- PDB-1cff: NMR SOLUTION STRUCTURE OF A COMPLEX OF CALMODULIN WITH A BINDING ... -
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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
CALCIUM PUMP
CALMODULIN
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 synthase binding / Ion transport by P-type ATPases / negative regulation of blood vessel endothelial cell migration / transport across blood-brain barrier / calcium ion import across plasma membrane / regulation of cardiac conduction / sperm flagellum / sodium channel regulator activity / presynaptic active zone membrane / enzyme regulator activity / nitric oxide-cGMP-mediated signaling / 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 / intracellular membrane-bounded organelle / signaling receptor binding / 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
Mass: 40.078 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Ca
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
1
HNCO
1
2
1
HNCA
1
3
1
CBCA(CO)NH
1
4
1
CBCANH
1
5
1
(H)CC(CO)NH
1
6
1
(H)CCH-TOCSY
1
7
1
NOESY-HSQC
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
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
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