BMRB Entry 25727

Name: 1H, 13C, and 15N Chemical Shift Assignments for Histamine-Binding Protein (D24R) bound to histamine
Published: 2017-06-27

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25727

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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:

1H, 13C, and 15N Chemical Shift Assignments for Histamine-Binding Protein (D24R) bound to histamine

Deposition date:

2015-07-27

Original release date:

2017-06-27

Authors:

Lim, Jackwee; Valentine, Kathleen; Kasinath, Vignesh; Harpole, Kyle; Sharp, Kim; Wand, Joshua

Citation:

Citation: Caro, Jose; Harpole, Kyle; Kasinath, Vignesh; Lim, Jackwee; Granja, Jeffrey; Valentine, Kathleen; Sharp, Kim; Wand, A Joshua. "Entropy in molecular recognition by proteins" Proc. Natl. Acad. Sci. U.S.A. 114, 6563-6568 (2017).
PubMed: 28584100

Assembly members:

Assembly members:
HBP(d24r), polymer, 173 residues, Formula weight is not available
HISTAMINE, non-polymer, 111.145 Da.

Natural source:

Natural source: Common Name: mites and ticks Taxonomy ID: 34631 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rhipicephalus appendiculatus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HBP(d24r): GSNQPDWADEAANGAHQDAW KSLKARVENVYYMVKATYKN DPVWGNDFTCVGVMANDVNE DEKSIQAEFLFMNNADTNMQ FATEKVTAVKMYGYNRENAF RYETEDGQVFTDVIAYSDDN CDVIYVPGTDGNEEGYELWT TDYDNIPANCLNKFNEYAVG RETRDVFTSACLE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
order_parameters
- order_parameter_1
- order_parameter_2

Data type	Count
13C chemical shifts	381
15N chemical shifts	160
1H chemical shifts	367
order parameters	210

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HBPd24r	1
2	histamine	2

Entities:

Entity 1, HBPd24r 173 residues - Formula weight is not available

1

GLY

SER

ASN

GLN

PRO

ASP

TRP

ALA

ASP

GLU

2

ALA

ASN

GLY

ALA

HIS

GLN

ASP

ALA

TRP

3

LYS

SER

LEU

LYS

ALA

ARG

VAL

GLU

ASN

VAL

4

TYR

MET

VAL

LYS

ALA

THR

TYR

LYS

ASN

5

ASP

PRO

VAL

TRP

GLY

ASN

ASP

PHE

THR

CYS

6

VAL

GLY

VAL

MET

ALA

ASN

ASP

VAL

ASN

GLU

7

ASP

GLU

LYS

SER

ILE

GLN

ALA

GLU

PHE

LEU

8

PHE

MET

ASN

ALA

ASP

THR

ASN

MET

GLN

9

PHE

ALA

THR

GLU

LYS

VAL

THR

ALA

VAL

LYS

10

MET

TYR

GLY

TYR

ASN

ARG

GLU

ASN

ALA

PHE

11

ARG

TYR

GLU

THR

GLU

ASP

GLY

GLN

VAL

PHE

12

THR

ASP

VAL

ILE

ALA

TYR

SER

ASP

ASN

13

CYS

ASP

VAL

ILE

TYR

VAL

PRO

GLY

THR

ASP

14

GLY

ASN

GLU

GLY

TYR

GLU

LEU

TRP

THR

15

THR

ASP

TYR

ASP

ASN

ILE

PRO

ALA

ASN

CYS

16

LEU

ASN

LYS

PHE

ASN

GLU

TYR

ALA

VAL

GLY

17

ARG

GLU

THR

ARG

ASP

VAL

PHE

THR

SER

ALA

18

CYS

LEU

GLU

Entity 2, histamine - C5 H9 N3 - 111.145 Da.

1

HSM

Samples:

sample_2: HBPd24r, [U-99% 15N], 1.5 mM; HBPd24r, [U-99% 13C; U-55% 2H], 1.5 mM; Histamine 2.5 mM; D2O, [U-2H], 5%; potassium phosphate 50 mM; sodium azide 0.02%; H2O 95%

sample_1: HBP(d24r) histamine bound, [U-99% 13C; U-99% 15N], 1.0 mM; Histamine 1.5 mM; potassium phosphate 50 mM; D2O 5%; sodium azide 0.02%; H2O, natuarl abundance, 95%

sample_conditions_1: ionic strength: 0.05 M; pH: 7.3; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 50 mM; pH: 7.3; pressure: 1 atm; temperature: 298 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 HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_2
N T1 relaxation	sample_2	isotropic	sample_conditions_2
N T2 relaxation	sample_2	isotropic	sample_conditions_2
N NOE relaxation	sample_2	isotropic	sample_conditions_2
Dz (IzCz) compensated relaxation	sample_2	isotropic	sample_conditions_2
Dy (IzCz) compensated relaxation	sample_2	isotropic	sample_conditions_2

Software:

Felix, Accelrys Software Inc. - processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 500 MHz
Bruker Avance 750 MHz

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