Fluorine in PDB 4ncj: Crystal Structure of Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride

The structure of Crystal Structure of Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride, PDB code: 4ncj was solved by S.Classen, G.J.Williams, A.S.Arvai, R.S.Williams, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.41 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	83.020, 108.482, 148.744, 90.00, 90.00, 90.00
R / Rfree (%)	22.3 / 25.8

The structure of Crystal Structure of Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride 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 Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride (pdb code 4ncj). 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 Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride, PDB code: 4ncj:
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 Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride


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 Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride within 5.0Å range: probe atom residue distance (Å) B Occ A:F902 b:14.4 occ:1.00 F1 A:BEF902 0.0 14.4 1.0 BE A:BEF902 1.5 12.1 1.0 MG A:MG903 2.0 19.4 1.0 HE22 A:GLN140 2.1 31.9 1.0 F2 A:BEF902 2.6 20.8 1.0 F3 A:BEF902 2.6 18.4 1.0 O3B A:ADP901 2.7 15.6 1.0 H C:GLY794 2.9 27.3 1.0 NE2 A:GLN140 2.9 26.6 1.0 OE1 A:GLN140 3.0 21.9 1.0 O A:HOH1053 3.0 23.5 1.0 H C:GLY795 3.1 29.0 1.0 O A:HOH1045 3.1 17.3 1.0 HB2 C:SER793 3.2 23.4 1.0 O A:HOH1003 3.3 28.6 1.0 CD A:GLN140 3.3 25.1 1.0 O1B A:ADP901 3.3 16.0 1.0 PB A:ADP901 3.5 16.8 1.0 N C:GLY794 3.5 22.7 1.0 HA3 C:GLY794 3.6 27.6 1.0 HE21 A:GLN140 3.6 31.9 1.0 HZ1 A:LYS36 3.8 31.0 1.0 N C:GLY795 3.9 24.2 1.0 OG A:SER37 3.9 19.8 1.0 CA C:GLY794 4.0 23.0 1.0 HD22 A:ASN32 4.1 28.4 1.0 CB C:SER793 4.2 19.5 1.0 HG C:SER793 4.3 22.0 1.0 HE2 A:LYS36 4.4 28.6 1.0 HA A:ASN32 4.4 25.6 1.0 H A:GLY33 4.4 26.4 1.0 C C:GLY794 4.5 24.0 1.0 O3A A:ADP901 4.5 17.8 1.0 C C:SER793 4.5 22.9 1.0 NZ A:LYS36 4.5 25.8 1.0 OG C:SER793 4.6 18.3 1.0 HZ3 A:LYS36 4.6 31.0 1.0 O2B A:ADP901 4.7 16.1 1.0 HA3 C:GLY795 4.7 30.0 1.0 ND2 A:ASN32 4.7 23.6 1.0 HB3 C:SER793 4.8 23.4 1.0 HB2 A:GLU823 4.8 27.5 1.0 HB3 C:TYR827 4.8 32.7 1.0 CA C:SER793 4.8 21.8 1.0 CG A:GLN140 4.8 27.1 1.0 HA C:SER793 4.9 26.2 1.0 CA C:GLY795 4.9 25.0 1.0 HA2 C:GLY794 4.9 27.6 1.0 CE A:LYS36 4.9 23.9 1.0 H A:SER37 5.0 21.4 1.0 HD21 A:ASN32 5.0 28.4 1.0

Fluorine binding site 2 out of 12 in the Crystal Structure of Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride


