4fc1 | pdb_00004fc1

Ultra-high resolution neutron structure of crambin at room-temperature

spinqualitylabelsall models 4fc1, resolution 1.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4fc1 is a 1 chain structure with sequence from Crambe hispanica subsp. abyssinica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: DOD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CRAM_CRAAB] The function of this hydrophobic plant seed protein is not known. Publication Abstract from PubMed The 1.1 A, ultrahigh resolution neutron structure of hydrogen/deuterium (H/D) exchanged crambin is reported. Two hundred ninety-nine out of 315, or 94.9%, of the hydrogen atom positions in the protein have been experimentally derived and resolved through nuclear density maps. A number of unconventional interactions are clearly defined, including a potential O horizontal line H...pi interaction between a water molecule and the aromatic ring of residue Y44, as well as a number of potential C horizontal line H...O hydrogen bonds. Hydrogen bonding networks that are ambiguous in the 0.85 A ultrahigh resolution X-ray structure can be resolved by accurate orientation of water molecules. Furthermore, the high resolution of the reported structure has allowed for the anisotropic description of 36 deuterium atoms in the protein. The visibility of hydrogen and deuterium atoms in the nuclear density maps is discussed in relation to the resolution of the neutron data. Direct observation of hydrogen atom dynamics and interactions by ultrahigh resolution neutron protein crystallography.,Chen JC, Hanson BL, Fisher SZ, Langan P, Kovalevsky AY Proc Natl Acad Sci U S A. 2012 Sep 4. PMID:22949690 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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