BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 25353

Title: Backbone 1H and 15N Chemical Shift Assignments for P177A mutant of Adenylate Kinase   PubMed: 26138143

Authors: Kovermann, Michael; Wolf-Watz, Magnus

Citation: Kovermann, Michael; Aden, Jorgen; Grundstrom, Christine; Sauer-Eriksson, Elisabeth; Sauer, Uwe; Wolf-Watz, Magnus. "Structural basis for catalytically restrictive dynamics of a high-energy enzyme state"  Nat. Commun. 6, .-. (2015).

Assembly members:
Kinase, polymer, 214 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
Kinase: MRIILLGAPGAGKGTQAQFI MEKYGIPQISTGDMLRAAVK SGSELGKQAKDIMDAGKLVT DELVIALVKERIAQEDCRNG FLLDGFPRTIPQADAMKEAG INVDYVLEFDVPDELIVDRI VGRRVHAPSGRVYHVKFNPP KVEGKDDVTGEELTTRKDDQ EETVRKRLVEYHQMTAALIG YYSKEAEAGNTKYAKVDGTK PVAEVRADLEKILG

Data sets:
Data typeCount
15N chemical shifts198
1H chemical shifts198

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Adenylate Kinase P177A1

Entities:

Entity 1, Adenylate Kinase P177A 214 residues - Formula weight is not available

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

Samples:

sample_1: Adenylate Kinase P177A, [U-100% 15N], 0.7 mM; sodium chloride 50 mM; MOPS 30 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Johnson, One Moon Scientific - collection, data analysis, processing

NMR spectrometers:

  • Bruker Avance 850 MHz

Related Database Links:

BMRB 18683 18685 18686 18687 19089 19090 19091 19092 19093 25357 25360 25361 25362 4152 4193 4350
PDB
DBJ BAA14303 BAB33950 BAE76253 BAG76023 BAI23848
EMBL CAA26840 CAF33430 CAF33431 CAF33432 CAF33433
GB AAA23461 AAB40228 AAC73576 AAG54823 AAM94352
REF NP_308554 NP_415007 NP_706367 WP_001220233 WP_001220235
SP A7ZIN4 A7ZXD2 B1IZC0 B1LJN2 B1XFR1