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 Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride within 5.0Å range: probe atom residue distance (Å) B Occ A:F902 b:20.8 occ:1.00 F2 A:BEF902 0.0 20.8 1.0 BE A:BEF902 1.6 12.1 1.0 HD22 A:ASN32 2.0 28.4 1.0 HZ1 A:LYS36 2.1 31.0 1.0 HA A:ASN32 2.5 25.6 1.0 F3 A:BEF902 2.6 18.4 1.0 F1 A:BEF902 2.6 14.4 1.0 O A:HOH1003 2.7 28.6 1.0 O3B A:ADP901 2.7 15.6 1.0 ND2 A:ASN32 2.8 23.6 1.0 NZ A:LYS36 2.9 25.8 1.0 HD21 A:ASN32 3.2 28.4 1.0 HZ2 A:LYS36 3.3 31.0 1.0 HZ3 A:LYS36 3.4 31.0 1.0 CA A:ASN32 3.4 21.3 1.0 HE3 A:LYS36 3.6 28.6 1.0 HD2 A:HIS855 3.6 29.4 1.0 HE2 A:LYS36 3.6 28.6 1.0 CE A:LYS36 3.7 23.9 1.0 HB3 A:HIS855 3.7 31.0 1.0 H A:GLY33 3.7 26.4 1.0 PB A:ADP901 3.8 16.8 1.0 CG A:ASN32 3.9 23.2 1.0 HE22 A:GLN140 4.0 31.9 1.0 N A:ASN32 4.0 21.7 1.0 O A:HOH1053 4.0 23.5 1.0 MG A:MG903 4.0 19.4 1.0 H C:GLY795 4.1 29.0 1.0 CB A:ASN32 4.1 22.2 1.0 O A:GLN31 4.1 23.0 1.0 HB3 A:ASN32 4.2 26.6 1.0 O2B A:ADP901 4.3 16.1 1.0 N A:GLY33 4.3 22.0 1.0 C A:GLN31 4.3 22.2 1.0 H A:ASN32 4.4 26.0 1.0 CD2 A:HIS855 4.4 24.5 1.0 C A:ASN32 4.4 22.6 1.0 O1B A:ADP901 4.5 16.0 1.0 HA3 C:GLY795 4.5 30.0 1.0 HB2 C:SER793 4.5 23.4 1.0 O C:TYR827 4.5 31.4 1.0 CB A:HIS855 4.6 25.9 1.0 NE2 A:GLN140 4.8 26.6 1.0 N C:GLY795 4.8 24.2 1.0 CG A:HIS855 4.9 25.9 1.0 O A:GLY30 4.9 25.0 1.0 OE2 A:GLU823 5.0 26.0 1.0 HB2 A:ASN32 5.0 26.6 1.0

Fluorine binding site 3 out of 12 in the Crystal Structure of Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride


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 Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride within 5.0Å range: probe atom residue distance (Å) B Occ A:F902 b:18.4 occ:1.00 F3 A:BEF902 0.0 18.4 1.0 BE A:BEF902 1.6 12.1 1.0 H C:GLY795 2.0 29.0 1.0 HG C:SER793 2.6 22.0 1.0 F2 A:BEF902 2.6 20.8 1.0 HD22 A:ASN32 2.6 28.4 1.0 F1 A:BEF902 2.6 14.4 1.0 HA3 C:GLY795 2.7 30.0 1.0 HA A:ASN32 2.8 25.6 1.0 O3B A:ADP901 2.8 15.6 1.0 N C:GLY795 2.8 24.2 1.0 HB2 C:SER793 2.8 23.4 1.0 OG C:SER793 2.9 18.3 1.0 HB3 A:ASN32 2.9 26.6 1.0 H A:GLY33 3.0 26.4 1.0 ND2 A:ASN32 3.1 23.6 1.0 CA C:GLY795 3.2 25.0 1.0 H C:GLU796 3.3 28.8 1.0 CB C:SER793 3.4 19.5 1.0 CB A:ASN32 3.4 22.2 1.0 CA A:ASN32 3.4 21.3 1.0 CG A:ASN32 3.5 23.2 1.0 H C:GLY794 3.5 27.3 1.0 HD21 A:ASN32 3.6 28.4 1.0 N A:GLY33 3.7 22.0 1.0 N C:GLY794 3.7 22.7 1.0 N C:GLU796 3.9 24.0 1.0 C C:GLY794 4.0 24.0 1.0 HA2 C:GLY795 4.0 30.0 1.0 HE22 A:GLN140 4.0 31.9 1.0 HB3 C:SER793 4.0 23.4 1.0 C A:ASN32 4.0 22.6 1.0 C C:GLY795 4.1 25.6 1.0 C C:SER793 4.1 22.9 1.0 HZ1 A:LYS36 4.2 31.0 1.0 PB A:ADP901 4.2 16.8 1.0 HG3 C:GLU796 4.3 25.4 1.0 CA C:GLY794 4.3 23.0 1.0 HB2 A:ASN32 4.3 26.6 1.0 HA3 C:GLY794 4.4 27.6 1.0 CA C:SER793 4.4 21.8 1.0 MG A:MG903 4.5 19.4 1.0 O C:TYR827 4.5 31.4 1.0 OD1 A:ASN32 4.5 24.1 1.0 HA2 A:GLY33 4.6 26.8 1.0 N A:ASN32 4.7 21.7 1.0 O3A A:ADP901 4.7 17.8 1.0 O A:HOH1003 4.7 28.6 1.0 HB3 C:TYR827 4.7 32.7 1.0 CA A:GLY33 4.8 22.3 1.0 NE2 A:GLN140 4.8 26.6 1.0 O C:SER793 4.8 23.8 1.0 O A:HOH1045 4.8 17.3 1.0 O1B A:ADP901 4.9 16.0 1.0 HA C:SER793 4.9 26.2 1.0

