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 17839

Title: Ga98 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:
Ga98, polymer, 56 residues, 6355.419 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   Vector: PPAL8

Entity Sequences (FASTA):
Ga98: TTYKLILNLKQAKEEAIKEL VDAGTAEKYFKLIANAKTVE GVWTLKDEIKTFTVTE

Data sets:
Data typeCount
13C chemical shifts213
15N chemical shifts56
1H chemical shifts334

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ga981

Entities:

Entity 1, Ga98 56 residues - 6355.419 Da.

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

Samples:

sample_1: Ga98, [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 vcns_solve 1.21, Brunger A. T. et.al. - refinement, structure solution

SPARKY, Goddard et al - data analysis

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

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

CSI v2.0, David Wishart, Brian Sykes - secondary structure prediction

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

Molmol, Koradi, Billeter and Wuthrich - structure display

TOPSPIN v2.0, Bruker Biospin - data collection

NOEID v1.20, Lisa Parsons - make noesy peak lists and CNS input tables

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

BMRB 16116 17840
PDB

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