Fluorine in PDB 5hev: Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium

The structure of Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium, PDB code: 5hev was solved by M.Davlieva, Y.Shamoo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.02 / 3.19
Space group	P 31
Cell size a, b, c (Å), α, β, γ (°)	68.032, 68.032, 276.949, 90.00, 90.00, 120.00
R / Rfree (%)	21.9 / 27

The structure of Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium also contains other interesting chemical elements:

Magnesium

(Mg)

4 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Fluorine atom in the Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium (pdb code 5hev). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 12 binding sites of Fluorine where determined in the Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium, PDB code: 5hev:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Fluorine binding site 1 out of 12 in the Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium within 5.0Å range: probe atom residue distance (Å) B Occ A:F302 b:40.1 occ:1.00 F1 A:BEF302 0.0 40.1 1.0 BE A:BEF302 1.5 32.6 1.0 MG A:MG301 1.9 29.2 1.0 OD2 A:ASP54 2.3 40.5 1.0 F3 A:BEF302 2.5 34.3 1.0 F2 A:BEF302 2.6 27.9 1.0 OD1 A:ASP54 3.0 34.4 1.0 O A:VAL56 3.0 28.5 1.0 CG A:ASP54 3.0 31.7 1.0 NZ A:LYS104 3.6 38.2 1.0 OD1 A:ASP9 3.8 47.9 1.0 C A:VAL56 4.0 30.0 1.0 CB A:VAL56 4.0 26.7 1.0 N A:VAL56 4.2 25.4 1.0 OD1 A:ASP8 4.2 36.8 1.0 CA A:VAL56 4.3 35.6 1.0 CE2 A:PHE84 4.5 30.1 1.0 CB A:ASP54 4.5 30.0 1.0 OG1 A:THR82 4.6 46.9 1.0 CG1 A:VAL56 4.6 13.0 1.0 CG A:ASP9 4.7 39.6 1.0 CD2 A:HIS10 4.8 50.8 1.0 OD2 A:ASP9 4.8 49.9 1.0 CE A:LYS104 4.8 33.2 1.0 NE2 A:HIS10 4.9 46.3 1.0 OG A:SER83 4.9 38.1 1.0 CG A:ASP8 5.0 28.9 1.0

Fluorine binding site 2 out of 12 in the Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium within 5.0Å range: probe atom residue distance (Å) B Occ A:F302 b:27.9 occ:1.00 F2 A:BEF302 0.0 27.9 1.0 BE A:BEF302 1.6 32.6 1.0 NZ A:LYS104 2.4 38.2 1.0 F3 A:BEF302 2.5 34.3 1.0 F1 A:BEF302 2.6 40.1 1.0 OG A:SER83 2.6 38.1 1.0 CE A:LYS104 3.2 33.2 1.0 N A:SER83 3.3 28.4 1.0 CD A:LYS104 3.6 37.0 1.0 CB A:SER83 3.6 34.0 1.0 OG1 A:THR82 3.6 46.9 1.0 OD1 A:ASP54 3.7 34.4 1.0 CA A:SER83 4.0 35.2 1.0 CE2 A:PHE84 4.0 30.1 1.0 CA A:THR82 4.1 40.2 1.0 OD2 A:ASP54 4.1 40.5 1.0 C A:THR82 4.1 31.1 1.0 CG A:ASP54 4.2 31.7 1.0 CD2 A:PHE84 4.3 44.1 1.0 MG A:MG301 4.4 29.2 1.0 CB A:THR82 4.4 40.2 1.0 CG A:LYS104 4.8 32.9 1.0 C A:SER83 4.9 38.7 1.0

