Chlorine in PDB 6nl8: Crystal Structure of De Novo Designed Metal-Controlled Dimer of Mutant B1 Immunoglobulin-Binding Domain of Streptococcal Protein G (L12H, T16L, V29H, Y33H, N37L)-Zinc

The structure of Crystal Structure of De Novo Designed Metal-Controlled Dimer of Mutant B1 Immunoglobulin-Binding Domain of Streptococcal Protein G (L12H, T16L, V29H, Y33H, N37L)-Zinc, PDB code: 6nl8 was solved by B.Maniaci, S.Boguslaw, T.Huxford, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.94 / 1.50
Space group	I 41
Cell size a, b, c (Å), α, β, γ (°)	69.828, 69.828, 24.157, 90.00, 90.00, 90.00
R / Rfree (%)	12.8 / 16.3

The structure of Crystal Structure of De Novo Designed Metal-Controlled Dimer of Mutant B1 Immunoglobulin-Binding Domain of Streptococcal Protein G (L12H, T16L, V29H, Y33H, N37L)-Zinc also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Chlorine atom in the Crystal Structure of De Novo Designed Metal-Controlled Dimer of Mutant B1 Immunoglobulin-Binding Domain of Streptococcal Protein G (L12H, T16L, V29H, Y33H, N37L)-Zinc (pdb code 6nl8). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of De Novo Designed Metal-Controlled Dimer of Mutant B1 Immunoglobulin-Binding Domain of Streptococcal Protein G (L12H, T16L, V29H, Y33H, N37L)-Zinc, PDB code: 6nl8:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of De Novo Designed Metal-Controlled Dimer of Mutant B1 Immunoglobulin-Binding Domain of Streptococcal Protein G (L12H, T16L, V29H, Y33H, N37L)-Zinc


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of De Novo Designed Metal-Controlled Dimer of Mutant B1 Immunoglobulin-Binding Domain of Streptococcal Protein G (L12H, T16L, V29H, Y33H, N37L)-Zinc within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl103 b:31.0 occ:1.00 NE2 A:HIS33 2.5 40.9 1.0 CE1 A:HIS33 2.5 40.7 1.0 ZN A:ZN102 2.7 35.9 1.0 NE2 A:HIS29 2.7 32.5 1.0 CE1 A:HIS29 3.0 43.7 1.0 CD2 A:HIS29 3.5 35.2 1.0 ND1 A:HIS33 3.8 36.1 1.0 CD2 A:HIS33 3.8 48.0 1.0 ND1 A:HIS29 3.9 31.9 1.0 CG A:HIS29 4.1 32.9 1.0 CG A:HIS33 4.5 36.5 1.0 CL A:CL104 4.9 36.7 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of De Novo Designed Metal-Controlled Dimer of Mutant B1 Immunoglobulin-Binding Domain of Streptococcal Protein G (L12H, T16L, V29H, Y33H, N37L)-Zinc


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of De Novo Designed Metal-Controlled Dimer of Mutant B1 Immunoglobulin-Binding Domain of Streptococcal Protein G (L12H, T16L, V29H, Y33H, N37L)-Zinc within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl104 b:36.7 occ:1.00 ZN A:ZN102 2.2 35.9 1.0 O A:THR17 3.0 31.9 1.0 C A:THR17 3.7 26.0 1.0 NE2 A:HIS29 3.8 32.5 1.0 CB A:LEU16 3.8 22.5 1.0 NE2 A:HIS33 3.8 40.9 1.0 CD2 A:HIS33 3.8 48.0 1.0 CB A:THR18 3.9 29.2 1.0 N A:THR17 4.0 21.2 1.0 CE1 A:PHE30 4.1 24.4 1.0 N A:THR18 4.4 21.6 1.0 OG1 A:THR18 4.4 44.5 1.0 C A:LEU16 4.4 22.4 1.0 CD2 A:HIS29 4.5 35.2 1.0 CA A:THR17 4.5 23.4 1.0 CA A:THR18 4.6 24.6 1.0 CD1 A:LEU16 4.6 29.4 1.0 CA A:LEU16 4.6 21.7 1.0 CG A:LEU16 4.6 25.9 1.0 CD1 A:PHE30 4.8 21.4 1.0 CD2 A:LEU16 4.8 32.6 1.0 CE1 A:HIS29 4.9 43.7 1.0 CG2 A:THR18 4.9 30.1 1.0 CL A:CL103 4.9 31.0 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of De Novo Designed Metal-Controlled Dimer of Mutant B1 Immunoglobulin-Binding Domain of Streptococcal Protein G (L12H, T16L, V29H, Y33H, N37L)-Zinc


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of De Novo Designed Metal-Controlled Dimer of Mutant B1 Immunoglobulin-Binding Domain of Streptococcal Protein G (L12H, T16L, V29H, Y33H, N37L)-Zinc within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl105 b:24.4 occ:1.00 ZN A:ZN101 2.2 21.2 1.0 O A:HOH203 3.3 35.3 1.0 N A:MET1 3.4 20.7 1.0 CA A:MET1 3.5 20.1 0.7 OE1 A:GLU19 3.6 27.6 1.0 OE2 A:GLU19 3.6 26.4 1.0 CA A:MET1 3.7 20.2 0.3 CD A:GLU19 3.9 29.3 1.0 C A:MET1 4.4 20.7 1.0 CG A:MET1 4.6 24.9 0.7 CB A:MET1 4.6 21.6 0.7 SD A:MET1 4.7 23.2 0.3 N A:THR2 4.7 19.2 1.0 O A:HOH230 4.8 37.0 1.0 CB A:MET1 5.0 18.4 0.3

B.Maniaci, C.H.Lipper, D.L.Anipindi, H.Erlandsen, J.L.Cole, B.Stec, T.Huxford, J.J.Love. Design of High-Affinity Metal-Controlled Protein Dimers. Biochemistry V. 58 2199 2019.
ISSN: ISSN 0006-2960
PubMed: 30938154
DOI: 10.1021/ACS.BIOCHEM.9B00055