Fluorine in PDB 1d1c: Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with N- Methyl-O-Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride.

The structure of Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with N- Methyl-O-Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride., PDB code: 1d1c was solved by A.M.Gulick, C.B.Bauer, J.B.Thoden, E.Pate, R.G.Yount, I.Rayment, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 2.30
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	103.900, 180.900, 54.100, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The structure of Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with N- Methyl-O-Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride. also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Fluorine atom in the Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with N- Methyl-O-Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride. (pdb code 1d1c). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with N- Methyl-O-Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride., PDB code: 1d1c:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with N- Methyl-O-Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with N- Methyl-O-Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride. within 5.0Å range: probe atom residue distance (Å) B Occ A:F999 b:17.3 occ:1.00 F1 A:NMQ999 0.0 17.3 1.0 BE A:NMQ999 1.5 25.4 1.0 F2 A:NMQ999 2.5 18.1 1.0 F3 A:NMQ999 2.5 24.7 1.0 OB3 A:NMQ999 2.5 28.1 1.0 NZ A:LYS185 2.8 11.0 1.0 O A:HOH1357 3.2 37.1 1.0 CA A:SER181 3.4 1.1 1.0 CE A:LYS185 3.4 7.2 1.0 PB A:NMQ999 3.6 14.6 1.0 O A:HOH1464 3.6 34.6 1.0 CB A:SER181 3.7 7.7 1.0 OB1 A:NMQ999 3.8 12.6 1.0 OB2 A:NMQ999 3.9 12.4 1.0 OG A:SER181 3.9 16.9 1.0 MG A:MG998 4.0 21.8 1.0 N A:SER181 4.1 18.5 1.0 N A:GLY182 4.1 29.9 1.0 C A:SER181 4.3 17.7 1.0 O A:GLU180 4.3 6.9 1.0 O A:HOH1452 4.4 33.8 1.0 C A:GLU180 4.5 7.0 1.0 O A:SER237 4.6 17.6 1.0 OG A:SER236 4.6 23.8 1.0 N A:SER237 4.7 10.2 1.0 CB A:SER237 4.9 30.2 1.0 O A:GLY179 4.9 10.3 1.0 CD A:LYS185 4.9 20.6 1.0 O A:HOH1458 4.9 70.0 1.0 OA3 A:NMQ999 5.0 24.7 1.0 O A:HOH1005 5.0 9.7 1.0

Fluorine binding site 2 out of 3 in the Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with N- Methyl-O-Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with N- Methyl-O-Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride. within 5.0Å range: probe atom residue distance (Å) B Occ A:F999 b:18.1 occ:1.00 F2 A:NMQ999 0.0 18.1 1.0 BE A:NMQ999 1.5 25.4 1.0 MG A:MG998 2.0 21.8 1.0 F3 A:NMQ999 2.4 24.7 1.0 F1 A:NMQ999 2.5 17.3 1.0 OB3 A:NMQ999 2.6 28.1 1.0 O A:HOH1005 2.6 9.7 1.0 OB2 A:NMQ999 2.6 12.4 1.0 N A:SER237 2.8 10.2 1.0 OG A:SER237 2.9 12.1 1.0 CB A:SER237 3.0 30.2 1.0 PB A:NMQ999 3.2 14.6 1.0 CA A:SER237 3.5 9.6 1.0 O A:HOH1357 3.8 37.1 1.0 C A:SER236 3.9 17.8 1.0 O A:SER237 3.9 17.6 1.0 ND2 A:ASN233 3.9 27.6 1.0 CA A:SER236 4.0 27.2 1.0 OG1 A:THR186 4.0 78.9 1.0 O A:HOH1458 4.2 70.0 1.0 OG A:SER236 4.2 23.8 1.0 OB1 A:NMQ999 4.2 12.6 1.0 C A:SER237 4.3 16.7 1.0 OA3 A:NMQ999 4.3 24.7 1.0 NZ A:LYS185 4.4 11.0 1.0 CE A:LYS185 4.6 7.2 1.0 O A:ASN235 4.7 22.6 1.0 CB A:SER236 4.7 13.8 1.0 OA2 A:NMQ999 4.8 18.9 1.0 CB A:THR186 4.9 7.3 1.0 O A:SER236 5.0 27.2 1.0

Fluorine binding site 3 out of 3 in the Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with N- Methyl-O-Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with N- Methyl-O-Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride. within 5.0Å range: probe atom residue distance (Å) B Occ A:F999 b:24.7 occ:1.00 F3 A:NMQ999 0.0 24.7 1.0 BE A:NMQ999 1.5 25.4 1.0 F2 A:NMQ999 2.4 18.1 1.0 OB3 A:NMQ999 2.5 28.1 1.0 F1 A:NMQ999 2.5 17.3 1.0 OG A:SER236 2.7 23.8 1.0 OG A:SER181 2.8 16.9 1.0 ND2 A:ASN233 3.1 27.6 1.0 CA A:SER236 3.2 27.2 1.0 CB A:SER236 3.3 13.8 1.0 N A:SER237 3.5 10.2 1.0 CB A:SER181 3.6 7.7 1.0 N A:GLY182 3.7 29.9 1.0 CA A:SER181 3.8 1.1 1.0 C A:SER236 3.8 17.8 1.0 CB A:ASN233 3.9 8.4 1.0 PB A:NMQ999 3.9 14.6 1.0 CG A:ASN233 4.0 40.8 1.0 C A:SER181 4.2 17.7 1.0 O A:HOH1464 4.2 34.6 1.0 OB2 A:NMQ999 4.3 12.4 1.0 O A:HOH1005 4.3 9.7 1.0 O A:HOH1135 4.4 25.1 1.0 N A:SER236 4.4 20.2 1.0 O A:SER237 4.4 17.6 1.0 MG A:MG998 4.4 21.8 1.0 CA A:SER237 4.6 9.6 1.0 CA A:GLY182 4.7 1.3 1.0 OA3 A:NMQ999 4.7 24.7 1.0 CB A:SER237 4.8 30.2 1.0 OB1 A:NMQ999 4.9 12.6 1.0 O A:HOH1357 4.9 37.1 1.0 C A:SER237 4.9 16.7 1.0 NH2 A:ARG238 5.0 24.6 1.0 NZ A:LYS185 5.0 11.0 1.0 O A:ASN235 5.0 22.6 1.0

A.M.Gulick, C.B.Bauer, J.B.Thoden, E.Pate, R.G.Yount, I.Rayment. X-Ray Structures of the Dictyostelium Discoideum Myosin Motor Domain with Six Non-Nucleotide Analogs. J.Biol.Chem. V. 275 398 2000.
ISSN: ISSN 0021-9258
PubMed: 10617631
DOI: 10.1074/JBC.275.1.398