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 16297

Title: AIDA-1 SAM domain tandem   PubMed: 19666031

Deposition date: 2009-05-12 Original release date: 2009-09-04

Authors: Donaldson, Logan; Kurabi, Arwa

Citation: Kurabi, Arwa; Brener, Stacey; Mobli, Mehdi; Kwan, Jamie; Donaldson, Logan. "A Nuclear Localization Signal at the SAM-SAM Domain Interface of AIDA-1 Suggests a Requirement for Domain Uncoupling Prior to Nuclear Import"  J. Mol. Biol. 392, 1168-1177 (2009).

Assembly members:
AIDA-1 SAM domain, polymer, 148 residues, 15101.473 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
AIDA-1 SAM domain: MHHHHHHLVPRGSVQTVGQW LESIGLPQYENHLMANGFDN VQAMGSNVMEDQDLLEIGIL NSGHRQRILQAIQLLPKMRP IGHDGAHPTSVAEWLDSIEL GDYTKAFLINGYTSMDLLKK IAEVELINVLKINLIGHRKR ILASLGDR

Data sets:
Data typeCount
13C chemical shifts510
15N chemical shifts121
1H chemical shifts791

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1AIDA-1 SAM domain1

Entities:

Entity 1, AIDA-1 SAM domain 148 residues - 15101.473 Da.

1   METHISHISHISHISHISHISLEUVALPRO
2   ARGGLYSERVALGLNTHRVALGLYGLNTRP
3   LEUGLUSERILEGLYLEUPROGLNTYRGLU
4   ASNHISLEUMETALAASNGLYPHEASPASN
5   VALGLNALAMETGLYSERASNVALMETGLU
6   ASPGLNASPLEULEUGLUILEGLYILELEU
7   ASNSERGLYHISARGGLNARGILELEUGLN
8   ALAILEGLNLEULEUPROLYSMETARGPRO
9   ILEGLYHISASPGLYALAHISPROTHRSER
10   VALALAGLUTRPLEUASPSERILEGLULEU
11   GLYASPTYRTHRLYSALAPHELEUILEASN
12   GLYTYRTHRSERMETASPLEULEULYSLYS
13   ILEALAGLUVALGLULEUILEASNVALLEU
14   LYSILEASNLEUILEGLYHISARGLYSARG
15   ILELEUALASERLEUGLYASPARG

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 1.1 mM; D2O 10%; H2O 90%; sodium azide 0.05%; sodium phosphate 5 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 7.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian Uniform NMR System 600 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
GB AIC60436

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts