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Criterion (A) is passed narrowly: length 5 has 9,555 strands and length 4 has 9,404 (1.6% apart), with length 6 at 8,666 and lengths 2 and 3 at 8,327 and 8,016; the distribution is a broad plateau over 2 to 6 residues rather than a sharp peak, so the mode is in [3, 6] but would be fragile to a different assignment method. Strand assignments are PDBe's as served by the secondary_structure endpoint. The PDBe API documentation (openapi.json, retrieved 2026-11-08) describes them only as 'residue ranges of regular secondary structures (alpha helices and beta strands)' and does not name the method; whether they are the depositors' mmCIF struct_sheet_range records or a DSSP-style recomputation is not stated there and was not verified. Lengths use PDBe's mmCIF residue_number, so author numbering gaps do not affect them. Lengths are in residues, mapped to the model's 3-4 hydrogen bonds by the pre-registered assumption (band [3, 6] residues); no hydrogen bonds were measured. Sampling biases: the PDB over-represents crystallisable, well-folded proteins and the filter keeps only X-ray entries at or better than 2.5 A; the representative is the first entity of each cluster in file order (an arbitrary, not a quality-based, choice) and the first chain listed for that entity; clusters are at 30% sequence identity at the entity level, so fold-level redundancy remains; the 15,500 representatives screened are the first 5.7% of the 272,527 clusters, and the cluster file is sorted by cluster size, so the sample is drawn from the largest families; 631 chains with no strand of at least 2 residues were excluded by design, so the distribution is conditional on a chain having a strand; the exptl.method exact match on 'X-RAY DIFFRACTION' also admits hybrid X-ray entries. 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