Volume 80, Issue 5 pp. 714-715
Erratum
Free Access

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

Kenji Okuyama

Kenji Okuyama

Faculty of Technology, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan

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Chizuru Hongo

Chizuru Hongo

Faculty of Technology, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan

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Rie Fukushima

Rie Fukushima

Faculty of Technology, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan

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Guanghan Wu

Guanghan Wu

Faculty of Technology, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan

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Hirotaka Narita

Hirotaka Narita

Faculty of Technology, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan

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Keiichi Noguchi

Keiichi Noguchi

Faculty of Technology, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan

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Yuji Tanaka

Yuji Tanaka

Faculty of Engineering, Kyushu Institute of Technology, Kitakyushu 804-8550, Japan

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Norikazu Nishino

Norikazu Nishino

Faculty of Engineering, Kyushu Institute of Technology, Kitakyushu 804-8550, Japan

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First published: 28 March 2005
Citations: 1

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.

Table III. Conformational Angles of χ1 of Proline Ring Puckering at the X and Y Positions in the X-Y-Gly Sequence
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 −10.1 −29.4 −22.5 −11.4 7.8
 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 25.5 −13.0 −9.0 −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.

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