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 27210

Title: PhoBN F20D assignment   PubMed: 29299752

Deposition date: 2017-08-08 Original release date: 2018-02-02

Authors: Kou, Xinhui

Citation: Kou, Xinhui; Liu, Xinghong; Liu, Yixiang; Li, Conggang; Liu, Maili; Jiang, Ling. "Backbone resonance assignment of the Escherichia coli protein mutation PhoBNF20D"  Biomol. NMR Assign. 12, 133-137 (2018).

Assembly members:
PhoBNF20D, polymer, 125 residues, Formula weight is not available

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: PET28a

Entity Sequences (FASTA):
PhoBNF20D: MARRILVVEDEAPIREMVCD VLEQNGFQPVEAEDYDSAVN QLNEPWPDLILLDWMLPGGS GIQFIKHLKRESMTRDIPVV MLTARGEEEDRVRGLETGAD DYITKPFSPKELVARIKAVM RRISQ

Data sets:
Data typeCount
13C chemical shifts218
15N chemical shifts109
1H chemical shifts205

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PhoBNF20D1

Entities:

Entity 1, PhoBNF20D 125 residues - Formula weight is not available

1   METALAARGARGILELEUVALVALGLUASP
2   GLUALAPROILEARGGLUMETVALCYSASP
3   VALLEUGLUGLNASNGLYPHEGLNPROVAL
4   GLUALAGLUASPTYRASPSERALAVALASN
5   GLNLEUASNGLUPROTRPPROASPLEUILE
6   LEULEUASPTRPMETLEUPROGLYGLYSER
7   GLYILEGLNPHEILELYSHISLEULYSARG
8   GLUSERMETTHRARGASPILEPROVALVAL
9   METLEUTHRALAARGGLYGLUGLUGLUASP
10   ARGVALARGGLYLEUGLUTHRGLYALAASP
11   ASPTYRILETHRLYSPROPHESERPROLYS
12   GLULEUVALALAARGILELYSALAVALMET
13   ARGARGILESERGLN

Samples:

sample_1: PhoBNF20D, [U-98% 15N], 0.6 mM; PhoBNF20D, [U-95% 13C], 0.6 mM; soduim chloride 100 mM; DTT 10 mM; HEPES 20 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Uniform NMR System 700 MHz

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