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 11318

Title: Solution Strutcure of the SH3 domain of the Cdc42-interacting protein 4

Deposition date: 2010-08-10 Original release date: 2011-08-19

Authors: Miyamoto, K.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation: Miyamoto, K.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution Strutcure of the SH3 domain of the Cdc42-interacting protein 4"  .

Assembly members:
SH3 domain, polymer, 70 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: P041213-01

Entity Sequences (FASTA):
SH3 domain: GSSGSSGGHCVAIYHFEGSS EGTISMAEGEDLSLMEEDKG DGWTRVRRKEGGEGYVPTSY LRVTSGPSSG

Data sets:
Data typeCount
13C chemical shifts257
15N chemical shifts61
1H chemical shifts389

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SH3 domain1

Entities:

Entity 1, SH3 domain 70 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYGLYHISCYS
2   VALALAILETYRHISPHEGLUGLYSERSER
3   GLUGLYTHRILESERMETALAGLUGLYGLU
4   ASPLEUSERLEUMETGLUGLUASPLYSGLY
5   ASPGLYTRPTHRARGVALARGARGLYSGLU
6   GLYGLYGLUGLYTYRVALPROTHRSERTYR
7   LEUARGVALTHRSERGLYPROSERSERGLY

Samples:

sample_1: SH3 domain, [U-13C; U-15N], 1.36 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: 296 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 v0.925, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 700 MHz

Related Database Links:

PDB
DBJ BAD96829 BAE00629 BAF80144 BAG36103 BAK63850
EMBL CAA04062 CAG38751 CAH90516
GB AAC41729 AAH13002 AAI33400 AAM46851 AAP35344
REF NP_001074999 NP_001125273 NP_001275891 NP_004231 XP_001092276
SP Q15642 Q5RCJ1
AlphaFold Q5RCJ1 Q15642

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