Chlorine in PDB 6ay9: Structure of the Native Full-Length Hiv-1 Capsid Protein in Complex with CPSF6 Peptide

The structure of Structure of the Native Full-Length Hiv-1 Capsid Protein in Complex with CPSF6 Peptide, PDB code: 6ay9 was solved by A.T.Gres, K.A.Kirby, S.G.Sarafianos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.03 / 2.50
Space group	P 6
Cell size a, b, c (Å), α, β, γ (°)	92.675, 92.675, 58.042, 90.00, 90.00, 120.00
R / Rfree (%)	24.2 / 27.3

The structure of Structure of the Native Full-Length Hiv-1 Capsid Protein in Complex with CPSF6 Peptide also contains other interesting chemical elements:

Iodine

(I)

6 atoms

The binding sites of Chlorine atom in the Structure of the Native Full-Length Hiv-1 Capsid Protein in Complex with CPSF6 Peptide (pdb code 6ay9). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Structure of the Native Full-Length Hiv-1 Capsid Protein in Complex with CPSF6 Peptide, PDB code: 6ay9:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Structure of the Native Full-Length Hiv-1 Capsid Protein in Complex with CPSF6 Peptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of the Native Full-Length Hiv-1 Capsid Protein in Complex with CPSF6 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl307 b:76.9 occ:1.00 N A:ARG162 3.2 67.5 1.0 CB A:ARG162 3.6 87.0 1.0 N A:PHE161 3.6 71.1 1.0 CA A:ARG162 3.9 75.0 1.0 CB A:PHE161 4.0 77.3 1.0 C A:PHE161 4.1 68.8 1.0 CA A:PHE161 4.1 71.5 1.0 CB A:PRO160 4.2 67.4 1.0 CA A:GLN219 4.3 98.4 1.0 C A:PRO160 4.3 75.9 1.0 O A:CYS218 4.5 94.5 1.0 CA A:PRO160 4.6 73.7 1.0 NE A:ARG162 4.7 99.6 1.0 O A:MET215 4.8 75.6 1.0 O A:GLN219 4.8 99.8 1.0 CG A:ARG162 4.8 93.4 1.0 CB A:GLN219 4.8 0.6 1.0 CG A:GLN219 4.8 0.4 1.0 N A:GLN219 5.0 95.2 1.0 C A:CYS218 5.0 93.4 1.0

Chlorine binding site 2 out of 4 in the Structure of the Native Full-Length Hiv-1 Capsid Protein in Complex with CPSF6 Peptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of the Native Full-Length Hiv-1 Capsid Protein in Complex with CPSF6 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl308 b:89.3 occ:1.00 NE A:ARG167 3.1 87.3 1.0 CB A:ARG167 3.8 75.2 1.0 NH2 A:ARG167 3.8 90.5 1.0 CG A:ARG167 3.9 79.7 1.0 CD1 A:ILE153 3.9 68.8 1.0 CZ A:ARG167 3.9 88.9 1.0 CD A:ARG167 4.0 84.8 1.0 CA A:ARG167 4.6 67.7 1.0 OG1 A:THR171 4.8 79.3 1.0

Chlorine binding site 3 out of 4 in the Structure of the Native Full-Length Hiv-1 Capsid Protein in Complex with CPSF6 Peptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Structure of the Native Full-Length Hiv-1 Capsid Protein in Complex with CPSF6 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl309 b:85.3 occ:1.00 O A:ASP152 3.5 67.8 1.0 CB A:ASP152 3.9 77.3 1.0 C A:ASP152 4.2 70.6 1.0 NH2 A:ARG167 4.6 90.5 1.0 CA A:ASP152 4.7 76.1 1.0 CD1 A:ILE153 4.9 68.8 1.0 N A:ILE153 5.0 73.3 1.0

Chlorine binding site 4 out of 4 in the Structure of the Native Full-Length Hiv-1 Capsid Protein in Complex with CPSF6 Peptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Structure of the Native Full-Length Hiv-1 Capsid Protein in Complex with CPSF6 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl310 b:85.3 occ:1.00 CG A:PRO38 3.3 72.3 1.0 CD A:PRO38 3.7 64.3 1.0 O A:HOH424 3.7 63.7 1.0 I A:IOD303 4.0 0.4 0.7 NH2 A:ARG173 4.0 59.4 1.0 CB A:PRO38 4.5 63.3 1.0 N A:PRO38 4.6 57.2 1.0 NE A:ARG173 4.9 46.6 1.0 CG2 A:ILE37 4.9 52.5 1.0 CZ A:ARG173 4.9 51.6 1.0 CA A:PRO38 4.9 60.6 1.0 CB A:ILE37 5.0 52.9 1.0

A.T.Gres, K.A.Kirby, S.G.Sarafianos. Characterization of Hiv-1 Capsid Interactions with Host Cell Factors To Be Published.