BMRB Entry 11154

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11154
MolProbity Validation Chart

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Title:
Solution structure of the SH3 domain of Sorbin and SH3 domain-containing protein 1
Deposition date:
2010-04-15
Original release date:
2011-05-05
Authors:
Abe, H.; Miyamoto, K.; Tochio, N.; Saito, K.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Abe, H.; Miyamoto, K.; Tochio, N.; Saito, K.; Kigawa, T.; Yokoyama, S.. "Solution structure of the SH3 domain of Sorbin and SH3 domain-containing protein 1"  .

Assembly members:

Assembly members:
SH3 domain, polymer, 70 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: cell free synthesis   Host organism: E. coli - cell free   Vector: P050613-24

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SH3 domain: GSSGSSGGEAIAKFNFNGDT QVEMSFRKGERITLLRQVDE NWYEGRIPGTSRQGIFPITY VDVISGPSSG

Data sets:
Data typeCount
13C chemical shifts277
15N chemical shifts64
1H chemical shifts432

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1SH3 domain1

Entities:

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

1   GLYSERSERGLYSERSERGLYGLYGLUALA
2   ILEALALYSPHEASNPHEASNGLYASPTHR
3   GLNVALGLUMETSERPHEARGLYSGLYGLU
4   ARGILETHRLEULEUARGGLNVALASPGLU
5   ASNTRPTYRGLUGLYARGILEPROGLYTHR
6   SERARGGLNGLYILEPHEPROILETHRTYR
7   VALASPVALILESERGLYPROSERSERGLY

Samples:

sample_1: SH3 domain, [U-13C; U-15N], 0.75 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

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