Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53877

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Please specify the pdb ID.

Title:

1H and 15N resonance assignments of the calmodulin 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, 169 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 EFVQMMTAK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
15N chemical shifts	147
1H chemical shifts	147

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	calmodulin	1
2	calcium ions, 1	2
3	calcium ions, 2	2
4	calcium ions, 3	2
5	calcium ions, 4	2

Entities:

Entity 1, calmodulin 169 residues - Formula weight is not available

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

ALA

ASP

GLN

LEU

THR

GLU

GLN

ILE

4

ALA

GLU

PHE

LYS

GLU

ALA

PHE

SER

LEU

PHE

5

ASP

LYS

ASP

GLY

ASP

GLY

THR

ILE

THR

6

LYS

GLU

LEU

GLY

THR

VAL

MET

ARG

SER

LEU

7

GLY

GLN

ASN

PRO

THR

GLU

ALA

GLU

LEU

GLN

8

ASP

MET

ILE

ASN

GLU

VAL

ASP

ALA

ASP

GLY

9

ASN

GLY

THR

ILE

ASP

PHE

PRO

GLU

PHE

LEU

10

THR

MET

ALA

ARG

LYS

MET

LYS

ASP

THR

11

ASP

SER

GLU

ILE

ARG

GLU

ALA

PHE

12

ARG

VAL

PHE

ASP

LYS

ASP

GLY

ASN

GLY

TYR

13

ILE

SER

ALA

GLU

LEU

ARG

HIS

VAL

MET

14

THR

ASN

LEU

GLY

GLU

LYS

LEU

THR

ASP

GLU

15

GLU

VAL

ASP

GLU

MET

ILE

ARG

GLU

ALA

ASP

16

ILE

ASP

GLY

ASP

GLY

GLN

VAL

ASN

TYR

GLU

17

GLU

PHE

VAL

GLN

MET

THR

ALA

LYS

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_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

BMRB Entry 53877