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- PDB-2bbn: SOLUTION STRUCTURE OF A CALMODULIN-TARGET PEPTIDE COMPLEX BY MULT... -
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Basic information
Entry | Database: PDB / ID: 2bbn | ||||||
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Title | SOLUTION STRUCTURE OF A CALMODULIN-TARGET PEPTIDE COMPLEX BY MULTIDIMENSIONAL NMR | ||||||
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![]() | CALCIUM-BINDING PROTEIN | ||||||
Function / homology | ![]() negative regulation of phospholipase C-activating phototransduction signaling pathway / myosin VI complex / myosin VI head/neck binding / myosin VII complex / negative regulation of opsin-mediated signaling pathway / photoreceptor cell axon guidance / rhabdomere development / rhabdomere / regulation of muscle filament sliding / myosin-light-chain kinase ...negative regulation of phospholipase C-activating phototransduction signaling pathway / myosin VI complex / myosin VI head/neck binding / myosin VII complex / negative regulation of opsin-mediated signaling pathway / photoreceptor cell axon guidance / rhabdomere development / rhabdomere / regulation of muscle filament sliding / myosin-light-chain kinase / detection of chemical stimulus involved in sensory perception of smell / myosin light chain kinase activity / myosin V complex / kinetochore organization / autophagic cell death / myosin light chain binding / G protein-coupled opsin signaling pathway / actin filament-based movement / myosin V binding / cardiac muscle tissue morphogenesis / cellular response to ethanol / calcium/calmodulin-dependent protein kinase activity / muscle cell cellular homeostasis / mitotic spindle pole / myosin heavy chain binding / channel regulator activity / centriole replication / enzyme regulator activity / striated muscle contraction / centriole / sensory perception of sound / mitotic spindle / spindle / sensory perception of smell / cell cortex / midbody / calmodulin binding / centrosome / calcium ion binding / nucleoplasm / ATP binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Clore, G.M. / Bax, A. / Ikura, M. / Gronenborn, A.M. | ||||||
![]() | ![]() Title: Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Authors: Ikura, M. / Clore, G.M. / Gronenborn, A.M. / Zhu, G. / Klee, C.B. / Bax, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 1.1 MB | Display | ![]() |
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PDB format | ![]() | 925.4 KB | Display | ![]() |
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-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: 16694.324 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Protein/peptide | Mass: 2972.538 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source References: UniProt: P07313 |
#3: Chemical | ChemComp-CA / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
Refinement | Software ordinal: 1 Details: DETAILS OF THE STRUCTURE DETERMINATION AND ALL STRUCTURAL STATISTICS ARE GIVEN IN THE PAPER CITED ON *JRNL* RECORDS ABOVE (I.E. AGREEMENT WITH EXPERIMENTAL RESTRAINTS, DEVIATIONS FROM ...Details: DETAILS OF THE STRUCTURE DETERMINATION AND ALL STRUCTURAL STATISTICS ARE GIVEN IN THE PAPER CITED ON *JRNL* RECORDS ABOVE (I.E. AGREEMENT WITH EXPERIMENTAL RESTRAINTS, DEVIATIONS FROM IDEALITY FOR BOND LENGTHS, ANGLES, PLANES AND CHIRALITY, NON-BONDED CONTACTS, ATOMIC RMS DIFFERENCES BETWEEN THE CALCULATED STRUCTURES). THE STRUCTURES ARE BASED ON 1827 INTERPROTON DISTANCE RESTRAINTS DERIVED FROM NOE MEASUREMENTS; 148 HYDROGEN-BONDING DISTANCE RESTRAINTS FOR 74 HYDROGEN-BONDS IDENTIFIED ON THE BASIS OF THE NOE AND AMIDE PROTON EXCHANGE DATA, AS WELL AS THE INITIAL STRUCTURE CALCULATIONS; 24 RESTRAINTS FOR THE 4 CALCIUM IONS, AND 113 PHI TORSION ANGLE RESTRAINTS DERIVED FROM COUPLING DATA, CONSTANTS, NOE AND 13C SECONDARY CHEMICAL SHIFTS. THE METHOD USED TO DETERMINE THE STRUCTURES IS THE HYBRID METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING METHOD [M.NILGES, G.M.CLORE, AND A.M.GRONENBORN, FEBS LETT. 229, 317-324 (1988)]. THE QUANTITY PRESENTED IN THE B VALUE FIELD OF ATOM AND HETATM RECORDS BELOW HAS NO MEANING. |
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NMR ensemble | Conformers submitted total number: 21 |