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 11322

Title: Solution structure of the SANT domain of human KIAA1915 protein   PubMed: 17428495

Deposition date: 2010-08-10 Original release date: 2010-12-01

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

Citation: Yoneyama, Misao; Tochio, Naoya; Umehara, Takashi; Koshiba, Seizo; Inoue, Makoto; Yabuki, Takashi; Aoki, Masaaki; Seki, Eiko; Matsuda, Takayoshi; Watanabe, Satoru; Tomo, Yasuko; Nishimura, Yuji; Harada, Takushi; Terada, Takaho; Shirouzu, Mikako; Hayashizaki, Yoshihide; Ohara, Osamu; Tanaka, Akiko; Kigawa, Takanori; Yokoyama, Shigeyuki. "Structural and functional differences of SWIRM domain subtypes."  J. Mol. Biol. 369, 222-238 (2007).

Assembly members:
SANT domain, polymer, 72 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: P041018-13

Entity Sequences (FASTA):
SANT domain: GSSGSSGYSVKWTIEEKELF EQGLAKFGRRWTKISKLIGS RTVLQVKSYARQYFKNKVKC GLDKETPNQKTG

Data sets:
Data typeCount
13C chemical shifts329
15N chemical shifts80
1H chemical shifts519

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SANT domain1

Entities:

Entity 1, SANT domain 72 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYTYRSERVAL
2   LYSTRPTHRILEGLUGLULYSGLULEUPHE
3   GLUGLNGLYLEUALALYSPHEGLYARGARG
4   TRPTHRLYSILESERLYSLEUILEGLYSER
5   ARGTHRVALLEUGLNVALLYSSERTYRALA
6   ARGGLNTYRPHELYSASNLYSVALLYSCYS
7   GLYLEUASPLYSGLUTHRPROASNGLNLYS
8   THRGLY

Samples:

sample_1: SANT domain, [U-13C; U-15N], 0.83 mM; Acetate buffer Na 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYsample_1isotropiccondition_1
3D 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 v0.9295, Kobayashi, N. - data analysis

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

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAB67808
GB AAI67849
REF NP_001078956 XP_003824269 XP_004025928 XP_006710377 XP_008976222
SP Q5VVJ2
AlphaFold Q5VVJ2

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