Sodium in PDB 5nmn: Atomic Resolution Structure of Ll-37 in A Monomeric State

The structure of Atomic Resolution Structure of Ll-37 in A Monomeric State, PDB code: 5nmn was solved by K.Zeth, E.Sancho-Vaello, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.14 / 0.95
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	60.381, 17.832, 34.032, 90.00, 105.19, 90.00
R / Rfree (%)	15.6 / 15.4

The binding sites of Sodium atom in the Atomic Resolution Structure of Ll-37 in A Monomeric State (pdb code 5nmn). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Atomic Resolution Structure of Ll-37 in A Monomeric State, PDB code: 5nmn:

Sodium binding site 1 out of 1 in the Atomic Resolution Structure of Ll-37 in A Monomeric State


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Atomic Resolution Structure of Ll-37 in A Monomeric State within 5.0Å range: probe atom residue distance (Å) B Occ A:Na101 b:14.4 occ:1.00 HH12 A:ARG23 2.3 69.5 1.0 HD22 A:ASN30 2.5 19.1 1.0 HH22 A:ARG23 2.7 91.7 1.0 HA A:PHE27 2.8 14.2 1.0 HD1 A:PHE27 3.1 16.4 1.0 NH1 A:ARG23 3.1 57.9 1.0 ND2 A:ASN30 3.3 15.9 1.0 NH2 A:ARG23 3.4 76.4 1.0 HB2 A:ASN30 3.5 15.4 1.0 CA A:PHE27 3.7 11.9 1.0 HB2 A:PHE27 3.8 15.0 1.0 CZ A:ARG23 3.8 65.1 1.0 HH11 A:ARG23 3.8 69.5 1.0 HD21 A:ASN30 3.8 19.1 1.0 CD1 A:PHE27 4.0 13.7 1.0 CB A:ASN30 4.2 12.9 1.0 HB3 A:ASN30 4.2 15.4 1.0 CB A:PHE27 4.2 12.5 1.0 O A:HOH201 4.2 35.2 1.0 HH21 A:ARG23 4.2 91.7 1.0 CG A:ASN30 4.2 14.1 1.0 N A:PHE27 4.3 12.4 1.0 CG A:PHE27 4.5 12.9 1.0 O A:ASP26 4.6 13.3 1.0 H A:PHE27 4.6 14.9 1.0 C A:ASP26 4.6 12.5 1.0 HB3 A:ASP26 4.8 20.2 1.0 O A:PHE27 4.8 12.1 1.0 C A:PHE27 4.8 11.0 1.0 CE1 A:PHE27 5.0 14.7 1.0 HE1 A:PHE27 5.0 17.6 1.0

E.Sancho-Vaello, P.Francois, E.J.Bonetti, H.Lilie, S.Finger, F.Gil-Ortiz, D.Gil-Carton, K.Zeth. Structural Remodeling and Oligomerization of Human Cathelicidin on Membranes Suggest Fibril-Like Structures As Active Species. Sci Rep V. 7 15371 2017.
ISSN: ESSN 2045-2322
PubMed: 29133814
DOI: 10.1038/S41598-017-14206-1