| pubmed-article:7678499 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7678499 | lifeskim:mentions | umls-concept:C0082584 | lld:lifeskim |
| pubmed-article:7678499 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:7678499 | lifeskim:mentions | umls-concept:C0024485 | lld:lifeskim |
| pubmed-article:7678499 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
| pubmed-article:7678499 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:7678499 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
| pubmed-article:7678499 | lifeskim:mentions | umls-concept:C0450363 | lld:lifeskim |
| pubmed-article:7678499 | lifeskim:mentions | umls-concept:C0104311 | lld:lifeskim |
| pubmed-article:7678499 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:7678499 | pubmed:dateCreated | 1993-2-25 | lld:pubmed |
| pubmed-article:7678499 | pubmed:abstractText | A high-resolution three-dimensional solution structure of the FKBP/ascomycin complex has been determined using heteronuclear multidimensional nuclear magnetic resonance spectroscopy (NMR) and a distance geometry/simulated annealing protocol. A total of 43 structures of the complex, including 3 tightly bound water molecules, were obtained using 1958 experimental restraints consisting of 1724 nuclear Overhauser effect (NOE) derived distances, 66 chi 1 and 46 phi angular restraints, and 122 hydrogen bond restraints. The root mean square (rms) deviations between the 43 FKBP/ascomycin solution structures and the mean atomic coordinates were 0.43 +/- 0.08 A for the backbone heavy atoms and 0.80 +/- 0.08 A for all non-hydrogen atoms. Angular order parameters for the family of 43 conformations were calculated to determine dihedral convergence. Order parameters for phi, psi, and chi 1 angles exhibited mean values of 0.98, 0.97, and 0.95, respectively, while the mean of the chi 2 order parameter was 0.63. Comparisons were made between the FKBP/ascomycin complex and two NMR-derived solution structures of unbound FKBP and the X-ray crystal structure of an FKBP/FK506 complex. Differences were observed between the FKBP/ascomycin complex and uncomplexed FKBP for residues 33-45 and 78-92. In contrast, the NMR-derived solution structure of the FKBP/ascomycin complex and the X-ray crystal structure of the FKBP/FK506 complex were very similar. Differences between the two complexes were mainly observed in the conformations of some highly solvent exposed side chains. | lld:pubmed |
| pubmed-article:7678499 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7678499 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7678499 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7678499 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7678499 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7678499 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7678499 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:7678499 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:7678499 | pubmed:author | pubmed-author:SmithHH | lld:pubmed |
| pubmed-article:7678499 | pubmed:author | pubmed-author:DeS CSC | lld:pubmed |
| pubmed-article:7678499 | pubmed:author | pubmed-author:FesikS WSW | lld:pubmed |
| pubmed-article:7678499 | pubmed:author | pubmed-author:OlejniczakE... | lld:pubmed |
| pubmed-article:7678499 | pubmed:author | pubmed-author:PetrovA BAB | lld:pubmed |
| pubmed-article:7678499 | pubmed:author | pubmed-author:HolzmanT FTF | lld:pubmed |
| pubmed-article:7678499 | pubmed:author | pubmed-author:NettesheimD... | lld:pubmed |
| pubmed-article:7678499 | pubmed:author | pubmed-author:SeverinJJ | lld:pubmed |
| pubmed-article:7678499 | pubmed:author | pubmed-author:MeadowsR PRP | lld:pubmed |
| pubmed-article:7678499 | pubmed:author | pubmed-author:GubbinsEE | lld:pubmed |
| pubmed-article:7678499 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7678499 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:7678499 | pubmed:volume | 32 | lld:pubmed |
| pubmed-article:7678499 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7678499 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7678499 | pubmed:pagination | 754-65 | lld:pubmed |
| pubmed-article:7678499 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:7678499 | pubmed:meshHeading | pubmed-meshheading:7678499-... | lld:pubmed |
| pubmed-article:7678499 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:7678499 | pubmed:articleTitle | Three-dimensional structure of the FK506 binding protein/ascomycin complex in solution by heteronuclear three- and four-dimensional NMR. | lld:pubmed |
| pubmed-article:7678499 | pubmed:affiliation | Pharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, Illinois 60064. | lld:pubmed |
| pubmed-article:7678499 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7678499 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:7678499 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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