Chlorine in PDB 5wo2: Chaperone Spy Bound to Casein Fragment (Casein Un-Modeled)

The structure of Chaperone Spy Bound to Casein Fragment (Casein Un-Modeled), PDB code: 5wo2 was solved by S.Horowitz, P.Koldewey, R.Martin, J.C.A.Bardwell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.76 / 1.77
Space group	P 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	42.960, 42.960, 258.169, 90.00, 90.00, 90.00
R / Rfree (%)	21.5 / 25.2

The structure of Chaperone Spy Bound to Casein Fragment (Casein Un-Modeled) also contains other interesting chemical elements:

Zinc

(Zn)

24 atoms

The binding sites of Chlorine atom in the Chaperone Spy Bound to Casein Fragment (Casein Un-Modeled) (pdb code 5wo2). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Chaperone Spy Bound to Casein Fragment (Casein Un-Modeled), PDB code: 5wo2:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Chaperone Spy Bound to Casein Fragment (Casein Un-Modeled)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Chaperone Spy Bound to Casein Fragment (Casein Un-Modeled) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl209 b:55.4 occ:1.00 ZN A:ZN208 2.3 28.1 1.0 HB3 A:ARG61 2.9 53.9 1.0 HE1 B:PHE119 2.9 40.1 1.0 HD1 B:PHE119 3.0 38.8 1.0 HA A:ARG62 3.0 47.0 1.0 HB2 A:HIS65 3.1 44.1 1.0 O B:HOH331 3.1 39.4 1.0 HG2 A:ARG62 3.3 64.7 1.0 O A:ARG61 3.5 37.2 1.0 OE1 B:GLU120 3.5 37.3 1.0 C A:ARG61 3.6 38.9 1.0 CE1 B:PHE119 3.6 33.4 1.0 CD1 B:PHE119 3.6 32.3 1.0 N A:ARG62 3.7 40.0 1.0 CB A:ARG61 3.7 44.9 1.0 CA A:ARG62 3.7 39.2 1.0 HB2 A:ARG61 3.8 53.9 1.0 ND1 A:HIS65 3.8 39.3 1.0 OE2 B:GLU120 3.9 32.3 1.0 CB A:HIS65 3.9 36.7 1.0 CD B:GLU120 4.0 34.9 1.0 HA B:GLU120 4.0 43.7 1.0 CG A:ARG62 4.1 53.9 1.0 H A:ARG62 4.1 48.0 1.0 HB3 A:HIS65 4.1 44.1 1.0 HG3 A:ARG62 4.1 64.7 1.0 CG A:HIS65 4.2 36.7 1.0 CA A:ARG61 4.3 40.4 1.0 HE A:ARG61 4.4 59.5 1.0 CB A:ARG62 4.5 45.6 1.0 H A:HIS65 4.6 40.0 1.0 O B:HOH329 4.7 36.0 1.0 HA A:ARG61 4.7 48.5 1.0 O B:PHE119 4.8 33.9 1.0 CE1 A:HIS65 4.8 42.0 1.0 CG A:ARG61 4.9 48.3 1.0 HG3 A:ARG61 4.9 57.9 1.0 CZ B:PHE119 4.9 33.7 1.0 CG B:PHE119 4.9 32.9 1.0 HB3 A:ARG62 4.9 54.7 1.0 NE A:ARG61 4.9 49.6 1.0 C A:ARG62 4.9 36.9 1.0 CA B:GLU120 5.0 36.4 1.0

Chlorine binding site 2 out of 2 in the Chaperone Spy Bound to Casein Fragment (Casein Un-Modeled)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Chaperone Spy Bound to Casein Fragment (Casein Un-Modeled) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl214 b:19.6 occ:0.51 ZN B:ZN202 2.3 25.2 0.7 HG2 B:ARG62 2.9 58.0 1.0 HG3 B:ARG61 2.9 69.7 1.0 HA B:ARG62 3.0 52.7 1.0 HE1 A:PHE119 3.0 50.9 1.0 HD1 A:PHE119 3.0 50.4 1.0 H2 B:IMD201 3.1 43.1 1.0 HB2 B:HIS65 3.1 41.4 1.0 HG2 B:ARG61 3.2 69.7 1.0 OE2 A:GLU120 3.2 45.5 1.0 HN3 B:IMD201 3.3 41.7 1.0 CG B:ARG61 3.5 58.1 1.0 CD1 A:PHE119 3.6 42.0 1.0 CE1 A:PHE119 3.6 42.4 1.0 C2 B:IMD201 3.6 36.0 1.0 ND1 B:HIS65 3.6 32.4 1.0 N3 B:IMD201 3.7 34.8 1.0 CA B:ARG62 3.8 43.9 1.0 CB B:HIS65 3.8 34.5 1.0 HB3 B:HIS65 3.8 41.4 1.0 CG B:ARG62 3.9 48.4 1.0 O B:ARG61 3.9 42.7 1.0 CD A:GLU120 3.9 38.7 1.0 N B:ARG62 3.9 45.4 1.0 HE B:ARG61 4.0 81.3 1.0 C B:ARG61 4.0 46.0 1.0 OE1 A:GLU120 4.1 41.6 1.0 HE B:ARG62 4.1 70.8 1.0 CG B:HIS65 4.1 32.0 1.0 HA A:GLU120 4.1 49.9 1.0 HB3 B:ARG61 4.2 67.3 1.0 HG3 B:ARG62 4.3 58.0 1.0 CB B:ARG62 4.3 46.1 1.0 H B:ARG62 4.4 54.5 1.0 CB B:ARG61 4.4 56.0 1.0 HB3 B:ARG62 4.6 55.3 1.0 NE B:ARG61 4.6 67.8 1.0 CD B:ARG61 4.6 63.9 1.0 NE B:ARG62 4.7 59.0 1.0 CE1 B:HIS65 4.7 32.0 1.0 CD B:ARG62 4.7 52.5 1.0 H B:HIS65 4.8 41.8 1.0 O A:PHE119 4.8 44.1 1.0 N1 B:IMD201 4.8 37.5 1.0 HD3 B:ARG62 4.8 63.0 1.0 CA B:ARG61 4.9 51.6 1.0 CZ A:PHE119 4.9 42.3 1.0 CG A:PHE119 4.9 40.9 1.0 C4 B:IMD201 4.9 33.9 1.0 HE1 B:HIS65 4.9 38.4 1.0 C B:ARG62 5.0 40.3 1.0

S.Horowitz, L.Salmon, P.Koldewey, L.S.Ahlstrom, R.Martin, S.Quan, P.V.Afonine, H.Van Den Bedem, L.Wang, Q.Xu, R.C.Trievel, C.L.Brooks, J.C.Bardwell. Visualizing Chaperone-Assisted Protein Folding. Nat. Struct. Mol. Biol. V. 23 691 2016.
ISSN: ESSN 1545-9985
PubMed: 27239796
DOI: 10.1038/NSMB.3237