BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 5933

Title: Sequence-specific backbone and sidechain resonance assignments of the Ste50 binding domain of the MAPKKK Ste11   PubMed: 15544813

Authors: Bhattacharjya, Surajit; Xu, Ping; Shaykhutdinov, Rustem; Gingras, Richard; Ni, Feng

Citation: Bhattacharjya, Surajit; Xu, Ping; Gingras, R.; Shaykhutdinov, R.; Wu, C.; Whiteway, M.; Ni, Feng. "Solution structure of the dimeric SAM domain of MAPKKK Ste11 and its interactions with the adaptor protein Ste50 from the budding yeast: implications for Ste11 activation and signal transmission through the Ste50-Ste11 complex"  J. Mol. Biol. 344, 1071-1087 (2004).

Assembly members:
SAM domain of Ste11, polymer, 68 residues, Formula weight is not available

Natural source:   Common Name: Budding yeast   Taxonomy ID: 4932   Superkingdom: Eucaryote   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

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

Entity Sequences (FASTA):
SAM domain of Ste11: DEKTNDLPFVQLFLEEIGCT QYLDSFIQCNLVTEEEIKYL DKDILIALGVNKIGDRLKIL RKSKSFQR

Data sets:
Data typeCount
1H chemical shifts474
13C chemical shifts299
15N chemical shifts72

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Ste11 SAM, chain 11
2Ste11 SAM, chain 21

Entities:

Entity 1, Ste11 SAM, chain 1 68 residues - Formula weight is not available

1   ASPGLULYSTHRASNASPLEUPROPHEVAL
2   GLNLEUPHELEUGLUGLUILEGLYCYSTHR
3   GLNTYRLEUASPSERPHEILEGLNCYSASN
4   LEUVALTHRGLUGLUGLUILELYSTYRLEU
5   ASPLYSASPILELEUILEALALEUGLYVAL
6   ASNLYSILEGLYASPARGLEULYSILELEU
7   ARGLYSSERLYSSERPHEGLNARG

Samples:

sample_1: SAM domain of Ste11, [U-15N], 0.8 mM; K-phosphate buffer 10 mM; NaCl 300 mM

sample_2: SAM domain of Ste11, [U-15N; U-13C], 0.8 mM; K-phosphate buffer 10 mM; NaCl 300 mM

sample_conditions_set_1: pH: 5.8; temperature: 288 K; ionic strength: 0.01 M

Experiments:

NameSampleSample stateSample conditions
2D (1H-15N) HSQCnot availablenot availablenot available
2D (1H-1H) NOESYnot availablenot availablenot available
3D (1H-15N) NOESY-HSQCnot availablenot availablenot available
3D (1H-15N) TOCSY-HSQCnot availablenot availablenot available
3D HNCAnot availablenot availablenot available
3D HN(CO)CAnot availablenot availablenot available
3D CBCA(CO)NHnot availablenot availablenot available
3D HNCOnot availablenot availablenot available
3D HBHA(C0)NHnot availablenot availablenot available
3D (H)CCH-COSYnot availablenot availablenot available
3D (1H-13C) NOESY-HSQCnot availablenot availablenot available

Software:

NMR-PIPE - FID transformations

NMR-View - spectral analysis

NMR spectrometers:

  • Bruker DRX 800 MHz

Related Database Links:

PDB
DBJ GAA25223
EMBL CAA37522 CAY81586
GB AAB67571 AHY78717 EDN59268 EDZ70440 EEU06456
REF NP_013466
SP A7A1P0 B5VNQ3 P23561
TPG DAA09666