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BMRB Entry 16164

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16164
MolProbity Validation Chart

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Title: Solution structure of XcpT, the main component of the type 2 secretion system of Pseudomonas aeruginosa   PubMed: 19747550

Deposition date: 2009-02-10 Original release date: 2009-10-16

Authors: Alphonse, Sebastien; Durand, Eric; Douzi, Badreddine; Darbon, Herve; Filloux, Alain; Voulhoux, Rome; Bernard, Cedric

Citation: Alphonse, Sebastien; Durand, Eric; Douzi, Badreddine; Waegele, Brigitte; Darbon, Herve; Filloux, Alain; Voulhoux, Rome; Bernard, Cedric. "Structure of the Pseudomonas aeruginosa XcpT pseudopilin, a major component of the type II secretion system."  J. Struct. Biol. 169, 75-80 (2010).

Assembly members:
XcpT, polymer, 110 residues, 11957.407 Da.

Natural source:   Common Name: Pseudomonas aeruginosa   Taxonomy ID: 287   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pseudomonas aeruginosa

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

Entity Sequences (FASTA):
XcpT: MSRPDQAKVTVAKGDIKAIA AALDMYKLDNFAYPSTQQGL EALVKKPTGNPQPKNWNKDG YLKKLPVDPWGNPYQYLAPG TKGPFDLYSLGADGKEGGSD NDADIGNWDN

Data sets:
Data typeCount
13C chemical shifts387
15N chemical shifts116
1H chemical shifts716

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1XcpT1

Entities:

Entity 1, XcpT 110 residues - 11957.407 Da.

1   METSERARGPROASPGLNALALYSVALTHR
2   VALALALYSGLYASPILELYSALAILEALA
3   ALAALALEUASPMETTYRLYSLEUASPASN
4   PHEALATYRPROSERTHRGLNGLNGLYLEU
5   GLUALALEUVALLYSLYSPROTHRGLYASN
6   PROGLNPROLYSASNTRPASNLYSASPGLY
7   TYRLEULYSLYSLEUPROVALASPPROTRP
8   GLYASNPROTYRGLNTYRLEUALAPROGLY
9   THRLYSGLYPROPHEASPLEUTYRSERLEU
10   GLYALAASPGLYLYSGLUGLYGLYSERASP
11   ASNASPALAASPILEGLYASNTRPASPASN

Samples:

sample_cold: XcpT 1.3 mM; sodium phosphate 50 mM; sodium chloride 150 mM

sample_15N: XcpT, [U-15N], 0.9 mM; sodium phosphate 50 mM; sodium chloride 150 mM

sample_15N-d2O: XcpT, [U-15N], 0.9 mM; sodium phosphate 50 mM; sodium chloride 150 mM

sample_15N-13C: XcpT, [U-13C; U-15N], 0.9 mM; sodium phosphate 50 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 200 mM; pH: 7; pressure: 1.0 atm; temperature: 290 K

sample_conditions_2: ionic strength: 200 mM; pH: 7; pressure: 1.0 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_coldisotropicsample_conditions_2
2D 1H-1H NOESYsample_coldisotropicsample_conditions_2
2D 1H-15N HSQCsample_15Nisotropicsample_conditions_1
2D 1H-13C HSQCsample_15N-13Cisotropicsample_conditions_1
3D CBCA(CO)NHsample_15N-13Cisotropicsample_conditions_1
3D HNCOsample_15N-13Cisotropicsample_conditions_1
3D HNCAsample_15N-13Cisotropicsample_conditions_1
3D HNCACBsample_15N-13Cisotropicsample_conditions_1
3D HBHA(CO)NHsample_15N-13Cisotropicsample_conditions_1
3D HN(CO)CAsample_15N-13Cisotropicsample_conditions_1
3D HCCH-TOCSYsample_15N-13Cisotropicsample_conditions_1
3D HNHAsample_15Nisotropicsample_conditions_1
3D 1H-15N NOESYsample_15Nisotropicsample_conditions_1
3D 1H-15N TOCSYsample_15Nisotropicsample_conditions_1
3D HNHBsample_15N-13Cisotropicsample_conditions_1
3D HCACOsample_15N-13Cisotropicsample_conditions_1
2D 1H-15N HSQCsample_15N-d2Oisotropicsample_conditions_1
2D 1H-1H NOESYsample_15N-d2Oisotropicsample_conditions_1

Software:

TOPSPIN v2.0, Bruker Biospin - collection

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

NMRView v5.2.2.01, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

TALOS v3.851, Cornilescu, Delaglio and Bax - geometry optimization

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

ProcheckNMR v3.4, Laskowski and MacArthur - data analysis

WhatIF v20080408-2247, Vriend - data analysis

QUEEN v1.1, Nabuurs, Spronk, Krieger, Maassen, Vriend and Vuister - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 500 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
DBJ BAK91055 BAP22292 BAP49919 BAQ38804 BAR66863
EMBL CAA44535 CAW26687 CCQ87087 CDH70211 CDH76300
GB AAA25946 AAG06489 AAT49508 ABJ12333 ABR84270
REF NP_251791 WP_003119751 WP_042115257 WP_042159357 WP_045175661
SP Q00514

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