BMRB Entry 25342

Title:
NMR structure of the protein YP_193882.1 from Lactobacillus acidophilus NCFM in presence of FMN
Deposition date:
2014-11-13
Original release date:
2014-12-08
Authors:
Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt
Citation:

Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the protein YP_193882.1 from Lactobacillus acidophilus NCFM in presence of FMN"  .

Assembly members:

Assembly members:
entity, polymer, 151 residues, 17079.189 Da.
FLAVIN MONONUCLEOTIDE, non-polymer, 456.344 Da.

Natural source:

Natural source:   Common Name: firmicutes   Taxonomy ID: 272621   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Lactobacillus acidophilus

Experimental source:

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

Data sets:
Data typeCount
1H chemical shifts1024
13C chemical shifts607
15N chemical shifts161

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1
2Flavin Mononucleotide2

Entities:

Entity 1, entity 151 residues - 17079.189 Da.

1   GLYMETALALYSLYSTHRLEUILELEUTYR
2   TYRSERTRPSERGLYGLUTHRLYSLYSMET
3   ALAGLULYSILEASNSERGLUILELYSASP
4   SERGLULEULYSGLUVALLYSVALSERGLU
5   GLYTHRPHEASPALAASPMETTYRLYSTHR
6   SERASPILEALALEUASPGLNILEGLNGLY
7   ASNLYSASPPHEPROGLUILEGLNLEUASP
8   ASNILEASPTYRASNASNTYRASPLEUILE
9   LEUILEGLYSERPROVALTRPSERGLYTYR
10   PROALATHRPROILELYSTHRLEULEUASP
11   GLNMETLYSASNTYRARGGLYGLUVALALA
12   SERPHEPHETHRSERALAGLYTHRASNHIS
13   LYSALATYRVALSERHISPHEASNGLUTRP
14   ALAASPGLYLEUASNVALILEGLYVALALA
15   ARGASPASPSERGLUVALASPLYSTRPSER
16   LYS

Entity 2, Flavin Mononucleotide - C17 H21 N4 O9 P - 456.344 Da.

1   FMN

Samples:

sample_1: entity, [U-99% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM; H2O 95%; D2O 5%

sample_conditions_1: temperature: 298 K; pH: 6.0; pressure: 1 atm; ionic strength: 0.0798 M

Experiments:

NameSampleSample stateSample conditions
APSY 4D-HACANHsample_1isotropicsample_conditions_1
APSY 5D-HACACONHsample_1isotropicsample_conditions_1
APSY 5D-CBCACONHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

CYANA v3.0, G ntert P., Herrmann, Guntert and Wuthrich - refinement, peak picking, chemical shift assignment, structure solution

TOPSPIN v3.1, Bruker Biospin - collection, processing

PROSA, Guntert - processing

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - geometry optimization

j-UNIO, Herrmann, Volk, Fiorito, Damberger, Guntert and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
BMRB 25567
EMBL CDF67787 CDF69462 CDF71219 CDF73047 CDF75037
GB AAV42851 AGK94185 AJP46408 EEJ75695 KHE30356
REF WP_003547179 WP_021874216 YP_193882

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