BMRB Entry 17747

Title:
Solution NMR Structure of Fumarate reductase flavoprotein subunit from Lactobacillus plantarum, Northeast Structural Genomics Consortium Target LpR145J
Deposition date:
2011-06-29
Original release date:
2011-08-03
Authors:
Liu, Gaohua; Tang, Yuefeng; Xiao, Rong; Janjua, Haleema; Ciccosanti, colleen; Wang, Huang; Acton, Thomas; Everett, John; Montelione, Gaetano
Citation:

Citation: Liu, Gaohua; Tang, Yuefeng; Xiao, Rong; Janjua, Haleema; Ciccosanti, colleen; Wang, Huang; Acton, Thomas; Everett, John; Montelione, Gaetano. "Northeast Structural Genomics Consortium Target LpR145J"  To be published ., .-..

Assembly members:

Assembly members:
LpR145J, polymer, 160 residues, 18527.973 Da.

Natural source:

Natural source:   Common Name: Lactobacillus plantarum   Taxonomy ID: 1590   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Lactobacillus plantarum

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET 21-23C

Data sets:
Data typeCount
13C chemical shifts676
15N chemical shifts143
1H chemical shifts1080

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1LpR145J1

Entities:

Entity 1, LpR145J 160 residues - 18527.973 Da.

1   METVALGLUPROGLYVALALALYSLEUTHR
2   THRTYRALASERLYSGLNALATHRASPMET
3   GLYALAILETYRVALASNSERLYSGLYASP
4   ARGILEVALASNGLUSERASNVALTYRTHR
5   THRPHEARGASNALAILELEULYSGLNALA
6   ASPLYSVALALATYRLEUVALMETASPGLU
7   ARGTHRTRPLYSLYSVALTYRASPLEULEU
8   ILELEUHISASPPHETHRPROGLUGLUILE
9   LYSSERPHEPHEGLUASNLYSGLYLYSARG
10   PROVALPHEVALLYSGLYSERLEUGLUSER
11   ALAALAGLUGLNALAGLYILEVALVALASP
12   GLULEUVALGLNTHRVALLYSASNTYRGLN
13   GLYTYRVALGLNASPGLYHISASPHISASP
14   PHEGLYARGASPPROLYSTYRLEUHISGLN
15   PHEGLUGLYGLUTHRPHETYRILEILEGLU
16   GLNARGLEUGLUHISHISHISHISHISHIS

Samples:

sample_NC: LpR145J, [U-100% 13C; U-100% 15N], 1.41 mM; H2O 90%; D2O 10%

sample_NC5: LpR145J, [U-100% 13C; U-100% 15N], 0.90 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_NCisotropicsample_conditions_1
2D 1H-13C HSQCsample_NCisotropicsample_conditions_1
3D HNCOsample_NCisotropicsample_conditions_1
3D CBCA(CO)NHsample_NCisotropicsample_conditions_1
3D HNCACBsample_NCisotropicsample_conditions_1
3D 1H-13C arom NOESYsample_NCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_NCisotropicsample_conditions_1
3D HCCH-TOCSYsample_NCisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_NC5isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

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

XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

SPARKY, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CCC80459 CDN28269
GB ACT63669 ADO00073 AGE37659 AGL65584 AGO09388
REF WP_003643070 WP_003643562 WP_003645691 WP_015641109 WP_021730084

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