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Open data
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Basic information
Entry | Database: PDB / ID: 2maj | ||||||
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Title | Solution Structure of the STIM1 CC1-CC2 homodimer. | ||||||
![]() | Stromal interaction molecule 1 | ||||||
![]() | SIGNALING PROTEIN / STIM1 / coiled-coil / TRANSPORT PROTEIN | ||||||
Function / homology | ![]() store-operated calcium entry / activation of store-operated calcium channel activity / regulation of store-operated calcium entry / enamel mineralization / Elevation of cytosolic Ca2+ levels / cortical endoplasmic reticulum / positive regulation of adenylate cyclase activity / microtubule plus-end binding / plasma membrane raft / regulation of calcium ion transport ...store-operated calcium entry / activation of store-operated calcium channel activity / regulation of store-operated calcium entry / enamel mineralization / Elevation of cytosolic Ca2+ levels / cortical endoplasmic reticulum / positive regulation of adenylate cyclase activity / microtubule plus-end binding / plasma membrane raft / regulation of calcium ion transport / detection of calcium ion / calcium channel regulator activity / Ion homeostasis / sarcoplasmic reticulum membrane / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / intracellular calcium ion homeostasis / positive regulation of angiogenesis / protease binding / microtubule / calcium ion binding / endoplasmic reticulum membrane / endoplasmic reticulum / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
![]() | Stathopulos, P.B. / Ikura, M. | ||||||
![]() | ![]() Title: STIM1/Orai1 coiled-coil interplay in the regulation of store-operated calcium entry. Authors: Stathopulos, P.B. / Schindl, R. / Fahrner, M. / Zheng, L. / Gasmi-Seabrook, G.M. / Muik, M. / Romanin, C. / Ikura, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.2 MB | Display | ![]() |
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PDB format | ![]() | 1 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 9702.989 Da / Num. of mol.: 2 / Fragment: UNP residues 312-387 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
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Sample |
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Sample conditions | Ionic strength: 0.02 / pH: 5.5 / Pressure: ambient / Temperature: 308 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: Used the RECOORD scripts in CNS to water refine the CYANA-determined structures (Nederveen et al., Proteins. 2005 Jun 1;59(4):662-72). | ||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 2199 / NOE intraresidue total count: 578 / NOE long range total count: 474 / NOE medium range total count: 643 / NOE sequential total count: 504 / Hydrogen bond constraints total count: 236 / Protein phi angle constraints total count: 134 / Protein psi angle constraints total count: 134 | ||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 / Maximum torsion angle constraint violation: 3.94 ° / Maximum upper distance constraint violation: -0.24 Å Torsion angle constraint violation method: RECOORD in CNS (Proteins. 2005 Jun 1;59(4):662-72) | ||||||||||||||||||||||||||||||||||||
NMR ensemble rms | Distance rms dev: 0.024 Å / Distance rms dev error: 0.001 Å |