Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53301

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

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Name: Titration of sMyBP-C LKR-Mutant M-domain with NaCl
Published: 2026-05-04

Title:

Titration of sMyBP-C LKR-Mutant M-domain with NaCl

Deposition date:

2025-08-02

Original release date:

2026-05-04

Authors:

Iyer, Aishwarya

Citation:

Citation: Iyer, Aishwarya; Wright, Nathan; Cook, Mary; Takagi, Yasuharu; Johnson, Bruce; Biancalana, Valerie; Massier, Marie; Spodenkiewicz, Marta; Poirsier, Celine; Vallecillo, Brice; Boyer, Francois; Pineau, Charlotte; Hensley, Lindsey; Sellers, James; Varney, Kristen; Weber, David; Kontrogianni-Konstantopoulos, Aikaterini. "Structural and biochemical alterations in the MYBPC1 M-domain underlie Myotrem pathogenicity" .

Assembly members:

Assembly members:
entity_1, polymer, 106 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: pET-11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MHHHHHHESTGTTPNIDIRS AFKRSGEGQEDAGELDFSGL LKRREVKQQEEEPQVDVWEL LKNAKPSEYEKIAFQYGITD LRGMLKRLKRLKRMRREEKK SAAFAK

Data sets:

assigned_chemical_shifts

Data type	Count
15N chemical shifts	480
1H chemical shifts	480

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	M-domain LKR-mutant	1

Entities:

Entity 1, M-domain LKR-mutant 106 residues - Formula weight is not available

1

MET

HIS

GLU

SER

THR

2

GLY

THR

PRO

ASN

ILE

ASP

ILE

ARG

SER

3

ALA

PHE

LYS

ARG

SER

GLY

GLU

GLY

GLN

GLU

4

ASP

ALA

GLY

GLU

LEU

ASP

PHE

SER

GLY

LEU

5

LEU

LYS

ARG

GLU

VAL

LYS

GLN

GLU

6

GLU

PRO

GLN

VAL

ASP

VAL

TRP

GLU

LEU

7

LEU

LYS

ASN

ALA

LYS

PRO

SER

GLU

TYR

GLU

8

LYS

ILE

ALA

PHE

GLN

TYR

GLY

ILE

THR

ASP

9

LEU

ARG

GLY

MET

LEU

LYS

ARG

LEU

LYS

ARG

10

LEU

LYS

ARG

MET

ARG

GLU

LYS

11

SER

ALA

PHE

ALA

LYS

Samples:

sample_1: M-domain LKR-mutant, [U-15N], 0.1 mM; HEPES 20 mM; NaCl 50 mM; TCEP 1 mM; EGTA 1 mM; NaN3 0.01%; D2O 10%

sample_2: M-domain LKR-mutant, [U-15N], 0.1 mM; HEPES 20 mM; NaCl 75 mM; TCEP 1 mM; EGTA 1 mM; NaN3 0.01%; D2O 10%

sample_3: M-domain LKR-mutant, [U-15N], 0.1 mM; HEPES 20 mM; NaCl 100 mM; TCEP 1 mM; EGTA 1 mM; NaN3 0.01%; D2O 10%

sample_4: M-domain LKR-mutant, [U-15N], 0.1 mM; HEPES 20 mM; NaCl 125 mM; TCEP 1 mM; EGTA 1 mM; NaN3 0.01%; D2O 10%

sample_5: M-domain LKR-mutant, [U-15N], 0.1 mM; HEPES 20 mM; NaCl 150 mM; TCEP 1 mM; EGTA 1 mM; NaN3 0.01%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.075 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

sample_conditions_3: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

sample_conditions_4: ionic strength: 0.125 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

sample_conditions_5: ionic strength: 0.150 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_3
2D 1H-15N HSQC	sample_4	isotropic	sample_conditions_4
2D 1H-15N HSQC	sample_5	isotropic	sample_conditions_5

Software:

NMRPipe - processing

CcpNMR - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 950 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 53301