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Magnesium in PDB 5uwo: Crystal Structure of Engineered Fmrp-1B Nes Peptide in Complex with CRM1-Ran-RANBP1

Protein crystallography data

The structure of Crystal Structure of Engineered Fmrp-1B Nes Peptide in Complex with CRM1-Ran-RANBP1, PDB code: 5uwo was solved by H.Y.J.Fung, Y.M.Chook, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.07 / 2.35
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 106.475, 106.475, 304.314, 90.00, 90.00, 90.00
R / Rfree (%) 18.8 / 22.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Engineered Fmrp-1B Nes Peptide in Complex with CRM1-Ran-RANBP1 (pdb code 5uwo). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Engineered Fmrp-1B Nes Peptide in Complex with CRM1-Ran-RANBP1, PDB code: 5uwo:

Magnesium binding site 1 out of 1 in 5uwo

Go back to Magnesium Binding Sites List in 5uwo
Magnesium binding site 1 out of 1 in the Crystal Structure of Engineered Fmrp-1B Nes Peptide in Complex with CRM1-Ran-RANBP1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Engineered Fmrp-1B Nes Peptide in Complex with CRM1-Ran-RANBP1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg302

b:20.8
occ:1.00
O2G A:GNP301 1.9 26.3 1.0
O A:HOH422 2.0 21.3 1.0
OG1 A:THR24 2.1 41.3 1.0
OG1 A:THR42 2.1 48.3 1.0
O A:HOH435 2.2 24.9 1.0
O1B A:GNP301 2.2 23.8 1.0
HB A:THR42 2.7 58.9 1.0
H A:THR42 2.9 36.1 1.0
CB A:THR42 3.0 49.1 1.0
HB A:THR24 3.0 43.7 1.0
CB A:THR24 3.1 36.4 1.0
PG A:GNP301 3.2 26.1 1.0
PB A:GNP301 3.4 25.9 1.0
H A:THR24 3.5 34.2 1.0
N A:THR42 3.6 30.1 1.0
N3B A:GNP301 3.6 26.9 1.0
CA A:THR42 3.8 51.7 1.0
HG21 A:THR24 3.9 46.4 1.0
O3G A:GNP301 4.0 26.2 1.0
OD2 A:ASP65 4.0 33.9 1.0
N A:THR24 4.0 28.5 1.0
CG2 A:THR24 4.1 38.7 1.0
O A:HOH413 4.1 36.7 1.0
HB2 A:LYS23 4.1 29.4 1.0
HG21 A:THR42 4.1 59.9 1.0
CA A:THR24 4.1 30.7 1.0
OD1 A:ASP65 4.1 32.5 1.0
CG2 A:THR42 4.2 49.9 1.0
O1A A:GNP301 4.2 32.4 1.0
HA A:THR42 4.2 62.0 1.0
O2B A:GNP301 4.3 26.3 1.0
O1G A:GNP301 4.3 25.4 1.0
HNB3 A:GNP301 4.4 32.3 1.0
HA A:THR24 4.4 36.9 1.0
CG A:ASP65 4.4 33.4 1.0
HA A:ALA41 4.5 41.6 1.0
HA A:ALA67 4.5 35.0 1.0
HE2 A:LYS23 4.5 34.5 1.0
HG23 A:THR24 4.5 46.4 1.0
O3A A:GNP301 4.5 26.3 1.0
O A:THR66 4.5 28.9 1.0
O2A A:GNP301 4.5 33.1 1.0
O A:VAL40 4.6 33.6 1.0
HG23 A:THR42 4.6 59.9 1.0
PA A:GNP301 4.7 30.7 1.0
HE1 A:TYR39 4.7 48.4 1.0
C A:ALA41 4.7 35.2 1.0
HZ1 A:LYS23 4.8 35.0 1.0
HG22 A:THR24 4.8 46.4 1.0
HG22 A:THR42 4.8 59.9 1.0
HZ3 A:LYS23 4.9 35.0 1.0

Reference:

H.Y.Fung, S.C.Fu, Y.M.Chook. Nuclear Export Receptor CRM1 Recognizes Diverse Conformations in Nuclear Export Signals. Elife V. 6 2017.
ISSN: ESSN 2050-084X
PubMed: 28282025
DOI: 10.7554/ELIFE.23961
Page generated: Mon Sep 30 05:26:27 2024

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