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 51607

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51607

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Title: Assignment of PCaP1   PubMed: 36608581

Deposition date: 2022-08-31 Original release date: 2023-02-08

Authors: Vallet, Alicia; Martin-Laffon, Jacqueline; Favier, Adrien; Revel, Benoit; Bonnot, Titouan; Vidaud, Claude; Armengaud, Jean; Gaillard, Jean-Charles; Delangle, Pascale; Devime, Fabienne; Figuet, Sylvie; Serre, Nelson; Boeri Erba, Elisabetta; Brutscher, Bernhard; Ravanel, Stephane; Bourguignon, Jacques; Alban, Claude

Citation: Vallet, Alicia; Martin-Laffon, Jacqueline; Favier, Adrien; Revel, Benoit; Bonnot, Titouan; Vidaud, Claude; Armengaud, Jean; Gaillard, Jean-Charles; Delangle, Pascale; Devime, Fabienne; Figuet, Sylvie; Serre, Nelson; Boeri Erba, Elisabetta; Brutscher, Bernhard; Ravanel, Stephane; Bourguignon, Jacques; Alban, Claude. "The plasma membrane-associated cation-binding protein PCaP1 of Arabidopsis thaliana is a uranyl-binding protein"  J. Hazard. Mater. 446, 130668-130668 (2023).

Assembly members:
entity_1, polymer, 225 residues, Formula weight is not available

Natural source:   Common Name: Thale cress   Taxonomy ID: 3702   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Arabidopsis thaliana

Experimental source:   Production method: purified from the natural source

Entity Sequences (FASTA):
entity_1: MGYWNSKVVPKFKKLFEKNS AKKAAAAEATKTFDESKETI NKEIEEKKTELQPKVVETYE ATSAEVKALVRDPKVAGLKK NSAAVQKYLEELVKIEFPGS KAVSEASSSFGAGYVAGPVT FIFEKVSVFLPEEVKTKEIP VEEVKAEEPAKTEEPAKTEG TSGEKEEIVEETKKGETPET AVVEEKKPEVEEKKEEATPA PAVVETPVKEPETTTTAPVA EPPKP

Data sets:
Data typeCount
13C chemical shifts336
15N chemical shifts120
1H chemical shifts120

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1PCaP11

Entities:

Entity 1, PCaP1 225 residues - Formula weight is not available

1   METGLYTYRTRPASNSERLYSVALVALPRO
2   LYSPHELYSLYSLEUPHEGLULYSASNSER
3   ALALYSLYSALAALAALAALAGLUALATHR
4   LYSTHRPHEASPGLUSERLYSGLUTHRILE
5   ASNLYSGLUILEGLUGLULYSLYSTHRGLU
6   LEUGLNPROLYSVALVALGLUTHRTYRGLU
7   ALATHRSERALAGLUVALLYSALALEUVAL
8   ARGASPPROLYSVALALAGLYLEULYSLYS
9   ASNSERALAALAVALGLNLYSTYRLEUGLU
10   GLULEUVALLYSILEGLUPHEPROGLYSER
11   LYSALAVALSERGLUALASERSERSERPHE
12   GLYALAGLYTYRVALALAGLYPROVALTHR
13   PHEILEPHEGLULYSVALSERVALPHELEU
14   PROGLUGLUVALLYSTHRLYSGLUILEPRO
15   VALGLUGLUVALLYSALAGLUGLUPROALA
16   LYSTHRGLUGLUPROALALYSTHRGLUGLY
17   THRSERGLYGLULYSGLUGLUILEVALGLU
18   GLUTHRLYSLYSGLYGLUTHRPROGLUTHR
19   ALAVALVALGLUGLULYSLYSPROGLUVAL
20   GLUGLULYSLYSGLUGLUALATHRPROALA
21   PROALAVALVALGLUTHRPROVALLYSGLU
22   PROGLUTHRTHRTHRTHRALAPROVALALA
23   GLUPROPROLYSPRO

Samples:

sample_1: PCaP1, [U-100% 13C; U-100% 15N], 200 uM

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection

CcpNMR vV3 - chemical shift assignment

SPARKY - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III HD 950 MHz

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