Fluorine binding site 4 out of 12 in the Crystal Structure of Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride


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 Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride within 5.0Å range: probe atom residue distance (Å) B Occ B:F902 b:19.4 occ:1.00 F1 B:BEF902 0.0 19.4 1.0 BE B:BEF902 1.5 18.2 1.0 HZ1 B:LYS36 2.0 35.3 1.0 HD22 B:ASN32 2.1 34.5 1.0 HA B:ASN32 2.4 32.7 1.0 F3 B:BEF902 2.5 18.3 1.0 F2 B:BEF902 2.6 17.8 1.0 O2B B:ADP901 2.6 18.1 1.0 O B:HOH1012 2.7 26.8 1.0 NZ B:LYS36 2.9 29.4 1.0 ND2 B:ASN32 2.9 28.8 1.0 HD21 B:ASN32 3.3 34.5 1.0 HZ3 B:LYS36 3.3 35.3 1.0 HZ2 B:LYS36 3.3 35.3 1.0 CA B:ASN32 3.4 27.3 1.0 HE2 B:LYS36 3.4 33.1 1.0 HE3 B:LYS36 3.5 33.1 1.0 CE B:LYS36 3.5 27.6 1.0 H B:GLY33 3.6 32.4 1.0 PB B:ADP901 3.7 20.8 1.0 HD2 B:HIS855 3.8 30.0 1.0 HB3 B:HIS855 3.9 33.3 1.0 O B:HOH1065 3.9 18.6 1.0 N B:ASN32 3.9 28.2 1.0 CG B:ASN32 3.9 29.9 1.0 MG B:MG903 4.0 21.0 1.0 HE22 B:GLN140 4.0 28.5 1.0 H D:GLY795 4.0 28.8 1.0 O B:GLN31 4.1 25.6 1.0 CB B:ASN32 4.1 29.1 1.0 HB3 B:ASN32 4.2 35.0 1.0 O3B B:ADP901 4.2 20.9 1.0 O1B B:ADP901 4.2 22.2 1.0 N B:GLY33 4.2 27.0 1.0 C B:GLN31 4.2 28.0 1.0 H B:ASN32 4.3 33.8 1.0 C B:ASN32 4.4 28.1 1.0 HB2 D:SER793 4.6 30.0 1.0 HA3 D:GLY795 4.6 28.5 1.0 CD2 B:HIS855 4.6 25.0 1.0 O D:TYR827 4.7 22.6 1.0 HG D:SER793 4.8 28.2 1.0 NE2 B:GLN140 4.8 23.8 1.0 CB B:HIS855 4.8 27.7 1.0 O B:GLY30 4.8 25.5 1.0 N D:GLY795 4.9 24.0 1.0 OE1 B:GLU823 4.9 27.1 1.0 CD B:LYS36 5.0 25.4 1.0 HB2 B:ASN32 5.0 35.0 1.0

