Osmium in PDB 5cws: Crystal Structure of the Intact Chaetomium Thermophilum NSP1-NUP49- NUP57 Channel Nucleoporin Heterotrimer Bound to Its NIC96 Nuclear Pore Complex Attachment Site

The structure of Crystal Structure of the Intact Chaetomium Thermophilum NSP1-NUP49- NUP57 Channel Nucleoporin Heterotrimer Bound to Its NIC96 Nuclear Pore Complex Attachment Site, PDB code: 5cws was solved by C.J.Bley, S.Petrovic, M.Paduch, V.Lu, A.A.Kossiakoff, A.Hoelz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.67 / 3.77
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	123.180, 162.820, 212.870, 90.00, 90.00, 90.00
R / Rfree (%)	22.9 / 26.5

The binding sites of Osmium atom in the Crystal Structure of the Intact Chaetomium Thermophilum NSP1-NUP49- NUP57 Channel Nucleoporin Heterotrimer Bound to Its NIC96 Nuclear Pore Complex Attachment Site (pdb code 5cws). This binding sites where shown within 5.0 Angstroms radius around Osmium atom.
In total 2 binding sites of Osmium where determined in the Crystal Structure of the Intact Chaetomium Thermophilum NSP1-NUP49- NUP57 Channel Nucleoporin Heterotrimer Bound to Its NIC96 Nuclear Pore Complex Attachment Site, PDB code: 5cws:
Jump to Osmium binding site number: 1; 2;

Osmium binding site 1 out of 2 in the Crystal Structure of the Intact Chaetomium Thermophilum NSP1-NUP49- NUP57 Channel Nucleoporin Heterotrimer Bound to Its NIC96 Nuclear Pore Complex Attachment Site


Mono view


Stereo pair view

A full contact list of Osmium with other atoms in the Os binding site number 1 of Crystal Structure of the Intact Chaetomium Thermophilum NSP1-NUP49- NUP57 Channel Nucleoporin Heterotrimer Bound to Its NIC96 Nuclear Pore Complex Attachment Site within 5.0Å range: probe atom residue distance (Å) B Occ C:Os701 b:0.9 occ:1.00 HG21 C:THR617 2.1 0.9 1.0 HG23 C:THR617 2.9 0.9 1.0 CG2 C:THR617 2.9 0.4 1.0 O C:PRO612 3.0 0.1 1.0 HH22 C:ARG621 3.2 0.1 1.0 NH2 C:ARG621 3.3 0.9 1.0 HH12 C:ARG621 3.3 0.2 1.0 CZ C:ARG621 3.4 0.8 1.0 NH1 C:ARG621 3.4 0.3 1.0 HG22 C:THR617 3.5 0.9 1.0 HG1 C:THR617 3.5 0.1 1.0 HH21 C:ARG621 3.7 0.1 1.0 HH11 C:ARG621 3.9 0.2 1.0 OG1 C:THR617 4.0 0.8 1.0 CB C:THR617 4.0 0.8 1.0 C C:PRO612 4.1 0.7 1.0 NE C:ARG621 4.2 1.0 1.0 HB C:THR617 4.4 0.9 1.0 HA C:PRO612 4.5 0.1 1.0 HE C:ARG621 4.6 0.8 1.0 HA C:ASP613 4.6 0.6 1.0 HD2 C:ARG621 4.6 0.9 1.0 OD2 C:ASP614 4.8 0.2 1.0 CA C:PRO612 4.8 0.5 1.0 HB3 C:PRO612 4.8 0.6 1.0

Osmium binding site 2 out of 2 in the Crystal Structure of the Intact Chaetomium Thermophilum NSP1-NUP49- NUP57 Channel Nucleoporin Heterotrimer Bound to Its NIC96 Nuclear Pore Complex Attachment Site


Mono view


Stereo pair view

A full contact list of Osmium with other atoms in the Os binding site number 2 of Crystal Structure of the Intact Chaetomium Thermophilum NSP1-NUP49- NUP57 Channel Nucleoporin Heterotrimer Bound to Its NIC96 Nuclear Pore Complex Attachment Site within 5.0Å range: probe atom residue distance (Å) B Occ I:Os701 b:1.0 occ:1.00 O I:PRO612 2.2 0.2 1.0 HA I:PRO612 2.4 0.8 1.0 HH22 I:ARG621 2.7 0.4 1.0 C I:PRO612 2.8 0.9 1.0 CA I:PRO612 2.9 0.4 1.0 HB2 I:PRO612 2.9 0.7 1.0 NH2 I:ARG621 2.9 0.3 1.0 HH12 I:ARG621 3.1 0.4 1.0 CZ I:ARG621 3.2 0.2 1.0 CB I:PRO612 3.2 0.1 1.0 NH1 I:ARG621 3.3 0.7 1.0 HH21 I:ARG621 3.3 0.4 1.0 HB3 I:PRO612 3.4 0.7 1.0 HH11 I:ARG621 3.8 0.4 1.0 OG1 I:THR617 3.9 0.1 1.0 NE I:ARG621 4.0 0.8 1.0 N I:ASP613 4.1 0.1 1.0 HB I:THR617 4.2 0.3 1.0 N I:PRO612 4.3 0.1 1.0 HE I:ARG621 4.3 0.8 1.0 O I:LYS611 4.5 0.4 1.0 HA I:ASP613 4.5 0.9 1.0 HG1 I:THR617 4.5 0.7 1.0 CB I:THR617 4.6 0.1 1.0 HD2 I:ARG621 4.6 0.2 1.0 CG I:PRO612 4.7 0.7 1.0 H I:ASP613 4.8 0.6 1.0 HG21 I:THR617 4.8 0.6 1.0 HG2 I:PRO612 4.9 0.2 1.0 C I:LYS611 4.9 0.1 1.0 CA I:ASP613 4.9 0.6 1.0 CD I:ARG621 5.0 0.2 1.0

T.Stuwe, C.J.Bley, K.Thierbach, S.Petrovic, S.Schilbach, D.J.Mayo, T.Perriches, E.J.Rundlet, Y.E.Jeon, L.N.Collins, F.M.Huber, D.H.Lin, M.Paduch, A.Koide, V.Lu, J.Fischer, E.Hurt, S.Koide, A.A.Kossiakoff, A.Hoelz. Architecture of the Fungal Nuclear Pore Inner Ring Complex. Science V. 350 56 2015.
ISSN: ESSN 1095-9203
PubMed: 26316600
DOI: 10.1126/SCIENCE.AAC9176