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 19242

Title: The solution NMR structure of E. coli apo-HisJ   PubMed: 24036119

Deposition date: 2013-05-15 Original release date: 2013-09-30

Authors: Chu, Byron; Vogel, Hans

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).

Assembly members:
apo-HisJ, polymer, 241 residues, 26264.783 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-15

Entity Sequences (FASTA):
apo-HisJ: GGMAIPQNIRIGTDPTYAPF ESKNSQGELVGFDIDLAKEL CKRINTQCTFVENPLDALIP SLKAKKIDAIMSSLSITEKR QQEIAFTDKLYAADSRLVVA KNSDIQPTVESLKGKRVGVL QGTTQETFGNEHWAPKGIEI VSYQGQDNIYSDLTAGRIDA AFQDEVAASEGFLKQPVGKD YKFGGPSVKDEKLFGVGTGM GLRKEDNELREALNKAFAEM RADGTYEKLAKKYFDFDVYG G

Data sets:
Data typeCount
13C chemical shifts697
15N chemical shifts229
1H chemical shifts229

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1apo-HisJ1

Entities:

Entity 1, apo-HisJ 241 residues - 26264.783 Da.

1   GLYGLYMETALAILEPROGLNASNILEARG
2   ILEGLYTHRASPPROTHRTYRALAPROPHE
3   GLUSERLYSASNSERGLNGLYGLULEUVAL
4   GLYPHEASPILEASPLEUALALYSGLULEU
5   CYSLYSARGILEASNTHRGLNCYSTHRPHE
6   VALGLUASNPROLEUASPALALEUILEPRO
7   SERLEULYSALALYSLYSILEASPALAILE
8   METSERSERLEUSERILETHRGLULYSARG
9   GLNGLNGLUILEALAPHETHRASPLYSLEU
10   TYRALAALAASPSERARGLEUVALVALALA
11   LYSASNSERASPILEGLNPROTHRVALGLU
12   SERLEULYSGLYLYSARGVALGLYVALLEU
13   GLNGLYTHRTHRGLNGLUTHRPHEGLYASN
14   GLUHISTRPALAPROLYSGLYILEGLUILE
15   VALSERTYRGLNGLYGLNASPASNILETYR
16   SERASPLEUTHRALAGLYARGILEASPALA
17   ALAPHEGLNASPGLUVALALAALASERGLU
18   GLYPHELEULYSGLNPROVALGLYLYSASP
19   TYRLYSPHEGLYGLYPROSERVALLYSASP
20   GLULYSLEUPHEGLYVALGLYTHRGLYMET
21   GLYLEUARGLYSGLUASPASNGLULEUARG
22   GLUALALEUASNLYSALAPHEALAGLUMET
23   ARGALAASPGLYTHRTYRGLULYSLEUALA
24   LYSLYSTYRPHEASPPHEASPVALTYRGLY
25   GLY

Samples:

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

sample_2: apo-HisJ, [U-13C; U-15N], 1 mM; sodium phosphate 50 mM; D2O 10%; H2O 90%; DSS 0.5 mM

sample_3: apo-HisJ, [U-13C; U-15N], 1 mM; sodium phosphate 50 mM; D2O 100%; DSS 0.5 mM

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

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

BMRB 16204 16205 19245
PDB
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 P0AEU1 P0AEU0 P02910 P0AEU2

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