Magnesium in PDB 8qxv: In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography

Enzymatic activity of In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography

All present enzymatic activity of In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography:
5.6.1.7;

Other elements in 8qxv:

The structure of In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography also contains other interesting chemical elements:

Potassium (K) 14 atoms

Magnesium Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 14;

Binding sites:

The binding sites of Magnesium atom in the In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography (pdb code 8qxv). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 14 binding sites of Magnesium where determined in the In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography, PDB code: 8qxv:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Magnesium binding site 1 out of 14 in 8qxv

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Magnesium binding site 1 out of 14 in the In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography


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Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg602

b:1000.0
occ:1.00
 OD1 A:ASP87 2.0 1000.0 1.0
O A:HOH704 2.0 1000.0 1.0
O1B A:ATP601 2.1 1000.0 1.0
O A:HOH710 2.2 1000.0 1.0
O3B A:ATP601 2.3 1000.0 1.0
O1G A:ATP601 2.4 1000.0 1.0
O2A A:ATP601 2.4 1000.0 1.0
PB A:ATP601 2.4 1000.0 1.0
PG A:ATP601 2.7 1000.0 1.0
O3A A:ATP601 2.7 1000.0 1.0
CG A:ASP87 2.9 1000.0 1.0
PA A:ATP601 3.2 1000.0 1.0
OD2 A:ASP87 3.2 1000.0 1.0
O2G A:ATP601 3.3 1000.0 1.0
O A:HOH718 3.6 1000.0 1.0
N A:GLY88 3.7 1000.0 1.0
O2B A:ATP601 3.9 1000.0 1.0
O A:SER151 4.0 1000.0 1.0
O A:HOH707 4.0 1000.0 1.0
O A:HOH719 4.0 1000.0 1.0
OG A:SER151 4.0 1000.0 1.0
O3G A:ATP601 4.1 1000.0 1.0
O5' A:ATP601 4.2 1000.0 1.0
CB A:ASP87 4.2 1000.0 1.0
C5' A:ATP601 4.2 1000.0 1.0
CA A:SER151 4.2 1000.0 1.0
O1A A:ATP601 4.3 1000.0 1.0
CA A:ASP87 4.4 1000.0 1.0
CA A:GLY88 4.5 1000.0 1.0
K A:K603 4.5 1000.0 1.0
C A:ASP87 4.6 1000.0 1.0
C A:SER151 4.6 1000.0 1.0
CB A:SER151 4.6 1000.0 1.0
OD2 A:ASP398 4.8 1000.0 1.0

Magnesium binding site 2 out of 14 in 8qxv

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Magnesium binding site 2 out of 14 in the In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg602

b:1000.0
occ:1.00
 O B:HOH704 2.1 1000.0 1.0
OD1 B:ASP87 2.1 1000.0 1.0
O1B B:ATP601 2.1 1000.0 1.0
O B:HOH719 2.2 1000.0 1.0
O3B B:ATP601 2.2 1000.0 1.0
O2A B:ATP601 2.3 1000.0 1.0
O1G B:ATP601 2.4 1000.0 1.0
PB B:ATP601 2.4 1000.0 1.0
PG B:ATP601 2.7 1000.0 1.0
O3A B:ATP601 2.8 1000.0 1.0
CG B:ASP87 3.0 1000.0 1.0
PA B:ATP601 3.2 1000.0 1.0
O2G B:ATP601 3.3 1000.0 1.0
OD2 B:ASP87 3.3 1000.0 1.0
O B:HOH710 3.6 1000.0 1.0
N B:GLY88 3.7 1000.0 1.0
O2B B:ATP601 3.9 1000.0 1.0
C5' B:ATP601 4.0 1000.0 1.0
OG B:SER151 4.0 1000.0 1.0
O5' B:ATP601 4.0 1000.0 1.0
O3G B:ATP601 4.1 1000.0 1.0
O B:HOH705 4.2 1000.0 1.0
O B:HOH714 4.2 1000.0 1.0
O B:SER151 4.2 1000.0 1.0
CB B:ASP87 4.2 1000.0 1.0
CA B:SER151 4.3 1000.0 1.0
O1A B:ATP601 4.3 1000.0 1.0
CA B:ASP87 4.4 1000.0 1.0
CA B:GLY88 4.4 1000.0 1.0
C B:ASP87 4.5 1000.0 1.0
CB B:SER151 4.6 1000.0 1.0
K B:K603 4.7 1000.0 1.0
C B:SER151 4.8 1000.0 1.0
OD2 B:ASP398 4.8 1000.0 1.0
C4' B:ATP601 4.9 1000.0 1.0
N B:THR89 5.0 1000.0 1.0

