BMRB Entry 19980

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19980

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Title:
NMR resonance assignments of the catalytic domain of human serine/threonine phosphatase calcineurin in unligated state
Deposition date:
2014-05-20
Original release date:
2014-10-09
Authors:
Takeuchi, Koh; Sun, Zhen-Yu; Gal, Maayan; Li, Shuai; Wagner, Gerhard
Citation:

Citation: Takeuchi, Koh; Sun, Zhen-Yu; Li, Shuai; Gal, Maayan; Wagner, Gerhard. "NMR resonance assignments of the catalytic domain of human serine/threonine phosphatase calcineurin in unligated and PVIVIT-peptide-bound states"  Biomol. NMR Assignments ., .-. (2014).
PubMed: 25209144

Assembly members:

Assembly members:
CnA, polymer, 350 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: pGEX-6P

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CnA: GPLGSEPKAIDPKLSTTDRV VKAVPFPPSHRLTAKEVFDN DGKPRVDILKAHLMKEGRLE ESVALRIITEGASILRQEKN LLDIDAPVTVCGDIHGQFFD LMKLFEVGGSPANTRYLFLG DYVDRGYFSIECVLYLWALK ILYPKTLFLLRGNHECRHLT EYFTFKQECKIKYSERVYDA CMDAFDCLPLAALMNQQFLC VHGGLSPEINTLDDIRKLDR FKEPPAYGPMCDILWSDPLE DFGNEKTQEHFTHNTVRGCS YFYSYPAVCEFLQHNNLLSI LRAHEAQDAGYRMYRKSQTT GFPSLITIFSAPNYLDVYNN KAAVLKYENNVMNIRQFNCS PHPSWAPNFD

Data sets:
Data typeCount
15N chemical shifts124
1H chemical shifts124

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CnA1

Entities:

Entity 1, CnA 350 residues - Formula weight is not available

CnA, comprising residues 2-347 with substitutions Y341S, L343A, and M347D. The protein was produced as a cleavable GST fusion protein. Cleavage of the fusion protein with PreScission protease produces CnA (2-347) with an additional GPLG sequence at its N-terminus.

1   GLYPROLEUGLYSERGLUPROLYSALAILE
2   ASPPROLYSLEUSERTHRTHRASPARGVAL
3   VALLYSALAVALPROPHEPROPROSERHIS
4   ARGLEUTHRALALYSGLUVALPHEASPASN
5   ASPGLYLYSPROARGVALASPILELEULYS
6   ALAHISLEUMETLYSGLUGLYARGLEUGLU
7   GLUSERVALALALEUARGILEILETHRGLU
8   GLYALASERILELEUARGGLNGLULYSASN
9   LEULEUASPILEASPALAPROVALTHRVAL
10   CYSGLYASPILEHISGLYGLNPHEPHEASP
11   LEUMETLYSLEUPHEGLUVALGLYGLYSER
12   PROALAASNTHRARGTYRLEUPHELEUGLY
13   ASPTYRVALASPARGGLYTYRPHESERILE
14   GLUCYSVALLEUTYRLEUTRPALALEULYS
15   ILELEUTYRPROLYSTHRLEUPHELEULEU
16   ARGGLYASNHISGLUCYSARGHISLEUTHR
17   GLUTYRPHETHRPHELYSGLNGLUCYSLYS
18   ILELYSTYRSERGLUARGVALTYRASPALA
19   CYSMETASPALAPHEASPCYSLEUPROLEU
20   ALAALALEUMETASNGLNGLNPHELEUCYS
21   VALHISGLYGLYLEUSERPROGLUILEASN
22   THRLEUASPASPILEARGLYSLEUASPARG
23   PHELYSGLUPROPROALATYRGLYPROMET
24   CYSASPILELEUTRPSERASPPROLEUGLU
25   ASPPHEGLYASNGLULYSTHRGLNGLUHIS
26   PHETHRHISASNTHRVALARGGLYCYSSER
27   TYRPHETYRSERTYRPROALAVALCYSGLU
28   PHELEUGLNHISASNASNLEULEUSERILE
29   LEUARGALAHISGLUALAGLNASPALAGLY
30   TYRARGMETTYRARGLYSSERGLNTHRTHR
31   GLYPHEPROSERLEUILETHRILEPHESER
32   ALAPROASNTYRLEUASPVALTYRASNASN
33   LYSALAALAVALLEULYSTYRGLUASNASN
34   VALMETASNILEARGGLNPHEASNCYSSER
35   PROHISPROSERTRPALAPROASNPHEASP

Samples:

sample_1: CnA, [U-13C; U-15N; U-2H], 0.4 mM; sodium phosphate 10 mM; sodium chloride 150 mM; DTT 2 mM; H2O 90%; D2O 10%

sample_2: CnA, [U-15N; U-2H; 1H14N-Arg], 0.4 mM; sodium phosphate 10 mM; sodium chloride 150 mM; DTT 2 mM; H2O 90%; D2O 10%

sample_3: CnA, [U-15N; U-2H; 1H14N-Lys], 0.4 mM; sodium phosphate 10 mM; sodium chloride 150 mM; DTT 2 mM; H2O 90%; D2O 10%

sample_4: CnA, [U-15N; U-2H; 1-13C-Leu], 0.4 mM; sodium phosphate 10 mM; sodium chloride 150 mM; DTT 2 mM; H2O 90%; D2O 10%

sample_5: CnA, [U-15N; U-2H; 1-13C-Val], 0.4 mM; sodium phosphate 10 mM; sodium chloride 150 mM; DTT 2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.18 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCOsample_4isotropicsample_conditions_1
3D HNCOsample_5isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D TROSY-hNcaNHsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker UnityPlus 750 MHz

Related Database Links:

BMRB 19981
PDB
DBJ BAA14083 BAE27131 BAE29521 BAF83221 BAG11443
EMBL CAA40398 CAB89253 CAH91746 CAL38363 CAL38589
GB AAA02631 AAA37359 AAA40940 AAC48473 AAH25714
PRF 1714202A
REF NP_000935 NP_001076161 NP_001124163 NP_001124164 NP_001127457
SP P48452 P63328 P63329 Q08209
TPG DAA28842
AlphaFold P48452 P63328 P63329 Q08209

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