BMRB Entry 34127

Name: NMR structure and 1H, 13C and 15N signal assignments for Dictyostelium discoidans MATB protein S71A mutant
Published: 2017-09-13

Click here to enlarge.

PDB ID: 5nr6
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34127
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

NMR structure and 1H, 13C and 15N signal assignments for Dictyostelium discoidans MATB protein S71A mutant

Deposition date:

2017-04-22

Original release date:

2017-09-13

Authors:

Neuhaus, D.; Hedgethorne, K.; Yang, J.-C.

Citation:

Citation: Hedgethorne, Katy; Eustermann, Sebastian; Yang, Ji-Chun; Ogden, Tom; Neuhaus, David; Bloomfield, Gareth. "Homeodomain-like DNA binding proteins control the haploid-to-diploid transition in Dictyostelium." Sci. Adv. 3, e1602937-e1602937 (2017).
PubMed: 28879231

Assembly members:

Assembly members:
entity_1, polymer, 113 residues, 12652.264 Da.

Natural source:

Natural source: Common Name: Slime mold Taxonomy ID: 44689 Superkingdom: Eukaryota Kingdom: not available Genus/species: Dictyostelium discoideum

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3) Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMASMDQLDEIIEQIQKE AINSNVVLKNPRVPTQKTGE LSEEQKKIVADYISEVGLNN LNATELSKRLNITVDKAKTY IKNSNRMGRTNNFKTIKMFE DDVSSASAQPNLP

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	349
15N chemical shifts	124
1H chemical shifts	746

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 113 residues - 12652.264 Da.

1

GLY

SER

HIS

MET

ALA

SER

MET

ASP

GLN

LEU

2

ASP

GLU

ILE

GLU

GLN

ILE

GLN

LYS

GLU

3

ALA

ILE

ASN

SER

ASN

VAL

LEU

LYS

ASN

4

PRO

ARG

VAL

PRO

THR

GLN

LYS

THR

GLY

GLU

5

LEU

SER

GLU

GLN

LYS

ILE

VAL

ALA

6

ASP

TYR

ILE

SER

GLU

VAL

GLY

LEU

ASN

7

LEU

ASN

ALA

THR

GLU

LEU

SER

LYS

ARG

LEU

8

ASN

ILE

THR

VAL

ASP

LYS

ALA

LYS

THR

TYR

9

ILE

LYS

ASN

SER

ASN

ARG

MET

GLY

ARG

THR

10

ASN

PHE

LYS

THR

ILE

LYS

MET

PHE

GLU

11

ASP

VAL

SER

ALA

SER

ALA

GLN

PRO

12

ASN

LEU

PRO

Samples:

sample_1: EDTA 50 uM; MATB, [U-15N], 600 ± 100 uM; sodium chloride 100 mM; sodium phosphate 25 mM

sample_2: EDTA 50 uM; MATB, [U-13C; U-15N], 600 ± 100 uM; sodium chloride 100 mM; sodium phosphate 25 mM

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 274 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNHAHB	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D [1H-13C-1H] HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D [13C-13C-1H] HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D [1H-13C-1H] HCCH-COSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY (mix. time 150ms)	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic (mix. time 150ms)	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic (mix. time 150ms)	sample_2	isotropic	sample_conditions_1

Software:

AMBER v11, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CcpNMR v2.4, CCPN - chemical shift assignment

TOPSPIN v3.1 and 3.2, Bruker Biospin - processing

UNIO v2.0.3, Herrmann - structure calculation

X-PLOR NIH v2.28, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

Bruker Avance 800 MHz
Bruker DMX 600 MHz

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