Potassium in PDB 8ft8: The Von Willebrand Factor A Domain of Human Capillary Morphogenesis Gene II, Flexibly Fused to the 1TEL Crystallization Chaperone, Thr- Val Linker Variant, Sumo Tag-Free Preparation

The structure of The Von Willebrand Factor A Domain of Human Capillary Morphogenesis Gene II, Flexibly Fused to the 1TEL Crystallization Chaperone, Thr- Val Linker Variant, Sumo Tag-Free Preparation, PDB code: 8ft8 was solved by P.L.Gajjar, C.M.Litchfield, M.Callahan, N.Redd, T.Doukov, J.D.Moody, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.87 / 1.60
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	100.882, 100.882, 49.754, 90, 90, 120
R / Rfree (%)	18.2 / 20.4

The structure of The Von Willebrand Factor A Domain of Human Capillary Morphogenesis Gene II, Flexibly Fused to the 1TEL Crystallization Chaperone, Thr- Val Linker Variant, Sumo Tag-Free Preparation also contains other interesting chemical elements:

Chlorine

(Cl)

3 atoms

The binding sites of Potassium atom in the The Von Willebrand Factor A Domain of Human Capillary Morphogenesis Gene II, Flexibly Fused to the 1TEL Crystallization Chaperone, Thr- Val Linker Variant, Sumo Tag-Free Preparation (pdb code 8ft8). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the The Von Willebrand Factor A Domain of Human Capillary Morphogenesis Gene II, Flexibly Fused to the 1TEL Crystallization Chaperone, Thr- Val Linker Variant, Sumo Tag-Free Preparation, PDB code: 8ft8:

Potassium binding site 1 out of 1 in the The Von Willebrand Factor A Domain of Human Capillary Morphogenesis Gene II, Flexibly Fused to the 1TEL Crystallization Chaperone, Thr- Val Linker Variant, Sumo Tag-Free Preparation


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of The Von Willebrand Factor A Domain of Human Capillary Morphogenesis Gene II, Flexibly Fused to the 1TEL Crystallization Chaperone, Thr- Val Linker Variant, Sumo Tag-Free Preparation within 5.0Å range: probe atom residue distance (Å) B Occ A:K305 b:86.7 occ:1.00 O A:HOH429 3.5 51.3 1.0 HG22 A:ILE152 3.8 55.4 1.0 HG12 A:VAL124 4.3 69.1 1.0 HA A:GLU121 4.3 49.9 1.0 HG21 A:ILE152 4.3 55.4 1.0 HD12 A:LEU156 4.3 57.5 1.0 HB A:ILE152 4.4 58.0 1.0 CG2 A:ILE152 4.5 46.1 1.0 HG2 A:GLU121 4.5 74.6 1.0 HB1 A:ALA120 4.5 51.5 1.0 O A:ARG149 4.5 60.0 1.0 HD11 A:LEU156 4.6 57.5 1.0 O A:ALA120 4.6 45.9 1.0 HG11 A:VAL124 4.6 69.1 1.0 HA A:ARG149 4.7 72.3 1.0 HA A:SER153 4.8 70.7 1.0 HG3 A:GLU121 4.8 74.6 1.0 CB A:ARG149 4.9 61.6 1.0 CD1 A:LEU156 4.9 47.9 1.0 CG1 A:VAL124 4.9 57.5 1.0 CB A:ILE152 5.0 48.3 1.0

P.L.Gajjar, M.J.Pedroza Romo, C.M.Litchfield, M.Callahan, N.Redd, S.Nawarathange, E.Wilson, J.Averett, S.Soleimani, C.Stewart, A.Lewis, T.Smith, S.Brown, Y.J.Tseng, T.Doukov, A.Lebedev, M.D.Moody. Decreasing the Flexibility of the Telsam-Target Protein Linker and Omitting the Cleavable Fusion Tag Improves Crystal Order and Diffraction Limits To Be Published.