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 17840

Title: GB98 solution structure   PubMed: 22325777

Deposition date: 2011-08-08 Original release date: 2012-02-28

Authors: He, Yanan; Chen, Yihong; Alexander, Patrick; Bryan, Philip; Orban, John

Citation: He, Yanan; Chen, Yihong; Alexander, Patrick; Bryan, Philip; Orban, John. "Mutational tipping points for switching protein folds and functions"  Structure 20, 283-291 (2012).

Assembly members:
GB98, polymer, 56 residues, 6405.436 Da.

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

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

Entity Sequences (FASTA):
GB98: TTYKLILNLKQAKEEAIKEL VDAGTAEKYFKLIANAKTVE GVWTYKDEIKTFTVTE

Data sets:
Data typeCount
13C chemical shifts213
15N chemical shifts56
1H chemical shifts346

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GB981

Entities:

Entity 1, GB98 56 residues - 6405.436 Da.

1   THRTHRTYRLYSLEUILELEUASNLEULYS
2   GLNALALYSGLUGLUALAILELYSGLULEU
3   VALASPALAGLYTHRALAGLULYSTYRPHE
4   LYSLEUILEALAASNALALYSTHRVALGLU
5   GLYVALTRPTHRTYRLYSASPGLUILELYS
6   THRPHETHRVALTHRGLU

Samples:

sample_1: GB98, [U-100% 13C; U-100% 15N], 0.1 – 0.3 mM; potassium phosphate 100 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - structure determination

TOPSPIN, Bruker Biospin - collection

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

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data processing display

SPARKY, Goddard - data analysis

Molmol, Koradi, Billeter and Wuthrich - structure display

CSI, Wishart, D.S. and B.D. Sykes. - secondary structure prediction

TALOS, Cornilescu, Delaglio and Bax - dihedral angle restraints determination

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - protein structure quality check

NOEID, Lisa Parsons - generate noe peak lists

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

BMRB 16117 17839 17843
PDB

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