comments_of_protein_by_blattner = {('B0957', 'H2Otex') :  """(OmpA is a member of the OmpA-OmpF Porin (OOP) family. OmpA is believed to be a nonspecific diffusion channel,
allowing various small solutes to cross the outer membrane. |CITS: [1370823]|  It is also believed to serve several other 
functions including, as a phage receptor |CITS: [330500]| , as a mediator of F-factor dependent conjugation  |CITS: [323051]|,
and in shape stabilization of the bacterium. It is 325 amino acids long and is one of the most abundant proteins in the 
outer membrane of <I>E. coli</I>. Structural data at 1.65 angstroms reveals that OmpA consists of an eight-stranded
all-next-neighbor antiparallel beta-barrel. There is some debate asto whether OmpA is truly a channel having both open
and closed conformation |CITS: [7517935]| , or whether the observed porin activity is artifactual.
OmpA was found as a dimer in the outer membrane |CITS:[16079137]|.
Targeting of OmpA to the Sec-translocase for transport across the inner membrane
is SecB-dependent |CITS:[16352602]|.)""",
('B3875', 'H2Otex') :  """(OmpL is a member of the OmpG porin Family. It has been shown to localize to the outer membrane and exhibits
porin type properties allowing a non-specific group of solutes smaller than 600 Daltons to pass into and out of 
the periplasm.  |CITS: [11080145]|  Sequence analysis suggests that it has a &beta;-barrel structure consisting 
of 12 &beta;-strands.  |CITS: [11080145]| It has also been claimed to have an effect on redox potential in the 
periplasm  |CITS: [11080145]|, however this point is currently contested.  |CITS: [12660153]|  OmpL also 
shows a low, but possibly significant similarity to members of the Cyclodextrin Porin (CDP) family.  |CITS: [12192075]|)""",
}