| pubmed-article:1793542 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1793542 | lifeskim:mentions | umls-concept:C0004611 | lld:lifeskim |
| pubmed-article:1793542 | lifeskim:mentions | umls-concept:C0752243 | lld:lifeskim |
| pubmed-article:1793542 | lifeskim:mentions | umls-concept:C0023209 | lld:lifeskim |
| pubmed-article:1793542 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
| pubmed-article:1793542 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:1793542 | pubmed:dateCreated | 1992-4-6 | lld:pubmed |
| pubmed-article:1793542 | pubmed:abstractText | The alkaline proteinase from the mesophilic bacterium Bacillus mesentericus has been crystallized in a 1:1 complex with the inhibitor eglin-C from the medical leech. The crystals have cell dimensions of a = 43.0, b = 71.9, c = 48.3 A and beta = 110.0 degrees and are in the space group P2(1). Three-dimensional data to 2.0 A have been recorded on film from a single crystal. The orientation and position of the complex in the unit cell have been established using the refined coordinates of subtilisin Carlsberg and of eglin-C as independent models. The structure of the complex has been refined by restrained least-squares minimization. The crystallographic R factor (= sigma[magnitude of Fo - magnitude of Fc[/sigma magnitude of Fo) is 15.1% including two Ca2+ ions and 312 water molecules. The structure is discussed in terms of its physicochemical properties in solution and its relation to other Bacillus subtilisins. | lld:pubmed |
| pubmed-article:1793542 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1793542 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1793542 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1793542 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1793542 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1793542 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1793542 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1793542 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1793542 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1793542 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1793542 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1793542 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1793542 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:1793542 | pubmed:issn | 0108-7681 | lld:pubmed |
| pubmed-article:1793542 | pubmed:author | pubmed-author:GenovNN | lld:pubmed |
| pubmed-article:1793542 | pubmed:author | pubmed-author:WilsonK SKS | lld:pubmed |
| pubmed-article:1793542 | pubmed:author | pubmed-author:DauterZZ | lld:pubmed |
| pubmed-article:1793542 | pubmed:author | pubmed-author:BetzelCC | lld:pubmed |
| pubmed-article:1793542 | pubmed:author | pubmed-author:PiponNN | lld:pubmed |
| pubmed-article:1793542 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1793542 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:1793542 | pubmed:volume | 47 ( Pt 5) | lld:pubmed |
| pubmed-article:1793542 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1793542 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1793542 | pubmed:pagination | 707-30 | lld:pubmed |
| pubmed-article:1793542 | pubmed:dateRevised | 2007-7-24 | lld:pubmed |
| pubmed-article:1793542 | pubmed:meshHeading | pubmed-meshheading:1793542-... | lld:pubmed |
| pubmed-article:1793542 | pubmed:meshHeading | pubmed-meshheading:1793542-... | lld:pubmed |
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| pubmed-article:1793542 | pubmed:meshHeading | pubmed-meshheading:1793542-... | lld:pubmed |
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| pubmed-article:1793542 | pubmed:meshHeading | pubmed-meshheading:1793542-... | lld:pubmed |
| pubmed-article:1793542 | pubmed:meshHeading | pubmed-meshheading:1793542-... | lld:pubmed |
| pubmed-article:1793542 | pubmed:meshHeading | pubmed-meshheading:1793542-... | lld:pubmed |
| pubmed-article:1793542 | pubmed:meshHeading | pubmed-meshheading:1793542-... | lld:pubmed |
| pubmed-article:1793542 | pubmed:meshHeading | pubmed-meshheading:1793542-... | lld:pubmed |
| pubmed-article:1793542 | pubmed:meshHeading | pubmed-meshheading:1793542-... | lld:pubmed |
| pubmed-article:1793542 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1793542 | pubmed:articleTitle | Complex between the subtilisin from a mesophilic bacterium and the leech inhibitor eglin-C. | lld:pubmed |
| pubmed-article:1793542 | pubmed:affiliation | European Molecular Biology Laboratory (EMBL), Hamburg, Germany. | lld:pubmed |
| pubmed-article:1793542 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1793542 | pubmed:publicationType | Comparative Study | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1793542 | lld:pubmed |
