[English] 日本語
Yorodumi- PDB-1cff: NMR SOLUTION STRUCTURE OF A COMPLEX OF CALMODULIN WITH A BINDING ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1cff | ||||||
---|---|---|---|---|---|---|---|
Title | NMR SOLUTION STRUCTURE OF A COMPLEX OF CALMODULIN WITH A BINDING PEPTIDE OF THE CA2+-PUMP | ||||||
Components |
| ||||||
Keywords | CALMODULIN / C20W / PLASMA MEMBRANE CALCIUM PUMP | ||||||
Function / homology | Function and homology information negative regulation of the force of heart contraction / negative regulation of arginine catabolic process / negative regulation of cellular response to vascular endothelial growth factor stimulus / negative regulation of citrulline biosynthetic process / calcium ion transmembrane transporter activity / cellular response to acetylcholine / nitric-oxide synthase inhibitor activity / negative regulation of peptidyl-cysteine S-nitrosylation / negative regulation of nitric-oxide synthase activity / negative regulation of adenylate cyclase-activating adrenergic receptor signaling pathway ...negative regulation of the force of heart contraction / negative regulation of arginine catabolic process / negative regulation of cellular response to vascular endothelial growth factor stimulus / negative regulation of citrulline biosynthetic process / calcium ion transmembrane transporter activity / cellular response to acetylcholine / nitric-oxide synthase inhibitor activity / negative regulation of peptidyl-cysteine S-nitrosylation / negative regulation of nitric-oxide synthase activity / negative regulation of adenylate cyclase-activating adrenergic receptor signaling pathway / sperm principal piece / calcium ion export / response to hydrostatic pressure / regulation of sodium ion transmembrane transport / flagellated sperm motility / P-type Ca2+ transporter / neural retina development / regulation of cell cycle G1/S phase transition / urinary bladder smooth muscle contraction / P-type calcium transporter activity / negative regulation of nitric oxide biosynthetic process / protein phosphatase 2B binding / calcium ion transmembrane import into cytosol / negative regulation of cardiac muscle hypertrophy in response to stress / Reduction of cytosolic Ca++ levels / negative regulation of calcineurin-NFAT signaling cascade / nitric oxide-cGMP-mediated signaling / nitric-oxide synthase binding / Ion transport by P-type ATPases / calcium ion import across plasma membrane / negative regulation of blood vessel endothelial cell migration / transport across blood-brain barrier / regulation of cardiac conduction / sodium channel regulator activity / sperm flagellum / presynaptic active zone membrane / Ion homeostasis / monoatomic ion transmembrane transport / T-tubule / cellular response to epinephrine stimulus / regulation of cytosolic calcium ion concentration / negative regulation of angiogenesis / caveola / PDZ domain binding / hippocampus development / calcium ion transmembrane transport / positive regulation of protein localization to plasma membrane / Z disc / intracellular calcium ion homeostasis / scaffold protein binding / spermatogenesis / basolateral plasma membrane / calmodulin binding / membrane raft / negative regulation of gene expression / signaling receptor binding / intracellular membrane-bounded organelle / glutamatergic synapse / calcium ion binding / regulation of transcription by RNA polymerase II / protein kinase binding / ATP hydrolysis activity / protein-containing complex / ATP binding / membrane / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | Xenopus laevis (African clawed frog) Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Elshorst, B. / Hennig, M. / Foersterling, H. / Diener, A. / Maurer, M. / Schulte, P. / Schwalbe, H. / Krebs, J. / Schmid, H. / Vorherr, T. ...Elshorst, B. / Hennig, M. / Foersterling, H. / Diener, A. / Maurer, M. / Schulte, P. / Schwalbe, H. / Krebs, J. / Schmid, H. / Vorherr, T. / Carafoli, E. / Griesinger, C. | ||||||
Citation | Journal: Biochemistry / Year: 1999 Title: NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump. Authors: Elshorst, B. / Hennig, M. / Forsterling, H. / Diener, A. / Maurer, M. / Schulte, P. / Schwalbe, H. / Griesinger, C. / Krebs, J. / Schmid, H. / Vorherr, T. / Carafoli, E. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1cff.cif.gz | 1.3 MB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1cff.ent.gz | 1.1 MB | Display | PDB format |
PDBx/mmJSON format | 1cff.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cf/1cff ftp://data.pdbj.org/pub/pdb/validation_reports/cf/1cff | HTTPS FTP |
---|
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 16721.350 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Xenopus laevis (African clawed frog) / Strain: 71 / Cellular location (production host): CYTOPLASM / Gene (production host): CALMODULIN / Production host: Escherichia coli (E. coli) / Strain (production host): AR58 / References: UniProt: P62155, UniProt: P0DP33*PLUS |
---|---|
#2: Protein/peptide | Mass: 2501.997 Da / Num. of mol.: 1 / Fragment: CAM-BINDING DOMAIN / Mutation: C20W / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P23634, EC: 3.6.1.38 |
#3: Chemical | ChemComp-CA / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||||||||||||||||||||||
NMR details | Text: THE UNLABELED PEPTIDE C20W WAS ASSIGNED USING A 12C,14N-FILTERED NOESY- EXPERIMENT. INTERMOLECULAR NOES BETWEEN 13C,15N-LABELED CALMODULIN AND THE PEPTIDE WERE MEASURED USING A 12C,14N-F2- ...Text: THE UNLABELED PEPTIDE C20W WAS ASSIGNED USING A 12C,14N-FILTERED NOESY- EXPERIMENT. INTERMOLECULAR NOES BETWEEN 13C,15N-LABELED CALMODULIN AND THE PEPTIDE WERE MEASURED USING A 12C,14N-F2-FILTERED NOESY-HSQC EXPERIMENT |
-Sample preparation
Details | Contents: 90% H2O/10% D2O, 100% D2O |
---|---|
Sample conditions | Ionic strength: 0.115 / pH: 6.5 / Pressure: 1 atm / Temperature: 303 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
|
---|
-Processing
NMR software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing / Software ordinal: 1 Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. IT IS IMPOSSIBLE TO SUPERIMPOSE THE N- AND C-TERMINAL DOMAIN OF CAM SIMULTANEOUSLY DUE TO THE LACK OF NOES BETWEEN BOTH DOMAINS. ...Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. IT IS IMPOSSIBLE TO SUPERIMPOSE THE N- AND C-TERMINAL DOMAIN OF CAM SIMULTANEOUSLY DUE TO THE LACK OF NOES BETWEEN BOTH DOMAINS. THEREFOR THE 26 STRUCTURES ARE SUPERIMPOSED ONLY OVER THE BACKBONE ATOMS OF THE C-TERMINAL DOMAIN OF CAM AND THE PEPTIDE C20W. RMSD VALUES OF THE N-TERMINAL DOMAIN OF CAM (LEU A 4 - ALA A 73) ARE 0.85 (BACKBONE) AND 1.27 (HEAVY ATOMS) ANGSTROMS. RMSD VALUE FOR THE C- TERMINAL DOMAIN OF CAM AND THE PEPTIDE C20W (ILE A 85 - MET A 145, GLY B 4 - GLN B 16) ARE 0.57 (BACKBONE) AND 1.08 (HEAVY ATOMS) ANGSTROMS. RESIDUES ALA A 1 - GLN A 3, ARG A 74 - GLU A 84, THR A 146 - LYS A 148 OF CAM AND RESIDUES LEU B 1 - ARG B 3, THR B 17 - LYS B 20 OF THE PEPTIDE C20W ARE DISORDERED. | ||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 200 / Conformers submitted total number: 26 |