BMRB Entry 18823

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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/BMR18823
MolProbity Validation Chart

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Title:
1H, 13C and 15N resonance assignments of the C-terminal domain of PpdD
Deposition date:
2012-11-06
Original release date:
2013-01-29
Authors:
Amorim, Gisele; Cisneros, David; Delepierre, Muriel; Francetic, Olivera; Izadi-Pruneyre, Nadia
Citation:

Citation: Amorim, Gisele; Cisneros, David; Delepierre, Muriel; Francetic, Olivera; Izadi-Pruneyre, Nadia. "(1)H, (15)N and (13)C resonance assignments of PpdD, a type IV pilin from enterohemorrhagic Escherichia coli."  Biomol. NMR Assignments ., .-. (2012).
PubMed: 23242787

Assembly members:

Assembly members:
PpdD, polymer, 132 residues, 14227.7895 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PpdD: MENYLRKAALTDMLQTFVPY RTAVELCALEHGGLDTCDGG SNGIPSPTTTRYVSAMSVAK GVVSLTGQESLNGLSVVMTP GWDNANGVTGWARNCNIQSD SALQQACEDVFRFDDANLVP RGSGLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts460
15N chemical shifts124
1H chemical shifts759

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1prepilin peptidase-dependent protein D1

Entities:

Entity 1, prepilin peptidase-dependent protein D 132 residues - 14227.7895 Da.

1   METGLUASNTYRLEUARGLYSALAALALEU
2   THRASPMETLEUGLNTHRPHEVALPROTYR
3   ARGTHRALAVALGLULEUCYSALALEUGLU
4   HISGLYGLYLEUASPTHRCYSASPGLYGLY
5   SERASNGLYILEPROSERPROTHRTHRTHR
6   ARGTYRVALSERALAMETSERVALALALYS
7   GLYVALVALSERLEUTHRGLYGLNGLUSER
8   LEUASNGLYLEUSERVALVALMETTHRPRO
9   GLYTRPASPASNALAASNGLYVALTHRGLY
10   TRPALAARGASNCYSASNILEGLNSERASP
11   SERALALEUGLNGLNALACYSGLUASPVAL
12   PHEARGPHEASPASPALAASNLEUVALPRO
13   ARGGLYSERGLYLEUGLUHISHISHISHIS
14   HISHIS

Samples:

sample_1: PpdD, [U-13C; U-15N], 0.9 mM; sodium phosphate 50 mM; sodium chloride 50 mM; D2O 15%

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CcpNnmr_Analysis v2.1, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

DBJ BAB33535 BAB96678 BAG75632 BAI23471 BAI34110
EMBL CAQ30623 CAR01475 CAR06329 CAR11328 CAR16249
GB AAC36923 AAC73219 AAG54412 AAN41769 AAP15650
REF NP_308139 NP_414650 NP_706062 WP_000360887 WP_000360895
SP P36647
AlphaFold P36647

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