BMRB Entry 34163

Name: Structure of DNA-binding HU protein from micoplasma Spiroplasma melliferum
Published: 2017-08-18

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PDB ID: 5ogu
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34163
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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:

Structure of DNA-binding HU protein from micoplasma Spiroplasma melliferum

Deposition date:

2017-07-13

Original release date:

2017-08-18

Authors:

Altukhov, D.; Talyzina, A.; Agapova, Y.; Vlaskina, A.; Korzhenevskiy, D.; Bocharov, E.; Rakitina, T.; Timofeev, V.

Citation:

Citation: Timofeev, Vladimir; Altukhov, Dmitry; Talyzina, Anna; Agapova, Yulia; Vlaskina, Anna; Korzhenevskiy, Dmitry; Kleymenov, Sergey Yu; Bocharov, Eduard; Rakitina, Tatiana. "Structural plasticity and thermal stability of the histone-like protein from Spiroplasma melliferum are due to phenylalanine insertions into the conservative scaffold" J. Biomol. Struct. Dyn. 36, 4392-4404 (2018).
PubMed: 29283021

Assembly members:

Assembly members:
DNA-binding protein, polymer, 95 residues, 10291.794 Da.

Natural source:

Natural source: Common Name: Spiroplasma melliferum KC3 Taxonomy ID: 570509 Superkingdom: Bacteria Kingdom: not available Genus/species: Spiroplasma Melliferum

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DNA-binding protein: GHMSKKELAAQIAEKFTDVL SKTHAEEITNFVFDHIKKAL VAGKEVSIAGFGKFAVTERA ARDGRNPSTGETIKIPASKS AKFKAGKQLKTDLNN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	119
15N chemical shifts	78
1H chemical shifts	123

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1, chain 1	1
2	entity_1, chain 2	1

Entities:

Entity 1, entity_1, chain 1 95 residues - 10291.794 Da.

1

GLY

HIS

MET

SER

LYS

GLU

LEU

ALA

2

GLN

ILE

ALA

GLU

LYS

PHE

THR

ASP

VAL

LEU

3

SER

LYS

THR

HIS

ALA

GLU

ILE

THR

ASN

4

PHE

VAL

PHE

ASP

HIS

ILE

LYS

ALA

LEU

5

VAL

ALA

GLY

LYS

GLU

VAL

SER

ILE

ALA

GLY

6

PHE

GLY

LYS

PHE

ALA

VAL

THR

GLU

ARG

ALA

7

ALA

ARG

ASP

GLY

ARG

ASN

PRO

SER

THR

GLY

8

GLU

THR

ILE

LYS

ILE

PRO

ALA

SER

LYS

SER

9

ALA

LYS

PHE

LYS

ALA

GLY

LYS

GLN

LEU

LYS

10

THR

ASP

LEU

ASN

Samples:

sample_1: entity_1, na, mM; D2O, [U-2H], 5%

sample_conditions_1: ionic strength: 0.375 M; pH: 6.7; 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

Software:

GROMACS, Herman Berendsen's group, department of Biophysical Chemistry of Groningen University - refinement

TALOS++, Cornilescu, Delaglio and Bax - chemical shift assignment

NMR spectrometers:

Agilent Uniform NMR System 700 MHz

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