BMRB Entry 25281

Title:
NMR STRUCTURE OF YERSINIA PESTIS AIL (ATTACHMENT INVASION LOCUS) IN DECYLPHOSPHOCHOLINE MICELLES
Deposition date:
2014-10-10
Original release date:
2015-07-20
Authors:
Ding, Yi; Yao, Yong; Fujimoto, Lynn; Marassi, Francesca
Citation:

Citation: Marassi, Francesca; Ding, Yi; Schwieters, C.; Tian, Y.; Yao, Yong. "Backbone structure of Yersinia pestis Ail determined in micelles by NMR-restrained simulated annealing with implicit membrane solvation"  J. Biomol. NMR ., .-. (2015).

Assembly members:

Assembly members:
ATTACHMENT_INVASION_LOCUS_PROTEIN, polymer, 156 residues, 17492.549 Da.

Natural source:

Natural source:   Common Name: enterobacteria   Taxonomy ID: 187410   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Yersinia pestis

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-30b

Experimental source:

Natural source:   Common Name: enterobacteria   Taxonomy ID: 187410   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Yersinia pestis

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-30b

Data sets:
Data typeCount
13C chemical shifts280
15N chemical shifts146
1H chemical shifts146

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 156 residues - 17492.549 Da.

Residues 1-156 represent the mature sequence of the membrane protein after cleavage of the N-terminal signal sequence

1   GLUGLYGLUSERSERILESERILEGLYTYR
2   ALAGLNSERARGVALLYSGLUASPGLYTYR
3   LYSLEUASPLYSASNPROARGGLYPHEASN
4   LEULYSTYRARGTYRGLUPHEASNASNASP
5   TRPGLYVALILEGLYSERPHEALAGLNTHR
6   ARGARGGLYPHEGLUGLUSERVALASPGLY
7   PHELYSLEUILEASPGLYASPPHELYSTYR
8   TYRSERVALTHRALAGLYPROVALPHEARG
9   ILEASNGLUTYRVALSERLEUTYRGLYLEU
10   LEUGLYALAGLYHISGLYLYSALALYSPHE
11   SERSERILEPHEGLYGLNSERGLUSERARG
12   SERLYSTHRSERLEUALATYRGLYALAGLY
13   LEUGLNPHEASNPROHISPROASNPHEVAL
14   ILEASPALASERTYRGLUTYRSERLYSLEU
15   ASPASPVALLYSVALGLYTHRTRPMETLEU
16   GLYALAGLYTYRARGPHE

Samples:

sample_1: ATTACHMENT INVASION LOCUS PROTEIN, [U-13C; U-15N], 0.5 mM; potassium phosphate 20 mM; sodium chloride 5 mM; decylphosphocholine 170 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 25 mM; pH: 6.8; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

X-PLOR_NIH v2.36, Schwieters, Kuszewski, Tjandra and Clore - structure solution

TALOS vTALOS+, Cornilescu, Delaglio and Bax - chemical shift calculation

SPARKY, Goddard - data analysis

NMRView, Johnson, One Moon Scientific - chemical shift assignment

WhatIF, Vriend - structure validation

ProcheckNMR, Laskowski and MacArthur - structure validation

MolProbity, Chen, Arendall, Headd, Keedy, Immormino, Kapral, Murray, Richardson and Richardson - structure validation

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

NCBI NP_668646
UNP Q8D0Z7
PDB
DBJ GAE10604
EMBL CAH22105 CAL21516 CCC18813 CFQ79902 CFU96389
GB AAB36601 AAM84897 AAS62746 ABG14310 ABG17563
REF WP_002222198 WP_002227864 WP_012104793 WP_012229027 WP_012303842
SP Q56957
AlphaFold Q56957

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