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 11156

Title: Solution structure of the SH3 domain of human Nostrin

Deposition date: 2010-04-15 Original release date: 2011-05-05

Authors: Abe, H.; Tochio, N.; Miyamoto, K.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation: Abe, H.; Miyamoto, K.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the SH3 domain of human Nostrin"  .

Assembly members:
SH3 domain, polymer, 79 residues, Formula weight is not available

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

Experimental source:   Production method: cell free synthesis   Host organism: E. coli - cell free   Vector: P050620-15

Entity Sequences (FASTA):
SH3 domain: GSSGSSGRLCKALYSFQARQ DDELNLEKGDIVIIHEKKEE GWWFGSLNGKKGHFPAAYVE ELPSNAGNTATKASGPSSG

Data sets:
Data typeCount
13C chemical shifts318
15N chemical shifts73
1H chemical shifts488

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SH3 domain1

Entities:

Entity 1, SH3 domain 79 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYARGLEUCYS
2   LYSALALEUTYRSERPHEGLNALAARGGLN
3   ASPASPGLULEUASNLEUGLULYSGLYASP
4   ILEVALILEILEHISGLULYSLYSGLUGLU
5   GLYTRPTRPPHEGLYSERLEUASNGLYLYS
6   LYSGLYHISPHEPROALAALATYRVALGLU
7   GLULEUPROSERASNALAGLYASNTHRALA
8   THRLYSALASERGLYPROSERSERGLY

Samples:

sample_1: SH3 domain, [U-13C; U-15N], 1.1 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

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

Kujira v0.9747, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
REF XP_005573448 XP_007963454 XP_010352711 XP_011902294

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