Fluorine binding site 3 out of 12 in the Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium within 5.0Å range: probe atom residue distance (Å) B Occ A:F302 b:34.3 occ:1.00 F3 A:BEF302 0.0 34.3 1.0 BE A:BEF302 1.5 32.6 1.0 OD1 A:ASP54 2.1 34.4 1.0 OG1 A:THR82 2.2 46.9 1.0 F2 A:BEF302 2.5 27.9 1.0 F1 A:BEF302 2.5 40.1 1.0 CG A:ASP54 3.1 31.7 1.0 N A:VAL56 3.3 25.4 1.0 CB A:THR82 3.4 40.2 1.0 OD2 A:ASP54 3.5 40.5 1.0 CD2 A:PHE84 3.5 44.1 1.0 CE2 A:PHE84 3.6 30.1 1.0 N A:LEU55 3.7 28.9 1.0 CB A:VAL56 3.9 26.7 1.0 CA A:THR82 3.9 40.2 1.0 N A:SER83 4.0 28.4 1.0 MG A:MG301 4.0 29.2 1.0 CA A:VAL56 4.1 35.6 1.0 O A:VAL56 4.2 28.5 1.0 NZ A:LYS104 4.2 38.2 1.0 CB A:LEU55 4.2 37.0 1.0 CA A:LEU55 4.2 27.0 1.0 C A:LEU55 4.2 24.7 1.0 CG2 A:VAL56 4.3 31.1 1.0 OG A:SER83 4.3 38.1 1.0 CB A:ASP54 4.5 30.0 1.0 C A:THR82 4.5 31.1 1.0 CG2 A:THR82 4.6 30.1 1.0 C A:VAL56 4.6 30.0 1.0 C A:ASP54 4.6 34.5 1.0 CA A:ASP54 4.7 31.6 1.0 CE A:LYS104 4.7 33.2 1.0 CG A:PHE84 4.8 37.2 1.0 CZ A:PHE84 4.9 43.2 1.0 O A:VAL81 5.0 35.5 1.0

Fluorine binding site 4 out of 12 in the Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium within 5.0Å range: probe atom residue distance (Å) B Occ F:F302 b:46.5 occ:1.00 F1 F:BEF302 0.0 46.5 1.0 BE F:BEF302 1.5 53.3 1.0 OD1 F:ASP54 2.2 56.4 1.0 F3 F:BEF302 2.5 36.1 1.0 F2 F:BEF302 2.6 51.1 1.0 N F:VAL56 2.6 35.0 1.0 CG F:ASP54 3.0 48.6 1.0 CB F:VAL56 3.1 28.9 1.0 OD2 F:ASP54 3.1 44.4 1.0 CG2 F:THR82 3.3 33.2 1.0 CA F:VAL56 3.3 35.5 1.0 CG2 F:VAL56 3.5 41.1 1.0 O F:VAL56 3.5 48.7 1.0 N F:LEU55 3.5 34.2 1.0 CE2 F:PHE84 3.6 42.9 1.0 C F:LEU55 3.6 36.5 1.0 MG F:MG301 3.7 40.2 1.0 C F:VAL56 3.8 40.3 1.0 CA F:LEU55 3.9 34.3 1.0 CD2 F:PHE84 3.9 40.0 1.0 CB F:LEU55 4.1 42.7 1.0 CB F:ASP54 4.3 40.3 1.0 CG1 F:VAL56 4.4 47.3 1.0 C F:ASP54 4.5 32.7 1.0 CB F:THR82 4.6 37.9 1.0 CA F:ASP54 4.7 40.8 1.0 O F:LEU55 4.8 46.1 1.0 CZ F:PHE84 4.9 48.0 1.0 OG1 F:THR82 4.9 61.5 1.0 OG F:SER83 4.9 29.5 1.0 CA F:THR82 4.9 36.5 1.0 NZ F:LYS104 5.0 54.7 1.0

Fluorine binding site 5 out of 12 in the Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium within 5.0Å range: probe atom residue distance (Å) B Occ F:F302 b:51.1 occ:1.00 F2 F:BEF302 0.0 51.1 1.0 BE F:BEF302 1.6 53.3 1.0 F3 F:BEF302 2.5 36.1 1.0 NZ F:LYS104 2.5 54.7 1.0 F1 F:BEF302 2.6 46.5 1.0 OD1 F:ASP54 2.9 56.4 1.0 CE F:LYS104 3.1 40.9 1.0 OD2 F:ASP54 3.3 44.4 1.0 CG F:ASP54 3.4 48.6 1.0 OG F:SER83 3.4 29.5 1.0 CG2 F:THR82 3.9 33.2 1.0 MG F:MG301 4.0 40.2 1.0 N F:SER83 4.0 43.6 1.0 CD F:LYS104 4.1 36.7 1.0 CE2 F:PHE84 4.2 42.9 1.0 CA F:THR82 4.4 36.5 1.0 CB F:SER83 4.6 34.9 1.0 OD1 F:ASP8 4.6 46.5 1.0 CD2 F:PHE84 4.7 40.0 1.0 C F:THR82 4.7 40.5 1.0 OD2 F:ASP8 4.7 51.1 1.0 CB F:ASP54 4.7 40.3 1.0 CB F:THR82 4.8 37.9 1.0 O F:VAL56 4.9 48.7 1.0 CA F:SER83 5.0 36.1 1.0 CD2 F:HIS10 5.0 48.8 1.0 O F:VAL81 5.0 33.2 1.0

