1OMU

SOLUTION STRUCTURE OF OVOMUCOID (THIRD DOMAIN) FROM DOMESTIC TURKEY (298K, PH 4.1) (NMR, 50 STRUCTURES) (REFINED MODEL USING NETWORK EDITING ANALYSIS)

Summary for 1OMU

• Entry DOI: 10.2210/pdb1omu/pdb
• Descriptor: OVOMUCOID (THIRD DOMAIN) (1 entity in total)
• Functional Keywords: spin diffusion, network editing, bd-noesy, cbd-noesy, serine proteinase inhibitor
• Biological source: Meleagris gallopavo (turkey)
• Cellular location: Secreted: P68390
• Total number of polymer chains: 1
• Total formula weight: 6026.81

Authors

Hoogstraten, C.G.,Choe, S.,Westler, W.M.,Markley, J.L. (deposition date: 1995-10-11, release date: 1996-03-08, Last modification date: 2024-10-23)

Primary citation

Hoogstraten, C.G.,Choe, S.,Westler, W.M.,Markley, J.L.
Comparison of the accuracy of protein solution structures derived from conventional and network-edited NOESY data.
Protein Sci., 4:2289-2299, 1995

PubMed Abstract: Network-editing experiments are variants of the basic NOESY experiment that allow more accurate direct measurement of interproton distances in macromolecules by defeating specific spin-diffusion pathways. Two network-editing approaches, block-decoupled NOESY and complementary-block-decoupled-NOESY, were applied as three-dimensional, heteronuclear-edited experiments to distance measurement in a small protein, turkey ovomucoid third domain (OMTKY3). Two-hundred and twelve of the original 655 distance constraints observed in this molecule (Krezel AM et al., 1994, J Mol Biol 242:203-214) were improved by their replacement by distances derived from network-edited spectra, and distance geometry/simulated annealing solution structure calculations were performed from both the unimproved and improved distance sets. The resulting two families of structures were found to differ significantly, the most important differences being the hinge angle of a beta-turn and an expansion of the sampled conformation space in the region of the reactive-site loop. The structures calculated from network-editing data are interpreted as a more accurate model of the solution conformation of OMTKY3.

PubMed: 8563625

Experimental method

SOLUTION NMR