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 11454

Title: NMR Chemical Shift Assignments for QB domain of Sp1   PubMed: 22855260

Deposition date: 2011-09-26 Original release date: 2012-12-06

Authors: Hiramatsu, Naoko; Hibino, Emi; Matsuzaki, Katsumi; Kuwahara, Jun; Hoshino, Masaru

Citation: Hiramatsu, Naoko; Hibino, Emi; Matsuzaki, Katsumi; Kuwahara, Jun; Hoshino, Masaru. "Interaction between isolated transcriptional activation domains of Sp1 revealed by heteronuclear magnetic resonance"  Protein Sci. 21, 1481-1488 (2012).

Assembly members:
QB domain of Sp1, polymer, 172 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: recombinant technology   Host organism: Escherichia coli   Vector: pGEX1

Entity Sequences (FASTA):
QB domain of Sp1: GILTNSQGQTPQRVSGLQGS DALNIQQNQTSGGSLQAGQQ KEGEQNQQTQQQQILIQPQL VQGGQALQALQAAPLSGQTF TTQAISQETLQNLQLQAVPN SGPIIIRTPTVGPNGQVSWQ TLQLQNLQVQNPQAQTITLA PMQGVSLGQTPGGTLEDYKD DDDKGSHHHHHH

Data sets:
Data typeCount
13C chemical shifts304
15N chemical shifts143
1H chemical shifts143

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1QB domain of Sp11

Entities:

Entity 1, QB domain of Sp1 172 residues - Formula weight is not available

1   GLYILELEUTHRASNSERGLNGLYGLNTHR
2   PROGLNARGVALSERGLYLEUGLNGLYSER
3   ASPALALEUASNILEGLNGLNASNGLNTHR
4   SERGLYGLYSERLEUGLNALAGLYGLNGLN
5   LYSGLUGLYGLUGLNASNGLNGLNTHRGLN
6   GLNGLNGLNILELEUILEGLNPROGLNLEU
7   VALGLNGLYGLYGLNALALEUGLNALALEU
8   GLNALAALAPROLEUSERGLYGLNTHRPHE
9   THRTHRGLNALAILESERGLNGLUTHRLEU
10   GLNASNLEUGLNLEUGLNALAVALPROASN
11   SERGLYPROILEILEILEARGTHRPROTHR
12   VALGLYPROASNGLYGLNVALSERTRPGLN
13   THRLEUGLNLEUGLNASNLEUGLNVALGLN
14   ASNPROGLNALAGLNTHRILETHRLEUALA
15   PROMETGLNGLYVALSERLEUGLYGLNTHR
16   PROGLYGLYTHRLEUGLUASPTYRLYSASP
17   ASPASPASPLYSGLYSERHISHISHISHIS
18   HISHIS

Samples:

sample_1: QB domain of Sp1, [U-99% 15N], 50 – 550 uM; H2O 90%; D2O 10%; NaCl 140 mM; Na-Phosphate 20 mM

sample_2: QB domain of Sp1, [U-99% 13C; U-99% 15N], 500 uM; H2O 90%; D2O 10%; NaCl 140 mM; Na-Phosphate 20 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.3; pressure: 1 atm; temperature: 277 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D hNcocaNHsample_2isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Zhengrong and Bax - processing

NMRDraw, Delaglio, Zhengrong and Bax - data analysis

PIPP, Garrett - peak picking

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

DBJ BAB13476 BAD92915 BAI46444
EMBL CBM42955
GB AAA61154 AAF67726 AAH43224 AAH62539 ADL59934
REF NP_001238754 NP_001253853 NP_001272689 NP_003100 NP_612482
SP P08047
AlphaFold P08047

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