Magnesium binding site 3 out of 14 in 8qxv

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Magnesium binding site 3 out of 14 in the In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg602

b:1000.0
occ:1.00
 OD1 C:ASP87 2.1 1000.0 1.0
O C:HOH702 2.1 1000.0 1.0
O C:HOH720 2.1 1000.0 1.0
O3B C:ATP601 2.1 1000.0 1.0
O1B C:ATP601 2.2 1000.0 1.0
O2A C:ATP601 2.3 1000.0 1.0
PB C:ATP601 2.4 1000.0 1.0
O1G C:ATP601 2.7 1000.0 1.0
PG C:ATP601 2.9 1000.0 1.0
O3A C:ATP601 2.9 1000.0 1.0
CG C:ASP87 3.0 1000.0 1.0
PA C:ATP601 3.2 1000.0 1.0
OD2 C:ASP87 3.3 1000.0 1.0
O2G C:ATP601 3.5 1000.0 1.0
O C:HOH706 3.5 1000.0 1.0
N C:GLY88 3.7 1000.0 1.0
OG C:SER151 3.8 1000.0 1.0
C5' C:ATP601 3.9 1000.0 1.0
O2B C:ATP601 3.9 1000.0 1.0
O5' C:ATP601 4.0 1000.0 1.0
O3G C:ATP601 4.2 1000.0 1.0
CB C:ASP87 4.2 1000.0 1.0
CA C:SER151 4.3 1000.0 1.0
O C:SER151 4.3 1000.0 1.0
O C:HOH704 4.4 1000.0 1.0
O C:HOH715 4.4 1000.0 1.0
CA C:ASP87 4.4 1000.0 1.0
O1A C:ATP601 4.4 1000.0 1.0
CA C:GLY88 4.5 1000.0 1.0
CB C:SER151 4.5 1000.0 1.0
C C:ASP87 4.6 1000.0 1.0
OD2 C:ASP398 4.7 1000.0 1.0
C4' C:ATP601 4.7 1000.0 1.0
C C:SER151 4.8 1000.0 1.0
C3' C:ATP601 4.9 1000.0 1.0
CG C:ASP398 4.9 1000.0 1.0

Magnesium binding site 4 out of 14 in 8qxv

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Magnesium binding site 4 out of 14 in the In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg602

b:1000.0
occ:1.00
 OD1 D:ASP87 2.1 1000.0 1.0
O D:HOH706 2.1 1000.0 1.0
O1B D:ATP601 2.1 1000.0 1.0
O D:HOH705 2.2 1000.0 1.0
O3B D:ATP601 2.3 1000.0 1.0
PB D:ATP601 2.5 1000.0 1.0
O2A D:ATP601 2.5 1000.0 1.0
CG D:ASP87 2.9 1000.0 1.0
O1G D:ATP601 2.9 1000.0 1.0
O3A D:ATP601 3.0 1000.0 1.0
OD2 D:ASP87 3.1 1000.0 1.0
PG D:ATP601 3.1 1000.0 1.0
PA D:ATP601 3.4 1000.0 1.0
OG D:SER151 3.4 1000.0 1.0
O D:HOH712 3.6 1000.0 1.0
O2G D:ATP601 3.8 1000.0 1.0
N D:GLY88 3.9 1000.0 1.0
O2B D:ATP601 3.9 1000.0 1.0
O D:SER151 4.1 1000.0 1.0
CA D:SER151 4.1 1000.0 1.0
C5' D:ATP601 4.1 1000.0 1.0
O D:HOH719 4.1 1000.0 1.0
CB D:ASP87 4.2 1000.0 1.0
CB D:SER151 4.2 1000.0 1.0
O5' D:ATP601 4.2 1000.0 1.0
O3G D:ATP601 4.4 1000.0 1.0
O D:HOH709 4.4 1000.0 1.0
CA D:ASP87 4.5 1000.0 1.0
O1A D:ATP601 4.5 1000.0 1.0
C D:SER151 4.6 1000.0 1.0
CA D:GLY88 4.7 1000.0 1.0
C D:ASP87 4.8 1000.0 1.0
CB D:ASP398 4.8 1000.0 1.0
O D:HOH704 4.9 1000.0 1.0
C4' D:ATP601 5.0 1000.0 1.0

