BMRB Entry 27595

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27595

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Title:
Sequential backbone resonance assignment of AT-rich interaction domain of BAF200
Deposition date:
2018-09-03
Original release date:
2018-12-12
Authors:
Bastiray, Abhishek; Giri, Malyasree; Singh, Mahavir
Citation:

Citation: Bastiray, Abhishek; Giri, Malyasree; Singh, Mahavir. "Sequential backbone resonance assignment of AT-rich interaction domain of human BAF200"  Biomol. NMR Assignments 13, 115-119 (2019).
PubMed: 30535613

Assembly members:

Assembly members:
BAF200_ARID, polymer, 115 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: recombinant technology   Host organism: Escherichia coli   Vector: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BAF200_ARID: MANSTGKAPPDERRKGLAFL DELRQFHHSRGSPFKKIPAV GGKELDLHGLYTRVTTLGGF AKVSEKNQWGEIVEEFNFPR SCSNAAFALKQYYLRYLEKY EKVHHFGLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts417
15N chemical shifts102
1H chemical shifts632

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ARID monomer1

Entities:

Entity 1, ARID monomer 115 residues - Formula weight is not available

Residues 107-115 represent a non-native residues L, E and six H of affinity tag. This is the ARID domain of BAF200

1   METALAASNSERTHRGLYLYSALAPROPRO
2   ASPGLUARGARGLYSGLYLEUALAPHELEU
3   ASPGLULEUARGGLNPHEHISHISSERARG
4   GLYSERPROPHELYSLYSILEPROALAVAL
5   GLYGLYLYSGLULEUASPLEUHISGLYLEU
6   TYRTHRARGVALTHRTHRLEUGLYGLYPHE
7   ALALYSVALSERGLULYSASNGLNTRPGLY
8   GLUILEVALGLUGLUPHEASNPHEPROARG
9   SERCYSSERASNALAALAPHEALALEULYS
10   GLNTYRTYRLEUARGTYRLEUGLULYSTYR
11   GLULYSVALHISHISPHEGLYLEUGLUHIS
12   HISHISHISHISHIS

Samples:

sample_1: BAF200 ARID, [U-99% 15N], 0.5 ± 0.1 mM; D2O, [U-2H], 10 ± 0.1 %; sodium phosphate 50 ± 0.1 mM; sodium chloride 50 ± 0.1 mM; DTT 2 ± 0.1 mM; H2O 90 ± 0.1 %

sample_2: BAF200 ARID, [U-99% 13C; U-99% 15N], 0.6 ± 0.1 mM; D2O, [U-2H], 10 ± 0.1 %; sodium phosphate 50 ± 0.1 mM; sodium chloride 50 ± 0.1 mM; DTT 2 ± 0.1 mM; H2O 90 ± 0.1 %

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HCACOsample_2isotropicsample_conditions_1

Software:

VNMRJ, Varian - collection, data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, chemical shift calculation, data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - data analysis, dihedral angles

NMR spectrometers:

  • Agilent DRX 600 MHz

Related Database Links:

UNP Q68CP9
AlphaFold Q9HCL5

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