BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 19681

Title: NMR structure of E. coli LpoB   PubMed: 24691651

Authors: Egan, Alexander; Jean, Nicolas; Koumoutsi, Alexandra; Bougault, Catherine; Biboy, Jacob; Sassine, Jad; Solovyova, Alexandra; Breukink, Eefjan; Typas, Athanasios; Vollmer, Waldemar; Simorre, Jean-Pierre

Citation: Jean, Nicolas; Bougault, Catherine; Egan, Alexander; Vollmer, Waldemar; Simorre, Jean-Pierre. "Solution NMR assignment of LpoB, an outer-membrane anchored Penicillin-Binding Protein activator from Escherichia coli."  Biomol. NMR Assignments ., .-. (2014).

Assembly members:
LpoB, polymer, 197 residues, 20770.459 Da.

Natural source:   Common Name: E. 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):
LpoB: GSHMVGQREPAPVEEVKPAP EQPAEPQQPVPTVPSVPTIP QQPGPIEHEDQTAPPAPHIR HYDWNGAMQPMVSKMLGADG VTAGSVLLVDSVNNRTNGSL NAAEATETLRNALANNGKFT LVSAQQLSMAKQQLGLSPQD SLGTRSKAIGIARNVGAHYV LYSSASGNVNAPTLQMQLML VQTGEIIWSGKGAVSQQ

Data sets:
Data typeCount
13C chemical shifts756
15N chemical shifts197
1H chemical shifts1165

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1E. coli LpoB1

Entities:

Entity 1, E. coli LpoB 197 residues - 20770.459 Da.

Residues 1 to 4 are reminiscent of the hexahistidine-tag left after thrombine cleavage

1   GLYSERHISMETVALGLYGLNARGGLUPRO
2   ALAPROVALGLUGLUVALLYSPROALAPRO
3   GLUGLNPROALAGLUPROGLNGLNPROVAL
4   PROTHRVALPROSERVALPROTHRILEPRO
5   GLNGLNPROGLYPROILEGLUHISGLUASP
6   GLNTHRALAPROPROALAPROHISILEARG
7   HISTYRASPTRPASNGLYALAMETGLNPRO
8   METVALSERLYSMETLEUGLYALAASPGLY
9   VALTHRALAGLYSERVALLEULEUVALASP
10   SERVALASNASNARGTHRASNGLYSERLEU
11   ASNALAALAGLUALATHRGLUTHRLEUARG
12   ASNALALEUALAASNASNGLYLYSPHETHR
13   LEUVALSERALAGLNGLNLEUSERMETALA
14   LYSGLNGLNLEUGLYLEUSERPROGLNASP
15   SERLEUGLYTHRARGSERLYSALAILEGLY
16   ILEALAARGASNVALGLYALAHISTYRVAL
17   LEUTYRSERSERALASERGLYASNVALASN
18   ALAPROTHRLEUGLNMETGLNLEUMETLEU
19   VALGLNTHRGLYGLUILEILETRPSERGLY
20   LYSGLYALAVALSERGLNGLN

Samples:

LpoB(sol): LpoB, [U-100% 13C; U-100% 15N], 0.8 mM; CH3COOH/CH3COONa buffer 100.0 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 0.100 M; pH: 5.000; pressure: 1.000 atm; temperature: 308.000 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCLpoB(sol)isotropicsample_conditions_1
3D HNCOLpoB(sol)isotropicsample_conditions_1
3D HN(CA)COLpoB(sol)isotropicsample_conditions_1
3D BEST-HNCACBLpoB(sol)isotropicsample_conditions_1
3D BEST-HN(CO)CACBLpoB(sol)isotropicsample_conditions_1
3D HN(COCA)N(H)LpoB(sol)isotropicsample_conditions_1
2D Pro-HN(COCAN)LpoB(sol)isotropicsample_conditions_1
2D Pro-iHN(CAN)LpoB(sol)isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticLpoB(sol)isotropicsample_conditions_1
2D 1H-13C HSQC aromaticLpoB(sol)isotropicsample_conditions_1
2D methyl 1H-13C-CT-HSQCLpoB(sol)isotropicsample_conditions_1
2D 1H-15N HMQC optimized for His sidechainsLpoB(sol)isotropicsample_conditions_1
3D H(C)CH-TOCSYLpoB(sol)isotropicsample_conditions_1
3D H(CCO)NHLpoB(sol)isotropicsample_conditions_1
3D C(CO)NHLpoB(sol)isotropicsample_conditions_1
3D 1H-15N NOESYLpoB(sol)isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticLpoB(sol)isotropicsample_conditions_1
3D 1H-13C NOESY aromaticLpoB(sol)isotropicsample_conditions_1
3D methyl 1H-13C NOESYLpoB(sol)isotropicsample_conditions_1
Heteronuclear 1H-15N NOELpoB(sol)isotropicsample_conditions_1

Software:

Aria v2.3.1, Linge, O, http://aria.pasteur.fr/ - structure calculation

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - Refinement

CcpNmr_Analysis v2.2, CCPN - data analysis

Talos+, Yang Shen, Frank Delaglio, Gabriel Cornilescu, and Ad Bax - data analysis

Unio10' v2.0.2, Torsten Herrmann - peakpicking

nmrDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

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

NMR spectrometers:

  • Varian vnmrs 800 MHz
  • Varian vnmrs 600 MHz
  • Bruker US2 950 MHz

Related Database Links:

UNP P0AB38
PDB
DBJ BAA35912 BAB34906 BAG76694 BAI24739 BAI29989
EMBL CAP75597 CAQ31626 CAQ98004 CAR02445 CAR07449
GB AAC74189 AAG55851 AAN79848 AAP16615 AAZ87850
REF NP_309510 NP_415623 WP_000164436 WP_000164438 WP_000164439
SP P0AB38 P0AB39 Q3Z312