BMRB Entry 25196

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25196

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Title:
haloSRC assignment
Deposition date:
2014-09-02
Original release date:
2014-10-02
Authors:
Ortega, Gabriel; Millet, Oscar
Citation:

Citation: Ortega, Gabriel; Diercks, Tammo; Millet, Oscar. "Halophilic Protein Adaptation Results from Synergistic Residue-Ion Interactions in the Folded and Unfolded States"  Chem. Biol. 22, 1597-1607 (2015).
PubMed: 26628359

Assembly members:

Assembly members:
haloSRC, polymer, 95 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: pET16b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
haloSRC: MASNDSKPSDASQRRRSLET AENVHGAGGGATPASQTPSE PASADGHDGPSAAFAPAAAE PDLFGGFNSSDTVTSPQRAG PEAGGSAWSHPQFEK

Data sets:
Data typeCount
13C chemical shifts217
15N chemical shifts81
1H chemical shifts81

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1haloSRC1

Entities:

Entity 1, haloSRC 95 residues - Formula weight is not available

1   METALASERASNASPSERLYSPROSERASP
2   ALASERGLNARGARGARGSERLEUGLUTHR
3   ALAGLUASNVALHISGLYALAGLYGLYGLY
4   ALATHRPROALASERGLNTHRPROSERGLU
5   PROALASERALAASPGLYHISASPGLYPRO
6   SERALAALAPHEALAPROALAALAALAGLU
7   PROASPLEUPHEGLYGLYPHEASNSERSER
8   ASPTHRVALTHRSERPROGLNARGALAGLY
9   PROGLUALAGLYGLYSERALATRPSERHIS
10   PROGLNPHEGLULYS

Samples:

sample_1: haloSRC, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM; sodium phosphate 20 ± 1 mM; PMSF 1 ± 0.1 mM; sodium azide 1 ± 0.1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 mM; pH: 7.5; pressure: 1 atm; temperature: 280 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, peak picking

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz

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