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 30157

Title: NMR structure of the E. coli protein NPr, residues 1-85   PubMed: 18421563

Deposition date: 2016-08-18 Original release date: 2016-09-23

Authors: Wang, G.; Li, X.; Peterkofsky, A.

Citation: Li, X.; Peterkofsky, A.; Wang, G.. "Solution structure of NPr, a bacterial signal-transducing protein that controls the phosphorylation state of the potassium transporter-regulating protein IIA Ntr."  Amino Acids 35, 531-539 (2008).

Assembly members:
entity_1, polymer, 85 residues, 9254.570 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 83334   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity_1: MTVKQTVEITNKLGMHARPA MKLFELMQGFDAEVLLRNDE GTEAEANSVIALLMLDSAKG RQIEVEATGPQEEEALAAVI ALFNS

Data sets:
Data typeCount
13C chemical shifts312
15N chemical shifts88
1H chemical shifts417

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 85 residues - 9254.570 Da.

1   METTHRVALLYSGLNTHRVALGLUILETHR
2   ASNLYSLEUGLYMETHISALAARGPROALA
3   METLYSLEUPHEGLULEUMETGLNGLYPHE
4   ASPALAGLUVALLEULEUARGASNASPGLU
5   GLYTHRGLUALAGLUALAASNSERVALILE
6   ALALEULEUMETLEUASPSERALALYSGLY
7   ARGGLNILEGLUVALGLUALATHRGLYPRO
8   GLNGLUGLUGLUALALEUALAALAVALILE
9   ALALEUPHEASNSER

Samples:

sample_1: NPr, [U-13C; U-15N], 1 mM; Tris 25 mM

sample_conditions_1: ionic strength: 25 mM; pH: 7; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
4D HNHC NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

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

PIPP, Garrett - chemical shift assignment, peak picking

TALOS, Cornilescu, Delaglio and Bax - data analysis

VNMR, Varian - collection

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • 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