BMRB Entry 15679

Name: 3D NMR structure of domain cC0 of cardiac myosin bonding protein C (MyBP-C)
Published: 2009-10-13

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PDB ID: 2k1m
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15679
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

3D NMR structure of domain cC0 of cardiac myosin bonding protein C (MyBP-C)

Deposition date:

2008-03-10

Original release date:

2009-10-13

Authors:

Ratti, Joyce; Gautel, Mathias; Pfuhl, Mark

Citation:

Citation: Ratti, Joyce; Rostkova, Elena; Gautel, Mathias; Pfuhl, Mark. "Structure and interactions of myosin-binding protein C domain C0: cardiac-specific regulation of myosin at its neck?" J. Biol. Chem. 286, 12650-12658 (2011).
PubMed: 21297165

Assembly members:

Assembly members:
cC0_MyBPC, polymer, 95 residues, 10045.401 Da.

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-8C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
cC0_MyBPC: PEPGKKPVSAFSKKPRSVEV AAGSPAVFEAETERAGVKVR WQRGGSDISASNKYGLATEG TRHTLTVREVGPADQGSYAV IAGSSKVKFDLKVIE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	281
15N chemical shifts	85
1H chemical shifts	601

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	cC0_MyBPC	1

Entities:

Entity 1, cC0_MyBPC 95 residues - 10045.401 Da.

1

PRO

GLU

PRO

GLY

LYS

PRO

VAL

SER

ALA

2

PHE

SER

LYS

PRO

ARG

SER

VAL

GLU

VAL

3

ALA

GLY

SER

PRO

ALA

VAL

PHE

GLU

ALA

4

GLU

THR

GLU

ARG

ALA

GLY

VAL

LYS

VAL

ARG

5

TRP

GLN

ARG

GLY

SER

ASP

ILE

SER

ALA

6

SER

ASN

LYS

TYR

GLY

LEU

ALA

THR

GLU

GLY

7

THR

ARG

HIS

THR

LEU

THR

VAL

ARG

GLU

VAL

8

GLY

PRO

ALA

ASP

GLN

GLY

SER

TYR

ALA

VAL

9

ILE

ALA

GLY

SER

LYS

VAL

LYS

PHE

ASP

10

LEU

LYS

VAL

ILE

GLU

Samples:

cC0_13C_15N: cC0_MyBPC, [U-95% 13C; U-95% 15N], 1-1.5 ± 0.2 mM; D2O, [U-2H], 55.5 M; sodium phosphate 40 mM; sodium chloride 50 mM; DTT 2 mM

cC0_15N: cC0_MyBPC, [U-95% 15N], 1-1.5 ± 0.2 mM; H2O 55.5 M; sodium phosphate 40 mM; sodium chloride 50 mM; DTT 2 mM

cC0: cC0_MyBPC 1-1.5 ± 0.2 mM; H2O 55.5 M; sodium phosphate 40 mM; sodium chloride 50 mM; DTT 2 mM

sample_conditions_1: ionic strength: 185 mM; pH: 7; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-13C NOESY	cC0_13C_15N	isotropic	sample_conditions_1
2D 1H-15N HSQC	cC0_15N	isotropic	sample_conditions_1
3D HNCACB	cC0_13C_15N	isotropic	sample_conditions_1
3D CBCA(CO)NH	cC0_13C_15N	isotropic	sample_conditions_1
3D HNCO	cC0_13C_15N	isotropic	sample_conditions_1
3D HN(CO)CA	cC0_13C_15N	isotropic	sample_conditions_1
2D 1H-1H NOESY	cC0	isotropic	sample_conditions_1
2D 1H-13C HSQC	cC0_13C_15N	isotropic	sample_conditions_1
3D HCCH-TOCSY	cC0_13C_15N	isotropic	sample_conditions_1
3D 1H-15N NOESY	cC0_15N	isotropic	sample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - dihedral angles

ANALYSIS v1.0 release 15, Wim F. Vranken, Wayne Boucher, Tim J. Stevens, Rasmus H. Fogh - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz

PDB	2K1M
GB	ACH92817