BMRB Entry 25007

Name: STRUCTURAL CHARACTERIZATION OF THE C3 DOMAIN OF CARDIAC MYOSIN BINDING PROTEIN-C
Published: 2014-07-28

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PDB ID: 2mq0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25007
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

STRUCTURAL CHARACTERIZATION OF THE C3 DOMAIN OF CARDIAC MYOSIN BINDING PROTEIN-C

Deposition date:

2014-06-10

Original release date:

2014-07-28

Authors:

Zhang, Xiaolu Linda; De, Soumya; McIntosh, Lawrence; Paetzel, Mark

Citation:

Citation: Zhang, Xiaolu Linda; De, Soumya; McIntosh, Lawrence; Paetzel, Mark. "Structural Characterization of the C3 Domain of Cardiac Myosin Binding Protein-C and its Hypertrophic Cardiomyopathy-Related R502W Mutant" .

Assembly members:

Assembly members:
entity, polymer, 95 residues, 10827.413 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GSHMPVLITRPLEDQLVMVG QRVEFECEVSEEGAQVKWLK DGVELTREETFKYRFKKDGQ RHHLIINEAMLEDAGHYALC TSGGQALAELIVQEK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	674
13C chemical shifts	423
15N chemical shifts	99

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 95 residues - 10827.413 Da.

1

GLY

SER

HIS

MET

PRO

VAL

LEU

ILE

THR

ARG

2

PRO

LEU

GLU

ASP

GLN

LEU

VAL

MET

VAL

GLY

3

GLN

ARG

VAL

GLU

PHE

GLU

CYS

GLU

VAL

SER

4

GLU

GLY

ALA

GLN

VAL

LYS

TRP

LEU

LYS

5

ASP

GLY

VAL

GLU

LEU

THR

ARG

GLU

THR

6

PHE

LYS

TYR

ARG

PHE

LYS

ASP

GLY

GLN

7

ARG

HIS

LEU

ILE

ASN

GLU

ALA

MET

8

LEU

GLU

ASP

ALA

GLY

HIS

TYR

ALA

LEU

CYS

9

THR

SER

GLY

GLN

ALA

LEU

ALA

GLU

LEU

10

ILE

VAL

GLN

GLU

LYS

Samples:

sample_1: sodium phosphate 50 mM; sodium chloride 100 mM; protein, [U-100% 13C; U-100% 15N], 0.8 mM; H2O 90%; D2O 10%

sample_conditions_1: temperature: 298 K; pH: 6.5; pressure: 1 atm; ionic strength: 0.4 M

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

Bruker Avance 500 MHz
Bruker Avance 600 MHz