BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 18332

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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/BMR18332
MolProbity Validation Chart

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Title: E. coli Protein   PubMed: 22658749

Deposition date: 2012-03-16 Original release date: 2012-06-05

Authors: Prehna, Gerd; Zhang, Guijin; Gong, Xiandi; Duszyk, Marek; Okon, Mark; McIntosh, Lawrence; Weiner, Joel; Strynadka, Natalie

Citation: Prehna, Gerd; Zhang, Guijin; Gong, Xiandi; Duszyk, Marek; Okon, Mark; McIntosh, Lawrence; Weiner, Joel; Strynadka, Natalie. "A protein export pathway involving Escherichia coli porins."  Structure 20, 1154-1166 (2012).

Assembly members:
E_coli_protein, polymer, 99 residues, 11054.386 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
E_coli_protein: ANNETSKSVTFPKCEDLDAA GIAASVKRDYQQNRVARWAD DQKIVGQADPVAWVSLQDIQ GKDDKWSVPLTVRGKSADIH YQVSVDCKAGMAEYQRRLE

Data sets:
Data typeCount
13C chemical shifts239
15N chemical shifts67
1H chemical shifts462

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Escherichia coli Porins1

Entities:

Entity 1, Escherichia coli Porins 99 residues - 11054.386 Da.

1   ALAASNASNGLUTHRSERLYSSERVALTHR
2   PHEPROLYSCYSGLUASPLEUASPALAALA
3   GLYILEALAALASERVALLYSARGASPTYR
4   GLNGLNASNARGVALALAARGTRPALAASP
5   ASPGLNLYSILEVALGLYGLNALAASPPRO
6   VALALATRPVALSERLEUGLNASPILEGLN
7   GLYLYSASPASPLYSTRPSERVALPROLEU
8   THRVALARGGLYLYSSERALAASPILEHIS
9   TYRGLNVALSERVALASPCYSLYSALAGLY
10   METALAGLUTYRGLNARGARGLEUGLU

Samples:

sample_1: E coli protein, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; HEPES 50 mM; sodium chloride 100 mM; TCEP 0.1 mM; PMSF 0.1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
CCC-TOCSY-NNHsample_1isotropicsample_conditions_1
HCC-TOCSY-NNHsample_1isotropicsample_conditions_1
(HB)CB(CGCD)HD-aromaticsample_1isotropicsample_conditions_1
HBGCBGCCBGCACONNHsample_1isotropicsample_conditions_1
CT-HSQCsample_1isotropicsample_conditions_1

Software:

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

NMRDraw, Johnson, One Moon Scientific - data analysis, processing

SPARKY, Goddard - chemical shift assignment, peak picking

TALOS, Cornilescu, Delaglio and Bax - geometry optimization, structure solution

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Varian Unity 500 MHz
  • Varian Unity 600 MHz

Related Database Links:

PDB
DBJ BAA15653 BAB35980 BAG77546 BAI25924 BAI36219
EMBL CAP76337 CAQ32323 CAQ98773 CAR03207 CAR08244
GB AAA23859 AAC74917 AAG56837 AAN43416 AAN80718
REF NP_310584 NP_416361 NP_707709 WP_000414411 WP_000745667
SP P33219 Q322G8 Q3Z2J8 Q83KS1 Q8CVZ5

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