BMRB Entry 11286

Title:
Solution structure of the BSD domain of human Synapse associated protein 1
Deposition date:
2010-08-09
Original release date:
2011-08-18
Authors:
Yoneyama, M.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation:

Citation: Yoneyama, M.; Tochio, N.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of the BSD domain of human Synapse associated protein 1"  .

Assembly members:

Assembly members:
BSD domain, polymer, 100 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: P040531-07

Data sets:
Data typeCount
13C chemical shifts440
15N chemical shifts99
1H chemical shifts685

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BSD domain1

Entities:

Entity 1, BSD domain 100 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYTHRASNASP
2   GLUGLUTHRILEGLNGLNGLNILELEUALA
3   LEUSERALAASPLYSARGASNPHELEUARG
4   ASPPROPROALAGLYVALGLNPHEASNPHE
5   ASPPHEASPGLNMETTYRPROVALALALEU
6   VALMETLEUGLNGLUASPGLULEULEUSER
7   LYSMETARGPHEALALEUVALPROLYSLEU
8   VALLYSGLUGLUVALPHETRPARGASNTYR
9   PHETYRARGVALSERLEUILELYSGLNSER
10   ALAGLNLEUTHRSERGLYPROSERSERGLY

Samples:

sample_1: BSD domain, [U-13C; U-15N], 1.03 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 v2.6, Bruker - collection

NMRPipe v20031121, 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
DBJ BAB55087 BAD96576 BAG37229 BAG58299 BAG64741
EMBL CAH18697 CAH90135
GB AAH14657 AAK69273 AAK81893 ACE87132 AIC57513
REF NP_001125031 NP_116185 XP_001097183 XP_002762707 XP_003819572
SP Q96A49
AlphaFold Q96A49

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