Magnesium binding site 5 out of 14 in 8qxv

Go back to Magnesium Binding Sites List in 8qxv
Magnesium binding site 5 out of 14 in the In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg602

b:1000.0
occ:1.00
 OD1 E:ASP87 2.1 1000.0 1.0
O E:HOH2001 2.1 1000.0 1.0
O1B E:ATP601 2.1 1000.0 1.0
O3B E:ATP601 2.2 1000.0 1.0
O E:HOH2002 2.2 1000.0 1.0
PB E:ATP601 2.4 1000.0 1.0
O2A E:ATP601 2.6 1000.0 1.0
CG E:ASP87 2.9 1000.0 1.0
O3A E:ATP601 2.9 1000.0 1.0
PG E:ATP601 3.0 1000.0 1.0
O1G E:ATP601 3.1 1000.0 1.0
OD2 E:ASP87 3.1 1000.0 1.0
PA E:ATP601 3.3 1000.0 1.0
OG E:SER151 3.4 1000.0 1.0
O2G E:ATP601 3.5 1000.0 1.0
O E:HOH2011 3.6 1000.0 1.0
OD2 E:ASP398 3.9 1000.0 1.0
N E:GLY88 3.9 1000.0 1.0
O2B E:ATP601 3.9 1000.0 1.0
O E:HOH2014 3.9 1000.0 1.0
CG E:ASP398 4.0 1000.0 1.0
O E:SER151 4.1 1000.0 1.0
CB E:ASP87 4.2 1000.0 1.0
CA E:SER151 4.3 1000.0 1.0
CB E:SER151 4.3 1000.0 1.0
O1A E:ATP601 4.4 1000.0 1.0
O E:HOH2013 4.4 1000.0 1.0
O3G E:ATP601 4.4 1000.0 1.0
O5' E:ATP601 4.4 1000.0 1.0
CB E:ASP398 4.4 1000.0 1.0
OD1 E:ASP398 4.5 1000.0 1.0
CA E:ASP87 4.5 1000.0 1.0
C5' E:ATP601 4.5 1000.0 1.0
C E:SER151 4.7 1000.0 1.0
C E:ASP87 4.7 1000.0 1.0
CA E:GLY88 4.7 1000.0 1.0

Magnesium binding site 6 out of 14 in 8qxv

Go back to Magnesium Binding Sites List in 8qxv
Magnesium binding site 6 out of 14 in the In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg602

