BMRB Entry 16563

Title:
Solution NMR structure of Lin0431 protein from Listeria innocua. Northeast Structural Genomics Consortium Target LkR112
Deposition date:
2009-10-18
Original release date:
2009-11-23
Authors:
Tang, Yuefeng; Montelione, Gaetano; Ciccosanti, Colleen; Lee, Dan; Janjua, Haleema; Everett, John; Swapna, G.V.T.; Acton, Thomas; Rose, Burkhard; Xiao, Rong
Citation:

Citation: Tang, Yuefeng; Montelione, Gaetano; Ciccosanti, Colleen; Lee, Dan; Janjua, Haleema; Everett, John; Swapna, G.V.T.; Acton, Thomas; Rose, Burkhard; Xiao, Rong. "Solution NMR structure of Lin0431 protein from Listeria innocua. Northeast Structural Genomics Consortium Target LkR112"  .

Assembly members:

Assembly members:
LkR112, polymer, 114 residues, 12784.5 Da.

Natural source:

Natural source:   Common Name: Listeria innocua   Taxonomy ID: 1642   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Listeria innocua

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: LkR112-36-140-21.21

Data sets:
Data typeCount
13C chemical shifts474
15N chemical shifts117
1H chemical shifts781

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1LkR1121

Entities:

Entity 1, LkR112 114 residues - 12784.5 Da.

1   METLYSASNTHRGLYASPGLUVALVALALA
2   ILEILESERGLNASNGLYLYSVALILEARG
3   GLUILEPROLEUTHRGLYHISLYSGLYASN
4   GLUGLNPHETHRILELYSGLYLYSGLYALA
5   GLNTYRASNLEUMETGLUVALASPGLYGLU
6   ARGILEARGILELYSGLUASPASNSERPRO
7   ASPGLNVALGLYVALLYSMETGLYTRPLYS
8   SERLYSALAGLYASPTHRILEVALCYSLEU
9   PROHISLYSVALPHEVALGLUILELYSSER
10   THRGLNLYSASPSERLYSASPPROASPTHR
11   ASPLEUILEVALPROASNLEUGLUHISHIS
12   HISHISHISHIS

Samples:

sample_1: LkR112, [U-100% 13C; U-100% 15N], 0.851 mM; MES 20 mM; NaCl 200 mM; CaCl2 5 mM; DTT 10 mM; NaN3 0.02%; DSS 50 uM; H2O 95%; D2O 5%

sample_2: LkR112, [U-5% 13C; U-100% 15N], 0.887 mM; MES 20 mM; NaCl 200 mM; CaCl2 5 mM; DTT 10 mM; NaN3 0.02%; DSS 50 uM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D High Resolution 1H-13C HSQCsample_2isotropicsample_conditions_1
2D aromatic 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C aliphatic NOESYsample_1isotropicsample_conditions_1
3D 1H-13C aromatic NOESYsample_1isotropicsample_conditions_1
3D simutaeous NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

SPARKY v3.110, Goddard - data analysis

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution

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

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

PSVS, Bhattacharya and Montelione - structure validation

PDBStat v5.1, Tejero and Montelione - PDB analysis

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
EMBL CAC95664
GB EFR91908 EFR94989 EHN61892 KJR52371 KJR53096
REF WP_003760402

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