BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 26722

Title: 1H, 15N, 13C backbone shift assignments of PhyR protein from Erythrobacter litoralis   PubMed: 27524295

Deposition date: 2015-12-14 Original release date: 2016-09-01

Authors: Correa, Fernando; Gardner, Kevin

Citation: Correa, Fernando; Gardner, Kevin. "Basis of Mutual Domain Inhibition in a Bacterial Response Regulator"  Cell Chem. Biol. 23, 945-954 (2016).

Assembly members:
ELI10215, polymer, 270 residues, Formula weight is not available

Natural source:   Common Name: a-proteobacteria   Taxonomy ID: 39960   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Erythrobacter litoralis

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pHis - parallel

Entity Sequences (FASTA):
ELI10215: GAMGMSASQKIAANLPYLRR YARALTGSQQTGDTFVRATL EAAIADESLKQDVSEGRVPL YKAFNALWSSSYLEVEGDDG GDVVSAKEAGAGDRLKAVTP LNRQALLLTTLEDFSVEDAA EIMGLAPADVEGLVREAVAE IDRESSTNVLIIEDEPLISM QLEDLVRSLGHDIAGTAATR TQAQEAVAKEKPGLVLADIQ LADGSSGIDAVEDILGQFDV PVIFITAYPERLLTGDRPEP TYLVTKPFQESTVRTTISQA LFFQNSPTAV

Data sets:
Data typeCount
13C chemical shifts497
15N chemical shifts252
1H chemical shifts257

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ELI102151

Entities:

Entity 1, ELI10215 270 residues - Formula weight is not available

Residues 1-4 (GAMG) are cloning artifacts derived from the expression vector

1   GLYALAMETGLYMETSERALASERGLNLYS
2   ILEALAALAASNLEUPROTYRLEUARGARG
3   TYRALAARGALALEUTHRGLYSERGLNGLN
4   THRGLYASPTHRPHEVALARGALATHRLEU
5   GLUALAALAILEALAASPGLUSERLEULYS
6   GLNASPVALSERGLUGLYARGVALPROLEU
7   TYRLYSALAPHEASNALALEUTRPSERSER
8   SERTYRLEUGLUVALGLUGLYASPASPGLY
9   GLYASPVALVALSERALALYSGLUALAGLY
10   ALAGLYASPARGLEULYSALAVALTHRPRO
11   LEUASNARGGLNALALEULEULEUTHRTHR
12   LEUGLUASPPHESERVALGLUASPALAALA
13   GLUILEMETGLYLEUALAPROALAASPVAL
14   GLUGLYLEUVALARGGLUALAVALALAGLU
15   ILEASPARGGLUSERSERTHRASNVALLEU
16   ILEILEGLUASPGLUPROLEUILESERMET
17   GLNLEUGLUASPLEUVALARGSERLEUGLY
18   HISASPILEALAGLYTHRALAALATHRARG
19   THRGLNALAGLNGLUALAVALALALYSGLU
20   LYSPROGLYLEUVALLEUALAASPILEGLN
21   LEUALAASPGLYSERSERGLYILEASPALA
22   VALGLUASPILELEUGLYGLNPHEASPVAL
23   PROVALILEPHEILETHRALATYRPROGLU
24   ARGLEULEUTHRGLYASPARGPROGLUPRO
25   THRTYRLEUVALTHRLYSPROPHEGLNGLU
26   SERTHRVALARGTHRTHRILESERGLNALA
27   LEUPHEPHEGLNASNSERPROTHRALAVAL

Samples:

sample_1: ELI10215, [U-13C; U-15N; U-2H], 0.5 – 1 mM; TRIS 10 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_2: ELI10215, [U-99% 13C; U-99% 15N], 0.5 – 1 mM; TRIS 10 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 7; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)CBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-15N TROSY HSQCsample_1isotropicsample_conditions_1
2D 1H-15N TROSY HSQCsample_2isotropicsample_conditions_1

Software:

VNMRJ, Varian - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

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