› 2l8v

Solution NMR

Solution NMR structure of the phycobilisome linker polypeptide domain of CpcC (20-153) from Thermosynechococcus elongatus, Northeast Structural Genomics Consortium Target TeR219A

Released:
DOI: 10.2210/pdb2l8v/pdb
PDB entry 2l8v coloured by chain, ensemble of 20 models, front view.
PDB entry 2l8v coloured by chain, ensemble of 20 models, side view.
PDB entry 2l8v coloured by chain, ensemble of 20 models, top view.
Source organism: Thermosynechococcus vestitus BP-1
Entry authors: Ramelot TA, Yang Y, Cort JR, Lee D, Ciccosanti C, Hamilton K, Acton TB, Xiao R, Everett JK, Montelione GT, Kennedy MA, Northeast Structural Genomics Consortium (NESG)

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156116 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phycobilisome 32.1 kDa linker polypeptide, phycocyanin-associated, rod Chain: A
Molecule details ›
Chain: A
Length: 143 amino acids
Theoretical weight: 16.91 KDa
Source organism: Thermosynechococcus vestitus BP-1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P50034 (Residues: 20-153; Coverage: 47%)
Gene names: cpcC, tlr1959
Sequence domains: Phycobilisome Linker polypeptide
Structure domains: Phycobilisome linker domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 87%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

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