BMRB Entry 19244

Name: Backbone chemical shifts of isolated Domain 2 from E. coli HisJ
Published: 2013-09-30

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19244

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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:

Backbone chemical shifts of isolated Domain 2 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:
D2, polymer, 102 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):
D2: GGMDSRLVVAKNSDIQPTVE SLKGKRVGVLQGTTQETFGN EHWAPKGIEIVSYQGQDNIY SDLTAGRIDAAFQDEVAASE GFLKQPVGKDYKFGGPSVKD EK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	290
15N chemical shifts	94
1H chemical shifts	94

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Domain 2 from E. coli HisJ	1

Entities:

Entity 1, Domain 2 from E. coli HisJ 102 residues - Formula weight is not available

1

GLY

MET

ASP

SER

ARG

LEU

VAL

ALA

2

LYS

ASN

SER

ASP

ILE

GLN

PRO

THR

VAL

GLU

3

SER

LEU

LYS

GLY

LYS

ARG

VAL

GLY

VAL

LEU

4

GLN

GLY

THR

GLN

GLU

THR

PHE

GLY

ASN

5

GLU

HIS

TRP

ALA

PRO

LYS

GLY

ILE

GLU

ILE

6

VAL

SER

TYR

GLN

GLY

GLN

ASP

ASN

ILE

TYR

7

SER

ASP

LEU

THR

ALA

GLY

ARG

ILE

ASP

ALA

8

ALA

PHE

GLN

ASP

GLU

VAL

ALA

SER

GLU

9

GLY

PHE

LEU

LYS

GLN

PRO

VAL

GLY

LYS

ASP

10

TYR

LYS

PHE

GLY

PRO

SER

VAL

LYS

ASP

11

GLU

LYS

Samples:

sample_1: D2, [U-13C; U-15N], 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

BMRB	16204 16205 19242 19245
PDB	1HPB 1HSL 2M8C
DBJ	BAA16155 BAB36616 BAG66608 BAG78142 BAI26504
EMBL	CAA24658 CAA24659 CAD07586 CAJ55342 CAJ55343
GB	AAA75578 AAA85769 AAC75369 AAG57438 AAL21255
PIR	AH0800
PRF	0809313B
REF	NP_311220 NP_416812 NP_456896 NP_461296 NP_708191
SP	P02910 P0AEU0 P0AEU1 P0AEU2
AlphaFold	P02910 P0AEU0 P0AEU1 P0AEU2