BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 26553

Title: Solution Structure of the Smarc Domain

Deposition date: 2015-04-10 Original release date: 2015-08-03

Authors: Allen, Mark; Freund, S.; Bycroft, M.

Citation: Allen, Mark; Freund, S.; Bycroft, M.. "Solution Structure of the Smarc Domain"  To Be Published ., .-..

Assembly members:
SWI-SNF-RELATED_MATRIX-ASSOCIATED_ACTIN-DEPENDENT_OF_CHROMATIN_SUBFAMILY_B_M, polymer, 115 residues, 12981.9001 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
SWI-SNF-RELATED_MATRIX-ASSOCIATED_ACTIN-DEPENDENT_OF_CHROMATIN_SUBFAMILY_B_M: GGSMMMALSKTFGQKPVKFQ LEDDGEFYMIGSEVGNYLRM FRGSLYKRYPSLWRRLATVE ERKKIVASSHGKKTKPNTKD HGYTTLATSVTLLKASEVEE ILDGNDEKYKAVSIS

Data sets:
Data typeCount
13C chemical shifts333
15N chemical shifts110
1H chemical shifts828

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SWI/SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT OF CHROMATIN SUBFAMILY B M1

Entities:

Entity 1, SWI/SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT OF CHROMATIN SUBFAMILY B M 115 residues - 12981.9001 Da.

1   GLYGLYSERMETMETMETALALEUSERLYS
2   THRPHEGLYGLNLYSPROVALLYSPHEGLN
3   LEUGLUASPASPGLYGLUPHETYRMETILE
4   GLYSERGLUVALGLYASNTYRLEUARGMET
5   PHEARGGLYSERLEUTYRLYSARGTYRPRO
6   SERLEUTRPARGARGLEUALATHRVALGLU
7   GLUARGLYSLYSILEVALALASERSERHIS
8   GLYLYSLYSTHRLYSPROASNTHRLYSASP
9   HISGLYTYRTHRTHRLEUALATHRSERVAL
10   THRLEULEULYSALASERGLUVALGLUGLU
11   ILELEUASPGLYASNASPGLULYSTYRLYS
12   ALAVALSERILESER

Samples:

sample_1: SWI/SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT OF CHROMATIN SUBFAMILY B M, [U-13C; U-15N], 1.5 mM; potassium phosphate 20 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 100.000 mM; pH: 6.500; pressure: 1.000 atm; temperature: 293.000 K

Experiments:

NameSampleSample stateSample conditions
NOESYsample_1solutionsample_conditions_1
TOCSYsample_1solutionsample_conditions_1
DQF-COSYsample_1solutionsample_conditions_1
HSQCsample_1solutionsample_conditions_1
HNCACBsample_1solutionsample_conditions_1
CBCACONHsample_1solutionsample_conditions_1
HNCOsample_1solutionsample_conditions_1
HNCACOsample_1solutionsample_conditions_1
HNHBsample_1solutionsample_conditions_1

Software:

Ansig vany, Kraulis - chemical shift assignment

AutoDep v4.3, PDBe - chemical shift assignment

CNS vany, Brunger, Adams, Clore, Gros, Nilges and Read - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

UNP SNF5_HUMAN
PDB
DBJ BAA95062 BAB12427 BAC36045 BAE90809 BAG61393
EMBL CAA09758 CAA09760 CAA09761 CAA76639 CAG30467
GB AAA81905 AAB34227 AAH25163 AAI33573 AAO59167
REF NP_001035647 NP_001270057 NP_003064 NP_035548 XP_001169712
SP Q12824 Q5BIN2 Q9Z0H3
TPG DAA20401

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