BMRB Entry 27708

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27708

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Backbone 1H, 13C and 15N chemical shift assignment of myristoylated SH4-Unique-SH3 domains or myrUSH3 AAA (2-150; L63A, F64A, G65A) of human SRC
Deposition date:
2018-11-30
Original release date:
2019-01-02
Authors:
Le Roux, Anabel Lise; Mohammad, Irrem-Laareb; Mateos, Borja; Arbesu, Miguel; Gairi, Margarida; Khan, Farman; Teixeira, Joao; Pons, Miquel
Citation:

Citation: Le Roux, Anabel Lise; Mohammad, Irrem-Laareb; Mateos, Borja; Arbesu, Miguel; Gairi, Margarida; Khan, Farman; Teixeira, Joao; Pons, Miquel. "A myristoyl binding site in the SH3 domain modulates c-Src membrane anchoring"  iScience 12, 194-203 (2019).
PubMed: 30690395

Assembly members:

Assembly members:
myrUSH3_AAA, polymer, 156 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETDuet-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
myrUSH3_AAA: mGSNKSKPKNASQRRRSLEP AENVHGAGGGAFPASQTPSK PASADGHRGPSAAFAPAAAE PKAAAGFNSSDTVTSPQRAG PLAGGVTTFVALYDYESRTE TDLSFKKGERLQIVNNTEGD WWLAHSLSTGQTGYIPSNYV APSDSIQAEEHHHHHH

Data sets:
Data typeCount
13C chemical shifts549
15N chemical shifts169
1H chemical shifts169

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1myrUSH3 AAA1

Entities:

Entity 1, myrUSH3 AAA 156 residues - Formula weight is not available

The first residue in the entity is a myristoylated Gly (mG) which correspond to residue 2 in the sequence ; Residues 151-156 represent a non-native affinity tag

1   METGLYSERASNLYSSERLYSPROLYSASN
2   ALASERGLNARGARGARGSERLEUGLUPRO
3   ALAGLUASNVALHISGLYALAGLYGLYGLY
4   ALAPHEPROALASERGLNTHRPROSERLYS
5   PROALASERALAASPGLYHISARGGLYPRO
6   SERALAALAPHEALAPROALAALAALAGLU
7   PROLYSALAALAALAGLYPHEASNSERSER
8   ASPTHRVALTHRSERPROGLNARGALAGLY
9   PROLEUALAGLYGLYVALTHRTHRPHEVAL
10   ALALEUTYRASPTYRGLUSERARGTHRGLU
11   THRASPLEUSERPHELYSLYSGLYGLUARG
12   LEUGLNILEVALASNASNTHRGLUGLYASP
13   TRPTRPLEUALAHISSERLEUSERTHRGLY
14   GLNTHRGLYTYRILEPROSERASNTYRVAL
15   ALAPROSERASPSERILEGLNALAGLUGLU
16   HISHISHISHISHISHIS

Samples:

sample_1: myrUSH3 AAA, [U-13C; U-15N], 135 uM; sodium phosphate 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_2
3D HNCOsample_1isotropicsample_conditions_2
3D HN(CO)CAsample_1isotropicsample_conditions_2
3D HNCAsample_1isotropicsample_conditions_2
3D HN(CO)CACBsample_1isotropicsample_conditions_2
3D HNCACBsample_1isotropicsample_conditions_2
3D HN(CA)COsample_1isotropicsample_conditions_2

Software:

TANSY, TANSY-Vladislav Orekhov et al. - collection, processing, analysis, and automated backbone assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

UniProt P12931
AlphaFold Q9H5A8

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