BMRB Entry 19815

Name: NMR Assignment of Coiled Coil Domain of Myosin Binding Subunit of Myosin Light Chain Phosphatase
Published: 2014-03-24

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19815

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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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Title:

NMR Assignment of Coiled Coil Domain of Myosin Binding Subunit of Myosin Light Chain Phosphatase

Deposition date:

2014-02-24

Original release date:

2014-03-24

Authors:

SHARMA, ALOK; RIGBY, ALAN

Citation:

Citation: Sharma, Alok; Rigby, Alan. "NMR Assignment and Secondary Structure of Coiled Coil Domain of C-terminal Myosin Binding Subunit of Myosin Phosphatase." Protein Pept. Lett. 21, 639-645 (2014).
PubMed: 24693955

Assembly members:

Assembly members:
COILED_COIL_DOMAIN_OF_MLCP, polymer, 50 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: PET28A(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
COILED_COIL_DOMAIN_OF_MLCP: DFKKLYEQILAENEKLKAQL HDTNMELTDLKLQLEKATQR QERFADRSLL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	346
13C chemical shifts	206
15N chemical shifts	50

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SUBUNIT 12A, 1	1
2	SUBUNIT 12A, 2	1

Entities:

Entity 1, SUBUNIT 12A, 1 50 residues - Formula weight is not available

1	ASP	PHE	LYS	LYS	LEU	TYR	GLU	GLN	ILE	LEU
2	ALA	GLU	ASN	GLU	LYS	LEU	LYS	ALA	GLN	LEU
3	HIS	ASP	THR	ASN	MET	GLU	LEU	THR	ASP	LEU
4	LYS	LEU	GLN	LEU	GLU	LYS	ALA	THR	GLN	ARG
5	GLN	GLU	ARG	PHE	ALA	ASP	ARG	SER	LEU	LEU

Samples:

sample_1: COILED COIL DOMAIN OF MLCP, [U-13C; U-15N], 1.0 mM; H2O 92%; D2O 8%

sample_conditions_1: ionic strength: 0.01 M; pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment, processing

NMR spectrometers:

Bruker Avance 600 MHz

PDB	2MXR
DBJ	BAA07201 BAA07202 BAA22378 BAB23563 BAC28990
EMBL	CAH91185
GB	AAB32730 AAB32731 AAI11753 AAI25382 AAI37631
REF	NP_001137357 NP_001137358 NP_001231921 NP_001253022 NP_002471
SP	O14974 Q10728 Q90623 Q9DBR7
AlphaFold	O14974 Q10728 Q90623 Q9DBR7

1	ASP	PHE	LYS	LYS	LEU	TYR	GLU	GLN	ILE	LEU
2	ALA	GLU	ASN	GLU	LYS	LEU	LYS	ALA	GLN	LEU
3	HIS	ASP	THR	ASN	MET	GLU	LEU	THR	ASP	LEU
4	LYS	LEU	GLN	LEU	GLU	LYS	ALA	THR	GLN	ARG
5	GLN	GLU	ARG	PHE	ALA	ASP	ARG	SER	LEU	LEU

1	ASP	PHE	LYS	LYS	LEU	TYR	GLU	GLN	ILE	LEU
2	ALA	GLU	ASN	GLU	LYS	LEU	LYS	ALA	GLN	LEU
3	HIS	ASP	THR	ASN	MET	GLU	LEU	THR	ASP	LEU
4	LYS	LEU	GLN	LEU	GLU	LYS	ALA	THR	GLN	ARG
5	GLN	GLU	ARG	PHE	ALA	ASP	ARG	SER	LEU	LEU