| pubmed-article:8381492 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8381492 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8381492 | lifeskim:mentions | umls-concept:C0681842 | lld:lifeskim |
| pubmed-article:8381492 | lifeskim:mentions | umls-concept:C1321013 | lld:lifeskim |
| pubmed-article:8381492 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:8381492 | lifeskim:mentions | umls-concept:C0813983 | lld:lifeskim |
| pubmed-article:8381492 | lifeskim:mentions | umls-concept:C0449774 | lld:lifeskim |
| pubmed-article:8381492 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8381492 | pubmed:dateCreated | 1993-3-11 | lld:pubmed |
| pubmed-article:8381492 | pubmed:abstractText | The atomic co-ordinates of seven very high resolution (< 1.4 A) proteins have been used to define a water-hydrogen bond template for five polar side-chains (arginine, aspartic acid, glutamic acid, asparagine and glutamine). The average water molecule positions determined were consistent with the hydrogen bonding stereochemistry expected for each side-chain. Hydrogen bonding geometry around nitrogen atoms was significantly better localized than around oxygen atoms, perhaps because of the proton on nitrogen. A prediction algorithm written to locate water molecule sites around these side-chains from the protein co-ordinates only was tested for crambin as well as for two high resolution protein structures not included in the hydrogen bond data base. The root-mean-square deviation of the predicted positions from the crystallographically determined ones for these structures was better than the resolution of these structures. The method also successfully predicted water positions for X-ray refinement of two proteins, indicating that predicted water molecules are within the radius of convergence of refinement. This method has utility for X-ray models as well as for analysis of enzyme hydration and function. | lld:pubmed |
| pubmed-article:8381492 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8381492 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8381492 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8381492 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8381492 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8381492 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8381492 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8381492 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8381492 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8381492 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8381492 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8381492 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:8381492 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:8381492 | pubmed:author | pubmed-author:TeeterM MMM | lld:pubmed |
| pubmed-article:8381492 | pubmed:author | pubmed-author:RoeS MSM | lld:pubmed |
| pubmed-article:8381492 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8381492 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:8381492 | pubmed:volume | 229 | lld:pubmed |
| pubmed-article:8381492 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8381492 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8381492 | pubmed:pagination | 419-27 | lld:pubmed |
| pubmed-article:8381492 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8381492 | pubmed:meshHeading | pubmed-meshheading:8381492-... | lld:pubmed |
| pubmed-article:8381492 | pubmed:meshHeading | pubmed-meshheading:8381492-... | lld:pubmed |
| pubmed-article:8381492 | pubmed:meshHeading | pubmed-meshheading:8381492-... | lld:pubmed |
| pubmed-article:8381492 | pubmed:meshHeading | pubmed-meshheading:8381492-... | lld:pubmed |
| pubmed-article:8381492 | pubmed:meshHeading | pubmed-meshheading:8381492-... | lld:pubmed |
| pubmed-article:8381492 | pubmed:meshHeading | pubmed-meshheading:8381492-... | lld:pubmed |
| pubmed-article:8381492 | pubmed:meshHeading | pubmed-meshheading:8381492-... | lld:pubmed |
| pubmed-article:8381492 | pubmed:meshHeading | pubmed-meshheading:8381492-... | lld:pubmed |
| pubmed-article:8381492 | pubmed:meshHeading | pubmed-meshheading:8381492-... | lld:pubmed |
| pubmed-article:8381492 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8381492 | pubmed:articleTitle | Patterns for prediction of hydration around polar residues in proteins. | lld:pubmed |
| pubmed-article:8381492 | pubmed:affiliation | Department of Chemistry, Boston College, Chestnut Hill, MA 02167. | lld:pubmed |
| pubmed-article:8381492 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8381492 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8381492 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:8381492 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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