Fluorine binding site 5 out of 12 in the Crystal Structure of Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride


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 Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride within 5.0Å range: probe atom residue distance (Å) B Occ B:F902 b:17.8 occ:1.00 F2 B:BEF902 0.0 17.8 1.0 BE B:BEF902 1.5 18.2 1.0 H D:GLY795 2.0 28.8 1.0 HG D:SER793 2.3 28.2 1.0 F3 B:BEF902 2.5 18.3 1.0 F1 B:BEF902 2.6 19.4 1.0 HD22 B:ASN32 2.6 34.5 1.0 N D:GLY795 2.8 24.0 1.0 HA B:ASN32 2.8 32.7 1.0 OG D:SER793 2.8 23.5 1.0 HA3 D:GLY795 2.8 28.5 1.0 O2B B:ADP901 2.8 18.1 1.0 HB3 B:ASN32 2.9 35.0 1.0 HB2 D:SER793 3.0 30.0 1.0 H B:GLY33 3.0 32.4 1.0 ND2 B:ASN32 3.1 28.8 1.0 CA D:GLY795 3.3 23.8 1.0 H D:GLU796 3.3 28.5 1.0 CB D:SER793 3.4 25.0 1.0 H D:GLY794 3.4 28.0 1.0 CB B:ASN32 3.4 29.1 1.0 CA B:ASN32 3.5 27.3 1.0 N D:GLY794 3.6 23.3 1.0 CG B:ASN32 3.6 29.9 1.0 HD21 B:ASN32 3.7 34.5 1.0 N B:GLY33 3.7 27.0 1.0 HE22 B:GLN140 3.8 28.5 1.0 C D:GLY794 3.8 23.9 1.0 N D:GLU796 4.0 23.7 1.0 HA2 D:GLY795 4.0 28.5 1.0 C D:SER793 4.0 21.8 1.0 C B:ASN32 4.1 28.1 1.0 CA D:GLY794 4.1 24.4 1.0 HB3 D:SER793 4.1 30.0 1.0 HA3 D:GLY794 4.1 29.2 1.0 PB B:ADP901 4.1 20.8 1.0 C D:GLY795 4.2 23.0 1.0 HZ1 B:LYS36 4.2 35.3 1.0 MG B:MG903 4.3 21.0 1.0 CA D:SER793 4.4 23.4 1.0 HB2 B:ASN32 4.4 35.0 1.0 O B:HOH1003 4.5 17.1 1.0 O D:TYR827 4.6 22.6 1.0 HG3 D:GLU796 4.6 28.6 1.0 O B:HOH1012 4.6 26.8 1.0 NE2 B:GLN140 4.6 23.8 1.0 HA2 B:GLY33 4.6 32.2 1.0 O3B B:ADP901 4.7 20.9 1.0 OD1 B:ASN32 4.7 31.7 1.0 O3A B:ADP901 4.7 16.0 1.0 N B:ASN32 4.7 28.2 1.0 O D:SER793 4.7 19.2 1.0 HB3 D:TYR827 4.7 29.2 1.0 CA B:GLY33 4.8 26.9 1.0 HA D:SER793 4.9 28.1 1.0 HB2 D:GLU796 4.9 28.1 1.0 O D:GLY794 5.0 23.5 1.0

Fluorine binding site 6 out of 12 in the Crystal Structure of Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride


