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1JRM

NMR structure of MTH0637. Ontario Centre for Structural Proteomics target MTH0637_1_104; Northeast Structural Genomics Target TT135

Summary for 1JRM
Entry DOI10.2210/pdb1jrm/pdb
NMR InformationBMRB: 5104
DescriptorCONSERVED HYPOTHETICAL PROTEIN mth637 (1 entity in total)
Functional Keywordsalpha-beta protein, structural genomics, ocsp, nesg, protein structure initiative, psi, northeast structural genomics consortium, unknown function
Biological sourceMethanothermobacter thermautotrophicus
Total number of polymer chains1
Total formula weight11848.71
Authors
Pineda-Lucena, A.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2001-08-14, release date: 2002-02-27, Last modification date: 2024-05-22)
Primary citationYee, A.,Chang, X.,Pineda-Lucena, A.,Wu, B.,Semesi, A.,Le, B.,Ramelot, T.,Lee, G.M.,Bhattacharyya, S.,Gutierrez, P.,Denisov, A.,Lee, C.H.,Cort, J.R.,Kozlov, G.,Liao, J.,Finak, G.,Chen, L.,Wishart, D.,Lee, W.,McIntosh, L.P.,Gehring, K.,Kennedy, M.A.,Edwards, A.M.,Arrowsmith, C.H.
An NMR approach to structural proteomics.
Proc.Natl.Acad.Sci.USA, 99:1825-1830, 2002
Cited by
PubMed Abstract: The influx of genomic sequence information has led to the concept of structural proteomics, the determination of protein structures on a genome-wide scale. Here we describe an approach to structural proteomics of small proteins using NMR spectroscopy. Over 500 small proteins from several organisms were cloned, expressed, purified, and evaluated by NMR. Although there was variability among proteomes, overall 20% of these proteins were found to be readily amenable to NMR structure determination. NMR sample preparation was centralized in one facility, and a distributive approach was used for NMR data collection and analysis. Twelve structures are reported here as part of this approach, which allowed us to infer putative functions for several conserved hypothetical proteins.
PubMed: 11854485
DOI: 10.1073/pnas.042684599
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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