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- PDB-1mv4: TM9A251-284: A Peptide Model of the C-Terminus of a Rat Striated ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1mv4 | ||||||
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Title | TM9A251-284: A Peptide Model of the C-Terminus of a Rat Striated Alpha Tropomyosin | ||||||
![]() | Tropomyosin 1 alpha chain | ||||||
![]() | DE NOVO PROTEIN / TROPOMYOSIN / EXON 9A / ACTIN-BINDING / TROPONIN BINDING / MUSCLE / ALPHA-HELIX / COILED-COIL / DIMER / PEPTIDE-MODEL / TWO-CHAINED / DISULFIDE CROSS-LINKED | ||||||
Function / homology | ![]() Striated Muscle Contraction / Smooth Muscle Contraction / positive regulation of heart rate by epinephrine / bleb / negative regulation of vascular associated smooth muscle cell migration / muscle filament sliding / actin filament capping / ruffle organization / positive regulation of ATP-dependent activity / ventricular cardiac muscle tissue morphogenesis ...Striated Muscle Contraction / Smooth Muscle Contraction / positive regulation of heart rate by epinephrine / bleb / negative regulation of vascular associated smooth muscle cell migration / muscle filament sliding / actin filament capping / ruffle organization / positive regulation of ATP-dependent activity / ventricular cardiac muscle tissue morphogenesis / myofibril / sarcomere organization / negative regulation of vascular associated smooth muscle cell proliferation / positive regulation of cell adhesion / cardiac muscle contraction / stress fiber / positive regulation of stress fiber assembly / cytoskeletal protein binding / negative regulation of cell migration / muscle contraction / actin filament / actin filament organization / wound healing / ruffle membrane / cellular response to reactive oxygen species / disordered domain specific binding / actin filament binding / actin cytoskeleton / actin binding / regulation of cell shape / in utero embryonic development / protein heterodimerization activity / protein homodimerization activity / protein-containing complex / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / 1648 CONFORMATIONALLY- RESTRICTING NOE CONSTRAINTS (OUT OF A TOTAL OF 2036 NOE DERIVED DISTANCES) 52 LOOSE DIHEDRAL ANGLE CONSTRAINTS, 48 BACKBONE INTRA- HELICAL HYDROGEN BOND CONSTRAINTS WERE UTILILIZED. | ||||||
![]() | Greenfield, N.J. / Swapna, G.V.T. / Huang, Y. / Palm, T. / Graboski, S. / Montelione, G.T. / Hitchcock-Degregori, S.E. | ||||||
![]() | ![]() Title: The Structure of the Carboxyl Terminus of Striated alpha-Tropomyosin in Solution Reveals an Unusual Parallel Arrangement of Interacting alpha-Helices Authors: Greenfield, N.J. / Swapna, G.V.T. / Huang, Y. / Palm, T. / Graboski, S. / Montelione, G.T. / Hitchcock-DeGregori, S.E. | ||||||
History |
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Remark 999 | SEQUENCE THIS SEQUENCE HAS A SYNTHETIC GCG AT N-TERMINUS AND CONTAINS THE MUTATION N279K. THE ...SEQUENCE THIS SEQUENCE HAS A SYNTHETIC GCG AT N-TERMINUS AND CONTAINS THE MUTATION N279K. THE SEQUENCE DATABASE MATCH, HOWEVER, erroneously HAS A K AT THIS POSITION as well. The sequence in the database should have an ASN at position 279, which has been engineered to LYS in this entry. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 230.9 KB | Display | ![]() |
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PDB format | ![]() | 199.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 368.8 KB | Display | ![]() |
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Full document | ![]() | 497.7 KB | Display | |
Data in XML | ![]() | 18 KB | Display | |
Data in CIF | ![]() | 26.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar 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/peptide | Mass: 4177.707 Da / Num. of mol.: 2 / Fragment: C-TERMINAL (RESIDUES 251-284) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: THE RESONANCE ASSIGNMENTS WERE MADE USING THROUGH BOND TRIPLE RESONANCE EXPERIMENTS INCLUDING HN(CA)CO, HNCO, H(CA)(C0)NH, H(CA)NH, CA(CO)NH, CANH, CBCA(CO)NH, CBCANH, HCCH-COSY AND CCH-COSY |
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Sample preparation
Details | Contents: 1-2 MM Solvent system: 100 MM NACL, 20 MM POTASSIUM PHOSPHATE, 10% DUETERIUM OXIDE, 90% H20, PH 6.4 |
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Sample conditions | Ionic strength: 0.12 N / pH: 6.40 / Pressure: 1 atm / Temperature: 283.00 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: 1648 CONFORMATIONALLY- RESTRICTING NOE CONSTRAINTS (OUT OF A TOTAL OF 2036 NOE DERIVED DISTANCES) 52 LOOSE DIHEDRAL ANGLE CONSTRAINTS, 48 BACKBONE INTRA- HELICAL HYDROGEN BOND CONSTRAINTS WERE UTILILIZED. Software ordinal: 1 Details: REFINEMENT DETAILS CAN BE FOUND IN REFERENCE CITED ABOVE | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: STRUCTURES WITH COVALENT GEOMETRY, STRUCTURES WITH THE LEAST RESTRAINT VIOLATIONS Conformers calculated total number: 200 / Conformers submitted total number: 10 |