Chlorine in PDB 3sew: Zn-Mediated Polymer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization (Form I)

The structure of Zn-Mediated Polymer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization (Form I), PDB code: 3sew was solved by M.Zhao, A.B.Soriaga, A.Laganowsky, M.R.Sawaya, D.Cascio, T.O.Yeates, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	66.38 / 1.55
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	85.580, 63.440, 66.390, 90.00, 90.75, 90.00
R / Rfree (%)	16.1 / 18.8

The structure of Zn-Mediated Polymer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization (Form I) also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Chlorine atom in the Zn-Mediated Polymer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization (Form I) (pdb code 3sew). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Zn-Mediated Polymer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization (Form I), PDB code: 3sew:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Zn-Mediated Polymer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization (Form I)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Zn-Mediated Polymer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization (Form I) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl374 b:16.5 occ:1.00 O A:HOH579 3.0 32.7 1.0 N A:ASP288 3.2 9.5 1.0 CB A:THR287 3.8 10.8 1.0 CA A:THR287 3.8 10.0 1.0 CG A:ASP288 3.9 8.9 1.0 OD1 A:ASP288 4.0 10.5 1.0 CB A:ASP288 4.0 9.6 1.0 C A:THR287 4.0 11.1 1.0 CA A:ASP288 4.2 9.5 1.0 OD2 A:ASP288 4.3 11.2 1.0 CG2 A:THR287 4.4 12.4 1.0 O A:HOH556 4.5 29.5 1.0 O A:HOH423 4.6 14.8 1.0 OG1 A:THR287 4.9 9.2 1.0

Chlorine binding site 2 out of 4 in the Zn-Mediated Polymer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization (Form I)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Zn-Mediated Polymer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization (Form I) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl375 b:30.5 occ:1.00 O A:HOH523 2.6 22.7 1.0 O A:HOH649 2.7 25.1 1.0 N A:GLN336 3.0 9.7 1.0 CD A:PRO335 3.3 9.6 1.0 CB A:GLN336 3.4 11.7 1.0 N A:PRO335 3.4 8.9 1.0 CB A:ILE334 3.6 9.9 1.0 CG2 A:ILE179 3.6 26.2 1.0 CA A:GLN336 3.8 10.8 1.0 CB A:PRO335 3.8 9.7 1.0 C A:PRO335 3.9 12.6 1.0 CG1 A:ILE334 3.9 9.8 1.0 CA A:PRO335 3.9 9.4 1.0 CD1 A:ILE334 3.9 12.4 1.0 CG A:PRO335 3.9 10.9 1.0 C A:ILE334 4.0 8.5 1.0 CA A:ILE334 4.4 9.9 1.0 OE1 A:GLN336 4.4 24.5 1.0 CD1 A:ILE179 4.4 28.0 1.0 O A:HOH560 4.5 29.4 1.0 CG2 A:ILE334 4.6 12.4 1.0 CG A:GLN336 4.6 19.7 1.0 CB A:ILE179 4.7 25.3 1.0 O A:ILE334 4.7 9.7 1.0 O A:PRO335 5.0 13.9 1.0

Chlorine binding site 3 out of 4 in the Zn-Mediated Polymer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization (Form I)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Zn-Mediated Polymer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization (Form I) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl376 b:16.4 occ:1.00 ZN A:ZN373 2.2 16.4 1.0 O A:HOH470 2.9 29.9 1.0 NE2 A:HIS216 3.3 16.6 1.0 OE1 A:GLU222 3.5 16.1 1.0 CE1 A:HIS216 3.5 15.8 1.0 O A:HOH650 4.1 32.3 1.0 CD2 A:HIS216 4.6 13.9 1.0 CD A:GLU222 4.6 17.9 1.0 ND1 A:HIS220 4.7 26.5 1.0 ND1 A:HIS216 4.8 12.7 1.0

Chlorine binding site 4 out of 4 in the Zn-Mediated Polymer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization (Form I)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Zn-Mediated Polymer of Maltose-Binding Protein A216H/K220H By Synthetic Symmetrization (Form I) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl380 b:21.6 occ:1.00 O A:HOH595 3.0 33.8 1.0 ND2 A:ASN151 3.3 9.8 1.0 N A:TYR211 3.4 9.8 1.0 OD1 A:ASN151 3.6 9.1 1.0 CB A:TYR211 3.7 8.0 1.0 O A:HOH425 3.7 19.7 1.0 CB A:ASP210 3.7 12.2 1.0 CG A:ASN151 3.8 7.8 1.0 CA A:TYR211 4.2 8.7 1.0 CB A:GLN153 4.3 10.8 1.0 CA A:ASP210 4.3 12.0 1.0 C A:ASP210 4.4 12.8 1.0 CG A:GLU154 4.5 12.7 1.0 CG A:ASP210 4.6 16.2 1.0 CG A:GLN153 4.6 10.3 1.0 O A:HOH419 4.7 16.9 1.0 OD2 A:ASP210 4.9 19.9 1.0

A.Laganowsky, M.Zhao, A.B.Soriaga, M.R.Sawaya, D.Cascio, T.O.Yeates. An Approach to Crystallizing Proteins By Metal-Mediated Synthetic Symmetrization. Protein Sci. V. 20 1876 2011.
ISSN: ISSN 0961-8368
PubMed: 21898649
DOI: 10.1002/PRO.727