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 15563

Title: Backbone 1H, 13C and 15N chemical shift assignment of N-terminal end (1-85) of human SRC   PubMed: 19520085

Deposition date: 2007-11-26 Original release date: 2009-06-29

Authors: Perez, Yolanda; Bernad, Pau; Gair, Margarida; Pons, Miquel

Citation: Perez, Yolanda; Gairi, Margarida; Pons, Miquel; Bernado, Pau. "Structural Characterization of the Natively Unfolded N-Terminal Domain of Human c-Src Kinase: Insights into the Role of Phosphorylation of the Unique Domain."  J. Mol. Biol. 391, 136-148 (2009).

Assembly members:
USRC, polymer, 95 residues, Formula weight is not available

Natural source:   Common Name: not available   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet14a

Entity Sequences (FASTA):
USRC: MASNKSKPKDASQRRRSLEP AENVHGAGGGAFPASQTPSK PASADGHRGPSAAFAPAAAE PKLFGGFNSSDTVTSPQRAG PLAGGSAWSHPQFEK

Data sets:
Data typeCount
13C chemical shifts266
15N chemical shifts91
1H chemical shifts80

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1USRC1

Entities:

Entity 1, USRC 95 residues - Formula weight is not available

1   METALASERASNLYSSERLYSPROLYSASP
2   ALASERGLNARGARGARGSERLEUGLUPRO
3   ALAGLUASNVALHISGLYALAGLYGLYGLY
4   ALAPHEPROALASERGLNTHRPROSERLYS
5   PROALASERALAASPGLYHISARGGLYPRO
6   SERALAALAPHEALAPROALAALAALAGLU
7   PROLYSLEUPHEGLYGLYPHEASNSERSER
8   ASPTHRVALTHRSERPROGLNARGALAGLY
9   PROLEUALAGLYGLYSERALATRPSERHIS
10   PROGLNPHEGLULYS

Samples:

sample_1: USRC, [U-100% 13C; U-100% 15N], 0.6 mM; PMSF 0.2 mM; sodium acetate 50 mM; D2O, [U-99% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 50 mM; pH: 4.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D COCONsample_1isotropicsample_conditions_1
2D CONsample_1isotropicsample_conditions_1
3D CBCACONsample_1isotropicsample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin, Goddard - chemical shift assignment, collection, peak picking, processing

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz

Related Database Links:

PDB
DBJ BAI47379
GB AAA60584 AAH11566 AAH51270 AAX29840 ACE86438
REF NP_001248263 NP_005408 NP_938033 XP_004062179 XP_005569018
SP P12931
AlphaFold P12931

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