2ka7 | pdb_00002ka7

NMR solution structure of TM0212 at 40 C

spinqualitylabelsall models 2ka7, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ka7 is a 1 chain structure with sequence from Atcc 43589. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1zko Gene: gcvH, TM_0212 (ATCC 43589) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN Function [GCSH_THEMA] The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The J-UNIO (JCSG protocol using the software UNIO) procedure for automated protein structure determination by NMR in solution is introduced. In the present implementation, J-UNIO makes use of APSY-NMR spectroscopy, 3D heteronuclear-resolved [(1)H,(1)H]-NOESY experiments, and the software UNIO. Applications with proteins from the JCSG target list with sizes up to 150 residues showed that the procedure is highly robust and efficient. In all instances the correct polypeptide fold was obtained in the first round of automated data analysis and structure calculation. After interactive validation of the data obtained from the automated routine, the quality of the final structures was comparable to results from interactive structure determination. Special advantages are that the NMR data have been recorded with 6-10 days of instrument time per protein, that there is only a single step of chemical shift adjustments to relate the backbone signals in the APSY-NMR spectra with the corresponding backbone signals in the NOESY spectra, and that the NOE-based amino acid side chain chemical shift assignments are automatically focused on those residues that are heavily weighted in the structure calculation. The individual working steps of J-UNIO are illustrated with the structure determination of the protein YP_926445.1 from Shewanella amazonensis, and the results obtained with 17 JCSG targets are critically evaluated. The J-UNIO protocol for automated protein structure determination by NMR in solution.,Serrano P, Pedrini B, Mohanty B, Geralt M, Herrmann T, Wuthrich K J Biomol NMR. 2012 Aug;53(4):341-54. doi: 10.1007/s10858-012-9645-2. Epub 2012, Jul 3. PMID:22752932 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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