BMRB Entry 30532

Name: Solution NMR Structure of DANCER3-F34A, a rigid and natively folded single mutant of the dynamic protein DANCER-3
Published: 2019-08-16

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PDB ID: 6njf
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30532
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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:

Solution NMR Structure of DANCER3-F34A, a rigid and natively folded single mutant of the dynamic protein DANCER-3

Deposition date:

2018-10-31

Original release date:

2019-08-16

Authors:

Damry, A.; Mayer, M.; Goto, N.; Chica, R.

Citation:

Citation: Damry, Adam; Mayer, Marc; Broom, Aron; Goto, Natalie; Chica, Roberto. "Origin of conformational dynamics in a globular protein" Commun. Biol. 2, 433-433 (2019).
PubMed: 31799435

Assembly members:

Assembly members:
entity_1, polymer, 64 residues, 7230.964 Da.

Natural source:

Natural source: Common Name: Streptococcus sp. Taxonomy ID: 1320 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptococcus Streptococcus sp.

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MHHHHHHGMTFKLIINGKTL KGETTTEAVDAATAEKVFKQ YANDNGLDGEWTYDDATKTF TITE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	242
15N chemical shifts	62
1H chemical shifts	379

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 64 residues - 7230.964 Da.

1

MET

HIS

GLY

MET

THR

2

PHE

LYS

LEU

ILE

ASN

GLY

LYS

THR

LEU

3

LYS

GLY

GLU

THR

GLU

ALA

VAL

ASP

4

ALA

THR

ALA

GLU

LYS

VAL

PHE

LYS

GLN

5

TYR

ALA

ASN

ASP

ASN

GLY

LEU

ASP

GLY

GLU

6

TRP

THR

TYR

ASP

ALA

THR

LYS

THR

PHE

7

THR

ILE

THR

GLU

Samples:

sample_1: protein (GB1), [U-98% 15N], 1.0 mM; sodium phosphate 10 mM

sample_2: protein (GB1), [U-99% 13C; U-98% 15N], 1.0 mM; sodium phosphate 10 mM

sample_3: protein (GB1), [U-99% 13C; U-98% 15N], 1.0 mM; sodium phosphate 10 mM

sample_conditions_1: ionic strength: 10 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_3	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_3	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - collection

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

NMR spectrometers:

Bruker AVANCE III 600 MHz

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