BMRB Entry 25296

Name: Hha-H-NS46 charge zipper complex
Published: 2015-07-27

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PDB ID: 2mw2
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25296
MolProbity Validation Chart

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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:

Hha-H-NS46 charge zipper complex

Deposition date:

2014-10-24

Original release date:

2015-07-27

Authors:

Cordeiro, Tiago; Garcia, Jesus; Bernado, Pau; Millet, Oscar; Pons, Miquel

Citation:

Citation: Cordeiro, Tiago; Garcia, Jesus; Bernado, Pau; Millet, Oscar; Pons, Miquel. "A Three-protein Charge Zipper Stabilizes a Complex Modulating Bacterial Gene Silencing." J. Biol. Chem. 290, 21200-21212 (2015).
PubMed: 26085102

Assembly members:

Assembly members:
entity_1, polymer, 69 residues, 8068.402 Da.
entity_2, polymer, 46 residues, 5177.926 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: EKLTKTDYLMRLRRCQTIDT LERVIEKNKYELSDNELAVF YSAADHRLAELTMNKLYDKI PSSVWKFIR
entity_2: SEALKILNNIRTLRAQAREC TLETLEEMLEKLEVVVNERR EEESAA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
15N chemical shifts	115
1H chemical shifts	120

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	2
3	entity_2_2	2

Entities:

Entity 1, entity_1 69 residues - 8068.402 Da.

1

GLU

LYS

LEU

THR

LYS

THR

ASP

TYR

LEU

MET

2

ARG

LEU

ARG

CYS

GLN

THR

ILE

ASP

THR

3

LEU

GLU

ARG

VAL

ILE

GLU

LYS

ASN

LYS

TYR

4

GLU

LEU

SER

ASP

ASN

GLU

LEU

ALA

VAL

PHE

5

TYR

SER

ALA

ASP

HIS

ARG

LEU

ALA

GLU

6

LEU

THR

MET

ASN

LYS

LEU

TYR

ASP

LYS

ILE

7

PRO

SER

VAL

TRP

LYS

PHE

ILE

ARG

Entity 2, entity_2_1 46 residues - 5177.926 Da.

1

SER

GLU

ALA

LEU

LYS

ILE

LEU

ASN

ILE

2

ARG

THR

LEU

ARG

ALA

GLN

ALA

ARG

GLU

CYS

3

THR

LEU

GLU

THR

LEU

GLU

MET

LEU

GLU

4

LYS

LEU

GLU

VAL

ASN

GLU

ARG

5

GLU

SER

ALA

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_2
3D 1H-15N NOESY	sample_3	isotropic	sample_conditions_2
3D 1H-15N TOCSY	sample_3	isotropic	sample_conditions_2
2D 1H-15N HSQC	sample_4	isotropic	sample_conditions_2
3D 1H-15N NOESY	sample_4	isotropic	sample_conditions_2
3D 1H-15N TOCSY	sample_4	isotropic	sample_conditions_2

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BMRB Entry 25296

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: