BMRB Entry 10241

Title:
Solution structures of the SH3 domain of human rho guanine exchange factor (GEF) 16
Deposition date:
2008-10-24
Original release date:
2009-11-03
Authors:
Sato, M.; Saito, K.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Sato, M.; Saito, K.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structures of the SH3 domain of human rho guanine exchange factor (GEF) 16"  .

Assembly members:

Assembly members:
SH3 domain, polymer, 79 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   Vector: P040816-12

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts319
15N chemical shifts77
1H chemical shifts498

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   GLYSERSERGLYSERSERGLYTRPGLNGLY
2   LEUSERSERLYSGLYASPLEUPROGLNVAL
3   GLUILETHRLYSALAPHEPHEALALYSGLN
4   ALAASPGLUVALTHRLEUGLNGLNALAASP
5   VALVALLEUVALLEUGLNGLNGLUASPGLY
6   TRPLEUTYRGLYGLUARGLEUARGASPGLY
7   GLUTHRGLYTRPPHEPROGLUASPPHEALA
8   ARGPHEILESERGLYPROSERSERGLY

Samples:

sample_1: SH3 domain, [U-13C; U-15N], 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 13C-separated NOESYsample_1isotropiccondition_1
3D 15N-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20031121, Delaglio, F. - processing

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

Kujira v0.9295, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAA13745 BAG53186 BAG58889
GB AAH02681 AAH51838 AAP35934 AAP36764 AAX29017
REF NP_055263 XP_004024598 XP_008968944 XP_009234043 XP_009445318
SP Q5VV41
AlphaFold Q5VV41

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