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DESCRIBE <http://purl.uniprot.org/SHA-384/E04A30CFE5F95A8CC363B2CFCF09E9B1B7D7D1A76FE29BFD735FA992AC55C6D2C26314AE746731883A9EBC3DF1307C4F>
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http://purl.uniprot.org/SHA-384/E04A30CFE5F95A8CC363B2CFCF09E9B1B7D7D1A76FE29BFD735FA992AC55C6D2C26314AE746731883A9EBC3DF1307C4F
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/E04A30CFE5F95A8CC363B2CFCF09E9B1B7D7D1A76FE29BFD735FA992AC55C6D2C26314AE746731883A9EBC3DF1307C4F
http://www.w3.org/2000/01/rdf-schema#comment
"solution structure of the inner DysF domain of the dysferlin paralogue myoferlin which has a unique fold held together by stacking of arginine and tryptophans mutations that lead to clinical disease in dysferlin"
xsd:string
http://purl.uniprot.org/uniprot/#_9D56078D61271830C98C35C6B2D089BDF70242E7C92FB1D8FCE8DDD3966CA46FA5835D77F7672BCCCDFC4C7FFFEB45ED
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/E04A30CFE5F95A8CC363B2CFCF09E9B1B7D7D1A76FE29BFD735FA992AC55C6D2C26314AE746731883A9EBC3DF1307C4F
http://purl.uniprot.org/uniprot/Q7Z6P1
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/E04A30CFE5F95A8CC363B2CFCF09E9B1B7D7D1A76FE29BFD735FA992AC55C6D2C26314AE746731883A9EBC3DF1307C4F
http://purl.uniprot.org/uniprot/#_Q7Z6P1-mappedCitation-18495154
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/E04A30CFE5F95A8CC363B2CFCF09E9B1B7D7D1A76FE29BFD735FA992AC55C6D2C26314AE746731883A9EBC3DF1307C4F