Protein with 83 residues, VPA0419 (residues 17–99, numbered 1–83) (gi|81726230, SwissProt/TrEMBL ID Q87J34_VIBPA, accession number {"type":"entrez-protein","attrs":{"text":"Q87J34","term_id":"81726230","term_text":"Q87J34"}}Q87J34)1 from Vibrio parahaemolyticus and 99-residue protein yiiS (gi|81722782, SwissProt/TrEMBL ID Q83IT9_SHIFL, accession number {"type":"entrez-protein","attrs":{"text":"Q83IT9","term_id":"81722782","term_text":"Q83IT9"}}Q83IT9)2, 3 from Shigella flexneri were selected as targets for the Protein Structure Initiative-2 and assigned to the Northeast Structural Genomics Consortium (NESG) for structure determination (NESG target ID VpR68 for VPA0419 and SfR90 for yiiS). VPA0419 and yiiS share 36% sequence identity, but show no significant sequence identity with any protein with known three-dimensional structure in the Protein Data Bank (PDB4). The two proteins belong to Pfam5 domain family PF04175 which currently contains 123 members with unknown three-dimensional structures and functional annotation, all of which appear to be found in gamma proteobacteria (for a sequence alignment, see Fig. S1 in Supporting Information). The NMR structures of VPA0419 and yiiS were solved using a protocol for high-throughput protein structure determination6 and represent the first ones for protein family PF04175. As these structures are the first for PF04175, “high leverage”7 of the experimental structures can be expected for calculating homology models.8, 9