b:1000.0
occ:1.00
 O F:HOH702 2.1 1000.0 1.0
OD1 F:ASP87 2.1 1000.0 1.0
O1B F:ATP601 2.1 1000.0 1.0
O3B F:ATP601 2.3 1000.0 1.0
O F:HOH704 2.3 1000.0 1.0
PB F:ATP601 2.4 1000.0 1.0
O2A F:ATP601 2.6 1000.0 1.0
O1G F:ATP601 2.9 1000.0 1.0
O3A F:ATP601 2.9 1000.0 1.0
PG F:ATP601 2.9 1000.0 1.0
CG F:ASP87 2.9 1000.0 1.0
O2G F:ATP601 3.2 1000.0 1.0
OD2 F:ASP87 3.2 1000.0 1.0
PA F:ATP601 3.3 1000.0 1.0
OG F:SER151 3.5 1000.0 1.0
O F:HOH721 3.8 1000.0 1.0
N F:GLY88 3.8 1000.0 1.0
O F:HOH712 3.9 1000.0 1.0
OD2 F:ASP398 3.9 1000.0 1.0
O2B F:ATP601 3.9 1000.0 1.0
CG F:ASP398 4.1 1000.0 1.0
O F:SER151 4.2 1000.0 1.0
CB F:ASP87 4.2 1000.0 1.0
O1A F:ATP601 4.3 1000.0 1.0
O3G F:ATP601 4.3 1000.0 1.0
CB F:ASP398 4.4 1000.0 1.0
CA F:SER151 4.4 1000.0 1.0
CA F:ASP87 4.4 1000.0 1.0
O F:HOH719 4.4 1000.0 1.0
O5' F:ATP601 4.4 1000.0 1.0
CB F:SER151 4.5 1000.0 1.0
C5' F:ATP601 4.6 1000.0 1.0
OD1 F:ASP398 4.6 1000.0 1.0
CA F:GLY88 4.6 1000.0 1.0
C F:ASP87 4.7 1000.0 1.0
C F:SER151 4.8 1000.0 1.0
K F:K603 5.0 1000.0 1.0

Magnesium binding site 7 out of 14 in 8qxv

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Magnesium binding site 7 out of 14 in the In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 7 of In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Mg602

b:1000.0
occ:1.00
 O G:HOH702 2.1 1000.0 1.0
OD1 G:ASP87 2.1 1000.0 1.0
O1B G:ATP601 2.2 1000.0 1.0
O G:HOH706 2.2 1000.0 1.0
O3B G:ATP601 2.3 1000.0 1.0
O2A G:ATP601 2.3 1000.0 1.0
O1G G:ATP601 2.3 1000.0 1.0
PB G:ATP601 2.4 1000.0 1.0
PG G:ATP601 2.7 1000.0 1.0
O3A G:ATP601 2.7 1000.0 1.0
CG G:ASP87 2.9 1000.0 1.0
PA G:ATP601 3.1 1000.0 1.0
OD2 G:ASP87 3.2 1000.0 1.0
O2G G:ATP601 3.3 1000.0 1.0
N G:GLY88 3.7 1000.0 1.0
O G:HOH721 3.8 1000.0 1.0
OG G:SER151 3.9 1000.0 1.0
O2B G:ATP601 3.9 1000.0 1.0
O G:HOH707 4.0 1000.0 1.0
O1A G:ATP601 4.1 1000.0 1.0
O3G G:ATP601 4.1 1000.0 1.0
O G:SER151 4.1 1000.0 1.0
O5' G:ATP601 4.2 1000.0 1.0
CB G:ASP87 4.2 1000.0 1.0
O G:HOH720 4.3 1000.0 1.0
C5' G:ATP601 4.3 1000.0 1.0
CA G:SER151 4.4 1000.0 1.0
OD2 G:ASP398 4.4 1000.0 1.0
CA G:ASP87 4.4 1000.0 1.0
CA G:GLY88 4.5 1000.0 1.0
C G:ASP87 4.6 1000.0 1.0
CG G:ASP398 4.6 1000.0 1.0
CB G:SER151 4.6 1000.0 1.0
C G:SER151 4.7 1000.0 1.0
CB G:ASP398 4.8 1000.0 1.0
K G:K603 4.9 1000.0 1.0

Magnesium binding site 8 out of 14 in 8qxv

Go back to Magnesium Binding Sites List in 8qxv
Magnesium binding site 8 out of 14 in the In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 8 of In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Mg602

