Chlorine in PDB 6u52: Anti-Sudan Ebolavirus Nucleoprotein Single Domain Antibody Sudan B (Sb) Complexed with Sudan Ebolavirus Nucleoprotein C-Terminal Domain 634-738

The structure of Anti-Sudan Ebolavirus Nucleoprotein Single Domain Antibody Sudan B (Sb) Complexed with Sudan Ebolavirus Nucleoprotein C-Terminal Domain 634-738, PDB code: 6u52 was solved by A.B.Taylor, L.J.Sherwood, P.J.Hart, A.Hayhurst, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.31 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	173.977, 44.984, 66.438, 90.00, 105.94, 90.00
R / Rfree (%)	19.8 / 24.3

The binding sites of Chlorine atom in the Anti-Sudan Ebolavirus Nucleoprotein Single Domain Antibody Sudan B (Sb) Complexed with Sudan Ebolavirus Nucleoprotein C-Terminal Domain 634-738 (pdb code 6u52). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 5 binding sites of Chlorine where determined in the Anti-Sudan Ebolavirus Nucleoprotein Single Domain Antibody Sudan B (Sb) Complexed with Sudan Ebolavirus Nucleoprotein C-Terminal Domain 634-738, PDB code: 6u52:
Jump to Chlorine binding site number: 1; 2; 3; 4; 5;

Chlorine binding site 1 out of 5 in the Anti-Sudan Ebolavirus Nucleoprotein Single Domain Antibody Sudan B (Sb) Complexed with Sudan Ebolavirus Nucleoprotein C-Terminal Domain 634-738


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Anti-Sudan Ebolavirus Nucleoprotein Single Domain Antibody Sudan B (Sb) Complexed with Sudan Ebolavirus Nucleoprotein C-Terminal Domain 634-738 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:43.6 occ:1.00 O A:HOH337 3.0 39.4 1.0 O A:HOH353 3.2 39.0 1.0 N A:TYR59 3.4 34.3 1.0 NZ A:LYS64 3.4 57.9 1.0 CA A:ILE58 3.8 31.2 1.0 CD1 A:TYR59 3.9 33.9 1.0 CD A:LYS64 3.9 52.5 1.0 CE A:LYS64 3.9 53.8 1.0 C A:ILE58 4.0 34.6 1.0 CG1 A:ILE58 4.2 39.4 1.0 CG A:LYS64 4.2 45.1 1.0 CB A:TYR59 4.3 39.0 1.0 CA A:TYR59 4.3 38.7 1.0 O A:TYR59 4.4 36.9 1.0 O A:THR57 4.4 41.2 1.0 CB A:ILE58 4.6 33.6 1.0 CG A:TYR59 4.6 33.5 1.0 N A:ILE58 4.7 34.5 1.0 C A:TYR59 4.8 36.7 1.0 CE1 A:TYR59 4.9 32.5 1.0 C A:THR57 4.9 34.6 1.0

Chlorine binding site 2 out of 5 in the Anti-Sudan Ebolavirus Nucleoprotein Single Domain Antibody Sudan B (Sb) Complexed with Sudan Ebolavirus Nucleoprotein C-Terminal Domain 634-738


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Anti-Sudan Ebolavirus Nucleoprotein Single Domain Antibody Sudan B (Sb) Complexed with Sudan Ebolavirus Nucleoprotein C-Terminal Domain 634-738 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl801 b:45.4 occ:1.00 ND1 B:HIS654 2.8 33.9 1.0 N C:LEU47 3.2 32.6 1.0 CE1 B:HIS654 3.6 34.7 1.0 CA C:GLU46 3.7 35.0 1.0 CG B:HIS654 3.8 37.0 1.0 CB C:LEU47 3.9 31.3 1.0 C C:GLU46 3.9 35.4 1.0 CB B:HIS654 4.1 29.2 1.0 CD2 B:LEU655 4.1 37.5 1.0 CG2 B:THR651 4.1 27.2 1.0 CA C:LEU47 4.1 33.4 1.0 CB C:GLU46 4.3 38.9 1.0 CG B:LEU655 4.4 31.9 1.0 CG C:GLU46 4.5 55.0 1.0 O C:ARG45 4.5 45.8 1.0 O C:HOH322 4.7 55.2 1.0 O B:THR651 4.7 28.9 1.0 O C:LEU47 4.8 36.8 1.0 NE2 B:HIS654 4.8 39.5 1.0 N C:GLU46 4.9 43.1 1.0 N B:LEU655 4.9 27.8 1.0 CD2 B:HIS654 4.9 41.1 1.0 CA B:THR651 5.0 34.8 1.0 C C:LEU47 5.0 31.0 1.0

