Chlorine in PDB 5mus: Structure of the C-Terminal Domain of A Reptarenavirus L Protein

The structure of Structure of the C-Terminal Domain of A Reptarenavirus L Protein, PDB code: 5mus was solved by M.Rosenthal, N.Gogrefe, J.Reguera, D.Vogel, B.Rauschenberger, S.Cusack, S.Gunther, S.Reindl, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	63.95 / 2.01
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	76.392, 76.942, 116.920, 90.00, 90.00, 90.00
R / Rfree (%)	19.8 / 24.2

The binding sites of Chlorine atom in the Structure of the C-Terminal Domain of A Reptarenavirus L Protein (pdb code 5mus). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Structure of the C-Terminal Domain of A Reptarenavirus L Protein, PDB code: 5mus:

Chlorine binding site 1 out of 1 in the Structure of the C-Terminal Domain of A Reptarenavirus L Protein


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 C-Terminal Domain of A Reptarenavirus L Protein within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl2102 b:39.3 occ:1.00 N A:GLU2045 3.2 39.1 1.0 NZ B:LYS2008 3.3 33.2 1.0 CD B:LYS2008 3.5 32.8 1.0 CE1 B:HIS2006 3.6 33.5 1.0 CD2 A:LEU2044 3.6 33.7 1.0 CE B:LYS2008 3.8 32.4 1.0 CB A:GLU2045 3.8 39.4 1.0 CA A:LEU2044 3.9 30.7 1.0 CE B:LYS2009 4.0 40.7 1.0 C A:LEU2044 4.1 31.9 1.0 CB A:LEU2044 4.1 31.5 1.0 CA A:GLU2045 4.1 35.1 1.0 NE2 B:HIS2006 4.2 30.1 1.0 CB B:LYS2008 4.4 27.2 1.0 CG B:LYS2008 4.4 34.0 1.0 CG A:LEU2044 4.5 35.1 1.0 CG B:LYS2009 4.6 33.5 1.0 ND1 B:HIS2006 4.6 29.8 1.0 O A:GLU2045 4.8 33.5 1.0 OE1 A:GLU2045 4.9 57.1 1.0 OE2 A:GLU2042 4.9 44.8 1.0 CD B:LYS2009 4.9 38.0 1.0 C A:GLU2045 5.0 35.8 1.0

M.Rosenthal, N.Gogrefe, D.Vogel, J.Reguera, B.Rauschenberger, S.Cusack, S.Gunther, S.Reindl. Structural Insights Into Reptarenavirus Cap-Snatching Machinery. Plos Pathog. V. 13 06400 2017.
ISSN: ESSN 1553-7374
PubMed: 28505175
DOI: 10.1371/JOURNAL.PPAT.1006400