Chlorine in PDB 4zqw: Cdii From Escherichia Coli EC869 in Complex with A Macrocyclic Peptide

The structure of Cdii From Escherichia Coli EC869 in Complex with A Macrocyclic Peptide, PDB code: 4zqw was solved by R.P.Morse, C.W.Goulding, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.81 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	34.779, 128.166, 44.953, 90.00, 112.73, 90.00
R / Rfree (%)	18.4 / 23.1

The binding sites of Chlorine atom in the Cdii From Escherichia Coli EC869 in Complex with A Macrocyclic Peptide (pdb code 4zqw). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Cdii From Escherichia Coli EC869 in Complex with A Macrocyclic Peptide, PDB code: 4zqw:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Cdii From Escherichia Coli EC869 in Complex with A Macrocyclic Peptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Cdii From Escherichia Coli EC869 in Complex with A Macrocyclic Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl101 b:57.2 occ:1.00 N A:SER1 3.2 48.7 1.0 N A:THR13 3.2 46.0 1.0 N B:MET30 3.3 55.0 1.0 C B:GLY29 3.3 53.3 1.0 O B:GLY29 3.4 42.3 1.0 OG A:SER1 3.4 67.0 1.0 CA B:MET30 3.5 48.3 1.0 CA A:LEU12 3.5 40.5 1.0 CB A:SER1 3.6 61.7 1.0 C A:LEU12 3.8 40.5 1.0 CB A:LEU12 3.9 42.7 1.0 CB B:MET30 4.0 50.6 1.0 CA A:SER1 4.0 55.1 1.0 C A:THR13 4.1 51.8 1.0 CA B:GLY29 4.1 60.1 1.0 CA A:THR13 4.2 48.0 1.0 CD2 A:LEU12 4.3 52.1 1.0 OG1 A:THR13 4.6 51.3 1.0 O A:HOH203 4.7 45.7 1.0 CG A:LEU12 4.7 47.5 1.0 O A:GLU11 4.7 40.1 1.0 CG B:MET30 4.8 48.4 1.0 N A:LEU12 4.8 41.9 1.0 O A:LEU12 4.8 38.6 1.0 C B:MET30 4.9 44.2 1.0

Chlorine binding site 2 out of 2 in the Cdii From Escherichia Coli EC869 in Complex with A Macrocyclic Peptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Cdii From Escherichia Coli EC869 in Complex with A Macrocyclic Peptide within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl101 b:57.7 occ:1.00 N C:THR13 3.2 47.8 1.0 N C:SER1 3.2 45.5 1.0 N D:MET30 3.2 43.0 1.0 C D:GLY29 3.3 44.1 1.0 OG C:SER1 3.4 61.9 1.0 O D:GLY29 3.4 37.4 1.0 CA D:MET30 3.5 36.1 1.0 CA C:LEU12 3.5 41.2 1.0 CB C:SER1 3.6 56.8 1.0 C C:LEU12 3.7 42.3 1.0 CB C:LEU12 3.8 40.5 1.0 CB D:MET30 4.0 40.5 1.0 CA C:SER1 4.1 49.1 1.0 CA D:GLY29 4.1 48.2 1.0 C C:THR13 4.2 48.3 1.0 CA C:THR13 4.3 47.9 1.0 CD2 C:LEU12 4.3 50.4 1.0 OG1 C:THR13 4.6 51.9 1.0 CG C:LEU12 4.6 45.2 1.0 O C:HOH205 4.7 44.6 1.0 O C:GLU11 4.7 39.8 1.0 CG D:MET30 4.8 39.8 1.0 N C:LEU12 4.8 39.3 1.0 O C:LEU12 4.8 37.1 1.0 C D:MET30 4.8 35.8 1.0

R.P.Morse, J.L.Willett, P.M.Johnson, J.Zheng, A.Credali, A.Iniguez, J.S.Nowick, C.S.Hayes, C.W.Goulding. Diversification of Beta-Augmentation Interactions Between Cdi Toxin/Immunity Proteins. J.Mol.Biol. V. 427 3766 2015.
ISSN: ESSN 1089-8638
PubMed: 26449640
DOI: 10.1016/J.JMB.2015.09.020