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\section{Introduction}  Evolutions of proteins generate homologous collections of proteins with similar structures.  The conserved  tertiary structures of a the  protein impose hard constraints on the amino acid homologous  sequences. that can produce by evolutions to form function and structure related protein families.   This These  constraints can be detected using methods that quantify conservations and  direct correlations between positions in an alignment of the sequences of families proteins.  Most of the proteins evolved to perform interactions with other proteins ranging from quaternary assembly to functional docking, for example in signals transduction or enzymatic interactions. protein families.  In this work we are interested in detect Most of the proteins evolved to perform several interactions with other proteins partners ranging from  quaternary assembly co-evolutionary to functional docking, for example in  signals between different chains. transduction or enzymatic interactions.  One problem that In this work  we face is that the co- occurrence of different signals, presumably that have are interested in detect quaternary assembly co-evolutionary signals between  different magnitude: intra-chains structure constraint signal can shade chains.   To restrict  the inter-chains structure signals that problem and avoid technical hard problems  we search. focus on homo-oligomers.  One problem that we face is that the co- occurrence of different signals (presumably with different magnitude): the intra-chains folding signals can cover up the inter-chains signals that we search.  The main idea is to perform a large-scale analysis to detect the co-evolutionary signals that does not have a intra-chain structure origin and see if it comes from quaternary assembly constraints.  \section{Database} 
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We collect all PDB with a biological assembly that contains homo-oligomers of the pfam domains selected.  We create a map between the alignment positions and the 3D inter-residues real positions for each pfam - PDB.  To do so we extract the real positions between residues:  within the domains on the differents different  chains, i.e. the \textit{intra-chains distances}, between different chains (pairing of the domains with the homo-oligomers), i.e. the \textit{inter-chains distances}.  \section{Preliminary Results}