| pubmed-article:21592348 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21592348 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:21592348 | lifeskim:mentions | umls-concept:C1510464 | lld:lifeskim |
| pubmed-article:21592348 | lifeskim:mentions | umls-concept:C0018017 | lld:lifeskim |
| pubmed-article:21592348 | lifeskim:mentions | umls-concept:C1514721 | lld:lifeskim |
| pubmed-article:21592348 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:21592348 | lifeskim:mentions | umls-concept:C1571702 | lld:lifeskim |
| pubmed-article:21592348 | pubmed:dateCreated | 2011-6-22 | lld:pubmed |
| pubmed-article:21592348 | pubmed:abstractText | The automation of objectively selecting amino acid residue ranges for structure superpositions is important for meaningful and consistent protein structure analyses. So far there is no widely-used standard for choosing these residue ranges for experimentally determined protein structures, where the manual selection of residue ranges or the use of suboptimal criteria remain commonplace. | lld:pubmed |
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| pubmed-article:21592348 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21592348 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21592348 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21592348 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21592348 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21592348 | pubmed:issn | 1471-2105 | lld:pubmed |
| pubmed-article:21592348 | pubmed:author | pubmed-author:GüntertPeterP | lld:pubmed |
| pubmed-article:21592348 | pubmed:author | pubmed-author:KirchnerDonat... | lld:pubmed |
| pubmed-article:21592348 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21592348 | pubmed:volume | 12 | lld:pubmed |
| pubmed-article:21592348 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21592348 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21592348 | pubmed:pagination | 170 | lld:pubmed |
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| pubmed-article:21592348 | pubmed:meshHeading | pubmed-meshheading:21592348... | lld:pubmed |
| pubmed-article:21592348 | pubmed:meshHeading | pubmed-meshheading:21592348... | lld:pubmed |
| pubmed-article:21592348 | pubmed:meshHeading | pubmed-meshheading:21592348... | lld:pubmed |
| pubmed-article:21592348 | pubmed:meshHeading | pubmed-meshheading:21592348... | lld:pubmed |
| pubmed-article:21592348 | pubmed:meshHeading | pubmed-meshheading:21592348... | lld:pubmed |
| pubmed-article:21592348 | pubmed:meshHeading | pubmed-meshheading:21592348... | lld:pubmed |
| pubmed-article:21592348 | pubmed:meshHeading | pubmed-meshheading:21592348... | lld:pubmed |
| pubmed-article:21592348 | pubmed:meshHeading | pubmed-meshheading:21592348... | lld:pubmed |
| pubmed-article:21592348 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21592348 | pubmed:articleTitle | Objective identification of residue ranges for the superposition of protein structures. | lld:pubmed |
| pubmed-article:21592348 | pubmed:affiliation | Institute of Biophysical Chemistry, Center for Biomolecular Magnetic Resonance, and Frankfurt Institute for Advanced Studies, Goethe University Frankfurt am Main, Max-von-Laue-Str, 9, 60438 Frankfurt am Main, Germany. | lld:pubmed |
| pubmed-article:21592348 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21592348 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
