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- PDB-6umx: Structural basis for specific inhibition of extracellular activat... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6umx | ||||||
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Title | Structural basis for specific inhibition of extracellular activation of pro/latent myostatin by SRK-015 | ||||||
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![]() | SIGNALING PROTEIN/IMMUNE SYSTEM / Myostatin / GDF8 / transforming growth factor beta / muscle wasting disease / antibody / fab / SIGNALING PROTEIN-IMMUNE SYSTEM complex | ||||||
Function / homology | ![]() negative regulation of muscle hypertrophy / negative regulation of skeletal muscle tissue growth / negative regulation of myoblast proliferation / skeletal muscle satellite cell differentiation / negative regulation of satellite cell differentiation / myoblast migration involved in skeletal muscle regeneration / negative regulation of skeletal muscle satellite cell proliferation / skeletal muscle atrophy / ovulation cycle process / FOXO-mediated transcription of cell cycle genes ...negative regulation of muscle hypertrophy / negative regulation of skeletal muscle tissue growth / negative regulation of myoblast proliferation / skeletal muscle satellite cell differentiation / negative regulation of satellite cell differentiation / myoblast migration involved in skeletal muscle regeneration / negative regulation of skeletal muscle satellite cell proliferation / skeletal muscle atrophy / ovulation cycle process / FOXO-mediated transcription of cell cycle genes / response to gravity / negative regulation of myoblast differentiation / CD22 mediated BCR regulation / IgG immunoglobulin complex / response to muscle activity / Fc epsilon receptor (FCERI) signaling / muscle organ development / Classical antibody-mediated complement activation / muscle cell cellular homeostasis / Initial triggering of complement / positive regulation of macrophage chemotaxis / response to testosterone / FCGR activation / immunoglobulin mediated immune response / negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / Role of phospholipids in phagocytosis / Role of LAT2/NTAL/LAB on calcium mobilization / Scavenging of heme from plasma / positive regulation of lamellipodium assembly / response to electrical stimulus / negative regulation of insulin receptor signaling pathway / FCERI mediated Ca+2 mobilization / cellular response to dexamethasone stimulus / FCGR3A-mediated IL10 synthesis / transforming growth factor beta receptor signaling pathway / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / cytokine activity / Regulation of Complement cascade / Cell surface interactions at the vascular wall / FCERI mediated MAPK activation / FCGR3A-mediated phagocytosis / antigen binding / growth factor activity / Regulation of actin dynamics for phagocytic cup formation / FCERI mediated NF-kB activation / response to estrogen / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / heparin binding / cellular response to hypoxia / response to ethanol / Potential therapeutics for SARS / blood microparticle / signaling receptor binding / positive regulation of DNA-templated transcription / protein homodimerization activity / extracellular space / extracellular exosome / extracellular region / identical protein binding / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Dagbay, K.B. / Treece, E. / Streich Jr., F.C. / Jackson, J.W. / Faucette, R.R. / Nikiforov, A. / Lin, S.C. / Bostion, C.J. / Nicholls, S.B. / Capili, A.D. / Carven, G.J. | ||||||
![]() | ![]() Title: Structural basis of specific inhibition of extracellular activation of pro- or latent myostatin by the monoclonal antibody SRK-015. Authors: Dagbay, K.B. / Treece, E. / Streich Jr., F.C. / Jackson, J.W. / Faucette, R.R. / Nikiforov, A. / Lin, S.C. / Boston, C.J. / Nicholls, S.B. / Capili, A.D. / Carven, G.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 560.6 KB | Display | ![]() |
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PDB format | ![]() | 467.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 266.3 KB | Display | ![]() |
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Full document | ![]() | 266.3 KB | Display | |
Data in XML | ![]() | 1.4 KB | Display | |
Data in CIF | ![]() | 14.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3hh2S ![]() 3rjrS ![]() 5f3hS ![]() 5gguS ![]() 5ntuS S: Starting model for refinement |
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Similar structure data |
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: _ / Refine code: _
NCS ensembles :
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Components
#1: Protein | Mass: 41642.332 Da / Num. of mol.: 2 / Fragment: UNP residues 24-375 / Mutation: D99A, R263A, R266A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Antibody | Mass: 22655.908 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #3: Antibody | Mass: 24725.869 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #4: Chemical | ChemComp-GOL / | #5: Water | ChemComp-HOH / | Has ligand of interest | N | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 54.46 % |
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Crystal grow | Temperature: 296 K / Method: vapor diffusion, sitting drop / pH: 5.5 Details: 0.1 M sodium citrate, pH 5.5, 20% PEG3350, 15% 2-propanol, 3% trimethylamine N-oxide |
-Data collection
Diffraction | Mean temperature: 93 K / Serial crystal experiment: N | |||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | |||||||||||||||||||||
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Aug 22, 2017 | |||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 | |||||||||||||||||||||
Reflection | Resolution: 2.79→146.63 Å / Num. obs: 49196 / % possible obs: 100 % / Redundancy: 5.1 % / Biso Wilson estimate: 79.718 Å2 / Rpim(I) all: 0.035 / Rrim(I) all: 0.079 / Net I/σ(I): 14.1 | |||||||||||||||||||||
Reflection shell | Diffraction-ID: 1 / % possible all: 100
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-Phasing
Phasing | Method: ![]() |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entries 5GGU, 5F3H, 3HH2, 3RJR, & 5NTU Resolution: 2.79→40.43 Å / Cor.coef. Fo:Fc: 0.939 / Cor.coef. Fo:Fc free: 0.927 / SU B: 39.776 / SU ML: 0.337 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 1.216 / ESU R Free: 0.364 Details: U VALUES : WITH TLS ADDED HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 240.21 Å2 / Biso mean: 98.061 Å2 / Biso min: 30 Å2
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Refinement step | Cycle: final / Resolution: 2.79→40.43 Å
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Refine LS restraints |
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Refine LS restraints NCS | Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05
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LS refinement shell | Resolution: 2.79→2.862 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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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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