Fluorine binding site 6 out of 12 in the Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium within 5.0Å range: probe atom residue distance (Å) B Occ F:F302 b:36.1 occ:1.00 F3 F:BEF302 0.0 36.1 1.0 BE F:BEF302 1.5 53.3 1.0 MG F:MG301 1.9 40.2 1.0 OD2 F:ASP54 2.3 44.4 1.0 F2 F:BEF302 2.5 51.1 1.0 F1 F:BEF302 2.5 46.5 1.0 O F:VAL56 2.8 48.7 1.0 CG F:ASP54 3.2 48.6 1.0 OD1 F:ASP54 3.3 56.4 1.0 OD1 F:ASP9 3.5 48.1 1.0 CB F:VAL56 3.7 28.9 1.0 C F:VAL56 3.8 40.3 1.0 CA F:VAL56 4.1 35.5 1.0 OD1 F:ASP8 4.1 46.5 1.0 N F:VAL56 4.1 35.0 1.0 NE2 F:HIS10 4.2 51.5 1.0 NZ F:LYS104 4.2 54.7 1.0 CD2 F:HIS10 4.3 48.8 1.0 CG1 F:VAL56 4.4 47.3 1.0 CG F:ASP9 4.4 39.6 1.0 OD2 F:ASP9 4.5 34.9 1.0 CB F:ASP54 4.6 40.3 1.0 CE2 F:PHE84 4.7 42.9 1.0 CG2 F:VAL56 4.8 41.1 1.0 CE1 F:HIS10 4.9 50.4 1.0 N F:MET57 5.0 45.5 1.0

Fluorine binding site 7 out of 12 in the Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 7 of Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium within 5.0Å range: probe atom residue distance (Å) B Occ B:F302 b:51.1 occ:1.00 F1 B:BEF302 0.0 51.1 1.0 BE B:BEF302 1.5 45.0 1.0 MG B:MG301 1.9 40.6 1.0 OD2 B:ASP54 2.3 49.5 1.0 F3 B:BEF302 2.5 41.4 1.0 F2 B:BEF302 2.6 31.4 1.0 OD1 B:ASP54 2.9 43.8 1.0 CG B:ASP54 2.9 46.1 1.0 CG2 B:VAL56 3.1 44.9 1.0 OD1 B:ASP9 3.6 47.9 1.0 O B:VAL56 3.6 44.8 1.0 NZ B:LYS104 3.8 40.8 1.0 OD1 B:ASP8 4.3 47.6 1.0 OG B:SER83 4.3 50.2 1.0 N B:VAL56 4.4 35.6 1.0 CB B:ASP54 4.4 38.6 1.0 CB B:VAL56 4.4 34.4 1.0 OD2 B:ASP9 4.4 53.5 1.0 CG B:ASP9 4.4 53.1 1.0 C B:VAL56 4.5 35.3 1.0 NE2 B:HIS10 4.6 41.2 1.0 OG1 B:THR82 4.7 36.5 1.0 CA B:VAL56 4.7 42.5 1.0 CD2 B:HIS10 4.7 42.3 1.0 CE B:LYS104 4.7 38.0 1.0 CE2 B:PHE84 4.9 35.2 1.0 N B:LEU55 5.0 37.6 1.0

Fluorine binding site 8 out of 12 in the Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 8 of Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium within 5.0Å range: probe atom residue distance (Å) B Occ B:F302 b:31.4 occ:1.00 F2 B:BEF302 0.0 31.4 1.0 BE B:BEF302 1.6 45.0 1.0 OD1 B:ASP54 2.1 43.8 1.0 OG1 B:THR82 2.4 36.5 1.0 F3 B:BEF302 2.5 41.4 1.0 F1 B:BEF302 2.6 51.1 1.0 CG B:ASP54 3.1 46.1 1.0 CG2 B:VAL56 3.1 44.9 1.0 N B:VAL56 3.3 35.6 1.0 OD2 B:ASP54 3.4 49.5 1.0 N B:LEU55 3.4 37.6 1.0 CB B:THR82 3.6 35.9 1.0 MG B:MG301 3.8 40.6 1.0 CD2 B:PHE84 3.8 48.0 1.0 CB B:LEU55 3.9 41.5 1.0 CA B:LEU55 4.0 31.2 1.0 CE2 B:PHE84 4.0 35.2 1.0 NZ B:LYS104 4.0 40.8 1.0 C B:LEU55 4.1 33.9 1.0 CB B:VAL56 4.1 34.4 1.0 N B:SER83 4.1 29.8 1.0 CA B:THR82 4.2 37.6 1.0 OG B:SER83 4.2 50.2 1.0 CA B:VAL56 4.2 42.5 1.0 CB B:ASP54 4.4 38.6 1.0 O B:VAL56 4.4 44.8 1.0 C B:ASP54 4.5 37.9 1.0 CG1 B:VAL56 4.6 41.9 1.0 CA B:ASP54 4.7 36.9 1.0 C B:THR82 4.7 34.5 1.0 CG B:PHE84 4.7 42.6 1.0 CG B:LEU55 4.7 42.2 1.0 CG2 B:THR82 4.8 41.0 1.0 C B:VAL56 4.8 35.3 1.0 CZ B:PHE84 4.9 27.9 1.0

