BMRB Entry 53875

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53875

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Title:
1H, 15N, and 13C resonance assignments of the calmodulin-LL-37 fusion protein in the Ca2+-bound state
Deposition date:
2026-06-17
Original release date:
2026-09-18
Authors:
Shibagaki, Mitsuki; Kumeta, Hiroyuki; Aizawa, Tomoyasu
Citation:

Citation: Shibagaki, Mitsuki; Chrisnanto, Jeremia; Tefera, Dessalegn; Kumeta, Hiroyuki; Maeda, Kosuke; Tsukioka, Kotaro; Ueda, Waka; Hirai, Fumi; Kumaki, Yasuhiro; Tsuda, Sakae; Arai, Tatsuya; Aizawa, Tomoyasu. "Calmodulin-tagging prevents aggregation and facilitates the proteolytic release of the recombinant human cathelicidin LL-37 by accommodating its hydrophobic regions "  Int. J. Biol. Macromol. 382, 154370-154370 (2026).
PubMed: 42727664

Assembly members:

Assembly members:
entity_1, polymer, 214 residues, Formula weight is not available
entity_CA, non-polymer, 40.078 Da.

Natural source:

Natural source:   Common Name: chicken   Taxonomy ID: 9031   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Gallus gallus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MADQLTEEQIAEFKEAFSLF DKDGDGTITTKELGTVMRSL GQNPTEAELQDMINEVDADG NGTIDFPEFLTMMARKMKDT DSEEEIREAFRVFDKDGNGY ISAAELRHVMTNLGEKLTDE EVDEMIREADIDGDGQVNYE EFVQMMTAKGGTDDDDKLLG DFFRKSKEKIGKEFKRIVQR IKDFLRNLVPRTES

Data sets:
Data typeCount
13C chemical shifts389
15N chemical shifts161
1H chemical shifts214

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1calmodulin-LL-37 fusion protein1
2calcium ions, 12
3calcium ions, 22
4calcium ions, 32
5calcium ions, 42

Entities:

Entity 1, calmodulin-LL-37 fusion protein 214 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METALAASPGLNLEUTHRGLUGLUGLNILE
4   ALAGLUPHELYSGLUALAPHESERLEUPHE
5   ASPLYSASPGLYASPGLYTHRILETHRTHR
6   LYSGLULEUGLYTHRVALMETARGSERLEU
7   GLYGLNASNPROTHRGLUALAGLULEUGLN
8   ASPMETILEASNGLUVALASPALAASPGLY
9   ASNGLYTHRILEASPPHEPROGLUPHELEU
10   THRMETMETALAARGLYSMETLYSASPTHR
11   ASPSERGLUGLUGLUILEARGGLUALAPHE
12   ARGVALPHEASPLYSASPGLYASNGLYTYR
13   ILESERALAALAGLULEUARGHISVALMET
14   THRASNLEUGLYGLULYSLEUTHRASPGLU
15   GLUVALASPGLUMETILEARGGLUALAASP
16   ILEASPGLYASPGLYGLNVALASNTYRGLU
17   GLUPHEVALGLNMETMETTHRALALYSGLY
18   GLYTHRASPASPASPASPLYSLEULEUGLY
19   ASPPHEPHEARGLYSSERLYSGLULYSILE
20   GLYLYSGLUPHELYSARGILEVALGLNARG
21   ILELYSASPPHELEUARGASNLEUVALPRO
22   ARGTHRGLUSER

Entity 2, calcium ions, 1 - Ca - 40.078 Da.

1   CA

Samples:

sample_1: calmodulin-LL-37 fusion protein, [U-99% 13C; U-99% 15N], 0.1 mM; D2O, [U-99% 2H], 5%; HEPES 50 mM; calcium chloride 3 mM; sodium azide 0.05%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v4.1.4 - collection, processing

NMRFAM-SPARKY v1.470 - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz

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