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Figure 1 | BMC Structural Biology

Figure 1

From: Structure determination of human Lck unique and SH3 domains by nuclear magnetic resonance spectroscopy

Figure 1

Number of experimental distance constraints per residue and dynamic behavior of Lck unique and SH3 domains, as well as local precision of SH3 domain conformation. A: Number of intraresidual (black), sequential (light gray), medium (dark gray) and long range (white) NOE distance constraints per residue of Lck(1–120). B: Heteronuclear 1H-15N-NOE values of Lck(1120) amide resonances. Proline residues are indicated (P), the position of the unique and the SH3 domains are marked with labeled horizontal bars. C: Average local displacement values among the 25 obtained solution structures of Lck(64–120). For each three-residue window the average displacement of the backbone atoms was calculated and plotted against the residue number that corresponds to the central residue of the window. Location of secondary structure elements is given at the bottom.

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