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- PDB-2bbm: SOLUTION STRUCTURE OF A CALMODULIN-TARGET PEPTIDE COMPLEX BY MULT... -
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Basic information
Entry | Database: PDB / ID: 2bbm | ||||||
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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 / photoreceptor cell axon guidance / negative regulation of opsin-mediated signaling pathway / rhabdomere development / regulation of muscle filament sliding / rhabdomere / detection of chemical stimulus involved in sensory perception of smell ...negative regulation of phospholipase C-activating phototransduction signaling pathway / myosin VI complex / myosin VI head/neck binding / myosin VII complex / photoreceptor cell axon guidance / negative regulation of opsin-mediated signaling pathway / rhabdomere development / regulation of muscle filament sliding / rhabdomere / detection of chemical stimulus involved in sensory perception of smell / myosin-light-chain kinase / myosin light chain kinase activity / myosin V complex / kinetochore organization / autophagic cell death / G protein-coupled opsin signaling pathway / actin filament-based movement / myosin V binding / cellular response to ethanol / calcium/calmodulin-dependent protein kinase activity / muscle cell cellular homeostasis / myosin heavy chain binding / mitotic spindle pole / channel regulator activity / centriole replication / enzyme regulator activity / centriole / sensory perception of sound / mitotic spindle / microtubule cytoskeleton organization / 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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Downloads & links
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PDBx/mmCIF format | ![]() | 73.2 KB | Display | ![]() |
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PDB format | ![]() | 55.2 KB | Display | ![]() |
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-Validation report
Summary document | ![]() | 297.1 KB | Display | ![]() |
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Full document | ![]() | 296.8 KB | Display | |
Data in XML | ![]() | 5.8 KB | Display | |
Data in CIF | ![]() | 7.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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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)]. A TOTAL OF 21 STRUCTURES WERE CALCULATED. THE COORDINATES OF THE RESTRAINED MINIMIZED STRUCTURE ARE PRESENTED IN THIS ENTRY. THIS WAS OBTAINED BY AVERAGING THE COORDINATES OF THE INDIVIDUAL STRUCTURES AND SUBJECTING THE RESULTING COORDINATES TO RESTRAINED MINIMIZATION. THE COORDINATES OF THE 21 INDIVIDUAL SA STRUCTURES ARE PRESENTED IN PROTEIN DATA BANK ENTRY 2BBN. THE LAST COLUMN IN THIS COORDINATE FILE REPRESENTS THE ATOMIC RMS DEVIATION OF THE INDIVIDUAL STRUCTURES ABOUT THE MEAN COORDINATE POSITIONS. |
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NMR ensemble | Conformers submitted total number: 1 |