PDBsum entry 1kth

Structural protein

PDB id: 1kth

Contents

Protein chain

58 a.a. *

Ligands

PO4 ×2

Waters ×86

* Residue conservation analysis

PDB id:

1kth

Name:

Structural protein

Title:

The anisotropic refinement of kunitz type domain c5 at 0.95 angstrom

Structure:

Collagen alpha 3(vi) chain. Chain: a. Fragment: kunitz-type domain c5, c-terminus. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.

Resolution:

0.95Å R-factor: 0.139 R-free: 0.167

Authors:

B.Arnoux,A.Ducruix,T.Prange

Key ref:

B.Arnoux et al. (2002). Anisotropic behaviour of the C-terminal Kunitz-type domain of the alpha3 chain of human type VI collagen at atomic resolution (0.9 A). Acta Crystallogr D Biol Crystallogr, 58, 1252-1254. PubMed id: 12077460 DOI: 10.1107/S0907444902007333

Date:

16-Jan-02 Release date: 06-Feb-02

Protein chain

P12111  (CO6A3_HUMAN) -  Collagen alpha-3(VI) chain from Homo sapiens

Seq: 3177 a.a.

Struc: 58 a.a.

DOI no: 10.1107/S0907444902007333

Acta Crystallogr D Biol Crystallogr 58:1252-1254 (2002)

PubMed id: 12077460

Anisotropic behaviour of the C-terminal Kunitz-type domain of the alpha3 chain of human type VI collagen at atomic resolution (0.9 A).

B.Arnoux, A.Ducruix, T.Prangé.

ABSTRACT

The C-terminal Kunitz-type domain from the alpha3 chain of human type VI collagen (C5), a single amino-acid residue chain with three disulfide bridges, was refined at 0.9 A resolution in a monoclinic form, space group P2(1) with one molecule per asymmetric unit, using data collected at cryogenic temperature (110 K). The average protein factor decreases from 21 A(2) at room temperature (RT) to 12 A(2) at cryotemperature (100 K, CT). The spatially close N- and C-termini remain highly disordered. The different structural motifs of C5 were analyzed in terms of rigid-body displacement (TLS analyses) and show dominant libration motion for the secondary structure.

Selected figure(s)

Figure 1.
Figure 1 (a) Comparison between room-temperature (RT, red) and cryotemperature (CT, blue) average factors in residues. The residual factors after correction from a rigid-body motion are also displayed as a green curve. (b) MOLSCRIPT/RASMOL representation of the anisotropic structure (Kraulis, 1991[Kraulis, P. E. (1991). J. Appl. Cryst. 24, 946-950.]; Merritt & Bacon, 1997[Merritt, E. A. & Bacon, D. J. (1997). Methods Enzymol. 277, 505-524.]). The ellipsoids are colour-coded from blue to red over the range 4-40 Å2.

The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2002, 58, 1252-1254) copyright 2002.