transfer of a phosphoryl group from ATP to AMP

Domain flexibility in ligand-free and inhibitor-bound Escherichia coli adenylate kinase based on a mode-coupling analysis of 15N spin relaxation.

Structure Of The Complex Between Adenylate Kinase From Escherichia Coli And The Inhibitor Ap5a Refined At 1.9 Angstroms Resolut

The Closed Conformation Of A Highly Flexible Protein: The Structure Of E. Cloi Adenylate Kinase With Bound Amp And Amppnp

Mutant G10v Of Adenylate Kinase From E. Coli, Modified In The Gly-Loop

Mutant P9l Of Adenylate Kinase From E. Coli, Modified In The Gly-Loop

Crystal Structure Of Wild-Type Adenylate Kinase From E. Coli, In Complex With Ap5a

Crystal Structure Of V148g Adenylate Kinase From E. Coli, In Complex With Ap5a

Crystal Structure Of Adenylate Kinase Of E. Coli With Adp/amp Bound

adenylate kinase [Escherichia coli K-12]

adenylate kinase [Escherichia coli O157:H7 str. Sakai]

adenylate kinase [Escherichia coli str. K-12 substr. W3110]

adenylate kinase [Escherichia coli SE11]

adenylate kinase Adk [Escherichia coli O26:H11 str. 11368]

unnamed protein product [Escherichia coli]

adenylate kinase [Escherichia coli str. K-12 substr. MG1655]

adenylate kinase activity; pleiotropic effects on glycerol-3-phosphate acyltransferase activity [Escherichia coli O157:H7 str.

adenylate kinase [Escherichia coli O157:H7 str. EDL933]

adenylate kinase [Shigella flexneri 2a str. 301]

adenylate kinase [Escherichia coli CFT073]

RecName: Full=Adenylate kinase; Short=AK; AltName: Full=ATP-AMP transphosphorylase; AltName: Full=ATP:AMP phosphotransferase; A

This depositions contains 15N T1, 15N T2,
15N-{1H} NOE and eta(xy) data for Adenylate
kinase from E. coli in the ligand-free form
and in complex with two-substrate mimicking
inhibitor Ap5A, obtained at two magnetic fields
of 14.10 T and 18.79 T.
15N-{1H} NOE values were corrected for incomplete
1H T1 recovery with equation by S. Grzeciek &
A. Bax. JACS, 1993, 115, 12593-12594. (The values
of corrections were significantly less than
experimental errors.)
The cross-correlation rates, eta(xy), between
15N CSA and 15N-1H dipolar interaction were
calculated as the median values obtained with
dephasing delays 2*delta of 14 ms (<15NT2>/8)
and 32 ms.

15N Relaxation Data of Escherichia coli Adenylate Kinase in Ligand-Free Form
Obtained at Magnetic Fields of 14.10 and 18.79 T

15N CSA - 15N-1H cross-correlation rate, eta(xy)

adenylate kinase in complex with inhibitor Ap5A

Delaglio, F., Grzesiek, S., Vuister, G.W.,
Zhu, G., Pfeifer, J., and Bax, A. (1995)
J. Biomol. NMR 6, 277-293.