BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 17431

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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/BMR17431
MolProbity Validation Chart

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Title: Solution structure of the E. coli outer membrane protein RcsF (periplasmatic domain)   PubMed: 21471196

Deposition date: 2011-01-27 Original release date: 2011-04-08

Authors: Rogov, Vladimir; Doetsch, Volker; Rogova, Natalia; Bernhard, Frank; Loehr, Frank

Citation: Rogov, Vladimir; Rogova, Natalia Yu; Bernhard, Frank; Lohr, Frank; Dotsch, Volker. "A Disulfide Bridge Network within the Soluble Periplasmic Domain Determines Structure and Function of the Outer Membrane Protein RCSF."  J. Biol. Chem. 286, 18775-18783 (2011).

Assembly members:
RcsF, polymer, 105 residues, 11121.772 Da.

Natural source:   Common Name: Escherichia 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):
RcsF: MAPQPKAEPAKPKAPRATPV RIYTNAEELVGKPFRDLGEV SGDSCQASNQDSPPSIPTAR KRMQINASKMKANAVLLHSC EVTSGTPGCYRQAVCIGSAL NITAK

Data sets:
Data typeCount
13C chemical shifts403
15N chemical shifts86
1H chemical shifts612

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1RcsF1

Entities:

Entity 1, RcsF 105 residues - 11121.772 Da.

Residues 1 represent a non-native cloning artefact

1   METALAPROGLNPROLYSALAGLUPROALA
2   LYSPROLYSALAPROARGALATHRPROVAL
3   ARGILETYRTHRASNALAGLUGLULEUVAL
4   GLYLYSPROPHEARGASPLEUGLYGLUVAL
5   SERGLYASPSERCYSGLNALASERASNGLN
6   ASPSERPROPROSERILEPROTHRALAARG
7   LYSARGMETGLNILEASNALASERLYSMET
8   LYSALAASNALAVALLEULEUHISSERCYS
9   GLUVALTHRSERGLYTHRPROGLYCYSTYR
10   ARGGLNALAVALCYSILEGLYSERALALEU
11   ASNILETHRALALYS

Samples:

sample_1: RcsF(31-134), [U-98% 13C; U-98% 15N], 0.6 ± 0.05 mM; sodium phosphate 50 mM; sodium chloride 100 mM; protease inhibitors cocktail 4.6 mM; DSS 0.3 mM

sample_conditions_1: ionic strength: 0.100 M; pH: 7.0; 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 HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D (HCA)CO(CA)NHsample_1isotropicsample_conditions_1
3D H(CC)(CO)NH-TOCSYsample_1isotropicsample_conditions_1
3D (H)CC(CO)NH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2., Bruker Biospin - collection, processing

SPARKY v112, Goddard - data analysis

CYANA v1.0.5, Guntert, Mumenthaler and Wuthrich - structure solution

ARIA v1, Linge, O, . - refinement

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAA03656 BAA77873 BAB33621 BAG75722 BAI23558
EMBL CAP74766 CAQ30711 CAQ87800 CAQ97085 CAR01572
GB AAA24508 AAB08624 AAC73307 AAG54498 AAN41849
REF NP_308225 NP_414738 NP_706142 WP_001202318 WP_001202319
SP P69411 P69412

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