BMRB Entry 18268

Title:
Unliganded (apo) C-terminal EF-hand domain from human polycystin-2
Deposition date:
2012-02-15
Original release date:
2012-05-08
Authors:
Petri, Edward; Celic, Andjelka; Ehrlich, Barbara; Boggon, Titus; Hodsdon, Michael
Citation:

Citation: Celic, Andjelka; Petri, Edward; Benbow, Jennifer; Hodsdon, Michael; Ehrlich, Barbara; Boggon, Titus. "Calcium-induced Conformational Changes in C-terminal Tail of Polycystin-2 Are Necessary for Channel Gating."  J. Biol. Chem. 287, 17232-17240 (2012).
PubMed: 22474326

Assembly members:

Assembly members:
EF-hand_domain_of_polycystin-2, polymer, 78 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Humans   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-28(a+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
EF-hand_domain_of_polycystin-2: NTVDDISESLRQGGGKLNFD ELRQDLKGKGHTDAEIEAIF TKYDQDGDQELTEHEHQQMR DDLEKEREDLDLDHSSLP

Data sets:
Data typeCount
13C chemical shifts145
15N chemical shifts72
1H chemical shifts163

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EF-hand_domain_of_polycystin-21

Entities:

Entity 1, EF-hand_domain_of_polycystin-2 78 residues - Formula weight is not available

1   ASNTHRVALASPASPILESERGLUSERLEU
2   ARGGLNGLYGLYGLYLYSLEUASNPHEASP
3   GLULEUARGGLNASPLEULYSGLYLYSGLY
4   HISTHRASPALAGLUILEGLUALAILEPHE
5   THRLYSTYRASPGLNASPGLYASPGLNGLU
6   LEUTHRGLUHISGLUHISGLNGLNMETARG
7   ASPASPLEUGLULYSGLUARGGLUASPLEU
8   ASPLEUASPHISSERSERLEUPRO

Samples:

sample_1: EF-hand_domain_of_polycystin-2, [U-100% 13C; U-100% 15N], 1.0 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0.15 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

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

VNMR v6.2c, Varian - collection

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 16191 16590 17621
PDB
DBJ BAG56956 BAG57494
EMBL CAG31243 CAI38797
GB AAC16004 AAC50520 AAC50933 AAI11455 AAI12262
REF NP_000288 NP_001026311 NP_001039777 NP_001232908 XP_001099242
SP Q13563 Q4GZT3
TPG DAA28806
AlphaFold Q13563 Q4GZT3

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