BMRB Entry 25776

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25776
MolProbity Validation Chart

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Title:
Solution NMR structure of Outer Membrane Protein G P92A mutant from Pseudomonas aeruginosa
Deposition date:
2015-08-27
Original release date:
2015-12-28
Authors:
Kucharska, Iga; Seelheim, Patrick; Edrington, Thomas; Liang, Binyong; Tamm, Lukas
Citation:

Citation: Kucharska, Iga; Seelheim, Patrick; Edrington, Thomas; Liang, Binyong; Tamm, Lukas. "OprG Harnesses the Dynamics of its Extracellular Loops to Transport Small Amino Acids across the Outer Membrane of Pseudomonas aeruginosa"  Structure 23, 2234-2245 (2015).
PubMed: 26655471

Assembly members:

Assembly members:
entity, polymer, 215 residues, 22998.037 Da.

Natural source:

Natural source:   Common Name: g-proteobacteria   Taxonomy ID: 287   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pseudomonas aeruginosa

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: Pet30a+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MHKAGDFIIRGGFATVDPDD SSSDIKLDGAKQRGTKATVD SDTQLGLTFTYMFADKWGVE LVAATPFNHQVDVKGLGPGL DGKLADIKQLPATLLLQYYP MGGTNSAFQPYGGLGVNYTT FFDEDLASNRKAQGFSSMKL QDSWGLAGELGFDYMLNEHA LFNMAVWYMDIDTKASINGP SALGVNKTKVDVDVDPWVYM IGFGYKFLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts488
15N chemical shifts155
1H chemical shifts155

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 215 residues - 22998.037 Da.

1   METHISLYSALAGLYASPPHEILEILEARG
2   GLYGLYPHEALATHRVALASPPROASPASP
3   SERSERSERASPILELYSLEUASPGLYALA
4   LYSGLNARGGLYTHRLYSALATHRVALASP
5   SERASPTHRGLNLEUGLYLEUTHRPHETHR
6   TYRMETPHEALAASPLYSTRPGLYVALGLU
7   LEUVALALAALATHRPROPHEASNHISGLN
8   VALASPVALLYSGLYLEUGLYPROGLYLEU
9   ASPGLYLYSLEUALAASPILELYSGLNLEU
10   PROALATHRLEULEULEUGLNTYRTYRPRO
11   METGLYGLYTHRASNSERALAPHEGLNPRO
12   TYRGLYGLYLEUGLYVALASNTYRTHRTHR
13   PHEPHEASPGLUASPLEUALASERASNARG
14   LYSALAGLNGLYPHESERSERMETLYSLEU
15   GLNASPSERTRPGLYLEUALAGLYGLULEU
16   GLYPHEASPTYRMETLEUASNGLUHISALA
17   LEUPHEASNMETALAVALTRPTYRMETASP
18   ILEASPTHRLYSALASERILEASNGLYPRO
19   SERALALEUGLYVALASNLYSTHRLYSVAL
20   ASPVALASPVALASPPROTRPVALTYRMET
21   ILEGLYPHEGLYTYRLYSPHELEUGLUHIS
22   HISHISHISHISHIS

Samples:

sample_1: entity, [U-13C; U-15N; U-2H], 1 mM; sodium phosphate 25 mM; potassium chloride 50 mM; sodium azide 0.05%; 1,2-dihexanoyl-sn-glycero-3-phosphocholine 0.9%; H2O 90%; D2O 10%

sample_2: entity, [U-13C; U-15N; U-2H], 1 mM; sodium phosphate 25 mM; potassium chloride 50 mM; sodium azide 0.05%; 1,2-dihexanoyl-sn-glycero-3-phosphocholine 0.9%; D2O 100%

sample_3: entity 1 mM; sodium phosphate 25 mM; potassium chloride 50 mM; sodium azide 0.05%; 1,2-dihexanoyl-sn-glycero-3-phosphocholine 0.9%; H2O 90%; D2O 10%

sample_4: entity 1 mM; sodium phosphate 25 mM; potassium chloride 50 mM; sodium azide 0.05%; 1,2-dihexanoyl-sn-glycero-3-phosphocholine 0.9%; H2O 90%; D2O 10%

sample_5: entity 1 mM; sodium phosphate 25 mM; potassium chloride 50 mM; sodium azide 0.05%; 1,2-dihexanoyl-sn-glycero-3-phosphocholine 0.9%; H2O 90%; D2O 10%

sample_6: entity 1 mM; sodium phosphate 25 mM; potassium chloride 50 mM; sodium azide 0.05%; 1,2-dihexanoyl-sn-glycero-3-phosphocholine 0.9%; H2O 90%; D2O 10%

sample_7: entity, [U-15N]-Leu, 1 mM; sodium phosphate 25 mM; potassium chloride 50 mM; sodium azide 0.05%; 1,2-dihexanoyl-sn-glycero-3-phosphocholine 0.9%; H2O 90%; D2O 10%

sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H 15N TROSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCBsample_1isotropicsample_conditions_1
3D HNCA(CO)sample_1isotropicsample_conditions_1
2D 1H 15N TROSYsample_2isotropicsample_conditions_1
2D 1H 15N TROSYsample_3isotropicsample_conditions_1
2D 1H 15N TROSYsample_4isotropicsample_conditions_1
2D 1H 15N TROSYsample_5isotropicsample_conditions_1
2D 1H 15N TROSYsample_6isotropicsample_conditions_1
2D 1H 15N TROSYsample_7isotropicsample_conditions_1
3D 15N 1H 1H NOESY TROSYsample_1isotropicsample_conditions_1
4D 15N 1H 15N HSQC NOESY HSQCsample_1isotropicsample_conditions_1

Software:

TALOS vTalos+, Yang Shen, Frank Delaglio, Gabriel Cornilescu, and Ad Bax - rediction of Protein Backbone Torsion Angles from NMR Chemical Shifts

SPARKY, T. D. Goddard and D. G. Kneller - NMR assignments

CNS v1.2, Brunger, A.T et al - structure solution

Bruker_TopSpin v2.1.6, Bruker - collection

NMRPipe, F. Delaglio, S. Grzesiek, G. W. Vuister, G. Zhu, J. Pfeifer and A. Bax - processing

NMR spectrometers:

  • Bruker Bruker Avance III 800 MHz

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