Erratum: Crystal structures of collagen model peptides with Pro-Hyp-Gly repeating sequence at 1.26 Å resolution: Implications for proline ring puckering, Kenji Okuyama, Chizuru Hongo, Rie Fukushima, Guanghan Wu, Hirotaka Narita, Keiichi Noguchi, Yuji Tanaka, Norikazu Nishino, Biopolymers (Peptide Science)(2004)76(5) 367–377
Abstract
The original article to which this Erratum refers was published in Biopolymers (Peptide Science) (2004) 76(5) 367–377
Please note correction to the above article: For Table III in the above article, an error was made in the identification of the column heads. The amended Table III, on the next page, shows the correct table configuration. We apologize for any confusion caused by this error.
Temperature: Resolution (Å): | This study | POG10R_N RT 1.9 | PPG10R_N RT 1.9 | PPG10R′_K1 259 K 1.97 | PPG10R_K2 RT 1.60 | PPG10R_V RT 1.30 | PPG9R_H RT 1.0 | ||
---|---|---|---|---|---|---|---|---|---|
POG11L_O 100 K 1.26 | POG11R_O RT 1.25 | POG10L_O 100 K 1.25 | |||||||
χ1 at the X position | |||||||||
X1 | −20.0 | 16.0 | −11.0 | 32.3 | 23.8 | 36.0 | 37.5 | 28.9 | 21.7 |
X2 | −25.4 | −6.5 | −23.5 | 18.6 | 34.4 | 38.2 | 31.2 | 33.1 | 29.4 |
X3 | 13.5 | 15.0 | 16.4 | 26.8 | 0.9 | 31.4 | 29.3 | 24.5 | 20.6 |
X4 | 36.0 | 26.0 | 33.7 | 16.4 | 2.2 | 29.7 | 28.9 | 26.4 | 30.7 |
X5 | 34.5 | 11.4 | 25.2 | 37.0 | 27.6 | 35.5 | 29.2 | 26.5 | 25.7 |
X6 | 26.8 | 26.4 | 20.6 | 28.9 | 25.6 | 31.7 | 29.9 | 26.7 | 32.5 |
X7 | −18.1 | 22.9 | −16.3 | 29.2 | 23.6 | 35.8 | 30.0 | 28.9 | 31.0 |
χ1 at the Y position | |||||||||
Y1 | −25.6 | −21.9 | −27.9 | −26.6 | −10.1a | −29.4 | −22.5 | −11.4 | 7.8a |
Y2 | −24.6 | −24.8 | −24.2 | −19.5 | 15.1 | −34.9 | −10.4 | −19.4 | −25.9 |
Y3 | −24.9 | −26.5 | −24.8 | −16.0 | −14.2 | −19.7 | −14.9 | −26.5 | −24.5 |
Y4 | −19.6 | −20.7 | −20.6 | −20.5 | 22.0 | −33.7 | −26.1 | −22.0 | −18.7 |
Y5 | −23.4 | −24.3 | −29.0 | −24.5 | −24.0 | −26.6 | −18.2 | −21.6 | −25.2 |
Y6 | −24.4 | −23.3 | −25.4 | −25.2 | 15.1 | −30.3 | −15.3 | −13.2 | −21.2 |
Y7 | −25.2 | −24.2 | −26.2 | −15.7 | −12.2 | 25.5a | −13.0a | −9.0a | −13.5 |
- a Y positions having marked χ1 values in the Gly-Pro-Pro sequence are located in similar positions in lateral packing. Therefore, these Pro residues have similar interaction with adjacent triple helices.