BMRB Entry 27017

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27017

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Title:
Backbone and sidechain chemical shift assignments of the complex of calmodulin bound to a beta calcineurin A peptide
Deposition date:
2017-01-27
Original release date:
2017-09-11
Authors:
Fowler, C.; Nunez Hernandez, Maria; Shea, Madeline
Citation:

Citation: Fowler, C.; Nunez Hernandez, Maria; O'Donnell, Susan; Yu, Liping; Shea, Madeline. "Backbone and side-chain resonance assignments of (Ca2+)4-calmodulin bound to beta calcineurin A CaMBD peptide"  Biomol. NMR Assign. 11, 275-280 (2017).
PubMed: 28815458

Assembly members:

Assembly members:
calmodulin, polymer, 148 residues, Formula weight is not available
beta_calcineurin_A_peptide, polymer, 34 residues, Formula weight is not available
entity_CA, non-polymer, 40.078 Da.

Natural source:

Natural source:   Common Name: Paramecium tetraurelia   Taxonomy ID: 5888   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Paramecium tetraurelia

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PT7-7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
calmodulin: AEQLTEEQIAEFKEAFALFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLSLMARKMKEQD SEEELIEAFKVFDRDGNGLI SAAELRHVMTNLGEKLTDDE VDEMIREADIDGDGHINYEE FVRMMVSK
beta_calcineurin_A_peptide: GPGSSAAARKEIIRNKIRAI GKMARVFSVLREES

Data typeCount
13C chemical shifts798
15N chemical shifts199
1H chemical shifts1231

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1calmodulin1
2beta calcineurin2
3calcium3

Entities:

Entity 1, calmodulin 148 residues - Formula weight is not available

1   ALAGLUGLNLEUTHRGLUGLUGLNILEALA
2   GLUPHELYSGLUALAPHEALALEUPHEASP
3   LYSASPGLYASPGLYTHRILETHRTHRLYS
4   GLULEUGLYTHRVALMETARGSERLEUGLY
5   GLNASNPROTHRGLUALAGLULEUGLNASP
6   METILEASNGLUVALASPALAASPGLYASN
7   GLYTHRILEASPPHEPROGLUPHELEUSER
8   LEUMETALAARGLYSMETLYSGLUGLNASP
9   SERGLUGLUGLULEUILEGLUALAPHELYS
10   VALPHEASPARGASPGLYASNGLYLEUILE
11   SERALAALAGLULEUARGHISVALMETTHR
12   ASNLEUGLYGLULYSLEUTHRASPASPGLU
13   VALASPGLUMETILEARGGLUALAASPILE
14   ASPGLYASPGLYHISILEASNTYRGLUGLU
15   PHEVALARGMETMETVALSERLYS

Entity 2, beta calcineurin 34 residues - Formula weight is not available

First four residues (GPGS, -4 to -1) are part of a 3C protease cleavage site; beta calcineurin residue S397 is residue 5 of the peptide.

1   GLYPROGLYSERSERALAALAALAARGLYS
2   GLUILEILEARGASNLYSILEARGALAILE
3   GLYLYSMETALAARGVALPHESERVALLEU
4   ARGGLUGLUSER

Entity 3, calcium - Ca - 40.078 Da.

1   CA

Samples:

sample_1: calmodulin, [U-99% 13C; U-99% 15N], 0.85 mM; beta calcineurin A peptide, [U-99% 13C; U-99% 15N], 0.85 mM; calcium 5 mM; potassium chloride 100 mM; imidazole, [U-99% 2H], 10 mM; sodium azide 0.01%

sample_2: calmodulin, [U-99% 13C; U-99% 15N], 0.85 mM; beta calcineurin A peptide, [U-99% 13C; U-99% 15N], 0.85 mM; calcium 5 mM; potassium chloride 100 mM; imidazole, [U-99% 2H], 10 mM; sodium azide 0.01%

sample_3: calmodulin, [U-99% 15N], 0.78 mM; beta calcineurin A peptide, [U-99% 15N], 0.78 mM; calcium 5 mM; potassium chloride 100 mM; imidazole, [U-99% 2H], 10 mM; sodium azide 0.01%

sample_4: calmodulin 0.9 mM; beta calcineurin A peptide 0.9 mM; calcium 5 mM; potassium chloride 100 mM; imidazole, [U-99% 2H], 10 mM; sodium azide 0.01%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
2D 1H-13C HMQCsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HCACOsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-13C CT-HSQC aromaticsample_2isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_2isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_2isotropicsample_conditions_1
2D 1H-1H gCOSYsample_4isotropicsample_conditions_1
2D 1H-1H TOCSYsample_4isotropicsample_conditions_1
2D 1H-1H NOESYsample_4isotropicsample_conditions_1

Software:

VNMRJ v2.1B, Varian - collection

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

Analysis, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

NCBI AAB20487.1 5532
UniProt P07463 P16298
AlphaFold A0DD49 Q8N3W4

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