Image:Crypticrepeats.jpg

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Summary

2Fo-Fc electron density maps contoured around thymine at position ‘0’ and tryptophan 232 in the ‘−1’ repeat. b: Residues 221 to 239 and residues 256 to 273 each form a helix and an adjoining loop that resembles helix 1 and the RVD loop in the canonical repeats; the remaining residues in each region are poorly ordered. W232 forms a non polar van der Waals contact with the methyl carbon of the thymine base at position 0.

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Philipp Warmer

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(current)10:58, 3 January 2013Philipp Warmer (Talk | contribs)599×29639 KB2Fo-Fc electron density maps contoured around thymine at position ‘0’ and tryptophan 232 in the ‘−1’ repeat. b: Residues 221 to 239 and residues 256 to 273 each form a helix and an adjoining loop that resembles helix 1 and the RVD loop in the ca

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Proteopedia Page Contributors and Editors (what is this?)

Philipp Warmer

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