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 11284

Title: Solution structure of the SH3 domain of human hypothetical protein FLJ21522

Deposition date: 2010-08-09 Original release date: 2011-08-18

Authors: Yoneyama, M.; Saito, K.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation: Yoneyama, M.; Saito, K.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the SH3 domain of human hypothetical protein FLJ21522"  .

Assembly members:
SH3 domain, polymer, 68 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: P040517-02

Entity Sequences (FASTA):
SH3 domain: GSSGSSGLKMQVLYEFEARN PRELTVVQGEKLEVLDHSKR WWLVKNEAGRSGYIPSNILE PLSGPSSG

Data sets:
Data typeCount
13C chemical shifts279
15N chemical shifts60
1H chemical shifts443

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SH3 domain1

Entities:

Entity 1, SH3 domain 68 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYLEULYSMET
2   GLNVALLEUTYRGLUPHEGLUALAARGASN
3   PROARGGLULEUTHRVALVALGLNGLYGLU
4   LYSLEUGLUVALLEUASPHISSERLYSARG
5   TRPTRPLEUVALLYSASNGLUALAGLYARG
6   SERGLYTYRILEPROSERASNILELEUGLU
7   PROLEUSERGLYPROSERSERGLY

Samples:

sample_1: SH3 domain, [U-13C; U-15N], 1.33 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
4D 13C-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

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

Kujira v0.921, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
GB EAW56414
REF NP_620641 XP_011540429 XP_011540430 XP_011540431 XP_011540432

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