Effective neutralizing human antibodies have unusual features, a result of unusual recombination, somatic mutation, or both. CD4-binding site antibodies, represented here by VRC01. A number of effective neutralizers use mimicry of CD4 by their heavy chain to affect near-pan-neutralization. All of these derive from similar VH genes, VH1-2 or VH1-46, but otherwise display a variety of CDR H3 lengths and Vκ or Vλ partners. Deep sequencing and systems-level bioinformatics allow specific CDR H3 lineages to be traced to identify thousands of clonal variants. For VRC01, only the more highly affinity matured antibodies are capable of neutralizing HIV-1. V1V2-directed antibodies, represented here by PG9. All V1V2-directed broadly neutralizing antibodies identified to date display unusually long CDR H3s. These are likely required to penetrate the glycan shield to reach conserved features of Env protein surface. For PG9, recombination that generates a 29-amino acid CDR H3 appears to occur as an early event, with somatic mutation fine-tuning glycan recognition. Glycan-V3-directed antibodies, represented here by PGT128. Antibodies directed towards this site are highly diverse. Some, such as PGT128 have CDR H3s that are not so unusual, but display high degrees of somatic mutation. MPER-directed antibodies, represented here by 10E8. These gp41-directed neutralizers are quite diverse, with some such as 2F5, Z13 and 4E10 requiring significant degrees of β-strand interactions, while 10E8 interacts entirely through its CDR loops. Despite this diversity, all show moderately long CDR H3s and unusual degrees of somatic mutation.