKVDA AQMPQEAQKI QSDLTSHEIS LEEMKKHNQG KEAAQRVLSQ IDVAQKKLQD VSMKFRLFQK PANFELRLQE SKMILDEVKM HLPALETKSV EQEVVQSQLN HCVNLYKSLS EVKSEVEMVI KTGRQIVQKK QTENPKELDE RVTALKLHYN ELGAKVTERK QQLEKCLKLS RKMRKEMNVL TEWLAATDME LTKRSAVEGM PSNLDSEVAW GKATQKEIEK QKVHLKSITE VGEALKTVLG KKETLVEDKL SLLNSNWIAV TSRAEEWLNL LLEYQKHMET FDQNVDHITK WIIQADTLLD ESEKKKPQQK EDVLKRLKAE LNDIRPKVDS TRDQAANLMA NRGDHCRKLV EPQISELNHR FAAISHRIKT GKASIPLKEL EQFNSDIQKL LEPLEAEIQQ GVNLKEEDFN KDMNEDNEGT VKELLQRGDN LQQRITDERK REEIKIKQQL LQTKHNALKD LRSQRRKKAL EISHQWYQYK RQADDLLKCL DDIEKKLASL PEPRDERKIK EIDRELQKKK EELNAVRRQA EGLSEDGAAM AVEPTQIQLS KRWREIESKF AQFRRLNFAQ |
-Experimental information
Beam | Instrument name: SOLEIL SWING / City: Saint-Aubin / 国: France / Type of source: X-ray synchrotron / Wavelength: 0.1033 Å / Dist. spec. to detc.: 1.8 mm | ||||||||||||||||||
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Detector | Name: AVIEX PCCD170170 / Type: CCD | ||||||||||||||||||
Scan | Title: Conformation of R8-15 human dystrophin fragment / Measurement date: Sep 23, 2015 / Cell temperature: 15 °C / Exposure time: 1.5 sec. / Number of frames: 38 / Unit: 1/A /
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Distance distribution function P(R) | Sofotware P(R): GNOM 4.6 / Number of points: 478 /
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Result | Experimental MW: 88 kDa / Type of curve: sec Comments: SEC-SAXS was performed at 15°C using the following parameters: Column: BioSEC5-500Å (4.6 mm id * 300 mm); Flow rate: 0.2 mL/min; Sample injection concentration: 4 mg/mL; Injection volume: ...Comments: SEC-SAXS was performed at 15°C using the following parameters: Column: BioSEC5-500Å (4.6 mm id * 300 mm); Flow rate: 0.2 mL/min; Sample injection concentration: 4 mg/mL; Injection volume: 60μL. The data were collected through the SEC peak of the protein as a series of 38 x 1.5 second exposures. The experimental molecular weight was determined from the volume of correlation, Vc.
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