BMRB Entry 16205

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16205

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for apo HisJ and holo HisJ
Deposition date:
2009-03-09
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

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:
Data typeCount
13C chemical shifts755
15N chemical shifts213
1H chemical shifts613

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit11

Entities:

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

1   ALAILEPROGLNASNILEARGILEGLYTHR
2   ASPPROTHRTYRALAPROPHEGLUSERLYS
3   ASNSERGLNGLYGLULEUVALGLYPHEASP
4   ILEASPLEUALALYSGLULEUCYSLYSARG
5   ILEASNTHRGLNCYSTHRPHEVALGLUASN
6   PROLEUASPALALEUILEPROSERLEULYS
7   ALALYSLYSILEASPALAILEMETSERSER
8   LEUSERILETHRGLULYSARGGLNGLNGLU
9   ILEALAPHETHRASPLYSLEUTYRALAALA
10   ASPSERARGLEUVALVALALALYSASNSER
11   ASPILEGLNPROTHRVALGLUSERLEULYS
12   GLYLYSARGVALGLYVALLEUGLNGLYTHR
13   THRGLNGLUTHRPHEGLYASNGLUHISTRP
14   ALAPROLYSGLYILEGLUILEVALSERTYR
15   GLNGLYGLNASPASNILETYRSERASPLEU
16   THRALAGLYARGILEASPALAALAPHEGLN
17   ASPGLUVALALAALASERGLUGLYPHELEU
18   LYSGLNPROVALGLYLYSASPTYRLYSPHE
19   GLYGLYPROSERVALLYSASPGLULYSLEU
20   PHEGLYVALGLYTHRGLYMETGLYLEUARG
21   LYSGLUASPASNGLULEUARGGLUALALEU
22   ASNLYSALAPHEALAGLUMETARGALAASP
23   GLYTHRTYRGLULYSLEUALALYSLYSTYR
24   PHEASPPHEASPVALTYRGLYGLY

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

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; 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 HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 16204 19242 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 P02910 P0AEU0 P0AEU1 P0AEU2

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