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DESCRIBE <http://purl.uniprot.org/SHA-384/C1B935BFC1C82EB7441DC3DE99842D6A97104E9D7003109A3556F16F86AD804BE90D5182D338963ED4B2A16A15505911>
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http://purl.uniprot.org/SHA-384/C1B935BFC1C82EB7441DC3DE99842D6A97104E9D7003109A3556F16F86AD804BE90D5182D338963ED4B2A16A15505911
http://www.w3.org/1999/02/22-rdf-syntax-ns#type
http://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/C1B935BFC1C82EB7441DC3DE99842D6A97104E9D7003109A3556F16F86AD804BE90D5182D338963ED4B2A16A15505911
http://www.w3.org/2000/01/rdf-schema#comment
"The catalytic domain point mutants show a decreased thermal and thermodynamic stability and decreased activation energy relative to phosphatase activity when compared to wild- type"
xsd:string
http://purl.uniprot.org/uniprot/#_27433904F40ED8460BD589FD91A8FD4651A9E1FC53FF939AE77E7404B136AC1B0A0201D51A8077586DB691F48CED04C9
http://www.w3.org/1999/02/22-rdf-syntax-ns#subject
http://purl.uniprot.org/SHA-384/C1B935BFC1C82EB7441DC3DE99842D6A97104E9D7003109A3556F16F86AD804BE90D5182D338963ED4B2A16A15505911
http://purl.uniprot.org/uniprot/O14522
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/C1B935BFC1C82EB7441DC3DE99842D6A97104E9D7003109A3556F16F86AD804BE90D5182D338963ED4B2A16A15505911
http://purl.uniprot.org/uniprot/#_O14522-mappedCitation-22389709
http://purl.uniprot.org/core/mappedAnnotation
http://purl.uniprot.org/SHA-384/C1B935BFC1C82EB7441DC3DE99842D6A97104E9D7003109A3556F16F86AD804BE90D5182D338963ED4B2A16A15505911