BMRB Entry 16910

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16910

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Title:
Assignment of HN,HA,HB,N,CA,CB and C' of the STAS domain of motor protein Prestin (Anion Transporter SLC26A5)
Deposition date:
2010-04-30
Original release date:
2011-05-02
Authors:
Bellanda, Massimo; Gesiot, Lorenzo
Citation:

Citation: Pasqualetto, Elisa; Aiello, Rosa; Gesiot, Lorenzo; Bonetto, Greta; Bellanda, Massimo; Battistutta, Roberto. "Structure of the cytosolic portion of motor protein prestin and functional role of the STAS domain in SLC26/SulP anion transporters."  J. Mol. Biol. 400, 448-462 (2010).
PubMed: 20471983

Assembly members:

Assembly members:
Prestin_STAS, polymer, 152 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Norway rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET SUMO (Invitrogen)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Prestin_STAS: SPSYTVLGQLPDTDVYIDID AYEEVKEIPGIKIFQINAPI YYANSDLYSSALKRKTGVNG SENIHTVILDFTQVNFMDSV GVKTLAGIVKEYGDVGIYVY LAGCSAQVVNDLTSNRFFEN PALKELLFHSIHDAVLGSQV REAMAEQETTVL

Data sets:
Data typeCount
13C chemical shifts372
15N chemical shifts121
1H chemical shifts453

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Prestin_STAS1

Entities:

Entity 1, Prestin_STAS 152 residues - Formula weight is not available

1   SERPROSERTYRTHRVALLEUGLYGLNLEU
2   PROASPTHRASPVALTYRILEASPILEASP
3   ALATYRGLUGLUVALLYSGLUILEPROGLY
4   ILELYSILEPHEGLNILEASNALAPROILE
5   TYRTYRALAASNSERASPLEUTYRSERSER
6   ALALEULYSARGLYSTHRGLYVALASNGLY
7   SERGLUASNILEHISTHRVALILELEUASP
8   PHETHRGLNVALASNPHEMETASPSERVAL
9   GLYVALLYSTHRLEUALAGLYILEVALLYS
10   GLUTYRGLYASPVALGLYILETYRVALTYR
11   LEUALAGLYCYSSERALAGLNVALVALASN
12   ASPLEUTHRSERASNARGPHEPHEGLUASN
13   PROALALEULYSGLULEULEUPHEHISSER
14   ILEHISASPALAVALLEUGLYSERGLNVAL
15   ARGGLUALAMETALAGLUGLNGLUTHRTHR
16   VALLEU

Samples:

sample_1: Prestin_STAS, [U-13C; U-15N], 1.2 mM; DTT 10 mM; EDTA 1 mM; potassium phosphate 30 mM; sodium chloride 50 mM; sodium azide 0.05 %w/v; DSS 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HA(CA)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

TOPSPIN, Bruker Biospin - processing

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

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 500 MHz

Related Database Links:

PDB

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