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 Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride within 5.0Å range: probe atom residue distance (Å) B Occ B:F902 b:18.3 occ:1.00 F3 B:BEF902 0.0 18.3 1.0 BE B:BEF902 1.5 18.2 1.0 MG B:MG903 2.0 21.0 1.0 HE22 B:GLN140 2.2 28.5 1.0 F2 B:BEF902 2.5 17.8 1.0 F1 B:BEF902 2.5 19.4 1.0 O2B B:ADP901 2.8 18.1 1.0 H D:GLY794 2.9 28.0 1.0 O B:HOH1065 3.0 18.6 1.0 NE2 B:GLN140 3.0 23.8 1.0 O B:HOH1003 3.0 17.1 1.0 OE1 B:GLN140 3.0 24.8 1.0 H D:GLY795 3.1 28.8 1.0 O3B B:ADP901 3.1 20.9 1.0 O B:HOH1012 3.2 26.8 1.0 HB2 D:SER793 3.3 30.0 1.0 PB B:ADP901 3.4 20.8 1.0 CD B:GLN140 3.4 24.5 1.0 HA3 D:GLY794 3.5 29.2 1.0 N D:GLY794 3.6 23.3 1.0 HE21 B:GLN140 3.7 28.5 1.0 HZ1 B:LYS36 3.8 35.3 1.0 N D:GLY795 3.9 24.0 1.0 HD22 B:ASN32 4.0 34.5 1.0 CA D:GLY794 4.0 24.4 1.0 HG D:SER793 4.0 28.2 1.0 OG B:SER37 4.1 21.7 1.0 CB D:SER793 4.2 25.0 1.0 HE2 B:LYS36 4.2 33.1 1.0 HA B:ASN32 4.3 32.7 1.0 H B:GLY33 4.3 32.4 1.0 OG D:SER793 4.4 23.5 1.0 O3A B:ADP901 4.4 16.0 1.0 C D:GLY794 4.5 23.9 1.0 NZ B:LYS36 4.5 29.4 1.0 C D:SER793 4.5 21.8 1.0 O1B B:ADP901 4.6 22.2 1.0 HZ3 B:LYS36 4.6 35.3 1.0 ND2 B:ASN32 4.7 28.8 1.0 HA3 D:GLY795 4.7 28.5 1.0 CE B:LYS36 4.8 27.6 1.0 CA D:SER793 4.8 23.4 1.0 O2A B:ADP901 4.8 17.9 1.0 HB2 B:SER37 4.8 25.3 1.0 HA D:SER793 4.8 28.1 1.0 HB3 D:SER793 4.9 30.0 1.0 HA2 D:GLY794 4.9 29.2 1.0 HB3 D:TYR827 4.9 29.2 1.0 CG B:GLN140 4.9 24.7 1.0 HB2 B:GLU823 4.9 28.3 1.0 HD21 B:ASN32 4.9 34.5 1.0 CA D:GLY795 4.9 23.8 1.0 HE3 B:LYS36 4.9 33.1 1.0 H B:SER37 5.0 25.6 1.0

Fluorine binding site 7 out of 12 in the Crystal Structure of Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride


