BMRB Entry 27996

Title:
Chemical shift assignments of calcineurin catalytic subunit A residues 27-348 in complex with RCAN1 128-164
Deposition date:
2019-08-09
Original release date:
2020-07-09
Authors:
Peti, Wolfgang; Li, Yang; Page, Rebecca
Citation:

Citation: Li, Yang; Sheftic, Sarah; Grigoriu, Simina; Schwieters, Charles; Page, Rebecca; Peti, Wolfgang. "The structure of the RCAN1:CN complex explains the inhibition of and substrate recruitment by calcineurin"  Sci. Adv. 6, 3681-3681 (2020).
PubMed: 32936779

Assembly members:

Assembly members:
Calcineurin catalytic subunit A residues 27-348, polymer, 327 residues, Formula weight is not available
RCAN1 residues 128-164, polymer, 40 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: RP1B

Data sets:
Data typeCount
13C chemical shifts206
15N chemical shifts111
1H chemical shifts111

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Calcineurin1
2RCAN12

Entities:

Entity 1, Calcineurin 327 residues - Formula weight is not available

GHM are cloning artifact; calcineurin sequence starts with HRLT; the C-terminal DD are introduced to increase solubility.

1   GLYHISMETHISARGLEUTHRALALYSGLU
2   VALPHEASPASNASPGLYLYSPROARGVAL
3   ASPILELEULYSALAHISLEUMETLYSGLU
4   GLYARGLEUGLUGLUSERVALALALEUARG
5   ILEILETHRGLUGLYALASERILELEUARG
6   GLNGLULYSASNLEULEUASPILEASPALA
7   PROVALTHRVALCYSGLYASPILEHISGLY
8   GLNPHEPHEASPLEUMETLYSLEUPHEGLU
9   VALGLYGLYSERPROALAASNTHRARGTYR
10   LEUPHELEUGLYASPTYRVALASPARGGLY
11   TYRPHESERILEGLUCYSVALLEUTYRLEU
12   TRPALALEULYSILELEUTYRPROLYSTHR
13   LEUPHELEULEUARGGLYASNHISGLUCYS
14   ARGHISLEUTHRGLUTYRPHETHRPHELYS
15   GLNGLUCYSLYSILELYSTYRSERGLUARG
16   VALTYRASPALACYSMETASPALAPHEASP
17   CYSLEUPROLEUALAALALEUMETASNGLN
18   GLNPHELEUCYSVALHISGLYGLYLEUSER
19   PROGLUILEASNTHRLEUASPASPILEARG
20   LYSLEUASPARGPHELYSGLUPROPROALA
21   TYRGLYPROMETCYSASPILELEUTRPSER
22   ASPPROLEUGLUASPPHEGLYASNGLULYS
23   THRGLNGLUHISPHETHRHISASNTHRVAL
24   ARGGLYCYSSERTYRPHETYRSERTYRPRO
25   ALAVALCYSGLUPHELEUGLNHISASNASN
26   LEULEUSERILELEUARGALAHISGLUALA
27   GLNASPALAGLYTYRARGMETTYRARGLYS
28   SERGLNTHRTHRGLYPHEPROSERLEUILE
29   THRILEPHESERALAPROASNTYRLEUASP
30   VALTYRASNASNLYSALAALAVALLEULYS
31   TYRGLUASNASNVALMETASNILEARGGLN
32   PHEASNCYSSERPROHISPROTYRTRPLEU
33   PROASNPHEMETASPASPASP

Entity 2, RCAN1 40 residues - Formula weight is not available

GHM are cloning artifact; RCAN1 sequence starts with NYDL

1   GLYHISMETASNTYRASPLEULEUTYRALA
2   ILESERLYSLEUGLYPROGLYGLULYSTYR
3   GLULEUHISALAALATHRASPTHRTHRPRO
4   SERVALVALILETHRVALCYSGLUSERASP

Samples:

sample_1: Calcineurin catalytic subunit A residues 27-348, [U-13C; U-15N; U-2H], 0.13 mM; RCAN1 residues 128-164 0.65 mM; sodium phosphate 20 mM; sodium chloride 50 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 850 MHz

Related Database Links:

UNP Q08209 P53805-2 P53805-2
AlphaFold Q8TAW9 Q9UME4 Q9UME4

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