BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 25727

Title: 1H, 13C, and 15N Chemical Shift Assignments for Histamine-Binding Protein (D24R) bound to histamine   PubMed: 28584100

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: 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).

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

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

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

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

Data sets:
Data typeCount
13C chemical shifts381
15N chemical shifts160
1H chemical shifts367
order parameters210

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1HBPd24r1
2histamine2

Entities:

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

1   GLYSERASNGLNPROASPTRPALAASPGLU
2   ALAALAASNGLYALAHISGLNASPALATRP
3   LYSSERLEULYSALAARGVALGLUASNVAL
4   TYRTYRMETVALLYSALATHRTYRLYSASN
5   ASPPROVALTRPGLYASNASPPHETHRCYS
6   VALGLYVALMETALAASNASPVALASNGLU
7   ASPGLULYSSERILEGLNALAGLUPHELEU
8   PHEMETASNASNALAASPTHRASNMETGLN
9   PHEALATHRGLULYSVALTHRALAVALLYS
10   METTYRGLYTYRASNARGGLUASNALAPHE
11   ARGTYRGLUTHRGLUASPGLYGLNVALPHE
12   THRASPVALILEALATYRSERASPASPASN
13   CYSASPVALILETYRVALPROGLYTHRASP
14   GLYASNGLUGLUGLYTYRGLULEUTRPTHR
15   THRASPTYRASPASNILEPROALAASNCYS
16   LEUASNLYSPHEASNGLUTYRALAVALGLY
17   ARGGLUTHRARGASPVALPHETHRSERALA
18   CYSLEUGLU

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
2D 1H-13C HSQCsample_2isotropicsample_conditions_2
N T1 relaxationsample_2isotropicsample_conditions_2
N T2 relaxationsample_2isotropicsample_conditions_2
N NOE relaxationsample_2isotropicsample_conditions_2
Dz (IzCz) compensated relaxationsample_2isotropicsample_conditions_2
Dy (IzCz) compensated relaxationsample_2isotropicsample_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 shifts
SPARKY: Backbone or all simulated shifts