Comparison of aggregation predictions and experimental available data for human globular proteins and proximity of aggregation-prone regions to predicted and real interfaces.

1Percentage of residues in the aggregation-prone region at less than 3 Å from a protein predicted interaction residue.
2Percentage of residues in the aggregation-prone region at less than 3 Å from a residue located at the interface of the following complexes: β2-microglubulin in complex with HLA heavy chain [1DUZ] and with HFE [1A6Z]. Native tetrameric structure of transthyretin (PDB code 1TTA). Dimeric structure of SOD1 (PDB code 2C9V). Lysozyme in complex with a camelid antibody (PDB code 1OP9). Dimeric structure of Immunoglobulin LC variable domain (PDB code 2Q20). HCs and LCs of a IgG1 human immunoglobulin (PDB code 1HZH).
1,2In brackets the percentage of residues in the aggregation-prone region close to a random surface of the same size than the considered interface.

1. 易聚集区域（aggregation-prone region）内，与蛋白质预测互作残基距离小于3埃的残基占比。
2. 易聚集区域内，与以下复合物界面处残基距离小于3埃的残基占比：与人类白细胞抗原（HLA）重链结合的β2微球蛋白（β2-microglobulin，PDB编号1DUZ）以及与HFE结合的β2微球蛋白（PDB编号1A6Z）；运甲状腺素蛋白的天然四聚体结构（PDB编号1TTA）；超氧化物歧化酶1（SOD1）的二聚体结构（PDB编号2C9V）；与骆驼科抗体结合的溶菌酶（PDB编号1OP9）；免疫球蛋白轻链可变结构域的二聚体结构（PDB编号2Q20）；人IgG1免疫球蛋白的重链（HCs）与轻链（LCs）（PDB编号1HZH）。
针对上述1、2两项指标，括号内的数值为易聚集区域内，与所研究界面尺寸相同的随机表面接近的残基占比。