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 34496

Title: Ca2+-bound Calmodulin mutant N53I   PubMed: 32317284

Deposition date: 2020-03-06 Original release date: 2020-04-27

Authors: Holt, C.; Nielsen, L.; Lau, K.; Brohus, M.; Sorensen, A.; Larsen, K.; Sommer, C.; Petegem, F.; Overgaard, M.; Wimmer, R.

Citation: Holt, C.; Hamborg, L.; Lau, K.; Brohus, M.; Sorensen, A.; Larsen, K.; Sommer, C.; Petegem, F.; Overgaard, M.; Wimmer, R.. "The arrhythmogenic N53I variant subtly changes the structure and dynamics in the calmodulin N-domain, altering its interaction with the cardiac ryanodine receptor"  J. Biol. Chem. ., .-. (2020).

Assembly members:
entity_1, polymer, 148 residues, 16720.404 Da.
entity_CA, non-polymer, 40.078 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
entity_1: ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMIIEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFDKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEE FVQMMTAK

Data sets:
Data typeCount
13C chemical shifts631
15N chemical shifts157
1H chemical shifts992
T1 relaxation values141
T2 relaxation values143
heteronuclear NOE values143

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22
3unit_32
4unit_42
5unit_52

Entities:

Entity 1, unit_1 148 residues - 16720.404 Da.

1   ALAASPGLNLEUTHRGLUGLUGLNILEALA
2   GLUPHELYSGLUALAPHESERLEUPHEASP
3   LYSASPGLYASPGLYTHRILETHRTHRLYS
4   GLULEUGLYTHRVALMETARGSERLEUGLY
5   GLNASNPROTHRGLUALAGLULEUGLNASP
6   METILEILEGLUVALASPALAASPGLYASN
7   GLYTHRILEASPPHEPROGLUPHELEUTHR
8   METMETALAARGLYSMETLYSASPTHRASP
9   SERGLUGLUGLUILEARGGLUALAPHEARG
10   VALPHEASPLYSASPGLYASNGLYTYRILE
11   SERALAALAGLULEUARGHISVALMETTHR
12   ASNLEUGLYGLULYSLEUTHRASPGLUGLU
13   VALASPGLUMETILEARGGLUALAASPILE
14   ASPGLYASPGLYGLNVALASNTYRGLUGLU
15   PHEVALGLNMETMETTHRALALYS

Entity 2, unit_2 - Ca - 40.078 Da.

1   CA

Samples:

sample_1: Calmodulin N53I, [U-99% 13C; U-99% 15N], 0.56 mM; HEPES 2 mM; potassium chloride 100 mM; calcium chloride 10 mM; sodium acetate 50 mM; sodium azide 2 mM; TSP 0.05 mM

sample_2: Calmodulin N53I, [U-99% 15N], 1.0 mM; HEPES 2 mM; potassium chloride 10 mM; calcium chloride 10 mM; sodium azide 2 mM; TSP 0.05 mM

sample_3: Calmodulin, [U-99% 13C; U-99% 15N], 1.0 mM; HEPES 2 mM; potassium chloride 10 mM; calcium chloride 10 mM; sodium azide 2 mM; TSP 0.05 mM

sample_conditions_1: ionic strength: 182 mM; pH: 6.57; pressure: 1 atm; temperature: 298.1 K

sample_conditions_2: ionic strength: 42 mM; pH: 6.57; pressure: 1 atm; temperature: 298.1 K

sample_conditions_3: ionic strength: 42 mM; pH: 6.57; pressure: 1 atm; temperature: 298.1 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
{1H}-15N NOEsample_2isotropicsample_conditions_2
15N-T2sample_2isotropicsample_conditions_2
15N-T1sample_2isotropicsample_conditions_2
T2 relaxation dispersionsample_2isotropicsample_conditions_2
15N-T1sample_3isotropicsample_conditions_3
15N-T2sample_3isotropicsample_conditions_3
{1H}-15N NOEsample_3isotropicsample_conditions_3
T2 relaxation dispersionsample_3isotropicsample_conditions_3
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

YASARA v14.12.2, YASARA Biosciences GmbH - refinement

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure calculation

TALOS vTALOS+, Cornilescu, Delaglio and Bax - structure calculation

CARA v1.8.4.2, Keller and Wuthrich - chemical shift assignment, peak picking

TopSpin v3.2, Bruker Biospin - processing

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III HD 900 MHz

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