b:1000.0
occ:1.00
 OD1 H:ASP87 2.1 1000.0 1.0
O2A H:ADP601 2.1 1000.0 1.0
O H:HOH706 2.1 1000.0 1.0
O H:HOH701 2.2 1000.0 1.0
O H:HOH709 2.4 1000.0 1.0
O2B H:ADP601 2.5 1000.0 1.0
O1B H:ADP601 2.5 1000.0 1.0
CG H:ASP87 2.9 1000.0 1.0
PB H:ADP601 2.9 1000.0 1.0
OD2 H:ASP87 3.0 1000.0 1.0
PA H:ADP601 3.3 1000.0 1.0
O3A H:ADP601 3.6 1000.0 1.0
N H:GLY88 4.2 1000.0 1.0
CB H:ASP87 4.3 1000.0 1.0
O3B H:ADP601 4.3 1000.0 1.0
O1A H:ADP601 4.4 1000.0 1.0
O5' H:ADP601 4.4 1000.0 1.0
C5' H:ADP601 4.7 1000.0 1.0
CA H:ASP87 4.7 1000.0 1.0
O H:HOH707 4.8 1000.0 1.0

Magnesium binding site 9 out of 14 in 8qxv

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Magnesium binding site 9 out of 14 in the In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 9 of In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Mg602

b:1000.0
occ:1.00
 O2B I:ADP601 2.0 1000.0 1.0
O I:HOH709 2.2 1000.0 1.0
O2A I:ADP601 2.2 1000.0 1.0
O I:HOH703 2.2 1000.0 1.0
OD1 I:ASP87 2.2 1000.0 1.0
O I:HOH701 2.4 898.2 1.0
O1B I:ADP601 2.8 1000.0 1.0
PB I:ADP601 2.8 1000.0 1.0
CG I:ASP87 3.0 1000.0 1.0
OD2 I:ASP87 3.1 1000.0 1.0
PA I:ADP601 3.4 1000.0 1.0
O3A I:ADP601 3.5 1000.0 1.0
O3B I:ADP601 4.2 1000.0 1.0
O5' I:ADP601 4.2 1000.0 1.0
N I:GLY88 4.3 1000.0 1.0
CB I:ASP87 4.4 1000.0 1.0
C5' I:ADP601 4.6 1000.0 1.0
O1A I:ADP601 4.6 1000.0 1.0
CA I:ASP87 4.9 1000.0 1.0
CA I:GLY88 5.0 1000.0 1.0

Magnesium binding site 10 out of 14 in 8qxv

Go back to Magnesium Binding Sites List in 8qxv
Magnesium binding site 10 out of 14 in the In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 10 of In Situ Structure Average of GROEL14-GROES7 Complexes with Narrow GROEL7 Trans Ring Conformation in Escherichia Coli Cytosol Obtained By Cryo Electron Tomography within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Mg602

b:1000.0
occ:1.00
 O2B J:ADP601 2.1 1000.0 1.0
O J:HOH708 2.1 1000.0 1.0
O J:HOH704 2.2 1000.0 1.0
O J:HOH706 2.3 1000.0 1.0
OD1 J:ASP87 2.5 1000.0 1.0
O1B J:ADP601 2.7 1000.0 1.0
O2A J:ADP601 2.8 1000.0 1.0
PB J:ADP601 2.9 1000.0 1.0
CG J:ASP87 3.1 1000.0 1.0
OD2 J:ASP87 3.1 1000.0 1.0
O3A J:ADP601 3.9 1000.0 1.0
PA J:ADP601 3.9 1000.0 1.0
N J:GLY88 4.0 1000.0 1.0
C5' J:ADP601 4.1 1000.0 1.0
O3B J:ADP601 4.1 1000.0 1.0
CB J:ASP87 4.5 1000.0 1.0
O5' J:ADP601 4.5 1000.0 1.0
O J:HOH703 4.6 1000.0 1.0
CA J:GLY88 4.7 1000.0 1.0
CA J:ASP87 4.9 1000.0 1.0
C J:ASP87 4.9 1000.0 1.0

Reference:

J.Wagner, A.I.Caravajal, F.Beck, A.Bracher, W.Wan, S.Bohn, R.Koerner, W.Baumeister, R.Fernandez-Busnadiego, F.U.Hartl. Visualizing Chaperonin Function in Situ By Cryo-Electron Tomography Nature 2024.
ISSN: ESSN 1476-4687
Page generated: Fri Oct 4 17:17:47 2024

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