Fig. 1.
Fig. 1. Structure of cdb3 monomer. / (A) Diagram of cdb3 secondary structure with the following sequence assignments: β157-66, β273-82, β384-88, β492–96, α1104–116, β5117–122, α2128–141, α3146–158, α4166–170, β6176–180, β7182–185, α5196–201, α6212–220, β8224–234, β9239–247, β10263–271, α7278–290, α8292–300, α9304–316, β11318–323, and α10328–347. (B) Ribbon diagram of cdb3 monomer, with blue corresponding to the peripheral protein binding domain and red to the dimerization arm. (C) Stereo drawing of the α-carbon trace for the cdb3 monomer in approximately the same orientation as in panel B. Colors change from blue at the N-terminus to red at the C-terminus.

Structure of cdb3 monomer.

(A) Diagram of cdb3 secondary structure with the following sequence assignments: β157-66, β273-82, β384-88, β492–96, α1104–116, β5117–122, α2128–141, α3146–158, α4166–170, β6176–180, β7182–185, α5196–201, α6212–220, β8224–234, β9239–247, β10263–271, α7278–290, α8292–300, α9304–316, β11318–323, and α10328–347. (B) Ribbon diagram of cdb3 monomer, with blue corresponding to the peripheral protein binding domain and red to the dimerization arm. (C) Stereo drawing of the α-carbon trace for the cdb3 monomer in approximately the same orientation as in panel B. Colors change from blue at the N-terminus to red at the C-terminus.

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