Chlorine binding site 3 out of 5 in the Anti-Sudan Ebolavirus Nucleoprotein Single Domain Antibody Sudan B (Sb) Complexed with Sudan Ebolavirus Nucleoprotein C-Terminal Domain 634-738


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Anti-Sudan Ebolavirus Nucleoprotein Single Domain Antibody Sudan B (Sb) Complexed with Sudan Ebolavirus Nucleoprotein C-Terminal Domain 634-738 within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl201 b:57.3 occ:1.00 O C:HOH311 3.2 52.4 1.0 N C:LYS3 3.4 49.2 1.0 CG C:LYS3 3.8 37.1 1.0 CB C:LYS3 4.0 40.8 1.0 CD1 C:TYR109 4.0 33.0 1.0 CA C:VAL2 4.0 79.1 1.0 C C:VAL2 4.2 63.4 1.0 CA C:LYS3 4.3 43.5 1.0 CG1 C:VAL2 4.4 82.1 1.0 CB C:TYR109 4.6 32.3 1.0 CB C:VAL2 4.7 87.0 1.0 O C:TRP110 4.8 34.8 1.0 CG C:TYR109 4.8 31.1 1.0 N C:LEU4 4.8 38.0 1.0 CE1 C:TYR109 4.9 35.2 1.0 CA C:TYR109 5.0 30.5 1.0 N C:VAL2 5.0 80.2 1.0

Chlorine binding site 4 out of 5 in the Anti-Sudan Ebolavirus Nucleoprotein Single Domain Antibody Sudan B (Sb) Complexed with Sudan Ebolavirus Nucleoprotein C-Terminal Domain 634-738


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Anti-Sudan Ebolavirus Nucleoprotein Single Domain Antibody Sudan B (Sb) Complexed with Sudan Ebolavirus Nucleoprotein C-Terminal Domain 634-738 within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl202 b:51.2 occ:1.00 N C:TYR59 3.1 33.3 1.0 CA C:ILE58 3.5 37.5 1.0 C C:ILE58 3.8 41.8 1.0 O C:HOH313 3.8 58.5 1.0 CD1 C:TYR59 3.9 40.9 1.0 CG1 C:ILE58 3.9 37.4 1.0 CB C:TYR59 4.0 36.7 1.0 CA C:TYR59 4.0 33.4 1.0 O C:TYR59 4.0 43.4 1.0 CB C:ILE58 4.3 39.6 1.0 CG C:TYR59 4.4 39.1 1.0 O C:THR57 4.4 46.0 1.0 C C:TYR59 4.5 40.4 1.0 N C:ILE58 4.5 36.4 1.0 C C:THR57 4.8 42.8 1.0 CD C:LYS64 4.9 83.1 1.0 O C:ILE58 4.9 38.9 1.0 CE1 C:TYR59 5.0 40.5 1.0 CD1 C:ILE58 5.0 43.8 1.0

Chlorine binding site 5 out of 5 in the Anti-Sudan Ebolavirus Nucleoprotein Single Domain Antibody Sudan B (Sb) Complexed with Sudan Ebolavirus Nucleoprotein C-Terminal Domain 634-738


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 5 of Anti-Sudan Ebolavirus Nucleoprotein Single Domain Antibody Sudan B (Sb) Complexed with Sudan Ebolavirus Nucleoprotein C-Terminal Domain 634-738 within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl801 b:64.3 occ:1.00 OG D:SER645 3.1 58.2 1.0 CB D:SER645 4.1 59.0 1.0 N D:SER645 4.5 57.1 1.0 CA D:SER645 4.9 57.8 1.0

L.J.Sherwood, A.B.Taylor, P.J.Hart, A.Hayhurst. Paratope Duality and Gullying Are Among the Atypical Recognition Mechanisms Employed By A Trio of Nanobodies to Differentiate Ebolavirus Nucleoproteins. J.Mol.Biol. 2019.
ISSN: ESSN 1089-8638
PubMed: 31626803
DOI: 10.1016/J.JMB.2019.10.005