+Open data
-Basic information
Entry | Database: PDB / ID: 2l4h | ||||||
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Title | The Solution Structure of Calcium Bound CIB1 | ||||||
Components | Calcium and integrin-binding protein 1 | ||||||
Keywords | METAL BINDING PROTEIN / Calcium and Integrin Binding protein 1 | ||||||
Function / homology | Function and homology information calcium-dependent protein kinase inhibitor activity / thrombopoietin-mediated signaling pathway / endomitotic cell cycle / positive regulation of male germ cell proliferation / filopodium tip / positive regulation of calcineurin-NFAT signaling cascade / negative regulation of microtubule depolymerization / protein serine/threonine kinase inhibitor activity / positive regulation of cell adhesion mediated by integrin / positive regulation of cell-matrix adhesion ...calcium-dependent protein kinase inhibitor activity / thrombopoietin-mediated signaling pathway / endomitotic cell cycle / positive regulation of male germ cell proliferation / filopodium tip / positive regulation of calcineurin-NFAT signaling cascade / negative regulation of microtubule depolymerization / protein serine/threonine kinase inhibitor activity / positive regulation of cell adhesion mediated by integrin / positive regulation of cell-matrix adhesion / platelet formation / positive regulation of cell migration involved in sprouting angiogenesis / positive regulation of catalytic activity / regulation of cell division / spermatid development / positive regulation of protein targeting to membrane / negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / negative regulation of megakaryocyte differentiation / cytoplasmic microtubule organization / protein-membrane adaptor activity / positive regulation of substrate adhesion-dependent cell spreading / extrinsic apoptotic signaling pathway / cellular response to nerve growth factor stimulus / negative regulation of protein phosphorylation / cell periphery / response to ischemia / positive regulation of protein localization to plasma membrane / sarcolemma / positive regulation of protein serine/threonine kinase activity / cellular response to growth factor stimulus / ruffle membrane / small GTPase binding / double-strand break repair / negative regulation of neuron projection development / lamellipodium / cellular response to tumor necrosis factor / positive regulation of NF-kappaB transcription factor activity / regulation of cell population proliferation / growth cone / perikaryon / positive regulation of cell growth / angiogenesis / vesicle / transmembrane transporter binding / positive regulation of ERK1 and ERK2 cascade / cell adhesion / neuron projection / positive regulation of cell migration / positive regulation of protein phosphorylation / apical plasma membrane / cell division / axon / negative regulation of cell population proliferation / centrosome / neuronal cell body / apoptotic process / DNA damage response / calcium ion binding / positive regulation of cell population proliferation / negative regulation of apoptotic process / perinuclear region of cytoplasm / Golgi apparatus / magnesium ion binding / endoplasmic reticulum / extracellular exosome / nucleoplasm / membrane / nucleus / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Huang, H. / Vogel, H.J. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2011 Title: Solution Structures of Ca2+-CIB1 and Mg2+-CIB1 and Their Interactions with the Platelet Integrin {alpha}IIb Cytoplasmic Domain. Authors: Huang, H. / Ishida, H. / Yamniuk, A.P. / Vogel, H.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2l4h.cif.gz | 631.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2l4h.ent.gz | 543.1 KB | Display | PDB format |
PDBx/mmJSON format | 2l4h.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l4/2l4h ftp://data.pdbj.org/pub/pdb/validation_reports/l4/2l4h | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 24507.264 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CIB1, CIB, KIP, PRKDCIP / Plasmid: pET19b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: Q99828 |
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#2: Chemical |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 200 / pH: 7.5 / Pressure: ambient / Temperature: 310 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: Avance / Field strength: 700 MHz |
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-Processing
NMR software | Name: X-PLOR_NIH / Version: 2.18 / Developer: Schwieters, Kuszewski, Tjandra and Clore / Classification: refinement |
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Refinement | Method: simulated annealing / Software ordinal: 1 / Details: two steps: 1st step, 200K-20K; 2nd step, 20K-2K |
NMR constraints | NOE constraints total: 1069 / NOE intraresidue total count: 80 / NOE long range total count: 118 / NOE medium range total count: 71 / NOE sequential total count: 167 / Protein chi angle constraints total count: 0 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 174 / Protein psi angle constraints total count: 174 |
NMR representative | Selection criteria: lowest energy |
NMR ensemble | Average torsion angle constraint violation: 2.38 ° Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 11 / Maximum lower distance constraint violation: 1.8 Å / Maximum torsion angle constraint violation: 30 ° / Maximum upper distance constraint violation: 8 Å / Torsion angle constraint violation method: TALOS |
NMR ensemble rms | Distance rms dev: 0.086 Å / Distance rms dev error: 0.005 Å |