Fluorine binding site 9 out of 12 in the Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 9 of Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium within 5.0Å range: probe atom residue distance (Å) B Occ B:F302 b:41.4 occ:1.00 F3 B:BEF302 0.0 41.4 1.0 BE B:BEF302 1.5 45.0 1.0 NZ B:LYS104 2.0 40.8 1.0 F2 B:BEF302 2.5 31.4 1.0 F1 B:BEF302 2.5 51.1 1.0 OG B:SER83 2.8 50.2 1.0 OD1 B:ASP54 2.9 43.8 1.0 N B:SER83 3.0 29.8 1.0 OG1 B:THR82 3.1 36.5 1.0 CE B:LYS104 3.1 38.0 1.0 CA B:THR82 3.4 37.6 1.0 CG B:ASP54 3.5 46.1 1.0 C B:THR82 3.6 34.5 1.0 CB B:SER83 3.7 44.7 1.0 CD B:LYS104 3.7 28.4 1.0 OD2 B:ASP54 3.7 49.5 1.0 CB B:THR82 3.9 35.9 1.0 CA B:SER83 3.9 43.1 1.0 CG B:LYS104 4.3 24.8 1.0 MG B:MG301 4.3 40.6 1.0 N B:THR82 4.6 37.1 1.0 O B:THR82 4.7 46.7 1.0 CB B:ASP54 4.7 38.6 1.0 CG2 B:VAL56 4.8 44.9 1.0 O B:VAL81 4.8 47.9 1.0 C B:SER83 4.9 45.6 1.0

Fluorine binding site 10 out of 12 in the Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 10 of Crystal Structure of the Beryllofluoride-Activated Liar From Enterococcus Faecium within 5.0Å range: probe atom residue distance (Å) B Occ C:F302 b:59.1 occ:1.00 F1 C:BEF302 0.0 59.1 1.0 BE C:BEF302 1.5 49.3 1.0 F3 C:BEF302 2.5 52.3 1.0 F2 C:BEF302 2.6 34.6 1.0 NZ C:LYS104 3.3 54.9 1.0 OG C:SER83 3.4 32.5 1.0 CE C:LYS104 3.7 39.3 1.0 OD2 C:ASP54 3.8 51.4 1.0 OD1 C:ASP54 3.9 51.6 1.0 MG C:MG301 3.9 36.7 1.0 CE2 C:PHE84 4.1 52.6 1.0 OG1 C:THR82 4.2 51.4 1.0 CG C:ASP54 4.2 48.7 1.0 N C:SER83 4.2 39.0 1.0 CB C:SER83 4.3 31.6 1.0 CD C:LYS104 4.4 45.8 1.0 CD2 C:HIS10 4.6 37.3 1.0 CD2 C:PHE84 4.6 56.4 1.0 NE2 C:HIS10 4.7 43.2 1.0 CA C:SER83 4.9 36.1 1.0 CZ C:PHE84 5.0 62.0 1.0 CA C:THR82 5.0 48.9 1.0

M.Davlieva, A.Tovar-Yanez, K.Debruler, P.G.Leonard, M.R.Zianni, C.A.Arias, Y.Shamoo. An Adaptive Mutation in Enterococcus Faecium Liar Associated with Antimicrobial Peptide Resistance Mimics Phosphorylation and Stabilizes Liar in An Activated State. J.Mol.Biol. V. 428 4503 2016.
ISSN: ISSN 0022-2836
PubMed: 27670715
DOI: 10.1016/J.JMB.2016.09.016