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 Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride within 5.0Å range: probe atom residue distance (Å) B Occ C:F902 b:20.3 occ:1.00 F1 C:BEF902 0.0 20.3 1.0 BE C:BEF902 1.5 19.1 1.0 MG C:MG903 2.0 22.5 1.0 HE22 C:GLN140 2.2 36.6 1.0 F3 C:BEF902 2.5 20.7 1.0 F2 C:BEF902 2.6 19.1 1.0 OE1 C:GLN140 2.8 28.7 1.0 H A:GLY794 2.9 32.4 1.0 O C:HOH1002 2.9 21.3 1.0 NE2 C:GLN140 2.9 30.5 1.0 O1B C:ADP901 2.9 19.8 1.0 O A:HOH1083 3.1 40.1 1.0 H A:GLY795 3.1 26.9 1.0 O C:HOH1001 3.1 20.1 1.0 O2B C:ADP901 3.2 22.6 1.0 CD C:GLN140 3.2 29.2 1.0 HB2 A:SER793 3.3 31.0 1.0 O C:HOH1023 3.3 28.0 1.0 HZ2 C:LYS36 3.4 37.2 1.0 PB C:ADP901 3.5 22.6 1.0 N A:GLY794 3.6 27.0 1.0 HA3 A:GLY794 3.6 30.2 1.0 HE21 C:GLN140 3.7 36.6 1.0 HZ1 C:LYS36 3.7 37.2 1.0 N A:GLY795 3.9 22.4 1.0 NZ C:LYS36 4.0 31.0 1.0 HG A:SER793 4.0 30.6 1.0 OG C:SER37 4.0 23.4 1.0 CA A:GLY794 4.0 25.2 1.0 HD22 C:ASN32 4.0 33.9 1.0 CB A:SER793 4.2 25.8 1.0 HZ3 C:LYS36 4.3 37.2 1.0 HA C:ASN32 4.3 34.3 1.0 OG A:SER793 4.4 25.5 1.0 H C:GLY33 4.4 34.3 1.0 O3A C:ADP901 4.5 20.6 1.0 C A:GLY794 4.5 23.0 1.0 C A:SER793 4.5 26.4 1.0 ND2 C:ASN32 4.7 28.3 1.0 HB3 A:TYR827 4.7 29.9 1.0 O3B C:ADP901 4.7 24.7 1.0 HA3 A:GLY795 4.7 28.5 1.0 CG C:GLN140 4.8 28.2 1.0 HB2 C:GLU823 4.8 29.6 1.0 CA A:SER793 4.8 26.4 1.0 HA A:SER793 4.8 31.7 1.0 HB3 A:SER793 4.9 31.0 1.0 HA2 A:GLY794 4.9 30.2 1.0 O2A C:ADP901 4.9 20.6 1.0 CA A:GLY795 4.9 23.7 1.0 HD21 C:ASN32 4.9 33.9 1.0 H C:SER37 5.0 28.1 1.0

Fluorine binding site 8 out of 12 in the Crystal Structure of Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride


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 Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride within 5.0Å range: probe atom residue distance (Å) B Occ C:F902 b:19.1 occ:1.00 F2 C:BEF902 0.0 19.1 1.0 BE C:BEF902 1.6 19.1 1.0 HZ1 C:LYS36 1.7 37.2 1.0 HD22 C:ASN32 2.0 33.9 1.0 NZ C:LYS36 2.2 31.0 1.0 HZ2 C:LYS36 2.3 37.2 1.0 HZ3 C:LYS36 2.3 37.2 1.0 HA C:ASN32 2.4 34.3 1.0 F3 C:BEF902 2.6 20.7 1.0 F1 C:BEF902 2.6 20.3 1.0 O C:HOH1023 2.6 28.0 1.0 O1B C:ADP901 2.7 19.8 1.0 ND2 C:ASN32 2.8 28.3 1.0 O A:HOH1083 3.1 40.1 1.0 HD21 C:ASN32 3.2 33.9 1.0 CA C:ASN32 3.3 28.6 1.0 CE C:LYS36 3.6 32.0 1.0 H C:GLY33 3.6 34.3 1.0 HB3 C:HIS855 3.6 36.2 1.0 PB C:ADP901 3.7 22.6 1.0 HD2 C:HIS855 3.8 34.3 1.0 HE3 C:LYS36 3.8 38.4 1.0 CG C:ASN32 3.9 28.7 1.0 N C:ASN32 3.9 28.8 1.0 HE2 C:LYS36 3.9 38.4 1.0 O C:HOH1002 3.9 21.3 1.0 CB C:ASN32 4.0 28.9 1.0 MG C:MG903 4.0 22.5 1.0 HE22 C:GLN140 4.0 36.6 1.0 HB3 C:ASN32 4.1 34.7 1.0 O C:GLN31 4.1 25.8 1.0 O2B C:ADP901 4.2 22.6 1.0 H A:GLY795 4.2 26.9 1.0 C C:GLN31 4.2 28.2 1.0 N C:GLY33 4.2 28.6 1.0 H C:ASN32 4.3 34.6 1.0 O3B C:ADP901 4.3 24.7 1.0 C C:ASN32 4.3 29.3 1.0 CD2 C:HIS855 4.5 28.6 1.0 CB C:HIS855 4.6 30.2 1.0 HB2 A:SER793 4.6 31.0 1.0 HD2 C:LYS36 4.6 37.1 1.0 HA3 A:GLY795 4.7 28.5 1.0 O A:TYR827 4.7 25.8 1.0 O C:GLY30 4.7 31.4 1.0 CD C:LYS36 4.7 30.9 1.0 HG A:SER793 4.8 30.6 1.0 NE2 C:GLN140 4.8 30.5 1.0 HB2 C:LYS36 4.8 32.0 1.0 HB2 C:ASN32 4.9 34.7 1.0 OE2 C:GLU823 4.9 25.6 1.0 CG C:HIS855 4.9 30.5 1.0

