BMRB Entry 16204

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for apo HisJ and holo HisJ
Published: 2010-01-11

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16204

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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 1H, 13C, and 15N Chemical Shift Assignments for apo HisJ and holo HisJ

Deposition date:

2009-03-08

Original release date:

2010-01-11

Authors:

Igarashi, Shunsuke; Osawa, Masanori; Shimada, Ichio

Citation:

Citation: Igarashi, Shunsuke; Osawa, Masanori; Ozawa, Shin-Ichiro; Shimada, Ichio. "Backbone resonance assignments for the ligand binding subunit of the histidine permease complex (HisJ) from Escherichia coli, under histidine-bound and unbound states." Biomol. NMR Assignments 4, 17-20 (2010).
PubMed: 19921465

Assembly members:

Assembly members:
HisJ, polymer, 238 residues, Formula weight is not available
HIS, non-polymer, 156.162 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HisJ: AIPQNIRIGTDPTYAPFESK NSQGELVGFDIDLAKELCKR INTQCTFVENPLDALIPSLK AKKIDAIMSSLSITEKRQQE IAFTDKLYAADSRLVVAKNS DIQPTVESLKGKRVGVLQGT TQETFGNEHWAPKGIEIVSY QGQDNIYSDLTAGRIDAAFQ DEVAASEGFLKQPVGKDYKF GGPSVKDEKLFGVGTGMGLR KEDNELREALNKAFAEMRAD GTYEKLAKKYFDFDVYGG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	702
15N chemical shifts	227
1H chemical shifts	601

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	subunit1	1
2	ligand	2

Entities:

Entity 1, subunit1 238 residues - Formula weight is not available

1

ALA

ILE

PRO

GLN

ASN

ILE

ARG

ILE

GLY

THR

2

ASP

PRO

THR

TYR

ALA

PRO

PHE

GLU

SER

LYS

3

ASN

SER

GLN

GLY

GLU

LEU

VAL

GLY

PHE

ASP

4

ILE

ASP

LEU

ALA

LYS

GLU

LEU

CYS

LYS

ARG

5

ILE

ASN

THR

GLN

CYS

THR

PHE

VAL

GLU

ASN

6

PRO

LEU

ASP

ALA

LEU

ILE

PRO

SER

LEU

LYS

7

ALA

LYS

ILE

ASP

ALA

ILE

MET

SER

8

LEU

SER

ILE

THR

GLU

LYS

ARG

GLN

GLU

9

ILE

ALA

PHE

THR

ASP

LYS

LEU

TYR

ALA

10

ASP

SER

ARG

LEU

VAL

ALA

LYS

ASN

SER

11

ASP

ILE

GLN

PRO

THR

VAL

GLU

SER

LEU

LYS

12

GLY

LYS

ARG

VAL

GLY

VAL

LEU

GLN

GLY

THR

13

THR

GLN

GLU

THR

PHE

GLY

ASN

GLU

HIS

TRP

14

ALA

PRO

LYS

GLY

ILE

GLU

ILE

VAL

SER

TYR

15

GLN

GLY

GLN

ASP

ASN

ILE

TYR

SER

ASP

LEU

16

THR

ALA

GLY

ARG

ILE

ASP

ALA

PHE

GLN

17

ASP

GLU

VAL

ALA

SER

GLU

GLY

PHE

LEU

18

LYS

GLN

PRO

VAL

GLY

LYS

ASP

TYR

LYS

PHE

19

GLY

PRO

SER

VAL

LYS

ASP

GLU

LYS

LEU

20

PHE

GLY

VAL

GLY

THR

GLY

MET

GLY

LEU

ARG

21

LYS

GLU

ASP

ASN

GLU

LEU

ARG

GLU

ALA

LEU

22

ASN

LYS

ALA

PHE

ALA

GLU

MET

ARG

ALA

ASP

23

GLY

THR

TYR

GLU

LYS

LEU

ALA

LYS

TYR

24

PHE

ASP

PHE

ASP

VAL

TYR

GLY

Entity 2, ligand - C6 H10 N3 O2 - 156.162 Da.

1

HIS

Samples:

sample_1: H2O 90%; D2O 10%; sodium chloride 50 mM; sodium phosphate 50 mM; TSP 1 mM; HisJ, [U-99% 13C; U-99% 15N], 2 mM; histidine, [U-98% 2H], 5 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

Bruker Avance 600 MHz

BMRB	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