Potassium in PDB 4zn8: Using Molecular Dynamics Simulations to Predict Domain Swapping of Computationally Designed Protein Variants

The structure of Using Molecular Dynamics Simulations to Predict Domain Swapping of Computationally Designed Protein Variants, PDB code: 4zn8 was solved by P.-S.Huang, L.M.Thomas, S.L.Mayo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.00 / 3.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.456, 62.682, 76.698, 90.00, 90.00, 90.00
R / Rfree (%)	25 / 31.2

The binding sites of Potassium atom in the Using Molecular Dynamics Simulations to Predict Domain Swapping of Computationally Designed Protein Variants (pdb code 4zn8). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 4 binding sites of Potassium where determined in the Using Molecular Dynamics Simulations to Predict Domain Swapping of Computationally Designed Protein Variants, PDB code: 4zn8:
Jump to Potassium binding site number: 1; 2; 3; 4;

Potassium binding site 1 out of 4 in the Using Molecular Dynamics Simulations to Predict Domain Swapping of Computationally Designed Protein Variants


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Using Molecular Dynamics Simulations to Predict Domain Swapping of Computationally Designed Protein Variants within 5.0Å range: probe atom residue distance (Å) B Occ A:K101 b:53.9 occ:1.00 NH1 D:ARG20 3.9 16.4 1.0 O A:GLN31 4.0 45.5 1.0 NH2 D:ARG20 4.7 21.7 1.0 CZ D:ARG20 4.8 18.0 1.0 CB A:GLN31 4.8 40.6 1.0 CD1 A:TRP28 4.8 21.1 1.0 NE1 A:TRP28 4.9 19.1 1.0 OE1 A:GLN31 4.9 48.5 1.0 C A:GLN31 4.9 39.3 1.0

Potassium binding site 2 out of 4 in the Using Molecular Dynamics Simulations to Predict Domain Swapping of Computationally Designed Protein Variants


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Using Molecular Dynamics Simulations to Predict Domain Swapping of Computationally Designed Protein Variants within 5.0Å range: probe atom residue distance (Å) B Occ C:K101 b:39.9 occ:1.00 NH2 B:ARG20 3.0 15.7 1.0 CD C:GLN31 3.1 41.0 1.0 OE1 C:GLN31 3.2 31.4 1.0 NE2 C:GLN31 3.3 40.7 1.0 CB C:GLN31 3.3 39.4 1.0 CG C:GLN31 3.8 44.8 1.0 CZ B:ARG20 4.2 14.8 1.0 NH1 B:ARG20 4.5 13.9 1.0 CD1 C:TRP28 4.6 14.8 1.0 CA C:GLN31 4.7 28.8 1.0 C C:GLN31 4.8 34.9 1.0

Potassium binding site 3 out of 4 in the Using Molecular Dynamics Simulations to Predict Domain Swapping of Computationally Designed Protein Variants


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Using Molecular Dynamics Simulations to Predict Domain Swapping of Computationally Designed Protein Variants within 5.0Å range: probe atom residue distance (Å) B Occ C:K102 b:73.3 occ:1.00 NE C:ARG46 3.8 51.0 1.0 NE C:ARG45 3.8 55.4 1.0 NH2 C:ARG46 4.1 57.4 1.0 NH2 C:ARG45 4.2 50.0 1.0 CZ C:ARG46 4.4 60.9 1.0 CZ C:ARG45 4.5 52.4 1.0 CG C:ARG46 4.6 49.6 1.0 CD C:ARG45 4.8 49.0 1.0 CD C:ARG46 4.8 51.4 1.0

Potassium binding site 4 out of 4 in the Using Molecular Dynamics Simulations to Predict Domain Swapping of Computationally Designed Protein Variants


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 4 of Using Molecular Dynamics Simulations to Predict Domain Swapping of Computationally Designed Protein Variants within 5.0Å range: probe atom residue distance (Å) B Occ D:K101 b:73.3 occ:1.00 O D:ARG46 3.4 53.5 1.0 O D:LYS47 3.5 37.0 1.0 C D:LYS47 4.1 34.6 1.0 C D:ARG46 4.3 50.4 1.0 O D:ARG45 4.4 39.7 1.0 CA D:LYS47 4.6 33.9 1.0 N D:LYS47 4.8 51.4 1.0

P.-S.Huang, L.M.Thomas, S.L.Mayo. Using Molecular Dynamics Simulations to Predict Domain Swapping of Computationally Designed Protein Variants. To Be Published.