TABLE 1.

Crystallographic statistics for the Fv4E10[W(H100)A] epitope/peptide complex structure

ParameterValuea
Data collection
    Space groupP6522
    Cell dimensions (Å)a = b = 92.4, c = 272.8
    Resolution (Å)69.02-2.70 (2.80-2.70)
    No. of observed reflections89,106 (8,305)
    No. of unique reflections19,557 (1,937)
    Redundancy4.56 (4.29)
    Completeness (%)98.6 (99.6)
    Rmerge0.104 (0.347)
    Avg I/σ(I)7.5 (2.9)
Structure refinement
    Resolution (Å)60.08-2.70
    Rwork/Rfree0.229/0.287
    No. of atoms
        Protein3,794
        Water55
        Other (Ca2+)1
    RMSD from ideal values
        Bond lengths (Å)0.008
        Bond angles (°)1.109
        Chiral vol (Å3)0.061
    Ramachandran plot statistics (Procheck)
        Residues in most favored regions (%)88.0
        Residues in additional allowed regions (%)11.5
        Residues in generously allowed regions (%)0.0
        Residues in disallowed regions (%)0.5 (2 residuesb)
        Est. coordinate error (max. likelihood ESUc) (Å)0.26
    Avg B-factor (molecule A/molecule B)
        Fv light chains68.8/59.5
        Fv heavy chains53.7/52.9
        Epitope scaffolds69.0/70.7
        Waters47.3
  • a Values in parentheses are for the highest-resolution shell.

  • b Fv light chain residue 52 (51 by Kabat numbering) is in a highly conserved γ-turn.

  • c ESU, estimated standard uncertainty.