BMRB Entry 25918

Name: Solution NMR structure of Erythrobacter litoralis PhyR response regulator REC domain
Published: 2016-09-01

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PDB ID: 2n9u
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25918
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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:

Solution NMR structure of Erythrobacter litoralis PhyR response regulator REC domain

Deposition date:

2015-12-09

Original release date:

2016-09-01

Authors:

Correa, Fernando; Gardner, Kevin

Citation:

Citation: Correa, Fernando; Gardner, Kevin. "Basis of Mutual Domain Inhibition in a Bacterial Response Regulator" Cell Chem. Biol. S2451-9456, 30240-30249 (2016).
PubMed: 27524295

Assembly members:

Assembly members:
entity, polymer, 129 residues, 13823.661 Da.

Natural source:

Natural source: Common Name: a-proteobacteria Taxonomy ID: 39660 Superkingdom: Bacteria Kingdom: not available Genus/species: Erythrobacter litoralis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pHis - parallel

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GAMGSTNVLIIEDEPLISMQ LEDLVRSLGHDIAGTAATRT QAQEAVAKEKPGLVLADIQL ADGSSGIDAVEDILGQFDVP VIFITAYPERLLTGDRPEPT YLVTKPFQESTVRTTISQAL FFQNSPTAV

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	557
15N chemical shifts	131
1H chemical shifts	913

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 129 residues - 13823.661 Da.

1

GLY

ALA

MET

GLY

SER

THR

ASN

VAL

LEU

ILE

2

ILE

GLU

ASP

GLU

PRO

LEU

ILE

SER

MET

GLN

3

LEU

GLU

ASP

LEU

VAL

ARG

SER

LEU

GLY

HIS

4

ASP

ILE

ALA

GLY

THR

ALA

THR

ARG

THR

5

GLN

ALA

GLN

GLU

ALA

VAL

ALA

LYS

GLU

LYS

6

PRO

GLY

LEU

VAL

LEU

ALA

ASP

ILE

GLN

LEU

7

ALA

ASP

GLY

SER

GLY

ILE

ASP

ALA

VAL

8

GLU

ASP

ILE

LEU

GLY

GLN

PHE

ASP

VAL

PRO

9

VAL

ILE

PHE

ILE

THR

ALA

TYR

PRO

GLU

ARG

10

LEU

THR

GLY

ASP

ARG

PRO

GLU

PRO

THR

11

TYR

LEU

VAL

THR

LYS

PRO

PHE

GLN

GLU

SER

12

THR

VAL

ARG

THR

ILE

SER

GLN

ALA

LEU

13

PHE

GLN

ASN

SER

PRO

THR

ALA

VAL

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 0.5 – 1 mM; TRIS 10 mM; sodium chloride 50 mM; H2O 90 mM; D2O 10 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 7; pressure: 1 atm; temperature: 298.15 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
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - chemical shift assignment, refinement, structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis

VNMRJ, Varian - collection

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 800 MHz

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