BMRB Entry 10025

Title:
Solution structure of kinase associated domain 1 of mouse MAP/microtubule affinity-regulating kinase 3
Deposition date:
2006-09-07
Original release date:
2008-07-16
Authors:
Tochio, N.; Koshiba, S.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Tochio, N.; Koshiba, S.; Kobayashi, N.; Inoue, M.; Yabuki, T.; Aoki, M.; Seki, E.; Matsuda, T.; Tomo, Y.; Motoda, Y.; Kobayashi, A.; Tanaka, A.; Hayashizaki, Y.; Terada, T.; Shirouzu, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the kinase-associated domain 1 of mouse microtubule-associated protein/microtubule affinity-regulating kinase 3"  Protein Sci. 15, 2534-2543 (2006).
PubMed: 17075132

Assembly members:

Assembly members:
kinase associated domain 1(KA1), polymer, 102 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: cell free synthesis   Vector: P021202-01

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts436
15N chemical shifts102
1H chemical shifts696

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1kinase associated domain 1(KA1)1

Entities:

Entity 1, kinase associated domain 1(KA1) 102 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYARGPHETHR
2   TRPSERMETLYSTHRTHRSERSERMETASP
3   PROSERASPMETMETARGGLUILEARGLYS
4   VALLEUGLYALAASNASNCYSASPTYRGLU
5   GLNARGGLUARGPHELEULEUPHECYSVAL
6   HISGLYASPGLYHISALAGLUASNLEUVAL
7   GLNTRPGLUMETGLUVALCYSLYSLEUPRO
8   ARGLEUSERLEUASNGLYVALARGPHELYS
9   ARGILESERGLYTHRSERILEALAPHELYS
10   ASNILEALASERLYSILEALAASNGLULEU
11   LYSLEU

Samples:

sample_1: KA1 domain, [U-13C; U-15N], 1.0 mM; phosphate 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; D2O 10%; H2O 90%

condition_1: ionic strength: 120 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1isotropiccondition_1
3D 15N-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.853, Kobayashi, N. - data analysis

CYANA v2.0.17, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAC35922 BAD92779 BAE21056 BAE38602 BAG59243
EMBL CAD61882 CAD62578
GB AAA59991 AAC15093 AAD48007 AAD51631 AAF64455
REF NP_001122390 NP_001122391 NP_001122392 NP_001122393 NP_002367
SP P27448 Q03141
AlphaFold P27448 Q03141

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