BMRB Entry 16684

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16684
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Structural homology between the C-terminal domain of the PapC usher and its plug
Deposition date:
2010-01-19
Original release date:
2010-01-27
Authors:
Ford, Bradley; Rego, Ana Toste; Ragan, Timothy; Pinkner, Jerome; Dodson, Karen; Driscoll, Paul; Hultgren, Scott; Waksman, Gabriel
Citation:

Citation: Ford, Bradley; Rego, Ana Toste; Ragan, Timothy; Pinkner, Jerome; Dodson, Karen; Driscoll, Paul; Hultgren, Scott; Waksman, Gabriel. "Structural Homology between the C-Terminal Domain of the PapC Usher and Its Plug."  J. Bacteriol. 192, 1824-1831 (2010).
PubMed: 20118254

Assembly members:

Assembly members:
CTD_Actual, polymer, 95 residues, 10261.6904 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CTD_Actual: VLKGKRLFAILRLADGSQPP FGASVTSEKGRELGMVADEG LAWLSGVTPGETLSVNWDGK IQCQVNVPETAISDQQLLLP CTPQKSAWSHPQFEK

Data typeCount
13C chemical shifts308
15N chemical shifts91
1H chemical shifts496

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CTD Actual1

Entities:

Entity 1, CTD Actual 95 residues - 10261.6904 Da.

1   VALLEULYSGLYLYSARGLEUPHEALAILE
2   LEUARGLEUALAASPGLYSERGLNPROPRO
3   PHEGLYALASERVALTHRSERGLULYSGLY
4   ARGGLULEUGLYMETVALALAASPGLUGLY
5   LEUALATRPLEUSERGLYVALTHRPROGLY
6   GLUTHRLEUSERVALASNTRPASPGLYLYS
7   ILEGLNCYSGLNVALASNVALPROGLUTHR
8   ALAILESERASPGLNGLNLEULEULEUPRO
9   CYSTHRPROGLNLYSSERALATRPSERHIS
10   PROGLNPHEGLULYS

Samples:

15N: MES 20 mM; sodium chloride 20 mM; CTD_Actual, [U-15N], 300-500 mM

13C15N: MES 20 mM; sodium chloride 20 mM; CTD_Actual, [U-13C; U-15N], 300-500 mM

Standard_Conditions: pH: 6.5; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15NisotropicStandard_Conditions
3D HNCA13C15NisotropicStandard_Conditions
3D HN(CO)CA13C15NisotropicStandard_Conditions
3D HNCO13C15NisotropicStandard_Conditions
HN(Ca)Co13C15NisotropicStandard_Conditions
CbCa(Co)NH13C15NisotropicStandard_Conditions
3D HNCACB13C15NisotropicStandard_Conditions
3D 1H-15N TOCSY short15NisotropicStandard_Conditions
3D 1H-15N TOCSY long15NisotropicStandard_Conditions
3D HCCH-TOCSY13C15NisotropicStandard_Conditions
TSNoesy_N13C15NisotropicStandard_Conditions
3D 1H-13C NOESY13C15NisotropicStandard_Conditions
3D HN(CO)CA13C15NisotropicStandard_Conditions
CBCAcoNH13C15NisotropicStandard_Conditions
2D 1H-1H NOESY15NisotropicStandard_Conditions

Software:

ANALYSIS v2.1, CCPN - chemical shift assignment, peak picking

DANGLE v1.1, 1 - data analysis

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

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Varian Unity 600 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz

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