BMRB Entry 26068

Name: Structure of DNA-binding HU protein from micoplasma Mycoplasma gallisepticum
Published: 2016-11-03

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PDB ID: 2ndp
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR26068
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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 Mycoplasma gallisepticum

Deposition date:

2016-09-13

Original release date:

2016-11-03

Authors:

Altukhov, Dmitry; Talyzina, Anna; Agapova, Yulia; Vlaskina, Anna; Korzhenevskiy, Dmitry; Bocharov, Eduard; Rakitina, Tatiana; Timofeev, Vladimir; Popov, Vladimir

Citation:

Citation: Altukhov, Dmitry; Talyzina, Anna; Agapova, Yulia; Vlaskina, Anna; Korzhenevskiy, Dmitry; Bocharov, Eduard; Rakitina, Tatiana; Timofeev, Vladimir; Popov, Vladimir. "Structure of DNA-binding HU protein from micoplasma Mycoplasma gallisepticum" Biochem. Biophys. Res. Commun. ., .-..

Assembly members:

Assembly members:
entity, polymer, 99 residues, 10983.192 Da.

Natural source:

Natural source: Common Name: Mycoplasma gallisepticum Taxonomy ID: 2096 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycoplasma gallisepticum

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MAKIKSLSAAEYLKEMADET NIKVQDIRLVVTSLQKVLAK ELATTGEVRLFDIGKFKLVT TKPRTGINPKTKQKIQIPAG KKIKLTVSKILTDAVDSHK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	251
15N chemical shifts	94
1H chemical shifts	163

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 99 residues - 10983.192 Da.

1

MET

ALA

LYS

ILE

LYS

SER

LEU

SER

ALA

2

GLU

TYR

LEU

LYS

GLU

MET

ALA

ASP

GLU

THR

3

ASN

ILE

LYS

VAL

GLN

ASP

ILE

ARG

LEU

VAL

4

VAL

THR

SER

LEU

GLN

LYS

VAL

LEU

ALA

LYS

5

GLU

LEU

ALA

THR

GLY

GLU

VAL

ARG

LEU

6

PHE

ASP

ILE

GLY

LYS

PHE

LYS

LEU

VAL

THR

7

THR

LYS

PRO

ARG

THR

GLY

ILE

ASN

PRO

LYS

8

THR

LYS

GLN

LYS

ILE

GLN

ILE

PRO

ALA

GLY

9

LYS

ILE

LYS

LEU

THR

VAL

SER

LYS

ILE

10

LEU

THR

ASP

ALA

VAL

ASP

SER

HIS

LYS

Samples:

sample_1: entity, [U-13C; U-15N], 1 mM; D2O, [U-2H], 5%; sodium phosphate 50 mM; sodium azide 0.1 mM

sample_conditions_1: ionic strength: 0.375 M; pH: 6.7; pressure: 1 atm; temperature: 308 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:

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

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

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