Fluorine binding site 9 out of 12 in the Crystal Structure of Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride


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 Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride within 5.0Å range: probe atom residue distance (Å) B Occ C:F902 b:20.7 occ:1.00 F3 C:BEF902 0.0 20.7 1.0 BE C:BEF902 1.6 19.1 1.0 H A:GLY795 2.2 26.9 1.0 HG A:SER793 2.3 30.6 1.0 F1 C:BEF902 2.5 20.3 1.0 F2 C:BEF902 2.6 19.1 1.0 HA C:ASN32 2.7 34.3 1.0 O1B C:ADP901 2.7 19.8 1.0 HB3 C:ASN32 2.7 34.7 1.0 HD22 C:ASN32 2.7 33.9 1.0 OG A:SER793 2.7 25.5 1.0 HB2 A:SER793 2.9 31.0 1.0 HA3 A:GLY795 3.0 28.5 1.0 N A:GLY795 3.0 22.4 1.0 H C:GLY33 3.0 34.3 1.0 ND2 C:ASN32 3.2 28.3 1.0 CB C:ASN32 3.2 28.9 1.0 CA C:ASN32 3.3 28.6 1.0 CB A:SER793 3.3 25.8 1.0 CA A:GLY795 3.4 23.7 1.0 CG C:ASN32 3.5 28.7 1.0 H A:GLY794 3.5 32.4 1.0 H A:GLU796 3.5 29.3 1.0 N C:GLY33 3.6 28.6 1.0 O A:HOH1083 3.6 40.1 1.0 N A:GLY794 3.7 27.0 1.0 HD21 C:ASN32 3.7 33.9 1.0 HZ1 C:LYS36 3.9 37.2 1.0 HE22 C:GLN140 3.9 36.6 1.0 C C:ASN32 3.9 29.3 1.0 HB3 A:SER793 4.0 31.0 1.0 PB C:ADP901 4.0 22.6 1.0 C A:GLY794 4.1 23.0 1.0 C A:SER793 4.1 26.4 1.0 N A:GLU796 4.1 24.4 1.0 HB2 C:ASN32 4.1 34.7 1.0 HA2 A:GLY795 4.2 28.5 1.0 HG3 A:GLU796 4.3 28.4 1.0 CA A:GLY794 4.3 25.2 1.0 C A:GLY795 4.3 24.4 1.0 MG C:MG903 4.3 22.5 1.0 CA A:SER793 4.4 26.4 1.0 HA3 A:GLY794 4.4 30.2 1.0 HZ2 C:LYS36 4.4 37.2 1.0 OD1 C:ASN32 4.5 29.1 1.0 NZ C:LYS36 4.5 31.0 1.0 HA2 C:GLY33 4.6 34.2 1.0 N C:ASN32 4.6 28.8 1.0 O2B C:ADP901 4.6 22.6 1.0 O3A C:ADP901 4.6 20.6 1.0 O C:HOH1001 4.7 20.1 1.0 O A:TYR827 4.7 25.8 1.0 O C:HOH1023 4.7 28.0 1.0 CA C:GLY33 4.7 28.5 1.0 NE2 C:GLN140 4.7 30.5 1.0 HB3 A:TYR827 4.8 29.9 1.0 O A:SER793 4.8 25.0 1.0 HZ3 C:LYS36 4.9 37.2 1.0 HA A:SER793 4.9 31.7 1.0 H C:ASN32 4.9 34.6 1.0

