BMRB Entry 30158

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30158
MolProbity Validation Chart

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Title:
Solution-state NMR structural ensemble of NPr (1-85) refined with RDCs and PCS
Deposition date:
2016-08-19
Original release date:
2016-11-14
Authors:
Strickland, M.; Wang, G.; Peterkofsky, A.; Tjandra, N.
Citation:

Citation: Strickland, Madeleine; Stanley, Ann Marie; Wang, Guangshun; Botos, Istvan; Schwieters, Charles; Buchanan, Susan; Peterkofsky, Alan; Tjandra, Nico. "Structure of the NPr:EINNtr Complex: Mechanism for Specificity in Paralogous Phosphotransferase Systems"  Structure 24, 2127-2137 (2016).
PubMed: 27839951

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETDuet1

Entity Sequences (FASTA):

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

Data sets:
Data typeCount
13C chemical shifts152
15N chemical shifts74
1H chemical shifts74

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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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_2: EDTA 0.5 mM; NPr, [U-13C; U-15N; U-2H], 0.6 mM; TRIS 10 mM; sodium chloride 100 mM

sample_3: EDTA 0.5 mM; NPr, [U-13C; U-15N; U-2H], 0.6 mM; TRIS 10 mM; sodium chloride 100 mM

sample_4: EDTA 0.5 mM; NPr, [U-15N; U-2H], 0.6 mM; TRIS 10 mM; sodium chloride 100 mM

sample_5: EDTA 0.5 mM; NPr, [U-15N; U-2H], 0.6 mM; TRIS 10 mM; sodium chloride 100 mM

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

sample_conditions_2: ionic strength: 108 mM; pH: 7.5; pressure: 1 atm; temperature: 300 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_3isotropicsample_conditions_1
2D IPAPsample_3isotropicsample_conditions_2
2D IPAPsample_2anisotropicsample_conditions_2
3D HNCACBsample_3isotropicsample_conditions_2
2D 1H-15N HSQCsample_5anisotropicsample_conditions_2
2D 1H-15N HSQCsample_4isotropicsample_conditions_2

Software:

Analysis v2.4.2, CCPN - chemical shift assignment, peak picking

Gaussian v9, Gaussian, Inc. - geometry optimization

NMRPipe v8.2, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

PIPP, Garrett - chemical shift assignment, peak picking

TALOS-N v4.12, Cornilescu, Delaglio and Bax - data analysis

TOPSPIN v3.0, Bruker Biospin - collection

VNMR, Varian - collection

X-PLOR NIH v2.37.7, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

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