Chlorine in PDB 5wnw: Chaperone Spy Bound to IM7 6-45 Ensemble

The structure of Chaperone Spy Bound to IM7 6-45 Ensemble, PDB code: 5wnw was solved by S.Horowitz, L.Salmon, P.Koldewey, L.S.Ahlstrom, R.Martin, Q.Xu, P.V.Afonine, R.C.Trievel, C.L.Brooks, J.C.A.Bardwell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.49 / 1.79
Space group	P 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	42.900, 42.900, 260.200, 90.00, 90.00, 90.00
R / Rfree (%)	21.8 / 23.8

The structure of Chaperone Spy Bound to IM7 6-45 Ensemble also contains other interesting chemical elements:

Zinc

(Zn)

13 atoms

The binding sites of Chlorine atom in the Chaperone Spy Bound to IM7 6-45 Ensemble (pdb code 5wnw). 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 IM7 6-45 Ensemble, PDB code: 5wnw:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Chaperone Spy Bound to IM7 6-45 Ensemble


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 IM7 6-45 Ensemble within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl206 b:37.4 occ:0.91 ZN A:ZN205 2.3 31.2 0.6 HA B:ARG62 2.8 50.1 1.0 HN3 A:IMD201 3.0 47.6 1.0 HE1 A:PHE119 3.0 58.5 1.0 HD1 A:PHE119 3.0 62.5 1.0 HB2 B:HIS65 3.2 55.4 1.0 HG2 B:ARG61 3.3 72.2 0.6 HG3 B:ARG61 3.3 72.2 0.6 O A:HOH311 3.4 56.8 1.0 OE2 A:GLU120 3.4 43.4 1.0 N3 A:IMD201 3.5 39.7 1.0 H2 A:IMD201 3.5 49.1 1.0 O B:ARG61 3.6 40.4 0.5 O B:ARG61 3.6 40.3 0.6 CE1 A:PHE119 3.6 48.8 1.0 CD1 A:PHE119 3.6 52.1 1.0 ND1 B:HIS65 3.7 37.6 1.0 CA B:ARG62 3.7 41.8 1.0 CG B:ARG61 3.7 60.2 0.6 HE B:ARG62 3.7 73.6 1.0 C B:ARG61 3.8 39.6 0.5 C B:ARG61 3.8 42.8 0.6 C2 A:IMD201 3.8 41.0 1.0 N B:ARG62 3.8 42.4 1.0 HB3 B:ARG61 3.8 72.1 0.5 HB3 B:ARG61 3.9 72.3 0.6 CB B:HIS65 3.9 46.2 1.0 HB2 B:ARG61 4.0 72.1 0.5 OE1 A:GLU120 4.0 50.8 1.0 HB3 B:HIS65 4.0 55.4 1.0 CD A:GLU120 4.0 50.7 1.0 HG3 B:ARG62 4.1 74.5 1.0 HA A:GLU120 4.1 47.0 1.0 CG B:HIS65 4.2 35.8 1.0 CB B:ARG61 4.3 60.3 0.6 H B:ARG62 4.3 50.8 1.0 HB2 B:ARG62 4.3 58.5 1.0 CB B:ARG61 4.3 60.1 0.5 CB B:ARG62 4.5 48.8 1.0 HH21 B:ARG62 4.5 93.2 1.0 NE B:ARG62 4.6 61.3 1.0 C4 A:IMD201 4.6 41.5 1.0 HE B:ARG61 4.6 69.9 0.6 CA B:ARG61 4.7 58.1 0.6 CA B:ARG61 4.7 58.4 0.5 O A:PHE119 4.7 49.6 1.0 CE1 B:HIS65 4.7 35.4 1.0 CG B:ARG62 4.7 62.1 1.0 H B:HIS65 4.8 45.2 1.0 C B:ARG62 4.8 50.8 1.0 O B:ARG62 4.9 40.0 1.0 N1 A:IMD201 4.9 46.5 1.0 CG A:PHE119 5.0 46.1 1.0 HE1 B:HIS65 5.0 42.4 1.0 CZ A:PHE119 5.0 42.4 1.0 O A:HOH322 5.0 54.6 1.0

Chlorine binding site 2 out of 2 in the Chaperone Spy Bound to IM7 6-45 Ensemble


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 IM7 6-45 Ensemble within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl203 b:31.9 occ:1.00 ZN A:ZN208 2.2 27.2 0.5 O B:HOH344 3.0 52.1 1.0 HA A:ARG62 3.0 40.0 1.0 HB2 A:HIS65 3.1 35.7 1.0 HD1 B:PHE119 3.1 41.2 1.0 HG2 A:ARG62 3.1 71.5 1.0 HE1 B:PHE119 3.2 42.5 1.0 HB3 A:ARG61 3.2 57.5 1.0 OE2 B:GLU120 3.5 39.1 1.0 ND1 A:HIS65 3.5 36.2 1.0 OE1 B:GLU120 3.6 43.7 1.0 O A:ARG61 3.7 33.8 1.0 CD1 B:PHE119 3.7 34.4 1.0 C A:ARG61 3.8 35.7 1.0 CA A:ARG62 3.8 33.4 1.0 CB A:HIS65 3.8 29.8 1.0 CE1 B:PHE119 3.8 35.4 1.0 CD B:GLU120 3.9 39.2 1.0 N A:ARG62 3.9 38.7 1.0 O A:HOH302 3.9 52.1 1.0 HB3 A:HIS65 3.9 35.7 1.0 CG A:ARG62 4.0 59.6 1.0 HA B:GLU120 4.0 46.5 1.0 CB A:ARG61 4.0 48.0 1.0 HB2 A:ARG61 4.1 57.5 1.0 CG A:HIS65 4.1 35.2 1.0 HG3 A:ARG62 4.1 71.5 1.0 H A:ARG62 4.4 46.4 1.0 CB A:ARG62 4.5 44.8 1.0 CA A:ARG61 4.6 38.7 1.0 CE1 A:HIS65 4.6 36.4 1.0 H A:HIS65 4.7 39.0 1.0 HD21 A:LEU58 4.8 0.2 1.0 O B:HOH336 4.8 46.2 1.0 HE A:ARG61 4.8 78.2 1.0 O B:PHE119 4.9 38.0 1.0 HE1 A:HIS65 4.9 43.6 1.0 CA B:GLU120 4.9 38.8 1.0 HB3 A:ARG62 4.9 53.7 1.0 C A:ARG62 5.0 31.2 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