BMRB Entry 19243

Name: Backbone chemical shifts of isolated Domain 1 from E. coli HisJ
Published: 2013-09-30

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19243

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:

Backbone chemical shifts of isolated Domain 1 from E. coli HisJ

Deposition date:

2013-05-15

Original release date:

2013-09-30

Authors:

Chu, Byron; Vogel, Hans

Citation:

Citation: Chu, Byron; Dewolf, Timothy; Vogel, Hans. "Role of the Two Structural Domains from the Periplasmic Escherichia coli Histidine-binding Protein HisJ." J. Biol. Chem. 288, 31409-31422 (2013).
PubMed: 24036119

Assembly members:

Assembly members:
D1, polymer, 148 residues, Formula weight is not available

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: pET-15

Entity Sequences (FASTA):

Entity Sequences (FASTA):
D1: GGMAIPQNIRIGTDPTYAPF ESKNSQGELVGFDIDLAKEL CKRINTQCTFVENPLDALIP SLKAKKIDAIMSSLSITEKR QQEIAFTDKLYAAGGGGSGL FGVGTGMGLRKEDNELREAL NKAFAEMRADGTYEKLAKKY FDFDVYGG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	425
15N chemical shifts	139
1H chemical shifts	139

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Domain 1 from E. coli HisJ	1

Entities:

Entity 1, Domain 1 from E. coli HisJ 148 residues - Formula weight is not available

1

GLY

MET

ALA

ILE

PRO

GLN

ASN

ILE

ARG

2

ILE

GLY

THR

ASP

PRO

THR

TYR

ALA

PRO

PHE

3

GLU

SER

LYS

ASN

SER

GLN

GLY

GLU

LEU

VAL

4

GLY

PHE

ASP

ILE

ASP

LEU

ALA

LYS

GLU

LEU

5

CYS

LYS

ARG

ILE

ASN

THR

GLN

CYS

THR

PHE

6

VAL

GLU

ASN

PRO

LEU

ASP

ALA

LEU

ILE

PRO

7

SER

LEU

LYS

ALA

LYS

ILE

ASP

ALA

ILE

8

MET

SER

LEU

SER

ILE

THR

GLU

LYS

ARG

9

GLN

GLU

ILE

ALA

PHE

THR

ASP

LYS

LEU

10

TYR

ALA

GLY

SER

GLY

LEU

11

PHE

GLY

VAL

GLY

THR

GLY

MET

GLY

LEU

ARG

12

LYS

GLU

ASP

ASN

GLU

LEU

ARG

GLU

ALA

LEU

13

ASN

LYS

ALA

PHE

ALA

GLU

MET

ARG

ALA

ASP

14

GLY

THR

TYR

GLU

LYS

LEU

ALA

LYS

TYR

15

PHE

ASP

PHE

ASP

VAL

TYR

GLY

Samples:

sample_1: D1, [U-13C; U-15N; U-2H], 1 mM; sodium phosphate 50 mM; D2O 10%; H2O 90%; DSS 0.5 mM

sample_conditions_1: ionic strength: 0 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - peak picking

NMR spectrometers:

Bruker Avance 700 MHz

EMBL	CAJ55342 CAJ55343 CAJ55344
GB	AEW46917 AEW46918 AEW46919 AHA92022 AHS49988