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- PDB-2tma: TROPOMYOSIN CRYSTAL STRUCTURE AND MUSCLE REGULATION. APPENDIX. CO... -

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Basic information

Entry
Database: PDB / ID: 2tma
TitleTROPOMYOSIN CRYSTAL STRUCTURE AND MUSCLE REGULATION. APPENDIX. CONSTRUCTION OF AN ATOMIC MODEL FOR TROPOMYOSIN AND IMPLICATIONS FOR INTERACTIONS WITH ACTIN
ComponentsTROPOMYOSIN
KeywordsCONTRACTILE SYSTEM PROTEIN
Function / homology
Function and homology information


troponin I binding / actin filament / actin filament binding / actin cytoskeleton / protein heterodimerization activity / protein homodimerization activity / identical protein binding / cytoplasm
Similarity search - Function
Tropomyosins signature. / Tropomyosin / Tropomyosin
Similarity search - Domain/homology
Tropomyosin alpha-1 chain
Similarity search - Component
Biological speciesOryctolagus cuniculus (rabbit)
MethodX-RAY DIFFRACTION / Resolution: 15 Å
AuthorsPhillips Jr., G.N. / Cohen, C.
Citation
Journal: J.Mol.Biol. / Year: 1986
Title: Construction of an atomic model for tropomyosin and implications for interactions with actin.
Authors: Phillips Jr., G.N.
#1: Journal: J.Mol.Biol. / Year: 1986
Title: Tropomyosin Crystal Structure and Muscle Regulation
Authors: Phillipsjunior, G.N. / Fillers, J.P. / Cohen, C.
#2: Journal: Nature / Year: 1979
Title: Crystal Structure and Molecular Interactions of Tropomyosin
Authors: Phillipsjunior, G.N. / Lattman, E.E. / Cummins, P. / Lee, K.Y. / Cohen, C.
History
DepositionSep 16, 1987Processing site: BNL
Revision 1.0Oct 16, 1987Provider: repository / Type: Initial release
Revision 1.1Mar 25, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Aug 24, 2011Group: Structure summary
Revision 1.4Feb 21, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: TROPOMYOSIN
B: TROPOMYOSIN


Theoretical massNumber of molelcules
Total (without water)65,4712
Polymers65,4712
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)119.600, 240.000, 298.000
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212

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Components

#1: Protein TROPOMYOSIN / / Coordinate model: Cα atoms only


Mass: 32735.609 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Oryctolagus cuniculus (rabbit) / References: UniProt: P58772
Compound detailsTHE MOLECULE CONSISTS OF TWO LONG HELICES MADE UP OF TWO POLYPEPTIDE CHAINS WITH IDENTICAL AMINO ...THE MOLECULE CONSISTS OF TWO LONG HELICES MADE UP OF TWO POLYPEPTIDE CHAINS WITH IDENTICAL AMINO ACID SEQUENCE.

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Processing

RefinementHighest resolution: 15 Å
Details: THE MOLECULE RUNS ALONG THE BODY DIAGONAL OF THE UNIT CELL.
Refinement stepCycle: LAST / Highest resolution: 15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms568 0 0 0 568
Refinement
*PLUS
Highest resolution: 15 Å
Solvent computation
*PLUS
Displacement parameters
*PLUS

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