BMRB Entry 27954

Title:
Adenylate kinase mutant R119K bound to ATP
Deposition date:
2019-06-24
Original release date:
2019-07-30
Authors:
Rogne, Per; Wolf-Watz, Magnus
Citation:

Citation: Rogne, Per; Andersson, David; Grundstrom, Christin; Sauer-Eriksson, Elisabeth; Linusson, Anna; Wolf-Watz, Magnus. "Nucleation of an Activating Conformational Change by a Cation-pi Interaction"  Biochemistry 58, 3408-3412 (2019).
PubMed: 31339702

Assembly members:

Assembly members:
Adenylate_kinase, polymer, 214 residues, 23557 Da.
entity_ATP, non-polymer, 507.181 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pEAK91

Data sets:
Data typeCount
15N chemical shifts158
1H chemical shifts158

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Protein1
2ATP2

Entities:

Entity 1, Protein 214 residues - 23557 Da.

1   METARGILEILELEULEUGLYALAPROGLY
2   ALAGLYLYSGLYTHRGLNALAGLNPHEILE
3   METGLULYSTYRGLYILEPROGLNILESER
4   THRGLYASPMETLEUARGALAALAVALLYS
5   SERGLYSERGLULEUGLYLYSGLNALALYS
6   ASPILEMETASPALAGLYLYSLEUVALTHR
7   ASPGLULEUVALILEALALEUVALLYSGLU
8   ARGILEALAGLNGLUASPCYSARGASNGLY
9   PHELEULEUASPGLYPHEPROARGTHRILE
10   PROGLNALAASPALAMETLYSGLUALAGLY
11   ILEASNVALASPTYRVALLEUGLUPHEASP
12   VALPROASPGLULEUILEVALASPLYSILE
13   VALGLYARGARGVALHISALAPROSERGLY
14   ARGVALTYRHISVALLYSPHEASNPROPRO
15   LYSVALGLUGLYLYSASPASPVALTHRGLY
16   GLUGLULEUTHRTHRARGLYSASPASPGLN
17   GLUGLUTHRVALARGLYSARGLEUVALGLU
18   TYRHISGLNMETTHRALAPROLEUILEGLY
19   TYRTYRSERLYSGLUALAGLUALAGLYASN
20   THRLYSTYRALALYSVALASPGLYTHRLYS
21   PROVALALAGLUVALARGALAASPLEUGLU
22   LYSILELEUGLY

Entity 2, ATP - C10 H16 N5 O13 P3 - 507.181 Da.

1   ATP

Samples:

sample_1: Adenylate kinase, [U-100% 15N], 200 uM; ADENOSINE-5'-TRIPHOSPHATE 10 mM; MOPS 30 mM; sodium chloride 50 mM; D2O, [U-100% 2H], 7 % v/v

sample_conditions_1: ionic strength: 0.05 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.6, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

ANSIG, Kraulis - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 850 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks