BMRB Entry 25918

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25918
MolProbity Validation Chart

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Title:
Solution NMR structure of Erythrobacter litoralis PhyR response regulator REC domain
Deposition date:
2015-12-09
Original release date:
2016-09-01
Authors:
Correa, Fernando; Gardner, Kevin
Citation:

Citation: Correa, Fernando; Gardner, Kevin. "Basis of Mutual Domain Inhibition in a Bacterial Response Regulator"  Cell Chem. Biol. S2451-9456, 30240-30249 (2016).
PubMed: 27524295

Assembly members:

Assembly members:
entity, polymer, 129 residues, 13823.661 Da.

Natural source:

Natural source:   Common Name: a-proteobacteria   Taxonomy ID: 39660   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Erythrobacter litoralis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GAMGSTNVLIIEDEPLISMQ LEDLVRSLGHDIAGTAATRT QAQEAVAKEKPGLVLADIQL ADGSSGIDAVEDILGQFDVP VIFITAYPERLLTGDRPEPT YLVTKPFQESTVRTTISQAL FFQNSPTAV

Data sets:
Data typeCount
13C chemical shifts557
15N chemical shifts131
1H chemical shifts913

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 129 residues - 13823.661 Da.

1   GLYALAMETGLYSERTHRASNVALLEUILE
2   ILEGLUASPGLUPROLEUILESERMETGLN
3   LEUGLUASPLEUVALARGSERLEUGLYHIS
4   ASPILEALAGLYTHRALAALATHRARGTHR
5   GLNALAGLNGLUALAVALALALYSGLULYS
6   PROGLYLEUVALLEUALAASPILEGLNLEU
7   ALAASPGLYSERSERGLYILEASPALAVAL
8   GLUASPILELEUGLYGLNPHEASPVALPRO
9   VALILEPHEILETHRALATYRPROGLUARG
10   LEULEUTHRGLYASPARGPROGLUPROTHR
11   TYRLEUVALTHRLYSPROPHEGLNGLUSER
12   THRVALARGTHRTHRILESERGLNALALEU
13   PHEPHEGLNASNSERPROTHRALAVAL

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 0.5 – 1 mM; TRIS 10 mM; sodium chloride 50 mM; H2O 90 mM; D2O 10 mM

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - chemical shift assignment, refinement, structure solution

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis

VNMRJ, Varian - collection

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 800 MHz

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