BMRB Entry 25899

Name: Solution NMR Structure of Antiparallel Myosin-10:GCN4 Tandem Coiled-Coil
Published: 2016-06-08

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PDB ID: 2n9b
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25899
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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:

Solution NMR Structure of Antiparallel Myosin-10:GCN4 Tandem Coiled-Coil

Deposition date:

2015-11-12

Original release date:

2016-06-08

Authors:

Vavra, K.; Xia, Youlin; Rock, Ronald

Citation:

Citation: Vavra, K.; Xia, Youlin; Rock, Ronald. "Competition between Coiled-Coil Structures and the Impact on Myosin-10 Bundle Selection" Biophys. J. 110, 2517-2527 (2016).

Assembly members:

Assembly members:
entity, polymer, 69 residues, 8200.371 Da.

Natural source:

Natural source: Common Name: cow Taxonomy ID: 9913 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Bos taurus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GSHENKQVEEILRLEKEIED LQRMKERQELSLTEASLQKL QLEDKVEELLSKNYHLENEV ARLKKLVGE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	620
15N chemical shifts	148
1H chemical shifts	946

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	1

Entities:

Entity 1, entity_1 69 residues - 8200.371 Da.

1

GLY

SER

HIS

GLU

ASN

LYS

GLN

VAL

GLU

2

ILE

LEU

ARG

LEU

GLU

LYS

GLU

ILE

GLU

ASP

3

LEU

GLN

ARG

MET

LYS

GLU

ARG

GLN

GLU

LEU

4

SER

LEU

THR

GLU

ALA

SER

LEU

GLN

LYS

LEU

5

GLN

LEU

GLU

ASP

LYS

VAL

GLU

LEU

6

SER

LYS

ASN

TYR

HIS

LEU

GLU

ASN

GLU

VAL

7

ALA

ARG

LEU

LYS

LEU

VAL

GLY

GLU

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1.1 mM; potassium phosphate 100 mM; EDTA 1 mM; sodium azide 0.03%

sample_conditions_1: ionic strength: 0.6 M; pH: 6.5; pressure: 1 atm; temperature: 35 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCANH	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDHD	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC NH2 only	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

Xplor-NIH v2.38, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

CCPN v2.4.1, CCPN - chemical shift assignment, data analysis, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Bruker Avance 850 MHz
Varian INOVA 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks