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Biological Magnetic Resonance Data Bank


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BMRB Entry 18904

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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/BMR18904
MolProbity Validation Chart

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Title: NMR solution structure of the two domain PPIase SlpA from Escherichia coli

Deposition date: 2012-12-17 Original release date: 2013-12-16

Authors: Kovermann, Michael; Weininger, Ulrich; Balbach, Jochen

Citation: Kovermann, Michael; Geitner, Anne-Juliane; Weininger, Ulrich; Schmid, Franz-Xaver; Balbach, Jochen. "NMR solution structure of the two domain PPIase SlpA from Escherichia coli"  Not known ., .-..

Assembly members:
PPIase_SlpA, polymer, 148 residues, 16022.982 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):
PPIase_SlpA: MSESVQSNSAVLVHFTLKLD DGTTAESTRNNGKPALFRLG DASLSEGLEQHLLGLKVGDK TTFSLEPDAAFGVPSPDLIQ YFSRREFMDAGEPEIGAIML FTAMDGSEMPGVIREINGDS ITVDFNHPLAGQTVHFDIEV LEIDPALE

Data sets:
Data typeCount
13C chemical shifts466
15N chemical shifts151
1H chemical shifts1028

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1PPIase_SlpA1

Entities:

Entity 1, PPIase_SlpA 148 residues - 16022.982 Da.

1   METSERGLUSERVALGLNSERASNSERALA
2   VALLEUVALHISPHETHRLEULYSLEUASP
3   ASPGLYTHRTHRALAGLUSERTHRARGASN
4   ASNGLYLYSPROALALEUPHEARGLEUGLY
5   ASPALASERLEUSERGLUGLYLEUGLUGLN
6   HISLEULEUGLYLEULYSVALGLYASPLYS
7   THRTHRPHESERLEUGLUPROASPALAALA
8   PHEGLYVALPROSERPROASPLEUILEGLN
9   TYRPHESERARGARGGLUPHEMETASPALA
10   GLYGLUPROGLUILEGLYALAILEMETLEU
11   PHETHRALAMETASPGLYSERGLUMETPRO
12   GLYVALILEARGGLUILEASNGLYASPSER
13   ILETHRVALASPPHEASNHISPROLEUALA
14   GLYGLNTHRVALHISPHEASPILEGLUVAL
15   LEUGLUILEASPPROALALEUGLU

Samples:

sample_1: PPIase_SlpA, [U-99% 13C; U-99% 15N], 1 mM; potassium phosphate 100 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.3, Bruker Biospin - collection

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

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

ARIA, Linge, O, . - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAB33454 BAB96597 BAG75550 BAI23389 BAI28909
EMBL CAA38706 CAP74597 CAQ30548 CAQ87608 CAQ96919
GB AAC73139 AAG54330 AAN41690 AAN41691 AAN78532
REF NP_308058 NP_414569 NP_705983 NP_705984 WP_000004647
SP P0AEM0 P0AEM1 P0AEM2 P0AEM3

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