Atomistry » Fluorine » PDB 4ncj-4o16 » 4ncj
Atomistry »
  Fluorine »
    PDB 4ncj-4o16 »
      4ncj »

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

Protein crystallography data

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

Other elements in 4ncj:

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

Fluorine Binding Sites:

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 4ncj

Go back to Fluorine Binding Sites List in 4ncj
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 4ncj

Go back to Fluorine Binding Sites List in 4ncj
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 4ncj

Go back to Fluorine Binding Sites List in 4ncj
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 4ncj

Go back to Fluorine Binding Sites List in 4ncj
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 4ncj

Go back to Fluorine Binding Sites List in 4ncj
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 4ncj

Go back to Fluorine Binding Sites List in 4ncj
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 4ncj

Go back to Fluorine Binding Sites List in 4ncj
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 4ncj

Go back to Fluorine Binding Sites List in 4ncj
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 4ncj

Go back to Fluorine Binding Sites List in 4ncj
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 4ncj

Go back to Fluorine Binding Sites List in 4ncj
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

Reference:

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
Page generated: Thu Aug 1 04:15:38 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy