Iodine in PDB 5w0j: Antiparallel Coiled Coil Hexamer Formed By De Novo Peptides (Acc- HEX2).

The structure of Antiparallel Coiled Coil Hexamer Formed By De Novo Peptides (Acc- HEX2)., PDB code: 5w0j was solved by R.K.Spencer, A.I.Hochbaum, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.89 / 2.20
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	52.560, 52.560, 93.040, 90.00, 90.00, 120.00
R / Rfree (%)	22 / 27.7

The structure of Antiparallel Coiled Coil Hexamer Formed By De Novo Peptides (Acc- HEX2). also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Iodine atom in the Antiparallel Coiled Coil Hexamer Formed By De Novo Peptides (Acc- HEX2). (pdb code 5w0j). This binding sites where shown within 5.0 Angstroms radius around Iodine atom.
In total 2 binding sites of Iodine where determined in the Antiparallel Coiled Coil Hexamer Formed By De Novo Peptides (Acc- HEX2)., PDB code: 5w0j:
Jump to Iodine binding site number: 1; 2;

Iodine binding site 1 out of 2 in the Antiparallel Coiled Coil Hexamer Formed By De Novo Peptides (Acc- HEX2).


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 1 of Antiparallel Coiled Coil Hexamer Formed By De Novo Peptides (Acc- HEX2). within 5.0Å range: probe atom residue distance (Å) B Occ A:I23 b:0.5 occ:1.00 I A:PHI23 0.0 0.5 1.0 CZ A:PHI23 2.0 85.2 1.0 CE2 A:PHI23 3.0 75.9 1.0 CE1 A:PHI23 3.0 74.6 1.0 HE2 A:PHI23 3.1 91.2 1.0 HE1 A:PHI23 3.1 89.5 1.0 CD2 A:PHI23 4.3 66.0 1.0 CD1 A:PHI23 4.3 64.5 1.0 CG A:PHI23 4.8 56.1 1.0

Iodine binding site 2 out of 2 in the Antiparallel Coiled Coil Hexamer Formed By De Novo Peptides (Acc- HEX2).


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 2 of Antiparallel Coiled Coil Hexamer Formed By De Novo Peptides (Acc- HEX2). within 5.0Å range: probe atom residue distance (Å) B Occ B:I23 b:84.3 occ:1.00 I B:PHI23 0.0 84.3 1.0 CZ B:PHI23 2.0 79.5 1.0 HD2 B:LYS19 3.0 56.3 1.0 CE1 B:PHI23 3.0 76.9 1.0 CE2 B:PHI23 3.0 75.1 1.0 HE1 B:PHI23 3.1 92.3 1.0 HE2 B:PHI23 3.1 90.2 1.0 HA A:GLU9 3.4 51.2 1.0 HB2 A:LYS12 3.5 58.4 1.0 HB3 B:LYS19 3.7 43.5 1.0 CD B:LYS19 3.8 46.9 1.0 HG2 A:GLU9 3.9 86.4 1.0 HG2 A:LYS12 3.9 68.8 1.0 HE3 B:LYS19 3.9 66.0 1.0 HZ2 B:LYS19 3.9 70.0 1.0 HB3 A:LYS12 3.9 58.4 1.0 HB3 A:LYS8 4.0 59.8 1.0 HG3 B:LYS19 4.0 49.7 1.0 CB A:LYS12 4.1 48.7 1.0 O A:LYS8 4.1 44.9 1.0 CA A:GLU9 4.2 42.7 1.0 CE B:LYS19 4.3 55.0 1.0 C A:LYS8 4.3 45.4 1.0 CD1 B:PHI23 4.3 73.3 1.0 N A:GLU9 4.3 41.5 1.0 CD2 B:PHI23 4.3 71.8 1.0 CG B:LYS19 4.3 41.4 1.0 HG3 A:GLU9 4.3 86.4 1.0 O B:HOH206 4.4 56.0 1.0 CB B:LYS19 4.5 36.3 1.0 CG A:LYS12 4.5 57.3 1.0 CG A:GLU9 4.5 72.0 1.0 NZ B:LYS19 4.5 58.3 1.0 HD3 B:LYS19 4.6 56.3 1.0 HD3 A:LYS12 4.7 75.5 1.0 H A:GLU9 4.7 49.8 1.0 HB2 A:LYS8 4.7 59.8 1.0 CB A:LYS8 4.7 49.8 1.0 CG B:PHI23 4.9 71.4 1.0 CB A:GLU9 4.9 55.8 1.0 HB2 B:LYS19 5.0 43.5 1.0

R.K.Spencer, A.I.Hochbaum. The Phe-Ile Zipper: A Specific Interaction Motif Drives Antiparallel Coiled-Coil Hexamer Formation. Biochemistry V. 56 5300 2017.
ISSN: ISSN 1520-4995
PubMed: 28876052
DOI: 10.1021/ACS.BIOCHEM.7B00756