Fluorine binding site 10 out of 12 in the Crystal Structure of Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride


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 Pyrococcus Furiosis RAD50 R805E Mutation with Adp Beryllium Flouride within 5.0Å range: probe atom residue distance (Å) B Occ D:F902 b:16.5 occ:1.00 F1 D:BEF902 0.0 16.5 1.0 BE D:BEF902 1.5 14.8 1.0 MG D:MG903 1.9 21.4 1.0 HE22 D:GLN140 2.1 29.7 1.0 F3 D:BEF902 2.6 26.6 1.0 F2 D:BEF902 2.6 21.6 1.0 H B:GLY794 2.7 33.0 1.0 O3B D:ADP901 2.8 18.6 1.0 O D:HOH1004 2.9 24.4 1.0 NE2 D:GLN140 2.9 24.7 1.0 O D:HOH1005 2.9 18.6 1.0 OE1 D:GLN140 3.0 25.5 1.0 O D:HOH1086 3.0 38.1 1.0 O1B D:ADP901 3.1 20.8 1.0 H B:GLY795 3.1 28.1 1.0 HB2 B:SER793 3.3 28.8 1.0 HA3 B:GLY794 3.3 33.1 1.0 CD D:GLN140 3.3 25.5 1.0 N B:GLY794 3.4 27.5 1.0 PB D:ADP901 3.4 21.1 1.0 O D:HOH1024 3.4 30.2 1.0 HE21 D:GLN140 3.6 29.7 1.0 CA B:GLY794 3.8 27.6 1.0 HZ1 D:LYS36 3.8 36.0 1.0 N B:GLY795 3.9 23.4 1.0 HG B:SER793 3.9 30.2 1.0 OG D:SER37 4.0 21.5 1.0 HD22 D:ASN32 4.1 31.3 1.0 CB B:SER793 4.1 24.0 1.0 OG B:SER793 4.3 25.2 1.0 H D:GLY33 4.3 31.7 1.0 HA D:ASN32 4.4 34.2 1.0 C B:GLY794 4.4 24.7 1.0 O3A D:ADP901 4.4 20.6 1.0 C B:SER793 4.4 24.4 1.0 HE2 D:LYS36 4.5 34.5 1.0 HZ3 D:LYS36 4.5 36.0 1.0 NZ D:LYS36 4.5 30.0 1.0 O2B D:ADP901 4.6 22.5 1.0 HA2 B:GLY794 4.6 33.1 1.0 CA B:SER793 4.8 23.7 1.0 HA B:SER793 4.8 28.5 1.0 ND2 D:ASN32 4.8 26.1 1.0 O2A D:ADP901 4.8 23.0 1.0 HB2 D:SER37 4.8 27.0 1.0 HB3 B:SER793 4.8 28.8 1.0 HB3 B:TYR827 4.9 27.4 1.0 HA3 B:GLY795 4.9 28.7 1.0 CG D:GLN140 4.9 26.4 1.0 H D:SER37 4.9 29.5 1.0 HB2 D:GLU823 5.0 27.1 1.0

R.A.Deshpande, G.J.Williams, O.Limbo, R.S.Williams, J.Kuhnlein, J.H.Lee, S.Classen, G.Guenther, P.Russell, J.A.Tainer, T.T.Paull. Atp-Driven RAD50 Conformations Regulate Dna Tethering, End Resection, and Atm Checkpoint Signaling. Embo J. V. 33 482 2014.
ISSN: ISSN 0261-4189
PubMed: 24493214
DOI: 10.1002/EMBJ.201386100