1MV4

TM9A251-284: A Peptide Model of the C-Terminus of a Rat Striated Alpha Tropomyosin

Summary for 1MV4

Related1IHQ 1TMZ 1IC2
DescriptorTropomyosin 1 alpha chain (1 entity in total)
Functional Keywordstropomyosin, exon 9a, actin-binding, troponin binding, muscle, alpha-helix, coiled-coil, dimer, peptide-model, two-chained, disulfide cross-linked, de novo protein
Biological sourceRattus norvegicus (Norway rat)
Cellular locationCytoplasm, cytoskeleton P04692
Total number of polymer chains2
Total molecular weight8355.41
Authors
Greenfield, N.J.,Swapna, G.V.T.,Huang, Y.,Palm, T.,Graboski, S.,Montelione, G.T.,Hitchcock-Degregori, S.E. (deposition date: 2002-09-24, release date: 2003-02-18, Last modification date: 2011-07-13)
Primary citation
Greenfield, N.J.,Swapna, G.V.T.,Huang, Y.,Palm, T.,Graboski, S.,Montelione, G.T.,Hitchcock-DeGregori, S.E.
The Structure of the Carboxyl Terminus of Striated alpha-Tropomyosin in Solution Reveals an Unusual Parallel Arrangement of Interacting alpha-Helices
Biochemistry, 42:614-619, 2003
PubMed: 12534273 (PDB entries with the same primary citation)
DOI: 10.1021/bi026989e
MImport into Mendeley
Experimental method
SOLUTION NMR
NMR Information
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Structure validation

ClashscoreRamachandran outliersSidechain outliers26039.6%MetricValuePercentile RanksWorseBetterPercentile relative to all structuresPercentile relative to all NMR structures